data_9F25
# 
_entry.id   9F25 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9F25         pdb_00009f25 10.2210/pdb9f25/pdb 
WWPDB D_1292138029 ?            ?                   
EMDB  EMD-50138    ?            ?                   
# 
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 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-12 ? 
2 'EM metadata'     1 0 2025-03-12 ? 
3 FSC               1 0 2025-03-12 ? 
4 'Half map'        1 0 2025-03-12 1 
5 'Half map'        1 0 2025-03-12 2 
6 Image             1 0 2025-03-12 ? 
7 Mask              1 0 2025-03-12 1 
8 'Primary map'     1 0 2025-03-12 ? 
# 
loop_
_pdbx_audit_revision_details.ordinal 
_pdbx_audit_revision_details.revision_ordinal 
_pdbx_audit_revision_details.data_content_type 
_pdbx_audit_revision_details.provider 
_pdbx_audit_revision_details.type 
_pdbx_audit_revision_details.description 
_pdbx_audit_revision_details.details 
1 1 'Structure model' repository 'Initial release' ? ? 
2 2 'EM metadata'     repository 'Initial release' ? ? 
3 3 FSC               repository 'Initial release' ? ? 
4 4 'Half map'        repository 'Initial release' ? ? 
5 5 'Half map'        repository 'Initial release' ? ? 
6 6 Image             repository 'Initial release' ? ? 
7 7 Mask              repository 'Initial release' ? ? 
8 8 'Primary map'     repository 'Initial release' ? ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9F25 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-22 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        EMDB 
_pdbx_database_related.details        'Cryo-EM structure of Botulinum neurotoxin A LC-HN domain' 
_pdbx_database_related.db_id          EMD-50138 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              volodymyr.korkhov@psi.ch 
_pdbx_contact_author.name_first         Volodymyr 
_pdbx_contact_author.name_last          Korkhov 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-0962-9433 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Khanppnavar, B.' 1 0000-0002-6637-3550 
'Leka, O.'        2 ?                   
'Korkhov, V.'     3 0000-0002-0962-9433 
'Kammerer, R.'    4 0000-0003-4570-5197 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                1224 
_citation.page_last                 1224 
_citation.title                     
'Cryo-EM structure of the botulinum neurotoxin A/SV2B complex and its implications for translocation.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-56304-z 
_citation.pdbx_database_id_PubMed   39934119 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Khanppnavar, B.' 1 0000-0002-6637-3550 
primary 'Leka, O.'        2 ?                   
primary 'Pal, S.K.'       3 0000-0002-6193-9762 
primary 'Korkhov, V.M.'   4 0000-0002-0962-9433 
primary 'Kammerer, R.A.'  5 0000-0003-4570-5197 
# 
_entity.id                         1 
_entity.type                       polymer 
_entity.src_method                 man 
_entity.pdbx_description           'Botulinum neurotoxin type A' 
_entity.formula_weight             153083.734 
_entity.pdbx_number_of_molecules   1 
_entity.pdbx_ec                    ? 
_entity.pdbx_mutation              ? 
_entity.pdbx_fragment              ? 
_entity.details                    ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'BoNT/A,Bontoxilysin-A,BOTOX,Botulinum neurotoxin type A1' 
# 
_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       
;MRGSHHHHHHGSLVPRGSPFVNKQFNYKDPVNGVDIAYIKIPNAGQMQPVKAFKIHNKIWVIPERDTFTNPEEGDLNPPP
EAKQVPVSYYDSTYLSTDNEKDNYLKGVTKLFERIYSTDLGRMLLTSIVRGIPFWGGSTIDTELKVIDTNCINVIQPDGS
YRSEELNLVIIGPSADIIQFECKSFGHEVLNLTRNGYGSTQYIRFSPDFTFGFEESLEVDTNPLLGAGKFATDPAVTLAH
QLIHAGHRLYGIAINPNRVFKVNTNAYYEMSGLEVSFEELRTFGGHDAKFIDSLQENEFRLYYYNKFKDIASTLNKAKSI
VGTTASLQYMKNVFKEKYLLSEDTSGKFSVDKLKFDKLYKMLTEIYTEDNFVKFFKVLNAKTFLNFDKAVFKINIVPKVN
YTIYDGFNLRNTNLAANFNGQNTEINNMNFTKLKNFTGLFEFYKLLCVRGIITSKTKSLDKGYNKALNDLCIKVNNWDLF
FSPSEDNFTNDLNKGEEITSDTNIEAAEENISLDLIQQYYLTFNFDNEPENISIENLSSDIIGQLELMPNIERFPNGKKY
ELDKYTMFHYLRAQEFEHGKSRIALTNSVNEALLNPSRVYTFFSSDYVKKVNKATEAAMFLGWVEQLVYDFTDETSEVST
TDKIADITIIIPYIGPALNIGNMLYKDDFVGALIFSGAVILLEFIPEIAIPVLGTFALVSYIANKVLTVQTIDNALSKRN
EKWDEVYKYIVTNWLAKVNTQIDLIRKKMKEALENQAEATKAIINYQYNQYTEEEKNNINFNIDDLSSKLNESINKAMIN
INKFLNQCSVSYLMNSMIPYGVKRLEDFDASLKDALLKYIYDNRGTLIGQVDRLKDKVNNTLSTDIPFQLSKYVDNQRLL
STFTEYIKNIINTSILNLRYESNHLIDLSRYASKINIGSKVNFDPIDKNQIQLFNLESSKIEVILKNAIVYNSMYENFST
SFWIRIPKYFNSISLNNEYTIINCMENNSGWKVSLNYGEIIWTLQDTQEIKQRVVFKYSQMINISDYINRWIFVTITNNR
LNNSKIYINGRLIDQKPISNLGNIHASNNIMFKLDGCRDTHRYIWIKYFNLFDKELNEKEIKDLYDNQSNSGILKDFWGD
YLQYDKPYYMLNLYDPNKYVDVNNVGIRGYMYLKGPRGSVMTTNIYLNSSLYRGAKFIIKKYASGNKDNIVRNNDRVYIN
VVVKNKEYRLATNASQAGVEKILSALEIPDVGNLSQVVVMKSKNDQGITNKCKMNLQDNNGNDIGFIGFHQFNNIAKLVA
SNWYNRQIERSSRTLGCSWEFIPVDDGWGERPLVPPTPGSAWSHPQFEK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MRGSHHHHHHGSLVPRGSPFVNKQFNYKDPVNGVDIAYIKIPNAGQMQPVKAFKIHNKIWVIPERDTFTNPEEGDLNPPP
EAKQVPVSYYDSTYLSTDNEKDNYLKGVTKLFERIYSTDLGRMLLTSIVRGIPFWGGSTIDTELKVIDTNCINVIQPDGS
YRSEELNLVIIGPSADIIQFECKSFGHEVLNLTRNGYGSTQYIRFSPDFTFGFEESLEVDTNPLLGAGKFATDPAVTLAH
QLIHAGHRLYGIAINPNRVFKVNTNAYYEMSGLEVSFEELRTFGGHDAKFIDSLQENEFRLYYYNKFKDIASTLNKAKSI
VGTTASLQYMKNVFKEKYLLSEDTSGKFSVDKLKFDKLYKMLTEIYTEDNFVKFFKVLNAKTFLNFDKAVFKINIVPKVN
YTIYDGFNLRNTNLAANFNGQNTEINNMNFTKLKNFTGLFEFYKLLCVRGIITSKTKSLDKGYNKALNDLCIKVNNWDLF
FSPSEDNFTNDLNKGEEITSDTNIEAAEENISLDLIQQYYLTFNFDNEPENISIENLSSDIIGQLELMPNIERFPNGKKY
ELDKYTMFHYLRAQEFEHGKSRIALTNSVNEALLNPSRVYTFFSSDYVKKVNKATEAAMFLGWVEQLVYDFTDETSEVST
TDKIADITIIIPYIGPALNIGNMLYKDDFVGALIFSGAVILLEFIPEIAIPVLGTFALVSYIANKVLTVQTIDNALSKRN
EKWDEVYKYIVTNWLAKVNTQIDLIRKKMKEALENQAEATKAIINYQYNQYTEEEKNNINFNIDDLSSKLNESINKAMIN
INKFLNQCSVSYLMNSMIPYGVKRLEDFDASLKDALLKYIYDNRGTLIGQVDRLKDKVNNTLSTDIPFQLSKYVDNQRLL
STFTEYIKNIINTSILNLRYESNHLIDLSRYASKINIGSKVNFDPIDKNQIQLFNLESSKIEVILKNAIVYNSMYENFST
SFWIRIPKYFNSISLNNEYTIINCMENNSGWKVSLNYGEIIWTLQDTQEIKQRVVFKYSQMINISDYINRWIFVTITNNR
LNNSKIYINGRLIDQKPISNLGNIHASNNIMFKLDGCRDTHRYIWIKYFNLFDKELNEKEIKDLYDNQSNSGILKDFWGD
YLQYDKPYYMLNLYDPNKYVDVNNVGIRGYMYLKGPRGSVMTTNIYLNSSLYRGAKFIIKKYASGNKDNIVRNNDRVYIN
VVVKNKEYRLATNASQAGVEKILSALEIPDVGNLSQVVVMKSKNDQGITNKCKMNLQDNNGNDIGFIGFHQFNNIAKLVA
SNWYNRQIERSSRTLGCSWEFIPVDDGWGERPLVPPTPGSAWSHPQFEK
;
_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    MET n 
1 2    ARG n 
1 3    GLY n 
1 4    SER n 
1 5    HIS n 
1 6    HIS n 
1 7    HIS n 
1 8    HIS n 
1 9    HIS n 
1 10   HIS n 
1 11   GLY n 
1 12   SER n 
1 13   LEU n 
1 14   VAL n 
1 15   PRO n 
1 16   ARG n 
1 17   GLY n 
1 18   SER n 
1 19   PRO n 
1 20   PHE n 
1 21   VAL n 
1 22   ASN n 
1 23   LYS n 
1 24   GLN n 
1 25   PHE n 
1 26   ASN n 
1 27   TYR n 
1 28   LYS n 
1 29   ASP n 
1 30   PRO n 
1 31   VAL n 
1 32   ASN n 
1 33   GLY n 
1 34   VAL n 
1 35   ASP n 
1 36   ILE n 
1 37   ALA n 
1 38   TYR n 
1 39   ILE n 
1 40   LYS n 
1 41   ILE n 
1 42   PRO n 
1 43   ASN n 
1 44   ALA n 
1 45   GLY n 
1 46   GLN n 
1 47   MET n 
1 48   GLN n 
1 49   PRO n 
1 50   VAL n 
1 51   LYS n 
1 52   ALA n 
1 53   PHE n 
1 54   LYS n 
1 55   ILE n 
1 56   HIS n 
1 57   ASN n 
1 58   LYS n 
1 59   ILE n 
1 60   TRP n 
1 61   VAL n 
1 62   ILE n 
1 63   PRO n 
1 64   GLU n 
1 65   ARG n 
1 66   ASP n 
1 67   THR n 
1 68   PHE n 
1 69   THR n 
1 70   ASN n 
1 71   PRO n 
1 72   GLU n 
1 73   GLU n 
1 74   GLY n 
1 75   ASP n 
1 76   LEU n 
1 77   ASN n 
1 78   PRO n 
1 79   PRO n 
1 80   PRO n 
1 81   GLU n 
1 82   ALA n 
1 83   LYS n 
1 84   GLN n 
1 85   VAL n 
1 86   PRO n 
1 87   VAL n 
1 88   SER n 
1 89   TYR n 
1 90   TYR n 
1 91   ASP n 
1 92   SER n 
1 93   THR n 
1 94   TYR n 
1 95   LEU n 
1 96   SER n 
1 97   THR n 
1 98   ASP n 
1 99   ASN n 
1 100  GLU n 
1 101  LYS n 
1 102  ASP n 
1 103  ASN n 
1 104  TYR n 
1 105  LEU n 
1 106  LYS n 
1 107  GLY n 
1 108  VAL n 
1 109  THR n 
1 110  LYS n 
1 111  LEU n 
1 112  PHE n 
1 113  GLU n 
1 114  ARG n 
1 115  ILE n 
1 116  TYR n 
1 117  SER n 
1 118  THR n 
1 119  ASP n 
1 120  LEU n 
1 121  GLY n 
1 122  ARG n 
1 123  MET n 
1 124  LEU n 
1 125  LEU n 
1 126  THR n 
1 127  SER n 
1 128  ILE n 
1 129  VAL n 
1 130  ARG n 
1 131  GLY n 
1 132  ILE n 
1 133  PRO n 
1 134  PHE n 
1 135  TRP n 
1 136  GLY n 
1 137  GLY n 
1 138  SER n 
1 139  THR n 
1 140  ILE n 
1 141  ASP n 
1 142  THR n 
1 143  GLU n 
1 144  LEU n 
1 145  LYS n 
1 146  VAL n 
1 147  ILE n 
1 148  ASP n 
1 149  THR n 
1 150  ASN n 
1 151  CYS n 
1 152  ILE n 
1 153  ASN n 
1 154  VAL n 
1 155  ILE n 
1 156  GLN n 
1 157  PRO n 
1 158  ASP n 
1 159  GLY n 
1 160  SER n 
1 161  TYR n 
1 162  ARG n 
1 163  SER n 
1 164  GLU n 
1 165  GLU n 
1 166  LEU n 
1 167  ASN n 
1 168  LEU n 
1 169  VAL n 
1 170  ILE n 
1 171  ILE n 
1 172  GLY n 
1 173  PRO n 
1 174  SER n 
1 175  ALA n 
1 176  ASP n 
1 177  ILE n 
1 178  ILE n 
1 179  GLN n 
1 180  PHE n 
1 181  GLU n 
1 182  CYS n 
1 183  LYS n 
1 184  SER n 
1 185  PHE n 
1 186  GLY n 
1 187  HIS n 
1 188  GLU n 
1 189  VAL n 
1 190  LEU n 
1 191  ASN n 
1 192  LEU n 
1 193  THR n 
1 194  ARG n 
1 195  ASN n 
1 196  GLY n 
1 197  TYR n 
1 198  GLY n 
1 199  SER n 
1 200  THR n 
1 201  GLN n 
1 202  TYR n 
1 203  ILE n 
1 204  ARG n 
1 205  PHE n 
1 206  SER n 
1 207  PRO n 
1 208  ASP n 
1 209  PHE n 
1 210  THR n 
1 211  PHE n 
1 212  GLY n 
1 213  PHE n 
1 214  GLU n 
1 215  GLU n 
1 216  SER n 
1 217  LEU n 
1 218  GLU n 
1 219  VAL n 
1 220  ASP n 
1 221  THR n 
1 222  ASN n 
1 223  PRO n 
1 224  LEU n 
1 225  LEU n 
1 226  GLY n 
1 227  ALA n 
1 228  GLY n 
1 229  LYS n 
1 230  PHE n 
1 231  ALA n 
1 232  THR n 
1 233  ASP n 
1 234  PRO n 
1 235  ALA n 
1 236  VAL n 
1 237  THR n 
1 238  LEU n 
1 239  ALA n 
1 240  HIS n 
1 241  GLN n 
1 242  LEU n 
1 243  ILE n 
1 244  HIS n 
1 245  ALA n 
1 246  GLY n 
1 247  HIS n 
1 248  ARG n 
1 249  LEU n 
1 250  TYR n 
1 251  GLY n 
1 252  ILE n 
1 253  ALA n 
1 254  ILE n 
1 255  ASN n 
1 256  PRO n 
1 257  ASN n 
1 258  ARG n 
1 259  VAL n 
1 260  PHE n 
1 261  LYS n 
1 262  VAL n 
1 263  ASN n 
1 264  THR n 
1 265  ASN n 
1 266  ALA n 
1 267  TYR n 
1 268  TYR n 
1 269  GLU n 
1 270  MET n 
1 271  SER n 
1 272  GLY n 
1 273  LEU n 
1 274  GLU n 
1 275  VAL n 
1 276  SER n 
1 277  PHE n 
1 278  GLU n 
1 279  GLU n 
1 280  LEU n 
1 281  ARG n 
1 282  THR n 
1 283  PHE n 
1 284  GLY n 
1 285  GLY n 
1 286  HIS n 
1 287  ASP n 
1 288  ALA n 
1 289  LYS n 
1 290  PHE n 
1 291  ILE n 
1 292  ASP n 
1 293  SER n 
1 294  LEU n 
1 295  GLN n 
1 296  GLU n 
1 297  ASN n 
1 298  GLU n 
1 299  PHE n 
1 300  ARG n 
1 301  LEU n 
1 302  TYR n 
1 303  TYR n 
1 304  TYR n 
1 305  ASN n 
1 306  LYS n 
1 307  PHE n 
1 308  LYS n 
1 309  ASP n 
1 310  ILE n 
1 311  ALA n 
1 312  SER n 
1 313  THR n 
1 314  LEU n 
1 315  ASN n 
1 316  LYS n 
1 317  ALA n 
1 318  LYS n 
1 319  SER n 
1 320  ILE n 
1 321  VAL n 
1 322  GLY n 
1 323  THR n 
1 324  THR n 
1 325  ALA n 
1 326  SER n 
1 327  LEU n 
1 328  GLN n 
1 329  TYR n 
1 330  MET n 
1 331  LYS n 
1 332  ASN n 
1 333  VAL n 
1 334  PHE n 
1 335  LYS n 
1 336  GLU n 
1 337  LYS n 
1 338  TYR n 
1 339  LEU n 
1 340  LEU n 
1 341  SER n 
1 342  GLU n 
1 343  ASP n 
1 344  THR n 
1 345  SER n 
1 346  GLY n 
1 347  LYS n 
1 348  PHE n 
1 349  SER n 
1 350  VAL n 
1 351  ASP n 
1 352  LYS n 
1 353  LEU n 
1 354  LYS n 
1 355  PHE n 
1 356  ASP n 
1 357  LYS n 
1 358  LEU n 
1 359  TYR n 
1 360  LYS n 
1 361  MET n 
1 362  LEU n 
1 363  THR n 
1 364  GLU n 
1 365  ILE n 
1 366  TYR n 
1 367  THR n 
1 368  GLU n 
1 369  ASP n 
1 370  ASN n 
1 371  PHE n 
1 372  VAL n 
1 373  LYS n 
1 374  PHE n 
1 375  PHE n 
1 376  LYS n 
1 377  VAL n 
1 378  LEU n 
1 379  ASN n 
1 380  ALA n 
1 381  LYS n 
1 382  THR n 
1 383  PHE n 
1 384  LEU n 
1 385  ASN n 
1 386  PHE n 
1 387  ASP n 
1 388  LYS n 
1 389  ALA n 
1 390  VAL n 
1 391  PHE n 
1 392  LYS n 
1 393  ILE n 
1 394  ASN n 
1 395  ILE n 
1 396  VAL n 
1 397  PRO n 
1 398  LYS n 
1 399  VAL n 
1 400  ASN n 
1 401  TYR n 
1 402  THR n 
1 403  ILE n 
1 404  TYR n 
1 405  ASP n 
1 406  GLY n 
1 407  PHE n 
1 408  ASN n 
1 409  LEU n 
1 410  ARG n 
1 411  ASN n 
1 412  THR n 
1 413  ASN n 
1 414  LEU n 
1 415  ALA n 
1 416  ALA n 
1 417  ASN n 
1 418  PHE n 
1 419  ASN n 
1 420  GLY n 
1 421  GLN n 
1 422  ASN n 
1 423  THR n 
1 424  GLU n 
1 425  ILE n 
1 426  ASN n 
1 427  ASN n 
1 428  MET n 
1 429  ASN n 
1 430  PHE n 
1 431  THR n 
1 432  LYS n 
1 433  LEU n 
1 434  LYS n 
1 435  ASN n 
1 436  PHE n 
1 437  THR n 
1 438  GLY n 
1 439  LEU n 
1 440  PHE n 
1 441  GLU n 
1 442  PHE n 
1 443  TYR n 
1 444  LYS n 
1 445  LEU n 
1 446  LEU n 
1 447  CYS n 
1 448  VAL n 
1 449  ARG n 
1 450  GLY n 
1 451  ILE n 
1 452  ILE n 
1 453  THR n 
1 454  SER n 
1 455  LYS n 
1 456  THR n 
1 457  LYS n 
1 458  SER n 
1 459  LEU n 
1 460  ASP n 
1 461  LYS n 
1 462  GLY n 
1 463  TYR n 
1 464  ASN n 
1 465  LYS n 
1 466  ALA n 
1 467  LEU n 
1 468  ASN n 
1 469  ASP n 
1 470  LEU n 
1 471  CYS n 
1 472  ILE n 
1 473  LYS n 
1 474  VAL n 
1 475  ASN n 
1 476  ASN n 
1 477  TRP n 
1 478  ASP n 
1 479  LEU n 
1 480  PHE n 
1 481  PHE n 
1 482  SER n 
1 483  PRO n 
1 484  SER n 
1 485  GLU n 
1 486  ASP n 
1 487  ASN n 
1 488  PHE n 
1 489  THR n 
1 490  ASN n 
1 491  ASP n 
1 492  LEU n 
1 493  ASN n 
1 494  LYS n 
1 495  GLY n 
1 496  GLU n 
1 497  GLU n 
1 498  ILE n 
1 499  THR n 
1 500  SER n 
1 501  ASP n 
1 502  THR n 
1 503  ASN n 
1 504  ILE n 
1 505  GLU n 
1 506  ALA n 
1 507  ALA n 
1 508  GLU n 
1 509  GLU n 
1 510  ASN n 
1 511  ILE n 
1 512  SER n 
1 513  LEU n 
1 514  ASP n 
1 515  LEU n 
1 516  ILE n 
1 517  GLN n 
1 518  GLN n 
1 519  TYR n 
1 520  TYR n 
1 521  LEU n 
1 522  THR n 
1 523  PHE n 
1 524  ASN n 
1 525  PHE n 
1 526  ASP n 
1 527  ASN n 
1 528  GLU n 
1 529  PRO n 
1 530  GLU n 
1 531  ASN n 
1 532  ILE n 
1 533  SER n 
1 534  ILE n 
1 535  GLU n 
1 536  ASN n 
1 537  LEU n 
1 538  SER n 
1 539  SER n 
1 540  ASP n 
1 541  ILE n 
1 542  ILE n 
1 543  GLY n 
1 544  GLN n 
1 545  LEU n 
1 546  GLU n 
1 547  LEU n 
1 548  MET n 
1 549  PRO n 
1 550  ASN n 
1 551  ILE n 
1 552  GLU n 
1 553  ARG n 
1 554  PHE n 
1 555  PRO n 
1 556  ASN n 
1 557  GLY n 
1 558  LYS n 
1 559  LYS n 
1 560  TYR n 
1 561  GLU n 
1 562  LEU n 
1 563  ASP n 
1 564  LYS n 
1 565  TYR n 
1 566  THR n 
1 567  MET n 
1 568  PHE n 
1 569  HIS n 
1 570  TYR n 
1 571  LEU n 
1 572  ARG n 
1 573  ALA n 
1 574  GLN n 
1 575  GLU n 
1 576  PHE n 
1 577  GLU n 
1 578  HIS n 
1 579  GLY n 
1 580  LYS n 
1 581  SER n 
1 582  ARG n 
1 583  ILE n 
1 584  ALA n 
1 585  LEU n 
1 586  THR n 
1 587  ASN n 
1 588  SER n 
1 589  VAL n 
1 590  ASN n 
1 591  GLU n 
1 592  ALA n 
1 593  LEU n 
1 594  LEU n 
1 595  ASN n 
1 596  PRO n 
1 597  SER n 
1 598  ARG n 
1 599  VAL n 
1 600  TYR n 
1 601  THR n 
1 602  PHE n 
1 603  PHE n 
1 604  SER n 
1 605  SER n 
1 606  ASP n 
1 607  TYR n 
1 608  VAL n 
1 609  LYS n 
1 610  LYS n 
1 611  VAL n 
1 612  ASN n 
1 613  LYS n 
1 614  ALA n 
1 615  THR n 
1 616  GLU n 
1 617  ALA n 
1 618  ALA n 
1 619  MET n 
1 620  PHE n 
1 621  LEU n 
1 622  GLY n 
1 623  TRP n 
1 624  VAL n 
1 625  GLU n 
1 626  GLN n 
1 627  LEU n 
1 628  VAL n 
1 629  TYR n 
1 630  ASP n 
1 631  PHE n 
1 632  THR n 
1 633  ASP n 
1 634  GLU n 
1 635  THR n 
1 636  SER n 
1 637  GLU n 
1 638  VAL n 
1 639  SER n 
1 640  THR n 
1 641  THR n 
1 642  ASP n 
1 643  LYS n 
1 644  ILE n 
1 645  ALA n 
1 646  ASP n 
1 647  ILE n 
1 648  THR n 
1 649  ILE n 
1 650  ILE n 
1 651  ILE n 
1 652  PRO n 
1 653  TYR n 
1 654  ILE n 
1 655  GLY n 
1 656  PRO n 
1 657  ALA n 
1 658  LEU n 
1 659  ASN n 
1 660  ILE n 
1 661  GLY n 
1 662  ASN n 
1 663  MET n 
1 664  LEU n 
1 665  TYR n 
1 666  LYS n 
1 667  ASP n 
1 668  ASP n 
1 669  PHE n 
1 670  VAL n 
1 671  GLY n 
1 672  ALA n 
1 673  LEU n 
1 674  ILE n 
1 675  PHE n 
1 676  SER n 
1 677  GLY n 
1 678  ALA n 
1 679  VAL n 
1 680  ILE n 
1 681  LEU n 
1 682  LEU n 
1 683  GLU n 
1 684  PHE n 
1 685  ILE n 
1 686  PRO n 
1 687  GLU n 
1 688  ILE n 
1 689  ALA n 
1 690  ILE n 
1 691  PRO n 
1 692  VAL n 
1 693  LEU n 
1 694  GLY n 
1 695  THR n 
1 696  PHE n 
1 697  ALA n 
1 698  LEU n 
1 699  VAL n 
1 700  SER n 
1 701  TYR n 
1 702  ILE n 
1 703  ALA n 
1 704  ASN n 
1 705  LYS n 
1 706  VAL n 
1 707  LEU n 
1 708  THR n 
1 709  VAL n 
1 710  GLN n 
1 711  THR n 
1 712  ILE n 
1 713  ASP n 
1 714  ASN n 
1 715  ALA n 
1 716  LEU n 
1 717  SER n 
1 718  LYS n 
1 719  ARG n 
1 720  ASN n 
1 721  GLU n 
1 722  LYS n 
1 723  TRP n 
1 724  ASP n 
1 725  GLU n 
1 726  VAL n 
1 727  TYR n 
1 728  LYS n 
1 729  TYR n 
1 730  ILE n 
1 731  VAL n 
1 732  THR n 
1 733  ASN n 
1 734  TRP n 
1 735  LEU n 
1 736  ALA n 
1 737  LYS n 
1 738  VAL n 
1 739  ASN n 
1 740  THR n 
1 741  GLN n 
1 742  ILE n 
1 743  ASP n 
1 744  LEU n 
1 745  ILE n 
1 746  ARG n 
1 747  LYS n 
1 748  LYS n 
1 749  MET n 
1 750  LYS n 
1 751  GLU n 
1 752  ALA n 
1 753  LEU n 
1 754  GLU n 
1 755  ASN n 
1 756  GLN n 
1 757  ALA n 
1 758  GLU n 
1 759  ALA n 
1 760  THR n 
1 761  LYS n 
1 762  ALA n 
1 763  ILE n 
1 764  ILE n 
1 765  ASN n 
1 766  TYR n 
1 767  GLN n 
1 768  TYR n 
1 769  ASN n 
1 770  GLN n 
1 771  TYR n 
1 772  THR n 
1 773  GLU n 
1 774  GLU n 
1 775  GLU n 
1 776  LYS n 
1 777  ASN n 
1 778  ASN n 
1 779  ILE n 
1 780  ASN n 
1 781  PHE n 
1 782  ASN n 
1 783  ILE n 
1 784  ASP n 
1 785  ASP n 
1 786  LEU n 
1 787  SER n 
1 788  SER n 
1 789  LYS n 
1 790  LEU n 
1 791  ASN n 
1 792  GLU n 
1 793  SER n 
1 794  ILE n 
1 795  ASN n 
1 796  LYS n 
1 797  ALA n 
1 798  MET n 
1 799  ILE n 
1 800  ASN n 
1 801  ILE n 
1 802  ASN n 
1 803  LYS n 
1 804  PHE n 
1 805  LEU n 
1 806  ASN n 
1 807  GLN n 
1 808  CYS n 
1 809  SER n 
1 810  VAL n 
1 811  SER n 
1 812  TYR n 
1 813  LEU n 
1 814  MET n 
1 815  ASN n 
1 816  SER n 
1 817  MET n 
1 818  ILE n 
1 819  PRO n 
1 820  TYR n 
1 821  GLY n 
1 822  VAL n 
1 823  LYS n 
1 824  ARG n 
1 825  LEU n 
1 826  GLU n 
1 827  ASP n 
1 828  PHE n 
1 829  ASP n 
1 830  ALA n 
1 831  SER n 
1 832  LEU n 
1 833  LYS n 
1 834  ASP n 
1 835  ALA n 
1 836  LEU n 
1 837  LEU n 
1 838  LYS n 
1 839  TYR n 
1 840  ILE n 
1 841  TYR n 
1 842  ASP n 
1 843  ASN n 
1 844  ARG n 
1 845  GLY n 
1 846  THR n 
1 847  LEU n 
1 848  ILE n 
1 849  GLY n 
1 850  GLN n 
1 851  VAL n 
1 852  ASP n 
1 853  ARG n 
1 854  LEU n 
1 855  LYS n 
1 856  ASP n 
1 857  LYS n 
1 858  VAL n 
1 859  ASN n 
1 860  ASN n 
1 861  THR n 
1 862  LEU n 
1 863  SER n 
1 864  THR n 
1 865  ASP n 
1 866  ILE n 
1 867  PRO n 
1 868  PHE n 
1 869  GLN n 
1 870  LEU n 
1 871  SER n 
1 872  LYS n 
1 873  TYR n 
1 874  VAL n 
1 875  ASP n 
1 876  ASN n 
1 877  GLN n 
1 878  ARG n 
1 879  LEU n 
1 880  LEU n 
1 881  SER n 
1 882  THR n 
1 883  PHE n 
1 884  THR n 
1 885  GLU n 
1 886  TYR n 
1 887  ILE n 
1 888  LYS n 
1 889  ASN n 
1 890  ILE n 
1 891  ILE n 
1 892  ASN n 
1 893  THR n 
1 894  SER n 
1 895  ILE n 
1 896  LEU n 
1 897  ASN n 
1 898  LEU n 
1 899  ARG n 
1 900  TYR n 
1 901  GLU n 
1 902  SER n 
1 903  ASN n 
1 904  HIS n 
1 905  LEU n 
1 906  ILE n 
1 907  ASP n 
1 908  LEU n 
1 909  SER n 
1 910  ARG n 
1 911  TYR n 
1 912  ALA n 
1 913  SER n 
1 914  LYS n 
1 915  ILE n 
1 916  ASN n 
1 917  ILE n 
1 918  GLY n 
1 919  SER n 
1 920  LYS n 
1 921  VAL n 
1 922  ASN n 
1 923  PHE n 
1 924  ASP n 
1 925  PRO n 
1 926  ILE n 
1 927  ASP n 
1 928  LYS n 
1 929  ASN n 
1 930  GLN n 
1 931  ILE n 
1 932  GLN n 
1 933  LEU n 
1 934  PHE n 
1 935  ASN n 
1 936  LEU n 
1 937  GLU n 
1 938  SER n 
1 939  SER n 
1 940  LYS n 
1 941  ILE n 
1 942  GLU n 
1 943  VAL n 
1 944  ILE n 
1 945  LEU n 
1 946  LYS n 
1 947  ASN n 
1 948  ALA n 
1 949  ILE n 
1 950  VAL n 
1 951  TYR n 
1 952  ASN n 
1 953  SER n 
1 954  MET n 
1 955  TYR n 
1 956  GLU n 
1 957  ASN n 
1 958  PHE n 
1 959  SER n 
1 960  THR n 
1 961  SER n 
1 962  PHE n 
1 963  TRP n 
1 964  ILE n 
1 965  ARG n 
1 966  ILE n 
1 967  PRO n 
1 968  LYS n 
1 969  TYR n 
1 970  PHE n 
1 971  ASN n 
1 972  SER n 
1 973  ILE n 
1 974  SER n 
1 975  LEU n 
1 976  ASN n 
1 977  ASN n 
1 978  GLU n 
1 979  TYR n 
1 980  THR n 
1 981  ILE n 
1 982  ILE n 
1 983  ASN n 
1 984  CYS n 
1 985  MET n 
1 986  GLU n 
1 987  ASN n 
1 988  ASN n 
1 989  SER n 
1 990  GLY n 
1 991  TRP n 
1 992  LYS n 
1 993  VAL n 
1 994  SER n 
1 995  LEU n 
1 996  ASN n 
1 997  TYR n 
1 998  GLY n 
1 999  GLU n 
1 1000 ILE n 
1 1001 ILE n 
1 1002 TRP n 
1 1003 THR n 
1 1004 LEU n 
1 1005 GLN n 
1 1006 ASP n 
1 1007 THR n 
1 1008 GLN n 
1 1009 GLU n 
1 1010 ILE n 
1 1011 LYS n 
1 1012 GLN n 
1 1013 ARG n 
1 1014 VAL n 
1 1015 VAL n 
1 1016 PHE n 
1 1017 LYS n 
1 1018 TYR n 
1 1019 SER n 
1 1020 GLN n 
1 1021 MET n 
1 1022 ILE n 
1 1023 ASN n 
1 1024 ILE n 
1 1025 SER n 
1 1026 ASP n 
1 1027 TYR n 
1 1028 ILE n 
1 1029 ASN n 
1 1030 ARG n 
1 1031 TRP n 
1 1032 ILE n 
1 1033 PHE n 
1 1034 VAL n 
1 1035 THR n 
1 1036 ILE n 
1 1037 THR n 
1 1038 ASN n 
1 1039 ASN n 
1 1040 ARG n 
1 1041 LEU n 
1 1042 ASN n 
1 1043 ASN n 
1 1044 SER n 
1 1045 LYS n 
1 1046 ILE n 
1 1047 TYR n 
1 1048 ILE n 
1 1049 ASN n 
1 1050 GLY n 
1 1051 ARG n 
1 1052 LEU n 
1 1053 ILE n 
1 1054 ASP n 
1 1055 GLN n 
1 1056 LYS n 
1 1057 PRO n 
1 1058 ILE n 
1 1059 SER n 
1 1060 ASN n 
1 1061 LEU n 
1 1062 GLY n 
1 1063 ASN n 
1 1064 ILE n 
1 1065 HIS n 
1 1066 ALA n 
1 1067 SER n 
1 1068 ASN n 
1 1069 ASN n 
1 1070 ILE n 
1 1071 MET n 
1 1072 PHE n 
1 1073 LYS n 
1 1074 LEU n 
1 1075 ASP n 
1 1076 GLY n 
1 1077 CYS n 
1 1078 ARG n 
1 1079 ASP n 
1 1080 THR n 
1 1081 HIS n 
1 1082 ARG n 
1 1083 TYR n 
1 1084 ILE n 
1 1085 TRP n 
1 1086 ILE n 
1 1087 LYS n 
1 1088 TYR n 
1 1089 PHE n 
1 1090 ASN n 
1 1091 LEU n 
1 1092 PHE n 
1 1093 ASP n 
1 1094 LYS n 
1 1095 GLU n 
1 1096 LEU n 
1 1097 ASN n 
1 1098 GLU n 
1 1099 LYS n 
1 1100 GLU n 
1 1101 ILE n 
1 1102 LYS n 
1 1103 ASP n 
1 1104 LEU n 
1 1105 TYR n 
1 1106 ASP n 
1 1107 ASN n 
1 1108 GLN n 
1 1109 SER n 
1 1110 ASN n 
1 1111 SER n 
1 1112 GLY n 
1 1113 ILE n 
1 1114 LEU n 
1 1115 LYS n 
1 1116 ASP n 
1 1117 PHE n 
1 1118 TRP n 
1 1119 GLY n 
1 1120 ASP n 
1 1121 TYR n 
1 1122 LEU n 
1 1123 GLN n 
1 1124 TYR n 
1 1125 ASP n 
1 1126 LYS n 
1 1127 PRO n 
1 1128 TYR n 
1 1129 TYR n 
1 1130 MET n 
1 1131 LEU n 
1 1132 ASN n 
1 1133 LEU n 
1 1134 TYR n 
1 1135 ASP n 
1 1136 PRO n 
1 1137 ASN n 
1 1138 LYS n 
1 1139 TYR n 
1 1140 VAL n 
1 1141 ASP n 
1 1142 VAL n 
1 1143 ASN n 
1 1144 ASN n 
1 1145 VAL n 
1 1146 GLY n 
1 1147 ILE n 
1 1148 ARG n 
1 1149 GLY n 
1 1150 TYR n 
1 1151 MET n 
1 1152 TYR n 
1 1153 LEU n 
1 1154 LYS n 
1 1155 GLY n 
1 1156 PRO n 
1 1157 ARG n 
1 1158 GLY n 
1 1159 SER n 
1 1160 VAL n 
1 1161 MET n 
1 1162 THR n 
1 1163 THR n 
1 1164 ASN n 
1 1165 ILE n 
1 1166 TYR n 
1 1167 LEU n 
1 1168 ASN n 
1 1169 SER n 
1 1170 SER n 
1 1171 LEU n 
1 1172 TYR n 
1 1173 ARG n 
1 1174 GLY n 
1 1175 ALA n 
1 1176 LYS n 
1 1177 PHE n 
1 1178 ILE n 
1 1179 ILE n 
1 1180 LYS n 
1 1181 LYS n 
1 1182 TYR n 
1 1183 ALA n 
1 1184 SER n 
1 1185 GLY n 
1 1186 ASN n 
1 1187 LYS n 
1 1188 ASP n 
1 1189 ASN n 
1 1190 ILE n 
1 1191 VAL n 
1 1192 ARG n 
1 1193 ASN n 
1 1194 ASN n 
1 1195 ASP n 
1 1196 ARG n 
1 1197 VAL n 
1 1198 TYR n 
1 1199 ILE n 
1 1200 ASN n 
1 1201 VAL n 
1 1202 VAL n 
1 1203 VAL n 
1 1204 LYS n 
1 1205 ASN n 
1 1206 LYS n 
1 1207 GLU n 
1 1208 TYR n 
1 1209 ARG n 
1 1210 LEU n 
1 1211 ALA n 
1 1212 THR n 
1 1213 ASN n 
1 1214 ALA n 
1 1215 SER n 
1 1216 GLN n 
1 1217 ALA n 
1 1218 GLY n 
1 1219 VAL n 
1 1220 GLU n 
1 1221 LYS n 
1 1222 ILE n 
1 1223 LEU n 
1 1224 SER n 
1 1225 ALA n 
1 1226 LEU n 
1 1227 GLU n 
1 1228 ILE n 
1 1229 PRO n 
1 1230 ASP n 
1 1231 VAL n 
1 1232 GLY n 
1 1233 ASN n 
1 1234 LEU n 
1 1235 SER n 
1 1236 GLN n 
1 1237 VAL n 
1 1238 VAL n 
1 1239 VAL n 
1 1240 MET n 
1 1241 LYS n 
1 1242 SER n 
1 1243 LYS n 
1 1244 ASN n 
1 1245 ASP n 
1 1246 GLN n 
1 1247 GLY n 
1 1248 ILE n 
1 1249 THR n 
1 1250 ASN n 
1 1251 LYS n 
1 1252 CYS n 
1 1253 LYS n 
1 1254 MET n 
1 1255 ASN n 
1 1256 LEU n 
1 1257 GLN n 
1 1258 ASP n 
1 1259 ASN n 
1 1260 ASN n 
1 1261 GLY n 
1 1262 ASN n 
1 1263 ASP n 
1 1264 ILE n 
1 1265 GLY n 
1 1266 PHE n 
1 1267 ILE n 
1 1268 GLY n 
1 1269 PHE n 
1 1270 HIS n 
1 1271 GLN n 
1 1272 PHE n 
1 1273 ASN n 
1 1274 ASN n 
1 1275 ILE n 
1 1276 ALA n 
1 1277 LYS n 
1 1278 LEU n 
1 1279 VAL n 
1 1280 ALA n 
1 1281 SER n 
1 1282 ASN n 
1 1283 TRP n 
1 1284 TYR n 
1 1285 ASN n 
1 1286 ARG n 
1 1287 GLN n 
1 1288 ILE n 
1 1289 GLU n 
1 1290 ARG n 
1 1291 SER n 
1 1292 SER n 
1 1293 ARG n 
1 1294 THR n 
1 1295 LEU n 
1 1296 GLY n 
1 1297 CYS n 
1 1298 SER n 
1 1299 TRP n 
1 1300 GLU n 
1 1301 PHE n 
1 1302 ILE n 
1 1303 PRO n 
1 1304 VAL n 
1 1305 ASP n 
1 1306 ASP n 
1 1307 GLY n 
1 1308 TRP n 
1 1309 GLY n 
1 1310 GLU n 
1 1311 ARG n 
1 1312 PRO n 
1 1313 LEU n 
1 1314 VAL n 
1 1315 PRO n 
1 1316 PRO n 
1 1317 THR n 
1 1318 PRO n 
1 1319 GLY n 
1 1320 SER n 
1 1321 ALA n 
1 1322 TRP n 
1 1323 SER n 
1 1324 HIS n 
1 1325 PRO n 
1 1326 GLN n 
1 1327 PHE n 
1 1328 GLU n 
1 1329 LYS 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                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   1329 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'botA, atx, bonT' 
_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      'Clostridium botulinum' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1491 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
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 
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 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1    MET 1    -16  ?   ?   ?   A . n 
A 1 2    ARG 2    -15  ?   ?   ?   A . n 
A 1 3    GLY 3    -14  ?   ?   ?   A . n 
A 1 4    SER 4    -13  ?   ?   ?   A . n 
A 1 5    HIS 5    -12  ?   ?   ?   A . n 
A 1 6    HIS 6    -11  ?   ?   ?   A . n 
A 1 7    HIS 7    -10  ?   ?   ?   A . n 
A 1 8    HIS 8    -9   ?   ?   ?   A . n 
A 1 9    HIS 9    -8   ?   ?   ?   A . n 
A 1 10   HIS 10   -7   ?   ?   ?   A . n 
A 1 11   GLY 11   -6   ?   ?   ?   A . n 
A 1 12   SER 12   -5   ?   ?   ?   A . n 
A 1 13   LEU 13   -4   ?   ?   ?   A . n 
A 1 14   VAL 14   -3   ?   ?   ?   A . n 
A 1 15   PRO 15   -2   ?   ?   ?   A . n 
A 1 16   ARG 16   -1   ?   ?   ?   A . n 
A 1 17   GLY 17   0    ?   ?   ?   A . n 
A 1 18   SER 18   1    ?   ?   ?   A . n 
A 1 19   PRO 19   2    2   PRO PRO A . n 
A 1 20   PHE 20   3    3   PHE PHE A . n 
A 1 21   VAL 21   4    4   VAL VAL A . n 
A 1 22   ASN 22   5    5   ASN ASN A . n 
A 1 23   LYS 23   6    6   LYS LYS A . n 
A 1 24   GLN 24   7    7   GLN GLN A . n 
A 1 25   PHE 25   8    8   PHE PHE A . n 
A 1 26   ASN 26   9    9   ASN ASN A . n 
A 1 27   TYR 27   10   10  TYR TYR A . n 
A 1 28   LYS 28   11   11  LYS LYS A . n 
A 1 29   ASP 29   12   12  ASP ASP A . n 
A 1 30   PRO 30   13   13  PRO PRO A . n 
A 1 31   VAL 31   14   14  VAL VAL A . n 
A 1 32   ASN 32   15   15  ASN ASN A . n 
A 1 33   GLY 33   16   16  GLY GLY A . n 
A 1 34   VAL 34   17   17  VAL VAL A . n 
A 1 35   ASP 35   18   18  ASP ASP A . n 
A 1 36   ILE 36   19   19  ILE ILE A . n 
A 1 37   ALA 37   20   20  ALA ALA A . n 
A 1 38   TYR 38   21   21  TYR TYR A . n 
A 1 39   ILE 39   22   22  ILE ILE A . n 
A 1 40   LYS 40   23   23  LYS LYS A . n 
A 1 41   ILE 41   24   24  ILE ILE A . n 
A 1 42   PRO 42   25   25  PRO PRO A . n 
A 1 43   ASN 43   26   26  ASN ASN A . n 
A 1 44   ALA 44   27   27  ALA ALA A . n 
A 1 45   GLY 45   28   28  GLY GLY A . n 
A 1 46   GLN 46   29   29  GLN GLN A . n 
A 1 47   MET 47   30   30  MET MET A . n 
A 1 48   GLN 48   31   31  GLN GLN A . n 
A 1 49   PRO 49   32   32  PRO PRO A . n 
A 1 50   VAL 50   33   33  VAL VAL A . n 
A 1 51   LYS 51   34   34  LYS LYS A . n 
A 1 52   ALA 52   35   35  ALA ALA A . n 
A 1 53   PHE 53   36   36  PHE PHE A . n 
A 1 54   LYS 54   37   37  LYS LYS A . n 
A 1 55   ILE 55   38   38  ILE ILE A . n 
A 1 56   HIS 56   39   39  HIS HIS A . n 
A 1 57   ASN 57   40   40  ASN ASN A . n 
A 1 58   LYS 58   41   41  LYS LYS A . n 
A 1 59   ILE 59   42   42  ILE ILE A . n 
A 1 60   TRP 60   43   43  TRP TRP A . n 
A 1 61   VAL 61   44   44  VAL VAL A . n 
A 1 62   ILE 62   45   45  ILE ILE A . n 
A 1 63   PRO 63   46   46  PRO PRO A . n 
A 1 64   GLU 64   47   47  GLU GLU A . n 
A 1 65   ARG 65   48   48  ARG ARG A . n 
A 1 66   ASP 66   49   49  ASP ASP A . n 
A 1 67   THR 67   50   50  THR THR A . n 
A 1 68   PHE 68   51   51  PHE PHE A . n 
A 1 69   THR 69   52   52  THR THR A . n 
A 1 70   ASN 70   53   53  ASN ASN A . n 
A 1 71   PRO 71   54   54  PRO PRO A . n 
A 1 72   GLU 72   55   55  GLU GLU A . n 
A 1 73   GLU 73   56   56  GLU GLU A . n 
A 1 74   GLY 74   57   57  GLY GLY A . n 
A 1 75   ASP 75   58   58  ASP ASP A . n 
A 1 76   LEU 76   59   59  LEU LEU A . n 
A 1 77   ASN 77   60   60  ASN ASN A . n 
A 1 78   PRO 78   61   61  PRO PRO A . n 
A 1 79   PRO 79   62   62  PRO PRO A . n 
A 1 80   PRO 80   63   63  PRO PRO A . n 
A 1 81   GLU 81   64   64  GLU GLU A . n 
A 1 82   ALA 82   65   65  ALA ALA A . n 
A 1 83   LYS 83   66   66  LYS LYS A . n 
A 1 84   GLN 84   67   67  GLN GLN A . n 
A 1 85   VAL 85   68   68  VAL VAL A . n 
A 1 86   PRO 86   69   69  PRO PRO A . n 
A 1 87   VAL 87   70   70  VAL VAL A . n 
A 1 88   SER 88   71   71  SER SER A . n 
A 1 89   TYR 89   72   72  TYR TYR A . n 
A 1 90   TYR 90   73   73  TYR TYR A . n 
A 1 91   ASP 91   74   74  ASP ASP A . n 
A 1 92   SER 92   75   75  SER SER A . n 
A 1 93   THR 93   76   76  THR THR A . n 
A 1 94   TYR 94   77   77  TYR TYR A . n 
A 1 95   LEU 95   78   78  LEU LEU A . n 
A 1 96   SER 96   79   79  SER SER A . n 
A 1 97   THR 97   80   80  THR THR A . n 
A 1 98   ASP 98   81   81  ASP ASP A . n 
A 1 99   ASN 99   82   82  ASN ASN A . n 
A 1 100  GLU 100  83   83  GLU GLU A . n 
A 1 101  LYS 101  84   84  LYS LYS A . n 
A 1 102  ASP 102  85   85  ASP ASP A . n 
A 1 103  ASN 103  86   86  ASN ASN A . n 
A 1 104  TYR 104  87   87  TYR TYR A . n 
A 1 105  LEU 105  88   88  LEU LEU A . n 
A 1 106  LYS 106  89   89  LYS LYS A . n 
A 1 107  GLY 107  90   90  GLY GLY A . n 
A 1 108  VAL 108  91   91  VAL VAL A . n 
A 1 109  THR 109  92   92  THR THR A . n 
A 1 110  LYS 110  93   93  LYS LYS A . n 
A 1 111  LEU 111  94   94  LEU LEU A . n 
A 1 112  PHE 112  95   95  PHE PHE A . n 
A 1 113  GLU 113  96   96  GLU GLU A . n 
A 1 114  ARG 114  97   97  ARG ARG A . n 
A 1 115  ILE 115  98   98  ILE ILE A . n 
A 1 116  TYR 116  99   99  TYR TYR A . n 
A 1 117  SER 117  100  100 SER SER A . n 
A 1 118  THR 118  101  101 THR THR A . n 
A 1 119  ASP 119  102  102 ASP ASP A . n 
A 1 120  LEU 120  103  103 LEU LEU A . n 
A 1 121  GLY 121  104  104 GLY GLY A . n 
A 1 122  ARG 122  105  105 ARG ARG A . n 
A 1 123  MET 123  106  106 MET MET A . n 
A 1 124  LEU 124  107  107 LEU LEU A . n 
A 1 125  LEU 125  108  108 LEU LEU A . n 
A 1 126  THR 126  109  109 THR THR A . n 
A 1 127  SER 127  110  110 SER SER A . n 
A 1 128  ILE 128  111  111 ILE ILE A . n 
A 1 129  VAL 129  112  112 VAL VAL A . n 
A 1 130  ARG 130  113  113 ARG ARG A . n 
A 1 131  GLY 131  114  114 GLY GLY A . n 
A 1 132  ILE 132  115  115 ILE ILE A . n 
A 1 133  PRO 133  116  116 PRO PRO A . n 
A 1 134  PHE 134  117  117 PHE PHE A . n 
A 1 135  TRP 135  118  118 TRP TRP A . n 
A 1 136  GLY 136  119  119 GLY GLY A . n 
A 1 137  GLY 137  120  120 GLY GLY A . n 
A 1 138  SER 138  121  121 SER SER A . n 
A 1 139  THR 139  122  122 THR THR A . n 
A 1 140  ILE 140  123  123 ILE ILE A . n 
A 1 141  ASP 141  124  124 ASP ASP A . n 
A 1 142  THR 142  125  125 THR THR A . n 
A 1 143  GLU 143  126  126 GLU GLU A . n 
A 1 144  LEU 144  127  127 LEU LEU A . n 
A 1 145  LYS 145  128  128 LYS LYS A . n 
A 1 146  VAL 146  129  129 VAL VAL A . n 
A 1 147  ILE 147  130  130 ILE ILE A . n 
A 1 148  ASP 148  131  131 ASP ASP A . n 
A 1 149  THR 149  132  132 THR THR A . n 
A 1 150  ASN 150  133  133 ASN ASN A . n 
A 1 151  CYS 151  134  134 CYS CYS A . n 
A 1 152  ILE 152  135  135 ILE ILE A . n 
A 1 153  ASN 153  136  136 ASN ASN A . n 
A 1 154  VAL 154  137  137 VAL VAL A . n 
A 1 155  ILE 155  138  138 ILE ILE A . n 
A 1 156  GLN 156  139  139 GLN GLN A . n 
A 1 157  PRO 157  140  140 PRO PRO A . n 
A 1 158  ASP 158  141  141 ASP ASP A . n 
A 1 159  GLY 159  142  142 GLY GLY A . n 
A 1 160  SER 160  143  143 SER SER A . n 
A 1 161  TYR 161  144  144 TYR TYR A . n 
A 1 162  ARG 162  145  145 ARG ARG A . n 
A 1 163  SER 163  146  146 SER SER A . n 
A 1 164  GLU 164  147  147 GLU GLU A . n 
A 1 165  GLU 165  148  148 GLU GLU A . n 
A 1 166  LEU 166  149  149 LEU LEU A . n 
A 1 167  ASN 167  150  150 ASN ASN A . n 
A 1 168  LEU 168  151  151 LEU LEU A . n 
A 1 169  VAL 169  152  152 VAL VAL A . n 
A 1 170  ILE 170  153  153 ILE ILE A . n 
A 1 171  ILE 171  154  154 ILE ILE A . n 
A 1 172  GLY 172  155  155 GLY GLY A . n 
A 1 173  PRO 173  156  156 PRO PRO A . n 
A 1 174  SER 174  157  157 SER SER A . n 
A 1 175  ALA 175  158  158 ALA ALA A . n 
A 1 176  ASP 176  159  159 ASP ASP A . n 
A 1 177  ILE 177  160  160 ILE ILE A . n 
A 1 178  ILE 178  161  161 ILE ILE A . n 
A 1 179  GLN 179  162  162 GLN GLN A . n 
A 1 180  PHE 180  163  163 PHE PHE A . n 
A 1 181  GLU 181  164  164 GLU GLU A . n 
A 1 182  CYS 182  165  165 CYS CYS A . n 
A 1 183  LYS 183  166  166 LYS LYS A . n 
A 1 184  SER 184  167  167 SER SER A . n 
A 1 185  PHE 185  168  168 PHE PHE A . n 
A 1 186  GLY 186  169  169 GLY GLY A . n 
A 1 187  HIS 187  170  170 HIS HIS A . n 
A 1 188  GLU 188  171  171 GLU GLU A . n 
A 1 189  VAL 189  172  172 VAL VAL A . n 
A 1 190  LEU 190  173  173 LEU LEU A . n 
A 1 191  ASN 191  174  174 ASN ASN A . n 
A 1 192  LEU 192  175  175 LEU LEU A . n 
A 1 193  THR 193  176  176 THR THR A . n 
A 1 194  ARG 194  177  177 ARG ARG A . n 
A 1 195  ASN 195  178  178 ASN ASN A . n 
A 1 196  GLY 196  179  179 GLY GLY A . n 
A 1 197  TYR 197  180  180 TYR TYR A . n 
A 1 198  GLY 198  181  181 GLY GLY A . n 
A 1 199  SER 199  182  182 SER SER A . n 
A 1 200  THR 200  183  183 THR THR A . n 
A 1 201  GLN 201  184  184 GLN GLN A . n 
A 1 202  TYR 202  185  185 TYR TYR A . n 
A 1 203  ILE 203  186  186 ILE ILE A . n 
A 1 204  ARG 204  187  187 ARG ARG A . n 
A 1 205  PHE 205  188  188 PHE PHE A . n 
A 1 206  SER 206  189  189 SER SER A . n 
A 1 207  PRO 207  190  190 PRO PRO A . n 
A 1 208  ASP 208  191  191 ASP ASP A . n 
A 1 209  PHE 209  192  192 PHE PHE A . n 
A 1 210  THR 210  193  193 THR THR A . n 
A 1 211  PHE 211  194  194 PHE PHE A . n 
A 1 212  GLY 212  195  195 GLY GLY A . n 
A 1 213  PHE 213  196  196 PHE PHE A . n 
A 1 214  GLU 214  197  197 GLU GLU A . n 
A 1 215  GLU 215  198  198 GLU GLU A . n 
A 1 216  SER 216  199  199 SER SER A . n 
A 1 217  LEU 217  200  200 LEU LEU A . n 
A 1 218  GLU 218  201  201 GLU GLU A . n 
A 1 219  VAL 219  202  202 VAL VAL A . n 
A 1 220  ASP 220  203  203 ASP ASP A . n 
A 1 221  THR 221  204  204 THR THR A . n 
A 1 222  ASN 222  205  205 ASN ASN A . n 
A 1 223  PRO 223  206  206 PRO PRO A . n 
A 1 224  LEU 224  207  207 LEU LEU A . n 
A 1 225  LEU 225  208  208 LEU LEU A . n 
A 1 226  GLY 226  209  209 GLY GLY A . n 
A 1 227  ALA 227  210  210 ALA ALA A . n 
A 1 228  GLY 228  211  211 GLY GLY A . n 
A 1 229  LYS 229  212  212 LYS LYS A . n 
A 1 230  PHE 230  213  213 PHE PHE A . n 
A 1 231  ALA 231  214  214 ALA ALA A . n 
A 1 232  THR 232  215  215 THR THR A . n 
A 1 233  ASP 233  216  216 ASP ASP A . n 
A 1 234  PRO 234  217  217 PRO PRO A . n 
A 1 235  ALA 235  218  218 ALA ALA A . n 
A 1 236  VAL 236  219  219 VAL VAL A . n 
A 1 237  THR 237  220  220 THR THR A . n 
A 1 238  LEU 238  221  221 LEU LEU A . n 
A 1 239  ALA 239  222  222 ALA ALA A . n 
A 1 240  HIS 240  223  223 HIS HIS A . n 
A 1 241  GLN 241  224  224 GLN GLN A . n 
A 1 242  LEU 242  225  225 LEU LEU A . n 
A 1 243  ILE 243  226  226 ILE ILE A . n 
A 1 244  HIS 244  227  227 HIS HIS A . n 
A 1 245  ALA 245  228  228 ALA ALA A . n 
A 1 246  GLY 246  229  229 GLY GLY A . n 
A 1 247  HIS 247  230  230 HIS HIS A . n 
A 1 248  ARG 248  231  231 ARG ARG A . n 
A 1 249  LEU 249  232  232 LEU LEU A . n 
A 1 250  TYR 250  233  233 TYR TYR A . n 
A 1 251  GLY 251  234  234 GLY GLY A . n 
A 1 252  ILE 252  235  235 ILE ILE A . n 
A 1 253  ALA 253  236  236 ALA ALA A . n 
A 1 254  ILE 254  237  237 ILE ILE A . n 
A 1 255  ASN 255  238  238 ASN ASN A . n 
A 1 256  PRO 256  239  239 PRO PRO A . n 
A 1 257  ASN 257  240  240 ASN ASN A . n 
A 1 258  ARG 258  241  241 ARG ARG A . n 
A 1 259  VAL 259  242  242 VAL VAL A . n 
A 1 260  PHE 260  243  243 PHE PHE A . n 
A 1 261  LYS 261  244  244 LYS LYS A . n 
A 1 262  VAL 262  245  245 VAL VAL A . n 
A 1 263  ASN 263  246  246 ASN ASN A . n 
A 1 264  THR 264  247  247 THR THR A . n 
A 1 265  ASN 265  248  248 ASN ASN A . n 
A 1 266  ALA 266  249  249 ALA ALA A . n 
A 1 267  TYR 267  250  250 TYR TYR A . n 
A 1 268  TYR 268  251  251 TYR TYR A . n 
A 1 269  GLU 269  252  252 GLU GLU A . n 
A 1 270  MET 270  253  253 MET MET A . n 
A 1 271  SER 271  254  254 SER SER A . n 
A 1 272  GLY 272  255  255 GLY GLY A . n 
A 1 273  LEU 273  256  256 LEU LEU A . n 
A 1 274  GLU 274  257  257 GLU GLU A . n 
A 1 275  VAL 275  258  258 VAL VAL A . n 
A 1 276  SER 276  259  259 SER SER A . n 
A 1 277  PHE 277  260  260 PHE PHE A . n 
A 1 278  GLU 278  261  261 GLU GLU A . n 
A 1 279  GLU 279  262  262 GLU GLU A . n 
A 1 280  LEU 280  263  263 LEU LEU A . n 
A 1 281  ARG 281  264  264 ARG ARG A . n 
A 1 282  THR 282  265  265 THR THR A . n 
A 1 283  PHE 283  266  266 PHE PHE A . n 
A 1 284  GLY 284  267  267 GLY GLY A . n 
A 1 285  GLY 285  268  268 GLY GLY A . n 
A 1 286  HIS 286  269  269 HIS HIS A . n 
A 1 287  ASP 287  270  270 ASP ASP A . n 
A 1 288  ALA 288  271  271 ALA ALA A . n 
A 1 289  LYS 289  272  272 LYS LYS A . n 
A 1 290  PHE 290  273  273 PHE PHE A . n 
A 1 291  ILE 291  274  274 ILE ILE A . n 
A 1 292  ASP 292  275  275 ASP ASP A . n 
A 1 293  SER 293  276  276 SER SER A . n 
A 1 294  LEU 294  277  277 LEU LEU A . n 
A 1 295  GLN 295  278  278 GLN GLN A . n 
A 1 296  GLU 296  279  279 GLU GLU A . n 
A 1 297  ASN 297  280  280 ASN ASN A . n 
A 1 298  GLU 298  281  281 GLU GLU A . n 
A 1 299  PHE 299  282  282 PHE PHE A . n 
A 1 300  ARG 300  283  283 ARG ARG A . n 
A 1 301  LEU 301  284  284 LEU LEU A . n 
A 1 302  TYR 302  285  285 TYR TYR A . n 
A 1 303  TYR 303  286  286 TYR TYR A . n 
A 1 304  TYR 304  287  287 TYR TYR A . n 
A 1 305  ASN 305  288  288 ASN ASN A . n 
A 1 306  LYS 306  289  289 LYS LYS A . n 
A 1 307  PHE 307  290  290 PHE PHE A . n 
A 1 308  LYS 308  291  291 LYS LYS A . n 
A 1 309  ASP 309  292  292 ASP ASP A . n 
A 1 310  ILE 310  293  293 ILE ILE A . n 
A 1 311  ALA 311  294  294 ALA ALA A . n 
A 1 312  SER 312  295  295 SER SER A . n 
A 1 313  THR 313  296  296 THR THR A . n 
A 1 314  LEU 314  297  297 LEU LEU A . n 
A 1 315  ASN 315  298  298 ASN ASN A . n 
A 1 316  LYS 316  299  299 LYS LYS A . n 
A 1 317  ALA 317  300  300 ALA ALA A . n 
A 1 318  LYS 318  301  301 LYS LYS A . n 
A 1 319  SER 319  302  302 SER SER A . n 
A 1 320  ILE 320  303  303 ILE ILE A . n 
A 1 321  VAL 321  304  304 VAL VAL A . n 
A 1 322  GLY 322  305  305 GLY GLY A . n 
A 1 323  THR 323  306  306 THR THR A . n 
A 1 324  THR 324  307  307 THR THR A . n 
A 1 325  ALA 325  308  308 ALA ALA A . n 
A 1 326  SER 326  309  309 SER SER A . n 
A 1 327  LEU 327  310  310 LEU LEU A . n 
A 1 328  GLN 328  311  311 GLN GLN A . n 
A 1 329  TYR 329  312  312 TYR TYR A . n 
A 1 330  MET 330  313  313 MET MET A . n 
A 1 331  LYS 331  314  314 LYS LYS A . n 
A 1 332  ASN 332  315  315 ASN ASN A . n 
A 1 333  VAL 333  316  316 VAL VAL A . n 
A 1 334  PHE 334  317  317 PHE PHE A . n 
A 1 335  LYS 335  318  318 LYS LYS A . n 
A 1 336  GLU 336  319  319 GLU GLU A . n 
A 1 337  LYS 337  320  320 LYS LYS A . n 
A 1 338  TYR 338  321  321 TYR TYR A . n 
A 1 339  LEU 339  322  322 LEU LEU A . n 
A 1 340  LEU 340  323  323 LEU LEU A . n 
A 1 341  SER 341  324  324 SER SER A . n 
A 1 342  GLU 342  325  325 GLU GLU A . n 
A 1 343  ASP 343  326  326 ASP ASP A . n 
A 1 344  THR 344  327  327 THR THR A . n 
A 1 345  SER 345  328  328 SER SER A . n 
A 1 346  GLY 346  329  329 GLY GLY A . n 
A 1 347  LYS 347  330  330 LYS LYS A . n 
A 1 348  PHE 348  331  331 PHE PHE A . n 
A 1 349  SER 349  332  332 SER SER A . n 
A 1 350  VAL 350  333  333 VAL VAL A . n 
A 1 351  ASP 351  334  334 ASP ASP A . n 
A 1 352  LYS 352  335  335 LYS LYS A . n 
A 1 353  LEU 353  336  336 LEU LEU A . n 
A 1 354  LYS 354  337  337 LYS LYS A . n 
A 1 355  PHE 355  338  338 PHE PHE A . n 
A 1 356  ASP 356  339  339 ASP ASP A . n 
A 1 357  LYS 357  340  340 LYS LYS A . n 
A 1 358  LEU 358  341  341 LEU LEU A . n 
A 1 359  TYR 359  342  342 TYR TYR A . n 
A 1 360  LYS 360  343  343 LYS LYS A . n 
A 1 361  MET 361  344  344 MET MET A . n 
A 1 362  LEU 362  345  345 LEU LEU A . n 
A 1 363  THR 363  346  346 THR THR A . n 
A 1 364  GLU 364  347  347 GLU GLU A . n 
A 1 365  ILE 365  348  348 ILE ILE A . n 
A 1 366  TYR 366  349  349 TYR TYR A . n 
A 1 367  THR 367  350  350 THR THR A . n 
A 1 368  GLU 368  351  351 GLU GLU A . n 
A 1 369  ASP 369  352  352 ASP ASP A . n 
A 1 370  ASN 370  353  353 ASN ASN A . n 
A 1 371  PHE 371  354  354 PHE PHE A . n 
A 1 372  VAL 372  355  355 VAL VAL A . n 
A 1 373  LYS 373  356  356 LYS LYS A . n 
A 1 374  PHE 374  357  357 PHE PHE A . n 
A 1 375  PHE 375  358  358 PHE PHE A . n 
A 1 376  LYS 376  359  359 LYS LYS A . n 
A 1 377  VAL 377  360  360 VAL VAL A . n 
A 1 378  LEU 378  361  361 LEU LEU A . n 
A 1 379  ASN 379  362  362 ASN ASN A . n 
A 1 380  ALA 380  363  363 ALA ALA A . n 
A 1 381  LYS 381  364  364 LYS LYS A . n 
A 1 382  THR 382  365  365 THR THR A . n 
A 1 383  PHE 383  366  366 PHE PHE A . n 
A 1 384  LEU 384  367  367 LEU LEU A . n 
A 1 385  ASN 385  368  368 ASN ASN A . n 
A 1 386  PHE 386  369  369 PHE PHE A . n 
A 1 387  ASP 387  370  370 ASP ASP A . n 
A 1 388  LYS 388  371  371 LYS LYS A . n 
A 1 389  ALA 389  372  372 ALA ALA A . n 
A 1 390  VAL 390  373  373 VAL VAL A . n 
A 1 391  PHE 391  374  374 PHE PHE A . n 
A 1 392  LYS 392  375  375 LYS LYS A . n 
A 1 393  ILE 393  376  376 ILE ILE A . n 
A 1 394  ASN 394  377  377 ASN ASN A . n 
A 1 395  ILE 395  378  378 ILE ILE A . n 
A 1 396  VAL 396  379  379 VAL VAL A . n 
A 1 397  PRO 397  380  380 PRO PRO A . n 
A 1 398  LYS 398  381  381 LYS LYS A . n 
A 1 399  VAL 399  382  382 VAL VAL A . n 
A 1 400  ASN 400  383  383 ASN ASN A . n 
A 1 401  TYR 401  384  384 TYR TYR A . n 
A 1 402  THR 402  385  385 THR THR A . n 
A 1 403  ILE 403  386  386 ILE ILE A . n 
A 1 404  TYR 404  387  387 TYR TYR A . n 
A 1 405  ASP 405  388  388 ASP ASP A . n 
A 1 406  GLY 406  389  389 GLY GLY A . n 
A 1 407  PHE 407  390  390 PHE PHE A . n 
A 1 408  ASN 408  391  391 ASN ASN A . n 
A 1 409  LEU 409  392  392 LEU LEU A . n 
A 1 410  ARG 410  393  393 ARG ARG A . n 
A 1 411  ASN 411  394  394 ASN ASN A . n 
A 1 412  THR 412  395  395 THR THR A . n 
A 1 413  ASN 413  396  396 ASN ASN A . n 
A 1 414  LEU 414  397  397 LEU LEU A . n 
A 1 415  ALA 415  398  398 ALA ALA A . n 
A 1 416  ALA 416  399  399 ALA ALA A . n 
A 1 417  ASN 417  400  400 ASN ASN A . n 
A 1 418  PHE 418  401  401 PHE PHE A . n 
A 1 419  ASN 419  402  402 ASN ASN A . n 
A 1 420  GLY 420  403  403 GLY GLY A . n 
A 1 421  GLN 421  404  404 GLN GLN A . n 
A 1 422  ASN 422  405  405 ASN ASN A . n 
A 1 423  THR 423  406  406 THR THR A . n 
A 1 424  GLU 424  407  407 GLU GLU A . n 
A 1 425  ILE 425  408  408 ILE ILE A . n 
A 1 426  ASN 426  409  409 ASN ASN A . n 
A 1 427  ASN 427  410  410 ASN ASN A . n 
A 1 428  MET 428  411  411 MET MET A . n 
A 1 429  ASN 429  412  412 ASN ASN A . n 
A 1 430  PHE 430  413  413 PHE PHE A . n 
A 1 431  THR 431  414  414 THR THR A . n 
A 1 432  LYS 432  415  415 LYS LYS A . n 
A 1 433  LEU 433  416  416 LEU LEU A . n 
A 1 434  LYS 434  417  417 LYS LYS A . n 
A 1 435  ASN 435  418  418 ASN ASN A . n 
A 1 436  PHE 436  419  419 PHE PHE A . n 
A 1 437  THR 437  420  420 THR THR A . n 
A 1 438  GLY 438  421  421 GLY GLY A . n 
A 1 439  LEU 439  422  422 LEU LEU A . n 
A 1 440  PHE 440  423  423 PHE PHE A . n 
A 1 441  GLU 441  424  424 GLU GLU A . n 
A 1 442  PHE 442  425  425 PHE PHE A . n 
A 1 443  TYR 443  426  426 TYR TYR A . n 
A 1 444  LYS 444  427  427 LYS LYS A . n 
A 1 445  LEU 445  428  428 LEU LEU A . n 
A 1 446  LEU 446  429  429 LEU LEU A . n 
A 1 447  CYS 447  430  430 CYS CYS A . n 
A 1 448  VAL 448  431  431 VAL VAL A . n 
A 1 449  ARG 449  432  ?   ?   ?   A . n 
A 1 450  GLY 450  433  ?   ?   ?   A . n 
A 1 451  ILE 451  434  ?   ?   ?   A . n 
A 1 452  ILE 452  435  ?   ?   ?   A . n 
A 1 453  THR 453  436  ?   ?   ?   A . n 
A 1 454  SER 454  437  ?   ?   ?   A . n 
A 1 455  LYS 455  438  ?   ?   ?   A . n 
A 1 456  THR 456  439  ?   ?   ?   A . n 
A 1 457  LYS 457  440  ?   ?   ?   A . n 
A 1 458  SER 458  441  ?   ?   ?   A . n 
A 1 459  LEU 459  442  ?   ?   ?   A . n 
A 1 460  ASP 460  443  ?   ?   ?   A . n 
A 1 461  LYS 461  444  ?   ?   ?   A . n 
A 1 462  GLY 462  445  ?   ?   ?   A . n 
A 1 463  TYR 463  446  ?   ?   ?   A . n 
A 1 464  ASN 464  447  ?   ?   ?   A . n 
A 1 465  LYS 465  448  ?   ?   ?   A . n 
A 1 466  ALA 466  449  ?   ?   ?   A . n 
A 1 467  LEU 467  450  ?   ?   ?   A . n 
A 1 468  ASN 468  451  ?   ?   ?   A . n 
A 1 469  ASP 469  452  ?   ?   ?   A . n 
A 1 470  LEU 470  453  453 LEU LEU A . n 
A 1 471  CYS 471  454  454 CYS CYS A . n 
A 1 472  ILE 472  455  455 ILE ILE A . n 
A 1 473  LYS 473  456  456 LYS LYS A . n 
A 1 474  VAL 474  457  457 VAL VAL A . n 
A 1 475  ASN 475  458  458 ASN ASN A . n 
A 1 476  ASN 476  459  459 ASN ASN A . n 
A 1 477  TRP 477  460  460 TRP TRP A . n 
A 1 478  ASP 478  461  461 ASP ASP A . n 
A 1 479  LEU 479  462  462 LEU LEU A . n 
A 1 480  PHE 480  463  463 PHE PHE A . n 
A 1 481  PHE 481  464  464 PHE PHE A . n 
A 1 482  SER 482  465  465 SER SER A . n 
A 1 483  PRO 483  466  466 PRO PRO A . n 
A 1 484  SER 484  467  467 SER SER A . n 
A 1 485  GLU 485  468  468 GLU GLU A . n 
A 1 486  ASP 486  469  469 ASP ASP A . n 
A 1 487  ASN 487  470  470 ASN ASN A . n 
A 1 488  PHE 488  471  471 PHE PHE A . n 
A 1 489  THR 489  472  472 THR THR A . n 
A 1 490  ASN 490  473  473 ASN ASN A . n 
A 1 491  ASP 491  474  474 ASP ASP A . n 
A 1 492  LEU 492  475  475 LEU LEU A . n 
A 1 493  ASN 493  476  476 ASN ASN A . n 
A 1 494  LYS 494  477  477 LYS LYS A . n 
A 1 495  GLY 495  478  478 GLY GLY A . n 
A 1 496  GLU 496  479  479 GLU GLU A . n 
A 1 497  GLU 497  480  480 GLU GLU A . n 
A 1 498  ILE 498  481  481 ILE ILE A . n 
A 1 499  THR 499  482  482 THR THR A . n 
A 1 500  SER 500  483  483 SER SER A . n 
A 1 501  ASP 501  484  ?   ?   ?   A . n 
A 1 502  THR 502  485  ?   ?   ?   A . n 
A 1 503  ASN 503  486  ?   ?   ?   A . n 
A 1 504  ILE 504  487  ?   ?   ?   A . n 
A 1 505  GLU 505  488  ?   ?   ?   A . n 
A 1 506  ALA 506  489  ?   ?   ?   A . n 
A 1 507  ALA 507  490  ?   ?   ?   A . n 
A 1 508  GLU 508  491  ?   ?   ?   A . n 
A 1 509  GLU 509  492  ?   ?   ?   A . n 
A 1 510  ASN 510  493  ?   ?   ?   A . n 
A 1 511  ILE 511  494  ?   ?   ?   A . n 
A 1 512  SER 512  495  495 SER SER A . n 
A 1 513  LEU 513  496  496 LEU LEU A . n 
A 1 514  ASP 514  497  497 ASP ASP A . n 
A 1 515  LEU 515  498  498 LEU LEU A . n 
A 1 516  ILE 516  499  499 ILE ILE A . n 
A 1 517  GLN 517  500  500 GLN GLN A . n 
A 1 518  GLN 518  501  501 GLN GLN A . n 
A 1 519  TYR 519  502  502 TYR TYR A . n 
A 1 520  TYR 520  503  503 TYR TYR A . n 
A 1 521  LEU 521  504  504 LEU LEU A . n 
A 1 522  THR 522  505  505 THR THR A . n 
A 1 523  PHE 523  506  506 PHE PHE A . n 
A 1 524  ASN 524  507  507 ASN ASN A . n 
A 1 525  PHE 525  508  508 PHE PHE A . n 
A 1 526  ASP 526  509  509 ASP ASP A . n 
A 1 527  ASN 527  510  510 ASN ASN A . n 
A 1 528  GLU 528  511  511 GLU GLU A . n 
A 1 529  PRO 529  512  512 PRO PRO A . n 
A 1 530  GLU 530  513  513 GLU GLU A . n 
A 1 531  ASN 531  514  514 ASN ASN A . n 
A 1 532  ILE 532  515  515 ILE ILE A . n 
A 1 533  SER 533  516  516 SER SER A . n 
A 1 534  ILE 534  517  517 ILE ILE A . n 
A 1 535  GLU 535  518  518 GLU GLU A . n 
A 1 536  ASN 536  519  519 ASN ASN A . n 
A 1 537  LEU 537  520  520 LEU LEU A . n 
A 1 538  SER 538  521  521 SER SER A . n 
A 1 539  SER 539  522  522 SER SER A . n 
A 1 540  ASP 540  523  523 ASP ASP A . n 
A 1 541  ILE 541  524  524 ILE ILE A . n 
A 1 542  ILE 542  525  525 ILE ILE A . n 
A 1 543  GLY 543  526  526 GLY GLY A . n 
A 1 544  GLN 544  527  527 GLN GLN A . n 
A 1 545  LEU 545  528  528 LEU LEU A . n 
A 1 546  GLU 546  529  529 GLU GLU A . n 
A 1 547  LEU 547  530  530 LEU LEU A . n 
A 1 548  MET 548  531  531 MET MET A . n 
A 1 549  PRO 549  532  532 PRO PRO A . n 
A 1 550  ASN 550  533  533 ASN ASN A . n 
A 1 551  ILE 551  534  534 ILE ILE A . n 
A 1 552  GLU 552  535  535 GLU GLU A . n 
A 1 553  ARG 553  536  536 ARG ARG A . n 
A 1 554  PHE 554  537  537 PHE PHE A . n 
A 1 555  PRO 555  538  538 PRO PRO A . n 
A 1 556  ASN 556  539  539 ASN ASN A . n 
A 1 557  GLY 557  540  540 GLY GLY A . n 
A 1 558  LYS 558  541  541 LYS LYS A . n 
A 1 559  LYS 559  542  542 LYS LYS A . n 
A 1 560  TYR 560  543  543 TYR TYR A . n 
A 1 561  GLU 561  544  544 GLU GLU A . n 
A 1 562  LEU 562  545  545 LEU LEU A . n 
A 1 563  ASP 563  546  546 ASP ASP A . n 
A 1 564  LYS 564  547  547 LYS LYS A . n 
A 1 565  TYR 565  548  548 TYR TYR A . n 
A 1 566  THR 566  549  549 THR THR A . n 
A 1 567  MET 567  550  550 MET MET A . n 
A 1 568  PHE 568  551  551 PHE PHE A . n 
A 1 569  HIS 569  552  552 HIS HIS A . n 
A 1 570  TYR 570  553  553 TYR TYR A . n 
A 1 571  LEU 571  554  554 LEU LEU A . n 
A 1 572  ARG 572  555  555 ARG ARG A . n 
A 1 573  ALA 573  556  556 ALA ALA A . n 
A 1 574  GLN 574  557  557 GLN GLN A . n 
A 1 575  GLU 575  558  558 GLU GLU A . n 
A 1 576  PHE 576  559  559 PHE PHE A . n 
A 1 577  GLU 577  560  560 GLU GLU A . n 
A 1 578  HIS 578  561  561 HIS HIS A . n 
A 1 579  GLY 579  562  562 GLY GLY A . n 
A 1 580  LYS 580  563  563 LYS LYS A . n 
A 1 581  SER 581  564  564 SER SER A . n 
A 1 582  ARG 582  565  565 ARG ARG A . n 
A 1 583  ILE 583  566  566 ILE ILE A . n 
A 1 584  ALA 584  567  567 ALA ALA A . n 
A 1 585  LEU 585  568  568 LEU LEU A . n 
A 1 586  THR 586  569  569 THR THR A . n 
A 1 587  ASN 587  570  570 ASN ASN A . n 
A 1 588  SER 588  571  571 SER SER A . n 
A 1 589  VAL 589  572  572 VAL VAL A . n 
A 1 590  ASN 590  573  573 ASN ASN A . n 
A 1 591  GLU 591  574  574 GLU GLU A . n 
A 1 592  ALA 592  575  575 ALA ALA A . n 
A 1 593  LEU 593  576  576 LEU LEU A . n 
A 1 594  LEU 594  577  577 LEU LEU A . n 
A 1 595  ASN 595  578  578 ASN ASN A . n 
A 1 596  PRO 596  579  579 PRO PRO A . n 
A 1 597  SER 597  580  580 SER SER A . n 
A 1 598  ARG 598  581  581 ARG ARG A . n 
A 1 599  VAL 599  582  582 VAL VAL A . n 
A 1 600  TYR 600  583  583 TYR TYR A . n 
A 1 601  THR 601  584  584 THR THR A . n 
A 1 602  PHE 602  585  585 PHE PHE A . n 
A 1 603  PHE 603  586  586 PHE PHE A . n 
A 1 604  SER 604  587  587 SER SER A . n 
A 1 605  SER 605  588  588 SER SER A . n 
A 1 606  ASP 606  589  589 ASP ASP A . n 
A 1 607  TYR 607  590  590 TYR TYR A . n 
A 1 608  VAL 608  591  591 VAL VAL A . n 
A 1 609  LYS 609  592  592 LYS LYS A . n 
A 1 610  LYS 610  593  593 LYS LYS A . n 
A 1 611  VAL 611  594  594 VAL VAL A . n 
A 1 612  ASN 612  595  595 ASN ASN A . n 
A 1 613  LYS 613  596  596 LYS LYS A . n 
A 1 614  ALA 614  597  597 ALA ALA A . n 
A 1 615  THR 615  598  598 THR THR A . n 
A 1 616  GLU 616  599  599 GLU GLU A . n 
A 1 617  ALA 617  600  600 ALA ALA A . n 
A 1 618  ALA 618  601  601 ALA ALA A . n 
A 1 619  MET 619  602  602 MET MET A . n 
A 1 620  PHE 620  603  603 PHE PHE A . n 
A 1 621  LEU 621  604  604 LEU LEU A . n 
A 1 622  GLY 622  605  605 GLY GLY A . n 
A 1 623  TRP 623  606  606 TRP TRP A . n 
A 1 624  VAL 624  607  607 VAL VAL A . n 
A 1 625  GLU 625  608  608 GLU GLU A . n 
A 1 626  GLN 626  609  609 GLN GLN A . n 
A 1 627  LEU 627  610  610 LEU LEU A . n 
A 1 628  VAL 628  611  611 VAL VAL A . n 
A 1 629  TYR 629  612  612 TYR TYR A . n 
A 1 630  ASP 630  613  613 ASP ASP A . n 
A 1 631  PHE 631  614  614 PHE PHE A . n 
A 1 632  THR 632  615  615 THR THR A . n 
A 1 633  ASP 633  616  616 ASP ASP A . n 
A 1 634  GLU 634  617  617 GLU GLU A . n 
A 1 635  THR 635  618  618 THR THR A . n 
A 1 636  SER 636  619  619 SER SER A . n 
A 1 637  GLU 637  620  620 GLU GLU A . n 
A 1 638  VAL 638  621  621 VAL VAL A . n 
A 1 639  SER 639  622  622 SER SER A . n 
A 1 640  THR 640  623  623 THR THR A . n 
A 1 641  THR 641  624  624 THR THR A . n 
A 1 642  ASP 642  625  625 ASP ASP A . n 
A 1 643  LYS 643  626  626 LYS LYS A . n 
A 1 644  ILE 644  627  627 ILE ILE A . n 
A 1 645  ALA 645  628  628 ALA ALA A . n 
A 1 646  ASP 646  629  629 ASP ASP A . n 
A 1 647  ILE 647  630  630 ILE ILE A . n 
A 1 648  THR 648  631  631 THR THR A . n 
A 1 649  ILE 649  632  632 ILE ILE A . n 
A 1 650  ILE 650  633  633 ILE ILE A . n 
A 1 651  ILE 651  634  634 ILE ILE A . n 
A 1 652  PRO 652  635  635 PRO PRO A . n 
A 1 653  TYR 653  636  636 TYR TYR A . n 
A 1 654  ILE 654  637  637 ILE ILE A . n 
A 1 655  GLY 655  638  638 GLY GLY A . n 
A 1 656  PRO 656  639  639 PRO PRO A . n 
A 1 657  ALA 657  640  640 ALA ALA A . n 
A 1 658  LEU 658  641  641 LEU LEU A . n 
A 1 659  ASN 659  642  642 ASN ASN A . n 
A 1 660  ILE 660  643  643 ILE ILE A . n 
A 1 661  GLY 661  644  644 GLY GLY A . n 
A 1 662  ASN 662  645  645 ASN ASN A . n 
A 1 663  MET 663  646  646 MET MET A . n 
A 1 664  LEU 664  647  647 LEU LEU A . n 
A 1 665  TYR 665  648  648 TYR TYR A . n 
A 1 666  LYS 666  649  649 LYS LYS A . n 
A 1 667  ASP 667  650  650 ASP ASP A . n 
A 1 668  ASP 668  651  651 ASP ASP A . n 
A 1 669  PHE 669  652  652 PHE PHE A . n 
A 1 670  VAL 670  653  653 VAL VAL A . n 
A 1 671  GLY 671  654  654 GLY GLY A . n 
A 1 672  ALA 672  655  655 ALA ALA A . n 
A 1 673  LEU 673  656  656 LEU LEU A . n 
A 1 674  ILE 674  657  657 ILE ILE A . n 
A 1 675  PHE 675  658  658 PHE PHE A . n 
A 1 676  SER 676  659  659 SER SER A . n 
A 1 677  GLY 677  660  660 GLY GLY A . n 
A 1 678  ALA 678  661  661 ALA ALA A . n 
A 1 679  VAL 679  662  662 VAL VAL A . n 
A 1 680  ILE 680  663  663 ILE ILE A . n 
A 1 681  LEU 681  664  664 LEU LEU A . n 
A 1 682  LEU 682  665  665 LEU LEU A . n 
A 1 683  GLU 683  666  666 GLU GLU A . n 
A 1 684  PHE 684  667  667 PHE PHE A . n 
A 1 685  ILE 685  668  668 ILE ILE A . n 
A 1 686  PRO 686  669  669 PRO PRO A . n 
A 1 687  GLU 687  670  670 GLU GLU A . n 
A 1 688  ILE 688  671  671 ILE ILE A . n 
A 1 689  ALA 689  672  672 ALA ALA A . n 
A 1 690  ILE 690  673  673 ILE ILE A . n 
A 1 691  PRO 691  674  674 PRO PRO A . n 
A 1 692  VAL 692  675  675 VAL VAL A . n 
A 1 693  LEU 693  676  676 LEU LEU A . n 
A 1 694  GLY 694  677  677 GLY GLY A . n 
A 1 695  THR 695  678  678 THR THR A . n 
A 1 696  PHE 696  679  679 PHE PHE A . n 
A 1 697  ALA 697  680  680 ALA ALA A . n 
A 1 698  LEU 698  681  681 LEU LEU A . n 
A 1 699  VAL 699  682  682 VAL VAL A . n 
A 1 700  SER 700  683  683 SER SER A . n 
A 1 701  TYR 701  684  684 TYR TYR A . n 
A 1 702  ILE 702  685  685 ILE ILE A . n 
A 1 703  ALA 703  686  686 ALA ALA A . n 
A 1 704  ASN 704  687  687 ASN ASN A . n 
A 1 705  LYS 705  688  688 LYS LYS A . n 
A 1 706  VAL 706  689  689 VAL VAL A . n 
A 1 707  LEU 707  690  690 LEU LEU A . n 
A 1 708  THR 708  691  691 THR THR A . n 
A 1 709  VAL 709  692  692 VAL VAL A . n 
A 1 710  GLN 710  693  693 GLN GLN A . n 
A 1 711  THR 711  694  694 THR THR A . n 
A 1 712  ILE 712  695  695 ILE ILE A . n 
A 1 713  ASP 713  696  696 ASP ASP A . n 
A 1 714  ASN 714  697  697 ASN ASN A . n 
A 1 715  ALA 715  698  698 ALA ALA A . n 
A 1 716  LEU 716  699  699 LEU LEU A . n 
A 1 717  SER 717  700  700 SER SER A . n 
A 1 718  LYS 718  701  701 LYS LYS A . n 
A 1 719  ARG 719  702  702 ARG ARG A . n 
A 1 720  ASN 720  703  703 ASN ASN A . n 
A 1 721  GLU 721  704  704 GLU GLU A . n 
A 1 722  LYS 722  705  705 LYS LYS A . n 
A 1 723  TRP 723  706  706 TRP TRP A . n 
A 1 724  ASP 724  707  707 ASP ASP A . n 
A 1 725  GLU 725  708  708 GLU GLU A . n 
A 1 726  VAL 726  709  709 VAL VAL A . n 
A 1 727  TYR 727  710  710 TYR TYR A . n 
A 1 728  LYS 728  711  711 LYS LYS A . n 
A 1 729  TYR 729  712  712 TYR TYR A . n 
A 1 730  ILE 730  713  713 ILE ILE A . n 
A 1 731  VAL 731  714  714 VAL VAL A . n 
A 1 732  THR 732  715  715 THR THR A . n 
A 1 733  ASN 733  716  716 ASN ASN A . n 
A 1 734  TRP 734  717  717 TRP TRP A . n 
A 1 735  LEU 735  718  718 LEU LEU A . n 
A 1 736  ALA 736  719  719 ALA ALA A . n 
A 1 737  LYS 737  720  720 LYS LYS A . n 
A 1 738  VAL 738  721  721 VAL VAL A . n 
A 1 739  ASN 739  722  722 ASN ASN A . n 
A 1 740  THR 740  723  723 THR THR A . n 
A 1 741  GLN 741  724  724 GLN GLN A . n 
A 1 742  ILE 742  725  725 ILE ILE A . n 
A 1 743  ASP 743  726  726 ASP ASP A . n 
A 1 744  LEU 744  727  727 LEU LEU A . n 
A 1 745  ILE 745  728  728 ILE ILE A . n 
A 1 746  ARG 746  729  729 ARG ARG A . n 
A 1 747  LYS 747  730  730 LYS LYS A . n 
A 1 748  LYS 748  731  731 LYS LYS A . n 
A 1 749  MET 749  732  732 MET MET A . n 
A 1 750  LYS 750  733  733 LYS LYS A . n 
A 1 751  GLU 751  734  734 GLU GLU A . n 
A 1 752  ALA 752  735  735 ALA ALA A . n 
A 1 753  LEU 753  736  736 LEU LEU A . n 
A 1 754  GLU 754  737  737 GLU GLU A . n 
A 1 755  ASN 755  738  738 ASN ASN A . n 
A 1 756  GLN 756  739  739 GLN GLN A . n 
A 1 757  ALA 757  740  740 ALA ALA A . n 
A 1 758  GLU 758  741  741 GLU GLU A . n 
A 1 759  ALA 759  742  742 ALA ALA A . n 
A 1 760  THR 760  743  743 THR THR A . n 
A 1 761  LYS 761  744  744 LYS LYS A . n 
A 1 762  ALA 762  745  745 ALA ALA A . n 
A 1 763  ILE 763  746  746 ILE ILE A . n 
A 1 764  ILE 764  747  747 ILE ILE A . n 
A 1 765  ASN 765  748  748 ASN ASN A . n 
A 1 766  TYR 766  749  749 TYR TYR A . n 
A 1 767  GLN 767  750  750 GLN GLN A . n 
A 1 768  TYR 768  751  751 TYR TYR A . n 
A 1 769  ASN 769  752  752 ASN ASN A . n 
A 1 770  GLN 770  753  753 GLN GLN A . n 
A 1 771  TYR 771  754  754 TYR TYR A . n 
A 1 772  THR 772  755  755 THR THR A . n 
A 1 773  GLU 773  756  756 GLU GLU A . n 
A 1 774  GLU 774  757  757 GLU GLU A . n 
A 1 775  GLU 775  758  758 GLU GLU A . n 
A 1 776  LYS 776  759  759 LYS LYS A . n 
A 1 777  ASN 777  760  760 ASN ASN A . n 
A 1 778  ASN 778  761  761 ASN ASN A . n 
A 1 779  ILE 779  762  762 ILE ILE A . n 
A 1 780  ASN 780  763  763 ASN ASN A . n 
A 1 781  PHE 781  764  764 PHE PHE A . n 
A 1 782  ASN 782  765  765 ASN ASN A . n 
A 1 783  ILE 783  766  766 ILE ILE A . n 
A 1 784  ASP 784  767  767 ASP ASP A . n 
A 1 785  ASP 785  768  768 ASP ASP A . n 
A 1 786  LEU 786  769  769 LEU LEU A . n 
A 1 787  SER 787  770  770 SER SER A . n 
A 1 788  SER 788  771  771 SER SER A . n 
A 1 789  LYS 789  772  772 LYS LYS A . n 
A 1 790  LEU 790  773  773 LEU LEU A . n 
A 1 791  ASN 791  774  774 ASN ASN A . n 
A 1 792  GLU 792  775  775 GLU GLU A . n 
A 1 793  SER 793  776  776 SER SER A . n 
A 1 794  ILE 794  777  777 ILE ILE A . n 
A 1 795  ASN 795  778  778 ASN ASN A . n 
A 1 796  LYS 796  779  779 LYS LYS A . n 
A 1 797  ALA 797  780  780 ALA ALA A . n 
A 1 798  MET 798  781  781 MET MET A . n 
A 1 799  ILE 799  782  782 ILE ILE A . n 
A 1 800  ASN 800  783  783 ASN ASN A . n 
A 1 801  ILE 801  784  784 ILE ILE A . n 
A 1 802  ASN 802  785  785 ASN ASN A . n 
A 1 803  LYS 803  786  786 LYS LYS A . n 
A 1 804  PHE 804  787  787 PHE PHE A . n 
A 1 805  LEU 805  788  788 LEU LEU A . n 
A 1 806  ASN 806  789  789 ASN ASN A . n 
A 1 807  GLN 807  790  790 GLN GLN A . n 
A 1 808  CYS 808  791  791 CYS CYS A . n 
A 1 809  SER 809  792  792 SER SER A . n 
A 1 810  VAL 810  793  793 VAL VAL A . n 
A 1 811  SER 811  794  794 SER SER A . n 
A 1 812  TYR 812  795  795 TYR TYR A . n 
A 1 813  LEU 813  796  796 LEU LEU A . n 
A 1 814  MET 814  797  797 MET MET A . n 
A 1 815  ASN 815  798  798 ASN ASN A . n 
A 1 816  SER 816  799  799 SER SER A . n 
A 1 817  MET 817  800  800 MET MET A . n 
A 1 818  ILE 818  801  801 ILE ILE A . n 
A 1 819  PRO 819  802  802 PRO PRO A . n 
A 1 820  TYR 820  803  803 TYR TYR A . n 
A 1 821  GLY 821  804  804 GLY GLY A . n 
A 1 822  VAL 822  805  805 VAL VAL A . n 
A 1 823  LYS 823  806  806 LYS LYS A . n 
A 1 824  ARG 824  807  807 ARG ARG A . n 
A 1 825  LEU 825  808  808 LEU LEU A . n 
A 1 826  GLU 826  809  809 GLU GLU A . n 
A 1 827  ASP 827  810  810 ASP ASP A . n 
A 1 828  PHE 828  811  811 PHE PHE A . n 
A 1 829  ASP 829  812  812 ASP ASP A . n 
A 1 830  ALA 830  813  813 ALA ALA A . n 
A 1 831  SER 831  814  814 SER SER A . n 
A 1 832  LEU 832  815  815 LEU LEU A . n 
A 1 833  LYS 833  816  816 LYS LYS A . n 
A 1 834  ASP 834  817  817 ASP ASP A . n 
A 1 835  ALA 835  818  818 ALA ALA A . n 
A 1 836  LEU 836  819  819 LEU LEU A . n 
A 1 837  LEU 837  820  820 LEU LEU A . n 
A 1 838  LYS 838  821  821 LYS LYS A . n 
A 1 839  TYR 839  822  822 TYR TYR A . n 
A 1 840  ILE 840  823  823 ILE ILE A . n 
A 1 841  TYR 841  824  824 TYR TYR A . n 
A 1 842  ASP 842  825  ?   ?   ?   A . n 
A 1 843  ASN 843  826  ?   ?   ?   A . n 
A 1 844  ARG 844  827  ?   ?   ?   A . n 
A 1 845  GLY 845  828  ?   ?   ?   A . n 
A 1 846  THR 846  829  ?   ?   ?   A . n 
A 1 847  LEU 847  830  ?   ?   ?   A . n 
A 1 848  ILE 848  831  831 ILE ILE A . n 
A 1 849  GLY 849  832  832 GLY GLY A . n 
A 1 850  GLN 850  833  833 GLN GLN A . n 
A 1 851  VAL 851  834  834 VAL VAL A . n 
A 1 852  ASP 852  835  835 ASP ASP A . n 
A 1 853  ARG 853  836  836 ARG ARG A . n 
A 1 854  LEU 854  837  837 LEU LEU A . n 
A 1 855  LYS 855  838  838 LYS LYS A . n 
A 1 856  ASP 856  839  839 ASP ASP A . n 
A 1 857  LYS 857  840  840 LYS LYS A . n 
A 1 858  VAL 858  841  841 VAL VAL A . n 
A 1 859  ASN 859  842  842 ASN ASN A . n 
A 1 860  ASN 860  843  843 ASN ASN A . n 
A 1 861  THR 861  844  844 THR THR A . n 
A 1 862  LEU 862  845  845 LEU LEU A . n 
A 1 863  SER 863  846  846 SER SER A . n 
A 1 864  THR 864  847  847 THR THR A . n 
A 1 865  ASP 865  848  848 ASP ASP A . n 
A 1 866  ILE 866  849  849 ILE ILE A . n 
A 1 867  PRO 867  850  850 PRO PRO A . n 
A 1 868  PHE 868  851  851 PHE PHE A . n 
A 1 869  GLN 869  852  852 GLN GLN A . n 
A 1 870  LEU 870  853  853 LEU LEU A . n 
A 1 871  SER 871  854  854 SER SER A . n 
A 1 872  LYS 872  855  855 LYS LYS A . n 
A 1 873  TYR 873  856  856 TYR TYR A . n 
A 1 874  VAL 874  857  857 VAL VAL A . n 
A 1 875  ASP 875  858  858 ASP ASP A . n 
A 1 876  ASN 876  859  859 ASN ASN A . n 
A 1 877  GLN 877  860  860 GLN GLN A . n 
A 1 878  ARG 878  861  861 ARG ARG A . n 
A 1 879  LEU 879  862  862 LEU LEU A . n 
A 1 880  LEU 880  863  863 LEU LEU A . n 
A 1 881  SER 881  864  864 SER SER A . n 
A 1 882  THR 882  865  865 THR THR A . n 
A 1 883  PHE 883  866  866 PHE PHE A . n 
A 1 884  THR 884  867  867 THR THR A . n 
A 1 885  GLU 885  868  868 GLU GLU A . n 
A 1 886  TYR 886  869  869 TYR TYR A . n 
A 1 887  ILE 887  870  ?   ?   ?   A . n 
A 1 888  LYS 888  871  ?   ?   ?   A . n 
A 1 889  ASN 889  872  ?   ?   ?   A . n 
A 1 890  ILE 890  873  ?   ?   ?   A . n 
A 1 891  ILE 891  874  ?   ?   ?   A . n 
A 1 892  ASN 892  875  ?   ?   ?   A . n 
A 1 893  THR 893  876  ?   ?   ?   A . n 
A 1 894  SER 894  877  ?   ?   ?   A . n 
A 1 895  ILE 895  878  ?   ?   ?   A . n 
A 1 896  LEU 896  879  ?   ?   ?   A . n 
A 1 897  ASN 897  880  ?   ?   ?   A . n 
A 1 898  LEU 898  881  ?   ?   ?   A . n 
A 1 899  ARG 899  882  ?   ?   ?   A . n 
A 1 900  TYR 900  883  ?   ?   ?   A . n 
A 1 901  GLU 901  884  ?   ?   ?   A . n 
A 1 902  SER 902  885  ?   ?   ?   A . n 
A 1 903  ASN 903  886  ?   ?   ?   A . n 
A 1 904  HIS 904  887  ?   ?   ?   A . n 
A 1 905  LEU 905  888  ?   ?   ?   A . n 
A 1 906  ILE 906  889  ?   ?   ?   A . n 
A 1 907  ASP 907  890  ?   ?   ?   A . n 
A 1 908  LEU 908  891  ?   ?   ?   A . n 
A 1 909  SER 909  892  ?   ?   ?   A . n 
A 1 910  ARG 910  893  ?   ?   ?   A . n 
A 1 911  TYR 911  894  ?   ?   ?   A . n 
A 1 912  ALA 912  895  ?   ?   ?   A . n 
A 1 913  SER 913  896  ?   ?   ?   A . n 
A 1 914  LYS 914  897  ?   ?   ?   A . n 
A 1 915  ILE 915  898  ?   ?   ?   A . n 
A 1 916  ASN 916  899  ?   ?   ?   A . n 
A 1 917  ILE 917  900  ?   ?   ?   A . n 
A 1 918  GLY 918  901  ?   ?   ?   A . n 
A 1 919  SER 919  902  ?   ?   ?   A . n 
A 1 920  LYS 920  903  ?   ?   ?   A . n 
A 1 921  VAL 921  904  ?   ?   ?   A . n 
A 1 922  ASN 922  905  ?   ?   ?   A . n 
A 1 923  PHE 923  906  ?   ?   ?   A . n 
A 1 924  ASP 924  907  ?   ?   ?   A . n 
A 1 925  PRO 925  908  ?   ?   ?   A . n 
A 1 926  ILE 926  909  ?   ?   ?   A . n 
A 1 927  ASP 927  910  ?   ?   ?   A . n 
A 1 928  LYS 928  911  ?   ?   ?   A . n 
A 1 929  ASN 929  912  ?   ?   ?   A . n 
A 1 930  GLN 930  913  ?   ?   ?   A . n 
A 1 931  ILE 931  914  ?   ?   ?   A . n 
A 1 932  GLN 932  915  ?   ?   ?   A . n 
A 1 933  LEU 933  916  ?   ?   ?   A . n 
A 1 934  PHE 934  917  ?   ?   ?   A . n 
A 1 935  ASN 935  918  ?   ?   ?   A . n 
A 1 936  LEU 936  919  ?   ?   ?   A . n 
A 1 937  GLU 937  920  ?   ?   ?   A . n 
A 1 938  SER 938  921  ?   ?   ?   A . n 
A 1 939  SER 939  922  ?   ?   ?   A . n 
A 1 940  LYS 940  923  ?   ?   ?   A . n 
A 1 941  ILE 941  924  ?   ?   ?   A . n 
A 1 942  GLU 942  925  ?   ?   ?   A . n 
A 1 943  VAL 943  926  ?   ?   ?   A . n 
A 1 944  ILE 944  927  ?   ?   ?   A . n 
A 1 945  LEU 945  928  ?   ?   ?   A . n 
A 1 946  LYS 946  929  ?   ?   ?   A . n 
A 1 947  ASN 947  930  ?   ?   ?   A . n 
A 1 948  ALA 948  931  ?   ?   ?   A . n 
A 1 949  ILE 949  932  ?   ?   ?   A . n 
A 1 950  VAL 950  933  ?   ?   ?   A . n 
A 1 951  TYR 951  934  ?   ?   ?   A . n 
A 1 952  ASN 952  935  ?   ?   ?   A . n 
A 1 953  SER 953  936  ?   ?   ?   A . n 
A 1 954  MET 954  937  ?   ?   ?   A . n 
A 1 955  TYR 955  938  ?   ?   ?   A . n 
A 1 956  GLU 956  939  ?   ?   ?   A . n 
A 1 957  ASN 957  940  ?   ?   ?   A . n 
A 1 958  PHE 958  941  ?   ?   ?   A . n 
A 1 959  SER 959  942  ?   ?   ?   A . n 
A 1 960  THR 960  943  ?   ?   ?   A . n 
A 1 961  SER 961  944  ?   ?   ?   A . n 
A 1 962  PHE 962  945  ?   ?   ?   A . n 
A 1 963  TRP 963  946  ?   ?   ?   A . n 
A 1 964  ILE 964  947  ?   ?   ?   A . n 
A 1 965  ARG 965  948  ?   ?   ?   A . n 
A 1 966  ILE 966  949  ?   ?   ?   A . n 
A 1 967  PRO 967  950  ?   ?   ?   A . n 
A 1 968  LYS 968  951  ?   ?   ?   A . n 
A 1 969  TYR 969  952  ?   ?   ?   A . n 
A 1 970  PHE 970  953  ?   ?   ?   A . n 
A 1 971  ASN 971  954  ?   ?   ?   A . n 
A 1 972  SER 972  955  ?   ?   ?   A . n 
A 1 973  ILE 973  956  ?   ?   ?   A . n 
A 1 974  SER 974  957  ?   ?   ?   A . n 
A 1 975  LEU 975  958  ?   ?   ?   A . n 
A 1 976  ASN 976  959  ?   ?   ?   A . n 
A 1 977  ASN 977  960  ?   ?   ?   A . n 
A 1 978  GLU 978  961  ?   ?   ?   A . n 
A 1 979  TYR 979  962  ?   ?   ?   A . n 
A 1 980  THR 980  963  ?   ?   ?   A . n 
A 1 981  ILE 981  964  ?   ?   ?   A . n 
A 1 982  ILE 982  965  ?   ?   ?   A . n 
A 1 983  ASN 983  966  ?   ?   ?   A . n 
A 1 984  CYS 984  967  ?   ?   ?   A . n 
A 1 985  MET 985  968  ?   ?   ?   A . n 
A 1 986  GLU 986  969  ?   ?   ?   A . n 
A 1 987  ASN 987  970  ?   ?   ?   A . n 
A 1 988  ASN 988  971  ?   ?   ?   A . n 
A 1 989  SER 989  972  ?   ?   ?   A . n 
A 1 990  GLY 990  973  ?   ?   ?   A . n 
A 1 991  TRP 991  974  ?   ?   ?   A . n 
A 1 992  LYS 992  975  ?   ?   ?   A . n 
A 1 993  VAL 993  976  ?   ?   ?   A . n 
A 1 994  SER 994  977  ?   ?   ?   A . n 
A 1 995  LEU 995  978  ?   ?   ?   A . n 
A 1 996  ASN 996  979  ?   ?   ?   A . n 
A 1 997  TYR 997  980  ?   ?   ?   A . n 
A 1 998  GLY 998  981  ?   ?   ?   A . n 
A 1 999  GLU 999  982  ?   ?   ?   A . n 
A 1 1000 ILE 1000 983  ?   ?   ?   A . n 
A 1 1001 ILE 1001 984  ?   ?   ?   A . n 
A 1 1002 TRP 1002 985  ?   ?   ?   A . n 
A 1 1003 THR 1003 986  ?   ?   ?   A . n 
A 1 1004 LEU 1004 987  ?   ?   ?   A . n 
A 1 1005 GLN 1005 988  ?   ?   ?   A . n 
A 1 1006 ASP 1006 989  ?   ?   ?   A . n 
A 1 1007 THR 1007 990  ?   ?   ?   A . n 
A 1 1008 GLN 1008 991  ?   ?   ?   A . n 
A 1 1009 GLU 1009 992  ?   ?   ?   A . n 
A 1 1010 ILE 1010 993  ?   ?   ?   A . n 
A 1 1011 LYS 1011 994  ?   ?   ?   A . n 
A 1 1012 GLN 1012 995  ?   ?   ?   A . n 
A 1 1013 ARG 1013 996  ?   ?   ?   A . n 
A 1 1014 VAL 1014 997  ?   ?   ?   A . n 
A 1 1015 VAL 1015 998  ?   ?   ?   A . n 
A 1 1016 PHE 1016 999  ?   ?   ?   A . n 
A 1 1017 LYS 1017 1000 ?   ?   ?   A . n 
A 1 1018 TYR 1018 1001 ?   ?   ?   A . n 
A 1 1019 SER 1019 1002 ?   ?   ?   A . n 
A 1 1020 GLN 1020 1003 ?   ?   ?   A . n 
A 1 1021 MET 1021 1004 ?   ?   ?   A . n 
A 1 1022 ILE 1022 1005 ?   ?   ?   A . n 
A 1 1023 ASN 1023 1006 ?   ?   ?   A . n 
A 1 1024 ILE 1024 1007 ?   ?   ?   A . n 
A 1 1025 SER 1025 1008 ?   ?   ?   A . n 
A 1 1026 ASP 1026 1009 ?   ?   ?   A . n 
A 1 1027 TYR 1027 1010 ?   ?   ?   A . n 
A 1 1028 ILE 1028 1011 ?   ?   ?   A . n 
A 1 1029 ASN 1029 1012 ?   ?   ?   A . n 
A 1 1030 ARG 1030 1013 ?   ?   ?   A . n 
A 1 1031 TRP 1031 1014 ?   ?   ?   A . n 
A 1 1032 ILE 1032 1015 ?   ?   ?   A . n 
A 1 1033 PHE 1033 1016 ?   ?   ?   A . n 
A 1 1034 VAL 1034 1017 ?   ?   ?   A . n 
A 1 1035 THR 1035 1018 ?   ?   ?   A . n 
A 1 1036 ILE 1036 1019 ?   ?   ?   A . n 
A 1 1037 THR 1037 1020 ?   ?   ?   A . n 
A 1 1038 ASN 1038 1021 ?   ?   ?   A . n 
A 1 1039 ASN 1039 1022 ?   ?   ?   A . n 
A 1 1040 ARG 1040 1023 ?   ?   ?   A . n 
A 1 1041 LEU 1041 1024 ?   ?   ?   A . n 
A 1 1042 ASN 1042 1025 ?   ?   ?   A . n 
A 1 1043 ASN 1043 1026 ?   ?   ?   A . n 
A 1 1044 SER 1044 1027 ?   ?   ?   A . n 
A 1 1045 LYS 1045 1028 ?   ?   ?   A . n 
A 1 1046 ILE 1046 1029 ?   ?   ?   A . n 
A 1 1047 TYR 1047 1030 ?   ?   ?   A . n 
A 1 1048 ILE 1048 1031 ?   ?   ?   A . n 
A 1 1049 ASN 1049 1032 ?   ?   ?   A . n 
A 1 1050 GLY 1050 1033 ?   ?   ?   A . n 
A 1 1051 ARG 1051 1034 ?   ?   ?   A . n 
A 1 1052 LEU 1052 1035 ?   ?   ?   A . n 
A 1 1053 ILE 1053 1036 ?   ?   ?   A . n 
A 1 1054 ASP 1054 1037 ?   ?   ?   A . n 
A 1 1055 GLN 1055 1038 ?   ?   ?   A . n 
A 1 1056 LYS 1056 1039 ?   ?   ?   A . n 
A 1 1057 PRO 1057 1040 ?   ?   ?   A . n 
A 1 1058 ILE 1058 1041 ?   ?   ?   A . n 
A 1 1059 SER 1059 1042 ?   ?   ?   A . n 
A 1 1060 ASN 1060 1043 ?   ?   ?   A . n 
A 1 1061 LEU 1061 1044 ?   ?   ?   A . n 
A 1 1062 GLY 1062 1045 ?   ?   ?   A . n 
A 1 1063 ASN 1063 1046 ?   ?   ?   A . n 
A 1 1064 ILE 1064 1047 ?   ?   ?   A . n 
A 1 1065 HIS 1065 1048 ?   ?   ?   A . n 
A 1 1066 ALA 1066 1049 ?   ?   ?   A . n 
A 1 1067 SER 1067 1050 ?   ?   ?   A . n 
A 1 1068 ASN 1068 1051 ?   ?   ?   A . n 
A 1 1069 ASN 1069 1052 ?   ?   ?   A . n 
A 1 1070 ILE 1070 1053 ?   ?   ?   A . n 
A 1 1071 MET 1071 1054 ?   ?   ?   A . n 
A 1 1072 PHE 1072 1055 ?   ?   ?   A . n 
A 1 1073 LYS 1073 1056 ?   ?   ?   A . n 
A 1 1074 LEU 1074 1057 ?   ?   ?   A . n 
A 1 1075 ASP 1075 1058 ?   ?   ?   A . n 
A 1 1076 GLY 1076 1059 ?   ?   ?   A . n 
A 1 1077 CYS 1077 1060 ?   ?   ?   A . n 
A 1 1078 ARG 1078 1061 ?   ?   ?   A . n 
A 1 1079 ASP 1079 1062 ?   ?   ?   A . n 
A 1 1080 THR 1080 1063 ?   ?   ?   A . n 
A 1 1081 HIS 1081 1064 ?   ?   ?   A . n 
A 1 1082 ARG 1082 1065 ?   ?   ?   A . n 
A 1 1083 TYR 1083 1066 ?   ?   ?   A . n 
A 1 1084 ILE 1084 1067 ?   ?   ?   A . n 
A 1 1085 TRP 1085 1068 ?   ?   ?   A . n 
A 1 1086 ILE 1086 1069 ?   ?   ?   A . n 
A 1 1087 LYS 1087 1070 ?   ?   ?   A . n 
A 1 1088 TYR 1088 1071 ?   ?   ?   A . n 
A 1 1089 PHE 1089 1072 ?   ?   ?   A . n 
A 1 1090 ASN 1090 1073 ?   ?   ?   A . n 
A 1 1091 LEU 1091 1074 ?   ?   ?   A . n 
A 1 1092 PHE 1092 1075 ?   ?   ?   A . n 
A 1 1093 ASP 1093 1076 ?   ?   ?   A . n 
A 1 1094 LYS 1094 1077 ?   ?   ?   A . n 
A 1 1095 GLU 1095 1078 ?   ?   ?   A . n 
A 1 1096 LEU 1096 1079 ?   ?   ?   A . n 
A 1 1097 ASN 1097 1080 ?   ?   ?   A . n 
A 1 1098 GLU 1098 1081 ?   ?   ?   A . n 
A 1 1099 LYS 1099 1082 ?   ?   ?   A . n 
A 1 1100 GLU 1100 1083 ?   ?   ?   A . n 
A 1 1101 ILE 1101 1084 ?   ?   ?   A . n 
A 1 1102 LYS 1102 1085 ?   ?   ?   A . n 
A 1 1103 ASP 1103 1086 ?   ?   ?   A . n 
A 1 1104 LEU 1104 1087 ?   ?   ?   A . n 
A 1 1105 TYR 1105 1088 ?   ?   ?   A . n 
A 1 1106 ASP 1106 1089 ?   ?   ?   A . n 
A 1 1107 ASN 1107 1090 ?   ?   ?   A . n 
A 1 1108 GLN 1108 1091 ?   ?   ?   A . n 
A 1 1109 SER 1109 1092 ?   ?   ?   A . n 
A 1 1110 ASN 1110 1093 ?   ?   ?   A . n 
A 1 1111 SER 1111 1094 ?   ?   ?   A . n 
A 1 1112 GLY 1112 1095 ?   ?   ?   A . n 
A 1 1113 ILE 1113 1096 ?   ?   ?   A . n 
A 1 1114 LEU 1114 1097 ?   ?   ?   A . n 
A 1 1115 LYS 1115 1098 ?   ?   ?   A . n 
A 1 1116 ASP 1116 1099 ?   ?   ?   A . n 
A 1 1117 PHE 1117 1100 ?   ?   ?   A . n 
A 1 1118 TRP 1118 1101 ?   ?   ?   A . n 
A 1 1119 GLY 1119 1102 ?   ?   ?   A . n 
A 1 1120 ASP 1120 1103 ?   ?   ?   A . n 
A 1 1121 TYR 1121 1104 ?   ?   ?   A . n 
A 1 1122 LEU 1122 1105 ?   ?   ?   A . n 
A 1 1123 GLN 1123 1106 ?   ?   ?   A . n 
A 1 1124 TYR 1124 1107 ?   ?   ?   A . n 
A 1 1125 ASP 1125 1108 ?   ?   ?   A . n 
A 1 1126 LYS 1126 1109 ?   ?   ?   A . n 
A 1 1127 PRO 1127 1110 ?   ?   ?   A . n 
A 1 1128 TYR 1128 1111 ?   ?   ?   A . n 
A 1 1129 TYR 1129 1112 ?   ?   ?   A . n 
A 1 1130 MET 1130 1113 ?   ?   ?   A . n 
A 1 1131 LEU 1131 1114 ?   ?   ?   A . n 
A 1 1132 ASN 1132 1115 ?   ?   ?   A . n 
A 1 1133 LEU 1133 1116 ?   ?   ?   A . n 
A 1 1134 TYR 1134 1117 ?   ?   ?   A . n 
A 1 1135 ASP 1135 1118 ?   ?   ?   A . n 
A 1 1136 PRO 1136 1119 ?   ?   ?   A . n 
A 1 1137 ASN 1137 1120 ?   ?   ?   A . n 
A 1 1138 LYS 1138 1121 ?   ?   ?   A . n 
A 1 1139 TYR 1139 1122 ?   ?   ?   A . n 
A 1 1140 VAL 1140 1123 ?   ?   ?   A . n 
A 1 1141 ASP 1141 1124 ?   ?   ?   A . n 
A 1 1142 VAL 1142 1125 ?   ?   ?   A . n 
A 1 1143 ASN 1143 1126 ?   ?   ?   A . n 
A 1 1144 ASN 1144 1127 ?   ?   ?   A . n 
A 1 1145 VAL 1145 1128 ?   ?   ?   A . n 
A 1 1146 GLY 1146 1129 ?   ?   ?   A . n 
A 1 1147 ILE 1147 1130 ?   ?   ?   A . n 
A 1 1148 ARG 1148 1131 ?   ?   ?   A . n 
A 1 1149 GLY 1149 1132 ?   ?   ?   A . n 
A 1 1150 TYR 1150 1133 ?   ?   ?   A . n 
A 1 1151 MET 1151 1134 ?   ?   ?   A . n 
A 1 1152 TYR 1152 1135 ?   ?   ?   A . n 
A 1 1153 LEU 1153 1136 ?   ?   ?   A . n 
A 1 1154 LYS 1154 1137 ?   ?   ?   A . n 
A 1 1155 GLY 1155 1138 ?   ?   ?   A . n 
A 1 1156 PRO 1156 1139 ?   ?   ?   A . n 
A 1 1157 ARG 1157 1140 ?   ?   ?   A . n 
A 1 1158 GLY 1158 1141 ?   ?   ?   A . n 
A 1 1159 SER 1159 1142 ?   ?   ?   A . n 
A 1 1160 VAL 1160 1143 ?   ?   ?   A . n 
A 1 1161 MET 1161 1144 ?   ?   ?   A . n 
A 1 1162 THR 1162 1145 ?   ?   ?   A . n 
A 1 1163 THR 1163 1146 ?   ?   ?   A . n 
A 1 1164 ASN 1164 1147 ?   ?   ?   A . n 
A 1 1165 ILE 1165 1148 ?   ?   ?   A . n 
A 1 1166 TYR 1166 1149 ?   ?   ?   A . n 
A 1 1167 LEU 1167 1150 ?   ?   ?   A . n 
A 1 1168 ASN 1168 1151 ?   ?   ?   A . n 
A 1 1169 SER 1169 1152 ?   ?   ?   A . n 
A 1 1170 SER 1170 1153 ?   ?   ?   A . n 
A 1 1171 LEU 1171 1154 ?   ?   ?   A . n 
A 1 1172 TYR 1172 1155 ?   ?   ?   A . n 
A 1 1173 ARG 1173 1156 ?   ?   ?   A . n 
A 1 1174 GLY 1174 1157 ?   ?   ?   A . n 
A 1 1175 ALA 1175 1158 ?   ?   ?   A . n 
A 1 1176 LYS 1176 1159 ?   ?   ?   A . n 
A 1 1177 PHE 1177 1160 ?   ?   ?   A . n 
A 1 1178 ILE 1178 1161 ?   ?   ?   A . n 
A 1 1179 ILE 1179 1162 ?   ?   ?   A . n 
A 1 1180 LYS 1180 1163 ?   ?   ?   A . n 
A 1 1181 LYS 1181 1164 ?   ?   ?   A . n 
A 1 1182 TYR 1182 1165 ?   ?   ?   A . n 
A 1 1183 ALA 1183 1166 ?   ?   ?   A . n 
A 1 1184 SER 1184 1167 ?   ?   ?   A . n 
A 1 1185 GLY 1185 1168 ?   ?   ?   A . n 
A 1 1186 ASN 1186 1169 ?   ?   ?   A . n 
A 1 1187 LYS 1187 1170 ?   ?   ?   A . n 
A 1 1188 ASP 1188 1171 ?   ?   ?   A . n 
A 1 1189 ASN 1189 1172 ?   ?   ?   A . n 
A 1 1190 ILE 1190 1173 ?   ?   ?   A . n 
A 1 1191 VAL 1191 1174 ?   ?   ?   A . n 
A 1 1192 ARG 1192 1175 ?   ?   ?   A . n 
A 1 1193 ASN 1193 1176 ?   ?   ?   A . n 
A 1 1194 ASN 1194 1177 ?   ?   ?   A . n 
A 1 1195 ASP 1195 1178 ?   ?   ?   A . n 
A 1 1196 ARG 1196 1179 ?   ?   ?   A . n 
A 1 1197 VAL 1197 1180 ?   ?   ?   A . n 
A 1 1198 TYR 1198 1181 ?   ?   ?   A . n 
A 1 1199 ILE 1199 1182 ?   ?   ?   A . n 
A 1 1200 ASN 1200 1183 ?   ?   ?   A . n 
A 1 1201 VAL 1201 1184 ?   ?   ?   A . n 
A 1 1202 VAL 1202 1185 ?   ?   ?   A . n 
A 1 1203 VAL 1203 1186 ?   ?   ?   A . n 
A 1 1204 LYS 1204 1187 ?   ?   ?   A . n 
A 1 1205 ASN 1205 1188 ?   ?   ?   A . n 
A 1 1206 LYS 1206 1189 ?   ?   ?   A . n 
A 1 1207 GLU 1207 1190 ?   ?   ?   A . n 
A 1 1208 TYR 1208 1191 ?   ?   ?   A . n 
A 1 1209 ARG 1209 1192 ?   ?   ?   A . n 
A 1 1210 LEU 1210 1193 ?   ?   ?   A . n 
A 1 1211 ALA 1211 1194 ?   ?   ?   A . n 
A 1 1212 THR 1212 1195 ?   ?   ?   A . n 
A 1 1213 ASN 1213 1196 ?   ?   ?   A . n 
A 1 1214 ALA 1214 1197 ?   ?   ?   A . n 
A 1 1215 SER 1215 1198 ?   ?   ?   A . n 
A 1 1216 GLN 1216 1199 ?   ?   ?   A . n 
A 1 1217 ALA 1217 1200 ?   ?   ?   A . n 
A 1 1218 GLY 1218 1201 ?   ?   ?   A . n 
A 1 1219 VAL 1219 1202 ?   ?   ?   A . n 
A 1 1220 GLU 1220 1203 ?   ?   ?   A . n 
A 1 1221 LYS 1221 1204 ?   ?   ?   A . n 
A 1 1222 ILE 1222 1205 ?   ?   ?   A . n 
A 1 1223 LEU 1223 1206 ?   ?   ?   A . n 
A 1 1224 SER 1224 1207 ?   ?   ?   A . n 
A 1 1225 ALA 1225 1208 ?   ?   ?   A . n 
A 1 1226 LEU 1226 1209 ?   ?   ?   A . n 
A 1 1227 GLU 1227 1210 ?   ?   ?   A . n 
A 1 1228 ILE 1228 1211 ?   ?   ?   A . n 
A 1 1229 PRO 1229 1212 ?   ?   ?   A . n 
A 1 1230 ASP 1230 1213 ?   ?   ?   A . n 
A 1 1231 VAL 1231 1214 ?   ?   ?   A . n 
A 1 1232 GLY 1232 1215 ?   ?   ?   A . n 
A 1 1233 ASN 1233 1216 ?   ?   ?   A . n 
A 1 1234 LEU 1234 1217 ?   ?   ?   A . n 
A 1 1235 SER 1235 1218 ?   ?   ?   A . n 
A 1 1236 GLN 1236 1219 ?   ?   ?   A . n 
A 1 1237 VAL 1237 1220 ?   ?   ?   A . n 
A 1 1238 VAL 1238 1221 ?   ?   ?   A . n 
A 1 1239 VAL 1239 1222 ?   ?   ?   A . n 
A 1 1240 MET 1240 1223 ?   ?   ?   A . n 
A 1 1241 LYS 1241 1224 ?   ?   ?   A . n 
A 1 1242 SER 1242 1225 ?   ?   ?   A . n 
A 1 1243 LYS 1243 1226 ?   ?   ?   A . n 
A 1 1244 ASN 1244 1227 ?   ?   ?   A . n 
A 1 1245 ASP 1245 1228 ?   ?   ?   A . n 
A 1 1246 GLN 1246 1229 ?   ?   ?   A . n 
A 1 1247 GLY 1247 1230 ?   ?   ?   A . n 
A 1 1248 ILE 1248 1231 ?   ?   ?   A . n 
A 1 1249 THR 1249 1232 ?   ?   ?   A . n 
A 1 1250 ASN 1250 1233 ?   ?   ?   A . n 
A 1 1251 LYS 1251 1234 ?   ?   ?   A . n 
A 1 1252 CYS 1252 1235 ?   ?   ?   A . n 
A 1 1253 LYS 1253 1236 ?   ?   ?   A . n 
A 1 1254 MET 1254 1237 ?   ?   ?   A . n 
A 1 1255 ASN 1255 1238 ?   ?   ?   A . n 
A 1 1256 LEU 1256 1239 ?   ?   ?   A . n 
A 1 1257 GLN 1257 1240 ?   ?   ?   A . n 
A 1 1258 ASP 1258 1241 ?   ?   ?   A . n 
A 1 1259 ASN 1259 1242 ?   ?   ?   A . n 
A 1 1260 ASN 1260 1243 ?   ?   ?   A . n 
A 1 1261 GLY 1261 1244 ?   ?   ?   A . n 
A 1 1262 ASN 1262 1245 ?   ?   ?   A . n 
A 1 1263 ASP 1263 1246 ?   ?   ?   A . n 
A 1 1264 ILE 1264 1247 ?   ?   ?   A . n 
A 1 1265 GLY 1265 1248 ?   ?   ?   A . n 
A 1 1266 PHE 1266 1249 ?   ?   ?   A . n 
A 1 1267 ILE 1267 1250 ?   ?   ?   A . n 
A 1 1268 GLY 1268 1251 ?   ?   ?   A . n 
A 1 1269 PHE 1269 1252 ?   ?   ?   A . n 
A 1 1270 HIS 1270 1253 ?   ?   ?   A . n 
A 1 1271 GLN 1271 1254 ?   ?   ?   A . n 
A 1 1272 PHE 1272 1255 ?   ?   ?   A . n 
A 1 1273 ASN 1273 1256 ?   ?   ?   A . n 
A 1 1274 ASN 1274 1257 ?   ?   ?   A . n 
A 1 1275 ILE 1275 1258 ?   ?   ?   A . n 
A 1 1276 ALA 1276 1259 ?   ?   ?   A . n 
A 1 1277 LYS 1277 1260 ?   ?   ?   A . n 
A 1 1278 LEU 1278 1261 ?   ?   ?   A . n 
A 1 1279 VAL 1279 1262 ?   ?   ?   A . n 
A 1 1280 ALA 1280 1263 ?   ?   ?   A . n 
A 1 1281 SER 1281 1264 ?   ?   ?   A . n 
A 1 1282 ASN 1282 1265 ?   ?   ?   A . n 
A 1 1283 TRP 1283 1266 ?   ?   ?   A . n 
A 1 1284 TYR 1284 1267 ?   ?   ?   A . n 
A 1 1285 ASN 1285 1268 ?   ?   ?   A . n 
A 1 1286 ARG 1286 1269 ?   ?   ?   A . n 
A 1 1287 GLN 1287 1270 ?   ?   ?   A . n 
A 1 1288 ILE 1288 1271 ?   ?   ?   A . n 
A 1 1289 GLU 1289 1272 ?   ?   ?   A . n 
A 1 1290 ARG 1290 1273 ?   ?   ?   A . n 
A 1 1291 SER 1291 1274 ?   ?   ?   A . n 
A 1 1292 SER 1292 1275 ?   ?   ?   A . n 
A 1 1293 ARG 1293 1276 ?   ?   ?   A . n 
A 1 1294 THR 1294 1277 ?   ?   ?   A . n 
A 1 1295 LEU 1295 1278 ?   ?   ?   A . n 
A 1 1296 GLY 1296 1279 ?   ?   ?   A . n 
A 1 1297 CYS 1297 1280 ?   ?   ?   A . n 
A 1 1298 SER 1298 1281 ?   ?   ?   A . n 
A 1 1299 TRP 1299 1282 ?   ?   ?   A . n 
A 1 1300 GLU 1300 1283 ?   ?   ?   A . n 
A 1 1301 PHE 1301 1284 ?   ?   ?   A . n 
A 1 1302 ILE 1302 1285 ?   ?   ?   A . n 
A 1 1303 PRO 1303 1286 ?   ?   ?   A . n 
A 1 1304 VAL 1304 1287 ?   ?   ?   A . n 
A 1 1305 ASP 1305 1288 ?   ?   ?   A . n 
A 1 1306 ASP 1306 1289 ?   ?   ?   A . n 
A 1 1307 GLY 1307 1290 ?   ?   ?   A . n 
A 1 1308 TRP 1308 1291 ?   ?   ?   A . n 
A 1 1309 GLY 1309 1292 ?   ?   ?   A . n 
A 1 1310 GLU 1310 1293 ?   ?   ?   A . n 
A 1 1311 ARG 1311 1294 ?   ?   ?   A . n 
A 1 1312 PRO 1312 1295 ?   ?   ?   A . n 
A 1 1313 LEU 1313 1296 ?   ?   ?   A . n 
A 1 1314 VAL 1314 1297 ?   ?   ?   A . n 
A 1 1315 PRO 1315 1298 ?   ?   ?   A . n 
A 1 1316 PRO 1316 1299 ?   ?   ?   A . n 
A 1 1317 THR 1317 1300 ?   ?   ?   A . n 
A 1 1318 PRO 1318 1301 ?   ?   ?   A . n 
A 1 1319 GLY 1319 1302 ?   ?   ?   A . n 
A 1 1320 SER 1320 1303 ?   ?   ?   A . n 
A 1 1321 ALA 1321 1304 ?   ?   ?   A . n 
A 1 1322 TRP 1322 1305 ?   ?   ?   A . n 
A 1 1323 SER 1323 1306 ?   ?   ?   A . n 
A 1 1324 HIS 1324 1307 ?   ?   ?   A . n 
A 1 1325 PRO 1325 1308 ?   ?   ?   A . n 
A 1 1326 GLN 1326 1309 ?   ?   ?   A . n 
A 1 1327 PHE 1327 1310 ?   ?   ?   A . n 
A 1 1328 GLU 1328 1311 ?   ?   ?   A . n 
A 1 1329 LYS 1329 1312 ?   ?   ?   A . n 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LEU 647 ? CG  ? A LEU 664 CG  
2  1 Y 1 A LEU 647 ? CD1 ? A LEU 664 CD1 
3  1 Y 1 A LEU 647 ? CD2 ? A LEU 664 CD2 
4  1 Y 1 A ILE 831 ? CG1 ? A ILE 848 CG1 
5  1 Y 1 A ILE 831 ? CG2 ? A ILE 848 CG2 
6  1 Y 1 A ILE 831 ? CD1 ? A ILE 848 CD1 
7  1 Y 1 A ARG 861 ? CG  ? A ARG 878 CG  
8  1 Y 1 A ARG 861 ? CD  ? A ARG 878 CD  
9  1 Y 1 A ARG 861 ? NE  ? A ARG 878 NE  
10 1 Y 1 A ARG 861 ? CZ  ? A ARG 878 CZ  
11 1 Y 1 A ARG 861 ? NH1 ? A ARG 878 NH1 
12 1 Y 1 A ARG 861 ? NH2 ? A ARG 878 NH2 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9F25 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     1.00 
_cell.length_a_esd                 ? 
_cell.length_b                     1.00 
_cell.length_b_esd                 ? 
_cell.length_c                     1.00 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        ? 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9F25 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9F25 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9F25 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            3.7 
_refine.ls_d_res_low                             ? 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               NONE 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS)' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'ELECTRON MICROSCOPY' ? 0.002  ? 6862 ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.528  ? 9294 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 16.769 ? 2524 ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.040  ? 1036 ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.004  ? 1194 ? f_plane_restr      ? ? 
# 
_struct.entry_id                     9F25 
_struct.title                        'Cryo-EM structure of Botulinum neurotoxin A LC-HN domain' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9F25 
_struct_keywords.text            'Neurotoxin, synaptic vesicle glycoprotein, Clostridium botulinum, TOXIN' 
_struct_keywords.pdbx_keywords   TOXIN 
# 
_struct_asym.id                            A 
_struct_asym.pdbx_blank_PDB_chainid_flag   N 
_struct_asym.pdbx_modified                 N 
_struct_asym.entity_id                     1 
_struct_asym.details                       ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    BXA1_CLOBO 
_struct_ref.pdbx_db_accession          P0DPI0 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;PFVNKQFNYKDPVNGVDIAYIKIPNVGQMQPVKAFKIHNKIWVIPERDTFTNPEEGDLNPPPEAKQVPVSYYDSTYLSTD
NEKDNYLKGVTKLFERIYSTDLGRMLLTSIVRGIPFWGGSTIDTELKVIDTNCINVIQPDGSYRSEELNLVIIGPSADII
QFECKSFGHEVLNLTRNGYGSTQYIRFSPDFTFGFEESLEVDTNPLLGAGKFATDPAVTLAHELIHAGHRLYGIAINPNR
VFKVNTNAYYEMSGLEVSFEELRTFGGHDAKFIDSLQENEFRLYYYNKFKDIASTLNKAKSIVGTTASLQYMKNVFKEKY
LLSEDTSGKFSVDKLKFDKLYKMLTEIYTEDNFVKFFKVLNRKTYLNFDKAVFKINIVPKVNYTIYDGFNLRNTNLAANF
NGQNTEINNMNFTKLKNFTGLFEFYKLLCVRGIITSKTKSLDKGYNKALNDLCIKVNNWDLFFSPSEDNFTNDLNKGEEI
TSDTNIEAAEENISLDLIQQYYLTFNFDNEPENISIENLSSDIIGQLELMPNIERFPNGKKYELDKYTMFHYLRAQEFEH
GKSRIALTNSVNEALLNPSRVYTFFSSDYVKKVNKATEAAMFLGWVEQLVYDFTDETSEVSTTDKIADITIIIPYIGPAL
NIGNMLYKDDFVGALIFSGAVILLEFIPEIAIPVLGTFALVSYIANKVLTVQTIDNALSKRNEKWDEVYKYIVTNWLAKV
NTQIDLIRKKMKEALENQAEATKAIINYQYNQYTEEEKNNINFNIDDLSSKLNESINKAMININKFLNQCSVSYLMNSMI
PYGVKRLEDFDASLKDALLKYIYDNRGTLIGQVDRLKDKVNNTLSTDIPFQLSKYVDNQRLLSTFTEYIKNIINTSILNL
RYESNHLIDLSRYASKINIGSKVNFDPIDKNQIQLFNLESSKIEVILKNAIVYNSMYENFSTSFWIRIPKYFNSISLNNE
YTIINCMENNSGWKVSLNYGEIIWTLQDTQEIKQRVVFKYSQMINISDYINRWIFVTITNNRLNNSKIYINGRLIDQKPI
SNLGNIHASNNIMFKLDGCRDTHRYIWIKYFNLFDKELNEKEIKDLYDNQSNSGILKDFWGDYLQYDKPYYMLNLYDPNK
YVDVNNVGIRGYMYLKGPRGSVMTTNIYLNSSLYRGTKFIIKKYASGNKDNIVRNNDRVYINVVVKNKEYRLATNASQAG
VEKILSALEIPDVGNLSQVVVMKSKNDQGITNKCKMNLQDNNGNDIGFIGFHQFNNIAKLVASNWYNRQIERSSRTLGCS
WEFIPVDDGWGERPL
;
_struct_ref.pdbx_align_begin           2 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9F25 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 19 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 1313 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P0DPI0 
_struct_ref_seq.db_align_beg                  2 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1296 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       2 
_struct_ref_seq.pdbx_auth_seq_align_end       1296 
# 
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 9F25 MET A 1    ? UNP P0DPI0 ?   ?    'initiating methionine' -16  1  
1 9F25 ARG A 2    ? UNP P0DPI0 ?   ?    'expression tag'        -15  2  
1 9F25 GLY A 3    ? UNP P0DPI0 ?   ?    'expression tag'        -14  3  
1 9F25 SER A 4    ? UNP P0DPI0 ?   ?    'expression tag'        -13  4  
1 9F25 HIS A 5    ? UNP P0DPI0 ?   ?    'expression tag'        -12  5  
1 9F25 HIS A 6    ? UNP P0DPI0 ?   ?    'expression tag'        -11  6  
1 9F25 HIS A 7    ? UNP P0DPI0 ?   ?    'expression tag'        -10  7  
1 9F25 HIS A 8    ? UNP P0DPI0 ?   ?    'expression tag'        -9   8  
1 9F25 HIS A 9    ? UNP P0DPI0 ?   ?    'expression tag'        -8   9  
1 9F25 HIS A 10   ? UNP P0DPI0 ?   ?    'expression tag'        -7   10 
1 9F25 GLY A 11   ? UNP P0DPI0 ?   ?    'expression tag'        -6   11 
1 9F25 SER A 12   ? UNP P0DPI0 ?   ?    'expression tag'        -5   12 
1 9F25 LEU A 13   ? UNP P0DPI0 ?   ?    'expression tag'        -4   13 
1 9F25 VAL A 14   ? UNP P0DPI0 ?   ?    'expression tag'        -3   14 
1 9F25 PRO A 15   ? UNP P0DPI0 ?   ?    'expression tag'        -2   15 
1 9F25 ARG A 16   ? UNP P0DPI0 ?   ?    'expression tag'        -1   16 
1 9F25 GLY A 17   ? UNP P0DPI0 ?   ?    'expression tag'        0    17 
1 9F25 SER A 18   ? UNP P0DPI0 ?   ?    'expression tag'        1    18 
1 9F25 ALA A 44   ? UNP P0DPI0 VAL 27   variant                 27   19 
1 9F25 GLN A 241  ? UNP P0DPI0 GLU 224  'engineered mutation'   224  20 
1 9F25 ALA A 380  ? UNP P0DPI0 ARG 363  'engineered mutation'   363  21 
1 9F25 PHE A 383  ? UNP P0DPI0 TYR 366  'engineered mutation'   366  22 
1 9F25 ALA A 1175 ? UNP P0DPI0 THR 1158 conflict                1158 23 
1 9F25 VAL A 1314 ? UNP P0DPI0 ?   ?    'expression tag'        1297 24 
1 9F25 PRO A 1315 ? UNP P0DPI0 ?   ?    'expression tag'        1298 25 
1 9F25 PRO A 1316 ? UNP P0DPI0 ?   ?    'expression tag'        1299 26 
1 9F25 THR A 1317 ? UNP P0DPI0 ?   ?    'expression tag'        1300 27 
1 9F25 PRO A 1318 ? UNP P0DPI0 ?   ?    'expression tag'        1301 28 
1 9F25 GLY A 1319 ? UNP P0DPI0 ?   ?    'expression tag'        1302 29 
1 9F25 SER A 1320 ? UNP P0DPI0 ?   ?    'expression tag'        1303 30 
1 9F25 ALA A 1321 ? UNP P0DPI0 ?   ?    'expression tag'        1304 31 
1 9F25 TRP A 1322 ? UNP P0DPI0 ?   ?    'expression tag'        1305 32 
1 9F25 SER A 1323 ? UNP P0DPI0 ?   ?    'expression tag'        1306 33 
1 9F25 HIS A 1324 ? UNP P0DPI0 ?   ?    'expression tag'        1307 34 
1 9F25 PRO A 1325 ? UNP P0DPI0 ?   ?    'expression tag'        1308 35 
1 9F25 GLN A 1326 ? UNP P0DPI0 ?   ?    'expression tag'        1309 36 
1 9F25 PHE A 1327 ? UNP P0DPI0 ?   ?    'expression tag'        1310 37 
1 9F25 GLU A 1328 ? UNP P0DPI0 ?   ?    'expression tag'        1311 38 
1 9F25 LYS A 1329 ? UNP P0DPI0 ?   ?    'expression tag'        1312 39 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_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]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
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  AA1 THR A 97  ? THR A 118 ? THR A 80  THR A 101 1 ? 22 
HELX_P HELX_P2  AA2 THR A 118 ? GLY A 131 ? THR A 101 GLY A 114 1 ? 14 
HELX_P HELX_P3  AA3 ILE A 147 ? THR A 149 ? ILE A 130 THR A 132 5 ? 3  
HELX_P HELX_P4  AA4 ASP A 233 ? TYR A 250 ? ASP A 216 TYR A 233 1 ? 18 
HELX_P HELX_P5  AA5 SER A 276 ? GLY A 284 ? SER A 259 GLY A 267 1 ? 9  
HELX_P HELX_P6  AA6 GLY A 285 ? ILE A 291 ? GLY A 268 ILE A 274 5 ? 7  
HELX_P HELX_P7  AA7 ASP A 292 ? ALA A 317 ? ASP A 275 ALA A 300 1 ? 26 
HELX_P HELX_P8  AA8 SER A 326 ? LEU A 339 ? SER A 309 LEU A 322 1 ? 14 
HELX_P HELX_P9  AA9 ASP A 351 ? GLU A 364 ? ASP A 334 GLU A 347 1 ? 14 
HELX_P HELX_P10 AB1 THR A 367 ? LYS A 376 ? THR A 350 LYS A 359 1 ? 10 
HELX_P HELX_P11 AB2 ASN A 426 ? PHE A 430 ? ASN A 409 PHE A 413 5 ? 5  
HELX_P HELX_P12 AB3 TRP A 477 ? LEU A 479 ? TRP A 460 LEU A 462 5 ? 3  
HELX_P HELX_P13 AB4 LEU A 513 ? THR A 522 ? LEU A 496 THR A 505 1 ? 10 
HELX_P HELX_P14 AB5 THR A 566 ? ALA A 573 ? THR A 549 ALA A 556 1 ? 8  
HELX_P HELX_P15 AB6 SER A 588 ? ASN A 595 ? SER A 571 ASN A 578 1 ? 8  
HELX_P HELX_P16 AB7 SER A 604 ? LYS A 613 ? SER A 587 LYS A 596 1 ? 10 
HELX_P HELX_P17 AB8 MET A 619 ? SER A 636 ? MET A 602 SER A 619 1 ? 18 
HELX_P HELX_P18 AB9 TYR A 653 ? LEU A 658 ? TYR A 636 LEU A 641 1 ? 6  
HELX_P HELX_P19 AC1 TYR A 665 ? GLY A 677 ? TYR A 648 GLY A 660 1 ? 13 
HELX_P HELX_P20 AC2 ALA A 678 ? ILE A 680 ? ALA A 661 ILE A 663 5 ? 3  
HELX_P HELX_P21 AC3 ASN A 704 ? VAL A 738 ? ASN A 687 VAL A 721 1 ? 35 
HELX_P HELX_P22 AC4 VAL A 738 ? GLN A 770 ? VAL A 721 GLN A 753 1 ? 33 
HELX_P HELX_P23 AC5 THR A 772 ? ASN A 780 ? THR A 755 ASN A 763 1 ? 9  
HELX_P HELX_P24 AC6 ASN A 782 ? MET A 817 ? ASN A 765 MET A 800 1 ? 36 
HELX_P HELX_P25 AC7 MET A 817 ? TYR A 841 ? MET A 800 TYR A 824 1 ? 25 
HELX_P HELX_P26 AC8 GLN A 850 ? SER A 863 ? GLN A 833 SER A 846 1 ? 14 
HELX_P HELX_P27 AC9 GLN A 869 ? TYR A 873 ? GLN A 852 TYR A 856 5 ? 5  
HELX_P HELX_P28 AD1 ASN A 876 ? GLU A 885 ? ASN A 859 GLU A 868 1 ? 10 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            disulf1 
_struct_conn.conn_type_id                  disulf 
_struct_conn.pdbx_leaving_atom_flag        ? 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           A 
_struct_conn.ptnr1_label_comp_id           CYS 
_struct_conn.ptnr1_label_seq_id            447 
_struct_conn.ptnr1_label_atom_id           SG 
_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                1_555 
_struct_conn.ptnr2_label_asym_id           A 
_struct_conn.ptnr2_label_comp_id           CYS 
_struct_conn.ptnr2_label_seq_id            471 
_struct_conn.ptnr2_label_atom_id           SG 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            A 
_struct_conn.ptnr1_auth_comp_id            CYS 
_struct_conn.ptnr1_auth_seq_id             430 
_struct_conn.ptnr2_auth_asym_id            A 
_struct_conn.ptnr2_auth_comp_id            CYS 
_struct_conn.ptnr2_auth_seq_id             454 
_struct_conn.ptnr2_symmetry                1_555 
_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               1.999 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CYS 
_pdbx_modification_feature.label_asym_id                      A 
_pdbx_modification_feature.label_seq_id                       447 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      471 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       CYS 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        430 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       454 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               SG 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                . 
_pdbx_modification_feature.ref_pcm_id                         . 
_pdbx_modification_feature.ref_comp_id                        . 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 2 ? 
AA3 ? 4 ? 
AA4 ? 2 ? 
AA5 ? 3 ? 
AA6 ? 2 ? 
AA7 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? parallel      
AA1 6 7 ? parallel      
AA1 7 8 ? anti-parallel 
AA2 1 2 ? parallel      
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? parallel      
AA6 1 2 ? parallel      
AA7 1 2 ? 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 
AA1 1 TYR A 161 ? GLU A 165 ? TYR A 144 GLU A 148 
AA1 2 CYS A 151 ? ILE A 155 ? CYS A 134 ILE A 138 
AA1 3 ILE A 36  ? LYS A 40  ? ILE A 19  LYS A 23  
AA1 4 VAL A 50  ? HIS A 56  ? VAL A 33  HIS A 39  
AA1 5 ILE A 59  ? ARG A 65  ? ILE A 42  ARG A 48  
AA1 6 LEU A 168 ? GLY A 172 ? LEU A 151 GLY A 155 
AA1 7 GLN A 201 ? ARG A 204 ? GLN A 184 ARG A 187 
AA1 8 CYS A 182 ? LYS A 183 ? CYS A 165 LYS A 166 
AA2 1 GLU A 143 ? LYS A 145 ? GLU A 126 LYS A 128 
AA2 2 SER A 319 ? VAL A 321 ? SER A 302 VAL A 304 
AA3 1 PHE A 230 ? ALA A 231 ? PHE A 213 ALA A 214 
AA3 2 PHE A 209 ? PHE A 213 ? PHE A 192 PHE A 196 
AA3 3 ALA A 389 ? LYS A 392 ? ALA A 372 LYS A 375 
AA3 4 THR A 431 ? LYS A 432 ? THR A 414 LYS A 415 
AA4 1 SER A 341 ? GLU A 342 ? SER A 324 GLU A 325 
AA4 2 PHE A 348 ? SER A 349 ? PHE A 331 SER A 332 
AA5 1 ILE A 472 ? ASN A 475 ? ILE A 455 ASN A 458 
AA5 2 TYR A 443 ? CYS A 447 ? TYR A 426 CYS A 430 
AA5 3 LYS A 559 ? GLU A 561 ? LYS A 542 GLU A 544 
AA6 1 GLU A 496 ? ILE A 498 ? GLU A 479 ILE A 481 
AA6 2 PHE A 696 ? LEU A 698 ? PHE A 679 LEU A 681 
AA7 1 ALA A 584 ? THR A 586 ? ALA A 567 THR A 569 
AA7 2 ARG A 598 ? TYR A 600 ? ARG A 581 TYR A 583 
# 
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 
AA1 1 2 O ARG A 162 ? O ARG A 145 N VAL A 154 ? N VAL A 137 
AA1 2 3 O ILE A 155 ? O ILE A 138 N TYR A 38  ? N TYR A 21  
AA1 3 4 N ILE A 39  ? N ILE A 22  O VAL A 50  ? O VAL A 33  
AA1 4 5 N PHE A 53  ? N PHE A 36  O VAL A 61  ? O VAL A 44  
AA1 5 6 N ILE A 62  ? N ILE A 45  O ILE A 170 ? O ILE A 153 
AA1 6 7 N VAL A 169 ? N VAL A 152 O ILE A 203 ? O ILE A 186 
AA1 7 8 O TYR A 202 ? O TYR A 185 N LYS A 183 ? N LYS A 166 
AA2 1 2 N LEU A 144 ? N LEU A 127 O SER A 319 ? O SER A 302 
AA3 1 2 O PHE A 230 ? O PHE A 213 N PHE A 213 ? N PHE A 196 
AA3 2 3 N THR A 210 ? N THR A 193 O PHE A 391 ? O PHE A 374 
AA3 3 4 N LYS A 392 ? N LYS A 375 O THR A 431 ? O THR A 414 
AA4 1 2 N SER A 341 ? N SER A 324 O SER A 349 ? O SER A 332 
AA5 1 2 O VAL A 474 ? O VAL A 457 N LYS A 444 ? N LYS A 427 
AA5 2 3 N LEU A 445 ? N LEU A 428 O TYR A 560 ? O TYR A 543 
AA6 1 2 N ILE A 498 ? N ILE A 481 O ALA A 697 ? O ALA A 680 
AA7 1 2 N ALA A 584 ? N ALA A 567 O VAL A 599 ? O VAL A 582 
# 
_pdbx_entry_details.entry_id                   9F25 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 TYR A 10  ? ? -82.86  49.10   
2  1 LYS A 11  ? ? -140.33 -2.58   
3  1 VAL A 17  ? ? -120.39 -61.20  
4  1 ASP A 74  ? ? -160.66 116.67  
5  1 TRP A 118 ? ? -96.87  59.85   
6  1 THR A 132 ? ? -68.09  4.75    
7  1 SER A 157 ? ? -78.92  -164.70 
8  1 ASN A 409 ? ? -91.10  58.62   
9  1 GLN A 557 ? ? -99.93  31.36   
10 1 ILE A 634 ? ? -35.53  119.05  
11 1 ALA A 686 ? ? 69.30   -1.89   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9F25 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         ? 
_em_3d_fitting.ref_protocol      'RIGID BODY FIT' 
# 
_em_3d_fitting_list.id                            1 
_em_3d_fitting_list.3d_fitting_id                 1 
_em_3d_fitting_list.pdb_entry_id                  6UL6 
_em_3d_fitting_list.pdb_chain_id                  ? 
_em_3d_fitting_list.pdb_chain_residue_range       ? 
_em_3d_fitting_list.details                       ? 
_em_3d_fitting_list.chain_id                      ? 
_em_3d_fitting_list.chain_residue_range           ? 
_em_3d_fitting_list.source_name                   PDB 
_em_3d_fitting_list.type                          'experimental model' 
_em_3d_fitting_list.accession_code                6UL6 
_em_3d_fitting_list.initial_refinement_model_id   1 
# 
_em_3d_reconstruction.entry_id                    9F25 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  3.7 
_em_3d_reconstruction.resolution_method           'FSC 0.143 CUT-OFF' 
_em_3d_reconstruction.magnification_calibration   ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.num_particles               121176 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       ? 
_em_buffer.pH            8.0 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'Botulinum neurotoxin A' 
_em_entity_assembly.details              'Botulinum neurotoxin A' 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        9F25 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'TFS KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           ? 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            300 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_min             600 
_em_imaging.nominal_defocus_max             2400 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           ? 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         ? 
# 
_em_vitrification.entry_id              9F25 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              100 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   277.15 
_em_vitrification.instrument            'FEI VITROBOT MARK IV' 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9F25 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A MET -16  ? A MET 1    
2   1 Y 1 A ARG -15  ? A ARG 2    
3   1 Y 1 A GLY -14  ? A GLY 3    
4   1 Y 1 A SER -13  ? A SER 4    
5   1 Y 1 A HIS -12  ? A HIS 5    
6   1 Y 1 A HIS -11  ? A HIS 6    
7   1 Y 1 A HIS -10  ? A HIS 7    
8   1 Y 1 A HIS -9   ? A HIS 8    
9   1 Y 1 A HIS -8   ? A HIS 9    
10  1 Y 1 A HIS -7   ? A HIS 10   
11  1 Y 1 A GLY -6   ? A GLY 11   
12  1 Y 1 A SER -5   ? A SER 12   
13  1 Y 1 A LEU -4   ? A LEU 13   
14  1 Y 1 A VAL -3   ? A VAL 14   
15  1 Y 1 A PRO -2   ? A PRO 15   
16  1 Y 1 A ARG -1   ? A ARG 16   
17  1 Y 1 A GLY 0    ? A GLY 17   
18  1 Y 1 A SER 1    ? A SER 18   
19  1 Y 1 A ARG 432  ? A ARG 449  
20  1 Y 1 A GLY 433  ? A GLY 450  
21  1 Y 1 A ILE 434  ? A ILE 451  
22  1 Y 1 A ILE 435  ? A ILE 452  
23  1 Y 1 A THR 436  ? A THR 453  
24  1 Y 1 A SER 437  ? A SER 454  
25  1 Y 1 A LYS 438  ? A LYS 455  
26  1 Y 1 A THR 439  ? A THR 456  
27  1 Y 1 A LYS 440  ? A LYS 457  
28  1 Y 1 A SER 441  ? A SER 458  
29  1 Y 1 A LEU 442  ? A LEU 459  
30  1 Y 1 A ASP 443  ? A ASP 460  
31  1 Y 1 A LYS 444  ? A LYS 461  
32  1 Y 1 A GLY 445  ? A GLY 462  
33  1 Y 1 A TYR 446  ? A TYR 463  
34  1 Y 1 A ASN 447  ? A ASN 464  
35  1 Y 1 A LYS 448  ? A LYS 465  
36  1 Y 1 A ALA 449  ? A ALA 466  
37  1 Y 1 A LEU 450  ? A LEU 467  
38  1 Y 1 A ASN 451  ? A ASN 468  
39  1 Y 1 A ASP 452  ? A ASP 469  
40  1 Y 1 A ASP 484  ? A ASP 501  
41  1 Y 1 A THR 485  ? A THR 502  
42  1 Y 1 A ASN 486  ? A ASN 503  
43  1 Y 1 A ILE 487  ? A ILE 504  
44  1 Y 1 A GLU 488  ? A GLU 505  
45  1 Y 1 A ALA 489  ? A ALA 506  
46  1 Y 1 A ALA 490  ? A ALA 507  
47  1 Y 1 A GLU 491  ? A GLU 508  
48  1 Y 1 A GLU 492  ? A GLU 509  
49  1 Y 1 A ASN 493  ? A ASN 510  
50  1 Y 1 A ILE 494  ? A ILE 511  
51  1 Y 1 A ASP 825  ? A ASP 842  
52  1 Y 1 A ASN 826  ? A ASN 843  
53  1 Y 1 A ARG 827  ? A ARG 844  
54  1 Y 1 A GLY 828  ? A GLY 845  
55  1 Y 1 A THR 829  ? A THR 846  
56  1 Y 1 A LEU 830  ? A LEU 847  
57  1 Y 1 A ILE 870  ? A ILE 887  
58  1 Y 1 A LYS 871  ? A LYS 888  
59  1 Y 1 A ASN 872  ? A ASN 889  
60  1 Y 1 A ILE 873  ? A ILE 890  
61  1 Y 1 A ILE 874  ? A ILE 891  
62  1 Y 1 A ASN 875  ? A ASN 892  
63  1 Y 1 A THR 876  ? A THR 893  
64  1 Y 1 A SER 877  ? A SER 894  
65  1 Y 1 A ILE 878  ? A ILE 895  
66  1 Y 1 A LEU 879  ? A LEU 896  
67  1 Y 1 A ASN 880  ? A ASN 897  
68  1 Y 1 A LEU 881  ? A LEU 898  
69  1 Y 1 A ARG 882  ? A ARG 899  
70  1 Y 1 A TYR 883  ? A TYR 900  
71  1 Y 1 A GLU 884  ? A GLU 901  
72  1 Y 1 A SER 885  ? A SER 902  
73  1 Y 1 A ASN 886  ? A ASN 903  
74  1 Y 1 A HIS 887  ? A HIS 904  
75  1 Y 1 A LEU 888  ? A LEU 905  
76  1 Y 1 A ILE 889  ? A ILE 906  
77  1 Y 1 A ASP 890  ? A ASP 907  
78  1 Y 1 A LEU 891  ? A LEU 908  
79  1 Y 1 A SER 892  ? A SER 909  
80  1 Y 1 A ARG 893  ? A ARG 910  
81  1 Y 1 A TYR 894  ? A TYR 911  
82  1 Y 1 A ALA 895  ? A ALA 912  
83  1 Y 1 A SER 896  ? A SER 913  
84  1 Y 1 A LYS 897  ? A LYS 914  
85  1 Y 1 A ILE 898  ? A ILE 915  
86  1 Y 1 A ASN 899  ? A ASN 916  
87  1 Y 1 A ILE 900  ? A ILE 917  
88  1 Y 1 A GLY 901  ? A GLY 918  
89  1 Y 1 A SER 902  ? A SER 919  
90  1 Y 1 A LYS 903  ? A LYS 920  
91  1 Y 1 A VAL 904  ? A VAL 921  
92  1 Y 1 A ASN 905  ? A ASN 922  
93  1 Y 1 A PHE 906  ? A PHE 923  
94  1 Y 1 A ASP 907  ? A ASP 924  
95  1 Y 1 A PRO 908  ? A PRO 925  
96  1 Y 1 A ILE 909  ? A ILE 926  
97  1 Y 1 A ASP 910  ? A ASP 927  
98  1 Y 1 A LYS 911  ? A LYS 928  
99  1 Y 1 A ASN 912  ? A ASN 929  
100 1 Y 1 A GLN 913  ? A GLN 930  
101 1 Y 1 A ILE 914  ? A ILE 931  
102 1 Y 1 A GLN 915  ? A GLN 932  
103 1 Y 1 A LEU 916  ? A LEU 933  
104 1 Y 1 A PHE 917  ? A PHE 934  
105 1 Y 1 A ASN 918  ? A ASN 935  
106 1 Y 1 A LEU 919  ? A LEU 936  
107 1 Y 1 A GLU 920  ? A GLU 937  
108 1 Y 1 A SER 921  ? A SER 938  
109 1 Y 1 A SER 922  ? A SER 939  
110 1 Y 1 A LYS 923  ? A LYS 940  
111 1 Y 1 A ILE 924  ? A ILE 941  
112 1 Y 1 A GLU 925  ? A GLU 942  
113 1 Y 1 A VAL 926  ? A VAL 943  
114 1 Y 1 A ILE 927  ? A ILE 944  
115 1 Y 1 A LEU 928  ? A LEU 945  
116 1 Y 1 A LYS 929  ? A LYS 946  
117 1 Y 1 A ASN 930  ? A ASN 947  
118 1 Y 1 A ALA 931  ? A ALA 948  
119 1 Y 1 A ILE 932  ? A ILE 949  
120 1 Y 1 A VAL 933  ? A VAL 950  
121 1 Y 1 A TYR 934  ? A TYR 951  
122 1 Y 1 A ASN 935  ? A ASN 952  
123 1 Y 1 A SER 936  ? A SER 953  
124 1 Y 1 A MET 937  ? A MET 954  
125 1 Y 1 A TYR 938  ? A TYR 955  
126 1 Y 1 A GLU 939  ? A GLU 956  
127 1 Y 1 A ASN 940  ? A ASN 957  
128 1 Y 1 A PHE 941  ? A PHE 958  
129 1 Y 1 A SER 942  ? A SER 959  
130 1 Y 1 A THR 943  ? A THR 960  
131 1 Y 1 A SER 944  ? A SER 961  
132 1 Y 1 A PHE 945  ? A PHE 962  
133 1 Y 1 A TRP 946  ? A TRP 963  
134 1 Y 1 A ILE 947  ? A ILE 964  
135 1 Y 1 A ARG 948  ? A ARG 965  
136 1 Y 1 A ILE 949  ? A ILE 966  
137 1 Y 1 A PRO 950  ? A PRO 967  
138 1 Y 1 A LYS 951  ? A LYS 968  
139 1 Y 1 A TYR 952  ? A TYR 969  
140 1 Y 1 A PHE 953  ? A PHE 970  
141 1 Y 1 A ASN 954  ? A ASN 971  
142 1 Y 1 A SER 955  ? A SER 972  
143 1 Y 1 A ILE 956  ? A ILE 973  
144 1 Y 1 A SER 957  ? A SER 974  
145 1 Y 1 A LEU 958  ? A LEU 975  
146 1 Y 1 A ASN 959  ? A ASN 976  
147 1 Y 1 A ASN 960  ? A ASN 977  
148 1 Y 1 A GLU 961  ? A GLU 978  
149 1 Y 1 A TYR 962  ? A TYR 979  
150 1 Y 1 A THR 963  ? A THR 980  
151 1 Y 1 A ILE 964  ? A ILE 981  
152 1 Y 1 A ILE 965  ? A ILE 982  
153 1 Y 1 A ASN 966  ? A ASN 983  
154 1 Y 1 A CYS 967  ? A CYS 984  
155 1 Y 1 A MET 968  ? A MET 985  
156 1 Y 1 A GLU 969  ? A GLU 986  
157 1 Y 1 A ASN 970  ? A ASN 987  
158 1 Y 1 A ASN 971  ? A ASN 988  
159 1 Y 1 A SER 972  ? A SER 989  
160 1 Y 1 A GLY 973  ? A GLY 990  
161 1 Y 1 A TRP 974  ? A TRP 991  
162 1 Y 1 A LYS 975  ? A LYS 992  
163 1 Y 1 A VAL 976  ? A VAL 993  
164 1 Y 1 A SER 977  ? A SER 994  
165 1 Y 1 A LEU 978  ? A LEU 995  
166 1 Y 1 A ASN 979  ? A ASN 996  
167 1 Y 1 A TYR 980  ? A TYR 997  
168 1 Y 1 A GLY 981  ? A GLY 998  
169 1 Y 1 A GLU 982  ? A GLU 999  
170 1 Y 1 A ILE 983  ? A ILE 1000 
171 1 Y 1 A ILE 984  ? A ILE 1001 
172 1 Y 1 A TRP 985  ? A TRP 1002 
173 1 Y 1 A THR 986  ? A THR 1003 
174 1 Y 1 A LEU 987  ? A LEU 1004 
175 1 Y 1 A GLN 988  ? A GLN 1005 
176 1 Y 1 A ASP 989  ? A ASP 1006 
177 1 Y 1 A THR 990  ? A THR 1007 
178 1 Y 1 A GLN 991  ? A GLN 1008 
179 1 Y 1 A GLU 992  ? A GLU 1009 
180 1 Y 1 A ILE 993  ? A ILE 1010 
181 1 Y 1 A LYS 994  ? A LYS 1011 
182 1 Y 1 A GLN 995  ? A GLN 1012 
183 1 Y 1 A ARG 996  ? A ARG 1013 
184 1 Y 1 A VAL 997  ? A VAL 1014 
185 1 Y 1 A VAL 998  ? A VAL 1015 
186 1 Y 1 A PHE 999  ? A PHE 1016 
187 1 Y 1 A LYS 1000 ? A LYS 1017 
188 1 Y 1 A TYR 1001 ? A TYR 1018 
189 1 Y 1 A SER 1002 ? A SER 1019 
190 1 Y 1 A GLN 1003 ? A GLN 1020 
191 1 Y 1 A MET 1004 ? A MET 1021 
192 1 Y 1 A ILE 1005 ? A ILE 1022 
193 1 Y 1 A ASN 1006 ? A ASN 1023 
194 1 Y 1 A ILE 1007 ? A ILE 1024 
195 1 Y 1 A SER 1008 ? A SER 1025 
196 1 Y 1 A ASP 1009 ? A ASP 1026 
197 1 Y 1 A TYR 1010 ? A TYR 1027 
198 1 Y 1 A ILE 1011 ? A ILE 1028 
199 1 Y 1 A ASN 1012 ? A ASN 1029 
200 1 Y 1 A ARG 1013 ? A ARG 1030 
201 1 Y 1 A TRP 1014 ? A TRP 1031 
202 1 Y 1 A ILE 1015 ? A ILE 1032 
203 1 Y 1 A PHE 1016 ? A PHE 1033 
204 1 Y 1 A VAL 1017 ? A VAL 1034 
205 1 Y 1 A THR 1018 ? A THR 1035 
206 1 Y 1 A ILE 1019 ? A ILE 1036 
207 1 Y 1 A THR 1020 ? A THR 1037 
208 1 Y 1 A ASN 1021 ? A ASN 1038 
209 1 Y 1 A ASN 1022 ? A ASN 1039 
210 1 Y 1 A ARG 1023 ? A ARG 1040 
211 1 Y 1 A LEU 1024 ? A LEU 1041 
212 1 Y 1 A ASN 1025 ? A ASN 1042 
213 1 Y 1 A ASN 1026 ? A ASN 1043 
214 1 Y 1 A SER 1027 ? A SER 1044 
215 1 Y 1 A LYS 1028 ? A LYS 1045 
216 1 Y 1 A ILE 1029 ? A ILE 1046 
217 1 Y 1 A TYR 1030 ? A TYR 1047 
218 1 Y 1 A ILE 1031 ? A ILE 1048 
219 1 Y 1 A ASN 1032 ? A ASN 1049 
220 1 Y 1 A GLY 1033 ? A GLY 1050 
221 1 Y 1 A ARG 1034 ? A ARG 1051 
222 1 Y 1 A LEU 1035 ? A LEU 1052 
223 1 Y 1 A ILE 1036 ? A ILE 1053 
224 1 Y 1 A ASP 1037 ? A ASP 1054 
225 1 Y 1 A GLN 1038 ? A GLN 1055 
226 1 Y 1 A LYS 1039 ? A LYS 1056 
227 1 Y 1 A PRO 1040 ? A PRO 1057 
228 1 Y 1 A ILE 1041 ? A ILE 1058 
229 1 Y 1 A SER 1042 ? A SER 1059 
230 1 Y 1 A ASN 1043 ? A ASN 1060 
231 1 Y 1 A LEU 1044 ? A LEU 1061 
232 1 Y 1 A GLY 1045 ? A GLY 1062 
233 1 Y 1 A ASN 1046 ? A ASN 1063 
234 1 Y 1 A ILE 1047 ? A ILE 1064 
235 1 Y 1 A HIS 1048 ? A HIS 1065 
236 1 Y 1 A ALA 1049 ? A ALA 1066 
237 1 Y 1 A SER 1050 ? A SER 1067 
238 1 Y 1 A ASN 1051 ? A ASN 1068 
239 1 Y 1 A ASN 1052 ? A ASN 1069 
240 1 Y 1 A ILE 1053 ? A ILE 1070 
241 1 Y 1 A MET 1054 ? A MET 1071 
242 1 Y 1 A PHE 1055 ? A PHE 1072 
243 1 Y 1 A LYS 1056 ? A LYS 1073 
244 1 Y 1 A LEU 1057 ? A LEU 1074 
245 1 Y 1 A ASP 1058 ? A ASP 1075 
246 1 Y 1 A GLY 1059 ? A GLY 1076 
247 1 Y 1 A CYS 1060 ? A CYS 1077 
248 1 Y 1 A ARG 1061 ? A ARG 1078 
249 1 Y 1 A ASP 1062 ? A ASP 1079 
250 1 Y 1 A THR 1063 ? A THR 1080 
251 1 Y 1 A HIS 1064 ? A HIS 1081 
252 1 Y 1 A ARG 1065 ? A ARG 1082 
253 1 Y 1 A TYR 1066 ? A TYR 1083 
254 1 Y 1 A ILE 1067 ? A ILE 1084 
255 1 Y 1 A TRP 1068 ? A TRP 1085 
256 1 Y 1 A ILE 1069 ? A ILE 1086 
257 1 Y 1 A LYS 1070 ? A LYS 1087 
258 1 Y 1 A TYR 1071 ? A TYR 1088 
259 1 Y 1 A PHE 1072 ? A PHE 1089 
260 1 Y 1 A ASN 1073 ? A ASN 1090 
261 1 Y 1 A LEU 1074 ? A LEU 1091 
262 1 Y 1 A PHE 1075 ? A PHE 1092 
263 1 Y 1 A ASP 1076 ? A ASP 1093 
264 1 Y 1 A LYS 1077 ? A LYS 1094 
265 1 Y 1 A GLU 1078 ? A GLU 1095 
266 1 Y 1 A LEU 1079 ? A LEU 1096 
267 1 Y 1 A ASN 1080 ? A ASN 1097 
268 1 Y 1 A GLU 1081 ? A GLU 1098 
269 1 Y 1 A LYS 1082 ? A LYS 1099 
270 1 Y 1 A GLU 1083 ? A GLU 1100 
271 1 Y 1 A ILE 1084 ? A ILE 1101 
272 1 Y 1 A LYS 1085 ? A LYS 1102 
273 1 Y 1 A ASP 1086 ? A ASP 1103 
274 1 Y 1 A LEU 1087 ? A LEU 1104 
275 1 Y 1 A TYR 1088 ? A TYR 1105 
276 1 Y 1 A ASP 1089 ? A ASP 1106 
277 1 Y 1 A ASN 1090 ? A ASN 1107 
278 1 Y 1 A GLN 1091 ? A GLN 1108 
279 1 Y 1 A SER 1092 ? A SER 1109 
280 1 Y 1 A ASN 1093 ? A ASN 1110 
281 1 Y 1 A SER 1094 ? A SER 1111 
282 1 Y 1 A GLY 1095 ? A GLY 1112 
283 1 Y 1 A ILE 1096 ? A ILE 1113 
284 1 Y 1 A LEU 1097 ? A LEU 1114 
285 1 Y 1 A LYS 1098 ? A LYS 1115 
286 1 Y 1 A ASP 1099 ? A ASP 1116 
287 1 Y 1 A PHE 1100 ? A PHE 1117 
288 1 Y 1 A TRP 1101 ? A TRP 1118 
289 1 Y 1 A GLY 1102 ? A GLY 1119 
290 1 Y 1 A ASP 1103 ? A ASP 1120 
291 1 Y 1 A TYR 1104 ? A TYR 1121 
292 1 Y 1 A LEU 1105 ? A LEU 1122 
293 1 Y 1 A GLN 1106 ? A GLN 1123 
294 1 Y 1 A TYR 1107 ? A TYR 1124 
295 1 Y 1 A ASP 1108 ? A ASP 1125 
296 1 Y 1 A LYS 1109 ? A LYS 1126 
297 1 Y 1 A PRO 1110 ? A PRO 1127 
298 1 Y 1 A TYR 1111 ? A TYR 1128 
299 1 Y 1 A TYR 1112 ? A TYR 1129 
300 1 Y 1 A MET 1113 ? A MET 1130 
301 1 Y 1 A LEU 1114 ? A LEU 1131 
302 1 Y 1 A ASN 1115 ? A ASN 1132 
303 1 Y 1 A LEU 1116 ? A LEU 1133 
304 1 Y 1 A TYR 1117 ? A TYR 1134 
305 1 Y 1 A ASP 1118 ? A ASP 1135 
306 1 Y 1 A PRO 1119 ? A PRO 1136 
307 1 Y 1 A ASN 1120 ? A ASN 1137 
308 1 Y 1 A LYS 1121 ? A LYS 1138 
309 1 Y 1 A TYR 1122 ? A TYR 1139 
310 1 Y 1 A VAL 1123 ? A VAL 1140 
311 1 Y 1 A ASP 1124 ? A ASP 1141 
312 1 Y 1 A VAL 1125 ? A VAL 1142 
313 1 Y 1 A ASN 1126 ? A ASN 1143 
314 1 Y 1 A ASN 1127 ? A ASN 1144 
315 1 Y 1 A VAL 1128 ? A VAL 1145 
316 1 Y 1 A GLY 1129 ? A GLY 1146 
317 1 Y 1 A ILE 1130 ? A ILE 1147 
318 1 Y 1 A ARG 1131 ? A ARG 1148 
319 1 Y 1 A GLY 1132 ? A GLY 1149 
320 1 Y 1 A TYR 1133 ? A TYR 1150 
321 1 Y 1 A MET 1134 ? A MET 1151 
322 1 Y 1 A TYR 1135 ? A TYR 1152 
323 1 Y 1 A LEU 1136 ? A LEU 1153 
324 1 Y 1 A LYS 1137 ? A LYS 1154 
325 1 Y 1 A GLY 1138 ? A GLY 1155 
326 1 Y 1 A PRO 1139 ? A PRO 1156 
327 1 Y 1 A ARG 1140 ? A ARG 1157 
328 1 Y 1 A GLY 1141 ? A GLY 1158 
329 1 Y 1 A SER 1142 ? A SER 1159 
330 1 Y 1 A VAL 1143 ? A VAL 1160 
331 1 Y 1 A MET 1144 ? A MET 1161 
332 1 Y 1 A THR 1145 ? A THR 1162 
333 1 Y 1 A THR 1146 ? A THR 1163 
334 1 Y 1 A ASN 1147 ? A ASN 1164 
335 1 Y 1 A ILE 1148 ? A ILE 1165 
336 1 Y 1 A TYR 1149 ? A TYR 1166 
337 1 Y 1 A LEU 1150 ? A LEU 1167 
338 1 Y 1 A ASN 1151 ? A ASN 1168 
339 1 Y 1 A SER 1152 ? A SER 1169 
340 1 Y 1 A SER 1153 ? A SER 1170 
341 1 Y 1 A LEU 1154 ? A LEU 1171 
342 1 Y 1 A TYR 1155 ? A TYR 1172 
343 1 Y 1 A ARG 1156 ? A ARG 1173 
344 1 Y 1 A GLY 1157 ? A GLY 1174 
345 1 Y 1 A ALA 1158 ? A ALA 1175 
346 1 Y 1 A LYS 1159 ? A LYS 1176 
347 1 Y 1 A PHE 1160 ? A PHE 1177 
348 1 Y 1 A ILE 1161 ? A ILE 1178 
349 1 Y 1 A ILE 1162 ? A ILE 1179 
350 1 Y 1 A LYS 1163 ? A LYS 1180 
351 1 Y 1 A LYS 1164 ? A LYS 1181 
352 1 Y 1 A TYR 1165 ? A TYR 1182 
353 1 Y 1 A ALA 1166 ? A ALA 1183 
354 1 Y 1 A SER 1167 ? A SER 1184 
355 1 Y 1 A GLY 1168 ? A GLY 1185 
356 1 Y 1 A ASN 1169 ? A ASN 1186 
357 1 Y 1 A LYS 1170 ? A LYS 1187 
358 1 Y 1 A ASP 1171 ? A ASP 1188 
359 1 Y 1 A ASN 1172 ? A ASN 1189 
360 1 Y 1 A ILE 1173 ? A ILE 1190 
361 1 Y 1 A VAL 1174 ? A VAL 1191 
362 1 Y 1 A ARG 1175 ? A ARG 1192 
363 1 Y 1 A ASN 1176 ? A ASN 1193 
364 1 Y 1 A ASN 1177 ? A ASN 1194 
365 1 Y 1 A ASP 1178 ? A ASP 1195 
366 1 Y 1 A ARG 1179 ? A ARG 1196 
367 1 Y 1 A VAL 1180 ? A VAL 1197 
368 1 Y 1 A TYR 1181 ? A TYR 1198 
369 1 Y 1 A ILE 1182 ? A ILE 1199 
370 1 Y 1 A ASN 1183 ? A ASN 1200 
371 1 Y 1 A VAL 1184 ? A VAL 1201 
372 1 Y 1 A VAL 1185 ? A VAL 1202 
373 1 Y 1 A VAL 1186 ? A VAL 1203 
374 1 Y 1 A LYS 1187 ? A LYS 1204 
375 1 Y 1 A ASN 1188 ? A ASN 1205 
376 1 Y 1 A LYS 1189 ? A LYS 1206 
377 1 Y 1 A GLU 1190 ? A GLU 1207 
378 1 Y 1 A TYR 1191 ? A TYR 1208 
379 1 Y 1 A ARG 1192 ? A ARG 1209 
380 1 Y 1 A LEU 1193 ? A LEU 1210 
381 1 Y 1 A ALA 1194 ? A ALA 1211 
382 1 Y 1 A THR 1195 ? A THR 1212 
383 1 Y 1 A ASN 1196 ? A ASN 1213 
384 1 Y 1 A ALA 1197 ? A ALA 1214 
385 1 Y 1 A SER 1198 ? A SER 1215 
386 1 Y 1 A GLN 1199 ? A GLN 1216 
387 1 Y 1 A ALA 1200 ? A ALA 1217 
388 1 Y 1 A GLY 1201 ? A GLY 1218 
389 1 Y 1 A VAL 1202 ? A VAL 1219 
390 1 Y 1 A GLU 1203 ? A GLU 1220 
391 1 Y 1 A LYS 1204 ? A LYS 1221 
392 1 Y 1 A ILE 1205 ? A ILE 1222 
393 1 Y 1 A LEU 1206 ? A LEU 1223 
394 1 Y 1 A SER 1207 ? A SER 1224 
395 1 Y 1 A ALA 1208 ? A ALA 1225 
396 1 Y 1 A LEU 1209 ? A LEU 1226 
397 1 Y 1 A GLU 1210 ? A GLU 1227 
398 1 Y 1 A ILE 1211 ? A ILE 1228 
399 1 Y 1 A PRO 1212 ? A PRO 1229 
400 1 Y 1 A ASP 1213 ? A ASP 1230 
401 1 Y 1 A VAL 1214 ? A VAL 1231 
402 1 Y 1 A GLY 1215 ? A GLY 1232 
403 1 Y 1 A ASN 1216 ? A ASN 1233 
404 1 Y 1 A LEU 1217 ? A LEU 1234 
405 1 Y 1 A SER 1218 ? A SER 1235 
406 1 Y 1 A GLN 1219 ? A GLN 1236 
407 1 Y 1 A VAL 1220 ? A VAL 1237 
408 1 Y 1 A VAL 1221 ? A VAL 1238 
409 1 Y 1 A VAL 1222 ? A VAL 1239 
410 1 Y 1 A MET 1223 ? A MET 1240 
411 1 Y 1 A LYS 1224 ? A LYS 1241 
412 1 Y 1 A SER 1225 ? A SER 1242 
413 1 Y 1 A LYS 1226 ? A LYS 1243 
414 1 Y 1 A ASN 1227 ? A ASN 1244 
415 1 Y 1 A ASP 1228 ? A ASP 1245 
416 1 Y 1 A GLN 1229 ? A GLN 1246 
417 1 Y 1 A GLY 1230 ? A GLY 1247 
418 1 Y 1 A ILE 1231 ? A ILE 1248 
419 1 Y 1 A THR 1232 ? A THR 1249 
420 1 Y 1 A ASN 1233 ? A ASN 1250 
421 1 Y 1 A LYS 1234 ? A LYS 1251 
422 1 Y 1 A CYS 1235 ? A CYS 1252 
423 1 Y 1 A LYS 1236 ? A LYS 1253 
424 1 Y 1 A MET 1237 ? A MET 1254 
425 1 Y 1 A ASN 1238 ? A ASN 1255 
426 1 Y 1 A LEU 1239 ? A LEU 1256 
427 1 Y 1 A GLN 1240 ? A GLN 1257 
428 1 Y 1 A ASP 1241 ? A ASP 1258 
429 1 Y 1 A ASN 1242 ? A ASN 1259 
430 1 Y 1 A ASN 1243 ? A ASN 1260 
431 1 Y 1 A GLY 1244 ? A GLY 1261 
432 1 Y 1 A ASN 1245 ? A ASN 1262 
433 1 Y 1 A ASP 1246 ? A ASP 1263 
434 1 Y 1 A ILE 1247 ? A ILE 1264 
435 1 Y 1 A GLY 1248 ? A GLY 1265 
436 1 Y 1 A PHE 1249 ? A PHE 1266 
437 1 Y 1 A ILE 1250 ? A ILE 1267 
438 1 Y 1 A GLY 1251 ? A GLY 1268 
439 1 Y 1 A PHE 1252 ? A PHE 1269 
440 1 Y 1 A HIS 1253 ? A HIS 1270 
441 1 Y 1 A GLN 1254 ? A GLN 1271 
442 1 Y 1 A PHE 1255 ? A PHE 1272 
443 1 Y 1 A ASN 1256 ? A ASN 1273 
444 1 Y 1 A ASN 1257 ? A ASN 1274 
445 1 Y 1 A ILE 1258 ? A ILE 1275 
446 1 Y 1 A ALA 1259 ? A ALA 1276 
447 1 Y 1 A LYS 1260 ? A LYS 1277 
448 1 Y 1 A LEU 1261 ? A LEU 1278 
449 1 Y 1 A VAL 1262 ? A VAL 1279 
450 1 Y 1 A ALA 1263 ? A ALA 1280 
451 1 Y 1 A SER 1264 ? A SER 1281 
452 1 Y 1 A ASN 1265 ? A ASN 1282 
453 1 Y 1 A TRP 1266 ? A TRP 1283 
454 1 Y 1 A TYR 1267 ? A TYR 1284 
455 1 Y 1 A ASN 1268 ? A ASN 1285 
456 1 Y 1 A ARG 1269 ? A ARG 1286 
457 1 Y 1 A GLN 1270 ? A GLN 1287 
458 1 Y 1 A ILE 1271 ? A ILE 1288 
459 1 Y 1 A GLU 1272 ? A GLU 1289 
460 1 Y 1 A ARG 1273 ? A ARG 1290 
461 1 Y 1 A SER 1274 ? A SER 1291 
462 1 Y 1 A SER 1275 ? A SER 1292 
463 1 Y 1 A ARG 1276 ? A ARG 1293 
464 1 Y 1 A THR 1277 ? A THR 1294 
465 1 Y 1 A LEU 1278 ? A LEU 1295 
466 1 Y 1 A GLY 1279 ? A GLY 1296 
467 1 Y 1 A CYS 1280 ? A CYS 1297 
468 1 Y 1 A SER 1281 ? A SER 1298 
469 1 Y 1 A TRP 1282 ? A TRP 1299 
470 1 Y 1 A GLU 1283 ? A GLU 1300 
471 1 Y 1 A PHE 1284 ? A PHE 1301 
472 1 Y 1 A ILE 1285 ? A ILE 1302 
473 1 Y 1 A PRO 1286 ? A PRO 1303 
474 1 Y 1 A VAL 1287 ? A VAL 1304 
475 1 Y 1 A ASP 1288 ? A ASP 1305 
476 1 Y 1 A ASP 1289 ? A ASP 1306 
477 1 Y 1 A GLY 1290 ? A GLY 1307 
478 1 Y 1 A TRP 1291 ? A TRP 1308 
479 1 Y 1 A GLY 1292 ? A GLY 1309 
480 1 Y 1 A GLU 1293 ? A GLU 1310 
481 1 Y 1 A ARG 1294 ? A ARG 1311 
482 1 Y 1 A PRO 1295 ? A PRO 1312 
483 1 Y 1 A LEU 1296 ? A LEU 1313 
484 1 Y 1 A VAL 1297 ? A VAL 1314 
485 1 Y 1 A PRO 1298 ? A PRO 1315 
486 1 Y 1 A PRO 1299 ? A PRO 1316 
487 1 Y 1 A THR 1300 ? A THR 1317 
488 1 Y 1 A PRO 1301 ? A PRO 1318 
489 1 Y 1 A GLY 1302 ? A GLY 1319 
490 1 Y 1 A SER 1303 ? A SER 1320 
491 1 Y 1 A ALA 1304 ? A ALA 1321 
492 1 Y 1 A TRP 1305 ? A TRP 1322 
493 1 Y 1 A SER 1306 ? A SER 1323 
494 1 Y 1 A HIS 1307 ? A HIS 1324 
495 1 Y 1 A PRO 1308 ? A PRO 1325 
496 1 Y 1 A GLN 1309 ? A GLN 1326 
497 1 Y 1 A PHE 1310 ? A PHE 1327 
498 1 Y 1 A GLU 1311 ? A GLU 1328 
499 1 Y 1 A LYS 1312 ? A LYS 1329 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
ILE N    N N N 158 
ILE CA   C N S 159 
ILE C    C N N 160 
ILE O    O N N 161 
ILE CB   C N S 162 
ILE CG1  C N N 163 
ILE CG2  C N N 164 
ILE CD1  C N N 165 
ILE OXT  O N N 166 
ILE H    H N N 167 
ILE H2   H N N 168 
ILE HA   H N N 169 
ILE HB   H N N 170 
ILE HG12 H N N 171 
ILE HG13 H N N 172 
ILE HG21 H N N 173 
ILE HG22 H N N 174 
ILE HG23 H N N 175 
ILE HD11 H N N 176 
ILE HD12 H N N 177 
ILE HD13 H N N 178 
ILE HXT  H N N 179 
LEU N    N N N 180 
LEU CA   C N S 181 
LEU C    C N N 182 
LEU O    O N N 183 
LEU CB   C N N 184 
LEU CG   C N N 185 
LEU CD1  C N N 186 
LEU CD2  C N N 187 
LEU OXT  O N N 188 
LEU H    H N N 189 
LEU H2   H N N 190 
LEU HA   H N N 191 
LEU HB2  H N N 192 
LEU HB3  H N N 193 
LEU HG   H N N 194 
LEU HD11 H N N 195 
LEU HD12 H N N 196 
LEU HD13 H N N 197 
LEU HD21 H N N 198 
LEU HD22 H N N 199 
LEU HD23 H N N 200 
LEU HXT  H N N 201 
LYS N    N N N 202 
LYS CA   C N S 203 
LYS C    C N N 204 
LYS O    O N N 205 
LYS CB   C N N 206 
LYS CG   C N N 207 
LYS CD   C N N 208 
LYS CE   C N N 209 
LYS NZ   N N N 210 
LYS OXT  O N N 211 
LYS H    H N N 212 
LYS H2   H N N 213 
LYS HA   H N N 214 
LYS HB2  H N N 215 
LYS HB3  H N N 216 
LYS HG2  H N N 217 
LYS HG3  H N N 218 
LYS HD2  H N N 219 
LYS HD3  H N N 220 
LYS HE2  H N N 221 
LYS HE3  H N N 222 
LYS HZ1  H N N 223 
LYS HZ2  H N N 224 
LYS HZ3  H N N 225 
LYS HXT  H N N 226 
MET N    N N N 227 
MET CA   C N S 228 
MET C    C N N 229 
MET O    O N N 230 
MET CB   C N N 231 
MET CG   C N N 232 
MET SD   S N N 233 
MET CE   C N N 234 
MET OXT  O N N 235 
MET H    H N N 236 
MET H2   H N N 237 
MET HA   H N N 238 
MET HB2  H N N 239 
MET HB3  H N N 240 
MET HG2  H N N 241 
MET HG3  H N N 242 
MET HE1  H N N 243 
MET HE2  H N N 244 
MET HE3  H N N 245 
MET HXT  H N N 246 
PHE N    N N N 247 
PHE CA   C N S 248 
PHE C    C N N 249 
PHE O    O N N 250 
PHE CB   C N N 251 
PHE CG   C Y N 252 
PHE CD1  C Y N 253 
PHE CD2  C Y N 254 
PHE CE1  C Y N 255 
PHE CE2  C Y N 256 
PHE CZ   C Y N 257 
PHE OXT  O N N 258 
PHE H    H N N 259 
PHE H2   H N N 260 
PHE HA   H N N 261 
PHE HB2  H N N 262 
PHE HB3  H N N 263 
PHE HD1  H N N 264 
PHE HD2  H N N 265 
PHE HE1  H N N 266 
PHE HE2  H N N 267 
PHE HZ   H N N 268 
PHE HXT  H N N 269 
PRO N    N N N 270 
PRO CA   C N S 271 
PRO C    C N N 272 
PRO O    O N N 273 
PRO CB   C N N 274 
PRO CG   C N N 275 
PRO CD   C N N 276 
PRO OXT  O N N 277 
PRO H    H N N 278 
PRO HA   H N N 279 
PRO HB2  H N N 280 
PRO HB3  H N N 281 
PRO HG2  H N N 282 
PRO HG3  H N N 283 
PRO HD2  H N N 284 
PRO HD3  H N N 285 
PRO HXT  H N N 286 
SER N    N N N 287 
SER CA   C N S 288 
SER C    C N N 289 
SER O    O N N 290 
SER CB   C N N 291 
SER OG   O N N 292 
SER OXT  O N N 293 
SER H    H N N 294 
SER H2   H N N 295 
SER HA   H N N 296 
SER HB2  H N N 297 
SER HB3  H N N 298 
SER HG   H N N 299 
SER HXT  H N N 300 
THR N    N N N 301 
THR CA   C N S 302 
THR C    C N N 303 
THR O    O N N 304 
THR CB   C N R 305 
THR OG1  O N N 306 
THR CG2  C N N 307 
THR OXT  O N N 308 
THR H    H N N 309 
THR H2   H N N 310 
THR HA   H N N 311 
THR HB   H N N 312 
THR HG1  H N N 313 
THR HG21 H N N 314 
THR HG22 H N N 315 
THR HG23 H N N 316 
THR HXT  H N N 317 
TRP N    N N N 318 
TRP CA   C N S 319 
TRP C    C N N 320 
TRP O    O N N 321 
TRP CB   C N N 322 
TRP CG   C Y N 323 
TRP CD1  C Y N 324 
TRP CD2  C Y N 325 
TRP NE1  N Y N 326 
TRP CE2  C Y N 327 
TRP CE3  C Y N 328 
TRP CZ2  C Y N 329 
TRP CZ3  C Y N 330 
TRP CH2  C Y N 331 
TRP OXT  O N N 332 
TRP H    H N N 333 
TRP H2   H N N 334 
TRP HA   H N N 335 
TRP HB2  H N N 336 
TRP HB3  H N N 337 
TRP HD1  H N N 338 
TRP HE1  H N N 339 
TRP HE3  H N N 340 
TRP HZ2  H N N 341 
TRP HZ3  H N N 342 
TRP HH2  H N N 343 
TRP HXT  H N N 344 
TYR N    N N N 345 
TYR CA   C N S 346 
TYR C    C N N 347 
TYR O    O N N 348 
TYR CB   C N N 349 
TYR CG   C Y N 350 
TYR CD1  C Y N 351 
TYR CD2  C Y N 352 
TYR CE1  C Y N 353 
TYR CE2  C Y N 354 
TYR CZ   C Y N 355 
TYR OH   O N N 356 
TYR OXT  O N N 357 
TYR H    H N N 358 
TYR H2   H N N 359 
TYR HA   H N N 360 
TYR HB2  H N N 361 
TYR HB3  H N N 362 
TYR HD1  H N N 363 
TYR HD2  H N N 364 
TYR HE1  H N N 365 
TYR HE2  H N N 366 
TYR HH   H N N 367 
TYR HXT  H N N 368 
VAL N    N N N 369 
VAL CA   C N S 370 
VAL C    C N N 371 
VAL O    O N N 372 
VAL CB   C N N 373 
VAL CG1  C N N 374 
VAL CG2  C N N 375 
VAL OXT  O N N 376 
VAL H    H N N 377 
VAL H2   H N N 378 
VAL HA   H N N 379 
VAL HB   H N N 380 
VAL HG11 H N N 381 
VAL HG12 H N N 382 
VAL HG13 H N N 383 
VAL HG21 H N N 384 
VAL HG22 H N N 385 
VAL HG23 H N N 386 
VAL HXT  H N N 387 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
ILE N   CA   sing N N 150 
ILE N   H    sing N N 151 
ILE N   H2   sing N N 152 
ILE CA  C    sing N N 153 
ILE CA  CB   sing N N 154 
ILE CA  HA   sing N N 155 
ILE C   O    doub N N 156 
ILE C   OXT  sing N N 157 
ILE CB  CG1  sing N N 158 
ILE CB  CG2  sing N N 159 
ILE CB  HB   sing N N 160 
ILE CG1 CD1  sing N N 161 
ILE CG1 HG12 sing N N 162 
ILE CG1 HG13 sing N N 163 
ILE CG2 HG21 sing N N 164 
ILE CG2 HG22 sing N N 165 
ILE CG2 HG23 sing N N 166 
ILE CD1 HD11 sing N N 167 
ILE CD1 HD12 sing N N 168 
ILE CD1 HD13 sing N N 169 
ILE OXT HXT  sing N N 170 
LEU N   CA   sing N N 171 
LEU N   H    sing N N 172 
LEU N   H2   sing N N 173 
LEU CA  C    sing N N 174 
LEU CA  CB   sing N N 175 
LEU CA  HA   sing N N 176 
LEU C   O    doub N N 177 
LEU C   OXT  sing N N 178 
LEU CB  CG   sing N N 179 
LEU CB  HB2  sing N N 180 
LEU CB  HB3  sing N N 181 
LEU CG  CD1  sing N N 182 
LEU CG  CD2  sing N N 183 
LEU CG  HG   sing N N 184 
LEU CD1 HD11 sing N N 185 
LEU CD1 HD12 sing N N 186 
LEU CD1 HD13 sing N N 187 
LEU CD2 HD21 sing N N 188 
LEU CD2 HD22 sing N N 189 
LEU CD2 HD23 sing N N 190 
LEU OXT HXT  sing N N 191 
LYS N   CA   sing N N 192 
LYS N   H    sing N N 193 
LYS N   H2   sing N N 194 
LYS CA  C    sing N N 195 
LYS CA  CB   sing N N 196 
LYS CA  HA   sing N N 197 
LYS C   O    doub N N 198 
LYS C   OXT  sing N N 199 
LYS CB  CG   sing N N 200 
LYS CB  HB2  sing N N 201 
LYS CB  HB3  sing N N 202 
LYS CG  CD   sing N N 203 
LYS CG  HG2  sing N N 204 
LYS CG  HG3  sing N N 205 
LYS CD  CE   sing N N 206 
LYS CD  HD2  sing N N 207 
LYS CD  HD3  sing N N 208 
LYS CE  NZ   sing N N 209 
LYS CE  HE2  sing N N 210 
LYS CE  HE3  sing N N 211 
LYS NZ  HZ1  sing N N 212 
LYS NZ  HZ2  sing N N 213 
LYS NZ  HZ3  sing N N 214 
LYS OXT HXT  sing N N 215 
MET N   CA   sing N N 216 
MET N   H    sing N N 217 
MET N   H2   sing N N 218 
MET CA  C    sing N N 219 
MET CA  CB   sing N N 220 
MET CA  HA   sing N N 221 
MET C   O    doub N N 222 
MET C   OXT  sing N N 223 
MET CB  CG   sing N N 224 
MET CB  HB2  sing N N 225 
MET CB  HB3  sing N N 226 
MET CG  SD   sing N N 227 
MET CG  HG2  sing N N 228 
MET CG  HG3  sing N N 229 
MET SD  CE   sing N N 230 
MET CE  HE1  sing N N 231 
MET CE  HE2  sing N N 232 
MET CE  HE3  sing N N 233 
MET OXT HXT  sing N N 234 
PHE N   CA   sing N N 235 
PHE N   H    sing N N 236 
PHE N   H2   sing N N 237 
PHE CA  C    sing N N 238 
PHE CA  CB   sing N N 239 
PHE CA  HA   sing N N 240 
PHE C   O    doub N N 241 
PHE C   OXT  sing N N 242 
PHE CB  CG   sing N N 243 
PHE CB  HB2  sing N N 244 
PHE CB  HB3  sing N N 245 
PHE CG  CD1  doub Y N 246 
PHE CG  CD2  sing Y N 247 
PHE CD1 CE1  sing Y N 248 
PHE CD1 HD1  sing N N 249 
PHE CD2 CE2  doub Y N 250 
PHE CD2 HD2  sing N N 251 
PHE CE1 CZ   doub Y N 252 
PHE CE1 HE1  sing N N 253 
PHE CE2 CZ   sing Y N 254 
PHE CE2 HE2  sing N N 255 
PHE CZ  HZ   sing N N 256 
PHE OXT HXT  sing N N 257 
PRO N   CA   sing N N 258 
PRO N   CD   sing N N 259 
PRO N   H    sing N N 260 
PRO CA  C    sing N N 261 
PRO CA  CB   sing N N 262 
PRO CA  HA   sing N N 263 
PRO C   O    doub N N 264 
PRO C   OXT  sing N N 265 
PRO CB  CG   sing N N 266 
PRO CB  HB2  sing N N 267 
PRO CB  HB3  sing N N 268 
PRO CG  CD   sing N N 269 
PRO CG  HG2  sing N N 270 
PRO CG  HG3  sing N N 271 
PRO CD  HD2  sing N N 272 
PRO CD  HD3  sing N N 273 
PRO OXT HXT  sing N N 274 
SER N   CA   sing N N 275 
SER N   H    sing N N 276 
SER N   H2   sing N N 277 
SER CA  C    sing N N 278 
SER CA  CB   sing N N 279 
SER CA  HA   sing N N 280 
SER C   O    doub N N 281 
SER C   OXT  sing N N 282 
SER CB  OG   sing N N 283 
SER CB  HB2  sing N N 284 
SER CB  HB3  sing N N 285 
SER OG  HG   sing N N 286 
SER OXT HXT  sing N N 287 
THR N   CA   sing N N 288 
THR N   H    sing N N 289 
THR N   H2   sing N N 290 
THR CA  C    sing N N 291 
THR CA  CB   sing N N 292 
THR CA  HA   sing N N 293 
THR C   O    doub N N 294 
THR C   OXT  sing N N 295 
THR CB  OG1  sing N N 296 
THR CB  CG2  sing N N 297 
THR CB  HB   sing N N 298 
THR OG1 HG1  sing N N 299 
THR CG2 HG21 sing N N 300 
THR CG2 HG22 sing N N 301 
THR CG2 HG23 sing N N 302 
THR OXT HXT  sing N N 303 
TRP N   CA   sing N N 304 
TRP N   H    sing N N 305 
TRP N   H2   sing N N 306 
TRP CA  C    sing N N 307 
TRP CA  CB   sing N N 308 
TRP CA  HA   sing N N 309 
TRP C   O    doub N N 310 
TRP C   OXT  sing N N 311 
TRP CB  CG   sing N N 312 
TRP CB  HB2  sing N N 313 
TRP CB  HB3  sing N N 314 
TRP CG  CD1  doub Y N 315 
TRP CG  CD2  sing Y N 316 
TRP CD1 NE1  sing Y N 317 
TRP CD1 HD1  sing N N 318 
TRP CD2 CE2  doub Y N 319 
TRP CD2 CE3  sing Y N 320 
TRP NE1 CE2  sing Y N 321 
TRP NE1 HE1  sing N N 322 
TRP CE2 CZ2  sing Y N 323 
TRP CE3 CZ3  doub Y N 324 
TRP CE3 HE3  sing N N 325 
TRP CZ2 CH2  doub Y N 326 
TRP CZ2 HZ2  sing N N 327 
TRP CZ3 CH2  sing Y N 328 
TRP CZ3 HZ3  sing N N 329 
TRP CH2 HH2  sing N N 330 
TRP OXT HXT  sing N N 331 
TYR N   CA   sing N N 332 
TYR N   H    sing N N 333 
TYR N   H2   sing N N 334 
TYR CA  C    sing N N 335 
TYR CA  CB   sing N N 336 
TYR CA  HA   sing N N 337 
TYR C   O    doub N N 338 
TYR C   OXT  sing N N 339 
TYR CB  CG   sing N N 340 
TYR CB  HB2  sing N N 341 
TYR CB  HB3  sing N N 342 
TYR CG  CD1  doub Y N 343 
TYR CG  CD2  sing Y N 344 
TYR CD1 CE1  sing Y N 345 
TYR CD1 HD1  sing N N 346 
TYR CD2 CE2  doub Y N 347 
TYR CD2 HD2  sing N N 348 
TYR CE1 CZ   doub Y N 349 
TYR CE1 HE1  sing N N 350 
TYR CE2 CZ   sing Y N 351 
TYR CE2 HE2  sing N N 352 
TYR CZ  OH   sing N N 353 
TYR OH  HH   sing N N 354 
TYR OXT HXT  sing N N 355 
VAL N   CA   sing N N 356 
VAL N   H    sing N N 357 
VAL N   H2   sing N N 358 
VAL CA  C    sing N N 359 
VAL CA  CB   sing N N 360 
VAL CA  HA   sing N N 361 
VAL C   O    doub N N 362 
VAL C   OXT  sing N N 363 
VAL CB  CG1  sing N N 364 
VAL CB  CG2  sing N N 365 
VAL CB  HB   sing N N 366 
VAL CG1 HG11 sing N N 367 
VAL CG1 HG12 sing N N 368 
VAL CG1 HG13 sing N N 369 
VAL CG2 HG21 sing N N 370 
VAL CG2 HG22 sing N N 371 
VAL CG2 HG23 sing N N 372 
VAL OXT HXT  sing N N 373 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-04-22 
_em_admin.deposition_site    PDBE 
_em_admin.entry_id           9F25 
_em_admin.last_update        2025-03-12 
_em_admin.map_release_date   2025-03-12 
_em_admin.title              'Cryo-EM structure of Botulinum neurotoxin A LC-HN domain' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_molwt.entity_assembly_id   1 
_em_entity_assembly_molwt.experimental_flag    NO 
_em_entity_assembly_molwt.id                   1 
_em_entity_assembly_molwt.units                MEGADALTONS 
_em_entity_assembly_molwt.value                0.15 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          1491 
_em_entity_assembly_naturalsource.organism             'Clostridium botulinum' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          866768 
_em_entity_assembly_recombinant.organism             
;Escherichia coli 'BL21-Gold(DE3)pLysS AG'
;
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         80 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 BIOCONTINUUM (6k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'MODEL REFINEMENT'              ? 1  ? ? ? PHENIX ? 
'IMAGE ACQUISITION'             ? 2  1 1 1 ?      ? 
'PARTICLE SELECTION'            ? 3  1 1 1 ?      ? 
'VOLUME SELECTION'              ? 4  1 1 1 ?      ? 
CLASSIFICATION                  ? 5  1 1 1 ?      ? 
MASKING                         ? 6  1 1 1 ?      ? 
RECONSTRUCTION                  ? 7  1 1 1 ?      ? 
'INITIAL EULER ASSIGNMENT'      ? 8  1 1 1 ?      ? 
'FINAL EULER ASSIGNMENT'        ? 9  1 1 1 ?      ? 
'CTF CORRECTION'                ? 10 1 1 1 ?      ? 
'LAYERLINE INDEXING'            ? 11 1 1 1 ?      ? 
'DIFFRACTION INDEXING'          ? 12 1 1 1 ?      ? 
'MODEL FITTING'                 ? 13 1 1 1 ?      ? 
'SERIES ALIGNMENT'              ? 14 1 1 1 ?      ? 
'MOLECULAR REPLACEMENT'         ? 15 1 1 1 ?      ? 
'LATTICE DISTORTION CORRECTION' ? 16 1 1 1 ?      ? 
'SYMMETRY DETERMINATION'        ? 17 1 1 1 ?      ? 
'CRYSTALLOGRAPHY MERGING'       ? 18 1 1 1 ?      ? 
OTHER                           ? 19 1 1 1 ?      ? 
# 
_em_specimen.concentration           ? 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Swiss National Science Foundation' Switzerland 310030_212253 1 
'Swiss National Science Foundation' Switzerland 198545        2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6UL6 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9F25 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   1.000000 
_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]   1.000000 
_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]   1.000000 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM 1    N N   . PRO A 1 19  ? 133.717 98.128  94.847  1.00 51.00  ? 2   PRO A N   1 
ATOM 2    C CA  . PRO A 1 19  ? 133.890 99.427  95.506  1.00 51.00  ? 2   PRO A CA  1 
ATOM 3    C C   . PRO A 1 19  ? 133.793 100.591 94.526  1.00 51.00  ? 2   PRO A C   1 
ATOM 4    O O   . PRO A 1 19  ? 134.031 100.404 93.333  1.00 51.00  ? 2   PRO A O   1 
ATOM 5    C CB  . PRO A 1 19  ? 135.299 99.333  96.103  1.00 51.00  ? 2   PRO A CB  1 
ATOM 6    C CG  . PRO A 1 19  ? 135.577 97.868  96.196  1.00 51.00  ? 2   PRO A CG  1 
ATOM 7    C CD  . PRO A 1 19  ? 134.906 97.276  95.000  1.00 51.00  ? 2   PRO A CD  1 
ATOM 8    N N   . PHE A 1 20  ? 133.437 101.775 95.028  1.00 51.64  ? 3   PHE A N   1 
ATOM 9    C CA  . PHE A 1 20  ? 133.326 102.946 94.165  1.00 51.64  ? 3   PHE A CA  1 
ATOM 10   C C   . PHE A 1 20  ? 134.674 103.294 93.546  1.00 51.64  ? 3   PHE A C   1 
ATOM 11   O O   . PHE A 1 20  ? 134.840 103.264 92.321  1.00 51.64  ? 3   PHE A O   1 
ATOM 12   C CB  . PHE A 1 20  ? 132.778 104.134 94.956  1.00 51.64  ? 3   PHE A CB  1 
ATOM 13   C CG  . PHE A 1 20  ? 132.009 105.114 94.119  1.00 51.64  ? 3   PHE A CG  1 
ATOM 14   C CD1 . PHE A 1 20  ? 131.331 104.693 92.988  1.00 51.64  ? 3   PHE A CD1 1 
ATOM 15   C CD2 . PHE A 1 20  ? 131.985 106.459 94.445  1.00 51.64  ? 3   PHE A CD2 1 
ATOM 16   C CE1 . PHE A 1 20  ? 130.622 105.590 92.214  1.00 51.64  ? 3   PHE A CE1 1 
ATOM 17   C CE2 . PHE A 1 20  ? 131.284 107.361 93.667  1.00 51.64  ? 3   PHE A CE2 1 
ATOM 18   C CZ  . PHE A 1 20  ? 130.602 106.925 92.551  1.00 51.64  ? 3   PHE A CZ  1 
ATOM 19   N N   . VAL A 1 21  ? 135.653 103.624 94.383  1.00 53.45  ? 4   VAL A N   1 
ATOM 20   C CA  . VAL A 1 21  ? 136.990 103.975 93.916  1.00 53.45  ? 4   VAL A CA  1 
ATOM 21   C C   . VAL A 1 21  ? 137.733 102.680 93.606  1.00 53.45  ? 4   VAL A C   1 
ATOM 22   O O   . VAL A 1 21  ? 138.055 101.906 94.511  1.00 53.45  ? 4   VAL A O   1 
ATOM 23   C CB  . VAL A 1 21  ? 137.744 104.816 94.951  1.00 53.45  ? 4   VAL A CB  1 
ATOM 24   C CG1 . VAL A 1 21  ? 139.031 105.361 94.357  1.00 53.45  ? 4   VAL A CG1 1 
ATOM 25   C CG2 . VAL A 1 21  ? 136.862 105.946 95.460  1.00 53.45  ? 4   VAL A CG2 1 
ATOM 26   N N   . ASN A 1 22  ? 138.006 102.441 92.322  1.00 58.22  ? 5   ASN A N   1 
ATOM 27   C CA  . ASN A 1 22  ? 138.631 101.186 91.915  1.00 58.22  ? 5   ASN A CA  1 
ATOM 28   C C   . ASN A 1 22  ? 140.078 101.111 92.388  1.00 58.22  ? 5   ASN A C   1 
ATOM 29   O O   . ASN A 1 22  ? 140.468 100.172 93.092  1.00 58.22  ? 5   ASN A O   1 
ATOM 30   C CB  . ASN A 1 22  ? 138.548 101.030 90.396  1.00 58.22  ? 5   ASN A CB  1 
ATOM 31   C CG  . ASN A 1 22  ? 137.377 100.170 89.963  1.00 58.22  ? 5   ASN A CG  1 
ATOM 32   O OD1 . ASN A 1 22  ? 137.201 99.052  90.448  1.00 58.22  ? 5   ASN A OD1 1 
ATOM 33   N ND2 . ASN A 1 22  ? 136.568 100.689 89.047  1.00 58.22  ? 5   ASN A ND2 1 
ATOM 34   N N   . LYS A 1 23  ? 140.891 102.092 92.010  1.00 58.65  ? 6   LYS A N   1 
ATOM 35   C CA  . LYS A 1 23  ? 142.296 102.135 92.386  1.00 58.65  ? 6   LYS A CA  1 
ATOM 36   C C   . LYS A 1 23  ? 142.547 103.312 93.320  1.00 58.65  ? 6   LYS A C   1 
ATOM 37   O O   . LYS A 1 23  ? 141.937 104.377 93.174  1.00 58.65  ? 6   LYS A O   1 
ATOM 38   C CB  . LYS A 1 23  ? 143.195 102.223 91.145  1.00 58.65  ? 6   LYS A CB  1 
ATOM 39   C CG  . LYS A 1 23  ? 143.406 103.625 90.597  1.00 58.65  ? 6   LYS A CG  1 
ATOM 40   C CD  . LYS A 1 23  ? 143.884 103.593 89.154  1.00 58.65  ? 6   LYS A CD  1 
ATOM 41   C CE  . LYS A 1 23  ? 145.002 102.583 88.957  1.00 58.65  ? 6   LYS A CE  1 
ATOM 42   N NZ  . LYS A 1 23  ? 145.658 102.739 87.630  1.00 58.65  ? 6   LYS A NZ  1 
ATOM 43   N N   . GLN A 1 24  ? 143.424 103.104 94.297  1.00 62.78  ? 7   GLN A N   1 
ATOM 44   C CA  . GLN A 1 24  ? 143.728 104.147 95.265  1.00 62.78  ? 7   GLN A CA  1 
ATOM 45   C C   . GLN A 1 24  ? 144.608 105.224 94.639  1.00 62.78  ? 7   GLN A C   1 
ATOM 46   O O   . GLN A 1 24  ? 145.472 104.948 93.803  1.00 62.78  ? 7   GLN A O   1 
ATOM 47   C CB  . GLN A 1 24  ? 144.417 103.550 96.491  1.00 62.78  ? 7   GLN A CB  1 
ATOM 48   C CG  . GLN A 1 24  ? 143.560 102.549 97.251  1.00 62.78  ? 7   GLN A CG  1 
ATOM 49   C CD  . GLN A 1 24  ? 143.765 101.124 96.775  1.00 62.78  ? 7   GLN A CD  1 
ATOM 50   O OE1 . GLN A 1 24  ? 144.253 100.891 95.669  1.00 62.78  ? 7   GLN A OE1 1 
ATOM 51   N NE2 . GLN A 1 24  ? 143.388 100.162 97.608  1.00 62.78  ? 7   GLN A NE2 1 
ATOM 52   N N   . PHE A 1 25  ? 144.380 106.466 95.059  1.00 58.28  ? 8   PHE A N   1 
ATOM 53   C CA  . PHE A 1 25  ? 145.094 107.618 94.534  1.00 58.28  ? 8   PHE A CA  1 
ATOM 54   C C   . PHE A 1 25  ? 145.813 108.349 95.659  1.00 58.28  ? 8   PHE A C   1 
ATOM 55   O O   . PHE A 1 25  ? 145.325 108.419 96.791  1.00 58.28  ? 8   PHE A O   1 
ATOM 56   C CB  . PHE A 1 25  ? 144.143 108.587 93.819  1.00 58.28  ? 8   PHE A CB  1 
ATOM 57   C CG  . PHE A 1 25  ? 143.477 108.002 92.609  1.00 58.28  ? 8   PHE A CG  1 
ATOM 58   C CD1 . PHE A 1 25  ? 144.187 107.809 91.437  1.00 58.28  ? 8   PHE A CD1 1 
ATOM 59   C CD2 . PHE A 1 25  ? 142.140 107.647 92.642  1.00 58.28  ? 8   PHE A CD2 1 
ATOM 60   C CE1 . PHE A 1 25  ? 143.576 107.273 90.321  1.00 58.28  ? 8   PHE A CE1 1 
ATOM 61   C CE2 . PHE A 1 25  ? 141.524 107.110 91.530  1.00 58.28  ? 8   PHE A CE2 1 
ATOM 62   C CZ  . PHE A 1 25  ? 142.243 106.924 90.368  1.00 58.28  ? 8   PHE A CZ  1 
ATOM 63   N N   . ASN A 1 26  ? 146.980 108.897 95.331  1.00 56.36  ? 9   ASN A N   1 
ATOM 64   C CA  . ASN A 1 26  ? 147.767 109.690 96.262  1.00 56.36  ? 9   ASN A CA  1 
ATOM 65   C C   . ASN A 1 26  ? 148.382 110.859 95.510  1.00 56.36  ? 9   ASN A C   1 
ATOM 66   O O   . ASN A 1 26  ? 148.581 110.795 94.294  1.00 56.36  ? 9   ASN A O   1 
ATOM 67   C CB  . ASN A 1 26  ? 148.863 108.855 96.937  1.00 56.36  ? 9   ASN A CB  1 
ATOM 68   C CG  . ASN A 1 26  ? 149.516 107.874 95.984  1.00 56.36  ? 9   ASN A CG  1 
ATOM 69   O OD1 . ASN A 1 26  ? 149.385 107.991 94.766  1.00 56.36  ? 9   ASN A OD1 1 
ATOM 70   N ND2 . ASN A 1 26  ? 150.227 106.898 96.537  1.00 56.36  ? 9   ASN A ND2 1 
ATOM 71   N N   . TYR A 1 27  ? 148.688 111.931 96.241  1.00 61.52  ? 10  TYR A N   1 
ATOM 72   C CA  . TYR A 1 27  ? 149.195 113.138 95.602  1.00 61.52  ? 10  TYR A CA  1 
ATOM 73   C C   . TYR A 1 27  ? 150.696 113.012 95.361  1.00 61.52  ? 10  TYR A C   1 
ATOM 74   O O   . TYR A 1 27  ? 151.473 113.906 95.707  1.00 61.52  ? 10  TYR A O   1 
ATOM 75   C CB  . TYR A 1 27  ? 148.873 114.365 96.462  1.00 61.52  ? 10  TYR A CB  1 
ATOM 76   C CG  . TYR A 1 27  ? 148.845 115.680 95.712  1.00 61.52  ? 10  TYR A CG  1 
ATOM 77   C CD1 . TYR A 1 27  ? 149.996 116.435 95.535  1.00 61.52  ? 10  TYR A CD1 1 
ATOM 78   C CD2 . TYR A 1 27  ? 147.658 116.170 95.185  1.00 61.52  ? 10  TYR A CD2 1 
ATOM 79   C CE1 . TYR A 1 27  ? 149.968 117.635 94.852  1.00 61.52  ? 10  TYR A CE1 1 
ATOM 80   C CE2 . TYR A 1 27  ? 147.619 117.369 94.500  1.00 61.52  ? 10  TYR A CE2 1 
ATOM 81   C CZ  . TYR A 1 27  ? 148.777 118.098 94.336  1.00 61.52  ? 10  TYR A CZ  1 
ATOM 82   O OH  . TYR A 1 27  ? 148.744 119.293 93.656  1.00 61.52  ? 10  TYR A OH  1 
ATOM 83   N N   . LYS A 1 28  ? 151.109 111.887 94.776  1.00 60.87  ? 11  LYS A N   1 
ATOM 84   C CA  . LYS A 1 28  ? 152.470 111.708 94.291  1.00 60.87  ? 11  LYS A CA  1 
ATOM 85   C C   . LYS A 1 28  ? 152.522 110.965 92.965  1.00 60.87  ? 11  LYS A C   1 
ATOM 86   O O   . LYS A 1 28  ? 153.616 110.786 92.421  1.00 60.87  ? 11  LYS A O   1 
ATOM 87   C CB  . LYS A 1 28  ? 153.328 110.962 95.329  1.00 60.87  ? 11  LYS A CB  1 
ATOM 88   C CG  . LYS A 1 28  ? 153.667 111.776 96.570  1.00 60.87  ? 11  LYS A CG  1 
ATOM 89   C CD  . LYS A 1 28  ? 153.555 110.942 97.836  1.00 60.87  ? 11  LYS A CD  1 
ATOM 90   C CE  . LYS A 1 28  ? 154.075 111.705 99.045  1.00 60.87  ? 11  LYS A CE  1 
ATOM 91   N NZ  . LYS A 1 28  ? 152.989 112.431 99.759  1.00 60.87  ? 11  LYS A NZ  1 
ATOM 92   N N   . ASP A 1 29  ? 151.387 110.529 92.437  1.00 61.61  ? 12  ASP A N   1 
ATOM 93   C CA  . ASP A 1 29  ? 151.367 109.768 91.196  1.00 61.61  ? 12  ASP A CA  1 
ATOM 94   C C   . ASP A 1 29  ? 151.671 110.691 90.020  1.00 61.61  ? 12  ASP A C   1 
ATOM 95   O O   . ASP A 1 29  ? 151.002 111.718 89.859  1.00 61.61  ? 12  ASP A O   1 
ATOM 96   C CB  . ASP A 1 29  ? 149.999 109.104 91.025  1.00 61.61  ? 12  ASP A CB  1 
ATOM 97   C CG  . ASP A 1 29  ? 149.973 108.062 89.919  1.00 61.61  ? 12  ASP A CG  1 
ATOM 98   O OD1 . ASP A 1 29  ? 151.014 107.826 89.276  1.00 61.61  ? 12  ASP A OD1 1 
ATOM 99   O OD2 . ASP A 1 29  ? 148.896 107.470 89.694  1.00 61.61  ? 12  ASP A OD2 1 
ATOM 100  N N   . PRO A 1 30  ? 152.671 110.378 89.195  1.00 64.04  ? 13  PRO A N   1 
ATOM 101  C CA  . PRO A 1 30  ? 152.924 111.197 88.005  1.00 64.04  ? 13  PRO A CA  1 
ATOM 102  C C   . PRO A 1 30  ? 151.732 111.190 87.059  1.00 64.04  ? 13  PRO A C   1 
ATOM 103  O O   . PRO A 1 30  ? 150.966 110.225 86.993  1.00 64.04  ? 13  PRO A O   1 
ATOM 104  C CB  . PRO A 1 30  ? 154.154 110.538 87.368  1.00 64.04  ? 13  PRO A CB  1 
ATOM 105  C CG  . PRO A 1 30  ? 154.228 109.171 87.974  1.00 64.04  ? 13  PRO A CG  1 
ATOM 106  C CD  . PRO A 1 30  ? 153.674 109.312 89.355  1.00 64.04  ? 13  PRO A CD  1 
ATOM 107  N N   . VAL A 1 31  ? 151.581 112.298 86.327  1.00 63.61  ? 14  VAL A N   1 
ATOM 108  C CA  . VAL A 1 31  ? 150.412 112.491 85.479  1.00 63.61  ? 14  VAL A CA  1 
ATOM 109  C C   . VAL A 1 31  ? 150.333 111.402 84.419  1.00 63.61  ? 14  VAL A C   1 
ATOM 110  O O   . VAL A 1 31  ? 151.340 111.022 83.806  1.00 63.61  ? 14  VAL A O   1 
ATOM 111  C CB  . VAL A 1 31  ? 150.451 113.888 84.839  1.00 63.61  ? 14  VAL A CB  1 
ATOM 112  C CG1 . VAL A 1 31  ? 149.116 114.216 84.192  1.00 63.61  ? 14  VAL A CG1 1 
ATOM 113  C CG2 . VAL A 1 31  ? 150.819 114.932 85.879  1.00 63.61  ? 14  VAL A CG2 1 
ATOM 114  N N   . ASN A 1 32  ? 149.122 110.895 84.199  1.00 56.04  ? 15  ASN A N   1 
ATOM 115  C CA  . ASN A 1 32  ? 148.854 109.822 83.251  1.00 56.04  ? 15  ASN A CA  1 
ATOM 116  C C   . ASN A 1 32  ? 148.054 110.313 82.055  1.00 56.04  ? 15  ASN A C   1 
ATOM 117  O O   . ASN A 1 32  ? 148.479 110.136 80.909  1.00 56.04  ? 15  ASN A O   1 
ATOM 118  C CB  . ASN A 1 32  ? 148.111 108.682 83.977  1.00 56.04  ? 15  ASN A CB  1 
ATOM 119  C CG  . ASN A 1 32  ? 147.735 107.510 83.064  1.00 56.04  ? 15  ASN A CG  1 
ATOM 120  O OD1 . ASN A 1 32  ? 147.665 107.627 81.842  1.00 56.04  ? 15  ASN A OD1 1 
ATOM 121  N ND2 . ASN A 1 32  ? 147.485 106.361 83.682  1.00 56.04  ? 15  ASN A ND2 1 
ATOM 122  N N   . GLY A 1 33  ? 146.902 110.939 82.293  1.00 57.01  ? 16  GLY A N   1 
ATOM 123  C CA  . GLY A 1 33  ? 146.069 111.462 81.228  1.00 57.01  ? 16  GLY A CA  1 
ATOM 124  C C   . GLY A 1 33  ? 144.729 110.780 81.062  1.00 57.01  ? 16  GLY A C   1 
ATOM 125  O O   . GLY A 1 33  ? 143.974 111.159 80.159  1.00 57.01  ? 16  GLY A O   1 
ATOM 126  N N   . VAL A 1 34  ? 144.403 109.790 81.892  1.00 52.21  ? 17  VAL A N   1 
ATOM 127  C CA  . VAL A 1 34  ? 143.121 109.100 81.796  1.00 52.21  ? 17  VAL A CA  1 
ATOM 128  C C   . VAL A 1 34  ? 142.360 109.258 83.106  1.00 52.21  ? 17  VAL A C   1 
ATOM 129  O O   . VAL A 1 34  ? 141.264 109.827 83.135  1.00 52.21  ? 17  VAL A O   1 
ATOM 130  C CB  . VAL A 1 34  ? 143.309 107.612 81.447  1.00 52.21  ? 17  VAL A CB  1 
ATOM 131  C CG1 . VAL A 1 34  ? 141.970 106.974 81.113  1.00 52.21  ? 17  VAL A CG1 1 
ATOM 132  C CG2 . VAL A 1 34  ? 144.283 107.455 80.288  1.00 52.21  ? 17  VAL A CG2 1 
ATOM 133  N N   . ASP A 1 35  ? 142.937 108.756 84.198  1.00 51.90  ? 18  ASP A N   1 
ATOM 134  C CA  . ASP A 1 35  ? 142.321 108.860 85.515  1.00 51.90  ? 18  ASP A CA  1 
ATOM 135  C C   . ASP A 1 35  ? 142.952 109.929 86.396  1.00 51.90  ? 18  ASP A C   1 
ATOM 136  O O   . ASP A 1 35  ? 142.315 110.375 87.357  1.00 51.90  ? 18  ASP A O   1 
ATOM 137  C CB  . ASP A 1 35  ? 142.372 107.502 86.231  1.00 51.90  ? 18  ASP A CB  1 
ATOM 138  C CG  . ASP A 1 35  ? 143.793 106.987 86.432  1.00 51.90  ? 18  ASP A CG  1 
ATOM 139  O OD1 . ASP A 1 35  ? 144.760 107.762 86.273  1.00 51.90  ? 18  ASP A OD1 1 
ATOM 140  O OD2 . ASP A 1 35  ? 143.941 105.789 86.750  1.00 51.90  ? 18  ASP A OD2 1 
ATOM 141  N N   . ILE A 1 36  ? 144.179 110.341 86.093  1.00 51.70  ? 19  ILE A N   1 
ATOM 142  C CA  . ILE A 1 36  ? 144.869 111.416 86.793  1.00 51.70  ? 19  ILE A CA  1 
ATOM 143  C C   . ILE A 1 36  ? 145.336 112.410 85.738  1.00 51.70  ? 19  ILE A C   1 
ATOM 144  O O   . ILE A 1 36  ? 145.855 112.004 84.690  1.00 51.70  ? 19  ILE A O   1 
ATOM 145  C CB  . ILE A 1 36  ? 146.045 110.876 87.638  1.00 51.70  ? 19  ILE A CB  1 
ATOM 146  C CG1 . ILE A 1 36  ? 146.219 111.666 88.930  1.00 51.70  ? 19  ILE A CG1 1 
ATOM 147  C CG2 . ILE A 1 36  ? 147.360 110.843 86.877  1.00 51.70  ? 19  ILE A CG2 1 
ATOM 148  C CD1 . ILE A 1 36  ? 147.118 110.957 89.912  1.00 51.70  ? 19  ILE A CD1 1 
ATOM 149  N N   . ALA A 1 37  ? 145.099 113.701 85.974  1.00 49.85  ? 20  ALA A N   1 
ATOM 150  C CA  . ALA A 1 37  ? 145.494 114.654 84.941  1.00 49.85  ? 20  ALA A CA  1 
ATOM 151  C C   . ALA A 1 37  ? 145.401 116.075 85.466  1.00 49.85  ? 20  ALA A C   1 
ATOM 152  O O   . ALA A 1 37  ? 144.609 116.367 86.362  1.00 49.85  ? 20  ALA A O   1 
ATOM 153  C CB  . ALA A 1 37  ? 144.620 114.521 83.684  1.00 49.85  ? 20  ALA A CB  1 
ATOM 154  N N   . TYR A 1 38  ? 146.214 116.955 84.889  1.00 51.28  ? 21  TYR A N   1 
ATOM 155  C CA  . TYR A 1 38  ? 145.962 118.382 85.021  1.00 51.28  ? 21  TYR A CA  1 
ATOM 156  C C   . TYR A 1 38  ? 144.705 118.737 84.239  1.00 51.28  ? 21  TYR A C   1 
ATOM 157  O O   . TYR A 1 38  ? 144.481 118.234 83.135  1.00 51.28  ? 21  TYR A O   1 
ATOM 158  C CB  . TYR A 1 38  ? 147.152 119.192 84.509  1.00 51.28  ? 21  TYR A CB  1 
ATOM 159  C CG  . TYR A 1 38  ? 148.308 119.285 85.480  1.00 51.28  ? 21  TYR A CG  1 
ATOM 160  C CD1 . TYR A 1 38  ? 149.300 118.315 85.506  1.00 51.28  ? 21  TYR A CD1 1 
ATOM 161  C CD2 . TYR A 1 38  ? 148.409 120.348 86.367  1.00 51.28  ? 21  TYR A CD2 1 
ATOM 162  C CE1 . TYR A 1 38  ? 150.359 118.400 86.390  1.00 51.28  ? 21  TYR A CE1 1 
ATOM 163  C CE2 . TYR A 1 38  ? 149.463 120.441 87.255  1.00 51.28  ? 21  TYR A CE2 1 
ATOM 164  C CZ  . TYR A 1 38  ? 150.435 119.464 87.262  1.00 51.28  ? 21  TYR A CZ  1 
ATOM 165  O OH  . TYR A 1 38  ? 151.487 119.552 88.144  1.00 51.28  ? 21  TYR A OH  1 
ATOM 166  N N   . ILE A 1 39  ? 143.864 119.590 84.822  1.00 54.00  ? 22  ILE A N   1 
ATOM 167  C CA  . ILE A 1 39  ? 142.593 119.950 84.216  1.00 54.00  ? 22  ILE A CA  1 
ATOM 168  C C   . ILE A 1 39  ? 142.404 121.458 84.283  1.00 54.00  ? 22  ILE A C   1 
ATOM 169  O O   . ILE A 1 39  ? 143.047 122.164 85.066  1.00 54.00  ? 22  ILE A O   1 
ATOM 170  C CB  . ILE A 1 39  ? 141.391 119.244 84.885  1.00 54.00  ? 22  ILE A CB  1 
ATOM 171  C CG1 . ILE A 1 39  ? 141.116 119.841 86.263  1.00 54.00  ? 22  ILE A CG1 1 
ATOM 172  C CG2 . ILE A 1 39  ? 141.626 117.748 84.994  1.00 54.00  ? 22  ILE A CG2 1 
ATOM 173  C CD1 . ILE A 1 39  ? 139.768 119.458 86.818  1.00 54.00  ? 22  ILE A CD1 1 
ATOM 174  N N   . LYS A 1 40  ? 141.506 121.935 83.426  1.00 49.85  ? 23  LYS A N   1 
ATOM 175  C CA  . LYS A 1 40  ? 141.016 123.305 83.423  1.00 49.85  ? 23  LYS A CA  1 
ATOM 176  C C   . LYS A 1 40  ? 139.496 123.268 83.472  1.00 49.85  ? 23  LYS A C   1 
ATOM 177  O O   . LYS A 1 40  ? 138.858 122.572 82.670  1.00 49.85  ? 23  LYS A O   1 
ATOM 178  C CB  . LYS A 1 40  ? 141.494 124.072 82.185  1.00 49.85  ? 23  LYS A CB  1 
ATOM 179  C CG  . LYS A 1 40  ? 142.982 123.946 81.911  1.00 49.85  ? 23  LYS A CG  1 
ATOM 180  C CD  . LYS A 1 40  ? 143.418 124.878 80.793  1.00 49.85  ? 23  LYS A CD  1 
ATOM 181  C CE  . LYS A 1 40  ? 143.342 124.190 79.441  1.00 49.85  ? 23  LYS A CE  1 
ATOM 182  N NZ  . LYS A 1 40  ? 144.559 124.441 78.622  1.00 49.85  ? 23  LYS A NZ  1 
ATOM 183  N N   . ILE A 1 41  ? 138.927 124.009 84.418  1.00 51.48  ? 24  ILE A N   1 
ATOM 184  C CA  . ILE A 1 41  ? 137.482 124.070 84.622  1.00 51.48  ? 24  ILE A CA  1 
ATOM 185  C C   . ILE A 1 41  ? 136.988 125.434 84.152  1.00 51.48  ? 24  ILE A C   1 
ATOM 186  O O   . ILE A 1 41  ? 137.786 126.379 84.067  1.00 51.48  ? 24  ILE A O   1 
ATOM 187  C CB  . ILE A 1 41  ? 137.116 123.818 86.093  1.00 51.48  ? 24  ILE A CB  1 
ATOM 188  C CG1 . ILE A 1 41  ? 138.124 124.496 87.019  1.00 51.48  ? 24  ILE A CG1 1 
ATOM 189  C CG2 . ILE A 1 41  ? 137.067 122.331 86.382  1.00 51.48  ? 24  ILE A CG2 1 
ATOM 190  C CD1 . ILE A 1 41  ? 137.625 124.666 88.433  1.00 51.48  ? 24  ILE A CD1 1 
ATOM 191  N N   . PRO A 1 42  ? 135.706 125.580 83.819  1.00 50.00  ? 25  PRO A N   1 
ATOM 192  C CA  . PRO A 1 42  ? 135.204 126.889 83.381  1.00 50.00  ? 25  PRO A CA  1 
ATOM 193  C C   . PRO A 1 42  ? 135.433 127.964 84.433  1.00 50.00  ? 25  PRO A C   1 
ATOM 194  O O   . PRO A 1 42  ? 135.302 127.726 85.635  1.00 50.00  ? 25  PRO A O   1 
ATOM 195  C CB  . PRO A 1 42  ? 133.706 126.647 83.151  1.00 50.00  ? 25  PRO A CB  1 
ATOM 196  C CG  . PRO A 1 42  ? 133.449 125.201 83.433  1.00 50.00  ? 25  PRO A CG  1 
ATOM 197  C CD  . PRO A 1 42  ? 134.750 124.493 83.552  1.00 50.00  ? 25  PRO A CD  1 
ATOM 198  N N   . ASN A 1 43  ? 135.784 129.159 83.962  1.00 56.09  ? 26  ASN A N   1 
ATOM 199  C CA  . ASN A 1 43  ? 135.991 130.305 84.834  1.00 56.09  ? 26  ASN A CA  1 
ATOM 200  C C   . ASN A 1 43  ? 135.774 131.580 84.032  1.00 56.09  ? 26  ASN A C   1 
ATOM 201  O O   . ASN A 1 43  ? 135.824 131.576 82.799  1.00 56.09  ? 26  ASN A O   1 
ATOM 202  C CB  . ASN A 1 43  ? 137.389 130.291 85.466  1.00 56.09  ? 26  ASN A CB  1 
ATOM 203  C CG  . ASN A 1 43  ? 138.476 130.672 84.483  1.00 56.09  ? 26  ASN A CG  1 
ATOM 204  O OD1 . ASN A 1 43  ? 138.429 130.301 83.311  1.00 56.09  ? 26  ASN A OD1 1 
ATOM 205  N ND2 . ASN A 1 43  ? 139.467 131.417 84.959  1.00 56.09  ? 26  ASN A ND2 1 
ATOM 206  N N   . ALA A 1 44  ? 135.522 132.676 84.752  1.00 62.11  ? 27  ALA A N   1 
ATOM 207  C CA  . ALA A 1 44  ? 135.258 133.950 84.090  1.00 62.11  ? 27  ALA A CA  1 
ATOM 208  C C   . ALA A 1 44  ? 136.477 134.443 83.322  1.00 62.11  ? 27  ALA A C   1 
ATOM 209  O O   . ALA A 1 44  ? 136.351 134.948 82.200  1.00 62.11  ? 27  ALA A O   1 
ATOM 210  C CB  . ALA A 1 44  ? 134.812 134.992 85.115  1.00 62.11  ? 27  ALA A CB  1 
ATOM 211  N N   . GLY A 1 45  ? 137.664 134.307 83.905  1.00 61.56  ? 28  GLY A N   1 
ATOM 212  C CA  . GLY A 1 45  ? 138.878 134.757 83.252  1.00 61.56  ? 28  GLY A CA  1 
ATOM 213  C C   . GLY A 1 45  ? 139.735 133.619 82.739  1.00 61.56  ? 28  GLY A C   1 
ATOM 214  O O   . GLY A 1 45  ? 139.249 132.743 82.017  1.00 61.56  ? 28  GLY A O   1 
ATOM 215  N N   . GLN A 1 46  ? 141.014 133.623 83.102  1.00 56.90  ? 29  GLN A N   1 
ATOM 216  C CA  . GLN A 1 46  ? 141.951 132.577 82.718  1.00 56.90  ? 29  GLN A CA  1 
ATOM 217  C C   . GLN A 1 46  ? 142.575 131.987 83.973  1.00 56.90  ? 29  GLN A C   1 
ATOM 218  O O   . GLN A 1 46  ? 142.990 132.728 84.871  1.00 56.90  ? 29  GLN A O   1 
ATOM 219  C CB  . GLN A 1 46  ? 143.038 133.126 81.784  1.00 56.90  ? 29  GLN A CB  1 
ATOM 220  C CG  . GLN A 1 46  ? 144.272 132.237 81.620  1.00 56.90  ? 29  GLN A CG  1 
ATOM 221  C CD  . GLN A 1 46  ? 143.957 130.815 81.173  1.00 56.90  ? 29  GLN A CD  1 
ATOM 222  O OE1 . GLN A 1 46  ? 142.868 130.525 80.676  1.00 56.90  ? 29  GLN A OE1 1 
ATOM 223  N NE2 . GLN A 1 46  ? 144.920 129.918 81.353  1.00 56.90  ? 29  GLN A NE2 1 
ATOM 224  N N   . MET A 1 47  ? 142.640 130.659 84.034  1.00 59.98  ? 30  MET A N   1 
ATOM 225  C CA  . MET A 1 47  ? 143.192 129.958 85.183  1.00 59.98  ? 30  MET A CA  1 
ATOM 226  C C   . MET A 1 47  ? 144.265 128.980 84.727  1.00 59.98  ? 30  MET A C   1 
ATOM 227  O O   . MET A 1 47  ? 144.232 128.474 83.602  1.00 59.98  ? 30  MET A O   1 
ATOM 228  C CB  . MET A 1 47  ? 142.106 129.205 85.965  1.00 59.98  ? 30  MET A CB  1 
ATOM 229  C CG  . MET A 1 47  ? 141.103 128.465 85.094  1.00 59.98  ? 30  MET A CG  1 
ATOM 230  S SD  . MET A 1 47  ? 141.661 126.818 84.620  1.00 59.98  ? 30  MET A SD  1 
ATOM 231  C CE  . MET A 1 47  ? 141.313 125.899 86.115  1.00 59.98  ? 30  MET A CE  1 
ATOM 232  N N   . GLN A 1 48  ? 145.222 128.727 85.614  1.00 52.88  ? 31  GLN A N   1 
ATOM 233  C CA  . GLN A 1 48  ? 146.265 127.752 85.348  1.00 52.88  ? 31  GLN A CA  1 
ATOM 234  C C   . GLN A 1 48  ? 145.742 126.335 85.579  1.00 52.88  ? 31  GLN A C   1 
ATOM 235  O O   . GLN A 1 48  ? 144.831 126.127 86.385  1.00 52.88  ? 31  GLN A O   1 
ATOM 236  C CB  . GLN A 1 48  ? 147.474 128.012 86.242  1.00 52.88  ? 31  GLN A CB  1 
ATOM 237  C CG  . GLN A 1 48  ? 148.399 129.123 85.754  1.00 52.88  ? 31  GLN A CG  1 
ATOM 238  C CD  . GLN A 1 48  ? 148.757 128.999 84.282  1.00 52.88  ? 31  GLN A CD  1 
ATOM 239  O OE1 . GLN A 1 48  ? 148.030 129.473 83.409  1.00 52.88  ? 31  GLN A OE1 1 
ATOM 240  N NE2 . GLN A 1 48  ? 149.886 128.358 84.003  1.00 52.88  ? 31  GLN A NE2 1 
ATOM 241  N N   . PRO A 1 49  ? 146.294 125.347 84.875  1.00 49.85  ? 32  PRO A N   1 
ATOM 242  C CA  . PRO A 1 49  ? 145.854 123.962 85.081  1.00 49.85  ? 32  PRO A CA  1 
ATOM 243  C C   . PRO A 1 49  ? 146.107 123.501 86.508  1.00 49.85  ? 32  PRO A C   1 
ATOM 244  O O   . PRO A 1 49  ? 147.079 123.904 87.152  1.00 49.85  ? 32  PRO A O   1 
ATOM 245  C CB  . PRO A 1 49  ? 146.700 123.168 84.079  1.00 49.85  ? 32  PRO A CB  1 
ATOM 246  C CG  . PRO A 1 49  ? 147.097 124.167 83.044  1.00 49.85  ? 32  PRO A CG  1 
ATOM 247  C CD  . PRO A 1 49  ? 147.280 125.455 83.787  1.00 49.85  ? 32  PRO A CD  1 
ATOM 248  N N   . VAL A 1 50  ? 145.214 122.647 87.003  1.00 49.85  ? 33  VAL A N   1 
ATOM 249  C CA  . VAL A 1 50  ? 145.289 122.135 88.366  1.00 49.85  ? 33  VAL A CA  1 
ATOM 250  C C   . VAL A 1 50  ? 145.145 120.620 88.329  1.00 49.85  ? 33  VAL A C   1 
ATOM 251  O O   . VAL A 1 50  ? 144.312 120.088 87.590  1.00 49.85  ? 33  VAL A O   1 
ATOM 252  C CB  . VAL A 1 50  ? 144.211 122.773 89.270  1.00 49.85  ? 33  VAL A CB  1 
ATOM 253  C CG1 . VAL A 1 50  ? 142.838 122.665 88.625  1.00 49.85  ? 33  VAL A CG1 1 
ATOM 254  C CG2 . VAL A 1 50  ? 144.214 122.130 90.642  1.00 49.85  ? 33  VAL A CG2 1 
ATOM 255  N N   . LYS A 1 51  ? 145.972 119.924 89.105  1.00 51.70  ? 34  LYS A N   1 
ATOM 256  C CA  . LYS A 1 51  ? 145.927 118.467 89.117  1.00 51.70  ? 34  LYS A CA  1 
ATOM 257  C C   . LYS A 1 51  ? 144.602 117.975 89.689  1.00 51.70  ? 34  LYS A C   1 
ATOM 258  O O   . LYS A 1 51  ? 144.061 118.554 90.635  1.00 51.70  ? 34  LYS A O   1 
ATOM 259  C CB  . LYS A 1 51  ? 147.092 117.902 89.928  1.00 51.70  ? 34  LYS A CB  1 
ATOM 260  C CG  . LYS A 1 51  ? 147.301 116.407 89.744  1.00 51.70  ? 34  LYS A CG  1 
ATOM 261  C CD  . LYS A 1 51  ? 148.692 115.980 90.177  1.00 51.70  ? 34  LYS A CD  1 
ATOM 262  C CE  . LYS A 1 51  ? 148.881 114.482 90.007  1.00 51.70  ? 34  LYS A CE  1 
ATOM 263  N NZ  . LYS A 1 51  ? 150.263 114.054 90.354  1.00 51.70  ? 34  LYS A NZ  1 
ATOM 264  N N   . ALA A 1 52  ? 144.080 116.897 89.107  1.00 49.85  ? 35  ALA A N   1 
ATOM 265  C CA  . ALA A 1 52  ? 142.790 116.357 89.498  1.00 49.85  ? 35  ALA A CA  1 
ATOM 266  C C   . ALA A 1 52  ? 142.799 114.847 89.325  1.00 49.85  ? 35  ALA A C   1 
ATOM 267  O O   . ALA A 1 52  ? 143.480 114.303 88.442  1.00 49.85  ? 35  ALA A O   1 
ATOM 268  C CB  . ALA A 1 52  ? 141.649 116.973 88.683  1.00 49.85  ? 35  ALA A CB  1 
ATOM 269  N N   . PHE A 1 53  ? 142.022 114.180 90.178  1.00 49.85  ? 36  PHE A N   1 
ATOM 270  C CA  . PHE A 1 53  ? 141.942 112.726 90.229  1.00 49.85  ? 36  PHE A CA  1 
ATOM 271  C C   . PHE A 1 53  ? 140.509 112.308 89.940  1.00 49.85  ? 36  PHE A C   1 
ATOM 272  O O   . PHE A 1 53  ? 139.599 112.665 90.691  1.00 49.85  ? 36  PHE A O   1 
ATOM 273  C CB  . PHE A 1 53  ? 142.368 112.195 91.603  1.00 49.85  ? 36  PHE A CB  1 
ATOM 274  C CG  . PHE A 1 53  ? 143.609 112.839 92.157  1.00 49.85  ? 36  PHE A CG  1 
ATOM 275  C CD1 . PHE A 1 53  ? 143.547 114.055 92.815  1.00 49.85  ? 36  PHE A CD1 1 
ATOM 276  C CD2 . PHE A 1 53  ? 144.831 112.207 92.055  1.00 49.85  ? 36  PHE A CD2 1 
ATOM 277  C CE1 . PHE A 1 53  ? 144.689 114.638 93.327  1.00 49.85  ? 36  PHE A CE1 1 
ATOM 278  C CE2 . PHE A 1 53  ? 145.974 112.786 92.569  1.00 49.85  ? 36  PHE A CE2 1 
ATOM 279  C CZ  . PHE A 1 53  ? 145.902 114.001 93.206  1.00 49.85  ? 36  PHE A CZ  1 
ATOM 280  N N   . LYS A 1 54  ? 140.303 111.552 88.868  1.00 51.36  ? 37  LYS A N   1 
ATOM 281  C CA  . LYS A 1 54  ? 138.985 110.986 88.622  1.00 51.36  ? 37  LYS A CA  1 
ATOM 282  C C   . LYS A 1 54  ? 138.808 109.769 89.522  1.00 51.36  ? 37  LYS A C   1 
ATOM 283  O O   . LYS A 1 54  ? 139.708 108.929 89.625  1.00 51.36  ? 37  LYS A O   1 
ATOM 284  C CB  . LYS A 1 54  ? 138.812 110.626 87.143  1.00 51.36  ? 37  LYS A CB  1 
ATOM 285  C CG  . LYS A 1 54  ? 138.679 109.143 86.830  1.00 51.36  ? 37  LYS A CG  1 
ATOM 286  C CD  . LYS A 1 54  ? 138.288 108.917 85.379  1.00 51.36  ? 37  LYS A CD  1 
ATOM 287  C CE  . LYS A 1 54  ? 136.853 109.345 85.122  1.00 51.36  ? 37  LYS A CE  1 
ATOM 288  N NZ  . LYS A 1 54  ? 136.366 108.889 83.792  1.00 51.36  ? 37  LYS A NZ  1 
ATOM 289  N N   . ILE A 1 55  ? 137.676 109.700 90.218  1.00 49.85  ? 38  ILE A N   1 
ATOM 290  C CA  . ILE A 1 55  ? 137.446 108.619 91.168  1.00 49.85  ? 38  ILE A CA  1 
ATOM 291  C C   . ILE A 1 55  ? 136.423 107.609 90.673  1.00 49.85  ? 38  ILE A C   1 
ATOM 292  O O   . ILE A 1 55  ? 136.451 106.454 91.126  1.00 49.85  ? 38  ILE A O   1 
ATOM 293  C CB  . ILE A 1 55  ? 137.037 109.158 92.555  1.00 49.85  ? 38  ILE A CB  1 
ATOM 294  C CG1 . ILE A 1 55  ? 135.714 109.917 92.474  1.00 49.85  ? 38  ILE A CG1 1 
ATOM 295  C CG2 . ILE A 1 55  ? 138.129 110.047 93.125  1.00 49.85  ? 38  ILE A CG2 1 
ATOM 296  C CD1 . ILE A 1 55  ? 135.184 110.349 93.824  1.00 49.85  ? 38  ILE A CD1 1 
ATOM 297  N N   . HIS A 1 56  ? 135.533 107.993 89.767  1.00 49.85  ? 39  HIS A N   1 
ATOM 298  C CA  . HIS A 1 56  ? 134.602 107.066 89.141  1.00 49.85  ? 39  HIS A CA  1 
ATOM 299  C C   . HIS A 1 56  ? 134.159 107.692 87.827  1.00 49.85  ? 39  HIS A C   1 
ATOM 300  O O   . HIS A 1 56  ? 134.634 108.763 87.439  1.00 49.85  ? 39  HIS A O   1 
ATOM 301  C CB  . HIS A 1 56  ? 133.421 106.754 90.066  1.00 49.85  ? 39  HIS A CB  1 
ATOM 302  C CG  . HIS A 1 56  ? 132.649 105.534 89.671  1.00 49.85  ? 39  HIS A CG  1 
ATOM 303  N ND1 . HIS A 1 56  ? 133.071 104.258 89.975  1.00 49.85  ? 39  HIS A ND1 1 
ATOM 304  C CD2 . HIS A 1 56  ? 131.477 105.393 89.006  1.00 49.85  ? 39  HIS A CD2 1 
ATOM 305  C CE1 . HIS A 1 56  ? 132.197 103.384 89.510  1.00 49.85  ? 39  HIS A CE1 1 
ATOM 306  N NE2 . HIS A 1 56  ? 131.220 104.047 88.917  1.00 49.85  ? 39  HIS A NE2 1 
ATOM 307  N N   . ASN A 1 57  ? 133.255 107.010 87.131  1.00 53.34  ? 40  ASN A N   1 
ATOM 308  C CA  . ASN A 1 57  ? 132.728 107.540 85.883  1.00 53.34  ? 40  ASN A CA  1 
ATOM 309  C C   . ASN A 1 57  ? 132.044 108.879 86.128  1.00 53.34  ? 40  ASN A C   1 
ATOM 310  O O   . ASN A 1 57  ? 131.153 108.991 86.974  1.00 53.34  ? 40  ASN A O   1 
ATOM 311  C CB  . ASN A 1 57  ? 131.749 106.544 85.263  1.00 53.34  ? 40  ASN A CB  1 
ATOM 312  C CG  . ASN A 1 57  ? 131.726 106.615 83.751  1.00 53.34  ? 40  ASN A CG  1 
ATOM 313  O OD1 . ASN A 1 57  ? 132.620 107.190 83.131  1.00 53.34  ? 40  ASN A OD1 1 
ATOM 314  N ND2 . ASN A 1 57  ? 130.704 106.022 83.147  1.00 53.34  ? 40  ASN A ND2 1 
ATOM 315  N N   . LYS A 1 58  ? 132.486 109.900 85.393  1.00 49.85  ? 41  LYS A N   1 
ATOM 316  C CA  . LYS A 1 58  ? 131.915 111.245 85.429  1.00 49.85  ? 41  LYS A CA  1 
ATOM 317  C C   . LYS A 1 58  ? 132.057 111.917 86.793  1.00 49.85  ? 41  LYS A C   1 
ATOM 318  O O   . LYS A 1 58  ? 131.309 112.849 87.102  1.00 49.85  ? 41  LYS A O   1 
ATOM 319  C CB  . LYS A 1 58  ? 130.438 111.235 85.012  1.00 49.85  ? 41  LYS A CB  1 
ATOM 320  C CG  . LYS A 1 58  ? 130.146 110.470 83.733  1.00 49.85  ? 41  LYS A CG  1 
ATOM 321  C CD  . LYS A 1 58  ? 130.643 111.214 82.507  1.00 49.85  ? 41  LYS A CD  1 
ATOM 322  C CE  . LYS A 1 58  ? 130.270 110.471 81.234  1.00 49.85  ? 41  LYS A CE  1 
ATOM 323  N NZ  . LYS A 1 58  ? 130.711 111.200 80.014  1.00 49.85  ? 41  LYS A NZ  1 
ATOM 324  N N   . ILE A 1 59  ? 132.993 111.476 87.632  1.00 49.85  ? 42  ILE A N   1 
ATOM 325  C CA  . ILE A 1 59  ? 133.206 112.087 88.940  1.00 49.85  ? 42  ILE A CA  1 
ATOM 326  C C   . ILE A 1 59  ? 134.699 112.318 89.141  1.00 49.85  ? 42  ILE A C   1 
ATOM 327  O O   . ILE A 1 59  ? 135.489 111.363 89.138  1.00 49.85  ? 42  ILE A O   1 
ATOM 328  C CB  . ILE A 1 59  ? 132.633 111.234 90.083  1.00 49.85  ? 42  ILE A CB  1 
ATOM 329  C CG1 . ILE A 1 59  ? 131.126 111.044 89.906  1.00 49.85  ? 42  ILE A CG1 1 
ATOM 330  C CG2 . ILE A 1 59  ? 132.901 111.901 91.417  1.00 49.85  ? 42  ILE A CG2 1 
ATOM 331  C CD1 . ILE A 1 59  ? 130.471 110.265 91.024  1.00 49.85  ? 42  ILE A CD1 1 
ATOM 332  N N   . TRP A 1 60  ? 135.077 113.577 89.342  1.00 49.85  ? 43  TRP A N   1 
ATOM 333  C CA  . TRP A 1 60  ? 136.455 113.978 89.574  1.00 49.85  ? 43  TRP A CA  1 
ATOM 334  C C   . TRP A 1 60  ? 136.563 114.691 90.915  1.00 49.85  ? 43  TRP A C   1 
ATOM 335  O O   . TRP A 1 60  ? 135.573 115.189 91.458  1.00 49.85  ? 43  TRP A O   1 
ATOM 336  C CB  . TRP A 1 60  ? 136.967 114.901 88.459  1.00 49.85  ? 43  TRP A CB  1 
ATOM 337  C CG  . TRP A 1 60  ? 136.981 114.279 87.096  1.00 49.85  ? 43  TRP A CG  1 
ATOM 338  C CD1 . TRP A 1 60  ? 135.904 113.847 86.380  1.00 49.85  ? 43  TRP A CD1 1 
ATOM 339  C CD2 . TRP A 1 60  ? 138.130 114.036 86.277  1.00 49.85  ? 43  TRP A CD2 1 
ATOM 340  N NE1 . TRP A 1 60  ? 136.312 113.342 85.170  1.00 49.85  ? 43  TRP A NE1 1 
ATOM 341  C CE2 . TRP A 1 60  ? 137.674 113.447 85.082  1.00 49.85  ? 43  TRP A CE2 1 
ATOM 342  C CE3 . TRP A 1 60  ? 139.501 114.256 86.440  1.00 49.85  ? 43  TRP A CE3 1 
ATOM 343  C CZ2 . TRP A 1 60  ? 138.539 113.076 84.056  1.00 49.85  ? 43  TRP A CZ2 1 
ATOM 344  C CZ3 . TRP A 1 60  ? 140.357 113.887 85.420  1.00 49.85  ? 43  TRP A CZ3 1 
ATOM 345  C CH2 . TRP A 1 60  ? 139.874 113.303 84.244  1.00 49.85  ? 43  TRP A CH2 1 
ATOM 346  N N   . VAL A 1 61  ? 137.781 114.734 91.450  1.00 49.85  ? 44  VAL A N   1 
ATOM 347  C CA  . VAL A 1 61  ? 138.081 115.449 92.682  1.00 49.85  ? 44  VAL A CA  1 
ATOM 348  C C   . VAL A 1 61  ? 139.299 116.333 92.450  1.00 49.85  ? 44  VAL A C   1 
ATOM 349  O O   . VAL A 1 61  ? 140.227 115.963 91.718  1.00 49.85  ? 44  VAL A O   1 
ATOM 350  C CB  . VAL A 1 61  ? 138.311 114.494 93.876  1.00 49.85  ? 44  VAL A CB  1 
ATOM 351  C CG1 . VAL A 1 61  ? 137.161 113.508 94.007  1.00 49.85  ? 44  VAL A CG1 1 
ATOM 352  C CG2 . VAL A 1 61  ? 139.630 113.752 93.739  1.00 49.85  ? 44  VAL A CG2 1 
ATOM 353  N N   . ILE A 1 62  ? 139.271 117.518 93.052  1.00 49.85  ? 45  ILE A N   1 
ATOM 354  C CA  . ILE A 1 62  ? 140.354 118.493 92.976  1.00 49.85  ? 45  ILE A CA  1 
ATOM 355  C C   . ILE A 1 62  ? 140.743 118.877 94.398  1.00 49.85  ? 45  ILE A C   1 
ATOM 356  O O   . ILE A 1 62  ? 140.141 119.793 94.975  1.00 49.85  ? 45  ILE A O   1 
ATOM 357  C CB  . ILE A 1 62  ? 139.940 119.734 92.170  1.00 49.85  ? 45  ILE A CB  1 
ATOM 358  C CG1 . ILE A 1 62  ? 139.438 119.339 90.782  1.00 49.85  ? 45  ILE A CG1 1 
ATOM 359  C CG2 . ILE A 1 62  ? 141.104 120.707 92.052  1.00 49.85  ? 45  ILE A CG2 1 
ATOM 360  C CD1 . ILE A 1 62  ? 138.730 120.463 90.064  1.00 49.85  ? 45  ILE A CD1 1 
ATOM 361  N N   . PRO A 1 63  ? 141.726 118.214 95.006  1.00 49.85  ? 46  PRO A N   1 
ATOM 362  C CA  . PRO A 1 63  ? 142.096 118.555 96.386  1.00 49.85  ? 46  PRO A CA  1 
ATOM 363  C C   . PRO A 1 63  ? 142.796 119.900 96.480  1.00 49.85  ? 46  PRO A C   1 
ATOM 364  O O   . PRO A 1 63  ? 143.950 119.983 96.911  1.00 49.85  ? 46  PRO A O   1 
ATOM 365  C CB  . PRO A 1 63  ? 143.026 117.407 96.805  1.00 49.85  ? 46  PRO A CB  1 
ATOM 366  C CG  . PRO A 1 63  ? 142.941 116.383 95.712  1.00 49.85  ? 46  PRO A CG  1 
ATOM 367  C CD  . PRO A 1 63  ? 142.527 117.102 94.476  1.00 49.85  ? 46  PRO A CD  1 
ATOM 368  N N   . GLU A 1 64  ? 142.102 120.959 96.074  1.00 49.85  ? 47  GLU A N   1 
ATOM 369  C CA  . GLU A 1 64  ? 142.625 122.313 96.139  1.00 49.85  ? 47  GLU A CA  1 
ATOM 370  C C   . GLU A 1 64  ? 141.543 123.233 96.678  1.00 49.85  ? 47  GLU A C   1 
ATOM 371  O O   . GLU A 1 64  ? 140.348 122.954 96.547  1.00 49.85  ? 47  GLU A O   1 
ATOM 372  C CB  . GLU A 1 64  ? 143.095 122.810 94.766  1.00 49.85  ? 47  GLU A CB  1 
ATOM 373  C CG  . GLU A 1 64  ? 144.301 122.073 94.215  1.00 49.85  ? 47  GLU A CG  1 
ATOM 374  C CD  . GLU A 1 64  ? 145.612 122.640 94.720  1.00 49.85  ? 47  GLU A CD  1 
ATOM 375  O OE1 . GLU A 1 64  ? 145.616 123.790 95.208  1.00 49.85  ? 47  GLU A OE1 1 
ATOM 376  O OE2 . GLU A 1 64  ? 146.639 121.939 94.621  1.00 49.85  ? 47  GLU A OE2 1 
ATOM 377  N N   . ARG A 1 65  ? 141.975 124.327 97.299  1.00 54.18  ? 48  ARG A N   1 
ATOM 378  C CA  . ARG A 1 65  ? 141.042 125.331 97.782  1.00 54.18  ? 48  ARG A CA  1 
ATOM 379  C C   . ARG A 1 65  ? 140.328 125.991 96.608  1.00 54.18  ? 48  ARG A C   1 
ATOM 380  O O   . ARG A 1 65  ? 140.869 126.103 95.505  1.00 54.18  ? 48  ARG A O   1 
ATOM 381  C CB  . ARG A 1 65  ? 141.775 126.380 98.618  1.00 54.18  ? 48  ARG A CB  1 
ATOM 382  C CG  . ARG A 1 65  ? 141.907 126.015 100.087 1.00 54.18  ? 48  ARG A CG  1 
ATOM 383  C CD  . ARG A 1 65  ? 141.066 126.927 100.961 1.00 54.18  ? 48  ARG A CD  1 
ATOM 384  N NE  . ARG A 1 65  ? 141.190 126.597 102.375 1.00 54.18  ? 48  ARG A NE  1 
ATOM 385  C CZ  . ARG A 1 65  ? 142.133 127.074 103.176 1.00 54.18  ? 48  ARG A CZ  1 
ATOM 386  N NH1 . ARG A 1 65  ? 143.066 127.898 102.731 1.00 54.18  ? 48  ARG A NH1 1 
ATOM 387  N NH2 . ARG A 1 65  ? 142.142 126.711 104.455 1.00 54.18  ? 48  ARG A NH2 1 
ATOM 388  N N   . ASP A 1 66  ? 139.096 126.431 96.854  1.00 65.13  ? 49  ASP A N   1 
ATOM 389  C CA  . ASP A 1 66  ? 138.241 126.953 95.790  1.00 65.13  ? 49  ASP A CA  1 
ATOM 390  C C   . ASP A 1 66  ? 138.653 128.385 95.476  1.00 65.13  ? 49  ASP A C   1 
ATOM 391  O O   . ASP A 1 66  ? 138.199 129.343 96.103  1.00 65.13  ? 49  ASP A O   1 
ATOM 392  C CB  . ASP A 1 66  ? 136.773 126.870 96.187  1.00 65.13  ? 49  ASP A CB  1 
ATOM 393  C CG  . ASP A 1 66  ? 135.842 126.991 94.998  1.00 65.13  ? 49  ASP A CG  1 
ATOM 394  O OD1 . ASP A 1 66  ? 136.342 127.153 93.865  1.00 65.13  ? 49  ASP A OD1 1 
ATOM 395  O OD2 . ASP A 1 66  ? 134.612 126.919 95.193  1.00 65.13  ? 49  ASP A OD2 1 
ATOM 396  N N   . THR A 1 67  ? 139.534 128.526 94.484  1.00 69.05  ? 50  THR A N   1 
ATOM 397  C CA  . THR A 1 67  ? 139.929 129.829 93.966  1.00 69.05  ? 50  THR A CA  1 
ATOM 398  C C   . THR A 1 67  ? 139.770 129.909 92.453  1.00 69.05  ? 50  THR A C   1 
ATOM 399  O O   . THR A 1 67  ? 140.250 130.871 91.841  1.00 69.05  ? 50  THR A O   1 
ATOM 400  C CB  . THR A 1 67  ? 141.379 130.154 94.347  1.00 69.05  ? 50  THR A CB  1 
ATOM 401  O OG1 . THR A 1 67  ? 142.249 129.132 93.845  1.00 69.05  ? 50  THR A OG1 1 
ATOM 402  C CG2 . THR A 1 67  ? 141.530 130.244 95.855  1.00 69.05  ? 50  THR A CG2 1 
ATOM 403  N N   . PHE A 1 68  ? 139.110 128.930 91.837  1.00 70.66  ? 51  PHE A N   1 
ATOM 404  C CA  . PHE A 1 68  ? 138.988 128.841 90.388  1.00 70.66  ? 51  PHE A CA  1 
ATOM 405  C C   . PHE A 1 68  ? 137.574 129.112 89.897  1.00 70.66  ? 51  PHE A C   1 
ATOM 406  O O   . PHE A 1 68  ? 137.375 129.958 89.020  1.00 70.66  ? 51  PHE A O   1 
ATOM 407  C CB  . PHE A 1 68  ? 139.438 127.452 89.911  1.00 70.66  ? 51  PHE A CB  1 
ATOM 408  C CG  . PHE A 1 68  ? 140.754 127.006 90.484  1.00 70.66  ? 51  PHE A CG  1 
ATOM 409  C CD1 . PHE A 1 68  ? 141.803 127.898 90.634  1.00 70.66  ? 51  PHE A CD1 1 
ATOM 410  C CD2 . PHE A 1 68  ? 140.937 125.693 90.882  1.00 70.66  ? 51  PHE A CD2 1 
ATOM 411  C CE1 . PHE A 1 68  ? 143.011 127.486 91.163  1.00 70.66  ? 51  PHE A CE1 1 
ATOM 412  C CE2 . PHE A 1 68  ? 142.142 125.275 91.412  1.00 70.66  ? 51  PHE A CE2 1 
ATOM 413  C CZ  . PHE A 1 68  ? 143.180 126.172 91.553  1.00 70.66  ? 51  PHE A CZ  1 
ATOM 414  N N   . THR A 1 69  ? 136.582 128.403 90.441  1.00 72.32  ? 52  THR A N   1 
ATOM 415  C CA  . THR A 1 69  ? 135.207 128.572 89.981  1.00 72.32  ? 52  THR A CA  1 
ATOM 416  C C   . THR A 1 69  ? 134.687 129.972 90.283  1.00 72.32  ? 52  THR A C   1 
ATOM 417  O O   . THR A 1 69  ? 133.971 130.565 89.468  1.00 72.32  ? 52  THR A O   1 
ATOM 418  C CB  . THR A 1 69  ? 134.301 127.520 90.621  1.00 72.32  ? 52  THR A CB  1 
ATOM 419  O OG1 . THR A 1 69  ? 134.250 127.728 92.038  1.00 72.32  ? 52  THR A OG1 1 
ATOM 420  C CG2 . THR A 1 69  ? 134.825 126.123 90.339  1.00 72.32  ? 52  THR A CG2 1 
ATOM 421  N N   . ASN A 1 70  ? 135.037 130.519 91.446  1.00 80.43  ? 53  ASN A N   1 
ATOM 422  C CA  . ASN A 1 70  ? 134.524 131.816 91.874  1.00 80.43  ? 53  ASN A CA  1 
ATOM 423  C C   . ASN A 1 70  ? 135.633 132.858 91.824  1.00 80.43  ? 53  ASN A C   1 
ATOM 424  O O   . ASN A 1 70  ? 136.480 132.907 92.730  1.00 80.43  ? 53  ASN A O   1 
ATOM 425  C CB  . ASN A 1 70  ? 133.944 131.718 93.288  1.00 80.43  ? 53  ASN A CB  1 
ATOM 426  C CG  . ASN A 1 70  ? 133.076 132.907 93.647  1.00 80.43  ? 53  ASN A CG  1 
ATOM 427  O OD1 . ASN A 1 70  ? 132.847 133.793 92.825  1.00 80.43  ? 53  ASN A OD1 1 
ATOM 428  N ND2 . ASN A 1 70  ? 132.586 132.931 94.881  1.00 80.43  ? 53  ASN A ND2 1 
ATOM 429  N N   . PRO A 1 71  ? 135.683 133.703 90.790  1.00 89.67  ? 54  PRO A N   1 
ATOM 430  C CA  . PRO A 1 71  ? 136.685 134.781 90.775  1.00 89.67  ? 54  PRO A CA  1 
ATOM 431  C C   . PRO A 1 71  ? 136.542 135.750 91.933  1.00 89.67  ? 54  PRO A C   1 
ATOM 432  O O   . PRO A 1 71  ? 137.551 136.285 92.411  1.00 89.67  ? 54  PRO A O   1 
ATOM 433  C CB  . PRO A 1 71  ? 136.435 135.472 89.427  1.00 89.67  ? 54  PRO A CB  1 
ATOM 434  C CG  . PRO A 1 71  ? 135.750 134.441 88.592  1.00 89.67  ? 54  PRO A CG  1 
ATOM 435  C CD  . PRO A 1 71  ? 134.905 133.651 89.542  1.00 89.67  ? 54  PRO A CD  1 
ATOM 436  N N   . GLU A 1 72  ? 135.314 135.999 92.395  1.00 92.17  ? 55  GLU A N   1 
ATOM 437  C CA  . GLU A 1 72  ? 135.118 136.877 93.544  1.00 92.17  ? 55  GLU A CA  1 
ATOM 438  C C   . GLU A 1 72  ? 135.753 136.300 94.801  1.00 92.17  ? 55  GLU A C   1 
ATOM 439  O O   . GLU A 1 72  ? 136.249 137.053 95.648  1.00 92.17  ? 55  GLU A O   1 
ATOM 440  C CB  . GLU A 1 72  ? 133.624 137.131 93.769  1.00 92.17  ? 55  GLU A CB  1 
ATOM 441  C CG  . GLU A 1 72  ? 132.910 137.908 92.656  1.00 92.17  ? 55  GLU A CG  1 
ATOM 442  C CD  . GLU A 1 72  ? 132.678 137.105 91.382  1.00 92.17  ? 55  GLU A CD  1 
ATOM 443  O OE1 . GLU A 1 72  ? 133.298 136.035 91.209  1.00 92.17  ? 55  GLU A OE1 1 
ATOM 444  O OE2 . GLU A 1 72  ? 131.865 137.551 90.546  1.00 92.17  ? 55  GLU A OE2 1 
ATOM 445  N N   . GLU A 1 73  ? 135.750 134.978 94.943  1.00 88.60  ? 56  GLU A N   1 
ATOM 446  C CA  . GLU A 1 73  ? 136.399 134.313 96.072  1.00 88.60  ? 56  GLU A CA  1 
ATOM 447  C C   . GLU A 1 73  ? 137.861 134.003 95.767  1.00 88.60  ? 56  GLU A C   1 
ATOM 448  O O   . GLU A 1 73  ? 138.322 132.870 95.897  1.00 88.60  ? 56  GLU A O   1 
ATOM 449  C CB  . GLU A 1 73  ? 135.635 133.047 96.438  1.00 88.60  ? 56  GLU A CB  1 
ATOM 450  C CG  . GLU A 1 73  ? 135.698 132.689 97.912  1.00 88.60  ? 56  GLU A CG  1 
ATOM 451  C CD  . GLU A 1 73  ? 134.778 133.544 98.759  1.00 88.60  ? 56  GLU A CD  1 
ATOM 452  O OE1 . GLU A 1 73  ? 133.834 134.139 98.199  1.00 88.60  ? 56  GLU A OE1 1 
ATOM 453  O OE2 . GLU A 1 73  ? 134.999 133.622 99.986  1.00 88.60  ? 56  GLU A OE2 1 
ATOM 454  N N   . GLY A 1 74  ? 138.605 135.026 95.356  1.00 92.82  ? 57  GLY A N   1 
ATOM 455  C CA  . GLY A 1 74  ? 140.007 134.881 95.030  1.00 92.82  ? 57  GLY A CA  1 
ATOM 456  C C   . GLY A 1 74  ? 140.955 134.916 96.204  1.00 92.82  ? 57  GLY A C   1 
ATOM 457  O O   . GLY A 1 74  ? 142.169 134.805 96.010  1.00 92.82  ? 57  GLY A O   1 
ATOM 458  N N   . ASP A 1 75  ? 140.440 135.068 97.421  1.00 89.32  ? 58  ASP A N   1 
ATOM 459  C CA  . ASP A 1 75  ? 141.263 135.118 98.618  1.00 89.32  ? 58  ASP A CA  1 
ATOM 460  C C   . ASP A 1 75  ? 140.711 134.153 99.657  1.00 89.32  ? 58  ASP A C   1 
ATOM 461  O O   . ASP A 1 75  ? 139.523 133.821 99.652  1.00 89.32  ? 58  ASP A O   1 
ATOM 462  C CB  . ASP A 1 75  ? 141.325 136.537 99.202  1.00 89.32  ? 58  ASP A CB  1 
ATOM 463  C CG  . ASP A 1 75  ? 140.089 136.893 100.002 1.00 89.32  ? 58  ASP A CG  1 
ATOM 464  O OD1 . ASP A 1 75  ? 138.988 136.929 99.414  1.00 89.32  ? 58  ASP A OD1 1 
ATOM 465  O OD2 . ASP A 1 75  ? 140.218 137.136 101.221 1.00 89.32  ? 58  ASP A OD2 1 
ATOM 466  N N   . LEU A 1 76  ? 141.592 133.706 100.546 1.00 76.30  ? 59  LEU A N   1 
ATOM 467  C CA  . LEU A 1 76  ? 141.263 132.745 101.591 1.00 76.30  ? 59  LEU A CA  1 
ATOM 468  C C   . LEU A 1 76  ? 141.421 133.372 102.970 1.00 76.30  ? 59  LEU A C   1 
ATOM 469  O O   . LEU A 1 76  ? 141.922 132.747 103.907 1.00 76.30  ? 59  LEU A O   1 
ATOM 470  C CB  . LEU A 1 76  ? 142.126 131.493 101.461 1.00 76.30  ? 59  LEU A CB  1 
ATOM 471  C CG  . LEU A 1 76  ? 142.299 130.972 100.033 1.00 76.30  ? 59  LEU A CG  1 
ATOM 472  C CD1 . LEU A 1 76  ? 143.174 129.733 100.008 1.00 76.30  ? 59  LEU A CD1 1 
ATOM 473  C CD2 . LEU A 1 76  ? 140.940 130.672 99.422  1.00 76.30  ? 59  LEU A CD2 1 
ATOM 474  N N   . ASN A 1 77  ? 140.987 134.623 103.107 1.00 86.73  ? 60  ASN A N   1 
ATOM 475  C CA  . ASN A 1 77  ? 141.102 135.367 104.348 1.00 86.73  ? 60  ASN A CA  1 
ATOM 476  C C   . ASN A 1 77  ? 139.722 135.767 104.854 1.00 86.73  ? 60  ASN A C   1 
ATOM 477  O O   . ASN A 1 77  ? 138.796 135.957 104.058 1.00 86.73  ? 60  ASN A O   1 
ATOM 478  C CB  . ASN A 1 77  ? 141.962 136.625 104.164 1.00 86.73  ? 60  ASN A CB  1 
ATOM 479  C CG  . ASN A 1 77  ? 143.245 136.353 103.401 1.00 86.73  ? 60  ASN A CG  1 
ATOM 480  O OD1 . ASN A 1 77  ? 143.733 135.224 103.364 1.00 86.73  ? 60  ASN A OD1 1 
ATOM 481  N ND2 . ASN A 1 77  ? 143.798 137.392 102.787 1.00 86.73  ? 60  ASN A ND2 1 
ATOM 482  N N   . PRO A 1 78  ? 139.550 135.888 106.167 1.00 78.54  ? 61  PRO A N   1 
ATOM 483  C CA  . PRO A 1 78  ? 138.242 136.255 106.719 1.00 78.54  ? 61  PRO A CA  1 
ATOM 484  C C   . PRO A 1 78  ? 137.827 137.646 106.275 1.00 78.54  ? 61  PRO A C   1 
ATOM 485  O O   . PRO A 1 78  ? 138.596 138.609 106.417 1.00 78.54  ? 61  PRO A O   1 
ATOM 486  C CB  . PRO A 1 78  ? 138.472 136.202 108.237 1.00 78.54  ? 61  PRO A CB  1 
ATOM 487  C CG  . PRO A 1 78  ? 139.641 135.295 108.411 1.00 78.54  ? 61  PRO A CG  1 
ATOM 488  C CD  . PRO A 1 78  ? 140.515 135.534 107.221 1.00 78.54  ? 61  PRO A CD  1 
ATOM 489  N N   . PRO A 1 79  ? 136.624 137.791 105.729 1.00 89.23  ? 62  PRO A N   1 
ATOM 490  C CA  . PRO A 1 79  ? 136.117 139.122 105.386 1.00 89.23  ? 62  PRO A CA  1 
ATOM 491  C C   . PRO A 1 79  ? 135.807 139.918 106.639 1.00 89.23  ? 62  PRO A C   1 
ATOM 492  O O   . PRO A 1 79  ? 135.574 139.337 107.710 1.00 89.23  ? 62  PRO A O   1 
ATOM 493  C CB  . PRO A 1 79  ? 134.842 138.820 104.584 1.00 89.23  ? 62  PRO A CB  1 
ATOM 494  C CG  . PRO A 1 79  ? 134.413 137.475 105.054 1.00 89.23  ? 62  PRO A CG  1 
ATOM 495  C CD  . PRO A 1 79  ? 135.668 136.722 105.393 1.00 89.23  ? 62  PRO A CD  1 
ATOM 496  N N   . PRO A 1 80  ? 135.812 141.252 106.553 1.00 98.29  ? 63  PRO A N   1 
ATOM 497  C CA  . PRO A 1 80  ? 135.479 142.058 107.742 1.00 98.29  ? 63  PRO A CA  1 
ATOM 498  C C   . PRO A 1 80  ? 134.098 141.765 108.302 1.00 98.29  ? 63  PRO A C   1 
ATOM 499  O O   . PRO A 1 80  ? 133.911 141.793 109.525 1.00 98.29  ? 63  PRO A O   1 
ATOM 500  C CB  . PRO A 1 80  ? 135.591 143.501 107.230 1.00 98.29  ? 63  PRO A CB  1 
ATOM 501  C CG  . PRO A 1 80  ? 136.482 143.422 106.037 1.00 98.29  ? 63  PRO A CG  1 
ATOM 502  C CD  . PRO A 1 80  ? 136.238 142.082 105.413 1.00 98.29  ? 63  PRO A CD  1 
ATOM 503  N N   . GLU A 1 81  ? 133.122 141.485 107.442 1.00 100.03 ? 64  GLU A N   1 
ATOM 504  C CA  . GLU A 1 81  ? 131.762 141.181 107.874 1.00 100.03 ? 64  GLU A CA  1 
ATOM 505  C C   . GLU A 1 81  ? 131.614 139.669 108.004 1.00 100.03 ? 64  GLU A C   1 
ATOM 506  O O   . GLU A 1 81  ? 131.688 138.942 107.008 1.00 100.03 ? 64  GLU A O   1 
ATOM 507  C CB  . GLU A 1 81  ? 130.744 141.752 106.891 1.00 100.03 ? 64  GLU A CB  1 
ATOM 508  C CG  . GLU A 1 81  ? 130.397 143.215 107.129 1.00 100.03 ? 64  GLU A CG  1 
ATOM 509  C CD  . GLU A 1 81  ? 131.428 144.168 106.554 1.00 100.03 ? 64  GLU A CD  1 
ATOM 510  O OE1 . GLU A 1 81  ? 132.443 143.694 106.002 1.00 100.03 ? 64  GLU A OE1 1 
ATOM 511  O OE2 . GLU A 1 81  ? 131.222 145.396 106.654 1.00 100.03 ? 64  GLU A OE2 1 
ATOM 512  N N   . ALA A 1 82  ? 131.408 139.197 109.231 1.00 90.61  ? 65  ALA A N   1 
ATOM 513  C CA  . ALA A 1 82  ? 131.230 137.772 109.466 1.00 90.61  ? 65  ALA A CA  1 
ATOM 514  C C   . ALA A 1 82  ? 129.918 137.289 108.860 1.00 90.61  ? 65  ALA A C   1 
ATOM 515  O O   . ALA A 1 82  ? 128.914 138.006 108.856 1.00 90.61  ? 65  ALA A O   1 
ATOM 516  C CB  . ALA A 1 82  ? 131.261 137.470 110.963 1.00 90.61  ? 65  ALA A CB  1 
ATOM 517  N N   . LYS A 1 83  ? 129.931 136.062 108.346 1.00 78.53  ? 66  LYS A N   1 
ATOM 518  C CA  . LYS A 1 83  ? 128.744 135.498 107.727 1.00 78.53  ? 66  LYS A CA  1 
ATOM 519  C C   . LYS A 1 83  ? 127.689 135.165 108.780 1.00 78.53  ? 66  LYS A C   1 
ATOM 520  O O   . LYS A 1 83  ? 127.991 134.938 109.955 1.00 78.53  ? 66  LYS A O   1 
ATOM 521  C CB  . LYS A 1 83  ? 129.099 134.245 106.928 1.00 78.53  ? 66  LYS A CB  1 
ATOM 522  C CG  . LYS A 1 83  ? 128.325 134.103 105.629 1.00 78.53  ? 66  LYS A CG  1 
ATOM 523  C CD  . LYS A 1 83  ? 128.572 132.751 104.985 1.00 78.53  ? 66  LYS A CD  1 
ATOM 524  C CE  . LYS A 1 83  ? 127.283 132.168 104.432 1.00 78.53  ? 66  LYS A CE  1 
ATOM 525  N NZ  . LYS A 1 83  ? 127.467 130.774 103.948 1.00 78.53  ? 66  LYS A NZ  1 
ATOM 526  N N   . GLN A 1 84  ? 126.432 135.129 108.337 1.00 75.37  ? 67  GLN A N   1 
ATOM 527  C CA  . GLN A 1 84  ? 125.299 134.833 109.214 1.00 75.37  ? 67  GLN A CA  1 
ATOM 528  C C   . GLN A 1 84  ? 125.121 133.321 109.371 1.00 75.37  ? 67  GLN A C   1 
ATOM 529  O O   . GLN A 1 84  ? 124.090 132.738 109.036 1.00 75.37  ? 67  GLN A O   1 
ATOM 530  C CB  . GLN A 1 84  ? 124.034 135.491 108.677 1.00 75.37  ? 67  GLN A CB  1 
ATOM 531  C CG  . GLN A 1 84  ? 124.202 136.955 108.299 1.00 75.37  ? 67  GLN A CG  1 
ATOM 532  C CD  . GLN A 1 84  ? 124.720 137.803 109.446 1.00 75.37  ? 67  GLN A CD  1 
ATOM 533  O OE1 . GLN A 1 84  ? 124.432 137.536 110.613 1.00 75.37  ? 67  GLN A OE1 1 
ATOM 534  N NE2 . GLN A 1 84  ? 125.491 138.833 109.118 1.00 75.37  ? 67  GLN A NE2 1 
ATOM 535  N N   . VAL A 1 85  ? 126.165 132.689 109.894 1.00 69.61  ? 68  VAL A N   1 
ATOM 536  C CA  . VAL A 1 85  ? 126.190 131.247 110.125 1.00 69.61  ? 68  VAL A CA  1 
ATOM 537  C C   . VAL A 1 85  ? 126.657 131.035 111.561 1.00 69.61  ? 68  VAL A C   1 
ATOM 538  O O   . VAL A 1 85  ? 127.642 131.660 111.979 1.00 69.61  ? 68  VAL A O   1 
ATOM 539  C CB  . VAL A 1 85  ? 127.099 130.542 109.102 1.00 69.61  ? 68  VAL A CB  1 
ATOM 540  C CG1 . VAL A 1 85  ? 127.344 129.095 109.482 1.00 69.61  ? 68  VAL A CG1 1 
ATOM 541  C CG2 . VAL A 1 85  ? 126.492 130.628 107.709 1.00 69.61  ? 68  VAL A CG2 1 
ATOM 542  N N   . PRO A 1 86  ? 125.987 130.192 112.354 1.00 59.63  ? 69  PRO A N   1 
ATOM 543  C CA  . PRO A 1 86  ? 126.341 130.105 113.784 1.00 59.63  ? 69  PRO A CA  1 
ATOM 544  C C   . PRO A 1 86  ? 127.773 129.671 114.047 1.00 59.63  ? 69  PRO A C   1 
ATOM 545  O O   . PRO A 1 86  ? 128.362 130.104 115.046 1.00 59.63  ? 69  PRO A O   1 
ATOM 546  C CB  . PRO A 1 86  ? 125.332 129.096 114.355 1.00 59.63  ? 69  PRO A CB  1 
ATOM 547  C CG  . PRO A 1 86  ? 124.478 128.647 113.232 1.00 59.63  ? 69  PRO A CG  1 
ATOM 548  C CD  . PRO A 1 86  ? 124.973 129.204 111.949 1.00 59.63  ? 69  PRO A CD  1 
ATOM 549  N N   . VAL A 1 87  ? 128.357 128.834 113.194 1.00 63.01  ? 70  VAL A N   1 
ATOM 550  C CA  . VAL A 1 87  ? 129.730 128.376 113.366 1.00 63.01  ? 70  VAL A CA  1 
ATOM 551  C C   . VAL A 1 87  ? 130.487 128.561 112.056 1.00 63.01  ? 70  VAL A C   1 
ATOM 552  O O   . VAL A 1 87  ? 129.965 128.266 110.975 1.00 63.01  ? 70  VAL A O   1 
ATOM 553  C CB  . VAL A 1 87  ? 129.786 126.909 113.852 1.00 63.01  ? 70  VAL A CB  1 
ATOM 554  C CG1 . VAL A 1 87  ? 129.280 125.949 112.785 1.00 63.01  ? 70  VAL A CG1 1 
ATOM 555  C CG2 . VAL A 1 87  ? 131.201 126.546 114.278 1.00 63.01  ? 70  VAL A CG2 1 
ATOM 556  N N   . SER A 1 88  ? 131.709 129.080 112.154 1.00 66.81  ? 71  SER A N   1 
ATOM 557  C CA  . SER A 1 88  ? 132.533 129.324 110.971 1.00 66.81  ? 71  SER A CA  1 
ATOM 558  C C   . SER A 1 88  ? 133.992 129.327 111.393 1.00 66.81  ? 71  SER A C   1 
ATOM 559  O O   . SER A 1 88  ? 134.378 130.101 112.274 1.00 66.81  ? 71  SER A O   1 
ATOM 560  C CB  . SER A 1 88  ? 132.162 130.649 110.308 1.00 66.81  ? 71  SER A CB  1 
ATOM 561  O OG  . SER A 1 88  ? 132.536 131.745 111.122 1.00 66.81  ? 71  SER A OG  1 
ATOM 562  N N   . TYR A 1 89  ? 134.796 128.473 110.768 1.00 63.79  ? 72  TYR A N   1 
ATOM 563  C CA  . TYR A 1 89  ? 136.222 128.374 111.046 1.00 63.79  ? 72  TYR A CA  1 
ATOM 564  C C   . TYR A 1 89  ? 137.000 128.861 109.833 1.00 63.79  ? 72  TYR A C   1 
ATOM 565  O O   . TYR A 1 89  ? 136.759 128.402 108.712 1.00 63.79  ? 72  TYR A O   1 
ATOM 566  C CB  . TYR A 1 89  ? 136.614 126.936 111.392 1.00 63.79  ? 72  TYR A CB  1 
ATOM 567  C CG  . TYR A 1 89  ? 138.105 126.714 111.516 1.00 63.79  ? 72  TYR A CG  1 
ATOM 568  C CD1 . TYR A 1 89  ? 138.871 127.478 112.387 1.00 63.79  ? 72  TYR A CD1 1 
ATOM 569  C CD2 . TYR A 1 89  ? 138.745 125.735 110.769 1.00 63.79  ? 72  TYR A CD2 1 
ATOM 570  C CE1 . TYR A 1 89  ? 140.233 127.276 112.505 1.00 63.79  ? 72  TYR A CE1 1 
ATOM 571  C CE2 . TYR A 1 89  ? 140.106 125.526 110.880 1.00 63.79  ? 72  TYR A CE2 1 
ATOM 572  C CZ  . TYR A 1 89  ? 140.844 126.299 111.750 1.00 63.79  ? 72  TYR A CZ  1 
ATOM 573  O OH  . TYR A 1 89  ? 142.200 126.093 111.863 1.00 63.79  ? 72  TYR A OH  1 
ATOM 574  N N   . TYR A 1 90  ? 137.924 129.792 110.056 1.00 65.30  ? 73  TYR A N   1 
ATOM 575  C CA  . TYR A 1 90  ? 138.709 130.390 108.985 1.00 65.30  ? 73  TYR A CA  1 
ATOM 576  C C   . TYR A 1 90  ? 140.189 130.144 109.240 1.00 65.30  ? 73  TYR A C   1 
ATOM 577  O O   . TYR A 1 90  ? 140.699 130.465 110.319 1.00 65.30  ? 73  TYR A O   1 
ATOM 578  C CB  . TYR A 1 90  ? 138.431 131.891 108.875 1.00 65.30  ? 73  TYR A CB  1 
ATOM 579  C CG  . TYR A 1 90  ? 137.181 132.225 108.093 1.00 65.30  ? 73  TYR A CG  1 
ATOM 580  C CD1 . TYR A 1 90  ? 135.929 131.844 108.554 1.00 65.30  ? 73  TYR A CD1 1 
ATOM 581  C CD2 . TYR A 1 90  ? 137.254 132.914 106.892 1.00 65.30  ? 73  TYR A CD2 1 
ATOM 582  C CE1 . TYR A 1 90  ? 134.783 132.145 107.843 1.00 65.30  ? 73  TYR A CE1 1 
ATOM 583  C CE2 . TYR A 1 90  ? 136.114 133.219 106.173 1.00 65.30  ? 73  TYR A CE2 1 
ATOM 584  C CZ  . TYR A 1 90  ? 134.882 132.832 106.653 1.00 65.30  ? 73  TYR A CZ  1 
ATOM 585  O OH  . TYR A 1 90  ? 133.745 133.133 105.941 1.00 65.30  ? 73  TYR A OH  1 
ATOM 586  N N   . ASP A 1 91  ? 140.871 129.581 108.246 1.00 62.75  ? 74  ASP A N   1 
ATOM 587  C CA  . ASP A 1 91  ? 142.304 129.314 108.348 1.00 62.75  ? 74  ASP A CA  1 
ATOM 588  C C   . ASP A 1 91  ? 142.854 129.136 106.943 1.00 62.75  ? 74  ASP A C   1 
ATOM 589  O O   . ASP A 1 91  ? 142.461 128.198 106.242 1.00 62.75  ? 74  ASP A O   1 
ATOM 590  C CB  . ASP A 1 91  ? 142.573 128.073 109.199 1.00 62.75  ? 74  ASP A CB  1 
ATOM 591  C CG  . ASP A 1 91  ? 144.025 127.957 109.621 1.00 62.75  ? 74  ASP A CG  1 
ATOM 592  O OD1 . ASP A 1 91  ? 144.824 128.847 109.263 1.00 62.75  ? 74  ASP A OD1 1 
ATOM 593  O OD2 . ASP A 1 91  ? 144.366 126.974 110.313 1.00 62.75  ? 74  ASP A OD2 1 
ATOM 594  N N   . SER A 1 92  ? 143.758 130.027 106.534 1.00 63.06  ? 75  SER A N   1 
ATOM 595  C CA  . SER A 1 92  ? 144.311 129.980 105.186 1.00 63.06  ? 75  SER A CA  1 
ATOM 596  C C   . SER A 1 92  ? 145.379 128.907 105.015 1.00 63.06  ? 75  SER A C   1 
ATOM 597  O O   . SER A 1 92  ? 145.715 128.563 103.876 1.00 63.06  ? 75  SER A O   1 
ATOM 598  C CB  . SER A 1 92  ? 144.892 131.345 104.812 1.00 63.06  ? 75  SER A CB  1 
ATOM 599  O OG  . SER A 1 92  ? 145.846 131.772 105.769 1.00 63.06  ? 75  SER A OG  1 
ATOM 600  N N   . THR A 1 93  ? 145.917 128.373 106.113 1.00 60.83  ? 76  THR A N   1 
ATOM 601  C CA  . THR A 1 93  ? 147.001 127.400 106.014 1.00 60.83  ? 76  THR A CA  1 
ATOM 602  C C   . THR A 1 93  ? 146.506 126.045 105.517 1.00 60.83  ? 76  THR A C   1 
ATOM 603  O O   . THR A 1 93  ? 147.228 125.352 104.791 1.00 60.83  ? 76  THR A O   1 
ATOM 604  C CB  . THR A 1 93  ? 147.693 127.261 107.373 1.00 60.83  ? 76  THR A CB  1 
ATOM 605  O OG1 . THR A 1 93  ? 148.438 128.453 107.652 1.00 60.83  ? 76  THR A OG1 1 
ATOM 606  C CG2 . THR A 1 93  ? 148.644 126.071 107.392 1.00 60.83  ? 76  THR A CG2 1 
ATOM 607  N N   . TYR A 1 94  ? 145.279 125.666 105.872 1.00 49.85  ? 77  TYR A N   1 
ATOM 608  C CA  . TYR A 1 94  ? 144.776 124.334 105.561 1.00 49.85  ? 77  TYR A CA  1 
ATOM 609  C C   . TYR A 1 94  ? 144.754 124.090 104.055 1.00 49.85  ? 77  TYR A C   1 
ATOM 610  O O   . TYR A 1 94  ? 144.474 124.996 103.265 1.00 49.85  ? 77  TYR A O   1 
ATOM 611  C CB  . TYR A 1 94  ? 143.372 124.156 106.145 1.00 49.85  ? 77  TYR A CB  1 
ATOM 612  C CG  . TYR A 1 94  ? 142.609 122.965 105.604 1.00 49.85  ? 77  TYR A CG  1 
ATOM 613  C CD1 . TYR A 1 94  ? 143.089 121.673 105.768 1.00 49.85  ? 77  TYR A CD1 1 
ATOM 614  C CD2 . TYR A 1 94  ? 141.413 123.136 104.924 1.00 49.85  ? 77  TYR A CD2 1 
ATOM 615  C CE1 . TYR A 1 94  ? 142.394 120.585 105.272 1.00 49.85  ? 77  TYR A CE1 1 
ATOM 616  C CE2 . TYR A 1 94  ? 140.712 122.055 104.425 1.00 49.85  ? 77  TYR A CE2 1 
ATOM 617  C CZ  . TYR A 1 94  ? 141.207 120.783 104.601 1.00 49.85  ? 77  TYR A CZ  1 
ATOM 618  O OH  . TYR A 1 94  ? 140.512 119.704 104.106 1.00 49.85  ? 77  TYR A OH  1 
ATOM 619  N N   . LEU A 1 95  ? 145.069 122.851 103.667 1.00 49.85  ? 78  LEU A N   1 
ATOM 620  C CA  . LEU A 1 95  ? 145.062 122.417 102.268 1.00 49.85  ? 78  LEU A CA  1 
ATOM 621  C C   . LEU A 1 95  ? 146.038 123.229 101.420 1.00 49.85  ? 78  LEU A C   1 
ATOM 622  O O   . LEU A 1 95  ? 145.743 123.598 100.282 1.00 49.85  ? 78  LEU A O   1 
ATOM 623  C CB  . LEU A 1 95  ? 143.651 122.468 101.676 1.00 49.85  ? 78  LEU A CB  1 
ATOM 624  C CG  . LEU A 1 95  ? 143.000 121.105 101.437 1.00 49.85  ? 78  LEU A CG  1 
ATOM 625  C CD1 . LEU A 1 95  ? 141.548 121.263 101.020 1.00 49.85  ? 78  LEU A CD1 1 
ATOM 626  C CD2 . LEU A 1 95  ? 143.778 120.321 100.393 1.00 49.85  ? 78  LEU A CD2 1 
ATOM 627  N N   . SER A 1 96  ? 147.216 123.507 101.981 1.00 62.40  ? 79  SER A N   1 
ATOM 628  C CA  . SER A 1 96  ? 148.294 124.150 101.245 1.00 62.40  ? 79  SER A CA  1 
ATOM 629  C C   . SER A 1 96  ? 149.526 123.272 101.088 1.00 62.40  ? 79  SER A C   1 
ATOM 630  O O   . SER A 1 96  ? 150.387 123.590 100.262 1.00 62.40  ? 79  SER A O   1 
ATOM 631  C CB  . SER A 1 96  ? 148.703 125.463 101.928 1.00 62.40  ? 79  SER A CB  1 
ATOM 632  O OG  . SER A 1 96  ? 149.131 125.234 103.259 1.00 62.40  ? 79  SER A OG  1 
ATOM 633  N N   . THR A 1 97  ? 149.630 122.190 101.850 1.00 64.88  ? 80  THR A N   1 
ATOM 634  C CA  . THR A 1 97  ? 150.767 121.284 101.802 1.00 64.88  ? 80  THR A CA  1 
ATOM 635  C C   . THR A 1 97  ? 150.376 119.985 101.102 1.00 64.88  ? 80  THR A C   1 
ATOM 636  O O   . THR A 1 97  ? 149.200 119.622 101.025 1.00 64.88  ? 80  THR A O   1 
ATOM 637  C CB  . THR A 1 97  ? 151.279 120.993 103.218 1.00 64.88  ? 80  THR A CB  1 
ATOM 638  O OG1 . THR A 1 97  ? 151.230 122.195 103.997 1.00 64.88  ? 80  THR A OG1 1 
ATOM 639  C CG2 . THR A 1 97  ? 152.718 120.496 103.184 1.00 64.88  ? 80  THR A CG2 1 
ATOM 640  N N   . ASP A 1 98  ? 151.390 119.288 100.581 1.00 70.15  ? 81  ASP A N   1 
ATOM 641  C CA  . ASP A 1 98  ? 151.151 118.026 99.886  1.00 70.15  ? 81  ASP A CA  1 
ATOM 642  C C   . ASP A 1 98  ? 150.535 116.992 100.822 1.00 70.15  ? 81  ASP A C   1 
ATOM 643  O O   . ASP A 1 98  ? 149.643 116.233 100.421 1.00 70.15  ? 81  ASP A O   1 
ATOM 644  C CB  . ASP A 1 98  ? 152.463 117.514 99.286  1.00 70.15  ? 81  ASP A CB  1 
ATOM 645  C CG  . ASP A 1 98  ? 152.280 116.279 98.413  1.00 70.15  ? 81  ASP A CG  1 
ATOM 646  O OD1 . ASP A 1 98  ? 151.759 115.252 98.899  1.00 70.15  ? 81  ASP A OD1 1 
ATOM 647  O OD2 . ASP A 1 98  ? 152.667 116.337 97.228  1.00 70.15  ? 81  ASP A OD2 1 
ATOM 648  N N   . ASN A 1 99  ? 151.001 116.945 102.073 1.00 66.59  ? 82  ASN A N   1 
ATOM 649  C CA  . ASN A 1 99  ? 150.444 116.003 103.038 1.00 66.59  ? 82  ASN A CA  1 
ATOM 650  C C   . ASN A 1 99  ? 148.963 116.269 103.274 1.00 66.59  ? 82  ASN A C   1 
ATOM 651  O O   . ASN A 1 99  ? 148.161 115.331 103.357 1.00 66.59  ? 82  ASN A O   1 
ATOM 652  C CB  . ASN A 1 99  ? 151.216 116.082 104.355 1.00 66.59  ? 82  ASN A CB  1 
ATOM 653  C CG  . ASN A 1 99  ? 152.613 115.507 104.247 1.00 66.59  ? 82  ASN A CG  1 
ATOM 654  O OD1 . ASN A 1 99  ? 152.901 114.709 103.356 1.00 66.59  ? 82  ASN A OD1 1 
ATOM 655  N ND2 . ASN A 1 99  ? 153.490 115.911 105.158 1.00 66.59  ? 82  ASN A ND2 1 
ATOM 656  N N   . GLU A 1 100 ? 148.584 117.543 103.386 1.00 56.77  ? 83  GLU A N   1 
ATOM 657  C CA  . GLU A 1 100 ? 147.177 117.884 103.565 1.00 56.77  ? 83  GLU A CA  1 
ATOM 658  C C   . GLU A 1 100 ? 146.352 117.455 102.359 1.00 56.77  ? 83  GLU A C   1 
ATOM 659  O O   . GLU A 1 100 ? 145.224 116.973 102.510 1.00 56.77  ? 83  GLU A O   1 
ATOM 660  C CB  . GLU A 1 100 ? 147.028 119.385 103.812 1.00 56.77  ? 83  GLU A CB  1 
ATOM 661  C CG  . GLU A 1 100 ? 147.242 119.809 105.257 1.00 56.77  ? 83  GLU A CG  1 
ATOM 662  C CD  . GLU A 1 100 ? 146.089 119.426 106.166 1.00 56.77  ? 83  GLU A CD  1 
ATOM 663  O OE1 . GLU A 1 100 ? 145.051 118.956 105.655 1.00 56.77  ? 83  GLU A OE1 1 
ATOM 664  O OE2 . GLU A 1 100 ? 146.220 119.597 107.396 1.00 56.77  ? 83  GLU A OE2 1 
ATOM 665  N N   . LYS A 1 101 ? 146.896 117.627 101.152 1.00 55.09  ? 84  LYS A N   1 
ATOM 666  C CA  . LYS A 1 101 ? 146.178 117.217 99.949  1.00 55.09  ? 84  LYS A CA  1 
ATOM 667  C C   . LYS A 1 101 ? 145.985 115.706 99.909  1.00 55.09  ? 84  LYS A C   1 
ATOM 668  O O   . LYS A 1 101 ? 144.906 115.218 99.548  1.00 55.09  ? 84  LYS A O   1 
ATOM 669  C CB  . LYS A 1 101 ? 146.929 117.699 98.710  1.00 55.09  ? 84  LYS A CB  1 
ATOM 670  C CG  . LYS A 1 101 ? 146.667 119.153 98.364  1.00 55.09  ? 84  LYS A CG  1 
ATOM 671  C CD  . LYS A 1 101 ? 147.597 119.638 97.267  1.00 55.09  ? 84  LYS A CD  1 
ATOM 672  C CE  . LYS A 1 101 ? 147.913 121.113 97.434  1.00 55.09  ? 84  LYS A CE  1 
ATOM 673  N NZ  . LYS A 1 101 ? 148.636 121.380 98.706  1.00 55.09  ? 84  LYS A NZ  1 
ATOM 674  N N   . ASP A 1 102 ? 147.023 114.948 100.270 1.00 59.45  ? 85  ASP A N   1 
ATOM 675  C CA  . ASP A 1 102 ? 146.893 113.494 100.318 1.00 59.45  ? 85  ASP A CA  1 
ATOM 676  C C   . ASP A 1 102 ? 145.868 113.068 101.361 1.00 59.45  ? 85  ASP A C   1 
ATOM 677  O O   . ASP A 1 102 ? 145.063 112.157 101.121 1.00 59.45  ? 85  ASP A O   1 
ATOM 678  C CB  . ASP A 1 102 ? 148.251 112.856 100.607 1.00 59.45  ? 85  ASP A CB  1 
ATOM 679  C CG  . ASP A 1 102 ? 148.384 111.476 100.000 1.00 59.45  ? 85  ASP A CG  1 
ATOM 680  O OD1 . ASP A 1 102 ? 147.549 111.124 99.142  1.00 59.45  ? 85  ASP A OD1 1 
ATOM 681  O OD2 . ASP A 1 102 ? 149.322 110.745 100.379 1.00 59.45  ? 85  ASP A OD2 1 
ATOM 682  N N   . ASN A 1 103 ? 145.883 113.717 102.528 1.00 53.87  ? 86  ASN A N   1 
ATOM 683  C CA  . ASN A 1 103 ? 144.895 113.419 103.559 1.00 53.87  ? 86  ASN A CA  1 
ATOM 684  C C   . ASN A 1 103 ? 143.485 113.713 103.065 1.00 53.87  ? 86  ASN A C   1 
ATOM 685  O O   . ASN A 1 103 ? 142.557 112.934 103.309 1.00 53.87  ? 86  ASN A O   1 
ATOM 686  C CB  . ASN A 1 103 ? 145.199 114.225 104.821 1.00 53.87  ? 86  ASN A CB  1 
ATOM 687  C CG  . ASN A 1 103 ? 144.572 113.624 106.062 1.00 53.87  ? 86  ASN A CG  1 
ATOM 688  O OD1 . ASN A 1 103 ? 144.995 112.570 106.536 1.00 53.87  ? 86  ASN A OD1 1 
ATOM 689  N ND2 . ASN A 1 103 ? 143.555 114.291 106.593 1.00 53.87  ? 86  ASN A ND2 1 
ATOM 690  N N   . TYR A 1 104 ? 143.309 114.837 102.365 1.00 49.85  ? 87  TYR A N   1 
ATOM 691  C CA  . TYR A 1 104 ? 142.003 115.188 101.819 1.00 49.85  ? 87  TYR A CA  1 
ATOM 692  C C   . TYR A 1 104 ? 141.531 114.151 100.809 1.00 49.85  ? 87  TYR A C   1 
ATOM 693  O O   . TYR A 1 104 ? 140.363 113.746 100.823 1.00 49.85  ? 87  TYR A O   1 
ATOM 694  C CB  . TYR A 1 104 ? 142.074 116.577 101.180 1.00 49.85  ? 87  TYR A CB  1 
ATOM 695  C CG  . TYR A 1 104 ? 140.788 117.067 100.548 1.00 49.85  ? 87  TYR A CG  1 
ATOM 696  C CD1 . TYR A 1 104 ? 140.449 116.720 99.246  1.00 49.85  ? 87  TYR A CD1 1 
ATOM 697  C CD2 . TYR A 1 104 ? 139.923 117.895 101.249 1.00 49.85  ? 87  TYR A CD2 1 
ATOM 698  C CE1 . TYR A 1 104 ? 139.281 117.172 98.668  1.00 49.85  ? 87  TYR A CE1 1 
ATOM 699  C CE2 . TYR A 1 104 ? 138.754 118.352 100.678 1.00 49.85  ? 87  TYR A CE2 1 
ATOM 700  C CZ  . TYR A 1 104 ? 138.438 117.987 99.389  1.00 49.85  ? 87  TYR A CZ  1 
ATOM 701  O OH  . TYR A 1 104 ? 137.272 118.445 98.822  1.00 49.85  ? 87  TYR A OH  1 
ATOM 702  N N   . LEU A 1 105 ? 142.425 113.717 99.918  1.00 49.85  ? 88  LEU A N   1 
ATOM 703  C CA  . LEU A 1 105 ? 142.049 112.728 98.912  1.00 49.85  ? 88  LEU A CA  1 
ATOM 704  C C   . LEU A 1 105 ? 141.649 111.412 99.571  1.00 49.85  ? 88  LEU A C   1 
ATOM 705  O O   . LEU A 1 105 ? 140.629 110.806 99.213  1.00 49.85  ? 88  LEU A O   1 
ATOM 706  C CB  . LEU A 1 105 ? 143.206 112.522 97.932  1.00 49.85  ? 88  LEU A CB  1 
ATOM 707  C CG  . LEU A 1 105 ? 143.111 111.491 96.801  1.00 49.85  ? 88  LEU A CG  1 
ATOM 708  C CD1 . LEU A 1 105 ? 141.692 111.342 96.264  1.00 49.85  ? 88  LEU A CD1 1 
ATOM 709  C CD2 . LEU A 1 105 ? 144.073 111.848 95.680  1.00 49.85  ? 88  LEU A CD2 1 
ATOM 710  N N   . LYS A 1 106 ? 142.437 110.962 100.553 1.00 49.85  ? 89  LYS A N   1 
ATOM 711  C CA  . LYS A 1 106 ? 142.107 109.725 101.257 1.00 49.85  ? 89  LYS A CA  1 
ATOM 712  C C   . LYS A 1 106 ? 140.777 109.840 101.992 1.00 49.85  ? 89  LYS A C   1 
ATOM 713  O O   . LYS A 1 106 ? 139.961 108.910 101.962 1.00 49.85  ? 89  LYS A O   1 
ATOM 714  C CB  . LYS A 1 106 ? 143.227 109.358 102.230 1.00 49.85  ? 89  LYS A CB  1 
ATOM 715  C CG  . LYS A 1 106 ? 144.471 108.773 101.578 1.00 49.85  ? 89  LYS A CG  1 
ATOM 716  C CD  . LYS A 1 106 ? 144.113 107.861 100.415 1.00 49.85  ? 89  LYS A CD  1 
ATOM 717  C CE  . LYS A 1 106 ? 145.357 107.258 99.787  1.00 49.85  ? 89  LYS A CE  1 
ATOM 718  N NZ  . LYS A 1 106 ? 145.687 105.932 100.379 1.00 49.85  ? 89  LYS A NZ  1 
ATOM 719  N N   . GLY A 1 107 ? 140.542 110.972 102.657 1.00 49.85  ? 90  GLY A N   1 
ATOM 720  C CA  . GLY A 1 107 ? 139.284 111.157 103.360 1.00 49.85  ? 90  GLY A CA  1 
ATOM 721  C C   . GLY A 1 107 ? 138.090 111.164 102.427 1.00 49.85  ? 90  GLY A C   1 
ATOM 722  O O   . GLY A 1 107 ? 137.054 110.566 102.726 1.00 49.85  ? 90  GLY A O   1 
ATOM 723  N N   . VAL A 1 108 ? 138.218 111.836 101.280 1.00 49.85  ? 91  VAL A N   1 
ATOM 724  C CA  . VAL A 1 108 ? 137.121 111.871 100.317 1.00 49.85  ? 91  VAL A CA  1 
ATOM 725  C C   . VAL A 1 108 ? 136.842 110.475 99.776  1.00 49.85  ? 91  VAL A C   1 
ATOM 726  O O   . VAL A 1 108 ? 135.681 110.065 99.643  1.00 49.85  ? 91  VAL A O   1 
ATOM 727  C CB  . VAL A 1 108 ? 137.433 112.869 99.186  1.00 49.85  ? 91  VAL A CB  1 
ATOM 728  C CG1 . VAL A 1 108 ? 136.501 112.649 98.007  1.00 49.85  ? 91  VAL A CG1 1 
ATOM 729  C CG2 . VAL A 1 108 ? 137.316 114.295 99.697  1.00 49.85  ? 91  VAL A CG2 1 
ATOM 730  N N   . THR A 1 109 ? 137.898 109.718 99.460  1.00 49.85  ? 92  THR A N   1 
ATOM 731  C CA  . THR A 1 109 ? 137.696 108.360 98.962  1.00 49.85  ? 92  THR A CA  1 
ATOM 732  C C   . THR A 1 109 ? 137.020 107.481 100.009 1.00 49.85  ? 92  THR A C   1 
ATOM 733  O O   . THR A 1 109 ? 136.108 106.709 99.686  1.00 49.85  ? 92  THR A O   1 
ATOM 734  C CB  . THR A 1 109 ? 139.027 107.747 98.530  1.00 49.85  ? 92  THR A CB  1 
ATOM 735  O OG1 . THR A 1 109 ? 139.999 107.927 99.567  1.00 49.85  ? 92  THR A OG1 1 
ATOM 736  C CG2 . THR A 1 109 ? 139.525 108.402 97.252  1.00 49.85  ? 92  THR A CG2 1 
ATOM 737  N N   . LYS A 1 110 ? 137.449 107.587 101.270 1.00 49.85  ? 93  LYS A N   1 
ATOM 738  C CA  . LYS A 1 110 ? 136.832 106.787 102.323 1.00 49.85  ? 93  LYS A CA  1 
ATOM 739  C C   . LYS A 1 110 ? 135.374 107.177 102.537 1.00 49.85  ? 93  LYS A C   1 
ATOM 740  O O   . LYS A 1 110 ? 134.522 106.310 102.763 1.00 49.85  ? 93  LYS A O   1 
ATOM 741  C CB  . LYS A 1 110 ? 137.622 106.923 103.624 1.00 49.85  ? 93  LYS A CB  1 
ATOM 742  C CG  . LYS A 1 110 ? 137.594 105.672 104.489 1.00 49.85  ? 93  LYS A CG  1 
ATOM 743  C CD  . LYS A 1 110 ? 138.883 105.507 105.273 1.00 49.85  ? 93  LYS A CD  1 
ATOM 744  C CE  . LYS A 1 110 ? 138.797 104.332 106.232 1.00 49.85  ? 93  LYS A CE  1 
ATOM 745  N NZ  . LYS A 1 110 ? 140.069 104.128 106.977 1.00 49.85  ? 93  LYS A NZ  1 
ATOM 746  N N   . LEU A 1 111 ? 135.068 108.475 102.476 1.00 49.85  ? 94  LEU A N   1 
ATOM 747  C CA  . LEU A 1 111 ? 133.684 108.919 102.619 1.00 49.85  ? 94  LEU A CA  1 
ATOM 748  C C   . LEU A 1 111 ? 132.815 108.391 101.486 1.00 49.85  ? 94  LEU A C   1 
ATOM 749  O O   . LEU A 1 111 ? 131.684 107.942 101.715 1.00 49.85  ? 94  LEU A O   1 
ATOM 750  C CB  . LEU A 1 111 ? 133.629 110.445 102.669 1.00 49.85  ? 94  LEU A CB  1 
ATOM 751  C CG  . LEU A 1 111 ? 133.693 111.115 104.041 1.00 49.85  ? 94  LEU A CG  1 
ATOM 752  C CD1 . LEU A 1 111 ? 132.342 111.038 104.703 1.00 49.85  ? 94  LEU A CD1 1 
ATOM 753  C CD2 . LEU A 1 111 ? 134.733 110.460 104.920 1.00 49.85  ? 94  LEU A CD2 1 
ATOM 754  N N   . PHE A 1 112 ? 133.326 108.443 100.254 1.00 49.85  ? 95  PHE A N   1 
ATOM 755  C CA  . PHE A 1 112 ? 132.572 107.916 99.123  1.00 49.85  ? 95  PHE A CA  1 
ATOM 756  C C   . PHE A 1 112 ? 132.349 106.416 99.266  1.00 49.85  ? 95  PHE A C   1 
ATOM 757  O O   . PHE A 1 112 ? 131.258 105.913 98.976  1.00 49.85  ? 95  PHE A O   1 
ATOM 758  C CB  . PHE A 1 112 ? 133.296 108.237 97.816  1.00 49.85  ? 95  PHE A CB  1 
ATOM 759  C CG  . PHE A 1 112 ? 132.885 109.545 97.203  1.00 49.85  ? 95  PHE A CG  1 
ATOM 760  C CD1 . PHE A 1 112 ? 133.176 110.742 97.834  1.00 49.85  ? 95  PHE A CD1 1 
ATOM 761  C CD2 . PHE A 1 112 ? 132.213 109.578 95.995  1.00 49.85  ? 95  PHE A CD2 1 
ATOM 762  C CE1 . PHE A 1 112 ? 132.801 111.946 97.273  1.00 49.85  ? 95  PHE A CE1 1 
ATOM 763  C CE2 . PHE A 1 112 ? 131.836 110.779 95.428  1.00 49.85  ? 95  PHE A CE2 1 
ATOM 764  C CZ  . PHE A 1 112 ? 132.130 111.965 96.068  1.00 49.85  ? 95  PHE A CZ  1 
ATOM 765  N N   . GLU A 1 113 ? 133.372 105.686 99.721  1.00 49.85  ? 96  GLU A N   1 
ATOM 766  C CA  . GLU A 1 113 ? 133.216 104.254 99.957  1.00 49.85  ? 96  GLU A CA  1 
ATOM 767  C C   . GLU A 1 113 ? 132.162 103.978 101.023 1.00 49.85  ? 96  GLU A C   1 
ATOM 768  O O   . GLU A 1 113 ? 131.330 103.076 100.867 1.00 49.85  ? 96  GLU A O   1 
ATOM 769  C CB  . GLU A 1 113 ? 134.557 103.644 100.361 1.00 49.85  ? 96  GLU A CB  1 
ATOM 770  C CG  . GLU A 1 113 ? 134.706 102.174 100.013 1.00 49.85  ? 96  GLU A CG  1 
ATOM 771  C CD  . GLU A 1 113 ? 134.435 101.891 98.552  1.00 49.85  ? 96  GLU A CD  1 
ATOM 772  O OE1 . GLU A 1 113 ? 135.218 102.359 97.700  1.00 49.85  ? 96  GLU A OE1 1 
ATOM 773  O OE2 . GLU A 1 113 ? 133.441 101.197 98.256  1.00 49.85  ? 96  GLU A OE2 1 
ATOM 774  N N   . ARG A 1 114 ? 132.184 104.744 102.117 1.00 49.85  ? 97  ARG A N   1 
ATOM 775  C CA  . ARG A 1 114 ? 131.211 104.543 103.185 1.00 49.85  ? 97  ARG A CA  1 
ATOM 776  C C   . ARG A 1 114 ? 129.793 104.812 102.701 1.00 49.85  ? 97  ARG A C   1 
ATOM 777  O O   . ARG A 1 114 ? 128.865 104.065 103.033 1.00 49.85  ? 97  ARG A O   1 
ATOM 778  C CB  . ARG A 1 114 ? 131.547 105.436 104.378 1.00 49.85  ? 97  ARG A CB  1 
ATOM 779  C CG  . ARG A 1 114 ? 130.506 105.410 105.482 1.00 49.85  ? 97  ARG A CG  1 
ATOM 780  C CD  . ARG A 1 114 ? 131.150 105.631 106.834 1.00 49.85  ? 97  ARG A CD  1 
ATOM 781  N NE  . ARG A 1 114 ? 130.191 106.086 107.833 1.00 49.85  ? 97  ARG A NE  1 
ATOM 782  C CZ  . ARG A 1 114 ? 129.454 105.282 108.586 1.00 49.85  ? 97  ARG A CZ  1 
ATOM 783  N NH1 . ARG A 1 114 ? 129.539 103.966 108.480 1.00 49.85  ? 97  ARG A NH1 1 
ATOM 784  N NH2 . ARG A 1 114 ? 128.614 105.811 109.470 1.00 49.85  ? 97  ARG A NH2 1 
ATOM 785  N N   . ILE A 1 115 ? 129.602 105.877 101.921 1.00 49.85  ? 98  ILE A N   1 
ATOM 786  C CA  . ILE A 1 115 ? 128.271 106.166 101.395 1.00 49.85  ? 98  ILE A CA  1 
ATOM 787  C C   . ILE A 1 115 ? 127.831 105.076 100.424 1.00 49.85  ? 98  ILE A C   1 
ATOM 788  O O   . ILE A 1 115 ? 126.676 104.633 100.449 1.00 49.85  ? 98  ILE A O   1 
ATOM 789  C CB  . ILE A 1 115 ? 128.238 107.563 100.750 1.00 49.85  ? 98  ILE A CB  1 
ATOM 790  C CG1 . ILE A 1 115 ? 127.917 108.618 101.809 1.00 49.85  ? 98  ILE A CG1 1 
ATOM 791  C CG2 . ILE A 1 115 ? 127.220 107.619 99.620  1.00 49.85  ? 98  ILE A CG2 1 
ATOM 792  C CD1 . ILE A 1 115 ? 128.117 110.032 101.339 1.00 49.85  ? 98  ILE A CD1 1 
ATOM 793  N N   . TYR A 1 116 ? 128.744 104.611 99.568  1.00 49.85  ? 99  TYR A N   1 
ATOM 794  C CA  . TYR A 1 116 ? 128.428 103.528 98.644  1.00 49.85  ? 99  TYR A CA  1 
ATOM 795  C C   . TYR A 1 116 ? 128.131 102.218 99.360  1.00 49.85  ? 99  TYR A C   1 
ATOM 796  O O   . TYR A 1 116 ? 127.468 101.349 98.783  1.00 49.85  ? 99  TYR A O   1 
ATOM 797  C CB  . TYR A 1 116 ? 129.586 103.331 97.665  1.00 49.85  ? 99  TYR A CB  1 
ATOM 798  C CG  . TYR A 1 116 ? 129.236 102.517 96.442  1.00 49.85  ? 99  TYR A CG  1 
ATOM 799  C CD1 . TYR A 1 116 ? 128.579 103.092 95.364  1.00 49.85  ? 99  TYR A CD1 1 
ATOM 800  C CD2 . TYR A 1 116 ? 129.569 101.172 96.364  1.00 49.85  ? 99  TYR A CD2 1 
ATOM 801  C CE1 . TYR A 1 116 ? 128.261 102.351 94.244  1.00 49.85  ? 99  TYR A CE1 1 
ATOM 802  C CE2 . TYR A 1 116 ? 129.255 100.422 95.248  1.00 49.85  ? 99  TYR A CE2 1 
ATOM 803  C CZ  . TYR A 1 116 ? 128.600 101.017 94.191  1.00 49.85  ? 99  TYR A CZ  1 
ATOM 804  O OH  . TYR A 1 116 ? 128.284 100.275 93.077  1.00 49.85  ? 99  TYR A OH  1 
ATOM 805  N N   . SER A 1 117 ? 128.614 102.052 100.593 1.00 49.85  ? 100 SER A N   1 
ATOM 806  C CA  . SER A 1 117 ? 128.372 100.812 101.323 1.00 49.85  ? 100 SER A CA  1 
ATOM 807  C C   . SER A 1 117 ? 126.886 100.616 101.602 1.00 49.85  ? 100 SER A C   1 
ATOM 808  O O   . SER A 1 117 ? 126.352 99.513  101.439 1.00 49.85  ? 100 SER A O   1 
ATOM 809  C CB  . SER A 1 117 ? 129.172 100.808 102.626 1.00 49.85  ? 100 SER A CB  1 
ATOM 810  O OG  . SER A 1 117 ? 128.539 101.602 103.614 1.00 49.85  ? 100 SER A OG  1 
ATOM 811  N N   . THR A 1 118 ? 126.203 101.677 102.022 1.00 49.85  ? 101 THR A N   1 
ATOM 812  C CA  . THR A 1 118 ? 124.791 101.574 102.360 1.00 49.85  ? 101 THR A CA  1 
ATOM 813  C C   . THR A 1 118 ? 123.932 101.466 101.102 1.00 49.85  ? 101 THR A C   1 
ATOM 814  O O   . THR A 1 118 ? 124.353 101.804 99.992  1.00 49.85  ? 101 THR A O   1 
ATOM 815  C CB  . THR A 1 118 ? 124.349 102.774 103.196 1.00 49.85  ? 101 THR A CB  1 
ATOM 816  O OG1 . THR A 1 118 ? 124.408 103.964 102.401 1.00 49.85  ? 101 THR A OG1 1 
ATOM 817  C CG2 . THR A 1 118 ? 125.253 102.932 104.406 1.00 49.85  ? 101 THR A CG2 1 
ATOM 818  N N   . ASP A 1 119 ? 122.705 100.978 101.294 1.00 56.15  ? 102 ASP A N   1 
ATOM 819  C CA  . ASP A 1 119 ? 121.790 100.785 100.173 1.00 56.15  ? 102 ASP A CA  1 
ATOM 820  C C   . ASP A 1 119 ? 121.334 102.117 99.588  1.00 56.15  ? 102 ASP A C   1 
ATOM 821  O O   . ASP A 1 119 ? 121.373 102.319 98.367  1.00 56.15  ? 102 ASP A O   1 
ATOM 822  C CB  . ASP A 1 119 ? 120.588 99.957  100.628 1.00 56.15  ? 102 ASP A CB  1 
ATOM 823  C CG  . ASP A 1 119 ? 119.888 99.270  99.480  1.00 56.15  ? 102 ASP A CG  1 
ATOM 824  O OD1 . ASP A 1 119 ? 119.191 99.964  98.712  1.00 56.15  ? 102 ASP A OD1 1 
ATOM 825  O OD2 . ASP A 1 119 ? 120.034 98.037  99.347  1.00 56.15  ? 102 ASP A OD2 1 
ATOM 826  N N   . LEU A 1 120 ? 120.893 103.039 100.447 1.00 49.85  ? 103 LEU A N   1 
ATOM 827  C CA  . LEU A 1 120 ? 120.427 104.336 99.968  1.00 49.85  ? 103 LEU A CA  1 
ATOM 828  C C   . LEU A 1 120 ? 121.561 105.125 99.327  1.00 49.85  ? 103 LEU A C   1 
ATOM 829  O O   . LEU A 1 120 ? 121.355 105.829 98.331  1.00 49.85  ? 103 LEU A O   1 
ATOM 830  C CB  . LEU A 1 120 ? 119.801 105.125 101.117 1.00 49.85  ? 103 LEU A CB  1 
ATOM 831  C CG  . LEU A 1 120 ? 119.254 106.510 100.774 1.00 49.85  ? 103 LEU A CG  1 
ATOM 832  C CD1 . LEU A 1 120 ? 118.005 106.392 99.918  1.00 49.85  ? 103 LEU A CD1 1 
ATOM 833  C CD2 . LEU A 1 120 ? 118.969 107.296 102.039 1.00 49.85  ? 103 LEU A CD2 1 
ATOM 834  N N   . GLY A 1 121 ? 122.765 105.031 99.894  1.00 49.85  ? 104 GLY A N   1 
ATOM 835  C CA  . GLY A 1 121 ? 123.911 105.677 99.277  1.00 49.85  ? 104 GLY A CA  1 
ATOM 836  C C   . GLY A 1 121 ? 124.211 105.132 97.895  1.00 49.85  ? 104 GLY A C   1 
ATOM 837  O O   . GLY A 1 121 ? 124.571 105.883 96.987  1.00 49.85  ? 104 GLY A O   1 
ATOM 838  N N   . ARG A 1 122 ? 124.073 103.816 97.719  1.00 53.28  ? 105 ARG A N   1 
ATOM 839  C CA  . ARG A 1 122 ? 124.261 103.221 96.400  1.00 53.28  ? 105 ARG A CA  1 
ATOM 840  C C   . ARG A 1 122 ? 123.193 103.705 95.426  1.00 53.28  ? 105 ARG A C   1 
ATOM 841  O O   . ARG A 1 122 ? 123.494 104.018 94.266  1.00 53.28  ? 105 ARG A O   1 
ATOM 842  C CB  . ARG A 1 122 ? 124.253 101.697 96.515  1.00 53.28  ? 105 ARG A CB  1 
ATOM 843  C CG  . ARG A 1 122 ? 124.642 100.961 95.247  1.00 53.28  ? 105 ARG A CG  1 
ATOM 844  C CD  . ARG A 1 122 ? 123.963 99.604  95.173  1.00 53.28  ? 105 ARG A CD  1 
ATOM 845  N NE  . ARG A 1 122 ? 124.495 98.787  94.090  1.00 53.28  ? 105 ARG A NE  1 
ATOM 846  C CZ  . ARG A 1 122 ? 125.194 97.674  94.265  1.00 53.28  ? 105 ARG A CZ  1 
ATOM 847  N NH1 . ARG A 1 122 ? 125.467 97.212  95.475  1.00 53.28  ? 105 ARG A NH1 1 
ATOM 848  N NH2 . ARG A 1 122 ? 125.631 97.007  93.200  1.00 53.28  ? 105 ARG A NH2 1 
ATOM 849  N N   . MET A 1 123 ? 121.940 103.782 95.888  1.00 56.23  ? 106 MET A N   1 
ATOM 850  C CA  . MET A 1 123 ? 120.874 104.374 95.085  1.00 56.23  ? 106 MET A CA  1 
ATOM 851  C C   . MET A 1 123 ? 121.264 105.765 94.608  1.00 56.23  ? 106 MET A C   1 
ATOM 852  O O   . MET A 1 123 ? 121.187 106.082 93.414  1.00 56.23  ? 106 MET A O   1 
ATOM 853  C CB  . MET A 1 123 ? 119.593 104.481 95.911  1.00 56.23  ? 106 MET A CB  1 
ATOM 854  C CG  . MET A 1 123 ? 118.495 103.500 95.600  1.00 56.23  ? 106 MET A CG  1 
ATOM 855  S SD  . MET A 1 123 ? 117.336 103.534 96.979  1.00 56.23  ? 106 MET A SD  1 
ATOM 856  C CE  . MET A 1 123 ? 116.979 101.801 97.174  1.00 56.23  ? 106 MET A CE  1 
ATOM 857  N N   . LEU A 1 124 ? 121.678 106.610 95.552  1.00 49.85  ? 107 LEU A N   1 
ATOM 858  C CA  . LEU A 1 124 ? 121.983 108.002 95.248  1.00 49.85  ? 107 LEU A CA  1 
ATOM 859  C C   . LEU A 1 124 ? 123.162 108.117 94.293  1.00 49.85  ? 107 LEU A C   1 
ATOM 860  O O   . LEU A 1 124 ? 123.136 108.929 93.361  1.00 49.85  ? 107 LEU A O   1 
ATOM 861  C CB  . LEU A 1 124 ? 122.251 108.753 96.552  1.00 49.85  ? 107 LEU A CB  1 
ATOM 862  C CG  . LEU A 1 124 ? 122.676 110.218 96.548  1.00 49.85  ? 107 LEU A CG  1 
ATOM 863  C CD1 . LEU A 1 124 ? 122.263 110.844 97.852  1.00 49.85  ? 107 LEU A CD1 1 
ATOM 864  C CD2 . LEU A 1 124 ? 124.175 110.323 96.401  1.00 49.85  ? 107 LEU A CD2 1 
ATOM 865  N N   . LEU A 1 125 ? 124.214 107.330 94.518  1.00 49.85  ? 108 LEU A N   1 
ATOM 866  C CA  . LEU A 1 125 ? 125.390 107.411 93.661  1.00 49.85  ? 108 LEU A CA  1 
ATOM 867  C C   . LEU A 1 125 ? 125.074 106.942 92.247  1.00 49.85  ? 108 LEU A C   1 
ATOM 868  O O   . LEU A 1 125 ? 125.515 107.561 91.270  1.00 49.85  ? 108 LEU A O   1 
ATOM 869  C CB  . LEU A 1 125 ? 126.533 106.601 94.269  1.00 49.85  ? 108 LEU A CB  1 
ATOM 870  C CG  . LEU A 1 125 ? 127.345 107.354 95.325  1.00 49.85  ? 108 LEU A CG  1 
ATOM 871  C CD1 . LEU A 1 125 ? 128.603 106.591 95.691  1.00 49.85  ? 108 LEU A CD1 1 
ATOM 872  C CD2 . LEU A 1 125 ? 127.692 108.752 94.839  1.00 49.85  ? 108 LEU A CD2 1 
ATOM 873  N N   . THR A 1 126 ? 124.298 105.861 92.114  1.00 49.85  ? 109 THR A N   1 
ATOM 874  C CA  . THR A 1 126 ? 123.891 105.416 90.786  1.00 49.85  ? 109 THR A CA  1 
ATOM 875  C C   . THR A 1 126 ? 123.043 106.473 90.089  1.00 49.85  ? 109 THR A C   1 
ATOM 876  O O   . THR A 1 126 ? 123.237 106.751 88.899  1.00 49.85  ? 109 THR A O   1 
ATOM 877  C CB  . THR A 1 126 ? 123.133 104.091 90.887  1.00 49.85  ? 109 THR A CB  1 
ATOM 878  O OG1 . THR A 1 126 ? 124.070 103.013 91.000  1.00 49.85  ? 109 THR A OG1 1 
ATOM 879  C CG2 . THR A 1 126 ? 122.262 103.870 89.659  1.00 49.85  ? 109 THR A CG2 1 
ATOM 880  N N   . SER A 1 127 ? 122.110 107.091 90.821  1.00 49.85  ? 110 SER A N   1 
ATOM 881  C CA  . SER A 1 127 ? 121.270 108.125 90.223  1.00 49.85  ? 110 SER A CA  1 
ATOM 882  C C   . SER A 1 127 ? 122.095 109.327 89.779  1.00 49.85  ? 110 SER A C   1 
ATOM 883  O O   . SER A 1 127 ? 121.862 109.884 88.699  1.00 49.85  ? 110 SER A O   1 
ATOM 884  C CB  . SER A 1 127 ? 120.184 108.554 91.209  1.00 49.85  ? 110 SER A CB  1 
ATOM 885  O OG  . SER A 1 127 ? 119.181 107.560 91.326  1.00 49.85  ? 110 SER A OG  1 
ATOM 886  N N   . ILE A 1 128 ? 123.059 109.747 90.601  1.00 49.85  ? 111 ILE A N   1 
ATOM 887  C CA  . ILE A 1 128 ? 123.895 110.890 90.248  1.00 49.85  ? 111 ILE A CA  1 
ATOM 888  C C   . ILE A 1 128 ? 124.745 110.579 89.023  1.00 49.85  ? 111 ILE A C   1 
ATOM 889  O O   . ILE A 1 128 ? 124.863 111.404 88.109  1.00 49.85  ? 111 ILE A O   1 
ATOM 890  C CB  . ILE A 1 128 ? 124.763 111.311 91.447  1.00 49.85  ? 111 ILE A CB  1 
ATOM 891  C CG1 . ILE A 1 128 ? 123.955 112.183 92.406  1.00 49.85  ? 111 ILE A CG1 1 
ATOM 892  C CG2 . ILE A 1 128 ? 126.005 112.048 90.980  1.00 49.85  ? 111 ILE A CG2 1 
ATOM 893  C CD1 . ILE A 1 128 ? 124.719 112.583 93.640  1.00 49.85  ? 111 ILE A CD1 1 
ATOM 894  N N   . VAL A 1 129 ? 125.349 109.389 88.980  1.00 49.85  ? 112 VAL A N   1 
ATOM 895  C CA  . VAL A 1 129 ? 126.168 109.020 87.828  1.00 49.85  ? 112 VAL A CA  1 
ATOM 896  C C   . VAL A 1 129 ? 125.314 108.957 86.567  1.00 49.85  ? 112 VAL A C   1 
ATOM 897  O O   . VAL A 1 129 ? 125.744 109.376 85.485  1.00 49.85  ? 112 VAL A O   1 
ATOM 898  C CB  . VAL A 1 129 ? 126.896 107.690 88.099  1.00 49.85  ? 112 VAL A CB  1 
ATOM 899  C CG1 . VAL A 1 129 ? 127.205 106.962 86.799  1.00 49.85  ? 112 VAL A CG1 1 
ATOM 900  C CG2 . VAL A 1 129 ? 128.170 107.939 88.890  1.00 49.85  ? 112 VAL A CG2 1 
ATOM 901  N N   . ARG A 1 130 ? 124.084 108.453 86.690  1.00 49.85  ? 113 ARG A N   1 
ATOM 902  C CA  . ARG A 1 130 ? 123.207 108.351 85.529  1.00 49.85  ? 113 ARG A CA  1 
ATOM 903  C C   . ARG A 1 130 ? 122.727 109.716 85.049  1.00 49.85  ? 113 ARG A C   1 
ATOM 904  O O   . ARG A 1 130 ? 122.543 109.916 83.843  1.00 49.85  ? 113 ARG A O   1 
ATOM 905  C CB  . ARG A 1 130 ? 122.011 107.459 85.858  1.00 49.85  ? 113 ARG A CB  1 
ATOM 906  C CG  . ARG A 1 130 ? 122.201 105.998 85.490  1.00 49.85  ? 113 ARG A CG  1 
ATOM 907  C CD  . ARG A 1 130 ? 120.863 105.298 85.345  1.00 49.85  ? 113 ARG A CD  1 
ATOM 908  N NE  . ARG A 1 130 ? 119.909 105.756 86.348  1.00 49.85  ? 113 ARG A NE  1 
ATOM 909  C CZ  . ARG A 1 130 ? 118.611 105.487 86.326  1.00 49.85  ? 113 ARG A CZ  1 
ATOM 910  N NH1 . ARG A 1 130 ? 118.072 104.756 85.364  1.00 49.85  ? 113 ARG A NH1 1 
ATOM 911  N NH2 . ARG A 1 130 ? 117.834 105.962 87.295  1.00 49.85  ? 113 ARG A NH2 1 
ATOM 912  N N   . GLY A 1 131 ? 122.524 110.661 85.964  1.00 49.85  ? 114 GLY A N   1 
ATOM 913  C CA  . GLY A 1 131 ? 121.912 111.930 85.619  1.00 49.85  ? 114 GLY A CA  1 
ATOM 914  C C   . GLY A 1 131 ? 122.800 112.903 84.868  1.00 49.85  ? 114 GLY A C   1 
ATOM 915  O O   . GLY A 1 131 ? 123.122 113.978 85.381  1.00 49.85  ? 114 GLY A O   1 
ATOM 916  N N   . ILE A 1 132 ? 123.191 112.543 83.652  1.00 49.85  ? 115 ILE A N   1 
ATOM 917  C CA  . ILE A 1 132 ? 124.003 113.439 82.820  1.00 49.85  ? 115 ILE A CA  1 
ATOM 918  C C   . ILE A 1 132 ? 123.168 114.652 82.423  1.00 49.85  ? 115 ILE A C   1 
ATOM 919  O O   . ILE A 1 132 ? 121.977 114.498 82.097  1.00 49.85  ? 115 ILE A O   1 
ATOM 920  C CB  . ILE A 1 132 ? 124.525 112.689 81.589  1.00 49.85  ? 115 ILE A CB  1 
ATOM 921  C CG1 . ILE A 1 132 ? 125.331 113.617 80.677  1.00 49.85  ? 115 ILE A CG1 1 
ATOM 922  C CG2 . ILE A 1 132 ? 123.385 112.026 80.831  1.00 49.85  ? 115 ILE A CG2 1 
ATOM 923  C CD1 . ILE A 1 132 ? 125.988 112.905 79.516  1.00 49.85  ? 115 ILE A CD1 1 
ATOM 924  N N   . PRO A 1 133 ? 123.722 115.865 82.455  1.00 49.85  ? 116 PRO A N   1 
ATOM 925  C CA  . PRO A 1 133 ? 122.932 117.055 82.109  1.00 49.85  ? 116 PRO A CA  1 
ATOM 926  C C   . PRO A 1 133 ? 122.459 117.028 80.662  1.00 49.85  ? 116 PRO A C   1 
ATOM 927  O O   . PRO A 1 133 ? 122.874 116.202 79.846  1.00 49.85  ? 116 PRO A O   1 
ATOM 928  C CB  . PRO A 1 133 ? 123.908 118.210 82.359  1.00 49.85  ? 116 PRO A CB  1 
ATOM 929  C CG  . PRO A 1 133 ? 124.860 117.673 83.372  1.00 49.85  ? 116 PRO A CG  1 
ATOM 930  C CD  . PRO A 1 133 ? 125.037 116.226 83.012  1.00 49.85  ? 116 PRO A CD  1 
ATOM 931  N N   . PHE A 1 134 ? 121.567 117.964 80.348  1.00 49.85  ? 117 PHE A N   1 
ATOM 932  C CA  . PHE A 1 134 ? 120.945 118.038 79.034  1.00 49.85  ? 117 PHE A CA  1 
ATOM 933  C C   . PHE A 1 134 ? 121.790 118.862 78.071  1.00 49.85  ? 117 PHE A C   1 
ATOM 934  O O   . PHE A 1 134 ? 122.484 119.802 78.464  1.00 49.85  ? 117 PHE A O   1 
ATOM 935  C CB  . PHE A 1 134 ? 119.542 118.639 79.130  1.00 49.85  ? 117 PHE A CB  1 
ATOM 936  C CG  . PHE A 1 134 ? 118.709 118.431 77.897  1.00 49.85  ? 117 PHE A CG  1 
ATOM 937  C CD1 . PHE A 1 134 ? 118.413 117.155 77.451  1.00 49.85  ? 117 PHE A CD1 1 
ATOM 938  C CD2 . PHE A 1 134 ? 118.225 119.514 77.184  1.00 49.85  ? 117 PHE A CD2 1 
ATOM 939  C CE1 . PHE A 1 134 ? 117.649 116.963 76.317  1.00 49.85  ? 117 PHE A CE1 1 
ATOM 940  C CE2 . PHE A 1 134 ? 117.460 119.327 76.050  1.00 49.85  ? 117 PHE A CE2 1 
ATOM 941  C CZ  . PHE A 1 134 ? 117.172 118.050 75.616  1.00 49.85  ? 117 PHE A CZ  1 
ATOM 942  N N   . TRP A 1 135 ? 121.720 118.492 76.796  1.00 51.08  ? 118 TRP A N   1 
ATOM 943  C CA  . TRP A 1 135 ? 122.476 119.159 75.736  1.00 51.08  ? 118 TRP A CA  1 
ATOM 944  C C   . TRP A 1 135 ? 121.608 120.199 75.028  1.00 51.08  ? 118 TRP A C   1 
ATOM 945  O O   . TRP A 1 135 ? 121.368 120.137 73.823  1.00 51.08  ? 118 TRP A O   1 
ATOM 946  C CB  . TRP A 1 135 ? 123.015 118.125 74.754  1.00 51.08  ? 118 TRP A CB  1 
ATOM 947  C CG  . TRP A 1 135 ? 124.266 117.464 75.226  1.00 51.08  ? 118 TRP A CG  1 
ATOM 948  C CD1 . TRP A 1 135 ? 124.589 117.146 76.512  1.00 51.08  ? 118 TRP A CD1 1 
ATOM 949  C CD2 . TRP A 1 135 ? 125.362 117.027 74.417  1.00 51.08  ? 118 TRP A CD2 1 
ATOM 950  N NE1 . TRP A 1 135 ? 125.821 116.543 76.556  1.00 51.08  ? 118 TRP A NE1 1 
ATOM 951  C CE2 . TRP A 1 135 ? 126.317 116.458 75.282  1.00 51.08  ? 118 TRP A CE2 1 
ATOM 952  C CE3 . TRP A 1 135 ? 125.630 117.062 73.046  1.00 51.08  ? 118 TRP A CE3 1 
ATOM 953  C CZ2 . TRP A 1 135 ? 127.517 115.928 74.821  1.00 51.08  ? 118 TRP A CZ2 1 
ATOM 954  C CZ3 . TRP A 1 135 ? 126.822 116.538 72.592  1.00 51.08  ? 118 TRP A CZ3 1 
ATOM 955  C CH2 . TRP A 1 135 ? 127.751 115.979 73.476  1.00 51.08  ? 118 TRP A CH2 1 
ATOM 956  N N   . GLY A 1 136 ? 121.134 121.171 75.803  1.00 52.42  ? 119 GLY A N   1 
ATOM 957  C CA  . GLY A 1 136 ? 120.258 122.194 75.268  1.00 52.42  ? 119 GLY A CA  1 
ATOM 958  C C   . GLY A 1 136 ? 120.950 123.509 74.978  1.00 52.42  ? 119 GLY A C   1 
ATOM 959  O O   . GLY A 1 136 ? 120.355 124.579 75.137  1.00 52.42  ? 119 GLY A O   1 
ATOM 960  N N   . GLY A 1 137 ? 122.207 123.445 74.553  1.00 65.16  ? 120 GLY A N   1 
ATOM 961  C CA  . GLY A 1 137 ? 122.987 124.622 74.241  1.00 65.16  ? 120 GLY A CA  1 
ATOM 962  C C   . GLY A 1 137 ? 122.932 125.081 72.802  1.00 65.16  ? 120 GLY A C   1 
ATOM 963  O O   . GLY A 1 137 ? 123.682 125.989 72.428  1.00 65.16  ? 120 GLY A O   1 
ATOM 964  N N   . SER A 1 138 ? 122.072 124.489 71.980  1.00 79.99  ? 121 SER A N   1 
ATOM 965  C CA  . SER A 1 138 ? 121.996 124.811 70.563  1.00 79.99  ? 121 SER A CA  1 
ATOM 966  C C   . SER A 1 138 ? 120.786 125.690 70.277  1.00 79.99  ? 121 SER A C   1 
ATOM 967  O O   . SER A 1 138 ? 119.708 125.487 70.842  1.00 79.99  ? 121 SER A O   1 
ATOM 968  C CB  . SER A 1 138 ? 121.921 123.538 69.719  1.00 79.99  ? 121 SER A CB  1 
ATOM 969  O OG  . SER A 1 138 ? 122.060 123.834 68.341  1.00 79.99  ? 121 SER A OG  1 
ATOM 970  N N   . THR A 1 139 ? 120.974 126.669 69.389  1.00 92.72  ? 122 THR A N   1 
ATOM 971  C CA  . THR A 1 139 ? 119.883 127.547 68.988  1.00 92.72  ? 122 THR A CA  1 
ATOM 972  C C   . THR A 1 139 ? 118.901 126.867 68.044  1.00 92.72  ? 122 THR A C   1 
ATOM 973  O O   . THR A 1 139 ? 117.726 127.251 68.015  1.00 92.72  ? 122 THR A O   1 
ATOM 974  C CB  . THR A 1 139 ? 120.437 128.809 68.323  1.00 92.72  ? 122 THR A CB  1 
ATOM 975  O OG1 . THR A 1 139 ? 120.981 128.476 67.040  1.00 92.72  ? 122 THR A OG1 1 
ATOM 976  C CG2 . THR A 1 139 ? 121.525 129.431 69.184  1.00 92.72  ? 122 THR A CG2 1 
ATOM 977  N N   . ILE A 1 140 ? 119.351 125.876 67.276  1.00 96.19  ? 123 ILE A N   1 
ATOM 978  C CA  . ILE A 1 140 ? 118.461 125.165 66.366  1.00 96.19  ? 123 ILE A CA  1 
ATOM 979  C C   . ILE A 1 140 ? 117.481 124.326 67.174  1.00 96.19  ? 123 ILE A C   1 
ATOM 980  O O   . ILE A 1 140 ? 117.873 123.590 68.089  1.00 96.19  ? 123 ILE A O   1 
ATOM 981  C CB  . ILE A 1 140 ? 119.269 124.297 65.390  1.00 96.19  ? 123 ILE A CB  1 
ATOM 982  C CG1 . ILE A 1 140 ? 120.179 125.172 64.526  1.00 96.19  ? 123 ILE A CG1 1 
ATOM 983  C CG2 . ILE A 1 140 ? 118.341 123.470 64.517  1.00 96.19  ? 123 ILE A CG2 1 
ATOM 984  C CD1 . ILE A 1 140 ? 120.955 124.399 63.481  1.00 96.19  ? 123 ILE A CD1 1 
ATOM 985  N N   . ASP A 1 141 ? 116.194 124.436 66.839  1.00 102.39 ? 124 ASP A N   1 
ATOM 986  C CA  . ASP A 1 141 ? 115.151 123.722 67.566  1.00 102.39 ? 124 ASP A CA  1 
ATOM 987  C C   . ASP A 1 141 ? 115.208 122.213 67.364  1.00 102.39 ? 124 ASP A C   1 
ATOM 988  O O   . ASP A 1 141 ? 114.577 121.481 68.135  1.00 102.39 ? 124 ASP A O   1 
ATOM 989  C CB  . ASP A 1 141 ? 113.776 124.248 67.150  1.00 102.39 ? 124 ASP A CB  1 
ATOM 990  C CG  . ASP A 1 141 ? 112.673 123.812 68.094  1.00 102.39 ? 124 ASP A CG  1 
ATOM 991  O OD1 . ASP A 1 141 ? 112.925 123.752 69.317  1.00 102.39 ? 124 ASP A OD1 1 
ATOM 992  O OD2 . ASP A 1 141 ? 111.555 123.528 67.615  1.00 102.39 ? 124 ASP A OD2 1 
ATOM 993  N N   . THR A 1 142 ? 115.942 121.727 66.361  1.00 94.87  ? 125 THR A N   1 
ATOM 994  C CA  . THR A 1 142 ? 116.015 120.299 66.072  1.00 94.87  ? 125 THR A CA  1 
ATOM 995  C C   . THR A 1 142 ? 117.447 119.774 66.097  1.00 94.87  ? 125 THR A C   1 
ATOM 996  O O   . THR A 1 142 ? 117.737 118.745 65.479  1.00 94.87  ? 125 THR A O   1 
ATOM 997  C CB  . THR A 1 142 ? 115.362 119.991 64.722  1.00 94.87  ? 125 THR A CB  1 
ATOM 998  O OG1 . THR A 1 142 ? 115.471 118.590 64.444  1.00 94.87  ? 125 THR A OG1 1 
ATOM 999  C CG2 . THR A 1 142 ? 116.033 120.782 63.608  1.00 94.87  ? 125 THR A CG2 1 
ATOM 1000 N N   . GLU A 1 143 ? 118.348 120.454 66.805  1.00 89.09  ? 126 GLU A N   1 
ATOM 1001 C CA  . GLU A 1 143 ? 119.735 120.028 66.909  1.00 89.09  ? 126 GLU A CA  1 
ATOM 1002 C C   . GLU A 1 143 ? 120.199 120.180 68.349  1.00 89.09  ? 126 GLU A C   1 
ATOM 1003 O O   . GLU A 1 143 ? 119.898 121.184 69.001  1.00 89.09  ? 126 GLU A O   1 
ATOM 1004 C CB  . GLU A 1 143 ? 120.636 120.836 65.963  1.00 89.09  ? 126 GLU A CB  1 
ATOM 1005 C CG  . GLU A 1 143 ? 122.069 121.008 66.437  1.00 89.09  ? 126 GLU A CG  1 
ATOM 1006 C CD  . GLU A 1 143 ? 122.768 122.177 65.769  1.00 89.09  ? 126 GLU A CD  1 
ATOM 1007 O OE1 . GLU A 1 143 ? 123.104 122.064 64.572  1.00 89.09  ? 126 GLU A OE1 1 
ATOM 1008 O OE2 . GLU A 1 143 ? 122.983 123.207 66.440  1.00 89.09  ? 126 GLU A OE2 1 
ATOM 1009 N N   . LEU A 1 144 ? 120.924 119.180 68.844  1.00 76.57  ? 127 LEU A N   1 
ATOM 1010 C CA  . LEU A 1 144 ? 121.443 119.179 70.206  1.00 76.57  ? 127 LEU A CA  1 
ATOM 1011 C C   . LEU A 1 144 ? 122.944 119.426 70.187  1.00 76.57  ? 127 LEU A C   1 
ATOM 1012 O O   . LEU A 1 144 ? 123.672 118.799 69.410  1.00 76.57  ? 127 LEU A O   1 
ATOM 1013 C CB  . LEU A 1 144 ? 121.138 117.857 70.914  1.00 76.57  ? 127 LEU A CB  1 
ATOM 1014 C CG  . LEU A 1 144 ? 119.672 117.431 70.971  1.00 76.57  ? 127 LEU A CG  1 
ATOM 1015 C CD1 . LEU A 1 144 ? 119.553 115.915 71.018  1.00 76.57  ? 127 LEU A CD1 1 
ATOM 1016 C CD2 . LEU A 1 144 ? 118.975 118.066 72.163  1.00 76.57  ? 127 LEU A CD2 1 
ATOM 1017 N N   . LYS A 1 145 ? 123.399 120.337 71.044  1.00 57.39  ? 128 LYS A N   1 
ATOM 1018 C CA  . LYS A 1 145 ? 124.810 120.667 71.169  1.00 57.39  ? 128 LYS A CA  1 
ATOM 1019 C C   . LYS A 1 145 ? 125.157 120.793 72.644  1.00 57.39  ? 128 LYS A C   1 
ATOM 1020 O O   . LYS A 1 145 ? 124.368 121.328 73.429  1.00 57.39  ? 128 LYS A O   1 
ATOM 1021 C CB  . LYS A 1 145 ? 125.146 121.969 70.429  1.00 57.39  ? 128 LYS A CB  1 
ATOM 1022 C CG  . LYS A 1 145 ? 126.580 122.441 70.601  1.00 57.39  ? 128 LYS A CG  1 
ATOM 1023 C CD  . LYS A 1 145 ? 126.952 123.470 69.546  1.00 57.39  ? 128 LYS A CD  1 
ATOM 1024 C CE  . LYS A 1 145 ? 126.874 124.883 70.100  1.00 57.39  ? 128 LYS A CE  1 
ATOM 1025 N NZ  . LYS A 1 145 ? 128.108 125.252 70.847  1.00 57.39  ? 128 LYS A NZ  1 
ATOM 1026 N N   . VAL A 1 146 ? 126.335 120.291 73.018  1.00 50.61  ? 129 VAL A N   1 
ATOM 1027 C CA  . VAL A 1 146 ? 126.756 120.339 74.412  1.00 50.61  ? 129 VAL A CA  1 
ATOM 1028 C C   . VAL A 1 146 ? 126.990 121.785 74.834  1.00 50.61  ? 129 VAL A C   1 
ATOM 1029 O O   . VAL A 1 146 ? 127.328 122.654 74.018  1.00 50.61  ? 129 VAL A O   1 
ATOM 1030 C CB  . VAL A 1 146 ? 128.018 119.482 74.629  1.00 50.61  ? 129 VAL A CB  1 
ATOM 1031 C CG1 . VAL A 1 146 ? 129.246 120.173 74.054  1.00 50.61  ? 129 VAL A CG1 1 
ATOM 1032 C CG2 . VAL A 1 146 ? 128.216 119.179 76.108  1.00 50.61  ? 129 VAL A CG2 1 
ATOM 1033 N N   . ILE A 1 147 ? 126.792 122.050 76.116  1.00 49.85  ? 130 ILE A N   1 
ATOM 1034 C CA  . ILE A 1 147 ? 127.051 123.362 76.693  1.00 49.85  ? 130 ILE A CA  1 
ATOM 1035 C C   . ILE A 1 147 ? 128.484 123.388 77.201  1.00 49.85  ? 130 ILE A C   1 
ATOM 1036 O O   . ILE A 1 147 ? 128.974 122.407 77.772  1.00 49.85  ? 130 ILE A O   1 
ATOM 1037 C CB  . ILE A 1 147 ? 126.048 123.674 77.820  1.00 49.85  ? 130 ILE A CB  1 
ATOM 1038 C CG1 . ILE A 1 147 ? 124.614 123.495 77.321  1.00 49.85  ? 130 ILE A CG1 1 
ATOM 1039 C CG2 . ILE A 1 147 ? 126.248 125.089 78.341  1.00 49.85  ? 130 ILE A CG2 1 
ATOM 1040 C CD1 . ILE A 1 147 ? 123.579 123.506 78.422  1.00 49.85  ? 130 ILE A CD1 1 
ATOM 1041 N N   . ASP A 1 148 ? 129.168 124.513 76.979  1.00 49.85  ? 131 ASP A N   1 
ATOM 1042 C CA  . ASP A 1 148 ? 130.552 124.640 77.424  1.00 49.85  ? 131 ASP A CA  1 
ATOM 1043 C C   . ASP A 1 148 ? 130.654 124.565 78.942  1.00 49.85  ? 131 ASP A C   1 
ATOM 1044 O O   . ASP A 1 148 ? 131.604 123.987 79.482  1.00 49.85  ? 131 ASP A O   1 
ATOM 1045 C CB  . ASP A 1 148 ? 131.150 125.949 76.909  1.00 49.85  ? 131 ASP A CB  1 
ATOM 1046 C CG  . ASP A 1 148 ? 131.553 125.871 75.450  1.00 49.85  ? 131 ASP A CG  1 
ATOM 1047 O OD1 . ASP A 1 148 ? 131.151 124.902 74.772  1.00 49.85  ? 131 ASP A OD1 1 
ATOM 1048 O OD2 . ASP A 1 148 ? 132.271 126.779 74.981  1.00 49.85  ? 131 ASP A OD2 1 
ATOM 1049 N N   . THR A 1 149 ? 129.688 125.144 79.646  1.00 49.85  ? 132 THR A N   1 
ATOM 1050 C CA  . THR A 1 149 ? 129.686 125.178 81.107  1.00 49.85  ? 132 THR A CA  1 
ATOM 1051 C C   . THR A 1 149 ? 129.482 123.805 81.752  1.00 49.85  ? 132 THR A C   1 
ATOM 1052 O O   . THR A 1 149 ? 129.373 123.765 82.984  1.00 49.85  ? 132 THR A O   1 
ATOM 1053 C CB  . THR A 1 149 ? 128.606 126.138 81.606  1.00 49.85  ? 132 THR A CB  1 
ATOM 1054 O OG1 . THR A 1 149 ? 127.335 125.477 81.593  1.00 49.85  ? 132 THR A OG1 1 
ATOM 1055 C CG2 . THR A 1 149 ? 128.539 127.371 80.721  1.00 49.85  ? 132 THR A CG2 1 
ATOM 1056 N N   . ASN A 1 150 ? 129.418 122.693 81.018  1.00 52.50  ? 133 ASN A N   1 
ATOM 1057 C CA  . ASN A 1 150 ? 129.251 121.377 81.624  1.00 52.50  ? 133 ASN A CA  1 
ATOM 1058 C C   . ASN A 1 150 ? 130.353 120.400 81.228  1.00 52.50  ? 133 ASN A C   1 
ATOM 1059 O O   . ASN A 1 150 ? 130.232 119.201 81.505  1.00 52.50  ? 133 ASN A O   1 
ATOM 1060 C CB  . ASN A 1 150 ? 127.871 120.804 81.274  1.00 52.50  ? 133 ASN A CB  1 
ATOM 1061 C CG  . ASN A 1 150 ? 127.838 120.121 79.919  1.00 52.50  ? 133 ASN A CG  1 
ATOM 1062 O OD1 . ASN A 1 150 ? 128.118 118.929 79.801  1.00 52.50  ? 133 ASN A OD1 1 
ATOM 1063 N ND2 . ASN A 1 150 ? 127.487 120.877 78.888  1.00 52.50  ? 133 ASN A ND2 1 
ATOM 1064 N N   . CYS A 1 151 ? 131.430 120.878 80.609  1.00 49.85  ? 134 CYS A N   1 
ATOM 1065 C CA  . CYS A 1 151 ? 132.557 120.041 80.227  1.00 49.85  ? 134 CYS A CA  1 
ATOM 1066 C C   . CYS A 1 151 ? 133.851 120.711 80.664  1.00 49.85  ? 134 CYS A C   1 
ATOM 1067 O O   . CYS A 1 151 ? 133.925 121.938 80.767  1.00 49.85  ? 134 CYS A O   1 
ATOM 1068 C CB  . CYS A 1 151 ? 132.582 119.787 78.715  1.00 49.85  ? 134 CYS A CB  1 
ATOM 1069 S SG  . CYS A 1 151 ? 131.361 118.587 78.139  1.00 49.85  ? 134 CYS A SG  1 
ATOM 1070 N N   . ILE A 1 152 ? 134.876 119.896 80.924  1.00 49.85  ? 135 ILE A N   1 
ATOM 1071 C CA  . ILE A 1 152 ? 136.151 120.404 81.416  1.00 49.85  ? 135 ILE A CA  1 
ATOM 1072 C C   . ILE A 1 152 ? 137.281 119.830 80.574  1.00 49.85  ? 135 ILE A C   1 
ATOM 1073 O O   . ILE A 1 152 ? 137.158 118.764 79.969  1.00 49.85  ? 135 ILE A O   1 
ATOM 1074 C CB  . ILE A 1 152 ? 136.379 120.078 82.908  1.00 49.85  ? 135 ILE A CB  1 
ATOM 1075 C CG1 . ILE A 1 152 ? 136.510 118.568 83.110  1.00 49.85  ? 135 ILE A CG1 1 
ATOM 1076 C CG2 . ILE A 1 152 ? 135.253 120.643 83.757  1.00 49.85  ? 135 ILE A CG2 1 
ATOM 1077 C CD1 . ILE A 1 152 ? 137.633 118.174 84.041  1.00 49.85  ? 135 ILE A CD1 1 
ATOM 1078 N N   . ASN A 1 153 ? 138.404 120.546 80.551  1.00 49.85  ? 136 ASN A N   1 
ATOM 1079 C CA  . ASN A 1 153 ? 139.542 120.156 79.731  1.00 49.85  ? 136 ASN A CA  1 
ATOM 1080 C C   . ASN A 1 153 ? 140.558 119.391 80.567  1.00 49.85  ? 136 ASN A C   1 
ATOM 1081 O O   . ASN A 1 153 ? 140.824 119.752 81.714  1.00 49.85  ? 136 ASN A O   1 
ATOM 1082 C CB  . ASN A 1 153 ? 140.205 121.383 79.102  1.00 49.85  ? 136 ASN A CB  1 
ATOM 1083 C CG  . ASN A 1 153 ? 139.377 121.985 77.988  1.00 49.85  ? 136 ASN A CG  1 
ATOM 1084 O OD1 . ASN A 1 153 ? 138.594 121.293 77.339  1.00 49.85  ? 136 ASN A OD1 1 
ATOM 1085 N ND2 . ASN A 1 153 ? 139.548 123.281 77.757  1.00 49.85  ? 136 ASN A ND2 1 
ATOM 1086 N N   . VAL A 1 154 ? 141.119 118.331 79.990  1.00 49.85  ? 137 VAL A N   1 
ATOM 1087 C CA  . VAL A 1 154 ? 142.206 117.576 80.601  1.00 49.85  ? 137 VAL A CA  1 
ATOM 1088 C C   . VAL A 1 154 ? 143.418 117.679 79.685  1.00 49.85  ? 137 VAL A C   1 
ATOM 1089 O O   . VAL A 1 154 ? 143.303 117.488 78.469  1.00 49.85  ? 137 VAL A O   1 
ATOM 1090 C CB  . VAL A 1 154 ? 141.819 116.105 80.853  1.00 49.85  ? 137 VAL A CB  1 
ATOM 1091 C CG1 . VAL A 1 154 ? 140.761 116.019 81.938  1.00 49.85  ? 137 VAL A CG1 1 
ATOM 1092 C CG2 . VAL A 1 154 ? 141.321 115.443 79.578  1.00 49.85  ? 137 VAL A CG2 1 
ATOM 1093 N N   . ILE A 1 155 ? 144.571 117.997 80.264  1.00 51.08  ? 138 ILE A N   1 
ATOM 1094 C CA  . ILE A 1 155 ? 145.793 118.254 79.511  1.00 51.08  ? 138 ILE A CA  1 
ATOM 1095 C C   . ILE A 1 155 ? 146.712 117.052 79.661  1.00 51.08  ? 138 ILE A C   1 
ATOM 1096 O O   . ILE A 1 155 ? 147.138 116.719 80.773  1.00 51.08  ? 138 ILE A O   1 
ATOM 1097 C CB  . ILE A 1 155 ? 146.487 119.539 79.983  1.00 51.08  ? 138 ILE A CB  1 
ATOM 1098 C CG1 . ILE A 1 155 ? 145.466 120.667 80.134  1.00 51.08  ? 138 ILE A CG1 1 
ATOM 1099 C CG2 . ILE A 1 155 ? 147.587 119.937 79.012  1.00 51.08  ? 138 ILE A CG2 1 
ATOM 1100 C CD1 . ILE A 1 155 ? 145.201 121.054 81.567  1.00 51.08  ? 138 ILE A CD1 1 
ATOM 1101 N N   . GLN A 1 156 ? 147.016 116.405 78.540  1.00 56.76  ? 139 GLN A N   1 
ATOM 1102 C CA  . GLN A 1 156 ? 147.979 115.322 78.531  1.00 56.76  ? 139 GLN A CA  1 
ATOM 1103 C C   . GLN A 1 156 ? 149.386 115.878 78.739  1.00 56.76  ? 139 GLN A C   1 
ATOM 1104 O O   . GLN A 1 156 ? 149.623 117.074 78.553  1.00 56.76  ? 139 GLN A O   1 
ATOM 1105 C CB  . GLN A 1 156 ? 147.892 114.553 77.214  1.00 56.76  ? 139 GLN A CB  1 
ATOM 1106 C CG  . GLN A 1 156 ? 146.489 114.473 76.638  1.00 56.76  ? 139 GLN A CG  1 
ATOM 1107 C CD  . GLN A 1 156 ? 145.639 113.416 77.314  1.00 56.76  ? 139 GLN A CD  1 
ATOM 1108 O OE1 . GLN A 1 156 ? 145.541 112.285 76.839  1.00 56.76  ? 139 GLN A OE1 1 
ATOM 1109 N NE2 . GLN A 1 156 ? 145.014 113.781 78.427  1.00 56.76  ? 139 GLN A NE2 1 
ATOM 1110 N N   . PRO A 1 157 ? 150.338 115.031 79.147  1.00 64.46  ? 140 PRO A N   1 
ATOM 1111 C CA  . PRO A 1 157 ? 151.712 115.525 79.341  1.00 64.46  ? 140 PRO A CA  1 
ATOM 1112 C C   . PRO A 1 157 ? 152.315 116.156 78.097  1.00 64.46  ? 140 PRO A C   1 
ATOM 1113 O O   . PRO A 1 157 ? 153.144 117.066 78.220  1.00 64.46  ? 140 PRO A O   1 
ATOM 1114 C CB  . PRO A 1 157 ? 152.477 114.264 79.764  1.00 64.46  ? 140 PRO A CB  1 
ATOM 1115 C CG  . PRO A 1 157 ? 151.441 113.399 80.390  1.00 64.46  ? 140 PRO A CG  1 
ATOM 1116 C CD  . PRO A 1 157 ? 150.190 113.635 79.595  1.00 64.46  ? 140 PRO A CD  1 
ATOM 1117 N N   . ASP A 1 158 ? 151.932 115.698 76.903  1.00 69.51  ? 141 ASP A N   1 
ATOM 1118 C CA  . ASP A 1 158 ? 152.436 116.323 75.683  1.00 69.51  ? 141 ASP A CA  1 
ATOM 1119 C C   . ASP A 1 158 ? 151.943 117.761 75.552  1.00 69.51  ? 141 ASP A C   1 
ATOM 1120 O O   . ASP A 1 158 ? 152.695 118.641 75.116  1.00 69.51  ? 141 ASP A O   1 
ATOM 1121 C CB  . ASP A 1 158 ? 152.042 115.490 74.461  1.00 69.51  ? 141 ASP A CB  1 
ATOM 1122 C CG  . ASP A 1 158 ? 150.567 115.594 74.127  1.00 69.51  ? 141 ASP A CG  1 
ATOM 1123 O OD1 . ASP A 1 158 ? 150.183 116.537 73.404  1.00 69.51  ? 141 ASP A OD1 1 
ATOM 1124 O OD2 . ASP A 1 158 ? 149.791 114.729 74.583  1.00 69.51  ? 141 ASP A OD2 1 
ATOM 1125 N N   . GLY A 1 159 ? 150.690 118.020 75.921  1.00 67.59  ? 142 GLY A N   1 
ATOM 1126 C CA  . GLY A 1 159 ? 150.169 119.374 75.903  1.00 67.59  ? 142 GLY A CA  1 
ATOM 1127 C C   . GLY A 1 159 ? 148.836 119.532 75.200  1.00 67.59  ? 142 GLY A C   1 
ATOM 1128 O O   . GLY A 1 159 ? 148.125 120.515 75.429  1.00 67.59  ? 142 GLY A O   1 
ATOM 1129 N N   . SER A 1 160 ? 148.483 118.577 74.344  1.00 65.91  ? 143 SER A N   1 
ATOM 1130 C CA  . SER A 1 160 ? 147.239 118.645 73.578  1.00 65.91  ? 143 SER A CA  1 
ATOM 1131 C C   . SER A 1 160 ? 146.077 118.306 74.503  1.00 65.91  ? 143 SER A C   1 
ATOM 1132 O O   . SER A 1 160 ? 145.863 117.144 74.852  1.00 65.91  ? 143 SER A O   1 
ATOM 1133 C CB  . SER A 1 160 ? 147.290 117.698 72.385  1.00 65.91  ? 143 SER A CB  1 
ATOM 1134 O OG  . SER A 1 160 ? 147.620 116.382 72.795  1.00 65.91  ? 143 SER A OG  1 
ATOM 1135 N N   . TYR A 1 161 ? 145.319 119.324 74.900  1.00 58.70  ? 144 TYR A N   1 
ATOM 1136 C CA  . TYR A 1 161 ? 144.200 119.112 75.803  1.00 58.70  ? 144 TYR A CA  1 
ATOM 1137 C C   . TYR A 1 161 ? 143.014 118.493 75.068  1.00 58.70  ? 144 TYR A C   1 
ATOM 1138 O O   . TYR A 1 161 ? 142.871 118.606 73.847  1.00 58.70  ? 144 TYR A O   1 
ATOM 1139 C CB  . TYR A 1 161 ? 143.792 120.427 76.479  1.00 58.70  ? 144 TYR A CB  1 
ATOM 1140 C CG  . TYR A 1 161 ? 143.506 121.585 75.541  1.00 58.70  ? 144 TYR A CG  1 
ATOM 1141 C CD1 . TYR A 1 161 ? 142.408 121.570 74.689  1.00 58.70  ? 144 TYR A CD1 1 
ATOM 1142 C CD2 . TYR A 1 161 ? 144.336 122.697 75.514  1.00 58.70  ? 144 TYR A CD2 1 
ATOM 1143 C CE1 . TYR A 1 161 ? 142.148 122.626 73.838  1.00 58.70  ? 144 TYR A CE1 1 
ATOM 1144 C CE2 . TYR A 1 161 ? 144.084 123.758 74.665  1.00 58.70  ? 144 TYR A CE2 1 
ATOM 1145 C CZ  . TYR A 1 161 ? 142.989 123.717 73.830  1.00 58.70  ? 144 TYR A CZ  1 
ATOM 1146 O OH  . TYR A 1 161 ? 142.733 124.770 72.982  1.00 58.70  ? 144 TYR A OH  1 
ATOM 1147 N N   . ARG A 1 162 ? 142.161 117.823 75.837  1.00 53.86  ? 145 ARG A N   1 
ATOM 1148 C CA  . ARG A 1 162 ? 140.936 117.226 75.326  1.00 53.86  ? 145 ARG A CA  1 
ATOM 1149 C C   . ARG A 1 162 ? 139.798 117.536 76.284  1.00 53.86  ? 145 ARG A C   1 
ATOM 1150 O O   . ARG A 1 162 ? 139.965 117.453 77.502  1.00 53.86  ? 145 ARG A O   1 
ATOM 1151 C CB  . ARG A 1 162 ? 141.081 115.708 75.153  1.00 53.86  ? 145 ARG A CB  1 
ATOM 1152 C CG  . ARG A 1 162 ? 139.848 115.029 74.579  1.00 53.86  ? 145 ARG A CG  1 
ATOM 1153 C CD  . ARG A 1 162 ? 139.956 113.515 74.663  1.00 53.86  ? 145 ARG A CD  1 
ATOM 1154 N NE  . ARG A 1 162 ? 140.062 113.046 76.040  1.00 53.86  ? 145 ARG A NE  1 
ATOM 1155 C CZ  . ARG A 1 162 ? 140.919 112.123 76.452  1.00 53.86  ? 145 ARG A CZ  1 
ATOM 1156 N NH1 . ARG A 1 162 ? 141.765 111.542 75.617  1.00 53.86  ? 145 ARG A NH1 1 
ATOM 1157 N NH2 . ARG A 1 162 ? 140.927 111.771 77.735  1.00 53.86  ? 145 ARG A NH2 1 
ATOM 1158 N N   . SER A 1 163 ? 138.646 117.904 75.734  1.00 53.26  ? 146 SER A N   1 
ATOM 1159 C CA  . SER A 1 163 ? 137.480 118.165 76.562  1.00 53.26  ? 146 SER A CA  1 
ATOM 1160 C C   . SER A 1 163 ? 136.763 116.863 76.895  1.00 53.26  ? 146 SER A C   1 
ATOM 1161 O O   . SER A 1 163 ? 136.733 115.923 76.097  1.00 53.26  ? 146 SER A O   1 
ATOM 1162 C CB  . SER A 1 163 ? 136.522 119.125 75.858  1.00 53.26  ? 146 SER A CB  1 
ATOM 1163 O OG  . SER A 1 163 ? 137.238 120.104 75.129  1.00 53.26  ? 146 SER A OG  1 
ATOM 1164 N N   . GLU A 1 164 ? 136.196 116.810 78.098  1.00 52.95  ? 147 GLU A N   1 
ATOM 1165 C CA  . GLU A 1 164 ? 135.442 115.652 78.548  1.00 52.95  ? 147 GLU A CA  1 
ATOM 1166 C C   . GLU A 1 164 ? 134.233 116.107 79.348  1.00 52.95  ? 147 GLU A C   1 
ATOM 1167 O O   . GLU A 1 164 ? 134.262 117.142 80.026  1.00 52.95  ? 147 GLU A O   1 
ATOM 1168 C CB  . GLU A 1 164 ? 136.293 114.703 79.405  1.00 52.95  ? 147 GLU A CB  1 
ATOM 1169 C CG  . GLU A 1 164 ? 137.272 113.847 78.620  1.00 52.95  ? 147 GLU A CG  1 
ATOM 1170 C CD  . GLU A 1 164 ? 138.418 113.344 79.475  1.00 52.95  ? 147 GLU A CD  1 
ATOM 1171 O OE1 . GLU A 1 164 ? 138.639 113.910 80.566  1.00 52.95  ? 147 GLU A OE1 1 
ATOM 1172 O OE2 . GLU A 1 164 ? 139.097 112.382 79.059  1.00 52.95  ? 147 GLU A OE2 1 
ATOM 1173 N N   . GLU A 1 165 ? 133.168 115.314 79.258  1.00 54.64  ? 148 GLU A N   1 
ATOM 1174 C CA  . GLU A 1 165 ? 131.988 115.513 80.081  1.00 54.64  ? 148 GLU A CA  1 
ATOM 1175 C C   . GLU A 1 165 ? 132.263 115.066 81.512  1.00 54.64  ? 148 GLU A C   1 
ATOM 1176 O O   . GLU A 1 165 ? 133.212 114.329 81.793  1.00 54.64  ? 148 GLU A O   1 
ATOM 1177 C CB  . GLU A 1 165 ? 130.800 114.734 79.517  1.00 54.64  ? 148 GLU A CB  1 
ATOM 1178 C CG  . GLU A 1 165 ? 130.433 115.085 78.087  1.00 54.64  ? 148 GLU A CG  1 
ATOM 1179 C CD  . GLU A 1 165 ? 129.210 114.331 77.602  1.00 54.64  ? 148 GLU A CD  1 
ATOM 1180 O OE1 . GLU A 1 165 ? 128.082 114.816 77.830  1.00 54.64  ? 148 GLU A OE1 1 
ATOM 1181 O OE2 . GLU A 1 165 ? 129.376 113.253 76.995  1.00 54.64  ? 148 GLU A OE2 1 
ATOM 1182 N N   . LEU A 1 166 ? 131.409 115.518 82.424  1.00 49.85  ? 149 LEU A N   1 
ATOM 1183 C CA  . LEU A 1 166 ? 131.521 115.152 83.829  1.00 49.85  ? 149 LEU A CA  1 
ATOM 1184 C C   . LEU A 1 166 ? 130.208 115.501 84.516  1.00 49.85  ? 149 LEU A C   1 
ATOM 1185 O O   . LEU A 1 166 ? 129.369 116.219 83.966  1.00 49.85  ? 149 LEU A O   1 
ATOM 1186 C CB  . LEU A 1 166 ? 132.708 115.848 84.503  1.00 49.85  ? 149 LEU A CB  1 
ATOM 1187 C CG  . LEU A 1 166 ? 132.571 117.275 85.034  1.00 49.85  ? 149 LEU A CG  1 
ATOM 1188 C CD1 . LEU A 1 166 ? 133.919 117.733 85.532  1.00 49.85  ? 149 LEU A CD1 1 
ATOM 1189 C CD2 . LEU A 1 166 ? 132.062 118.237 83.976  1.00 49.85  ? 149 LEU A CD2 1 
ATOM 1190 N N   . ASN A 1 167 ? 130.039 114.975 85.727  1.00 49.85  ? 150 ASN A N   1 
ATOM 1191 C CA  . ASN A 1 167 ? 128.827 115.202 86.502  1.00 49.85  ? 150 ASN A CA  1 
ATOM 1192 C C   . ASN A 1 167 ? 129.070 115.747 87.898  1.00 49.85  ? 150 ASN A C   1 
ATOM 1193 O O   . ASN A 1 167 ? 128.138 116.311 88.483  1.00 49.85  ? 150 ASN A O   1 
ATOM 1194 C CB  . ASN A 1 167 ? 128.016 113.904 86.622  1.00 49.85  ? 150 ASN A CB  1 
ATOM 1195 C CG  . ASN A 1 167 ? 127.138 113.655 85.418  1.00 49.85  ? 150 ASN A CG  1 
ATOM 1196 O OD1 . ASN A 1 167 ? 125.936 113.911 85.450  1.00 49.85  ? 150 ASN A OD1 1 
ATOM 1197 N ND2 . ASN A 1 167 ? 127.736 113.155 84.344  1.00 49.85  ? 150 ASN A ND2 1 
ATOM 1198 N N   . LEU A 1 168 ? 130.272 115.610 88.451  1.00 49.85  ? 151 LEU A N   1 
ATOM 1199 C CA  . LEU A 1 168 ? 130.535 116.045 89.813  1.00 49.85  ? 151 LEU A CA  1 
ATOM 1200 C C   . LEU A 1 168 ? 131.998 116.432 89.947  1.00 49.85  ? 151 LEU A C   1 
ATOM 1201 O O   . LEU A 1 168 ? 132.874 115.787 89.366  1.00 49.85  ? 151 LEU A O   1 
ATOM 1202 C CB  . LEU A 1 168 ? 130.195 114.946 90.824  1.00 49.85  ? 151 LEU A CB  1 
ATOM 1203 C CG  . LEU A 1 168 ? 128.763 114.901 91.353  1.00 49.85  ? 151 LEU A CG  1 
ATOM 1204 C CD1 . LEU A 1 168 ? 128.677 113.952 92.529  1.00 49.85  ? 151 LEU A CD1 1 
ATOM 1205 C CD2 . LEU A 1 168 ? 128.286 116.288 91.741  1.00 49.85  ? 151 LEU A CD2 1 
ATOM 1206 N N   . VAL A 1 169 ? 132.252 117.490 90.711  1.00 49.85  ? 152 VAL A N   1 
ATOM 1207 C CA  . VAL A 1 169 ? 133.604 117.917 91.046  1.00 49.85  ? 152 VAL A CA  1 
ATOM 1208 C C   . VAL A 1 169 ? 133.630 118.276 92.522  1.00 49.85  ? 152 VAL A C   1 
ATOM 1209 O O   . VAL A 1 169 ? 132.759 119.009 93.002  1.00 49.85  ? 152 VAL A O   1 
ATOM 1210 C CB  . VAL A 1 169 ? 134.064 119.110 90.187  1.00 49.85  ? 152 VAL A CB  1 
ATOM 1211 C CG1 . VAL A 1 169 ? 135.182 119.860 90.876  1.00 49.85  ? 152 VAL A CG1 1 
ATOM 1212 C CG2 . VAL A 1 169 ? 134.526 118.631 88.835  1.00 49.85  ? 152 VAL A CG2 1 
ATOM 1213 N N   . ILE A 1 170 ? 134.622 117.764 93.242  1.00 49.85  ? 153 ILE A N   1 
ATOM 1214 C CA  . ILE A 1 170 ? 134.776 118.020 94.668  1.00 49.85  ? 153 ILE A CA  1 
ATOM 1215 C C   . ILE A 1 170 ? 136.009 118.894 94.853  1.00 49.85  ? 153 ILE A C   1 
ATOM 1216 O O   . ILE A 1 170 ? 137.121 118.500 94.484  1.00 49.85  ? 153 ILE A O   1 
ATOM 1217 C CB  . ILE A 1 170 ? 134.888 116.715 95.467  1.00 49.85  ? 153 ILE A CB  1 
ATOM 1218 C CG1 . ILE A 1 170 ? 133.616 115.878 95.290  1.00 49.85  ? 153 ILE A CG1 1 
ATOM 1219 C CG2 . ILE A 1 170 ? 135.149 117.012 96.933  1.00 49.85  ? 153 ILE A CG2 1 
ATOM 1220 C CD1 . ILE A 1 170 ? 132.604 116.028 96.407  1.00 49.85  ? 153 ILE A CD1 1 
ATOM 1221 N N   . ILE A 1 171 ? 135.808 120.078 95.423  1.00 57.46  ? 154 ILE A N   1 
ATOM 1222 C CA  . ILE A 1 171 ? 136.861 121.067 95.620  1.00 57.46  ? 154 ILE A CA  1 
ATOM 1223 C C   . ILE A 1 171 ? 136.860 121.475 97.084  1.00 57.46  ? 154 ILE A C   1 
ATOM 1224 O O   . ILE A 1 171 ? 135.792 121.673 97.674  1.00 57.46  ? 154 ILE A O   1 
ATOM 1225 C CB  . ILE A 1 171 ? 136.655 122.297 94.709  1.00 57.46  ? 154 ILE A CB  1 
ATOM 1226 C CG1 . ILE A 1 171 ? 136.816 121.910 93.239  1.00 57.46  ? 154 ILE A CG1 1 
ATOM 1227 C CG2 . ILE A 1 171 ? 137.610 123.417 95.074  1.00 57.46  ? 154 ILE A CG2 1 
ATOM 1228 C CD1 . ILE A 1 171 ? 136.724 123.081 92.287  1.00 57.46  ? 154 ILE A CD1 1 
ATOM 1229 N N   . GLY A 1 172 ? 138.049 121.576 97.681  1.00 49.85  ? 155 GLY A N   1 
ATOM 1230 C CA  . GLY A 1 172 ? 138.161 122.018 99.047  1.00 49.85  ? 155 GLY A CA  1 
ATOM 1231 C C   . GLY A 1 172 ? 137.491 123.363 99.226  1.00 49.85  ? 155 GLY A C   1 
ATOM 1232 O O   . GLY A 1 172 ? 137.481 124.203 98.321  1.00 49.85  ? 155 GLY A O   1 
ATOM 1233 N N   . PRO A 1 173 ? 136.909 123.587 100.400 1.00 56.73  ? 156 PRO A N   1 
ATOM 1234 C CA  . PRO A 1 173 ? 136.036 124.751 100.591 1.00 56.73  ? 156 PRO A CA  1 
ATOM 1235 C C   . PRO A 1 173 ? 136.789 126.066 100.457 1.00 56.73  ? 156 PRO A C   1 
ATOM 1236 O O   . PRO A 1 173 ? 138.020 126.130 100.452 1.00 56.73  ? 156 PRO A O   1 
ATOM 1237 C CB  . PRO A 1 173 ? 135.498 124.555 102.012 1.00 56.73  ? 156 PRO A CB  1 
ATOM 1238 C CG  . PRO A 1 173 ? 136.535 123.719 102.685 1.00 56.73  ? 156 PRO A CG  1 
ATOM 1239 C CD  . PRO A 1 173 ? 137.052 122.793 101.630 1.00 56.73  ? 156 PRO A CD  1 
ATOM 1240 N N   . SER A 1 174 ? 136.009 127.136 100.347 1.00 58.11  ? 157 SER A N   1 
ATOM 1241 C CA  . SER A 1 174 ? 136.533 128.490 100.239 1.00 58.11  ? 157 SER A CA  1 
ATOM 1242 C C   . SER A 1 174 ? 136.942 128.978 101.627 1.00 58.11  ? 157 SER A C   1 
ATOM 1243 O O   . SER A 1 174 ? 137.098 128.191 102.564 1.00 58.11  ? 157 SER A O   1 
ATOM 1244 C CB  . SER A 1 174 ? 135.504 129.404 99.582  1.00 58.11  ? 157 SER A CB  1 
ATOM 1245 O OG  . SER A 1 174 ? 135.346 129.087 98.210  1.00 58.11  ? 157 SER A OG  1 
ATOM 1246 N N   . ALA A 1 175 ? 137.145 130.293 101.764 1.00 62.83  ? 158 ALA A N   1 
ATOM 1247 C CA  . ALA A 1 175 ? 137.611 130.858 103.028 1.00 62.83  ? 158 ALA A CA  1 
ATOM 1248 C C   . ALA A 1 175 ? 136.745 130.422 104.203 1.00 62.83  ? 158 ALA A C   1 
ATOM 1249 O O   . ALA A 1 175 ? 137.257 130.223 105.310 1.00 62.83  ? 158 ALA A O   1 
ATOM 1250 C CB  . ALA A 1 175 ? 137.648 132.384 102.937 1.00 62.83  ? 158 ALA A CB  1 
ATOM 1251 N N   . ASP A 1 176 ? 135.443 130.261 103.986 1.00 64.76  ? 159 ASP A N   1 
ATOM 1252 C CA  . ASP A 1 176 ? 134.574 129.622 104.971 1.00 64.76  ? 159 ASP A CA  1 
ATOM 1253 C C   . ASP A 1 176 ? 134.772 128.117 104.843 1.00 64.76  ? 159 ASP A C   1 
ATOM 1254 O O   . ASP A 1 176 ? 134.229 127.479 103.938 1.00 64.76  ? 159 ASP A O   1 
ATOM 1255 C CB  . ASP A 1 176 ? 133.120 130.020 104.750 1.00 64.76  ? 159 ASP A CB  1 
ATOM 1256 C CG  . ASP A 1 176 ? 132.342 130.126 106.046 1.00 64.76  ? 159 ASP A CG  1 
ATOM 1257 O OD1 . ASP A 1 176 ? 132.008 129.072 106.627 1.00 64.76  ? 159 ASP A OD1 1 
ATOM 1258 O OD2 . ASP A 1 176 ? 132.062 131.262 106.483 1.00 64.76  ? 159 ASP A OD2 1 
ATOM 1259 N N   . ILE A 1 177 ? 135.558 127.543 105.758 1.00 55.26  ? 160 ILE A N   1 
ATOM 1260 C CA  . ILE A 1 177 ? 136.026 126.172 105.588 1.00 55.26  ? 160 ILE A CA  1 
ATOM 1261 C C   . ILE A 1 177 ? 134.932 125.142 105.834 1.00 55.26  ? 160 ILE A C   1 
ATOM 1262 O O   . ILE A 1 177 ? 135.085 123.981 105.441 1.00 55.26  ? 160 ILE A O   1 
ATOM 1263 C CB  . ILE A 1 177 ? 137.236 125.909 106.503 1.00 55.26  ? 160 ILE A CB  1 
ATOM 1264 C CG1 . ILE A 1 177 ? 138.227 124.979 105.808 1.00 55.26  ? 160 ILE A CG1 1 
ATOM 1265 C CG2 . ILE A 1 177 ? 136.792 125.315 107.830 1.00 55.26  ? 160 ILE A CG2 1 
ATOM 1266 C CD1 . ILE A 1 177 ? 139.004 125.654 104.707 1.00 55.26  ? 160 ILE A CD1 1 
ATOM 1267 N N   . ILE A 1 178 ? 133.830 125.523 106.478 1.00 56.72  ? 161 ILE A N   1 
ATOM 1268 C CA  . ILE A 1 178 ? 132.733 124.599 106.737 1.00 56.72  ? 161 ILE A CA  1 
ATOM 1269 C C   . ILE A 1 178 ? 131.468 124.973 105.990 1.00 56.72  ? 161 ILE A C   1 
ATOM 1270 O O   . ILE A 1 178 ? 130.437 124.309 106.171 1.00 56.72  ? 161 ILE A O   1 
ATOM 1271 C CB  . ILE A 1 178 ? 132.449 124.470 108.245 1.00 56.72  ? 161 ILE A CB  1 
ATOM 1272 C CG1 . ILE A 1 178 ? 132.249 125.848 108.874 1.00 56.72  ? 161 ILE A CG1 1 
ATOM 1273 C CG2 . ILE A 1 178 ? 133.577 123.723 108.934 1.00 56.72  ? 161 ILE A CG2 1 
ATOM 1274 C CD1 . ILE A 1 178 ? 132.005 125.794 110.361 1.00 56.72  ? 161 ILE A CD1 1 
ATOM 1275 N N   . GLN A 1 179 ? 131.506 126.010 105.158 1.00 64.26  ? 162 GLN A N   1 
ATOM 1276 C CA  . GLN A 1 179 ? 130.364 126.367 104.320 1.00 64.26  ? 162 GLN A CA  1 
ATOM 1277 C C   . GLN A 1 179 ? 130.380 125.453 103.102 1.00 64.26  ? 162 GLN A C   1 
ATOM 1278 O O   . GLN A 1 179 ? 131.118 125.685 102.142 1.00 64.26  ? 162 GLN A O   1 
ATOM 1279 C CB  . GLN A 1 179 ? 130.423 127.836 103.920 1.00 64.26  ? 162 GLN A CB  1 
ATOM 1280 C CG  . GLN A 1 179 ? 129.392 128.245 102.880 1.00 64.26  ? 162 GLN A CG  1 
ATOM 1281 C CD  . GLN A 1 179 ? 129.777 129.514 102.145 1.00 64.26  ? 162 GLN A CD  1 
ATOM 1282 O OE1 . GLN A 1 179 ? 129.745 130.606 102.712 1.00 64.26  ? 162 GLN A OE1 1 
ATOM 1283 N NE2 . GLN A 1 179 ? 130.143 129.376 100.876 1.00 64.26  ? 162 GLN A NE2 1 
ATOM 1284 N N   . PHE A 1 180 ? 129.570 124.399 103.145 1.00 50.85  ? 163 PHE A N   1 
ATOM 1285 C CA  . PHE A 1 180 ? 129.507 123.409 102.073 1.00 50.85  ? 163 PHE A CA  1 
ATOM 1286 C C   . PHE A 1 180 ? 128.298 123.741 101.205 1.00 50.85  ? 163 PHE A C   1 
ATOM 1287 O O   . PHE A 1 180 ? 127.188 123.262 101.439 1.00 50.85  ? 163 PHE A O   1 
ATOM 1288 C CB  . PHE A 1 180 ? 129.431 121.998 102.645 1.00 50.85  ? 163 PHE A CB  1 
ATOM 1289 C CG  . PHE A 1 180 ? 130.515 121.687 103.638 1.00 50.85  ? 163 PHE A CG  1 
ATOM 1290 C CD1 . PHE A 1 180 ? 131.809 122.138 103.437 1.00 50.85  ? 163 PHE A CD1 1 
ATOM 1291 C CD2 . PHE A 1 180 ? 130.239 120.947 104.775 1.00 50.85  ? 163 PHE A CD2 1 
ATOM 1292 C CE1 . PHE A 1 180 ? 132.807 121.853 104.349 1.00 50.85  ? 163 PHE A CE1 1 
ATOM 1293 C CE2 . PHE A 1 180 ? 131.233 120.659 105.690 1.00 50.85  ? 163 PHE A CE2 1 
ATOM 1294 C CZ  . PHE A 1 180 ? 132.518 121.113 105.477 1.00 50.85  ? 163 PHE A CZ  1 
ATOM 1295 N N   . GLU A 1 181 ? 128.520 124.579 100.195 1.00 49.85  ? 164 GLU A N   1 
ATOM 1296 C CA  . GLU A 1 181 ? 127.472 125.015 99.283  1.00 49.85  ? 164 GLU A CA  1 
ATOM 1297 C C   . GLU A 1 181 ? 127.814 124.569 97.870  1.00 49.85  ? 164 GLU A C   1 
ATOM 1298 O O   . GLU A 1 181 ? 128.923 124.822 97.387  1.00 49.85  ? 164 GLU A O   1 
ATOM 1299 C CB  . GLU A 1 181 ? 127.299 126.536 99.332  1.00 49.85  ? 164 GLU A CB  1 
ATOM 1300 C CG  . GLU A 1 181 ? 126.401 127.096 98.241  1.00 49.85  ? 164 GLU A CG  1 
ATOM 1301 C CD  . GLU A 1 181 ? 124.934 127.082 98.626  1.00 49.85  ? 164 GLU A CD  1 
ATOM 1302 O OE1 . GLU A 1 181 ? 124.632 126.832 99.812  1.00 49.85  ? 164 GLU A OE1 1 
ATOM 1303 O OE2 . GLU A 1 181 ? 124.084 127.320 97.743  1.00 49.85  ? 164 GLU A OE2 1 
ATOM 1304 N N   . CYS A 1 182 ? 126.865 123.906 97.215  1.00 49.85  ? 165 CYS A N   1 
ATOM 1305 C CA  . CYS A 1 182 ? 127.059 123.491 95.834  1.00 49.85  ? 165 CYS A CA  1 
ATOM 1306 C C   . CYS A 1 182 ? 127.051 124.701 94.908  1.00 49.85  ? 165 CYS A C   1 
ATOM 1307 O O   . CYS A 1 182 ? 126.315 125.666 95.127  1.00 49.85  ? 165 CYS A O   1 
ATOM 1308 C CB  . CYS A 1 182 ? 125.968 122.506 95.418  1.00 49.85  ? 165 CYS A CB  1 
ATOM 1309 S SG  . CYS A 1 182 ? 125.617 121.223 96.637  1.00 49.85  ? 165 CYS A SG  1 
ATOM 1310 N N   . LYS A 1 183 ? 127.879 124.647 93.869  1.00 49.85  ? 166 LYS A N   1 
ATOM 1311 C CA  . LYS A 1 183 ? 127.938 125.691 92.860  1.00 49.85  ? 166 LYS A CA  1 
ATOM 1312 C C   . LYS A 1 183 ? 127.739 125.080 91.479  1.00 49.85  ? 166 LYS A C   1 
ATOM 1313 O O   . LYS A 1 183 ? 127.881 123.870 91.286  1.00 49.85  ? 166 LYS A O   1 
ATOM 1314 C CB  . LYS A 1 183 ? 129.273 126.444 92.914  1.00 49.85  ? 166 LYS A CB  1 
ATOM 1315 C CG  . LYS A 1 183 ? 129.466 127.268 94.174  1.00 49.85  ? 166 LYS A CG  1 
ATOM 1316 C CD  . LYS A 1 183 ? 128.405 128.349 94.292  1.00 49.85  ? 166 LYS A CD  1 
ATOM 1317 C CE  . LYS A 1 183 ? 129.000 129.656 94.794  1.00 49.85  ? 166 LYS A CE  1 
ATOM 1318 N NZ  . LYS A 1 183 ? 127.968 130.540 95.404  1.00 49.85  ? 166 LYS A NZ  1 
ATOM 1319 N N   . SER A 1 184 ? 127.399 125.931 90.516  1.00 49.85  ? 167 SER A N   1 
ATOM 1320 C CA  . SER A 1 184 ? 127.220 125.479 89.144  1.00 49.85  ? 167 SER A CA  1 
ATOM 1321 C C   . SER A 1 184 ? 127.372 126.669 88.211  1.00 49.85  ? 167 SER A C   1 
ATOM 1322 O O   . SER A 1 184 ? 127.293 127.826 88.632  1.00 49.85  ? 167 SER A O   1 
ATOM 1323 C CB  . SER A 1 184 ? 125.857 124.808 88.944  1.00 49.85  ? 167 SER A CB  1 
ATOM 1324 O OG  . SER A 1 184 ? 125.425 124.926 87.600  1.00 49.85  ? 167 SER A OG  1 
ATOM 1325 N N   . PHE A 1 185 ? 127.591 126.366 86.936  1.00 50.84  ? 168 PHE A N   1 
ATOM 1326 C CA  . PHE A 1 185 ? 127.714 127.374 85.892  1.00 50.84  ? 168 PHE A CA  1 
ATOM 1327 C C   . PHE A 1 185 ? 126.488 127.285 84.995  1.00 50.84  ? 168 PHE A C   1 
ATOM 1328 O O   . PHE A 1 185 ? 126.230 126.237 84.393  1.00 50.84  ? 168 PHE A O   1 
ATOM 1329 C CB  . PHE A 1 185 ? 128.997 127.171 85.087  1.00 50.84  ? 168 PHE A CB  1 
ATOM 1330 C CG  . PHE A 1 185 ? 130.252 127.439 85.869  1.00 50.84  ? 168 PHE A CG  1 
ATOM 1331 C CD1 . PHE A 1 185 ? 130.657 128.735 86.134  1.00 50.84  ? 168 PHE A CD1 1 
ATOM 1332 C CD2 . PHE A 1 185 ? 131.024 126.391 86.343  1.00 50.84  ? 168 PHE A CD2 1 
ATOM 1333 C CE1 . PHE A 1 185 ? 131.809 128.983 86.855  1.00 50.84  ? 168 PHE A CE1 1 
ATOM 1334 C CE2 . PHE A 1 185 ? 132.176 126.633 87.064  1.00 50.84  ? 168 PHE A CE2 1 
ATOM 1335 C CZ  . PHE A 1 185 ? 132.569 127.930 87.320  1.00 50.84  ? 168 PHE A CZ  1 
ATOM 1336 N N   . GLY A 1 186 ? 125.737 128.383 84.905  1.00 52.43  ? 169 GLY A N   1 
ATOM 1337 C CA  . GLY A 1 186 ? 124.485 128.408 84.186  1.00 52.43  ? 169 GLY A CA  1 
ATOM 1338 C C   . GLY A 1 186 ? 124.629 128.916 82.762  1.00 52.43  ? 169 GLY A C   1 
ATOM 1339 O O   . GLY A 1 186 ? 125.726 129.050 82.216  1.00 52.43  ? 169 GLY A O   1 
ATOM 1340 N N   . HIS A 1 187 ? 123.481 129.204 82.157  1.00 65.31  ? 170 HIS A N   1 
ATOM 1341 C CA  . HIS A 1 187 ? 123.394 129.693 80.791  1.00 65.31  ? 170 HIS A CA  1 
ATOM 1342 C C   . HIS A 1 187 ? 122.878 131.126 80.796  1.00 65.31  ? 170 HIS A C   1 
ATOM 1343 O O   . HIS A 1 187 ? 122.410 131.641 81.815  1.00 65.31  ? 170 HIS A O   1 
ATOM 1344 C CB  . HIS A 1 187 ? 122.488 128.792 79.941  1.00 65.31  ? 170 HIS A CB  1 
ATOM 1345 C CG  . HIS A 1 187 ? 122.828 128.793 78.483  1.00 65.31  ? 170 HIS A CG  1 
ATOM 1346 N ND1 . HIS A 1 187 ? 122.275 129.683 77.589  1.00 65.31  ? 170 HIS A ND1 1 
ATOM 1347 C CD2 . HIS A 1 187 ? 123.668 128.011 77.764  1.00 65.31  ? 170 HIS A CD2 1 
ATOM 1348 C CE1 . HIS A 1 187 ? 122.757 129.450 76.382  1.00 65.31  ? 170 HIS A CE1 1 
ATOM 1349 N NE2 . HIS A 1 187 ? 123.605 128.440 76.460  1.00 65.31  ? 170 HIS A NE2 1 
ATOM 1350 N N   . GLU A 1 188 ? 122.977 131.774 79.633  1.00 74.20  ? 171 GLU A N   1 
ATOM 1351 C CA  . GLU A 1 188 ? 122.606 133.182 79.529  1.00 74.20  ? 171 GLU A CA  1 
ATOM 1352 C C   . GLU A 1 188 ? 121.120 133.390 79.799  1.00 74.20  ? 171 GLU A C   1 
ATOM 1353 O O   . GLU A 1 188 ? 120.737 134.247 80.604  1.00 74.20  ? 171 GLU A O   1 
ATOM 1354 C CB  . GLU A 1 188 ? 122.981 133.719 78.148  1.00 74.20  ? 171 GLU A CB  1 
ATOM 1355 C CG  . GLU A 1 188 ? 124.064 134.784 78.167  1.00 74.20  ? 171 GLU A CG  1 
ATOM 1356 C CD  . GLU A 1 188 ? 124.387 135.310 76.782  1.00 74.20  ? 171 GLU A CD  1 
ATOM 1357 O OE1 . GLU A 1 188 ? 123.446 135.498 75.982  1.00 74.20  ? 171 GLU A OE1 1 
ATOM 1358 O OE2 . GLU A 1 188 ? 125.581 135.535 76.494  1.00 74.20  ? 171 GLU A OE2 1 
ATOM 1359 N N   . VAL A 1 189 ? 120.266 132.614 79.136  1.00 68.80  ? 172 VAL A N   1 
ATOM 1360 C CA  . VAL A 1 189 ? 118.822 132.809 79.216  1.00 68.80  ? 172 VAL A CA  1 
ATOM 1361 C C   . VAL A 1 189 ? 118.094 131.640 79.860  1.00 68.80  ? 172 VAL A C   1 
ATOM 1362 O O   . VAL A 1 189 ? 116.895 131.768 80.151  1.00 68.80  ? 172 VAL A O   1 
ATOM 1363 C CB  . VAL A 1 189 ? 118.216 133.100 77.825  1.00 68.80  ? 172 VAL A CB  1 
ATOM 1364 C CG1 . VAL A 1 189 ? 119.088 134.081 77.059  1.00 68.80  ? 172 VAL A CG1 1 
ATOM 1365 C CG2 . VAL A 1 189 ? 118.042 131.808 77.041  1.00 68.80  ? 172 VAL A CG2 1 
ATOM 1366 N N   . LEU A 1 190 ? 118.758 130.514 80.094  1.00 61.63  ? 173 LEU A N   1 
ATOM 1367 C CA  . LEU A 1 190 ? 118.118 129.332 80.648  1.00 61.63  ? 173 LEU A CA  1 
ATOM 1368 C C   . LEU A 1 190 ? 118.504 129.151 82.110  1.00 61.63  ? 173 LEU A C   1 
ATOM 1369 O O   . LEU A 1 190 ? 119.610 129.506 82.528  1.00 61.63  ? 173 LEU A O   1 
ATOM 1370 C CB  . LEU A 1 190 ? 118.501 128.078 79.855  1.00 61.63  ? 173 LEU A CB  1 
ATOM 1371 C CG  . LEU A 1 190 ? 118.206 128.108 78.355  1.00 61.63  ? 173 LEU A CG  1 
ATOM 1372 C CD1 . LEU A 1 190 ? 119.088 127.118 77.614  1.00 61.63  ? 173 LEU A CD1 1 
ATOM 1373 C CD2 . LEU A 1 190 ? 116.737 127.820 78.095  1.00 61.63  ? 173 LEU A CD2 1 
ATOM 1374 N N   . ASN A 1 191 ? 117.573 128.599 82.885  1.00 55.43  ? 174 ASN A N   1 
ATOM 1375 C CA  . ASN A 1 191 ? 117.815 128.236 84.280  1.00 55.43  ? 174 ASN A CA  1 
ATOM 1376 C C   . ASN A 1 191 ? 118.015 126.725 84.314  1.00 55.43  ? 174 ASN A C   1 
ATOM 1377 O O   . ASN A 1 191 ? 117.071 125.959 84.508  1.00 55.43  ? 174 ASN A O   1 
ATOM 1378 C CB  . ASN A 1 191 ? 116.662 128.679 85.172  1.00 55.43  ? 174 ASN A CB  1 
ATOM 1379 C CG  . ASN A 1 191 ? 116.442 130.176 85.139  1.00 55.43  ? 174 ASN A CG  1 
ATOM 1380 O OD1 . ASN A 1 191 ? 117.374 130.947 84.910  1.00 55.43  ? 174 ASN A OD1 1 
ATOM 1381 N ND2 . ASN A 1 191 ? 115.204 130.598 85.370  1.00 55.43  ? 174 ASN A ND2 1 
ATOM 1382 N N   . LEU A 1 192 ? 119.266 126.298 84.126  1.00 49.85  ? 175 LEU A N   1 
ATOM 1383 C CA  . LEU A 1 192 ? 119.554 124.874 83.976  1.00 49.85  ? 175 LEU A CA  1 
ATOM 1384 C C   . LEU A 1 192 ? 119.232 124.089 85.240  1.00 49.85  ? 175 LEU A C   1 
ATOM 1385 O O   . LEU A 1 192 ? 118.954 122.886 85.168  1.00 49.85  ? 175 LEU A O   1 
ATOM 1386 C CB  . LEU A 1 192 ? 121.020 124.676 83.593  1.00 49.85  ? 175 LEU A CB  1 
ATOM 1387 C CG  . LEU A 1 192 ? 121.524 125.471 82.388  1.00 49.85  ? 175 LEU A CG  1 
ATOM 1388 C CD1 . LEU A 1 192 ? 123.040 125.415 82.307  1.00 49.85  ? 175 LEU A CD1 1 
ATOM 1389 C CD2 . LEU A 1 192 ? 120.900 124.952 81.107  1.00 49.85  ? 175 LEU A CD2 1 
ATOM 1390 N N   . THR A 1 193 ? 119.259 124.741 86.401  1.00 49.85  ? 176 THR A N   1 
ATOM 1391 C CA  . THR A 1 193 ? 119.052 124.044 87.663  1.00 49.85  ? 176 THR A CA  1 
ATOM 1392 C C   . THR A 1 193 ? 117.584 123.800 87.986  1.00 49.85  ? 176 THR A C   1 
ATOM 1393 O O   . THR A 1 193 ? 117.294 123.027 88.905  1.00 49.85  ? 176 THR A O   1 
ATOM 1394 C CB  . THR A 1 193 ? 119.695 124.830 88.808  1.00 49.85  ? 176 THR A CB  1 
ATOM 1395 O OG1 . THR A 1 193 ? 118.777 125.821 89.284  1.00 49.85  ? 176 THR A OG1 1 
ATOM 1396 C CG2 . THR A 1 193 ? 120.967 125.514 88.333  1.00 49.85  ? 176 THR A CG2 1 
ATOM 1397 N N   . ARG A 1 194 ? 116.654 124.427 87.263  1.00 49.85  ? 177 ARG A N   1 
ATOM 1398 C CA  . ARG A 1 194 ? 115.242 124.290 87.588  1.00 49.85  ? 177 ARG A CA  1 
ATOM 1399 C C   . ARG A 1 194 ? 114.328 124.150 86.378  1.00 49.85  ? 177 ARG A C   1 
ATOM 1400 O O   . ARG A 1 194 ? 113.109 124.074 86.562  1.00 49.85  ? 177 ARG A O   1 
ATOM 1401 C CB  . ARG A 1 194 ? 114.781 125.487 88.434  1.00 49.85  ? 177 ARG A CB  1 
ATOM 1402 C CG  . ARG A 1 194 ? 114.730 126.797 87.674  1.00 49.85  ? 177 ARG A CG  1 
ATOM 1403 C CD  . ARG A 1 194 ? 114.668 127.976 88.626  1.00 49.85  ? 177 ARG A CD  1 
ATOM 1404 N NE  . ARG A 1 194 ? 115.840 128.031 89.491  1.00 49.85  ? 177 ARG A NE  1 
ATOM 1405 C CZ  . ARG A 1 194 ? 116.765 128.980 89.439  1.00 49.85  ? 177 ARG A CZ  1 
ATOM 1406 N NH1 . ARG A 1 194 ? 116.679 129.982 88.579  1.00 49.85  ? 177 ARG A NH1 1 
ATOM 1407 N NH2 . ARG A 1 194 ? 117.802 128.922 90.269  1.00 49.85  ? 177 ARG A NH2 1 
ATOM 1408 N N   . ASN A 1 195 ? 114.860 124.110 85.159  1.00 49.85  ? 178 ASN A N   1 
ATOM 1409 C CA  . ASN A 1 195 ? 114.050 123.913 83.966  1.00 49.85  ? 178 ASN A CA  1 
ATOM 1410 C C   . ASN A 1 195 ? 114.139 122.492 83.428  1.00 49.85  ? 178 ASN A C   1 
ATOM 1411 O O   . ASN A 1 195 ? 113.635 122.220 82.334  1.00 49.85  ? 178 ASN A O   1 
ATOM 1412 C CB  . ASN A 1 195 ? 114.449 124.913 82.878  1.00 49.85  ? 178 ASN A CB  1 
ATOM 1413 C CG  . ASN A 1 195 ? 115.698 124.496 82.127  1.00 49.85  ? 178 ASN A CG  1 
ATOM 1414 O OD1 . ASN A 1 195 ? 116.600 123.877 82.691  1.00 49.85  ? 178 ASN A OD1 1 
ATOM 1415 N ND2 . ASN A 1 195 ? 115.755 124.831 80.843  1.00 49.85  ? 178 ASN A ND2 1 
ATOM 1416 N N   . GLY A 1 196 ? 114.768 121.583 84.168  1.00 49.85  ? 179 GLY A N   1 
ATOM 1417 C CA  . GLY A 1 196 ? 114.920 120.212 83.737  1.00 49.85  ? 179 GLY A CA  1 
ATOM 1418 C C   . GLY A 1 196 ? 116.146 119.928 82.899  1.00 49.85  ? 179 GLY A C   1 
ATOM 1419 O O   . GLY A 1 196 ? 116.380 118.764 82.552  1.00 49.85  ? 179 GLY A O   1 
ATOM 1420 N N   . TYR A 1 197 ? 116.938 120.947 82.560  1.00 49.85  ? 180 TYR A N   1 
ATOM 1421 C CA  . TYR A 1 197 ? 118.147 120.710 81.778  1.00 49.85  ? 180 TYR A CA  1 
ATOM 1422 C C   . TYR A 1 197 ? 119.235 120.071 82.633  1.00 49.85  ? 180 TYR A C   1 
ATOM 1423 O O   . TYR A 1 197 ? 119.790 119.027 82.273  1.00 49.85  ? 180 TYR A O   1 
ATOM 1424 C CB  . TYR A 1 197 ? 118.646 122.019 81.164  1.00 49.85  ? 180 TYR A CB  1 
ATOM 1425 C CG  . TYR A 1 197 ? 118.016 122.369 79.834  1.00 49.85  ? 180 TYR A CG  1 
ATOM 1426 C CD1 . TYR A 1 197 ? 116.815 121.800 79.437  1.00 49.85  ? 180 TYR A CD1 1 
ATOM 1427 C CD2 . TYR A 1 197 ? 118.625 123.273 78.974  1.00 49.85  ? 180 TYR A CD2 1 
ATOM 1428 C CE1 . TYR A 1 197 ? 116.240 122.121 78.222  1.00 49.85  ? 180 TYR A CE1 1 
ATOM 1429 C CE2 . TYR A 1 197 ? 118.057 123.600 77.759  1.00 49.85  ? 180 TYR A CE2 1 
ATOM 1430 C CZ  . TYR A 1 197 ? 116.864 123.020 77.388  1.00 49.85  ? 180 TYR A CZ  1 
ATOM 1431 O OH  . TYR A 1 197 ? 116.292 123.339 76.178  1.00 49.85  ? 180 TYR A OH  1 
ATOM 1432 N N   . GLY A 1 198 ? 119.551 120.680 83.764  1.00 49.85  ? 181 GLY A N   1 
ATOM 1433 C CA  . GLY A 1 198 ? 120.582 120.137 84.634  1.00 49.85  ? 181 GLY A CA  1 
ATOM 1434 C C   . GLY A 1 198 ? 121.971 120.595 84.241  1.00 49.85  ? 181 GLY A C   1 
ATOM 1435 O O   . GLY A 1 198 ? 122.252 120.928 83.091  1.00 49.85  ? 181 GLY A O   1 
ATOM 1436 N N   . SER A 1 199 ? 122.861 120.612 85.230  1.00 49.85  ? 182 SER A N   1 
ATOM 1437 C CA  . SER A 1 199 ? 124.244 121.006 85.011  1.00 49.85  ? 182 SER A CA  1 
ATOM 1438 C C   . SER A 1 199 ? 125.123 120.307 86.036  1.00 49.85  ? 182 SER A C   1 
ATOM 1439 O O   . SER A 1 199 ? 124.652 119.862 87.085  1.00 49.85  ? 182 SER A O   1 
ATOM 1440 C CB  . SER A 1 199 ? 124.420 122.526 85.102  1.00 49.85  ? 182 SER A CB  1 
ATOM 1441 O OG  . SER A 1 199 ? 123.941 123.019 86.341  1.00 49.85  ? 182 SER A OG  1 
ATOM 1442 N N   . THR A 1 200 ? 126.412 120.212 85.717  1.00 49.85  ? 183 THR A N   1 
ATOM 1443 C CA  . THR A 1 200 ? 127.364 119.622 86.647  1.00 49.85  ? 183 THR A CA  1 
ATOM 1444 C C   . THR A 1 200 ? 127.462 120.472 87.906  1.00 49.85  ? 183 THR A C   1 
ATOM 1445 O O   . THR A 1 200 ? 127.442 121.704 87.847  1.00 49.85  ? 183 THR A O   1 
ATOM 1446 C CB  . THR A 1 200 ? 128.738 119.494 85.994  1.00 49.85  ? 183 THR A CB  1 
ATOM 1447 O OG1 . THR A 1 200 ? 129.487 120.695 86.214  1.00 49.85  ? 183 THR A OG1 1 
ATOM 1448 C CG2 . THR A 1 200 ? 128.589 119.269 84.504  1.00 49.85  ? 183 THR A CG2 1 
ATOM 1449 N N   . GLN A 1 201 ? 127.568 119.808 89.052  1.00 49.85  ? 184 GLN A N   1 
ATOM 1450 C CA  . GLN A 1 201 ? 127.593 120.478 90.343  1.00 49.85  ? 184 GLN A CA  1 
ATOM 1451 C C   . GLN A 1 201 ? 128.980 120.369 90.956  1.00 49.85  ? 184 GLN A C   1 
ATOM 1452 O O   . GLN A 1 201 ? 129.533 119.269 91.065  1.00 49.85  ? 184 GLN A O   1 
ATOM 1453 C CB  . GLN A 1 201 ? 126.548 119.884 91.288  1.00 49.85  ? 184 GLN A CB  1 
ATOM 1454 C CG  . GLN A 1 201 ? 125.119 120.148 90.861  1.00 49.85  ? 184 GLN A CG  1 
ATOM 1455 C CD  . GLN A 1 201 ? 124.842 121.622 90.651  1.00 49.85  ? 184 GLN A CD  1 
ATOM 1456 O OE1 . GLN A 1 201 ? 125.158 122.451 91.502  1.00 49.85  ? 184 GLN A OE1 1 
ATOM 1457 N NE2 . GLN A 1 201 ? 124.249 121.955 89.511  1.00 49.85  ? 184 GLN A NE2 1 
ATOM 1458 N N   . TYR A 1 202 ? 129.535 121.509 91.353  1.00 49.85  ? 185 TYR A N   1 
ATOM 1459 C CA  . TYR A 1 202 ? 130.820 121.576 92.034  1.00 49.85  ? 185 TYR A CA  1 
ATOM 1460 C C   . TYR A 1 202 ? 130.535 121.651 93.529  1.00 49.85  ? 185 TYR A C   1 
ATOM 1461 O O   . TYR A 1 202 ? 129.987 122.648 94.012  1.00 49.85  ? 185 TYR A O   1 
ATOM 1462 C CB  . TYR A 1 202 ? 131.626 122.784 91.559  1.00 49.85  ? 185 TYR A CB  1 
ATOM 1463 C CG  . TYR A 1 202 ? 132.012 122.747 90.094  1.00 49.85  ? 185 TYR A CG  1 
ATOM 1464 C CD1 . TYR A 1 202 ? 131.054 122.870 89.095  1.00 49.85  ? 185 TYR A CD1 1 
ATOM 1465 C CD2 . TYR A 1 202 ? 133.336 122.599 89.710  1.00 49.85  ? 185 TYR A CD2 1 
ATOM 1466 C CE1 . TYR A 1 202 ? 131.403 122.838 87.760  1.00 49.85  ? 185 TYR A CE1 1 
ATOM 1467 C CE2 . TYR A 1 202 ? 133.695 122.565 88.376  1.00 49.85  ? 185 TYR A CE2 1 
ATOM 1468 C CZ  . TYR A 1 202 ? 132.724 122.686 87.406  1.00 49.85  ? 185 TYR A CZ  1 
ATOM 1469 O OH  . TYR A 1 202 ? 133.075 122.654 86.077  1.00 49.85  ? 185 TYR A OH  1 
ATOM 1470 N N   . ILE A 1 203 ? 130.883 120.594 94.254  1.00 49.85  ? 186 ILE A N   1 
ATOM 1471 C CA  . ILE A 1 203 ? 130.589 120.487 95.678  1.00 49.85  ? 186 ILE A CA  1 
ATOM 1472 C C   . ILE A 1 203 ? 131.814 120.927 96.465  1.00 49.85  ? 186 ILE A C   1 
ATOM 1473 O O   . ILE A 1 203 ? 132.899 120.353 96.315  1.00 49.85  ? 186 ILE A O   1 
ATOM 1474 C CB  . ILE A 1 203 ? 130.176 119.058 96.061  1.00 49.85  ? 186 ILE A CB  1 
ATOM 1475 C CG1 . ILE A 1 203 ? 129.063 118.555 95.143  1.00 49.85  ? 186 ILE A CG1 1 
ATOM 1476 C CG2 . ILE A 1 203 ? 129.743 119.005 97.515  1.00 49.85  ? 186 ILE A CG2 1 
ATOM 1477 C CD1 . ILE A 1 203 ? 128.839 117.065 95.228  1.00 49.85  ? 186 ILE A CD1 1 
ATOM 1478 N N   . ARG A 1 204 ? 131.641 121.942 97.305  1.00 50.83  ? 187 ARG A N   1 
ATOM 1479 C CA  . ARG A 1 204 ? 132.686 122.367 98.232  1.00 50.83  ? 187 ARG A CA  1 
ATOM 1480 C C   . ARG A 1 204 ? 132.590 121.485 99.469  1.00 50.83  ? 187 ARG A C   1 
ATOM 1481 O O   . ARG A 1 204 ? 131.767 121.726 100.355 1.00 50.83  ? 187 ARG A O   1 
ATOM 1482 C CB  . ARG A 1 204 ? 132.528 123.841 98.581  1.00 50.83  ? 187 ARG A CB  1 
ATOM 1483 C CG  . ARG A 1 204 ? 132.811 124.792 97.432  1.00 50.83  ? 187 ARG A CG  1 
ATOM 1484 C CD  . ARG A 1 204 ? 132.409 126.212 97.794  1.00 50.83  ? 187 ARG A CD  1 
ATOM 1485 N NE  . ARG A 1 204 ? 132.936 127.193 96.852  1.00 50.83  ? 187 ARG A NE  1 
ATOM 1486 C CZ  . ARG A 1 204 ? 132.589 128.473 96.833  1.00 50.83  ? 187 ARG A CZ  1 
ATOM 1487 N NH1 . ARG A 1 204 ? 131.707 128.963 97.689  1.00 50.83  ? 187 ARG A NH1 1 
ATOM 1488 N NH2 . ARG A 1 204 ? 133.140 129.281 95.932  1.00 50.83  ? 187 ARG A NH2 1 
ATOM 1489 N N   . PHE A 1 205 ? 133.429 120.455 99.536  1.00 49.85  ? 188 PHE A N   1 
ATOM 1490 C CA  . PHE A 1 205 ? 133.365 119.460 100.596 1.00 49.85  ? 188 PHE A CA  1 
ATOM 1491 C C   . PHE A 1 205 ? 134.709 119.355 101.302 1.00 49.85  ? 188 PHE A C   1 
ATOM 1492 O O   . PHE A 1 205 ? 135.765 119.472 100.672 1.00 49.85  ? 188 PHE A O   1 
ATOM 1493 C CB  . PHE A 1 205 ? 132.961 118.091 100.040 1.00 49.85  ? 188 PHE A CB  1 
ATOM 1494 C CG  . PHE A 1 205 ? 132.900 117.010 101.077 1.00 49.85  ? 188 PHE A CG  1 
ATOM 1495 C CD1 . PHE A 1 205 ? 131.980 117.075 102.110 1.00 49.85  ? 188 PHE A CD1 1 
ATOM 1496 C CD2 . PHE A 1 205 ? 133.760 115.928 101.020 1.00 49.85  ? 188 PHE A CD2 1 
ATOM 1497 C CE1 . PHE A 1 205 ? 131.921 116.080 103.066 1.00 49.85  ? 188 PHE A CE1 1 
ATOM 1498 C CE2 . PHE A 1 205 ? 133.706 114.930 101.973 1.00 49.85  ? 188 PHE A CE2 1 
ATOM 1499 C CZ  . PHE A 1 205 ? 132.785 115.007 102.997 1.00 49.85  ? 188 PHE A CZ  1 
ATOM 1500 N N   . SER A 1 206 ? 134.662 119.132 102.615 1.00 49.85  ? 189 SER A N   1 
ATOM 1501 C CA  . SER A 1 206 ? 135.860 118.971 103.429 1.00 49.85  ? 189 SER A CA  1 
ATOM 1502 C C   . SER A 1 206 ? 135.651 117.849 104.439 1.00 49.85  ? 189 SER A C   1 
ATOM 1503 O O   . SER A 1 206 ? 134.825 117.981 105.351 1.00 49.85  ? 189 SER A O   1 
ATOM 1504 C CB  . SER A 1 206 ? 136.207 120.277 104.143 1.00 49.85  ? 189 SER A CB  1 
ATOM 1505 O OG  . SER A 1 206 ? 137.263 120.086 105.066 1.00 49.85  ? 189 SER A OG  1 
ATOM 1506 N N   . PRO A 1 207 ? 136.376 116.733 104.315 1.00 49.85  ? 190 PRO A N   1 
ATOM 1507 C CA  . PRO A 1 207 ? 136.153 115.602 105.225 1.00 49.85  ? 190 PRO A CA  1 
ATOM 1508 C C   . PRO A 1 207 ? 136.891 115.706 106.549 1.00 49.85  ? 190 PRO A C   1 
ATOM 1509 O O   . PRO A 1 207 ? 136.541 114.976 107.486 1.00 49.85  ? 190 PRO A O   1 
ATOM 1510 C CB  . PRO A 1 207 ? 136.662 114.410 104.411 1.00 49.85  ? 190 PRO A CB  1 
ATOM 1511 C CG  . PRO A 1 207 ? 137.772 114.988 103.598 1.00 49.85  ? 190 PRO A CG  1 
ATOM 1512 C CD  . PRO A 1 207 ? 137.395 116.425 103.297 1.00 49.85  ? 190 PRO A CD  1 
ATOM 1513 N N   . ASP A 1 208 ? 137.882 116.584 106.666 1.00 53.64  ? 191 ASP A N   1 
ATOM 1514 C CA  . ASP A 1 208 ? 138.691 116.679 107.874 1.00 53.64  ? 191 ASP A CA  1 
ATOM 1515 C C   . ASP A 1 208 ? 138.055 117.545 108.954 1.00 53.64  ? 191 ASP A C   1 
ATOM 1516 O O   . ASP A 1 208 ? 138.643 117.697 110.029 1.00 53.64  ? 191 ASP A O   1 
ATOM 1517 C CB  . ASP A 1 208 ? 140.083 117.222 107.535 1.00 53.64  ? 191 ASP A CB  1 
ATOM 1518 C CG  . ASP A 1 208 ? 140.853 116.309 106.602 1.00 53.64  ? 191 ASP A CG  1 
ATOM 1519 O OD1 . ASP A 1 208 ? 140.822 115.079 106.814 1.00 53.64  ? 191 ASP A OD1 1 
ATOM 1520 O OD2 . ASP A 1 208 ? 141.490 116.820 105.658 1.00 53.64  ? 191 ASP A OD2 1 
ATOM 1521 N N   . PHE A 1 209 ? 136.878 118.112 108.700 1.00 49.85  ? 192 PHE A N   1 
ATOM 1522 C CA  . PHE A 1 209 ? 136.191 118.956 109.665 1.00 49.85  ? 192 PHE A CA  1 
ATOM 1523 C C   . PHE A 1 209 ? 134.753 118.484 109.815 1.00 49.85  ? 192 PHE A C   1 
ATOM 1524 O O   . PHE A 1 209 ? 134.169 117.920 108.885 1.00 49.85  ? 192 PHE A O   1 
ATOM 1525 C CB  . PHE A 1 209 ? 136.214 120.436 109.250 1.00 49.85  ? 192 PHE A CB  1 
ATOM 1526 C CG  . PHE A 1 209 ? 137.596 120.998 109.063 1.00 49.85  ? 192 PHE A CG  1 
ATOM 1527 C CD1 . PHE A 1 209 ? 138.348 120.681 107.944 1.00 49.85  ? 192 PHE A CD1 1 
ATOM 1528 C CD2 . PHE A 1 209 ? 138.145 121.841 110.012 1.00 49.85  ? 192 PHE A CD2 1 
ATOM 1529 C CE1 . PHE A 1 209 ? 139.617 121.195 107.774 1.00 49.85  ? 192 PHE A CE1 1 
ATOM 1530 C CE2 . PHE A 1 209 ? 139.415 122.358 109.848 1.00 49.85  ? 192 PHE A CE2 1 
ATOM 1531 C CZ  . PHE A 1 209 ? 140.152 122.035 108.727 1.00 49.85  ? 192 PHE A CZ  1 
ATOM 1532 N N   . THR A 1 210 ? 134.183 118.720 110.995 1.00 49.85  ? 193 THR A N   1 
ATOM 1533 C CA  . THR A 1 210 ? 132.832 118.260 111.274 1.00 49.85  ? 193 THR A CA  1 
ATOM 1534 C C   . THR A 1 210 ? 132.133 119.246 112.199 1.00 49.85  ? 193 THR A C   1 
ATOM 1535 O O   . THR A 1 210 ? 132.767 120.081 112.852 1.00 49.85  ? 193 THR A O   1 
ATOM 1536 C CB  . THR A 1 210 ? 132.826 116.854 111.886 1.00 49.85  ? 193 THR A CB  1 
ATOM 1537 O OG1 . THR A 1 210 ? 131.516 116.287 111.768 1.00 49.85  ? 193 THR A OG1 1 
ATOM 1538 C CG2 . THR A 1 210 ? 133.213 116.907 113.352 1.00 49.85  ? 193 THR A CG2 1 
ATOM 1539 N N   . PHE A 1 211 ? 130.809 119.127 112.246 1.00 54.61  ? 194 PHE A N   1 
ATOM 1540 C CA  . PHE A 1 211 ? 129.942 120.057 112.957 1.00 54.61  ? 194 PHE A CA  1 
ATOM 1541 C C   . PHE A 1 211 ? 129.584 119.438 114.305 1.00 54.61  ? 194 PHE A C   1 
ATOM 1542 O O   . PHE A 1 211 ? 128.952 118.378 114.350 1.00 54.61  ? 194 PHE A O   1 
ATOM 1543 C CB  . PHE A 1 211 ? 128.676 120.318 112.138 1.00 54.61  ? 194 PHE A CB  1 
ATOM 1544 C CG  . PHE A 1 211 ? 128.865 121.292 111.000 1.00 54.61  ? 194 PHE A CG  1 
ATOM 1545 C CD1 . PHE A 1 211 ? 128.848 122.659 111.211 1.00 54.61  ? 194 PHE A CD1 1 
ATOM 1546 C CD2 . PHE A 1 211 ? 129.039 120.825 109.708 1.00 54.61  ? 194 PHE A CD2 1 
ATOM 1547 C CE1 . PHE A 1 211 ? 129.014 123.541 110.161 1.00 54.61  ? 194 PHE A CE1 1 
ATOM 1548 C CE2 . PHE A 1 211 ? 129.206 121.702 108.654 1.00 54.61  ? 194 PHE A CE2 1 
ATOM 1549 C CZ  . PHE A 1 211 ? 129.192 123.061 108.882 1.00 54.61  ? 194 PHE A CZ  1 
ATOM 1550 N N   . GLY A 1 212 ? 129.981 120.089 115.399 1.00 54.24  ? 195 GLY A N   1 
ATOM 1551 C CA  . GLY A 1 212 ? 129.740 119.547 116.723 1.00 54.24  ? 195 GLY A CA  1 
ATOM 1552 C C   . GLY A 1 212 ? 128.594 120.217 117.452 1.00 54.24  ? 195 GLY A C   1 
ATOM 1553 O O   . GLY A 1 212 ? 128.698 121.382 117.859 1.00 54.24  ? 195 GLY A O   1 
ATOM 1554 N N   . PHE A 1 213 ? 127.500 119.479 117.631 1.00 59.24  ? 196 PHE A N   1 
ATOM 1555 C CA  . PHE A 1 213 ? 126.239 119.994 118.146 1.00 59.24  ? 196 PHE A CA  1 
ATOM 1556 C C   . PHE A 1 213 ? 125.841 119.252 119.416 1.00 59.24  ? 196 PHE A C   1 
ATOM 1557 O O   . PHE A 1 213 ? 126.408 118.215 119.765 1.00 59.24  ? 196 PHE A O   1 
ATOM 1558 C CB  . PHE A 1 213 ? 125.127 119.856 117.100 1.00 59.24  ? 196 PHE A CB  1 
ATOM 1559 C CG  . PHE A 1 213 ? 124.701 118.435 116.859 1.00 59.24  ? 196 PHE A CG  1 
ATOM 1560 C CD1 . PHE A 1 213 ? 125.448 117.602 116.045 1.00 59.24  ? 196 PHE A CD1 1 
ATOM 1561 C CD2 . PHE A 1 213 ? 123.554 117.932 117.449 1.00 59.24  ? 196 PHE A CD2 1 
ATOM 1562 C CE1 . PHE A 1 213 ? 125.060 116.295 115.825 1.00 59.24  ? 196 PHE A CE1 1 
ATOM 1563 C CE2 . PHE A 1 213 ? 123.162 116.627 117.232 1.00 59.24  ? 196 PHE A CE2 1 
ATOM 1564 C CZ  . PHE A 1 213 ? 123.916 115.808 116.419 1.00 59.24  ? 196 PHE A CZ  1 
ATOM 1565 N N   . GLU A 1 214 ? 124.833 119.791 120.097 1.00 66.24  ? 197 GLU A N   1 
ATOM 1566 C CA  . GLU A 1 214 ? 124.291 119.205 121.313 1.00 66.24  ? 197 GLU A CA  1 
ATOM 1567 C C   . GLU A 1 214 ? 122.951 118.533 121.030 1.00 66.24  ? 197 GLU A C   1 
ATOM 1568 O O   . GLU A 1 214 ? 122.225 118.918 120.111 1.00 66.24  ? 197 GLU A O   1 
ATOM 1569 C CB  . GLU A 1 214 ? 124.120 120.273 122.397 1.00 66.24  ? 197 GLU A CB  1 
ATOM 1570 C CG  . GLU A 1 214 ? 123.943 119.724 123.804 1.00 66.24  ? 197 GLU A CG  1 
ATOM 1571 C CD  . GLU A 1 214 ? 122.898 120.483 124.599 1.00 66.24  ? 197 GLU A CD  1 
ATOM 1572 O OE1 . GLU A 1 214 ? 121.798 120.726 124.058 1.00 66.24  ? 197 GLU A OE1 1 
ATOM 1573 O OE2 . GLU A 1 214 ? 123.176 120.836 125.764 1.00 66.24  ? 197 GLU A OE2 1 
ATOM 1574 N N   . GLU A 1 215 ? 122.630 117.521 121.834 1.00 72.26  ? 198 GLU A N   1 
ATOM 1575 C CA  . GLU A 1 215 ? 121.372 116.800 121.694 1.00 72.26  ? 198 GLU A CA  1 
ATOM 1576 C C   . GLU A 1 215 ? 120.992 116.200 123.041 1.00 72.26  ? 198 GLU A C   1 
ATOM 1577 O O   . GLU A 1 215 ? 121.856 115.708 123.771 1.00 72.26  ? 198 GLU A O   1 
ATOM 1578 C CB  . GLU A 1 215 ? 121.474 115.702 120.628 1.00 72.26  ? 198 GLU A CB  1 
ATOM 1579 C CG  . GLU A 1 215 ? 120.271 114.773 120.570 1.00 72.26  ? 198 GLU A CG  1 
ATOM 1580 C CD  . GLU A 1 215 ? 120.148 114.057 119.241 1.00 72.26  ? 198 GLU A CD  1 
ATOM 1581 O OE1 . GLU A 1 215 ? 121.041 113.248 118.916 1.00 72.26  ? 198 GLU A OE1 1 
ATOM 1582 O OE2 . GLU A 1 215 ? 119.155 114.299 118.524 1.00 72.26  ? 198 GLU A OE2 1 
ATOM 1583 N N   . SER A 1 216 ? 119.696 116.246 123.360 1.00 87.39  ? 199 SER A N   1 
ATOM 1584 C CA  . SER A 1 216 ? 119.179 115.677 124.599 1.00 87.39  ? 199 SER A CA  1 
ATOM 1585 C C   . SER A 1 216 ? 117.921 114.843 124.382 1.00 87.39  ? 199 SER A C   1 
ATOM 1586 O O   . SER A 1 216 ? 117.235 114.515 125.357 1.00 87.39  ? 199 SER A O   1 
ATOM 1587 C CB  . SER A 1 216 ? 118.893 116.784 125.622 1.00 87.39  ? 199 SER A CB  1 
ATOM 1588 O OG  . SER A 1 216 ? 118.137 117.832 125.041 1.00 87.39  ? 199 SER A OG  1 
ATOM 1589 N N   . LEU A 1 217 ? 117.599 114.491 123.136 1.00 97.32  ? 200 LEU A N   1 
ATOM 1590 C CA  . LEU A 1 217 ? 116.383 113.745 122.838 1.00 97.32  ? 200 LEU A CA  1 
ATOM 1591 C C   . LEU A 1 217 ? 116.549 112.239 123.006 1.00 97.32  ? 200 LEU A C   1 
ATOM 1592 O O   . LEU A 1 217 ? 115.545 111.520 123.021 1.00 97.32  ? 200 LEU A O   1 
ATOM 1593 C CB  . LEU A 1 217 ? 115.921 114.063 121.411 1.00 97.32  ? 200 LEU A CB  1 
ATOM 1594 C CG  . LEU A 1 217 ? 114.495 113.693 120.993 1.00 97.32  ? 200 LEU A CG  1 
ATOM 1595 C CD1 . LEU A 1 217 ? 113.854 114.840 120.231 1.00 97.32  ? 200 LEU A CD1 1 
ATOM 1596 C CD2 . LEU A 1 217 ? 114.489 112.428 120.149 1.00 97.32  ? 200 LEU A CD2 1 
ATOM 1597 N N   . GLU A 1 218 ? 117.779 111.747 123.156 1.00 103.05 ? 201 GLU A N   1 
ATOM 1598 C CA  . GLU A 1 218 ? 118.044 110.319 123.262 1.00 103.05 ? 201 GLU A CA  1 
ATOM 1599 C C   . GLU A 1 218 ? 118.117 109.847 124.711 1.00 103.05 ? 201 GLU A C   1 
ATOM 1600 O O   . GLU A 1 218 ? 118.618 108.749 124.977 1.00 103.05 ? 201 GLU A O   1 
ATOM 1601 C CB  . GLU A 1 218 ? 119.336 109.971 122.520 1.00 103.05 ? 201 GLU A CB  1 
ATOM 1602 C CG  . GLU A 1 218 ? 119.375 108.559 121.952 1.00 103.05 ? 201 GLU A CG  1 
ATOM 1603 C CD  . GLU A 1 218 ? 118.799 108.473 120.553 1.00 103.05 ? 201 GLU A CD  1 
ATOM 1604 O OE1 . GLU A 1 218 ? 118.202 109.467 120.089 1.00 103.05 ? 201 GLU A OE1 1 
ATOM 1605 O OE2 . GLU A 1 218 ? 118.941 107.408 119.916 1.00 103.05 ? 201 GLU A OE2 1 
ATOM 1606 N N   . VAL A 1 219 ? 117.629 110.656 125.654 1.00 102.74 ? 202 VAL A N   1 
ATOM 1607 C CA  . VAL A 1 219 ? 117.684 110.274 127.061 1.00 102.74 ? 202 VAL A CA  1 
ATOM 1608 C C   . VAL A 1 219 ? 116.764 109.090 127.339 1.00 102.74 ? 202 VAL A C   1 
ATOM 1609 O O   . VAL A 1 219 ? 117.091 108.210 128.144 1.00 102.74 ? 202 VAL A O   1 
ATOM 1610 C CB  . VAL A 1 219 ? 117.345 111.481 127.955 1.00 102.74 ? 202 VAL A CB  1 
ATOM 1611 C CG1 . VAL A 1 219 ? 118.513 112.453 127.997 1.00 102.74 ? 202 VAL A CG1 1 
ATOM 1612 C CG2 . VAL A 1 219 ? 116.088 112.178 127.460 1.00 102.74 ? 202 VAL A CG2 1 
ATOM 1613 N N   . ASP A 1 220 ? 115.598 109.052 126.687 1.00 111.15 ? 203 ASP A N   1 
ATOM 1614 C CA  . ASP A 1 220 ? 114.642 107.978 126.944 1.00 111.15 ? 203 ASP A CA  1 
ATOM 1615 C C   . ASP A 1 220 ? 115.192 106.624 126.510 1.00 111.15 ? 203 ASP A C   1 
ATOM 1616 O O   . ASP A 1 220 ? 115.052 105.630 127.232 1.00 111.15 ? 203 ASP A O   1 
ATOM 1617 C CB  . ASP A 1 220 ? 113.319 108.272 126.236 1.00 111.15 ? 203 ASP A CB  1 
ATOM 1618 C CG  . ASP A 1 220 ? 113.499 108.559 124.759 1.00 111.15 ? 203 ASP A CG  1 
ATOM 1619 O OD1 . ASP A 1 220 ? 114.398 109.352 124.412 1.00 111.15 ? 203 ASP A OD1 1 
ATOM 1620 O OD2 . ASP A 1 220 ? 112.742 107.990 123.944 1.00 111.15 ? 203 ASP A OD2 1 
ATOM 1621 N N   . THR A 1 221 ? 115.822 106.564 125.335 1.00 112.63 ? 204 THR A N   1 
ATOM 1622 C CA  . THR A 1 221 ? 116.373 105.303 124.854 1.00 112.63 ? 204 THR A CA  1 
ATOM 1623 C C   . THR A 1 221 ? 117.743 105.011 125.452 1.00 112.63 ? 204 THR A C   1 
ATOM 1624 O O   . THR A 1 221 ? 118.136 103.843 125.548 1.00 112.63 ? 204 THR A O   1 
ATOM 1625 C CB  . THR A 1 221 ? 116.464 105.312 123.327 1.00 112.63 ? 204 THR A CB  1 
ATOM 1626 O OG1 . THR A 1 221 ? 116.917 106.597 122.881 1.00 112.63 ? 204 THR A OG1 1 
ATOM 1627 C CG2 . THR A 1 221 ? 115.104 105.018 122.711 1.00 112.63 ? 204 THR A CG2 1 
ATOM 1628 N N   . ASN A 1 222 ? 118.478 106.046 125.854 1.00 107.32 ? 205 ASN A N   1 
ATOM 1629 C CA  . ASN A 1 222 ? 119.805 105.898 126.448 1.00 107.32 ? 205 ASN A CA  1 
ATOM 1630 C C   . ASN A 1 222 ? 119.844 106.687 127.749 1.00 107.32 ? 205 ASN A C   1 
ATOM 1631 O O   . ASN A 1 222 ? 120.259 107.855 127.768 1.00 107.32 ? 205 ASN A O   1 
ATOM 1632 C CB  . ASN A 1 222 ? 120.897 106.360 125.485 1.00 107.32 ? 205 ASN A CB  1 
ATOM 1633 C CG  . ASN A 1 222 ? 121.012 105.469 124.265 1.00 107.32 ? 205 ASN A CG  1 
ATOM 1634 O OD1 . ASN A 1 222 ? 120.436 105.755 123.216 1.00 107.32 ? 205 ASN A OD1 1 
ATOM 1635 N ND2 . ASN A 1 222 ? 121.758 104.378 124.398 1.00 107.32 ? 205 ASN A ND2 1 
ATOM 1636 N N   . PRO A 1 223 ? 119.405 106.086 128.857 1.00 106.36 ? 206 PRO A N   1 
ATOM 1637 C CA  . PRO A 1 223 ? 119.465 106.796 130.145 1.00 106.36 ? 206 PRO A CA  1 
ATOM 1638 C C   . PRO A 1 223 ? 120.875 107.182 130.556 1.00 106.36 ? 206 PRO A C   1 
ATOM 1639 O O   . PRO A 1 223 ? 121.049 108.148 131.309 1.00 106.36 ? 206 PRO A O   1 
ATOM 1640 C CB  . PRO A 1 223 ? 118.845 105.793 131.129 1.00 106.36 ? 206 PRO A CB  1 
ATOM 1641 C CG  . PRO A 1 223 ? 118.022 104.877 130.278 1.00 106.36 ? 206 PRO A CG  1 
ATOM 1642 C CD  . PRO A 1 223 ? 118.755 104.770 128.976 1.00 106.36 ? 206 PRO A CD  1 
ATOM 1643 N N   . LEU A 1 224 ? 121.889 106.456 130.084 1.00 106.10 ? 207 LEU A N   1 
ATOM 1644 C CA  . LEU A 1 224 ? 123.283 106.757 130.383 1.00 106.10 ? 207 LEU A CA  1 
ATOM 1645 C C   . LEU A 1 224 ? 123.940 107.595 129.291 1.00 106.10 ? 207 LEU A C   1 
ATOM 1646 O O   . LEU A 1 224 ? 125.151 107.487 129.070 1.00 106.10 ? 207 LEU A O   1 
ATOM 1647 C CB  . LEU A 1 224 ? 124.069 105.465 130.605 1.00 106.10 ? 207 LEU A CB  1 
ATOM 1648 C CG  . LEU A 1 224 ? 124.368 105.076 132.054 1.00 106.10 ? 207 LEU A CG  1 
ATOM 1649 C CD1 . LEU A 1 224 ? 125.539 105.885 132.593 1.00 106.10 ? 207 LEU A CD1 1 
ATOM 1650 C CD2 . LEU A 1 224 ? 123.140 105.253 132.935 1.00 106.10 ? 207 LEU A CD2 1 
ATOM 1651 N N   . LEU A 1 225 ? 123.160 108.421 128.596 1.00 107.60 ? 208 LEU A N   1 
ATOM 1652 C CA  . LEU A 1 225 ? 123.718 109.291 127.570 1.00 107.60 ? 208 LEU A CA  1 
ATOM 1653 C C   . LEU A 1 225 ? 124.687 110.289 128.191 1.00 107.60 ? 208 LEU A C   1 
ATOM 1654 O O   . LEU A 1 225 ? 124.387 110.912 129.213 1.00 107.60 ? 208 LEU A O   1 
ATOM 1655 C CB  . LEU A 1 225 ? 122.598 110.027 126.833 1.00 107.60 ? 208 LEU A CB  1 
ATOM 1656 C CG  . LEU A 1 225 ? 122.889 110.445 125.390 1.00 107.60 ? 208 LEU A CG  1 
ATOM 1657 C CD1 . LEU A 1 225 ? 122.989 109.228 124.484 1.00 107.60 ? 208 LEU A CD1 1 
ATOM 1658 C CD2 . LEU A 1 225 ? 121.826 111.408 124.885 1.00 107.60 ? 208 LEU A CD2 1 
ATOM 1659 N N   . GLY A 1 226 ? 125.853 110.436 127.569 1.00 111.80 ? 209 GLY A N   1 
ATOM 1660 C CA  . GLY A 1 226 ? 126.857 111.335 128.093 1.00 111.80 ? 209 GLY A CA  1 
ATOM 1661 C C   . GLY A 1 226 ? 126.490 112.793 127.904 1.00 111.80 ? 209 GLY A C   1 
ATOM 1662 O O   . GLY A 1 226 ? 125.642 113.159 127.090 1.00 111.80 ? 209 GLY A O   1 
ATOM 1663 N N   . ALA A 1 227 ? 127.151 113.642 128.685 1.00 103.30 ? 210 ALA A N   1 
ATOM 1664 C CA  . ALA A 1 227 ? 126.946 115.081 128.604 1.00 103.30 ? 210 ALA A CA  1 
ATOM 1665 C C   . ALA A 1 227 ? 127.764 115.643 127.442 1.00 103.30 ? 210 ALA A C   1 
ATOM 1666 O O   . ALA A 1 227 ? 128.316 114.905 126.621 1.00 103.30 ? 210 ALA A O   1 
ATOM 1667 C CB  . ALA A 1 227 ? 127.303 115.742 129.933 1.00 103.30 ? 210 ALA A CB  1 
ATOM 1668 N N   . GLY A 1 228 ? 127.851 116.966 127.361 1.00 86.33  ? 211 GLY A N   1 
ATOM 1669 C CA  . GLY A 1 228 ? 128.598 117.601 126.300 1.00 86.33  ? 211 GLY A CA  1 
ATOM 1670 C C   . GLY A 1 228 ? 127.860 117.580 124.974 1.00 86.33  ? 211 GLY A C   1 
ATOM 1671 O O   . GLY A 1 228 ? 126.663 117.291 124.884 1.00 86.33  ? 211 GLY A O   1 
ATOM 1672 N N   . LYS A 1 229 ? 128.608 117.896 123.922 1.00 74.88  ? 212 LYS A N   1 
ATOM 1673 C CA  . LYS A 1 229 ? 128.058 117.972 122.578 1.00 74.88  ? 212 LYS A CA  1 
ATOM 1674 C C   . LYS A 1 229 ? 128.204 116.620 121.879 1.00 74.88  ? 212 LYS A C   1 
ATOM 1675 O O   . LYS A 1 229 ? 128.619 115.624 122.478 1.00 74.88  ? 212 LYS A O   1 
ATOM 1676 C CB  . LYS A 1 229 ? 128.739 119.092 121.793 1.00 74.88  ? 212 LYS A CB  1 
ATOM 1677 C CG  . LYS A 1 229 ? 129.109 120.317 122.618 1.00 74.88  ? 212 LYS A CG  1 
ATOM 1678 C CD  . LYS A 1 229 ? 127.879 120.997 123.199 1.00 74.88  ? 212 LYS A CD  1 
ATOM 1679 C CE  . LYS A 1 229 ? 128.222 121.769 124.463 1.00 74.88  ? 212 LYS A CE  1 
ATOM 1680 N NZ  . LYS A 1 229 ? 128.390 120.872 125.639 1.00 74.88  ? 212 LYS A NZ  1 
ATOM 1681 N N   . PHE A 1 230 ? 127.855 116.577 120.596 1.00 59.42  ? 213 PHE A N   1 
ATOM 1682 C CA  . PHE A 1 230 ? 128.027 115.398 119.761 1.00 59.42  ? 213 PHE A CA  1 
ATOM 1683 C C   . PHE A 1 230 ? 128.630 115.820 118.430 1.00 59.42  ? 213 PHE A C   1 
ATOM 1684 O O   . PHE A 1 230 ? 128.466 116.962 117.993 1.00 59.42  ? 213 PHE A O   1 
ATOM 1685 C CB  . PHE A 1 230 ? 126.698 114.666 119.517 1.00 59.42  ? 213 PHE A CB  1 
ATOM 1686 C CG  . PHE A 1 230 ? 126.254 113.806 120.665 1.00 59.42  ? 213 PHE A CG  1 
ATOM 1687 C CD1 . PHE A 1 230 ? 125.775 114.375 121.832 1.00 59.42  ? 213 PHE A CD1 1 
ATOM 1688 C CD2 . PHE A 1 230 ? 126.313 112.426 120.574 1.00 59.42  ? 213 PHE A CD2 1 
ATOM 1689 C CE1 . PHE A 1 230 ? 125.366 113.584 122.888 1.00 59.42  ? 213 PHE A CE1 1 
ATOM 1690 C CE2 . PHE A 1 230 ? 125.907 111.630 121.625 1.00 59.42  ? 213 PHE A CE2 1 
ATOM 1691 C CZ  . PHE A 1 230 ? 125.431 112.210 122.784 1.00 59.42  ? 213 PHE A CZ  1 
ATOM 1692 N N   . ALA A 1 231 ? 129.325 114.889 117.784 1.00 52.45  ? 214 ALA A N   1 
ATOM 1693 C CA  . ALA A 1 231 ? 129.997 115.155 116.519 1.00 52.45  ? 214 ALA A CA  1 
ATOM 1694 C C   . ALA A 1 231 ? 129.194 114.562 115.370 1.00 52.45  ? 214 ALA A C   1 
ATOM 1695 O O   . ALA A 1 231 ? 128.870 113.370 115.382 1.00 52.45  ? 214 ALA A O   1 
ATOM 1696 C CB  . ALA A 1 231 ? 131.414 114.585 116.523 1.00 52.45  ? 214 ALA A CB  1 
ATOM 1697 N N   . THR A 1 232 ? 128.877 115.396 114.383 1.00 49.85  ? 215 THR A N   1 
ATOM 1698 C CA  . THR A 1 232 ? 128.139 114.934 113.216 1.00 49.85  ? 215 THR A CA  1 
ATOM 1699 C C   . THR A 1 232 ? 129.036 114.075 112.333 1.00 49.85  ? 215 THR A C   1 
ATOM 1700 O O   . THR A 1 232 ? 130.183 114.438 112.055 1.00 49.85  ? 215 THR A O   1 
ATOM 1701 C CB  . THR A 1 232 ? 127.603 116.124 112.420 1.00 49.85  ? 215 THR A CB  1 
ATOM 1702 O OG1 . THR A 1 232 ? 126.768 116.928 113.261 1.00 49.85  ? 215 THR A OG1 1 
ATOM 1703 C CG2 . THR A 1 232 ? 126.793 115.647 111.223 1.00 49.85  ? 215 THR A CG2 1 
ATOM 1704 N N   . ASP A 1 233 ? 128.515 112.937 111.900 1.00 49.85  ? 216 ASP A N   1 
ATOM 1705 C CA  . ASP A 1 233 ? 129.250 112.089 110.972 1.00 49.85  ? 216 ASP A CA  1 
ATOM 1706 C C   . ASP A 1 233 ? 129.407 112.816 109.641 1.00 49.85  ? 216 ASP A C   1 
ATOM 1707 O O   . ASP A 1 233 ? 128.411 113.286 109.079 1.00 49.85  ? 216 ASP A O   1 
ATOM 1708 C CB  . ASP A 1 233 ? 128.516 110.762 110.778 1.00 49.85  ? 216 ASP A CB  1 
ATOM 1709 C CG  . ASP A 1 233 ? 129.408 109.670 110.213 1.00 49.85  ? 216 ASP A CG  1 
ATOM 1710 O OD1 . ASP A 1 233 ? 130.249 109.966 109.340 1.00 49.85  ? 216 ASP A OD1 1 
ATOM 1711 O OD2 . ASP A 1 233 ? 129.263 108.507 110.644 1.00 49.85  ? 216 ASP A OD2 1 
ATOM 1712 N N   . PRO A 1 234 ? 130.627 112.941 109.111 1.00 49.85  ? 217 PRO A N   1 
ATOM 1713 C CA  . PRO A 1 234 ? 130.791 113.589 107.799 1.00 49.85  ? 217 PRO A CA  1 
ATOM 1714 C C   . PRO A 1 234 ? 130.086 112.857 106.673 1.00 49.85  ? 217 PRO A C   1 
ATOM 1715 O O   . PRO A 1 234 ? 129.830 113.463 105.625 1.00 49.85  ? 217 PRO A O   1 
ATOM 1716 C CB  . PRO A 1 234 ? 132.313 113.601 107.595 1.00 49.85  ? 217 PRO A CB  1 
ATOM 1717 C CG  . PRO A 1 234 ? 132.852 112.599 108.565 1.00 49.85  ? 217 PRO A CG  1 
ATOM 1718 C CD  . PRO A 1 234 ? 131.918 112.606 109.730 1.00 49.85  ? 217 PRO A CD  1 
ATOM 1719 N N   . ALA A 1 235 ? 129.769 111.572 106.854 1.00 49.85  ? 218 ALA A N   1 
ATOM 1720 C CA  . ALA A 1 235 ? 129.009 110.849 105.841 1.00 49.85  ? 218 ALA A CA  1 
ATOM 1721 C C   . ALA A 1 235 ? 127.641 111.480 105.629 1.00 49.85  ? 218 ALA A C   1 
ATOM 1722 O O   . ALA A 1 235 ? 127.165 111.577 104.494 1.00 49.85  ? 218 ALA A O   1 
ATOM 1723 C CB  . ALA A 1 235 ? 128.871 109.380 106.236 1.00 49.85  ? 218 ALA A CB  1 
ATOM 1724 N N   . VAL A 1 236 ? 126.997 111.926 106.710 1.00 49.85  ? 219 VAL A N   1 
ATOM 1725 C CA  . VAL A 1 236 ? 125.695 112.577 106.587 1.00 49.85  ? 219 VAL A CA  1 
ATOM 1726 C C   . VAL A 1 236 ? 125.818 113.884 105.813 1.00 49.85  ? 219 VAL A C   1 
ATOM 1727 O O   . VAL A 1 236 ? 124.979 114.199 104.961 1.00 49.85  ? 219 VAL A O   1 
ATOM 1728 C CB  . VAL A 1 236 ? 125.074 112.799 107.977 1.00 49.85  ? 219 VAL A CB  1 
ATOM 1729 C CG1 . VAL A 1 236 ? 123.833 113.664 107.867 1.00 49.85  ? 219 VAL A CG1 1 
ATOM 1730 C CG2 . VAL A 1 236 ? 124.744 111.467 108.628 1.00 49.85  ? 219 VAL A CG2 1 
ATOM 1731 N N   . THR A 1 237 ? 126.854 114.674 106.107 1.00 49.85  ? 220 THR A N   1 
ATOM 1732 C CA  . THR A 1 237 ? 127.048 115.933 105.393 1.00 49.85  ? 220 THR A CA  1 
ATOM 1733 C C   . THR A 1 237 ? 127.307 115.694 103.910 1.00 49.85  ? 220 THR A C   1 
ATOM 1734 O O   . THR A 1 237 ? 126.751 116.393 103.049 1.00 49.85  ? 220 THR A O   1 
ATOM 1735 C CB  . THR A 1 237 ? 128.202 116.715 106.021 1.00 49.85  ? 220 THR A CB  1 
ATOM 1736 O OG1 . THR A 1 237 ? 127.787 117.249 107.285 1.00 49.85  ? 220 THR A OG1 1 
ATOM 1737 C CG2 . THR A 1 237 ? 128.634 117.855 105.115 1.00 49.85  ? 220 THR A CG2 1 
ATOM 1738 N N   . LEU A 1 238 ? 128.147 114.707 103.591 1.00 49.85  ? 221 LEU A N   1 
ATOM 1739 C CA  . LEU A 1 238 ? 128.405 114.395 102.190 1.00 49.85  ? 221 LEU A CA  1 
ATOM 1740 C C   . LEU A 1 238 ? 127.144 113.885 101.506 1.00 49.85  ? 221 LEU A C   1 
ATOM 1741 O O   . LEU A 1 238 ? 126.904 114.188 100.334 1.00 49.85  ? 221 LEU A O   1 
ATOM 1742 C CB  . LEU A 1 238 ? 129.535 113.374 102.069 1.00 49.85  ? 221 LEU A CB  1 
ATOM 1743 C CG  . LEU A 1 238 ? 129.962 113.055 100.634 1.00 49.85  ? 221 LEU A CG  1 
ATOM 1744 C CD1 . LEU A 1 238 ? 130.260 114.331 99.864  1.00 49.85  ? 221 LEU A CD1 1 
ATOM 1745 C CD2 . LEU A 1 238 ? 131.160 112.124 100.616 1.00 49.85  ? 221 LEU A CD2 1 
ATOM 1746 N N   . ALA A 1 239 ? 126.319 113.120 102.225 1.00 49.85  ? 222 ALA A N   1 
ATOM 1747 C CA  . ALA A 1 239 ? 125.054 112.659 101.664 1.00 49.85  ? 222 ALA A CA  1 
ATOM 1748 C C   . ALA A 1 239 ? 124.109 113.823 101.397 1.00 49.85  ? 222 ALA A C   1 
ATOM 1749 O O   . ALA A 1 239 ? 123.391 113.827 100.394 1.00 49.85  ? 222 ALA A O   1 
ATOM 1750 C CB  . ALA A 1 239 ? 124.405 111.643 102.601 1.00 49.85  ? 222 ALA A CB  1 
ATOM 1751 N N   . HIS A 1 240 ? 124.085 114.813 102.290 1.00 49.85  ? 223 HIS A N   1 
ATOM 1752 C CA  . HIS A 1 240 ? 123.260 116.000 102.075 1.00 49.85  ? 223 HIS A CA  1 
ATOM 1753 C C   . HIS A 1 240 ? 123.710 116.761 100.833 1.00 49.85  ? 223 HIS A C   1 
ATOM 1754 O O   . HIS A 1 240 ? 122.893 117.129 99.975  1.00 49.85  ? 223 HIS A O   1 
ATOM 1755 C CB  . HIS A 1 240 ? 123.320 116.892 103.317 1.00 49.85  ? 223 HIS A CB  1 
ATOM 1756 C CG  . HIS A 1 240 ? 122.558 118.175 103.191 1.00 49.85  ? 223 HIS A CG  1 
ATOM 1757 N ND1 . HIS A 1 240 ? 121.395 118.419 103.889 1.00 49.85  ? 223 HIS A ND1 1 
ATOM 1758 C CD2 . HIS A 1 240 ? 122.808 119.296 102.475 1.00 49.85  ? 223 HIS A CD2 1 
ATOM 1759 C CE1 . HIS A 1 240 ? 120.952 119.628 103.595 1.00 49.85  ? 223 HIS A CE1 1 
ATOM 1760 N NE2 . HIS A 1 240 ? 121.792 120.181 102.738 1.00 49.85  ? 223 HIS A NE2 1 
ATOM 1761 N N   . GLN A 1 241 ? 125.018 117.002 100.719 1.00 49.85  ? 224 GLN A N   1 
ATOM 1762 C CA  . GLN A 1 241 ? 125.535 117.701 99.546  1.00 49.85  ? 224 GLN A CA  1 
ATOM 1763 C C   . GLN A 1 241 ? 125.287 116.898 98.276  1.00 49.85  ? 224 GLN A C   1 
ATOM 1764 O O   . GLN A 1 241 ? 124.997 117.465 97.217  1.00 49.85  ? 224 GLN A O   1 
ATOM 1765 C CB  . GLN A 1 241 ? 127.023 117.993 99.719  1.00 49.85  ? 224 GLN A CB  1 
ATOM 1766 C CG  . GLN A 1 241 ? 127.335 118.882 100.905 1.00 49.85  ? 224 GLN A CG  1 
ATOM 1767 C CD  . GLN A 1 241 ? 127.168 120.351 100.583 1.00 49.85  ? 224 GLN A CD  1 
ATOM 1768 O OE1 . GLN A 1 241 ? 127.840 120.886 99.702  1.00 49.85  ? 224 GLN A OE1 1 
ATOM 1769 N NE2 . GLN A 1 241 ? 126.266 121.014 101.296 1.00 49.85  ? 224 GLN A NE2 1 
ATOM 1770 N N   . LEU A 1 242 ? 125.382 115.571 98.367  1.00 49.85  ? 225 LEU A N   1 
ATOM 1771 C CA  . LEU A 1 242 ? 125.131 114.719 97.214  1.00 49.85  ? 225 LEU A CA  1 
ATOM 1772 C C   . LEU A 1 242 ? 123.659 114.725 96.825  1.00 49.85  ? 225 LEU A C   1 
ATOM 1773 O O   . LEU A 1 242 ? 123.337 114.654 95.637  1.00 49.85  ? 225 LEU A O   1 
ATOM 1774 C CB  . LEU A 1 242 ? 125.610 113.301 97.516  1.00 49.85  ? 225 LEU A CB  1 
ATOM 1775 C CG  . LEU A 1 242 ? 127.089 113.028 97.230  1.00 49.85  ? 225 LEU A CG  1 
ATOM 1776 C CD1 . LEU A 1 242 ? 127.414 111.546 97.338  1.00 49.85  ? 225 LEU A CD1 1 
ATOM 1777 C CD2 . LEU A 1 242 ? 127.474 113.562 95.867  1.00 49.85  ? 225 LEU A CD2 1 
ATOM 1778 N N   . ILE A 1 243 ? 122.755 114.810 97.803  1.00 49.85  ? 226 ILE A N   1 
ATOM 1779 C CA  . ILE A 1 243 ? 121.335 114.957 97.497  1.00 49.85  ? 226 ILE A CA  1 
ATOM 1780 C C   . ILE A 1 243 ? 121.091 116.267 96.762  1.00 49.85  ? 226 ILE A C   1 
ATOM 1781 O O   . ILE A 1 243 ? 120.344 116.315 95.776  1.00 49.85  ? 226 ILE A O   1 
ATOM 1782 C CB  . ILE A 1 243 ? 120.493 114.872 98.785  1.00 49.85  ? 226 ILE A CB  1 
ATOM 1783 C CG1 . ILE A 1 243 ? 120.380 113.427 99.265  1.00 49.85  ? 226 ILE A CG1 1 
ATOM 1784 C CG2 . ILE A 1 243 ? 119.105 115.443 98.554  1.00 49.85  ? 226 ILE A CG2 1 
ATOM 1785 C CD1 . ILE A 1 243 ? 119.954 113.299 100.708 1.00 49.85  ? 226 ILE A CD1 1 
ATOM 1786 N N   . HIS A 1 244 ? 121.718 117.349 97.231  1.00 49.85  ? 227 HIS A N   1 
ATOM 1787 C CA  . HIS A 1 244 ? 121.577 118.630 96.542  1.00 49.85  ? 227 HIS A CA  1 
ATOM 1788 C C   . HIS A 1 244 ? 122.103 118.548 95.113  1.00 49.85  ? 227 HIS A C   1 
ATOM 1789 O O   . HIS A 1 244 ? 121.468 119.050 94.174  1.00 49.85  ? 227 HIS A O   1 
ATOM 1790 C CB  . HIS A 1 244 ? 122.307 119.728 97.314  1.00 49.85  ? 227 HIS A CB  1 
ATOM 1791 C CG  . HIS A 1 244 ? 121.481 120.363 98.388  1.00 49.85  ? 227 HIS A CG  1 
ATOM 1792 N ND1 . HIS A 1 244 ? 120.132 120.604 98.246  1.00 49.85  ? 227 HIS A ND1 1 
ATOM 1793 C CD2 . HIS A 1 244 ? 121.816 120.815 99.619  1.00 49.85  ? 227 HIS A CD2 1 
ATOM 1794 C CE1 . HIS A 1 244 ? 119.670 121.172 99.345  1.00 49.85  ? 227 HIS A CE1 1 
ATOM 1795 N NE2 . HIS A 1 244 ? 120.672 121.311 100.194 1.00 49.85  ? 227 HIS A NE2 1 
ATOM 1796 N N   . ALA A 1 245 ? 123.264 117.915 94.931  1.00 49.85  ? 228 ALA A N   1 
ATOM 1797 C CA  . ALA A 1 245 ? 123.841 117.782 93.597  1.00 49.85  ? 228 ALA A CA  1 
ATOM 1798 C C   . ALA A 1 245 ? 122.958 116.931 92.693  1.00 49.85  ? 228 ALA A C   1 
ATOM 1799 O O   . ALA A 1 245 ? 122.798 117.236 91.507  1.00 49.85  ? 228 ALA A O   1 
ATOM 1800 C CB  . ALA A 1 245 ? 125.246 117.190 93.689  1.00 49.85  ? 228 ALA A CB  1 
ATOM 1801 N N   . GLY A 1 246 ? 122.384 115.855 93.231  1.00 49.85  ? 229 GLY A N   1 
ATOM 1802 C CA  . GLY A 1 246 ? 121.485 115.033 92.437  1.00 49.85  ? 229 GLY A CA  1 
ATOM 1803 C C   . GLY A 1 246 ? 120.219 115.769 92.049  1.00 49.85  ? 229 GLY A C   1 
ATOM 1804 O O   . GLY A 1 246 ? 119.705 115.596 90.940  1.00 49.85  ? 229 GLY A O   1 
ATOM 1805 N N   . HIS A 1 247 ? 119.692 116.594 92.957  1.00 49.85  ? 230 HIS A N   1 
ATOM 1806 C CA  . HIS A 1 247 ? 118.532 117.414 92.624  1.00 49.85  ? 230 HIS A CA  1 
ATOM 1807 C C   . HIS A 1 247 ? 118.860 118.387 91.501  1.00 49.85  ? 230 HIS A C   1 
ATOM 1808 O O   . HIS A 1 247 ? 118.104 118.512 90.531  1.00 49.85  ? 230 HIS A O   1 
ATOM 1809 C CB  . HIS A 1 247 ? 118.048 118.170 93.860  1.00 49.85  ? 230 HIS A CB  1 
ATOM 1810 C CG  . HIS A 1 247 ? 117.267 117.328 94.819  1.00 49.85  ? 230 HIS A CG  1 
ATOM 1811 N ND1 . HIS A 1 247 ? 116.972 117.740 96.100  1.00 49.85  ? 230 HIS A ND1 1 
ATOM 1812 C CD2 . HIS A 1 247 ? 116.721 116.097 94.684  1.00 49.85  ? 230 HIS A CD2 1 
ATOM 1813 C CE1 . HIS A 1 247 ? 116.277 116.800 96.714  1.00 49.85  ? 230 HIS A CE1 1 
ATOM 1814 N NE2 . HIS A 1 247 ? 116.112 115.792 95.876  1.00 49.85  ? 230 HIS A NE2 1 
ATOM 1815 N N   . ARG A 1 248 ? 119.990 119.086 91.614  1.00 51.78  ? 231 ARG A N   1 
ATOM 1816 C CA  . ARG A 1 248 ? 120.351 120.058 90.588  1.00 51.78  ? 231 ARG A CA  1 
ATOM 1817 C C   . ARG A 1 248 ? 120.762 119.400 89.275  1.00 51.78  ? 231 ARG A C   1 
ATOM 1818 O O   . ARG A 1 248 ? 120.695 120.049 88.227  1.00 51.78  ? 231 ARG A O   1 
ATOM 1819 C CB  . ARG A 1 248 ? 121.467 120.968 91.097  1.00 51.78  ? 231 ARG A CB  1 
ATOM 1820 C CG  . ARG A 1 248 ? 121.087 121.751 92.342  1.00 51.78  ? 231 ARG A CG  1 
ATOM 1821 C CD  . ARG A 1 248 ? 122.297 122.397 92.985  1.00 51.78  ? 231 ARG A CD  1 
ATOM 1822 N NE  . ARG A 1 248 ? 122.657 123.644 92.323  1.00 51.78  ? 231 ARG A NE  1 
ATOM 1823 C CZ  . ARG A 1 248 ? 122.243 124.842 92.709  1.00 51.78  ? 231 ARG A CZ  1 
ATOM 1824 N NH1 . ARG A 1 248 ? 121.448 124.994 93.755  1.00 51.78  ? 231 ARG A NH1 1 
ATOM 1825 N NH2 . ARG A 1 248 ? 122.634 125.915 92.027  1.00 51.78  ? 231 ARG A NH2 1 
ATOM 1826 N N   . LEU A 1 249 ? 121.185 118.135 89.307  1.00 49.85  ? 232 LEU A N   1 
ATOM 1827 C CA  . LEU A 1 249 ? 121.534 117.437 88.073  1.00 49.85  ? 232 LEU A CA  1 
ATOM 1828 C C   . LEU A 1 249 ? 120.295 117.123 87.244  1.00 49.85  ? 232 LEU A C   1 
ATOM 1829 O O   . LEU A 1 249 ? 120.337 117.172 86.010  1.00 49.85  ? 232 LEU A O   1 
ATOM 1830 C CB  . LEU A 1 249 ? 122.301 116.154 88.392  1.00 49.85  ? 232 LEU A CB  1 
ATOM 1831 C CG  . LEU A 1 249 ? 123.792 116.118 88.050  1.00 49.85  ? 232 LEU A CG  1 
ATOM 1832 C CD1 . LEU A 1 249 ? 124.562 117.139 88.863  1.00 49.85  ? 232 LEU A CD1 1 
ATOM 1833 C CD2 . LEU A 1 249 ? 124.353 114.725 88.275  1.00 49.85  ? 232 LEU A CD2 1 
ATOM 1834 N N   . TYR A 1 250 ? 119.187 116.795 87.902  1.00 49.85  ? 233 TYR A N   1 
ATOM 1835 C CA  . TYR A 1 250 ? 117.952 116.439 87.221  1.00 49.85  ? 233 TYR A CA  1 
ATOM 1836 C C   . TYR A 1 250 ? 117.090 117.648 86.887  1.00 49.85  ? 233 TYR A C   1 
ATOM 1837 O O   . TYR A 1 250 ? 116.012 117.481 86.307  1.00 49.85  ? 233 TYR A O   1 
ATOM 1838 C CB  . TYR A 1 250 ? 117.149 115.451 88.073  1.00 49.85  ? 233 TYR A CB  1 
ATOM 1839 C CG  . TYR A 1 250 ? 117.649 114.030 87.982  1.00 49.85  ? 233 TYR A CG  1 
ATOM 1840 C CD1 . TYR A 1 250 ? 118.712 113.598 88.762  1.00 49.85  ? 233 TYR A CD1 1 
ATOM 1841 C CD2 . TYR A 1 250 ? 117.062 113.120 87.117  1.00 49.85  ? 233 TYR A CD2 1 
ATOM 1842 C CE1 . TYR A 1 250 ? 119.175 112.300 88.683  1.00 49.85  ? 233 TYR A CE1 1 
ATOM 1843 C CE2 . TYR A 1 250 ? 117.518 111.819 87.032  1.00 49.85  ? 233 TYR A CE2 1 
ATOM 1844 C CZ  . TYR A 1 250 ? 118.575 111.415 87.816  1.00 49.85  ? 233 TYR A CZ  1 
ATOM 1845 O OH  . TYR A 1 250 ? 119.033 110.120 87.734  1.00 49.85  ? 233 TYR A OH  1 
ATOM 1846 N N   . GLY A 1 251 ? 117.536 118.851 87.233  1.00 49.85  ? 234 GLY A N   1 
ATOM 1847 C CA  . GLY A 1 251 ? 116.767 120.049 86.935  1.00 49.85  ? 234 GLY A CA  1 
ATOM 1848 C C   . GLY A 1 251 ? 115.421 120.101 87.622  1.00 49.85  ? 234 GLY A C   1 
ATOM 1849 O O   . GLY A 1 251 ? 114.424 120.488 87.000  1.00 49.85  ? 234 GLY A O   1 
ATOM 1850 N N   . ILE A 1 252 ? 115.367 119.714 88.896  1.00 49.85  ? 235 ILE A N   1 
ATOM 1851 C CA  . ILE A 1 252 ? 114.138 119.746 89.676  1.00 49.85  ? 235 ILE A CA  1 
ATOM 1852 C C   . ILE A 1 252 ? 114.285 120.584 90.939  1.00 49.85  ? 235 ILE A C   1 
ATOM 1853 O O   . ILE A 1 252 ? 113.430 120.519 91.823  1.00 49.85  ? 235 ILE A O   1 
ATOM 1854 C CB  . ILE A 1 252 ? 113.655 118.323 90.020  1.00 49.85  ? 235 ILE A CB  1 
ATOM 1855 C CG1 . ILE A 1 252 ? 114.613 117.654 91.006  1.00 49.85  ? 235 ILE A CG1 1 
ATOM 1856 C CG2 . ILE A 1 252 ? 113.514 117.486 88.760  1.00 49.85  ? 235 ILE A CG2 1 
ATOM 1857 C CD1 . ILE A 1 252 ? 114.045 116.414 91.654  1.00 49.85  ? 235 ILE A CD1 1 
ATOM 1858 N N   . ALA A 1 253 ? 115.350 121.373 91.042  1.00 49.85  ? 236 ALA A N   1 
ATOM 1859 C CA  . ALA A 1 253 ? 115.545 122.215 92.212  1.00 49.85  ? 236 ALA A CA  1 
ATOM 1860 C C   . ALA A 1 253 ? 114.515 123.338 92.246  1.00 49.85  ? 236 ALA A C   1 
ATOM 1861 O O   . ALA A 1 253 ? 114.033 123.804 91.211  1.00 49.85  ? 236 ALA A O   1 
ATOM 1862 C CB  . ALA A 1 253 ? 116.957 122.799 92.221  1.00 49.85  ? 236 ALA A CB  1 
ATOM 1863 N N   . ILE A 1 254 ? 114.178 123.770 93.456  1.00 50.34  ? 237 ILE A N   1 
ATOM 1864 C CA  . ILE A 1 254 ? 113.195 124.828 93.653  1.00 50.34  ? 237 ILE A CA  1 
ATOM 1865 C C   . ILE A 1 254 ? 113.861 126.178 93.425  1.00 50.34  ? 237 ILE A C   1 
ATOM 1866 O O   . ILE A 1 254 ? 115.043 126.364 93.739  1.00 50.34  ? 237 ILE A O   1 
ATOM 1867 C CB  . ILE A 1 254 ? 112.573 124.730 95.060  1.00 50.34  ? 237 ILE A CB  1 
ATOM 1868 C CG1 . ILE A 1 254 ? 111.701 123.480 95.175  1.00 50.34  ? 237 ILE A CG1 1 
ATOM 1869 C CG2 . ILE A 1 254 ? 111.750 125.966 95.395  1.00 50.34  ? 237 ILE A CG2 1 
ATOM 1870 C CD1 . ILE A 1 254 ? 112.430 122.274 95.702  1.00 50.34  ? 237 ILE A CD1 1 
ATOM 1871 N N   . ASN A 1 255 ? 113.107 127.116 92.860  1.00 57.13  ? 238 ASN A N   1 
ATOM 1872 C CA  . ASN A 1 255 ? 113.618 128.463 92.654  1.00 57.13  ? 238 ASN A CA  1 
ATOM 1873 C C   . ASN A 1 255 ? 114.068 129.052 93.988  1.00 57.13  ? 238 ASN A C   1 
ATOM 1874 O O   . ASN A 1 255 ? 113.335 128.953 94.982  1.00 57.13  ? 238 ASN A O   1 
ATOM 1875 C CB  . ASN A 1 255 ? 112.545 129.348 92.022  1.00 57.13  ? 238 ASN A CB  1 
ATOM 1876 C CG  . ASN A 1 255 ? 111.819 128.663 90.882  1.00 57.13  ? 238 ASN A CG  1 
ATOM 1877 O OD1 . ASN A 1 255 ? 111.196 127.618 91.067  1.00 57.13  ? 238 ASN A OD1 1 
ATOM 1878 N ND2 . ASN A 1 255 ? 111.879 129.262 89.699  1.00 57.13  ? 238 ASN A ND2 1 
ATOM 1879 N N   . PRO A 1 256 ? 115.256 129.655 94.058  1.00 63.50  ? 239 PRO A N   1 
ATOM 1880 C CA  . PRO A 1 256 ? 115.772 130.121 95.356  1.00 63.50  ? 239 PRO A CA  1 
ATOM 1881 C C   . PRO A 1 256 ? 114.935 131.209 96.004  1.00 63.50  ? 239 PRO A C   1 
ATOM 1882 O O   . PRO A 1 256 ? 115.024 131.385 97.225  1.00 63.50  ? 239 PRO A O   1 
ATOM 1883 C CB  . PRO A 1 256 ? 117.178 130.630 95.011  1.00 63.50  ? 239 PRO A CB  1 
ATOM 1884 C CG  . PRO A 1 256 ? 117.119 130.947 93.554  1.00 63.50  ? 239 PRO A CG  1 
ATOM 1885 C CD  . PRO A 1 256 ? 116.185 129.943 92.953  1.00 63.50  ? 239 PRO A CD  1 
ATOM 1886 N N   . ASN A 1 257 ? 114.128 131.948 95.239  1.00 57.03  ? 240 ASN A N   1 
ATOM 1887 C CA  . ASN A 1 257 ? 113.305 132.990 95.840  1.00 57.03  ? 240 ASN A CA  1 
ATOM 1888 C C   . ASN A 1 257 ? 112.163 132.427 96.676  1.00 57.03  ? 240 ASN A C   1 
ATOM 1889 O O   . ASN A 1 257 ? 111.540 133.184 97.428  1.00 57.03  ? 240 ASN A O   1 
ATOM 1890 C CB  . ASN A 1 257 ? 112.746 133.921 94.763  1.00 57.03  ? 240 ASN A CB  1 
ATOM 1891 C CG  . ASN A 1 257 ? 111.773 133.224 93.838  1.00 57.03  ? 240 ASN A CG  1 
ATOM 1892 O OD1 . ASN A 1 257 ? 112.058 132.149 93.317  1.00 57.03  ? 240 ASN A OD1 1 
ATOM 1893 N ND2 . ASN A 1 257 ? 110.613 133.836 93.629  1.00 57.03  ? 240 ASN A ND2 1 
ATOM 1894 N N   . ARG A 1 258 ? 111.875 131.129 96.566  1.00 57.21  ? 241 ARG A N   1 
ATOM 1895 C CA  . ARG A 1 258 ? 110.873 130.478 97.411  1.00 57.21  ? 241 ARG A CA  1 
ATOM 1896 C C   . ARG A 1 258 ? 111.475 130.247 98.798  1.00 57.21  ? 241 ARG A C   1 
ATOM 1897 O O   . ARG A 1 258 ? 111.794 129.129 99.208  1.00 57.21  ? 241 ARG A O   1 
ATOM 1898 C CB  . ARG A 1 258 ? 110.400 129.177 96.778  1.00 57.21  ? 241 ARG A CB  1 
ATOM 1899 C CG  . ARG A 1 258 ? 109.621 129.361 95.488  1.00 57.21  ? 241 ARG A CG  1 
ATOM 1900 C CD  . ARG A 1 258 ? 108.327 130.119 95.730  1.00 57.21  ? 241 ARG A CD  1 
ATOM 1901 N NE  . ARG A 1 258 ? 107.202 129.221 95.960  1.00 57.21  ? 241 ARG A NE  1 
ATOM 1902 C CZ  . ARG A 1 258 ? 106.526 128.606 95.000  1.00 57.21  ? 241 ARG A CZ  1 
ATOM 1903 N NH1 . ARG A 1 258 ? 106.835 128.766 93.724  1.00 57.21  ? 241 ARG A NH1 1 
ATOM 1904 N NH2 . ARG A 1 258 ? 105.513 127.809 95.328  1.00 57.21  ? 241 ARG A NH2 1 
ATOM 1905 N N   . VAL A 1 259 ? 111.626 131.345 99.524  1.00 51.98  ? 242 VAL A N   1 
ATOM 1906 C CA  . VAL A 1 259 ? 112.245 131.342 100.843 1.00 51.98  ? 242 VAL A CA  1 
ATOM 1907 C C   . VAL A 1 259 ? 111.159 131.185 101.897 1.00 51.98  ? 242 VAL A C   1 
ATOM 1908 O O   . VAL A 1 259 ? 110.070 131.759 101.781 1.00 51.98  ? 242 VAL A O   1 
ATOM 1909 C CB  . VAL A 1 259 ? 113.064 132.630 101.059 1.00 51.98  ? 242 VAL A CB  1 
ATOM 1910 C CG1 . VAL A 1 259 ? 112.243 133.856 100.686 1.00 51.98  ? 242 VAL A CG1 1 
ATOM 1911 C CG2 . VAL A 1 259 ? 113.564 132.726 102.494 1.00 51.98  ? 242 VAL A CG2 1 
ATOM 1912 N N   . PHE A 1 260 ? 111.450 130.393 102.929 1.00 49.85  ? 243 PHE A N   1 
ATOM 1913 C CA  . PHE A 1 260 ? 110.504 130.188 104.017 1.00 49.85  ? 243 PHE A CA  1 
ATOM 1914 C C   . PHE A 1 260 ? 110.438 131.439 104.881 1.00 49.85  ? 243 PHE A C   1 
ATOM 1915 O O   . PHE A 1 260 ? 111.148 131.547 105.885 1.00 49.85  ? 243 PHE A O   1 
ATOM 1916 C CB  . PHE A 1 260 ? 110.903 128.972 104.854 1.00 49.85  ? 243 PHE A CB  1 
ATOM 1917 C CG  . PHE A 1 260 ? 109.760 128.344 105.597 1.00 49.85  ? 243 PHE A CG  1 
ATOM 1918 C CD1 . PHE A 1 260 ? 108.602 127.982 104.932 1.00 49.85  ? 243 PHE A CD1 1 
ATOM 1919 C CD2 . PHE A 1 260 ? 109.845 128.113 106.959 1.00 49.85  ? 243 PHE A CD2 1 
ATOM 1920 C CE1 . PHE A 1 260 ? 107.549 127.402 105.612 1.00 49.85  ? 243 PHE A CE1 1 
ATOM 1921 C CE2 . PHE A 1 260 ? 108.795 127.534 107.644 1.00 49.85  ? 243 PHE A CE2 1 
ATOM 1922 C CZ  . PHE A 1 260 ? 107.646 127.179 106.970 1.00 49.85  ? 243 PHE A CZ  1 
ATOM 1923 N N   . LYS A 1 261 ? 109.593 132.390 104.486 1.00 49.85  ? 244 LYS A N   1 
ATOM 1924 C CA  . LYS A 1 261 ? 109.526 133.678 105.164 1.00 49.85  ? 244 LYS A CA  1 
ATOM 1925 C C   . LYS A 1 261 ? 109.129 133.508 106.625 1.00 49.85  ? 244 LYS A C   1 
ATOM 1926 O O   . LYS A 1 261 ? 108.215 132.749 106.955 1.00 49.85  ? 244 LYS A O   1 
ATOM 1927 C CB  . LYS A 1 261 ? 108.529 134.594 104.454 1.00 49.85  ? 244 LYS A CB  1 
ATOM 1928 C CG  . LYS A 1 261 ? 108.248 134.207 103.011 1.00 49.85  ? 244 LYS A CG  1 
ATOM 1929 C CD  . LYS A 1 261 ? 107.133 135.052 102.419 1.00 49.85  ? 244 LYS A CD  1 
ATOM 1930 C CE  . LYS A 1 261 ? 106.800 134.613 101.003 1.00 49.85  ? 244 LYS A CE  1 
ATOM 1931 N NZ  . LYS A 1 261 ? 107.922 134.871 100.060 1.00 49.85  ? 244 LYS A NZ  1 
ATOM 1932 N N   . VAL A 1 262 ? 109.830 134.223 107.501 1.00 49.85  ? 245 VAL A N   1 
ATOM 1933 C CA  . VAL A 1 262 ? 109.568 134.208 108.934 1.00 49.85  ? 245 VAL A CA  1 
ATOM 1934 C C   . VAL A 1 262 ? 109.438 135.645 109.420 1.00 49.85  ? 245 VAL A C   1 
ATOM 1935 O O   . VAL A 1 262 ? 110.182 136.530 108.983 1.00 49.85  ? 245 VAL A O   1 
ATOM 1936 C CB  . VAL A 1 262 ? 110.672 133.460 109.713 1.00 49.85  ? 245 VAL A CB  1 
ATOM 1937 C CG1 . VAL A 1 262 ? 110.694 131.992 109.322 1.00 49.85  ? 245 VAL A CG1 1 
ATOM 1938 C CG2 . VAL A 1 262 ? 112.033 134.090 109.460 1.00 49.85  ? 245 VAL A CG2 1 
ATOM 1939 N N   . ASN A 1 263 ? 108.473 135.880 110.304 1.00 49.85  ? 246 ASN A N   1 
ATOM 1940 C CA  . ASN A 1 263 ? 108.279 137.211 110.859 1.00 49.85  ? 246 ASN A CA  1 
ATOM 1941 C C   . ASN A 1 263 ? 109.441 137.579 111.773 1.00 49.85  ? 246 ASN A C   1 
ATOM 1942 O O   . ASN A 1 263 ? 109.942 136.748 112.535 1.00 49.85  ? 246 ASN A O   1 
ATOM 1943 C CB  . ASN A 1 263 ? 106.960 137.279 111.626 1.00 49.85  ? 246 ASN A CB  1 
ATOM 1944 C CG  . ASN A 1 263 ? 105.788 136.774 110.813 1.00 49.85  ? 246 ASN A CG  1 
ATOM 1945 O OD1 . ASN A 1 263 ? 105.700 137.022 109.611 1.00 49.85  ? 246 ASN A OD1 1 
ATOM 1946 N ND2 . ASN A 1 263 ? 104.879 136.059 111.465 1.00 49.85  ? 246 ASN A ND2 1 
ATOM 1947 N N   . THR A 1 264 ? 109.874 138.839 111.690 1.00 49.85  ? 247 THR A N   1 
ATOM 1948 C CA  . THR A 1 264 ? 111.019 139.317 112.451 1.00 49.85  ? 247 THR A CA  1 
ATOM 1949 C C   . THR A 1 264 ? 110.730 140.561 113.278 1.00 49.85  ? 247 THR A C   1 
ATOM 1950 O O   . THR A 1 264 ? 111.645 141.071 113.934 1.00 49.85  ? 247 THR A O   1 
ATOM 1951 C CB  . THR A 1 264 ? 112.202 139.618 111.515 1.00 49.85  ? 247 THR A CB  1 
ATOM 1952 O OG1 . THR A 1 264 ? 111.927 140.804 110.760 1.00 49.85  ? 247 THR A OG1 1 
ATOM 1953 C CG2 . THR A 1 264 ? 112.448 138.460 110.558 1.00 49.85  ? 247 THR A CG2 1 
ATOM 1954 N N   . ASN A 1 265 ? 109.496 141.066 113.269 1.00 54.03  ? 248 ASN A N   1 
ATOM 1955 C CA  . ASN A 1 265 ? 109.191 142.311 113.966 1.00 54.03  ? 248 ASN A CA  1 
ATOM 1956 C C   . ASN A 1 265 ? 109.114 142.132 115.477 1.00 54.03  ? 248 ASN A C   1 
ATOM 1957 O O   . ASN A 1 265 ? 109.395 143.077 116.222 1.00 54.03  ? 248 ASN A O   1 
ATOM 1958 C CB  . ASN A 1 265 ? 107.879 142.896 113.442 1.00 54.03  ? 248 ASN A CB  1 
ATOM 1959 C CG  . ASN A 1 265 ? 107.984 143.364 112.005 1.00 54.03  ? 248 ASN A CG  1 
ATOM 1960 O OD1 . ASN A 1 265 ? 109.082 143.546 111.478 1.00 54.03  ? 248 ASN A OD1 1 
ATOM 1961 N ND2 . ASN A 1 265 ? 106.840 143.561 111.361 1.00 54.03  ? 248 ASN A ND2 1 
ATOM 1962 N N   . ALA A 1 266 ? 108.737 140.948 115.949 1.00 49.85  ? 249 ALA A N   1 
ATOM 1963 C CA  . ALA A 1 266 ? 108.583 140.732 117.380 1.00 49.85  ? 249 ALA A CA  1 
ATOM 1964 C C   . ALA A 1 266 ? 109.929 140.477 118.050 1.00 49.85  ? 249 ALA A C   1 
ATOM 1965 O O   . ALA A 1 266 ? 110.879 139.996 117.427 1.00 49.85  ? 249 ALA A O   1 
ATOM 1966 C CB  . ALA A 1 266 ? 107.640 139.561 117.651 1.00 49.85  ? 249 ALA A CB  1 
ATOM 1967 N N   . TYR A 1 267 ? 109.998 140.815 119.341 1.00 50.63  ? 250 TYR A N   1 
ATOM 1968 C CA  . TYR A 1 267 ? 111.214 140.573 120.114 1.00 50.63  ? 250 TYR A CA  1 
ATOM 1969 C C   . TYR A 1 267 ? 111.492 139.082 120.259 1.00 50.63  ? 250 TYR A C   1 
ATOM 1970 O O   . TYR A 1 267 ? 112.649 138.652 120.192 1.00 50.63  ? 250 TYR A O   1 
ATOM 1971 C CB  . TYR A 1 267 ? 111.106 141.240 121.486 1.00 50.63  ? 250 TYR A CB  1 
ATOM 1972 C CG  . TYR A 1 267 ? 109.968 140.729 122.340 1.00 50.63  ? 250 TYR A CG  1 
ATOM 1973 C CD1 . TYR A 1 267 ? 108.696 141.273 122.230 1.00 50.63  ? 250 TYR A CD1 1 
ATOM 1974 C CD2 . TYR A 1 267 ? 110.167 139.712 123.263 1.00 50.63  ? 250 TYR A CD2 1 
ATOM 1975 C CE1 . TYR A 1 267 ? 107.653 140.813 123.006 1.00 50.63  ? 250 TYR A CE1 1 
ATOM 1976 C CE2 . TYR A 1 267 ? 109.129 139.244 124.044 1.00 50.63  ? 250 TYR A CE2 1 
ATOM 1977 C CZ  . TYR A 1 267 ? 107.875 139.799 123.912 1.00 50.63  ? 250 TYR A CZ  1 
ATOM 1978 O OH  . TYR A 1 267 ? 106.837 139.338 124.688 1.00 50.63  ? 250 TYR A OH  1 
ATOM 1979 N N   . TYR A 1 268 ? 110.449 138.279 120.457 1.00 49.85  ? 251 TYR A N   1 
ATOM 1980 C CA  . TYR A 1 268 ? 110.594 136.833 120.546 1.00 49.85  ? 251 TYR A CA  1 
ATOM 1981 C C   . TYR A 1 268 ? 110.785 136.181 119.186 1.00 49.85  ? 251 TYR A C   1 
ATOM 1982 O O   . TYR A 1 268 ? 110.810 134.949 119.101 1.00 49.85  ? 251 TYR A O   1 
ATOM 1983 C CB  . TYR A 1 268 ? 109.378 136.223 121.251 1.00 49.85  ? 251 TYR A CB  1 
ATOM 1984 C CG  . TYR A 1 268 ? 108.048 136.602 120.636 1.00 49.85  ? 251 TYR A CG  1 
ATOM 1985 C CD1 . TYR A 1 268 ? 107.564 135.941 119.514 1.00 49.85  ? 251 TYR A CD1 1 
ATOM 1986 C CD2 . TYR A 1 268 ? 107.275 137.618 121.180 1.00 49.85  ? 251 TYR A CD2 1 
ATOM 1987 C CE1 . TYR A 1 268 ? 106.351 136.284 118.950 1.00 49.85  ? 251 TYR A CE1 1 
ATOM 1988 C CE2 . TYR A 1 268 ? 106.060 137.967 120.623 1.00 49.85  ? 251 TYR A CE2 1 
ATOM 1989 C CZ  . TYR A 1 268 ? 105.603 137.297 119.509 1.00 49.85  ? 251 TYR A CZ  1 
ATOM 1990 O OH  . TYR A 1 268 ? 104.394 137.641 118.950 1.00 49.85  ? 251 TYR A OH  1 
ATOM 1991 N N   . GLU A 1 269 ? 110.916 136.972 118.129 1.00 55.81  ? 252 GLU A N   1 
ATOM 1992 C CA  . GLU A 1 269 ? 111.060 136.466 116.776 1.00 55.81  ? 252 GLU A CA  1 
ATOM 1993 C C   . GLU A 1 269 ? 112.514 136.543 116.327 1.00 55.81  ? 252 GLU A C   1 
ATOM 1994 O O   . GLU A 1 269 ? 113.313 137.326 116.846 1.00 55.81  ? 252 GLU A O   1 
ATOM 1995 C CB  . GLU A 1 269 ? 110.169 137.250 115.810 1.00 55.81  ? 252 GLU A CB  1 
ATOM 1996 C CG  . GLU A 1 269 ? 108.801 136.628 115.596 1.00 55.81  ? 252 GLU A CG  1 
ATOM 1997 C CD  . GLU A 1 269 ? 107.831 137.569 114.913 1.00 55.81  ? 252 GLU A CD  1 
ATOM 1998 O OE1 . GLU A 1 269 ? 108.272 138.633 114.432 1.00 55.81  ? 252 GLU A OE1 1 
ATOM 1999 O OE2 . GLU A 1 269 ? 106.626 137.245 114.860 1.00 55.81  ? 252 GLU A OE2 1 
ATOM 2000 N N   . MET A 1 270 ? 112.846 135.709 115.348 1.00 49.85  ? 253 MET A N   1 
ATOM 2001 C CA  . MET A 1 270 ? 114.205 135.644 114.837 1.00 49.85  ? 253 MET A CA  1 
ATOM 2002 C C   . MET A 1 270 ? 114.533 136.889 114.023 1.00 49.85  ? 253 MET A C   1 
ATOM 2003 O O   . MET A 1 270 ? 113.651 137.541 113.461 1.00 49.85  ? 253 MET A O   1 
ATOM 2004 C CB  . MET A 1 270 ? 114.377 134.399 113.970 1.00 49.85  ? 253 MET A CB  1 
ATOM 2005 C CG  . MET A 1 270 ? 115.024 133.238 114.688 1.00 49.85  ? 253 MET A CG  1 
ATOM 2006 S SD  . MET A 1 270 ? 115.661 131.988 113.566 1.00 49.85  ? 253 MET A SD  1 
ATOM 2007 C CE  . MET A 1 270 ? 116.301 130.816 114.752 1.00 49.85  ? 253 MET A CE  1 
ATOM 2008 N N   . SER A 1 271 ? 115.824 137.225 113.972 1.00 61.78  ? 254 SER A N   1 
ATOM 2009 C CA  . SER A 1 271 ? 116.266 138.278 113.063 1.00 61.78  ? 254 SER A CA  1 
ATOM 2010 C C   . SER A 1 271 ? 116.060 137.862 111.613 1.00 61.78  ? 254 SER A C   1 
ATOM 2011 O O   . SER A 1 271 ? 115.710 138.691 110.765 1.00 61.78  ? 254 SER A O   1 
ATOM 2012 C CB  . SER A 1 271 ? 117.733 138.621 113.319 1.00 61.78  ? 254 SER A CB  1 
ATOM 2013 O OG  . SER A 1 271 ? 117.900 139.265 114.569 1.00 61.78  ? 254 SER A OG  1 
ATOM 2014 N N   . GLY A 1 272 ? 116.278 136.586 111.313 1.00 63.58  ? 255 GLY A N   1 
ATOM 2015 C CA  . GLY A 1 272 ? 116.057 136.058 109.984 1.00 63.58  ? 255 GLY A CA  1 
ATOM 2016 C C   . GLY A 1 272 ? 116.745 134.726 109.774 1.00 63.58  ? 255 GLY A C   1 
ATOM 2017 O O   . GLY A 1 272 ? 117.888 134.536 110.200 1.00 63.58  ? 255 GLY A O   1 
ATOM 2018 N N   . LEU A 1 273 ? 116.059 133.796 109.116 1.00 71.35  ? 256 LEU A N   1 
ATOM 2019 C CA  . LEU A 1 273 ? 116.591 132.462 108.843 1.00 71.35  ? 256 LEU A CA  1 
ATOM 2020 C C   . LEU A 1 273 ? 116.351 132.175 107.364 1.00 71.35  ? 256 LEU A C   1 
ATOM 2021 O O   . LEU A 1 273 ? 115.270 131.717 106.981 1.00 71.35  ? 256 LEU A O   1 
ATOM 2022 C CB  . LEU A 1 273 ? 115.935 131.412 109.736 1.00 71.35  ? 256 LEU A CB  1 
ATOM 2023 C CG  . LEU A 1 273 ? 116.351 129.943 109.590 1.00 71.35  ? 256 LEU A CG  1 
ATOM 2024 C CD1 . LEU A 1 273 ? 117.817 129.802 109.191 1.00 71.35  ? 256 LEU A CD1 1 
ATOM 2025 C CD2 . LEU A 1 273 ? 116.070 129.179 110.876 1.00 71.35  ? 256 LEU A CD2 1 
ATOM 2026 N N   . GLU A 1 274 ? 117.359 132.443 106.538 1.00 78.21  ? 257 GLU A N   1 
ATOM 2027 C CA  . GLU A 1 274 ? 117.253 132.240 105.095 1.00 78.21  ? 257 GLU A CA  1 
ATOM 2028 C C   . GLU A 1 274 ? 117.346 130.748 104.811 1.00 78.21  ? 257 GLU A C   1 
ATOM 2029 O O   . GLU A 1 274 ? 118.408 130.215 104.489 1.00 78.21  ? 257 GLU A O   1 
ATOM 2030 C CB  . GLU A 1 274 ? 118.337 133.017 104.359 1.00 78.21  ? 257 GLU A CB  1 
ATOM 2031 C CG  . GLU A 1 274 ? 118.103 134.517 104.319 1.00 78.21  ? 257 GLU A CG  1 
ATOM 2032 C CD  . GLU A 1 274 ? 116.789 134.885 103.660 1.00 78.21  ? 257 GLU A CD  1 
ATOM 2033 O OE1 . GLU A 1 274 ? 116.491 134.339 102.577 1.00 78.21  ? 257 GLU A OE1 1 
ATOM 2034 O OE2 . GLU A 1 274 ? 116.052 135.722 104.224 1.00 78.21  ? 257 GLU A OE2 1 
ATOM 2035 N N   . VAL A 1 275 ? 116.212 130.064 104.933 1.00 61.07  ? 258 VAL A N   1 
ATOM 2036 C CA  . VAL A 1 275 ? 116.107 128.644 104.625 1.00 61.07  ? 258 VAL A CA  1 
ATOM 2037 C C   . VAL A 1 275 ? 115.216 128.495 103.398 1.00 61.07  ? 258 VAL A C   1 
ATOM 2038 O O   . VAL A 1 275 ? 114.076 128.976 103.381 1.00 61.07  ? 258 VAL A O   1 
ATOM 2039 C CB  . VAL A 1 275 ? 115.579 127.837 105.823 1.00 61.07  ? 258 VAL A CB  1 
ATOM 2040 C CG1 . VAL A 1 275 ? 114.254 128.394 106.329 1.00 61.07  ? 258 VAL A CG1 1 
ATOM 2041 C CG2 . VAL A 1 275 ? 115.434 126.371 105.448 1.00 61.07  ? 258 VAL A CG2 1 
ATOM 2042 N N   . SER A 1 276 ? 115.750 127.863 102.359 1.00 50.79  ? 259 SER A N   1 
ATOM 2043 C CA  . SER A 1 276 ? 115.004 127.676 101.127 1.00 50.79  ? 259 SER A CA  1 
ATOM 2044 C C   . SER A 1 276 ? 114.105 126.447 101.227 1.00 50.79  ? 259 SER A C   1 
ATOM 2045 O O   . SER A 1 276 ? 114.217 125.629 102.145 1.00 50.79  ? 259 SER A O   1 
ATOM 2046 C CB  . SER A 1 276 ? 115.955 127.543 99.939  1.00 50.79  ? 259 SER A CB  1 
ATOM 2047 O OG  . SER A 1 276 ? 115.333 126.865 98.862  1.00 50.79  ? 259 SER A OG  1 
ATOM 2048 N N   . PHE A 1 277 ? 113.196 126.324 100.259 1.00 51.59  ? 260 PHE A N   1 
ATOM 2049 C CA  . PHE A 1 277 ? 112.354 125.136 100.192 1.00 51.59  ? 260 PHE A CA  1 
ATOM 2050 C C   . PHE A 1 277 ? 113.156 123.917 99.760  1.00 51.59  ? 260 PHE A C   1 
ATOM 2051 O O   . PHE A 1 277 ? 112.805 122.785 100.115 1.00 51.59  ? 260 PHE A O   1 
ATOM 2052 C CB  . PHE A 1 277 ? 111.183 125.375 99.240  1.00 51.59  ? 260 PHE A CB  1 
ATOM 2053 C CG  . PHE A 1 277 ? 109.968 125.957 99.907  1.00 51.59  ? 260 PHE A CG  1 
ATOM 2054 C CD1 . PHE A 1 277 ? 110.092 126.987 100.824 1.00 51.59  ? 260 PHE A CD1 1 
ATOM 2055 C CD2 . PHE A 1 277 ? 108.703 125.476 99.615  1.00 51.59  ? 260 PHE A CD2 1 
ATOM 2056 C CE1 . PHE A 1 277 ? 108.978 127.525 101.439 1.00 51.59  ? 260 PHE A CE1 1 
ATOM 2057 C CE2 . PHE A 1 277 ? 107.585 126.011 100.227 1.00 51.59  ? 260 PHE A CE2 1 
ATOM 2058 C CZ  . PHE A 1 277 ? 107.724 127.036 101.140 1.00 51.59  ? 260 PHE A CZ  1 
ATOM 2059 N N   . GLU A 1 278 ? 114.234 124.127 99.001  1.00 53.30  ? 261 GLU A N   1 
ATOM 2060 C CA  . GLU A 1 278 ? 115.109 123.020 98.633  1.00 53.30  ? 261 GLU A CA  1 
ATOM 2061 C C   . GLU A 1 278 ? 115.760 122.404 99.864  1.00 53.30  ? 261 GLU A C   1 
ATOM 2062 O O   . GLU A 1 278 ? 115.910 121.181 99.950  1.00 53.30  ? 261 GLU A O   1 
ATOM 2063 C CB  . GLU A 1 278 ? 116.171 123.496 97.640  1.00 53.30  ? 261 GLU A CB  1 
ATOM 2064 C CG  . GLU A 1 278 ? 117.227 122.453 97.282  1.00 53.30  ? 261 GLU A CG  1 
ATOM 2065 C CD  . GLU A 1 278 ? 116.679 121.276 96.488  1.00 53.30  ? 261 GLU A CD  1 
ATOM 2066 O OE1 . GLU A 1 278 ? 115.492 121.296 96.104  1.00 53.30  ? 261 GLU A OE1 1 
ATOM 2067 O OE2 . GLU A 1 278 ? 117.446 120.320 96.250  1.00 53.30  ? 261 GLU A OE2 1 
ATOM 2068 N N   . GLU A 1 279 ? 116.158 123.239 100.828 1.00 49.85  ? 262 GLU A N   1 
ATOM 2069 C CA  . GLU A 1 279 ? 116.711 122.718 102.074 1.00 49.85  ? 262 GLU A CA  1 
ATOM 2070 C C   . GLU A 1 279 ? 115.687 121.871 102.818 1.00 49.85  ? 262 GLU A C   1 
ATOM 2071 O O   . GLU A 1 279 ? 116.017 120.802 103.344 1.00 49.85  ? 262 GLU A O   1 
ATOM 2072 C CB  . GLU A 1 279 ? 117.197 123.869 102.953 1.00 49.85  ? 262 GLU A CB  1 
ATOM 2073 C CG  . GLU A 1 279 ? 118.482 123.576 103.707 1.00 49.85  ? 262 GLU A CG  1 
ATOM 2074 C CD  . GLU A 1 279 ? 119.709 123.676 102.825 1.00 49.85  ? 262 GLU A CD  1 
ATOM 2075 O OE1 . GLU A 1 279 ? 119.853 124.696 102.119 1.00 49.85  ? 262 GLU A OE1 1 
ATOM 2076 O OE2 . GLU A 1 279 ? 120.531 122.735 102.837 1.00 49.85  ? 262 GLU A OE2 1 
ATOM 2077 N N   . LEU A 1 280 ? 114.435 122.335 102.873 1.00 49.85  ? 263 LEU A N   1 
ATOM 2078 C CA  . LEU A 1 280 ? 113.383 121.559 103.520 1.00 49.85  ? 263 LEU A CA  1 
ATOM 2079 C C   . LEU A 1 280 ? 113.173 120.225 102.818 1.00 49.85  ? 263 LEU A C   1 
ATOM 2080 O O   . LEU A 1 280 ? 113.016 119.187 103.472 1.00 49.85  ? 263 LEU A O   1 
ATOM 2081 C CB  . LEU A 1 280 ? 112.079 122.357 103.540 1.00 49.85  ? 263 LEU A CB  1 
ATOM 2082 C CG  . LEU A 1 280 ? 112.032 123.596 104.430 1.00 49.85  ? 263 LEU A CG  1 
ATOM 2083 C CD1 . LEU A 1 280 ? 110.698 124.305 104.280 1.00 49.85  ? 263 LEU A CD1 1 
ATOM 2084 C CD2 . LEU A 1 280 ? 112.266 123.205 105.872 1.00 49.85  ? 263 LEU A CD2 1 
ATOM 2085 N N   . ARG A 1 281 ? 113.163 120.234 101.484 1.00 49.85  ? 264 ARG A N   1 
ATOM 2086 C CA  . ARG A 1 281 ? 112.966 118.996 100.737 1.00 49.85  ? 264 ARG A CA  1 
ATOM 2087 C C   . ARG A 1 281 ? 114.124 118.029 100.952 1.00 49.85  ? 264 ARG A C   1 
ATOM 2088 O O   . ARG A 1 281 ? 113.913 116.817 101.076 1.00 49.85  ? 264 ARG A O   1 
ATOM 2089 C CB  . ARG A 1 281 ? 112.798 119.311 99.252  1.00 49.85  ? 264 ARG A CB  1 
ATOM 2090 C CG  . ARG A 1 281 ? 111.511 120.042 98.923  1.00 49.85  ? 264 ARG A CG  1 
ATOM 2091 C CD  . ARG A 1 281 ? 110.889 119.513 97.650  1.00 49.85  ? 264 ARG A CD  1 
ATOM 2092 N NE  . ARG A 1 281 ? 111.892 119.253 96.625  1.00 49.85  ? 264 ARG A NE  1 
ATOM 2093 C CZ  . ARG A 1 281 ? 111.614 118.854 95.392  1.00 49.85  ? 264 ARG A CZ  1 
ATOM 2094 N NH1 . ARG A 1 281 ? 110.368 118.656 94.995  1.00 49.85  ? 264 ARG A NH1 1 
ATOM 2095 N NH2 . ARG A 1 281 ? 112.610 118.650 94.535  1.00 49.85  ? 264 ARG A NH2 1 
ATOM 2096 N N   . THR A 1 282 ? 115.353 118.547 100.996 1.00 49.85  ? 265 THR A N   1 
ATOM 2097 C CA  . THR A 1 282 ? 116.521 117.690 101.163 1.00 49.85  ? 265 THR A CA  1 
ATOM 2098 C C   . THR A 1 282 ? 116.593 117.109 102.571 1.00 49.85  ? 265 THR A C   1 
ATOM 2099 O O   . THR A 1 282 ? 116.921 115.929 102.743 1.00 49.85  ? 265 THR A O   1 
ATOM 2100 C CB  . THR A 1 282 ? 117.792 118.478 100.837 1.00 49.85  ? 265 THR A CB  1 
ATOM 2101 O OG1 . THR A 1 282 ? 117.895 118.653 99.419  1.00 49.85  ? 265 THR A OG1 1 
ATOM 2102 C CG2 . THR A 1 282 ? 119.029 117.754 101.344 1.00 49.85  ? 265 THR A CG2 1 
ATOM 2103 N N   . PHE A 1 283 ? 116.281 117.917 103.588 1.00 49.85  ? 266 PHE A N   1 
ATOM 2104 C CA  . PHE A 1 283 ? 116.419 117.457 104.967 1.00 49.85  ? 266 PHE A CA  1 
ATOM 2105 C C   . PHE A 1 283 ? 115.501 116.276 105.256 1.00 49.85  ? 266 PHE A C   1 
ATOM 2106 O O   . PHE A 1 283 ? 115.915 115.301 105.894 1.00 49.85  ? 266 PHE A O   1 
ATOM 2107 C CB  . PHE A 1 283 ? 116.135 118.606 105.933 1.00 49.85  ? 266 PHE A CB  1 
ATOM 2108 C CG  . PHE A 1 283 ? 117.358 119.378 106.334 1.00 49.85  ? 266 PHE A CG  1 
ATOM 2109 C CD1 . PHE A 1 283 ? 118.470 118.727 106.838 1.00 49.85  ? 266 PHE A CD1 1 
ATOM 2110 C CD2 . PHE A 1 283 ? 117.394 120.756 106.210 1.00 49.85  ? 266 PHE A CD2 1 
ATOM 2111 C CE1 . PHE A 1 283 ? 119.597 119.436 107.208 1.00 49.85  ? 266 PHE A CE1 1 
ATOM 2112 C CE2 . PHE A 1 283 ? 118.517 121.470 106.579 1.00 49.85  ? 266 PHE A CE2 1 
ATOM 2113 C CZ  . PHE A 1 283 ? 119.620 120.809 107.078 1.00 49.85  ? 266 PHE A CZ  1 
ATOM 2114 N N   . GLY A 1 284 ? 114.257 116.342 104.798 1.00 49.85  ? 267 GLY A N   1 
ATOM 2115 C CA  . GLY A 1 284 ? 113.332 115.239 104.966 1.00 49.85  ? 267 GLY A CA  1 
ATOM 2116 C C   . GLY A 1 284 ? 112.840 115.104 106.396 1.00 49.85  ? 267 GLY A C   1 
ATOM 2117 O O   . GLY A 1 284 ? 113.162 115.890 107.285 1.00 49.85  ? 267 GLY A O   1 
ATOM 2118 N N   . GLY A 1 285 ? 112.045 114.058 106.612 1.00 55.06  ? 268 GLY A N   1 
ATOM 2119 C CA  . GLY A 1 285 ? 111.454 113.853 107.923 1.00 55.06  ? 268 GLY A CA  1 
ATOM 2120 C C   . GLY A 1 285 ? 110.486 114.969 108.261 1.00 55.06  ? 268 GLY A C   1 
ATOM 2121 O O   . GLY A 1 285 ? 109.787 115.506 107.393 1.00 55.06  ? 268 GLY A O   1 
ATOM 2122 N N   . HIS A 1 286 ? 110.451 115.335 109.546 1.00 61.13  ? 269 HIS A N   1 
ATOM 2123 C CA  . HIS A 1 286 ? 109.587 116.428 109.981 1.00 61.13  ? 269 HIS A CA  1 
ATOM 2124 C C   . HIS A 1 286 ? 109.907 117.719 109.242 1.00 61.13  ? 269 HIS A C   1 
ATOM 2125 O O   . HIS A 1 286 ? 109.021 118.559 109.045 1.00 61.13  ? 269 HIS A O   1 
ATOM 2126 C CB  . HIS A 1 286 ? 109.723 116.638 111.489 1.00 61.13  ? 269 HIS A CB  1 
ATOM 2127 C CG  . HIS A 1 286 ? 109.125 115.537 112.307 1.00 61.13  ? 269 HIS A CG  1 
ATOM 2128 N ND1 . HIS A 1 286 ? 108.432 114.486 111.747 1.00 61.13  ? 269 HIS A ND1 1 
ATOM 2129 C CD2 . HIS A 1 286 ? 109.119 115.321 113.644 1.00 61.13  ? 269 HIS A CD2 1 
ATOM 2130 C CE1 . HIS A 1 286 ? 108.025 113.670 112.703 1.00 61.13  ? 269 HIS A CE1 1 
ATOM 2131 N NE2 . HIS A 1 286 ? 108.428 114.155 113.863 1.00 61.13  ? 269 HIS A NE2 1 
ATOM 2132 N N   . ASP A 1 287 ? 111.160 117.885 108.812 1.00 52.90  ? 270 ASP A N   1 
ATOM 2133 C CA  . ASP A 1 287 ? 111.541 119.083 108.072 1.00 52.90  ? 270 ASP A CA  1 
ATOM 2134 C C   . ASP A 1 287 ? 110.757 119.197 106.772 1.00 52.90  ? 270 ASP A C   1 
ATOM 2135 O O   . ASP A 1 287 ? 110.429 120.304 106.330 1.00 52.90  ? 270 ASP A O   1 
ATOM 2136 C CB  . ASP A 1 287 ? 113.040 119.067 107.788 1.00 52.90  ? 270 ASP A CB  1 
ATOM 2137 C CG  . ASP A 1 287 ? 113.841 119.745 108.872 1.00 52.90  ? 270 ASP A CG  1 
ATOM 2138 O OD1 . ASP A 1 287 ? 113.627 120.950 109.099 1.00 52.90  ? 270 ASP A OD1 1 
ATOM 2139 O OD2 . ASP A 1 287 ? 114.696 119.077 109.487 1.00 52.90  ? 270 ASP A OD2 1 
ATOM 2140 N N   . ALA A 1 288 ? 110.449 118.061 106.144 1.00 49.85  ? 271 ALA A N   1 
ATOM 2141 C CA  . ALA A 1 288 ? 109.666 118.074 104.916 1.00 49.85  ? 271 ALA A CA  1 
ATOM 2142 C C   . ALA A 1 288 ? 108.194 118.373 105.162 1.00 49.85  ? 271 ALA A C   1 
ATOM 2143 O O   . ALA A 1 288 ? 107.454 118.579 104.195 1.00 49.85  ? 271 ALA A O   1 
ATOM 2144 C CB  . ALA A 1 288 ? 109.806 116.737 104.187 1.00 49.85  ? 271 ALA A CB  1 
ATOM 2145 N N   . LYS A 1 289 ? 107.755 118.403 106.418 1.00 51.59  ? 272 LYS A N   1 
ATOM 2146 C CA  . LYS A 1 289 ? 106.355 118.623 106.748 1.00 51.59  ? 272 LYS A CA  1 
ATOM 2147 C C   . LYS A 1 289 ? 106.026 120.090 106.994 1.00 51.59  ? 272 LYS A C   1 
ATOM 2148 O O   . LYS A 1 289 ? 104.891 120.402 107.368 1.00 51.59  ? 272 LYS A O   1 
ATOM 2149 C CB  . LYS A 1 289 ? 105.966 117.784 107.967 1.00 51.59  ? 272 LYS A CB  1 
ATOM 2150 C CG  . LYS A 1 289 ? 106.259 116.303 107.797 1.00 51.59  ? 272 LYS A CG  1 
ATOM 2151 C CD  . LYS A 1 289 ? 105.730 115.487 108.962 1.00 51.59  ? 272 LYS A CD  1 
ATOM 2152 C CE  . LYS A 1 289 ? 106.210 114.048 108.878 1.00 51.59  ? 272 LYS A CE  1 
ATOM 2153 N NZ  . LYS A 1 289 ? 105.732 113.378 107.638 1.00 51.59  ? 272 LYS A NZ  1 
ATOM 2154 N N   . PHE A 1 290 ? 106.985 120.994 106.794 1.00 49.85  ? 273 PHE A N   1 
ATOM 2155 C CA  . PHE A 1 290 ? 106.718 122.420 106.929 1.00 49.85  ? 273 PHE A CA  1 
ATOM 2156 C C   . PHE A 1 290 ? 106.072 123.021 105.688 1.00 49.85  ? 273 PHE A C   1 
ATOM 2157 O O   . PHE A 1 290 ? 105.701 124.199 105.713 1.00 49.85  ? 273 PHE A O   1 
ATOM 2158 C CB  . PHE A 1 290 ? 108.009 123.179 107.248 1.00 49.85  ? 273 PHE A CB  1 
ATOM 2159 C CG  . PHE A 1 290 ? 108.427 123.096 108.689 1.00 49.85  ? 273 PHE A CG  1 
ATOM 2160 C CD1 . PHE A 1 290 ? 107.888 122.140 109.533 1.00 49.85  ? 273 PHE A CD1 1 
ATOM 2161 C CD2 . PHE A 1 290 ? 109.360 123.982 109.201 1.00 49.85  ? 273 PHE A CD2 1 
ATOM 2162 C CE1 . PHE A 1 290 ? 108.273 122.068 110.857 1.00 49.85  ? 273 PHE A CE1 1 
ATOM 2163 C CE2 . PHE A 1 290 ? 109.749 123.915 110.524 1.00 49.85  ? 273 PHE A CE2 1 
ATOM 2164 C CZ  . PHE A 1 290 ? 109.205 122.956 111.353 1.00 49.85  ? 273 PHE A CZ  1 
ATOM 2165 N N   . ILE A 1 291 ? 105.931 122.250 104.613 1.00 62.60  ? 274 ILE A N   1 
ATOM 2166 C CA  . ILE A 1 291 ? 105.272 122.699 103.394 1.00 62.60  ? 274 ILE A CA  1 
ATOM 2167 C C   . ILE A 1 291 ? 103.941 121.971 103.270 1.00 62.60  ? 274 ILE A C   1 
ATOM 2168 O O   . ILE A 1 291 ? 103.839 120.776 103.577 1.00 62.60  ? 274 ILE A O   1 
ATOM 2169 C CB  . ILE A 1 291 ? 106.160 122.483 102.150 1.00 62.60  ? 274 ILE A CB  1 
ATOM 2170 C CG1 . ILE A 1 291 ? 106.185 121.012 101.726 1.00 62.60  ? 274 ILE A CG1 1 
ATOM 2171 C CG2 . ILE A 1 291 ? 107.572 122.985 102.411 1.00 62.60  ? 274 ILE A CG2 1 
ATOM 2172 C CD1 . ILE A 1 291 ? 107.033 120.743 100.502 1.00 62.60  ? 274 ILE A CD1 1 
ATOM 2173 N N   . ASP A 1 292 ? 102.909 122.705 102.865 1.00 71.95  ? 275 ASP A N   1 
ATOM 2174 C CA  . ASP A 1 292 ? 101.581 122.131 102.741 1.00 71.95  ? 275 ASP A CA  1 
ATOM 2175 C C   . ASP A 1 292 ? 101.479 121.301 101.461 1.00 71.95  ? 275 ASP A C   1 
ATOM 2176 O O   . ASP A 1 292 ? 102.330 121.370 100.571 1.00 71.95  ? 275 ASP A O   1 
ATOM 2177 C CB  . ASP A 1 292 ? 100.520 123.231 102.762 1.00 71.95  ? 275 ASP A CB  1 
ATOM 2178 C CG  . ASP A 1 292 ? 99.123  122.693 103.007 1.00 71.95  ? 275 ASP A CG  1 
ATOM 2179 O OD1 . ASP A 1 292 ? 98.978  121.464 103.178 1.00 71.95  ? 275 ASP A OD1 1 
ATOM 2180 O OD2 . ASP A 1 292 ? 98.169  123.499 103.032 1.00 71.95  ? 275 ASP A OD2 1 
ATOM 2181 N N   . SER A 1 293 ? 100.415 120.499 101.381 1.00 72.70  ? 276 SER A N   1 
ATOM 2182 C CA  . SER A 1 293 ? 100.217 119.645 100.215 1.00 72.70  ? 276 SER A CA  1 
ATOM 2183 C C   . SER A 1 293 ? 99.978  120.459 98.951  1.00 72.70  ? 276 SER A C   1 
ATOM 2184 O O   . SER A 1 293 ? 100.310 120.004 97.850  1.00 72.70  ? 276 SER A O   1 
ATOM 2185 C CB  . SER A 1 293 ? 99.049  118.689 100.459 1.00 72.70  ? 276 SER A CB  1 
ATOM 2186 O OG  . SER A 1 293 ? 99.069  117.613 99.537  1.00 72.70  ? 276 SER A OG  1 
ATOM 2187 N N   . LEU A 1 294 ? 99.401  121.656 99.082  1.00 72.10  ? 277 LEU A N   1 
ATOM 2188 C CA  . LEU A 1 294 ? 99.122  122.480 97.910  1.00 72.10  ? 277 LEU A CA  1 
ATOM 2189 C C   . LEU A 1 294 ? 100.409 122.893 97.204  1.00 72.10  ? 277 LEU A C   1 
ATOM 2190 O O   . LEU A 1 294 ? 100.519 122.789 95.977  1.00 72.10  ? 277 LEU A O   1 
ATOM 2191 C CB  . LEU A 1 294 ? 98.313  123.711 98.319  1.00 72.10  ? 277 LEU A CB  1 
ATOM 2192 C CG  . LEU A 1 294 ? 98.066  124.749 97.223  1.00 72.10  ? 277 LEU A CG  1 
ATOM 2193 C CD1 . LEU A 1 294 ? 97.133  124.193 96.160  1.00 72.10  ? 277 LEU A CD1 1 
ATOM 2194 C CD2 . LEU A 1 294 ? 97.506  126.033 97.815  1.00 72.10  ? 277 LEU A CD2 1 
ATOM 2195 N N   . GLN A 1 295 ? 101.397 123.367 97.967  1.00 71.24  ? 278 GLN A N   1 
ATOM 2196 C CA  . GLN A 1 295 ? 102.659 123.788 97.365  1.00 71.24  ? 278 GLN A CA  1 
ATOM 2197 C C   . GLN A 1 295 ? 103.410 122.604 96.769  1.00 71.24  ? 278 GLN A C   1 
ATOM 2198 O O   . GLN A 1 295 ? 104.024 122.725 95.701  1.00 71.24  ? 278 GLN A O   1 
ATOM 2199 C CB  . GLN A 1 295 ? 103.517 124.510 98.403  1.00 71.24  ? 278 GLN A CB  1 
ATOM 2200 C CG  . GLN A 1 295 ? 102.881 125.782 98.939  1.00 71.24  ? 278 GLN A CG  1 
ATOM 2201 C CD  . GLN A 1 295 ? 103.764 126.501 99.937  1.00 71.24  ? 278 GLN A CD  1 
ATOM 2202 O OE1 . GLN A 1 295 ? 104.697 127.211 99.561  1.00 71.24  ? 278 GLN A OE1 1 
ATOM 2203 N NE2 . GLN A 1 295 ? 103.474 126.323 101.221 1.00 71.24  ? 278 GLN A NE2 1 
ATOM 2204 N N   . GLU A 1 296 ? 103.380 121.454 97.447  1.00 74.66  ? 279 GLU A N   1 
ATOM 2205 C CA  . GLU A 1 296 ? 104.014 120.258 96.902  1.00 74.66  ? 279 GLU A CA  1 
ATOM 2206 C C   . GLU A 1 296 ? 103.364 119.845 95.587  1.00 74.66  ? 279 GLU A C   1 
ATOM 2207 O O   . GLU A 1 296 ? 104.058 119.495 94.625  1.00 74.66  ? 279 GLU A O   1 
ATOM 2208 C CB  . GLU A 1 296 ? 103.945 119.120 97.919  1.00 74.66  ? 279 GLU A CB  1 
ATOM 2209 C CG  . GLU A 1 296 ? 104.323 117.758 97.361  1.00 74.66  ? 279 GLU A CG  1 
ATOM 2210 C CD  . GLU A 1 296 ? 103.793 116.615 98.205  1.00 74.66  ? 279 GLU A CD  1 
ATOM 2211 O OE1 . GLU A 1 296 ? 103.330 116.872 99.336  1.00 74.66  ? 279 GLU A OE1 1 
ATOM 2212 O OE2 . GLU A 1 296 ? 103.838 115.458 97.736  1.00 74.66  ? 279 GLU A OE2 1 
ATOM 2213 N N   . ASN A 1 297 ? 102.031 119.886 95.526  1.00 70.39  ? 280 ASN A N   1 
ATOM 2214 C CA  . ASN A 1 297 ? 101.332 119.550 94.290  1.00 70.39  ? 280 ASN A CA  1 
ATOM 2215 C C   . ASN A 1 297 ? 101.656 120.547 93.184  1.00 70.39  ? 280 ASN A C   1 
ATOM 2216 O O   . ASN A 1 297 ? 101.821 120.161 92.021  1.00 70.39  ? 280 ASN A O   1 
ATOM 2217 C CB  . ASN A 1 297 ? 99.826  119.494 94.539  1.00 70.39  ? 280 ASN A CB  1 
ATOM 2218 C CG  . ASN A 1 297 ? 99.190  118.236 93.983  1.00 70.39  ? 280 ASN A CG  1 
ATOM 2219 O OD1 . ASN A 1 297 ? 99.460  117.839 92.850  1.00 70.39  ? 280 ASN A OD1 1 
ATOM 2220 N ND2 . ASN A 1 297 ? 98.341  117.601 94.782  1.00 70.39  ? 280 ASN A ND2 1 
ATOM 2221 N N   . GLU A 1 298 ? 101.744 121.835 93.528  1.00 67.68  ? 281 GLU A N   1 
ATOM 2222 C CA  . GLU A 1 298 ? 102.098 122.843 92.535  1.00 67.68  ? 281 GLU A CA  1 
ATOM 2223 C C   . GLU A 1 298 ? 103.494 122.597 91.977  1.00 67.68  ? 281 GLU A C   1 
ATOM 2224 O O   . GLU A 1 298 ? 103.705 122.665 90.759  1.00 67.68  ? 281 GLU A O   1 
ATOM 2225 C CB  . GLU A 1 298 ? 101.998 124.239 93.151  1.00 67.68  ? 281 GLU A CB  1 
ATOM 2226 C CG  . GLU A 1 298 ? 103.020 125.236 92.627  1.00 67.68  ? 281 GLU A CG  1 
ATOM 2227 C CD  . GLU A 1 298 ? 103.025 126.532 93.414  1.00 67.68  ? 281 GLU A CD  1 
ATOM 2228 O OE1 . GLU A 1 298 ? 101.985 126.864 94.019  1.00 67.68  ? 281 GLU A OE1 1 
ATOM 2229 O OE2 . GLU A 1 298 ? 104.070 127.216 93.430  1.00 67.68  ? 281 GLU A OE2 1 
ATOM 2230 N N   . PHE A 1 299 ? 104.459 122.299 92.852  1.00 59.34  ? 282 PHE A N   1 
ATOM 2231 C CA  . PHE A 1 299 ? 105.811 122.001 92.389  1.00 59.34  ? 282 PHE A CA  1 
ATOM 2232 C C   . PHE A 1 299 ? 105.831 120.755 91.514  1.00 59.34  ? 282 PHE A C   1 
ATOM 2233 O O   . PHE A 1 299 ? 106.505 120.725 90.476  1.00 59.34  ? 282 PHE A O   1 
ATOM 2234 C CB  . PHE A 1 299 ? 106.752 121.826 93.582  1.00 59.34  ? 282 PHE A CB  1 
ATOM 2235 C CG  . PHE A 1 299 ? 107.139 123.113 94.245  1.00 59.34  ? 282 PHE A CG  1 
ATOM 2236 C CD1 . PHE A 1 299 ? 107.288 124.273 93.505  1.00 59.34  ? 282 PHE A CD1 1 
ATOM 2237 C CD2 . PHE A 1 299 ? 107.364 123.162 95.611  1.00 59.34  ? 282 PHE A CD2 1 
ATOM 2238 C CE1 . PHE A 1 299 ? 107.646 125.458 94.115  1.00 59.34  ? 282 PHE A CE1 1 
ATOM 2239 C CE2 . PHE A 1 299 ? 107.723 124.343 96.226  1.00 59.34  ? 282 PHE A CE2 1 
ATOM 2240 C CZ  . PHE A 1 299 ? 107.865 125.493 95.478  1.00 59.34  ? 282 PHE A CZ  1 
ATOM 2241 N N   . ARG A 1 300 ? 105.099 119.714 91.920  1.00 64.12  ? 283 ARG A N   1 
ATOM 2242 C CA  . ARG A 1 300 ? 105.073 118.482 91.142  1.00 64.12  ? 283 ARG A CA  1 
ATOM 2243 C C   . ARG A 1 300 ? 104.486 118.718 89.757  1.00 64.12  ? 283 ARG A C   1 
ATOM 2244 O O   . ARG A 1 300 ? 105.023 118.229 88.759  1.00 64.12  ? 283 ARG A O   1 
ATOM 2245 C CB  . ARG A 1 300 ? 104.283 117.408 91.890  1.00 64.12  ? 283 ARG A CB  1 
ATOM 2246 C CG  . ARG A 1 300 ? 104.363 116.027 91.262  1.00 64.12  ? 283 ARG A CG  1 
ATOM 2247 C CD  . ARG A 1 300 ? 103.344 115.076 91.873  1.00 64.12  ? 283 ARG A CD  1 
ATOM 2248 N NE  . ARG A 1 300 ? 103.127 115.340 93.290  1.00 64.12  ? 283 ARG A NE  1 
ATOM 2249 C CZ  . ARG A 1 300 ? 101.953 115.652 93.822  1.00 64.12  ? 283 ARG A CZ  1 
ATOM 2250 N NH1 . ARG A 1 300 ? 100.861 115.745 93.081  1.00 64.12  ? 283 ARG A NH1 1 
ATOM 2251 N NH2 . ARG A 1 300 ? 101.872 115.876 95.131  1.00 64.12  ? 283 ARG A NH2 1 
ATOM 2252 N N   . LEU A 1 301 ? 103.394 119.482 89.673  1.00 64.86  ? 284 LEU A N   1 
ATOM 2253 C CA  . LEU A 1 301 ? 102.793 119.766 88.373  1.00 64.86  ? 284 LEU A CA  1 
ATOM 2254 C C   . LEU A 1 301 ? 103.702 120.639 87.515  1.00 64.86  ? 284 LEU A C   1 
ATOM 2255 O O   . LEU A 1 301 ? 103.807 120.431 86.300  1.00 64.86  ? 284 LEU A O   1 
ATOM 2256 C CB  . LEU A 1 301 ? 101.429 120.429 88.559  1.00 64.86  ? 284 LEU A CB  1 
ATOM 2257 C CG  . LEU A 1 301 ? 100.468 120.294 87.376  1.00 64.86  ? 284 LEU A CG  1 
ATOM 2258 C CD1 . LEU A 1 301 ? 99.724  118.969 87.440  1.00 64.86  ? 284 LEU A CD1 1 
ATOM 2259 C CD2 . LEU A 1 301 ? 99.494  121.460 87.340  1.00 64.86  ? 284 LEU A CD2 1 
ATOM 2260 N N   . TYR A 1 302 ? 104.368 121.622 88.127  1.00 56.72  ? 285 TYR A N   1 
ATOM 2261 C CA  . TYR A 1 302 ? 105.276 122.483 87.376  1.00 56.72  ? 285 TYR A CA  1 
ATOM 2262 C C   . TYR A 1 302 ? 106.431 121.680 86.791  1.00 56.72  ? 285 TYR A C   1 
ATOM 2263 O O   . TYR A 1 302 ? 106.797 121.849 85.620  1.00 56.72  ? 285 TYR A O   1 
ATOM 2264 C CB  . TYR A 1 302 ? 105.787 123.602 88.285  1.00 56.72  ? 285 TYR A CB  1 
ATOM 2265 C CG  . TYR A 1 302 ? 106.806 124.520 87.652  1.00 56.72  ? 285 TYR A CG  1 
ATOM 2266 C CD1 . TYR A 1 302 ? 106.409 125.638 86.933  1.00 56.72  ? 285 TYR A CD1 1 
ATOM 2267 C CD2 . TYR A 1 302 ? 108.166 124.283 87.796  1.00 56.72  ? 285 TYR A CD2 1 
ATOM 2268 C CE1 . TYR A 1 302 ? 107.337 126.484 86.359  1.00 56.72  ? 285 TYR A CE1 1 
ATOM 2269 C CE2 . TYR A 1 302 ? 109.101 125.123 87.226  1.00 56.72  ? 285 TYR A CE2 1 
ATOM 2270 C CZ  . TYR A 1 302 ? 108.682 126.222 86.510  1.00 56.72  ? 285 TYR A CZ  1 
ATOM 2271 O OH  . TYR A 1 302 ? 109.611 127.062 85.942  1.00 56.72  ? 285 TYR A OH  1 
ATOM 2272 N N   . TYR A 1 303 ? 107.009 120.779 87.587  1.00 53.19  ? 286 TYR A N   1 
ATOM 2273 C CA  . TYR A 1 303 ? 108.113 119.980 87.073  1.00 53.19  ? 286 TYR A CA  1 
ATOM 2274 C C   . TYR A 1 303 ? 107.628 118.902 86.112  1.00 53.19  ? 286 TYR A C   1 
ATOM 2275 O O   . TYR A 1 303 ? 108.383 118.480 85.233  1.00 53.19  ? 286 TYR A O   1 
ATOM 2276 C CB  . TYR A 1 303 ? 108.913 119.384 88.228  1.00 53.19  ? 286 TYR A CB  1 
ATOM 2277 C CG  . TYR A 1 303 ? 109.673 120.441 88.995  1.00 53.19  ? 286 TYR A CG  1 
ATOM 2278 C CD1 . TYR A 1 303 ? 110.446 121.382 88.328  1.00 53.19  ? 286 TYR A CD1 1 
ATOM 2279 C CD2 . TYR A 1 303 ? 109.606 120.513 90.377  1.00 53.19  ? 286 TYR A CD2 1 
ATOM 2280 C CE1 . TYR A 1 303 ? 111.136 122.357 89.016  1.00 53.19  ? 286 TYR A CE1 1 
ATOM 2281 C CE2 . TYR A 1 303 ? 110.294 121.485 91.075  1.00 53.19  ? 286 TYR A CE2 1 
ATOM 2282 C CZ  . TYR A 1 303 ? 111.057 122.404 90.389  1.00 53.19  ? 286 TYR A CZ  1 
ATOM 2283 O OH  . TYR A 1 303 ? 111.743 123.374 91.078  1.00 53.19  ? 286 TYR A OH  1 
ATOM 2284 N N   . TYR A 1 304 ? 106.373 118.466 86.237  1.00 61.22  ? 287 TYR A N   1 
ATOM 2285 C CA  . TYR A 1 304 ? 105.788 117.599 85.218  1.00 61.22  ? 287 TYR A CA  1 
ATOM 2286 C C   . TYR A 1 304 ? 105.681 118.325 83.883  1.00 61.22  ? 287 TYR A C   1 
ATOM 2287 O O   . TYR A 1 304 ? 105.971 117.752 82.824  1.00 61.22  ? 287 TYR A O   1 
ATOM 2288 C CB  . TYR A 1 304 ? 104.417 117.112 85.687  1.00 61.22  ? 287 TYR A CB  1 
ATOM 2289 C CG  . TYR A 1 304 ? 103.630 116.334 84.659  1.00 61.22  ? 287 TYR A CG  1 
ATOM 2290 C CD1 . TYR A 1 304 ? 104.130 115.160 84.114  1.00 61.22  ? 287 TYR A CD1 1 
ATOM 2291 C CD2 . TYR A 1 304 ? 102.378 116.765 84.246  1.00 61.22  ? 287 TYR A CD2 1 
ATOM 2292 C CE1 . TYR A 1 304 ? 103.408 114.443 83.179  1.00 61.22  ? 287 TYR A CE1 1 
ATOM 2293 C CE2 . TYR A 1 304 ? 101.649 116.056 83.313  1.00 61.22  ? 287 TYR A CE2 1 
ATOM 2294 C CZ  . TYR A 1 304 ? 102.168 114.896 82.783  1.00 61.22  ? 287 TYR A CZ  1 
ATOM 2295 O OH  . TYR A 1 304 ? 101.444 114.188 81.852  1.00 61.22  ? 287 TYR A OH  1 
ATOM 2296 N N   . ASN A 1 305 ? 105.269 119.595 83.918  1.00 59.77  ? 288 ASN A N   1 
ATOM 2297 C CA  . ASN A 1 305 ? 105.239 120.401 82.701  1.00 59.77  ? 288 ASN A CA  1 
ATOM 2298 C C   . ASN A 1 305 ? 106.639 120.581 82.125  1.00 59.77  ? 288 ASN A C   1 
ATOM 2299 O O   . ASN A 1 305 ? 106.838 120.494 80.907  1.00 59.77  ? 288 ASN A O   1 
ATOM 2300 C CB  . ASN A 1 305 ? 104.598 121.759 82.989  1.00 59.77  ? 288 ASN A CB  1 
ATOM 2301 C CG  . ASN A 1 305 ? 103.926 122.355 81.771  1.00 59.77  ? 288 ASN A CG  1 
ATOM 2302 O OD1 . ASN A 1 305 ? 103.614 121.649 80.812  1.00 59.77  ? 288 ASN A OD1 1 
ATOM 2303 N ND2 . ASN A 1 305 ? 103.699 123.662 81.801  1.00 59.77  ? 288 ASN A ND2 1 
ATOM 2304 N N   . LYS A 1 306 ? 107.624 120.832 82.988  1.00 55.40  ? 289 LYS A N   1 
ATOM 2305 C CA  . LYS A 1 306 ? 108.998 120.955 82.508  1.00 55.40  ? 289 LYS A CA  1 
ATOM 2306 C C   . LYS A 1 306 ? 109.485 119.654 81.879  1.00 55.40  ? 289 LYS A C   1 
ATOM 2307 O O   . LYS A 1 306 ? 110.161 119.670 80.844  1.00 55.40  ? 289 LYS A O   1 
ATOM 2308 C CB  . LYS A 1 306 ? 109.920 121.382 83.649  1.00 55.40  ? 289 LYS A CB  1 
ATOM 2309 C CG  . LYS A 1 306 ? 109.737 122.828 84.079  1.00 55.40  ? 289 LYS A CG  1 
ATOM 2310 C CD  . LYS A 1 306 ? 109.584 123.740 82.872  1.00 55.40  ? 289 LYS A CD  1 
ATOM 2311 C CE  . LYS A 1 306 ? 109.582 125.202 83.280  1.00 55.40  ? 289 LYS A CE  1 
ATOM 2312 N NZ  . LYS A 1 306 ? 110.714 125.523 84.191  1.00 55.40  ? 289 LYS A NZ  1 
ATOM 2313 N N   . PHE A 1 307 ? 109.145 118.514 82.484  1.00 52.91  ? 290 PHE A N   1 
ATOM 2314 C CA  . PHE A 1 307 ? 109.574 117.229 81.945  1.00 52.91  ? 290 PHE A CA  1 
ATOM 2315 C C   . PHE A 1 307 ? 108.904 116.929 80.609  1.00 52.91  ? 290 PHE A C   1 
ATOM 2316 O O   . PHE A 1 307 ? 109.537 116.364 79.711  1.00 52.91  ? 290 PHE A O   1 
ATOM 2317 C CB  . PHE A 1 307 ? 109.297 116.114 82.952  1.00 52.91  ? 290 PHE A CB  1 
ATOM 2318 C CG  . PHE A 1 307 ? 110.408 115.904 83.941  1.00 52.91  ? 290 PHE A CG  1 
ATOM 2319 C CD1 . PHE A 1 307 ? 111.091 116.983 84.477  1.00 52.91  ? 290 PHE A CD1 1 
ATOM 2320 C CD2 . PHE A 1 307 ? 110.774 114.627 84.330  1.00 52.91  ? 290 PHE A CD2 1 
ATOM 2321 C CE1 . PHE A 1 307 ? 112.114 116.792 85.384  1.00 52.91  ? 290 PHE A CE1 1 
ATOM 2322 C CE2 . PHE A 1 307 ? 111.796 114.430 85.238  1.00 52.91  ? 290 PHE A CE2 1 
ATOM 2323 C CZ  . PHE A 1 307 ? 112.467 115.514 85.765  1.00 52.91  ? 290 PHE A CZ  1 
ATOM 2324 N N   . LYS A 1 308 ? 107.627 117.289 80.452  1.00 61.13  ? 291 LYS A N   1 
ATOM 2325 C CA  . LYS A 1 308 ? 106.997 117.085 79.149  1.00 61.13  ? 291 LYS A CA  1 
ATOM 2326 C C   . LYS A 1 308 ? 107.576 118.029 78.100  1.00 61.13  ? 291 LYS A C   1 
ATOM 2327 O O   . LYS A 1 308 ? 107.682 117.659 76.924  1.00 61.13  ? 291 LYS A O   1 
ATOM 2328 C CB  . LYS A 1 308 ? 105.476 117.233 79.248  1.00 61.13  ? 291 LYS A CB  1 
ATOM 2329 C CG  . LYS A 1 308 ? 104.965 118.646 79.423  1.00 61.13  ? 291 LYS A CG  1 
ATOM 2330 C CD  . LYS A 1 308 ? 103.449 118.694 79.356  1.00 61.13  ? 291 LYS A CD  1 
ATOM 2331 C CE  . LYS A 1 308 ? 102.826 118.376 80.704  1.00 61.13  ? 291 LYS A CE  1 
ATOM 2332 N NZ  . LYS A 1 308 ? 101.462 117.796 80.563  1.00 61.13  ? 291 LYS A NZ  1 
ATOM 2333 N N   . ASP A 1 309 ? 107.978 119.237 78.507  1.00 67.33  ? 292 ASP A N   1 
ATOM 2334 C CA  . ASP A 1 309 ? 108.689 120.127 77.593  1.00 67.33  ? 292 ASP A CA  1 
ATOM 2335 C C   . ASP A 1 309 ? 110.006 119.486 77.157  1.00 67.33  ? 292 ASP A C   1 
ATOM 2336 O O   . ASP A 1 309 ? 110.358 119.507 75.970  1.00 67.33  ? 292 ASP A O   1 
ATOM 2337 C CB  . ASP A 1 309 ? 108.899 121.484 78.288  1.00 67.33  ? 292 ASP A CB  1 
ATOM 2338 C CG  . ASP A 1 309 ? 109.968 122.376 77.632  1.00 67.33  ? 292 ASP A CG  1 
ATOM 2339 O OD1 . ASP A 1 309 ? 110.494 122.080 76.541  1.00 67.33  ? 292 ASP A OD1 1 
ATOM 2340 O OD2 . ASP A 1 309 ? 110.293 123.414 78.250  1.00 67.33  ? 292 ASP A OD2 1 
ATOM 2341 N N   . ILE A 1 310 ? 110.731 118.885 78.105  1.00 54.39  ? 293 ILE A N   1 
ATOM 2342 C CA  . ILE A 1 310 ? 111.982 118.201 77.778  1.00 54.39  ? 293 ILE A CA  1 
ATOM 2343 C C   . ILE A 1 310 ? 111.723 117.041 76.825  1.00 54.39  ? 293 ILE A C   1 
ATOM 2344 O O   . ILE A 1 310 ? 112.500 116.794 75.895  1.00 54.39  ? 293 ILE A O   1 
ATOM 2345 C CB  . ILE A 1 310 ? 112.687 117.724 79.063  1.00 54.39  ? 293 ILE A CB  1 
ATOM 2346 C CG1 . ILE A 1 310 ? 113.053 118.910 79.957  1.00 54.39  ? 293 ILE A CG1 1 
ATOM 2347 C CG2 . ILE A 1 310 ? 113.926 116.906 78.728  1.00 54.39  ? 293 ILE A CG2 1 
ATOM 2348 C CD1 . ILE A 1 310 ? 113.639 120.081 79.213  1.00 54.39  ? 293 ILE A CD1 1 
ATOM 2349 N N   . ALA A 1 311 ? 110.639 116.298 77.056  1.00 63.50  ? 294 ALA A N   1 
ATOM 2350 C CA  . ALA A 1 311 ? 110.299 115.184 76.176  1.00 63.50  ? 294 ALA A CA  1 
ATOM 2351 C C   . ALA A 1 311 ? 110.012 115.669 74.761  1.00 63.50  ? 294 ALA A C   1 
ATOM 2352 O O   . ALA A 1 311 ? 110.450 115.051 73.784  1.00 63.50  ? 294 ALA A O   1 
ATOM 2353 C CB  . ALA A 1 311 ? 109.102 114.417 76.737  1.00 63.50  ? 294 ALA A CB  1 
ATOM 2354 N N   . SER A 1 312 ? 109.279 116.777 74.631  1.00 67.26  ? 295 SER A N   1 
ATOM 2355 C CA  . SER A 1 312 ? 109.035 117.348 73.308  1.00 67.26  ? 295 SER A CA  1 
ATOM 2356 C C   . SER A 1 312 ? 110.338 117.782 72.644  1.00 67.26  ? 295 SER A C   1 
ATOM 2357 O O   . SER A 1 312 ? 110.536 117.564 71.440  1.00 67.26  ? 295 SER A O   1 
ATOM 2358 C CB  . SER A 1 312 ? 108.068 118.527 73.417  1.00 67.26  ? 295 SER A CB  1 
ATOM 2359 O OG  . SER A 1 312 ? 107.802 119.089 72.145  1.00 67.26  ? 295 SER A OG  1 
ATOM 2360 N N   . THR A 1 313 ? 111.235 118.404 73.415  1.00 64.38  ? 296 THR A N   1 
ATOM 2361 C CA  . THR A 1 313 ? 112.522 118.827 72.869  1.00 64.38  ? 296 THR A CA  1 
ATOM 2362 C C   . THR A 1 313 ? 113.324 117.633 72.367  1.00 64.38  ? 296 THR A C   1 
ATOM 2363 O O   . THR A 1 313 ? 113.936 117.690 71.294  1.00 64.38  ? 296 THR A O   1 
ATOM 2364 C CB  . THR A 1 313 ? 113.312 119.599 73.928  1.00 64.38  ? 296 THR A CB  1 
ATOM 2365 O OG1 . THR A 1 313 ? 112.673 120.856 74.182  1.00 64.38  ? 296 THR A OG1 1 
ATOM 2366 C CG2 . THR A 1 313 ? 114.740 119.849 73.462  1.00 64.38  ? 296 THR A CG2 1 
ATOM 2367 N N   . LEU A 1 314 ? 113.329 116.540 73.132  1.00 62.55  ? 297 LEU A N   1 
ATOM 2368 C CA  . LEU A 1 314 ? 113.986 115.318 72.679  1.00 62.55  ? 297 LEU A CA  1 
ATOM 2369 C C   . LEU A 1 314 ? 113.326 114.774 71.419  1.00 62.55  ? 297 LEU A C   1 
ATOM 2370 O O   . LEU A 1 314 ? 114.007 114.271 70.518  1.00 62.55  ? 297 LEU A O   1 
ATOM 2371 C CB  . LEU A 1 314 ? 113.966 114.265 73.788  1.00 62.55  ? 297 LEU A CB  1 
ATOM 2372 C CG  . LEU A 1 314 ? 114.932 114.457 74.957  1.00 62.55  ? 297 LEU A CG  1 
ATOM 2373 C CD1 . LEU A 1 314 ? 114.546 113.557 76.117  1.00 62.55  ? 297 LEU A CD1 1 
ATOM 2374 C CD2 . LEU A 1 314 ? 116.356 114.174 74.512  1.00 62.55  ? 297 LEU A CD2 1 
ATOM 2375 N N   . ASN A 1 315 ? 111.996 114.858 71.346  1.00 75.10  ? 298 ASN A N   1 
ATOM 2376 C CA  . ASN A 1 315 ? 111.281 114.350 70.180  1.00 75.10  ? 298 ASN A CA  1 
ATOM 2377 C C   . ASN A 1 315 ? 111.657 115.110 68.915  1.00 75.10  ? 298 ASN A C   1 
ATOM 2378 O O   . ASN A 1 315 ? 111.875 114.504 67.860  1.00 75.10  ? 298 ASN A O   1 
ATOM 2379 C CB  . ASN A 1 315 ? 109.773 114.429 70.415  1.00 75.10  ? 298 ASN A CB  1 
ATOM 2380 C CG  . ASN A 1 315 ? 109.234 113.219 71.143  1.00 75.10  ? 298 ASN A CG  1 
ATOM 2381 O OD1 . ASN A 1 315 ? 108.604 112.351 70.542  1.00 75.10  ? 298 ASN A OD1 1 
ATOM 2382 N ND2 . ASN A 1 315 ? 109.475 113.156 72.446  1.00 75.10  ? 298 ASN A ND2 1 
ATOM 2383 N N   . LYS A 1 316 ? 111.743 116.439 68.998  1.00 76.45  ? 299 LYS A N   1 
ATOM 2384 C CA  . LYS A 1 316 ? 111.953 117.235 67.793  1.00 76.45  ? 299 LYS A CA  1 
ATOM 2385 C C   . LYS A 1 316 ? 113.403 117.265 67.325  1.00 76.45  ? 299 LYS A C   1 
ATOM 2386 O O   . LYS A 1 316 ? 113.653 117.649 66.178  1.00 76.45  ? 299 LYS A O   1 
ATOM 2387 C CB  . LYS A 1 316 ? 111.464 118.670 68.011  1.00 76.45  ? 299 LYS A CB  1 
ATOM 2388 C CG  . LYS A 1 316 ? 112.070 119.362 69.216  1.00 76.45  ? 299 LYS A CG  1 
ATOM 2389 C CD  . LYS A 1 316 ? 111.460 120.739 69.421  1.00 76.45  ? 299 LYS A CD  1 
ATOM 2390 C CE  . LYS A 1 316 ? 109.947 120.664 69.538  1.00 76.45  ? 299 LYS A CE  1 
ATOM 2391 N NZ  . LYS A 1 316 ? 109.513 120.360 70.928  1.00 76.45  ? 299 LYS A NZ  1 
ATOM 2392 N N   . ALA A 1 317 ? 114.357 116.871 68.165  1.00 77.49  ? 300 ALA A N   1 
ATOM 2393 C CA  . ALA A 1 317 ? 115.766 116.941 67.797  1.00 77.49  ? 300 ALA A CA  1 
ATOM 2394 C C   . ALA A 1 317 ? 116.148 115.795 66.868  1.00 77.49  ? 300 ALA A C   1 
ATOM 2395 O O   . ALA A 1 317 ? 115.741 114.648 67.075  1.00 77.49  ? 300 ALA A O   1 
ATOM 2396 C CB  . ALA A 1 317 ? 116.642 116.913 69.048  1.00 77.49  ? 300 ALA A CB  1 
ATOM 2397 N N   . LYS A 1 318 ? 116.961 116.110 65.854  1.00 85.64  ? 301 LYS A N   1 
ATOM 2398 C CA  . LYS A 1 318 ? 117.345 115.150 64.826  1.00 85.64  ? 301 LYS A CA  1 
ATOM 2399 C C   . LYS A 1 318 ? 118.846 115.006 64.610  1.00 85.64  ? 301 LYS A C   1 
ATOM 2400 O O   . LYS A 1 318 ? 119.260 114.031 63.974  1.00 85.64  ? 301 LYS A O   1 
ATOM 2401 C CB  . LYS A 1 318 ? 116.706 115.522 63.475  1.00 85.64  ? 301 LYS A CB  1 
ATOM 2402 C CG  . LYS A 1 318 ? 115.220 115.204 63.337  1.00 85.64  ? 301 LYS A CG  1 
ATOM 2403 C CD  . LYS A 1 318 ? 114.801 114.033 64.209  1.00 85.64  ? 301 LYS A CD  1 
ATOM 2404 C CE  . LYS A 1 318 ? 113.401 113.552 63.869  1.00 85.64  ? 301 LYS A CE  1 
ATOM 2405 N NZ  . LYS A 1 318 ? 112.777 112.823 65.009  1.00 85.64  ? 301 LYS A NZ  1 
ATOM 2406 N N   . SER A 1 319 ? 119.669 115.931 65.101  1.00 85.08  ? 302 SER A N   1 
ATOM 2407 C CA  . SER A 1 319 ? 121.094 115.905 64.799  1.00 85.08  ? 302 SER A CA  1 
ATOM 2408 C C   . SER A 1 319 ? 121.912 116.143 66.060  1.00 85.08  ? 302 SER A C   1 
ATOM 2409 O O   . SER A 1 319 ? 121.483 116.847 66.978  1.00 85.08  ? 302 SER A O   1 
ATOM 2410 C CB  . SER A 1 319 ? 121.463 116.950 63.738  1.00 85.08  ? 302 SER A CB  1 
ATOM 2411 O OG  . SER A 1 319 ? 121.410 118.260 64.272  1.00 85.08  ? 302 SER A OG  1 
ATOM 2412 N N   . ILE A 1 320 ? 123.102 115.545 66.088  1.00 82.65  ? 303 ILE A N   1 
ATOM 2413 C CA  . ILE A 1 320 ? 124.070 115.726 67.163  1.00 82.65  ? 303 ILE A CA  1 
ATOM 2414 C C   . ILE A 1 320 ? 125.320 116.363 66.574  1.00 82.65  ? 303 ILE A C   1 
ATOM 2415 O O   . ILE A 1 320 ? 125.890 115.843 65.608  1.00 82.65  ? 303 ILE A O   1 
ATOM 2416 C CB  . ILE A 1 320 ? 124.419 114.394 67.852  1.00 82.65  ? 303 ILE A CB  1 
ATOM 2417 C CG1 . ILE A 1 320 ? 123.172 113.762 68.469  1.00 82.65  ? 303 ILE A CG1 1 
ATOM 2418 C CG2 . ILE A 1 320 ? 125.489 114.609 68.911  1.00 82.65  ? 303 ILE A CG2 1 
ATOM 2419 C CD1 . ILE A 1 320 ? 122.623 114.529 69.646  1.00 82.65  ? 303 ILE A CD1 1 
ATOM 2420 N N   . VAL A 1 321 ? 125.742 117.482 67.154  1.00 75.15  ? 304 VAL A N   1 
ATOM 2421 C CA  . VAL A 1 321 ? 126.955 118.179 66.745  1.00 75.15  ? 304 VAL A CA  1 
ATOM 2422 C C   . VAL A 1 321 ? 127.884 118.272 67.947  1.00 75.15  ? 304 VAL A C   1 
ATOM 2423 O O   . VAL A 1 321 ? 127.468 118.701 69.030  1.00 75.15  ? 304 VAL A O   1 
ATOM 2424 C CB  . VAL A 1 321 ? 126.647 119.576 66.174  1.00 75.15  ? 304 VAL A CB  1 
ATOM 2425 C CG1 . VAL A 1 321 ? 126.101 119.458 64.762  1.00 75.15  ? 304 VAL A CG1 1 
ATOM 2426 C CG2 . VAL A 1 321 ? 125.656 120.311 67.064  1.00 75.15  ? 304 VAL A CG2 1 
ATOM 2427 N N   . GLY A 1 322 ? 129.134 117.857 67.760  1.00 75.86  ? 305 GLY A N   1 
ATOM 2428 C CA  . GLY A 1 322 ? 130.116 117.931 68.822  1.00 75.86  ? 305 GLY A CA  1 
ATOM 2429 C C   . GLY A 1 322 ? 130.876 116.641 69.051  1.00 75.86  ? 305 GLY A C   1 
ATOM 2430 O O   . GLY A 1 322 ? 132.064 116.670 69.385  1.00 75.86  ? 305 GLY A O   1 
ATOM 2431 N N   . THR A 1 323 ? 130.207 115.501 68.887  1.00 83.01  ? 306 THR A N   1 
ATOM 2432 C CA  . THR A 1 323 ? 130.819 114.194 69.090  1.00 83.01  ? 306 THR A CA  1 
ATOM 2433 C C   . THR A 1 323 ? 130.503 113.292 67.904  1.00 83.01  ? 306 THR A C   1 
ATOM 2434 O O   . THR A 1 323 ? 129.794 113.674 66.969  1.00 83.01  ? 306 THR A O   1 
ATOM 2435 C CB  . THR A 1 323 ? 130.338 113.529 70.387  1.00 83.01  ? 306 THR A CB  1 
ATOM 2436 O OG1 . THR A 1 323 ? 129.120 112.816 70.139  1.00 83.01  ? 306 THR A OG1 1 
ATOM 2437 C CG2 . THR A 1 323 ? 130.108 114.553 71.478  1.00 83.01  ? 306 THR A CG2 1 
ATOM 2438 N N   . THR A 1 324 ? 131.043 112.078 67.957  1.00 89.96  ? 307 THR A N   1 
ATOM 2439 C CA  . THR A 1 324 ? 130.750 111.037 66.983  1.00 89.96  ? 307 THR A CA  1 
ATOM 2440 C C   . THR A 1 324 ? 129.595 110.145 67.429  1.00 89.96  ? 307 THR A C   1 
ATOM 2441 O O   . THR A 1 324 ? 129.165 109.274 66.665  1.00 89.96  ? 307 THR A O   1 
ATOM 2442 C CB  . THR A 1 324 ? 132.010 110.196 66.732  1.00 89.96  ? 307 THR A CB  1 
ATOM 2443 O OG1 . THR A 1 324 ? 133.144 111.065 66.627  1.00 89.96  ? 307 THR A OG1 1 
ATOM 2444 C CG2 . THR A 1 324 ? 131.898 109.410 65.431  1.00 89.96  ? 307 THR A CG2 1 
ATOM 2445 N N   . ALA A 1 325 ? 129.073 110.357 68.636  1.00 93.63  ? 308 ALA A N   1 
ATOM 2446 C CA  . ALA A 1 325 ? 127.981 109.537 69.141  1.00 93.63  ? 308 ALA A CA  1 
ATOM 2447 C C   . ALA A 1 325 ? 126.735 109.708 68.281  1.00 93.63  ? 308 ALA A C   1 
ATOM 2448 O O   . ALA A 1 325 ? 126.390 110.818 67.867  1.00 93.63  ? 308 ALA A O   1 
ATOM 2449 C CB  . ALA A 1 325 ? 127.672 109.900 70.594  1.00 93.63  ? 308 ALA A CB  1 
ATOM 2450 N N   . SER A 1 326 ? 126.059 108.594 68.015  1.00 92.18  ? 309 SER A N   1 
ATOM 2451 C CA  . SER A 1 326 ? 124.893 108.596 67.149  1.00 92.18  ? 309 SER A CA  1 
ATOM 2452 C C   . SER A 1 326 ? 123.659 109.092 67.900  1.00 92.18  ? 309 SER A C   1 
ATOM 2453 O O   . SER A 1 326 ? 123.676 109.316 69.113  1.00 92.18  ? 309 SER A O   1 
ATOM 2454 C CB  . SER A 1 326 ? 124.645 107.197 66.586  1.00 92.18  ? 309 SER A CB  1 
ATOM 2455 O OG  . SER A 1 326 ? 124.201 106.311 67.599  1.00 92.18  ? 309 SER A OG  1 
ATOM 2456 N N   . LEU A 1 327 ? 122.572 109.271 67.145  1.00 80.96  ? 310 LEU A N   1 
ATOM 2457 C CA  . LEU A 1 327 ? 121.314 109.717 67.737  1.00 80.96  ? 310 LEU A CA  1 
ATOM 2458 C C   . LEU A 1 327 ? 120.769 108.695 68.726  1.00 80.96  ? 310 LEU A C   1 
ATOM 2459 O O   . LEU A 1 327 ? 120.267 109.062 69.794  1.00 80.96  ? 310 LEU A O   1 
ATOM 2460 C CB  . LEU A 1 327 ? 120.287 109.987 66.638  1.00 80.96  ? 310 LEU A CB  1 
ATOM 2461 C CG  . LEU A 1 327 ? 119.316 111.149 66.849  1.00 80.96  ? 310 LEU A CG  1 
ATOM 2462 C CD1 . LEU A 1 327 ? 120.052 112.410 67.268  1.00 80.96  ? 310 LEU A CD1 1 
ATOM 2463 C CD2 . LEU A 1 327 ? 118.490 111.390 65.595  1.00 80.96  ? 310 LEU A CD2 1 
ATOM 2464 N N   . GLN A 1 328 ? 120.846 107.408 68.379  1.00 86.95  ? 311 GLN A N   1 
ATOM 2465 C CA  . GLN A 1 328 ? 120.213 106.374 69.193  1.00 86.95  ? 311 GLN A CA  1 
ATOM 2466 C C   . GLN A 1 328 ? 120.839 106.283 70.579  1.00 86.95  ? 311 GLN A C   1 
ATOM 2467 O O   . GLN A 1 328 ? 120.126 106.155 71.583  1.00 86.95  ? 311 GLN A O   1 
ATOM 2468 C CB  . GLN A 1 328 ? 120.299 105.026 68.478  1.00 86.95  ? 311 GLN A CB  1 
ATOM 2469 C CG  . GLN A 1 328 ? 119.783 103.852 69.292  1.00 86.95  ? 311 GLN A CG  1 
ATOM 2470 C CD  . GLN A 1 328 ? 120.077 102.517 68.636  1.00 86.95  ? 311 GLN A CD  1 
ATOM 2471 O OE1 . GLN A 1 328 ? 120.673 102.460 67.560  1.00 86.95  ? 311 GLN A OE1 1 
ATOM 2472 N NE2 . GLN A 1 328 ? 119.660 101.435 69.282  1.00 86.95  ? 311 GLN A NE2 1 
ATOM 2473 N N   . TYR A 1 329 ? 122.171 106.342 70.656  1.00 73.24  ? 312 TYR A N   1 
ATOM 2474 C CA  . TYR A 1 329 ? 122.844 106.199 71.944  1.00 73.24  ? 312 TYR A CA  1 
ATOM 2475 C C   . TYR A 1 329 ? 122.465 107.331 72.890  1.00 73.24  ? 312 TYR A C   1 
ATOM 2476 O O   . TYR A 1 329 ? 122.136 107.098 74.059  1.00 73.24  ? 312 TYR A O   1 
ATOM 2477 C CB  . TYR A 1 329 ? 124.359 106.151 71.739  1.00 73.24  ? 312 TYR A CB  1 
ATOM 2478 C CG  . TYR A 1 329 ? 125.157 106.462 72.985  1.00 73.24  ? 312 TYR A CG  1 
ATOM 2479 C CD1 . TYR A 1 329 ? 125.153 105.596 74.070  1.00 73.24  ? 312 TYR A CD1 1 
ATOM 2480 C CD2 . TYR A 1 329 ? 125.912 107.624 73.078  1.00 73.24  ? 312 TYR A CD2 1 
ATOM 2481 C CE1 . TYR A 1 329 ? 125.881 105.875 75.211  1.00 73.24  ? 312 TYR A CE1 1 
ATOM 2482 C CE2 . TYR A 1 329 ? 126.642 107.913 74.216  1.00 73.24  ? 312 TYR A CE2 1 
ATOM 2483 C CZ  . TYR A 1 329 ? 126.623 107.035 75.279  1.00 73.24  ? 312 TYR A CZ  1 
ATOM 2484 O OH  . TYR A 1 329 ? 127.348 107.319 76.413  1.00 73.24  ? 312 TYR A OH  1 
ATOM 2485 N N   . MET A 1 330 ? 122.482 108.570 72.394  1.00 63.73  ? 313 MET A N   1 
ATOM 2486 C CA  . MET A 1 330 ? 122.141 109.699 73.250  1.00 63.73  ? 313 MET A CA  1 
ATOM 2487 C C   . MET A 1 330 ? 120.654 109.727 73.574  1.00 63.73  ? 313 MET A C   1 
ATOM 2488 O O   . MET A 1 330 ? 120.269 110.140 74.675  1.00 63.73  ? 313 MET A O   1 
ATOM 2489 C CB  . MET A 1 330 ? 122.576 111.009 72.597  1.00 63.73  ? 313 MET A CB  1 
ATOM 2490 C CG  . MET A 1 330 ? 122.665 112.156 73.579  1.00 63.73  ? 313 MET A CG  1 
ATOM 2491 S SD  . MET A 1 330 ? 124.214 112.094 74.496  1.00 63.73  ? 313 MET A SD  1 
ATOM 2492 C CE  . MET A 1 330 ? 124.336 113.783 75.061  1.00 63.73  ? 313 MET A CE  1 
ATOM 2493 N N   . LYS A 1 331 ? 119.807 109.289 72.640  1.00 72.39  ? 314 LYS A N   1 
ATOM 2494 C CA  . LYS A 1 331 ? 118.382 109.174 72.929  1.00 72.39  ? 314 LYS A CA  1 
ATOM 2495 C C   . LYS A 1 331 ? 118.141 108.195 74.070  1.00 72.39  ? 314 LYS A C   1 
ATOM 2496 O O   . LYS A 1 331 ? 117.375 108.479 74.996  1.00 72.39  ? 314 LYS A O   1 
ATOM 2497 C CB  . LYS A 1 331 ? 117.625 108.735 71.675  1.00 72.39  ? 314 LYS A CB  1 
ATOM 2498 C CG  . LYS A 1 331 ? 117.136 109.875 70.799  1.00 72.39  ? 314 LYS A CG  1 
ATOM 2499 C CD  . LYS A 1 331 ? 116.165 109.371 69.741  1.00 72.39  ? 314 LYS A CD  1 
ATOM 2500 C CE  . LYS A 1 331 ? 115.568 110.516 68.941  1.00 72.39  ? 314 LYS A CE  1 
ATOM 2501 N NZ  . LYS A 1 331 ? 114.293 110.123 68.280  1.00 72.39  ? 314 LYS A NZ  1 
ATOM 2502 N N   . ASN A 1 332 ? 118.805 107.037 74.025  1.00 65.63  ? 315 ASN A N   1 
ATOM 2503 C CA  . ASN A 1 332 ? 118.674 106.063 75.103  1.00 65.63  ? 315 ASN A CA  1 
ATOM 2504 C C   . ASN A 1 332 ? 119.225 106.612 76.413  1.00 65.63  ? 315 ASN A C   1 
ATOM 2505 O O   . ASN A 1 332 ? 118.640 106.395 77.483  1.00 65.63  ? 315 ASN A O   1 
ATOM 2506 C CB  . ASN A 1 332 ? 119.384 104.764 74.723  1.00 65.63  ? 315 ASN A CB  1 
ATOM 2507 C CG  . ASN A 1 332 ? 119.029 103.615 75.643  1.00 65.63  ? 315 ASN A CG  1 
ATOM 2508 O OD1 . ASN A 1 332 ? 119.626 103.450 76.707  1.00 65.63  ? 315 ASN A OD1 1 
ATOM 2509 N ND2 . ASN A 1 332 ? 118.054 102.810 75.237  1.00 65.63  ? 315 ASN A ND2 1 
ATOM 2510 N N   . VAL A 1 333 ? 120.351 107.327 76.349  1.00 60.56  ? 316 VAL A N   1 
ATOM 2511 C CA  . VAL A 1 333 ? 120.952 107.882 77.558  1.00 60.56  ? 316 VAL A CA  1 
ATOM 2512 C C   . VAL A 1 333 ? 120.007 108.878 78.218  1.00 60.56  ? 316 VAL A C   1 
ATOM 2513 O O   . VAL A 1 333 ? 119.793 108.841 79.435  1.00 60.56  ? 316 VAL A O   1 
ATOM 2514 C CB  . VAL A 1 333 ? 122.314 108.520 77.229  1.00 60.56  ? 316 VAL A CB  1 
ATOM 2515 C CG1 . VAL A 1 333 ? 122.667 109.586 78.251  1.00 60.56  ? 316 VAL A CG1 1 
ATOM 2516 C CG2 . VAL A 1 333 ? 123.395 107.454 77.174  1.00 60.56  ? 316 VAL A CG2 1 
ATOM 2517 N N   . PHE A 1 334 ? 119.404 109.768 77.428  1.00 57.23  ? 317 PHE A N   1 
ATOM 2518 C CA  . PHE A 1 334 ? 118.494 110.748 78.011  1.00 57.23  ? 317 PHE A CA  1 
ATOM 2519 C C   . PHE A 1 334 ? 117.179 110.112 78.447  1.00 57.23  ? 317 PHE A C   1 
ATOM 2520 O O   . PHE A 1 334 ? 116.569 110.568 79.423  1.00 57.23  ? 317 PHE A O   1 
ATOM 2521 C CB  . PHE A 1 334 ? 118.246 111.891 77.031  1.00 57.23  ? 317 PHE A CB  1 
ATOM 2522 C CG  . PHE A 1 334 ? 119.300 112.955 77.076  1.00 57.23  ? 317 PHE A CG  1 
ATOM 2523 C CD1 . PHE A 1 334 ? 119.576 113.619 78.260  1.00 57.23  ? 317 PHE A CD1 1 
ATOM 2524 C CD2 . PHE A 1 334 ? 120.016 113.293 75.942  1.00 57.23  ? 317 PHE A CD2 1 
ATOM 2525 C CE1 . PHE A 1 334 ? 120.547 114.596 78.312  1.00 57.23  ? 317 PHE A CE1 1 
ATOM 2526 C CE2 . PHE A 1 334 ? 120.987 114.274 75.987  1.00 57.23  ? 317 PHE A CE2 1 
ATOM 2527 C CZ  . PHE A 1 334 ? 121.253 114.926 77.174  1.00 57.23  ? 317 PHE A CZ  1 
ATOM 2528 N N   . LYS A 1 335 ? 116.727 109.066 77.749  1.00 62.87  ? 318 LYS A N   1 
ATOM 2529 C CA  . LYS A 1 335 ? 115.551 108.333 78.204  1.00 62.87  ? 318 LYS A CA  1 
ATOM 2530 C C   . LYS A 1 335 ? 115.795 107.711 79.571  1.00 62.87  ? 318 LYS A C   1 
ATOM 2531 O O   . LYS A 1 335 ? 114.934 107.777 80.454  1.00 62.87  ? 318 LYS A O   1 
ATOM 2532 C CB  . LYS A 1 335 ? 115.173 107.259 77.185  1.00 62.87  ? 318 LYS A CB  1 
ATOM 2533 C CG  . LYS A 1 335 ? 114.162 106.250 77.702  1.00 62.87  ? 318 LYS A CG  1 
ATOM 2534 C CD  . LYS A 1 335 ? 114.116 105.012 76.825  1.00 62.87  ? 318 LYS A CD  1 
ATOM 2535 C CE  . LYS A 1 335 ? 113.246 103.932 77.446  1.00 62.87  ? 318 LYS A CE  1 
ATOM 2536 N NZ  . LYS A 1 335 ? 113.127 102.738 76.564  1.00 62.87  ? 318 LYS A NZ  1 
ATOM 2537 N N   . GLU A 1 336 ? 116.965 107.097 79.762  1.00 59.55  ? 319 GLU A N   1 
ATOM 2538 C CA  . GLU A 1 336 ? 117.311 106.565 81.076  1.00 59.55  ? 319 GLU A CA  1 
ATOM 2539 C C   . GLU A 1 336 ? 117.480 107.677 82.102  1.00 59.55  ? 319 GLU A C   1 
ATOM 2540 O O   . GLU A 1 336 ? 117.182 107.478 83.285  1.00 59.55  ? 319 GLU A O   1 
ATOM 2541 C CB  . GLU A 1 336 ? 118.588 105.728 80.991  1.00 59.55  ? 319 GLU A CB  1 
ATOM 2542 C CG  . GLU A 1 336 ? 118.484 104.519 80.077  1.00 59.55  ? 319 GLU A CG  1 
ATOM 2543 C CD  . GLU A 1 336 ? 117.781 103.349 80.734  1.00 59.55  ? 319 GLU A CD  1 
ATOM 2544 O OE1 . GLU A 1 336 ? 117.477 103.436 81.942  1.00 59.55  ? 319 GLU A OE1 1 
ATOM 2545 O OE2 . GLU A 1 336 ? 117.533 102.339 80.042  1.00 59.55  ? 319 GLU A OE2 1 
ATOM 2546 N N   . LYS A 1 337 ? 117.961 108.845 81.672  1.00 54.10  ? 320 LYS A N   1 
ATOM 2547 C CA  . LYS A 1 337 ? 118.132 109.964 82.593  1.00 54.10  ? 320 LYS A CA  1 
ATOM 2548 C C   . LYS A 1 337 ? 116.792 110.460 83.124  1.00 54.10  ? 320 LYS A C   1 
ATOM 2549 O O   . LYS A 1 337 ? 116.639 110.685 84.330  1.00 54.10  ? 320 LYS A O   1 
ATOM 2550 C CB  . LYS A 1 337 ? 118.889 111.097 81.897  1.00 54.10  ? 320 LYS A CB  1 
ATOM 2551 C CG  . LYS A 1 337 ? 119.601 112.056 82.840  1.00 54.10  ? 320 LYS A CG  1 
ATOM 2552 C CD  . LYS A 1 337 ? 118.700 113.213 83.252  1.00 54.10  ? 320 LYS A CD  1 
ATOM 2553 C CE  . LYS A 1 337 ? 119.461 114.247 84.065  1.00 54.10  ? 320 LYS A CE  1 
ATOM 2554 N NZ  . LYS A 1 337 ? 118.785 115.573 84.051  1.00 54.10  ? 320 LYS A NZ  1 
ATOM 2555 N N   . TYR A 1 338 ? 115.808 110.633 82.244  1.00 54.77  ? 321 TYR A N   1 
ATOM 2556 C CA  . TYR A 1 338 ? 114.534 111.226 82.631  1.00 54.77  ? 321 TYR A CA  1 
ATOM 2557 C C   . TYR A 1 338 ? 113.411 110.209 82.791  1.00 54.77  ? 321 TYR A C   1 
ATOM 2558 O O   . TYR A 1 338 ? 112.306 110.594 83.186  1.00 54.77  ? 321 TYR A O   1 
ATOM 2559 C CB  . TYR A 1 338 ? 114.118 112.294 81.615  1.00 54.77  ? 321 TYR A CB  1 
ATOM 2560 C CG  . TYR A 1 338 ? 114.985 113.530 81.652  1.00 54.77  ? 321 TYR A CG  1 
ATOM 2561 C CD1 . TYR A 1 338 ? 114.953 114.390 82.741  1.00 54.77  ? 321 TYR A CD1 1 
ATOM 2562 C CD2 . TYR A 1 338 ? 115.840 113.835 80.602  1.00 54.77  ? 321 TYR A CD2 1 
ATOM 2563 C CE1 . TYR A 1 338 ? 115.744 115.519 82.782  1.00 54.77  ? 321 TYR A CE1 1 
ATOM 2564 C CE2 . TYR A 1 338 ? 116.635 114.962 80.635  1.00 54.77  ? 321 TYR A CE2 1 
ATOM 2565 C CZ  . TYR A 1 338 ? 116.583 115.800 81.727  1.00 54.77  ? 321 TYR A CZ  1 
ATOM 2566 O OH  . TYR A 1 338 ? 117.374 116.924 81.765  1.00 54.77  ? 321 TYR A OH  1 
ATOM 2567 N N   . LEU A 1 339 ? 113.665 108.934 82.507  1.00 59.37  ? 322 LEU A N   1 
ATOM 2568 C CA  . LEU A 1 339 ? 112.665 107.872 82.624  1.00 59.37  ? 322 LEU A CA  1 
ATOM 2569 C C   . LEU A 1 339 ? 111.402 108.224 81.837  1.00 59.37  ? 322 LEU A C   1 
ATOM 2570 O O   . LEU A 1 339 ? 110.304 108.347 82.383  1.00 59.37  ? 322 LEU A O   1 
ATOM 2571 C CB  . LEU A 1 339 ? 112.344 107.585 84.093  1.00 59.37  ? 322 LEU A CB  1 
ATOM 2572 C CG  . LEU A 1 339 ? 113.234 106.552 84.785  1.00 59.37  ? 322 LEU A CG  1 
ATOM 2573 C CD1 . LEU A 1 339 ? 112.919 106.479 86.272  1.00 59.37  ? 322 LEU A CD1 1 
ATOM 2574 C CD2 . LEU A 1 339 ? 113.086 105.186 84.133  1.00 59.37  ? 322 LEU A CD2 1 
ATOM 2575 N N   . LEU A 1 340 ? 111.580 108.388 80.531  1.00 68.57  ? 323 LEU A N   1 
ATOM 2576 C CA  . LEU A 1 340 ? 110.496 108.755 79.632  1.00 68.57  ? 323 LEU A CA  1 
ATOM 2577 C C   . LEU A 1 340 ? 110.020 107.530 78.862  1.00 68.57  ? 323 LEU A C   1 
ATOM 2578 O O   . LEU A 1 340 ? 110.825 106.695 78.441  1.00 68.57  ? 323 LEU A O   1 
ATOM 2579 C CB  . LEU A 1 340 ? 110.940 109.847 78.657  1.00 68.57  ? 323 LEU A CB  1 
ATOM 2580 C CG  . LEU A 1 340 ? 111.504 111.121 79.289  1.00 68.57  ? 323 LEU A CG  1 
ATOM 2581 C CD1 . LEU A 1 340 ? 111.743 112.188 78.232  1.00 68.57  ? 323 LEU A CD1 1 
ATOM 2582 C CD2 . LEU A 1 340 ? 110.585 111.637 80.383  1.00 68.57  ? 323 LEU A CD2 1 
ATOM 2583 N N   . SER A 1 341 ? 108.702 107.432 78.681  1.00 81.95  ? 324 SER A N   1 
ATOM 2584 C CA  . SER A 1 341 ? 108.089 106.278 78.022  1.00 81.95  ? 324 SER A CA  1 
ATOM 2585 C C   . SER A 1 341 ? 108.082 106.513 76.514  1.00 81.95  ? 324 SER A C   1 
ATOM 2586 O O   . SER A 1 341 ? 107.132 107.042 75.933  1.00 81.95  ? 324 SER A O   1 
ATOM 2587 C CB  . SER A 1 341 ? 106.685 106.038 78.563  1.00 81.95  ? 324 SER A CB  1 
ATOM 2588 O OG  . SER A 1 341 ? 105.938 107.241 78.591  1.00 81.95  ? 324 SER A OG  1 
ATOM 2589 N N   . GLU A 1 342 ? 109.175 106.109 75.874  1.00 88.70  ? 325 GLU A N   1 
ATOM 2590 C CA  . GLU A 1 342 ? 109.276 106.182 74.423  1.00 88.70  ? 325 GLU A CA  1 
ATOM 2591 C C   . GLU A 1 342 ? 108.558 104.992 73.798  1.00 88.70  ? 325 GLU A C   1 
ATOM 2592 O O   . GLU A 1 342 ? 108.757 103.847 74.215  1.00 88.70  ? 325 GLU A O   1 
ATOM 2593 C CB  . GLU A 1 342 ? 110.741 106.211 73.991  1.00 88.70  ? 325 GLU A CB  1 
ATOM 2594 C CG  . GLU A 1 342 ? 110.972 105.837 72.536  1.00 88.70  ? 325 GLU A CG  1 
ATOM 2595 C CD  . GLU A 1 342 ? 112.428 105.538 72.234  1.00 88.70  ? 325 GLU A CD  1 
ATOM 2596 O OE1 . GLU A 1 342 ? 113.248 105.554 73.176  1.00 88.70  ? 325 GLU A OE1 1 
ATOM 2597 O OE2 . GLU A 1 342 ? 112.753 105.289 71.054  1.00 88.70  ? 325 GLU A OE2 1 
ATOM 2598 N N   . ASP A 1 343 ? 107.725 105.264 72.798  1.00 100.51 ? 326 ASP A N   1 
ATOM 2599 C CA  . ASP A 1 343 ? 106.930 104.231 72.153  1.00 100.51 ? 326 ASP A CA  1 
ATOM 2600 C C   . ASP A 1 343 ? 107.699 103.635 70.973  1.00 100.51 ? 326 ASP A C   1 
ATOM 2601 O O   . ASP A 1 343 ? 108.901 103.860 70.807  1.00 100.51 ? 326 ASP A O   1 
ATOM 2602 C CB  . ASP A 1 343 ? 105.569 104.795 71.741  1.00 100.51 ? 326 ASP A CB  1 
ATOM 2603 C CG  . ASP A 1 343 ? 105.661 105.788 70.592  1.00 100.51 ? 326 ASP A CG  1 
ATOM 2604 O OD1 . ASP A 1 343 ? 106.781 106.212 70.236  1.00 100.51 ? 326 ASP A OD1 1 
ATOM 2605 O OD2 . ASP A 1 343 ? 104.600 106.148 70.040  1.00 100.51 ? 326 ASP A OD2 1 
ATOM 2606 N N   . THR A 1 344 ? 107.003 102.855 70.143  1.00 106.54 ? 327 THR A N   1 
ATOM 2607 C CA  . THR A 1 344 ? 107.643 102.243 68.982  1.00 106.54 ? 327 THR A CA  1 
ATOM 2608 C C   . THR A 1 344 ? 108.136 103.298 67.998  1.00 106.54 ? 327 THR A C   1 
ATOM 2609 O O   . THR A 1 344 ? 109.223 103.162 67.424  1.00 106.54 ? 327 THR A O   1 
ATOM 2610 C CB  . THR A 1 344 ? 106.674 101.284 68.292  1.00 106.54 ? 327 THR A CB  1 
ATOM 2611 O OG1 . THR A 1 344 ? 105.536 102.012 67.815  1.00 106.54 ? 327 THR A OG1 1 
ATOM 2612 C CG2 . THR A 1 344 ? 106.211 100.207 69.262  1.00 106.54 ? 327 THR A CG2 1 
ATOM 2613 N N   . SER A 1 345 ? 107.352 104.356 67.790  1.00 103.57 ? 328 SER A N   1 
ATOM 2614 C CA  . SER A 1 345 ? 107.695 105.411 66.847  1.00 103.57 ? 328 SER A CA  1 
ATOM 2615 C C   . SER A 1 345 ? 108.611 106.469 67.452  1.00 103.57 ? 328 SER A C   1 
ATOM 2616 O O   . SER A 1 345 ? 108.708 107.576 66.909  1.00 103.57 ? 328 SER A O   1 
ATOM 2617 C CB  . SER A 1 345 ? 106.422 106.067 66.306  1.00 103.57 ? 328 SER A CB  1 
ATOM 2618 O OG  . SER A 1 345 ? 105.618 106.565 67.361  1.00 103.57 ? 328 SER A OG  1 
ATOM 2619 N N   . GLY A 1 346 ? 109.283 106.156 68.555  1.00 96.84  ? 329 GLY A N   1 
ATOM 2620 C CA  . GLY A 1 346 ? 110.200 107.095 69.175  1.00 96.84  ? 329 GLY A CA  1 
ATOM 2621 C C   . GLY A 1 346 ? 109.546 108.343 69.727  1.00 96.84  ? 329 GLY A C   1 
ATOM 2622 O O   . GLY A 1 346 ? 110.127 109.432 69.641  1.00 96.84  ? 329 GLY A O   1 
ATOM 2623 N N   . LYS A 1 347 ? 108.348 108.214 70.293  1.00 96.61  ? 330 LYS A N   1 
ATOM 2624 C CA  . LYS A 1 347 ? 107.633 109.343 70.886  1.00 96.61  ? 330 LYS A CA  1 
ATOM 2625 C C   . LYS A 1 347 ? 107.849 109.287 72.394  1.00 96.61  ? 330 LYS A C   1 
ATOM 2626 O O   . LYS A 1 347 ? 107.179 108.542 73.111  1.00 96.61  ? 330 LYS A O   1 
ATOM 2627 C CB  . LYS A 1 347 ? 106.153 109.307 70.522  1.00 96.61  ? 330 LYS A CB  1 
ATOM 2628 C CG  . LYS A 1 347 ? 105.876 109.481 69.038  1.00 96.61  ? 330 LYS A CG  1 
ATOM 2629 C CD  . LYS A 1 347 ? 106.596 110.697 68.479  1.00 96.61  ? 330 LYS A CD  1 
ATOM 2630 C CE  . LYS A 1 347 ? 106.553 110.710 66.960  1.00 96.61  ? 330 LYS A CE  1 
ATOM 2631 N NZ  . LYS A 1 347 ? 107.205 109.503 66.380  1.00 96.61  ? 330 LYS A NZ  1 
ATOM 2632 N N   . PHE A 1 348 ? 108.799 110.083 72.877  1.00 84.82  ? 331 PHE A N   1 
ATOM 2633 C CA  . PHE A 1 348 ? 109.092 110.125 74.303  1.00 84.82  ? 331 PHE A CA  1 
ATOM 2634 C C   . PHE A 1 348 ? 107.977 110.864 75.032  1.00 84.82  ? 331 PHE A C   1 
ATOM 2635 O O   . PHE A 1 348 ? 107.711 112.037 74.749  1.00 84.82  ? 331 PHE A O   1 
ATOM 2636 C CB  . PHE A 1 348 ? 110.439 110.800 74.556  1.00 84.82  ? 331 PHE A CB  1 
ATOM 2637 C CG  . PHE A 1 348 ? 111.616 110.060 73.977  1.00 84.82  ? 331 PHE A CG  1 
ATOM 2638 C CD1 . PHE A 1 348 ? 111.831 110.023 72.608  1.00 84.82  ? 331 PHE A CD1 1 
ATOM 2639 C CD2 . PHE A 1 348 ? 112.509 109.402 74.806  1.00 84.82  ? 331 PHE A CD2 1 
ATOM 2640 C CE1 . PHE A 1 348 ? 112.911 109.344 72.079  1.00 84.82  ? 331 PHE A CE1 1 
ATOM 2641 C CE2 . PHE A 1 348 ? 113.591 108.722 74.282  1.00 84.82  ? 331 PHE A CE2 1 
ATOM 2642 C CZ  . PHE A 1 348 ? 113.793 108.693 72.917  1.00 84.82  ? 331 PHE A CZ  1 
ATOM 2643 N N   . SER A 1 349 ? 107.327 110.181 75.969  1.00 82.75  ? 332 SER A N   1 
ATOM 2644 C CA  . SER A 1 349 ? 106.227 110.749 76.731  1.00 82.75  ? 332 SER A CA  1 
ATOM 2645 C C   . SER A 1 349 ? 106.495 110.577 78.218  1.00 82.75  ? 332 SER A C   1 
ATOM 2646 O O   . SER A 1 349 ? 107.063 109.571 78.652  1.00 82.75  ? 332 SER A O   1 
ATOM 2647 C CB  . SER A 1 349 ? 104.888 110.097 76.362  1.00 82.75  ? 332 SER A CB  1 
ATOM 2648 O OG  . SER A 1 349 ? 104.965 108.685 76.459  1.00 82.75  ? 332 SER A OG  1 
ATOM 2649 N N   . VAL A 1 350 ? 106.077 111.572 78.996  1.00 71.71  ? 333 VAL A N   1 
ATOM 2650 C CA  . VAL A 1 350 ? 106.289 111.572 80.444  1.00 71.71  ? 333 VAL A CA  1 
ATOM 2651 C C   . VAL A 1 350 ? 105.110 110.821 81.056  1.00 71.71  ? 333 VAL A C   1 
ATOM 2652 O O   . VAL A 1 350 ? 104.055 111.392 81.337  1.00 71.71  ? 333 VAL A O   1 
ATOM 2653 C CB  . VAL A 1 350 ? 106.434 112.984 81.001  1.00 71.71  ? 333 VAL A CB  1 
ATOM 2654 C CG1 . VAL A 1 350 ? 106.687 112.939 82.498  1.00 71.71  ? 333 VAL A CG1 1 
ATOM 2655 C CG2 . VAL A 1 350 ? 107.560 113.711 80.293  1.00 71.71  ? 333 VAL A CG2 1 
ATOM 2656 N N   . ASP A 1 351 ? 105.292 109.517 81.253  1.00 75.14  ? 334 ASP A N   1 
ATOM 2657 C CA  . ASP A 1 351 ? 104.275 108.714 81.918  1.00 75.14  ? 334 ASP A CA  1 
ATOM 2658 C C   . ASP A 1 351 ? 104.075 109.216 83.342  1.00 75.14  ? 334 ASP A C   1 
ATOM 2659 O O   . ASP A 1 351 ? 105.042 109.486 84.060  1.00 75.14  ? 334 ASP A O   1 
ATOM 2660 C CB  . ASP A 1 351 ? 104.681 107.240 81.918  1.00 75.14  ? 334 ASP A CB  1 
ATOM 2661 C CG  . ASP A 1 351 ? 103.577 106.325 82.419  1.00 75.14  ? 334 ASP A CG  1 
ATOM 2662 O OD1 . ASP A 1 351 ? 103.215 106.412 83.611  1.00 75.14  ? 334 ASP A OD1 1 
ATOM 2663 O OD2 . ASP A 1 351 ? 103.068 105.516 81.615  1.00 75.14  ? 334 ASP A OD2 1 
ATOM 2664 N N   . LYS A 1 352 ? 102.809 109.349 83.746  1.00 68.76  ? 335 LYS A N   1 
ATOM 2665 C CA  . LYS A 1 352 ? 102.509 109.927 85.052  1.00 68.76  ? 335 LYS A CA  1 
ATOM 2666 C C   . LYS A 1 352 ? 103.051 109.066 86.185  1.00 68.76  ? 335 LYS A C   1 
ATOM 2667 O O   . LYS A 1 352 ? 103.627 109.586 87.147  1.00 68.76  ? 335 LYS A O   1 
ATOM 2668 C CB  . LYS A 1 352 ? 101.001 110.126 85.203  1.00 68.76  ? 335 LYS A CB  1 
ATOM 2669 C CG  . LYS A 1 352 ? 100.535 111.553 84.951  1.00 68.76  ? 335 LYS A CG  1 
ATOM 2670 C CD  . LYS A 1 352 ? 101.082 112.519 85.993  1.00 68.76  ? 335 LYS A CD  1 
ATOM 2671 C CE  . LYS A 1 352 ? 100.773 112.055 87.408  1.00 68.76  ? 335 LYS A CE  1 
ATOM 2672 N NZ  . LYS A 1 352 ? 101.061 113.116 88.413  1.00 68.76  ? 335 LYS A NZ  1 
ATOM 2673 N N   . LEU A 1 353 ? 102.887 107.745 86.087  1.00 71.38  ? 336 LEU A N   1 
ATOM 2674 C CA  . LEU A 1 353 ? 103.292 106.865 87.180  1.00 71.38  ? 336 LEU A CA  1 
ATOM 2675 C C   . LEU A 1 353 ? 104.807 106.847 87.351  1.00 71.38  ? 336 LEU A C   1 
ATOM 2676 O O   . LEU A 1 353 ? 105.317 106.998 88.468  1.00 71.38  ? 336 LEU A O   1 
ATOM 2677 C CB  . LEU A 1 353 ? 102.758 105.453 86.938  1.00 71.38  ? 336 LEU A CB  1 
ATOM 2678 C CG  . LEU A 1 353 ? 101.236 105.300 86.947  1.00 71.38  ? 336 LEU A CG  1 
ATOM 2679 C CD1 . LEU A 1 353 ? 100.838 103.868 86.626  1.00 71.38  ? 336 LEU A CD1 1 
ATOM 2680 C CD2 . LEU A 1 353 ? 100.661 105.733 88.286  1.00 71.38  ? 336 LEU A CD2 1 
ATOM 2681 N N   . LYS A 1 354 ? 105.544 106.654 86.254  1.00 65.75  ? 337 LYS A N   1 
ATOM 2682 C CA  . LYS A 1 354 ? 106.999 106.583 86.344  1.00 65.75  ? 337 LYS A CA  1 
ATOM 2683 C C   . LYS A 1 354 ? 107.596 107.911 86.793  1.00 65.75  ? 337 LYS A C   1 
ATOM 2684 O O   . LYS A 1 354 ? 108.500 107.939 87.639  1.00 65.75  ? 337 LYS A O   1 
ATOM 2685 C CB  . LYS A 1 354 ? 107.587 106.155 85.000  1.00 65.75  ? 337 LYS A CB  1 
ATOM 2686 C CG  . LYS A 1 354 ? 106.932 104.919 84.405  1.00 65.75  ? 337 LYS A CG  1 
ATOM 2687 C CD  . LYS A 1 354 ? 107.898 104.138 83.528  1.00 65.75  ? 337 LYS A CD  1 
ATOM 2688 C CE  . LYS A 1 354 ? 108.696 105.058 82.619  1.00 65.75  ? 337 LYS A CE  1 
ATOM 2689 N NZ  . LYS A 1 354 ? 107.814 105.846 81.714  1.00 65.75  ? 337 LYS A NZ  1 
ATOM 2690 N N   . PHE A 1 355 ? 107.104 109.022 86.241  1.00 60.48  ? 338 PHE A N   1 
ATOM 2691 C CA  . PHE A 1 355 ? 107.607 110.327 86.655  1.00 60.48  ? 338 PHE A CA  1 
ATOM 2692 C C   . PHE A 1 355 ? 107.269 110.607 88.112  1.00 60.48  ? 338 PHE A C   1 
ATOM 2693 O O   . PHE A 1 355 ? 108.077 111.191 88.840  1.00 60.48  ? 338 PHE A O   1 
ATOM 2694 C CB  . PHE A 1 355 ? 107.043 111.430 85.763  1.00 60.48  ? 338 PHE A CB  1 
ATOM 2695 C CG  . PHE A 1 355 ? 107.083 112.790 86.396  1.00 60.48  ? 338 PHE A CG  1 
ATOM 2696 C CD1 . PHE A 1 355 ? 108.277 113.483 86.497  1.00 60.48  ? 338 PHE A CD1 1 
ATOM 2697 C CD2 . PHE A 1 355 ? 105.934 113.369 86.905  1.00 60.48  ? 338 PHE A CD2 1 
ATOM 2698 C CE1 . PHE A 1 355 ? 108.323 114.731 87.085  1.00 60.48  ? 338 PHE A CE1 1 
ATOM 2699 C CE2 . PHE A 1 355 ? 105.974 114.615 87.495  1.00 60.48  ? 338 PHE A CE2 1 
ATOM 2700 C CZ  . PHE A 1 355 ? 107.170 115.298 87.584  1.00 60.48  ? 338 PHE A CZ  1 
ATOM 2701 N N   . ASP A 1 356 ? 106.070 110.216 88.550  1.00 65.59  ? 339 ASP A N   1 
ATOM 2702 C CA  . ASP A 1 356 ? 105.698 110.407 89.947  1.00 65.59  ? 339 ASP A CA  1 
ATOM 2703 C C   . ASP A 1 356 ? 106.605 109.601 90.866  1.00 65.59  ? 339 ASP A C   1 
ATOM 2704 O O   . ASP A 1 356 ? 107.034 110.094 91.915  1.00 65.59  ? 339 ASP A O   1 
ATOM 2705 C CB  . ASP A 1 356 ? 104.234 110.018 90.157  1.00 65.59  ? 339 ASP A CB  1 
ATOM 2706 C CG  . ASP A 1 356 ? 103.827 110.031 91.619  1.00 65.59  ? 339 ASP A CG  1 
ATOM 2707 O OD1 . ASP A 1 356 ? 104.371 110.852 92.387  1.00 65.59  ? 339 ASP A OD1 1 
ATOM 2708 O OD2 . ASP A 1 356 ? 102.962 109.216 92.001  1.00 65.59  ? 339 ASP A OD2 1 
ATOM 2709 N N   . LYS A 1 357 ? 106.914 108.359 90.485  1.00 65.42  ? 340 LYS A N   1 
ATOM 2710 C CA  . LYS A 1 357 ? 107.828 107.548 91.283  1.00 65.42  ? 340 LYS A CA  1 
ATOM 2711 C C   . LYS A 1 357 ? 109.215 108.177 91.340  1.00 65.42  ? 340 LYS A C   1 
ATOM 2712 O O   . LYS A 1 357 ? 109.835 108.233 92.409  1.00 65.42  ? 340 LYS A O   1 
ATOM 2713 C CB  . LYS A 1 357 ? 107.906 106.130 90.719  1.00 65.42  ? 340 LYS A CB  1 
ATOM 2714 C CG  . LYS A 1 357 ? 106.647 105.302 90.930  1.00 65.42  ? 340 LYS A CG  1 
ATOM 2715 C CD  . LYS A 1 357 ? 106.649 104.042 90.073  1.00 65.42  ? 340 LYS A CD  1 
ATOM 2716 C CE  . LYS A 1 357 ? 108.026 103.394 90.013  1.00 65.42  ? 340 LYS A CE  1 
ATOM 2717 N NZ  . LYS A 1 357 ? 108.512 102.974 91.357  1.00 65.42  ? 340 LYS A NZ  1 
ATOM 2718 N N   . LEU A 1 358 ? 109.713 108.664 90.201  1.00 55.99  ? 341 LEU A N   1 
ATOM 2719 C CA  . LEU A 1 358 ? 111.029 109.297 90.180  1.00 55.99  ? 341 LEU A CA  1 
ATOM 2720 C C   . LEU A 1 358 ? 111.053 110.553 91.043  1.00 55.99  ? 341 LEU A C   1 
ATOM 2721 O O   . LEU A 1 358 ? 112.017 110.794 91.779  1.00 55.99  ? 341 LEU A O   1 
ATOM 2722 C CB  . LEU A 1 358 ? 111.429 109.626 88.742  1.00 55.99  ? 341 LEU A CB  1 
ATOM 2723 C CG  . LEU A 1 358 ? 112.751 110.371 88.546  1.00 55.99  ? 341 LEU A CG  1 
ATOM 2724 C CD1 . LEU A 1 358 ? 113.901 109.599 89.171  1.00 55.99  ? 341 LEU A CD1 1 
ATOM 2725 C CD2 . LEU A 1 358 ? 113.012 110.622 87.069  1.00 55.99  ? 341 LEU A CD2 1 
ATOM 2726 N N   . TYR A 1 359 ? 109.999 111.367 90.961  1.00 52.73  ? 342 TYR A N   1 
ATOM 2727 C CA  . TYR A 1 359 ? 109.937 112.591 91.751  1.00 52.73  ? 342 TYR A CA  1 
ATOM 2728 C C   . TYR A 1 359 ? 109.837 112.286 93.240  1.00 52.73  ? 342 TYR A C   1 
ATOM 2729 O O   . TYR A 1 359 ? 110.458 112.969 94.061  1.00 52.73  ? 342 TYR A O   1 
ATOM 2730 C CB  . TYR A 1 359 ? 108.758 113.446 91.293  1.00 52.73  ? 342 TYR A CB  1 
ATOM 2731 C CG  . TYR A 1 359 ? 108.844 114.887 91.728  1.00 52.73  ? 342 TYR A CG  1 
ATOM 2732 C CD1 . TYR A 1 359 ? 108.305 115.298 92.938  1.00 52.73  ? 342 TYR A CD1 1 
ATOM 2733 C CD2 . TYR A 1 359 ? 109.462 115.837 90.929  1.00 52.73  ? 342 TYR A CD2 1 
ATOM 2734 C CE1 . TYR A 1 359 ? 108.380 116.613 93.342  1.00 52.73  ? 342 TYR A CE1 1 
ATOM 2735 C CE2 . TYR A 1 359 ? 109.542 117.156 91.324  1.00 52.73  ? 342 TYR A CE2 1 
ATOM 2736 C CZ  . TYR A 1 359 ? 108.998 117.538 92.531  1.00 52.73  ? 342 TYR A CZ  1 
ATOM 2737 O OH  . TYR A 1 359 ? 109.073 118.850 92.937  1.00 52.73  ? 342 TYR A OH  1 
ATOM 2738 N N   . LYS A 1 360 ? 109.056 111.267 93.608  1.00 55.70  ? 343 LYS A N   1 
ATOM 2739 C CA  . LYS A 1 360 ? 108.980 110.856 95.005  1.00 55.70  ? 343 LYS A CA  1 
ATOM 2740 C C   . LYS A 1 360 ? 110.330 110.361 95.503  1.00 55.70  ? 343 LYS A C   1 
ATOM 2741 O O   . LYS A 1 360 ? 110.737 110.664 96.631  1.00 55.70  ? 343 LYS A O   1 
ATOM 2742 C CB  . LYS A 1 360 ? 107.917 109.771 95.173  1.00 55.70  ? 343 LYS A CB  1 
ATOM 2743 C CG  . LYS A 1 360 ? 107.870 109.147 96.558  1.00 55.70  ? 343 LYS A CG  1 
ATOM 2744 C CD  . LYS A 1 360 ? 106.776 108.096 96.648  1.00 55.70  ? 343 LYS A CD  1 
ATOM 2745 C CE  . LYS A 1 360 ? 105.481 108.686 97.178  1.00 55.70  ? 343 LYS A CE  1 
ATOM 2746 N NZ  . LYS A 1 360 ? 104.332 107.761 96.979  1.00 55.70  ? 343 LYS A NZ  1 
ATOM 2747 N N   . MET A 1 361 ? 111.038 109.592 94.672  1.00 50.73  ? 344 MET A N   1 
ATOM 2748 C CA  . MET A 1 361 ? 112.348 109.084 95.059  1.00 50.73  ? 344 MET A CA  1 
ATOM 2749 C C   . MET A 1 361 ? 113.352 110.213 95.248  1.00 50.73  ? 344 MET A C   1 
ATOM 2750 O O   . MET A 1 361 ? 114.121 110.213 96.216  1.00 50.73  ? 344 MET A O   1 
ATOM 2751 C CB  . MET A 1 361 ? 112.844 108.096 94.007  1.00 50.73  ? 344 MET A CB  1 
ATOM 2752 C CG  . MET A 1 361 ? 113.719 106.994 94.551  1.00 50.73  ? 344 MET A CG  1 
ATOM 2753 S SD  . MET A 1 361 ? 114.370 105.980 93.220  1.00 50.73  ? 344 MET A SD  1 
ATOM 2754 C CE  . MET A 1 361 ? 115.224 107.211 92.240  1.00 50.73  ? 344 MET A CE  1 
ATOM 2755 N N   . LEU A 1 362 ? 113.360 111.186 94.336  1.00 49.85  ? 345 LEU A N   1 
ATOM 2756 C CA  . LEU A 1 362 ? 114.316 112.283 94.434  1.00 49.85  ? 345 LEU A CA  1 
ATOM 2757 C C   . LEU A 1 362 ? 113.943 113.280 95.523  1.00 49.85  ? 345 LEU A C   1 
ATOM 2758 O O   . LEU A 1 362 ? 114.821 113.971 96.049  1.00 49.85  ? 345 LEU A O   1 
ATOM 2759 C CB  . LEU A 1 362 ? 114.433 112.999 93.088  1.00 49.85  ? 345 LEU A CB  1 
ATOM 2760 C CG  . LEU A 1 362 ? 115.236 112.268 92.013  1.00 49.85  ? 345 LEU A CG  1 
ATOM 2761 C CD1 . LEU A 1 362 ? 115.158 113.007 90.688  1.00 49.85  ? 345 LEU A CD1 1 
ATOM 2762 C CD2 . LEU A 1 362 ? 116.680 112.102 92.454  1.00 49.85  ? 345 LEU A CD2 1 
ATOM 2763 N N   . THR A 1 363 ? 112.663 113.366 95.879  1.00 49.85  ? 346 THR A N   1 
ATOM 2764 C CA  . THR A 1 363 ? 112.192 114.384 96.808  1.00 49.85  ? 346 THR A CA  1 
ATOM 2765 C C   . THR A 1 363 ? 112.136 113.883 98.248  1.00 49.85  ? 346 THR A C   1 
ATOM 2766 O O   . THR A 1 363 ? 112.598 114.570 99.164  1.00 49.85  ? 346 THR A O   1 
ATOM 2767 C CB  . THR A 1 363 ? 110.811 114.882 96.373  1.00 49.85  ? 346 THR A CB  1 
ATOM 2768 O OG1 . THR A 1 363 ? 110.866 115.323 95.010  1.00 49.85  ? 346 THR A OG1 1 
ATOM 2769 C CG2 . THR A 1 363 ? 110.351 116.025 97.257  1.00 49.85  ? 346 THR A CG2 1 
ATOM 2770 N N   . GLU A 1 364 ? 111.580 112.694 98.463  1.00 57.10  ? 347 GLU A N   1 
ATOM 2771 C CA  . GLU A 1 364 ? 111.339 112.176 99.805  1.00 57.10  ? 347 GLU A CA  1 
ATOM 2772 C C   . GLU A 1 364 ? 112.235 111.008 100.181 1.00 57.10  ? 347 GLU A C   1 
ATOM 2773 O O   . GLU A 1 364 ? 112.644 110.904 101.340 1.00 57.10  ? 347 GLU A O   1 
ATOM 2774 C CB  . GLU A 1 364 ? 109.873 111.752 99.945  1.00 57.10  ? 347 GLU A CB  1 
ATOM 2775 C CG  . GLU A 1 364 ? 108.883 112.884 99.717  1.00 57.10  ? 347 GLU A CG  1 
ATOM 2776 C CD  . GLU A 1 364 ? 107.447 112.401 99.651  1.00 57.10  ? 347 GLU A CD  1 
ATOM 2777 O OE1 . GLU A 1 364 ? 106.862 112.123 100.719 1.00 57.10  ? 347 GLU A OE1 1 
ATOM 2778 O OE2 . GLU A 1 364 ? 106.904 112.302 98.531  1.00 57.10  ? 347 GLU A OE2 1 
ATOM 2779 N N   . ILE A 1 365 ? 112.543 110.113 99.242  1.00 50.29  ? 348 ILE A N   1 
ATOM 2780 C CA  . ILE A 1 365 ? 113.406 108.979 99.559  1.00 50.29  ? 348 ILE A CA  1 
ATOM 2781 C C   . ILE A 1 365 ? 114.838 109.445 99.791  1.00 50.29  ? 348 ILE A C   1 
ATOM 2782 O O   . ILE A 1 365 ? 115.477 109.075 100.783 1.00 50.29  ? 348 ILE A O   1 
ATOM 2783 C CB  . ILE A 1 365 ? 113.325 107.917 98.449  1.00 50.29  ? 348 ILE A CB  1 
ATOM 2784 C CG1 . ILE A 1 365 ? 111.998 107.165 98.537  1.00 50.29  ? 348 ILE A CG1 1 
ATOM 2785 C CG2 . ILE A 1 365 ? 114.490 106.947 98.550  1.00 50.29  ? 348 ILE A CG2 1 
ATOM 2786 C CD1 . ILE A 1 365 ? 111.871 106.036 97.544  1.00 50.29  ? 348 ILE A CD1 1 
ATOM 2787 N N   . TYR A 1 366 ? 115.363 110.273 98.886  1.00 53.05  ? 349 TYR A N   1 
ATOM 2788 C CA  . TYR A 1 366 ? 116.720 110.805 99.011  1.00 53.05  ? 349 TYR A CA  1 
ATOM 2789 C C   . TYR A 1 366 ? 116.686 111.986 99.975  1.00 53.05  ? 349 TYR A C   1 
ATOM 2790 O O   . TYR A 1 366 ? 116.602 113.153 99.585  1.00 53.05  ? 349 TYR A O   1 
ATOM 2791 C CB  . TYR A 1 366 ? 117.273 111.216 97.653  1.00 53.05  ? 349 TYR A CB  1 
ATOM 2792 C CG  . TYR A 1 366 ? 117.585 110.065 96.728  1.00 53.05  ? 349 TYR A CG  1 
ATOM 2793 C CD1 . TYR A 1 366 ? 117.620 108.759 97.194  1.00 53.05  ? 349 TYR A CD1 1 
ATOM 2794 C CD2 . TYR A 1 366 ? 117.849 110.289 95.385  1.00 53.05  ? 349 TYR A CD2 1 
ATOM 2795 C CE1 . TYR A 1 366 ? 117.906 107.708 96.346  1.00 53.05  ? 349 TYR A CE1 1 
ATOM 2796 C CE2 . TYR A 1 366 ? 118.136 109.246 94.531  1.00 53.05  ? 349 TYR A CE2 1 
ATOM 2797 C CZ  . TYR A 1 366 ? 118.164 107.959 95.015  1.00 53.05  ? 349 TYR A CZ  1 
ATOM 2798 O OH  . TYR A 1 366 ? 118.450 106.920 94.161  1.00 53.05  ? 349 TYR A OH  1 
ATOM 2799 N N   . THR A 1 367 ? 116.754 111.672 101.265 1.00 49.85  ? 350 THR A N   1 
ATOM 2800 C CA  . THR A 1 367 ? 116.674 112.692 102.298 1.00 49.85  ? 350 THR A CA  1 
ATOM 2801 C C   . THR A 1 367 ? 117.728 112.425 103.361 1.00 49.85  ? 350 THR A C   1 
ATOM 2802 O O   . THR A 1 367 ? 118.206 111.301 103.527 1.00 49.85  ? 350 THR A O   1 
ATOM 2803 C CB  . THR A 1 367 ? 115.279 112.746 102.929 1.00 49.85  ? 350 THR A CB  1 
ATOM 2804 O OG1 . THR A 1 367 ? 114.778 111.414 103.097 1.00 49.85  ? 350 THR A OG1 1 
ATOM 2805 C CG2 . THR A 1 367 ? 114.331 113.527 102.033 1.00 49.85  ? 350 THR A CG2 1 
ATOM 2806 N N   . GLU A 1 368 ? 118.091 113.490 104.080 1.00 49.85  ? 351 GLU A N   1 
ATOM 2807 C CA  . GLU A 1 368 ? 119.109 113.374 105.119 1.00 49.85  ? 351 GLU A CA  1 
ATOM 2808 C C   . GLU A 1 368 ? 118.636 112.487 106.265 1.00 49.85  ? 351 GLU A C   1 
ATOM 2809 O O   . GLU A 1 368 ? 119.438 111.764 106.866 1.00 49.85  ? 351 GLU A O   1 
ATOM 2810 C CB  . GLU A 1 368 ? 119.489 114.761 105.634 1.00 49.85  ? 351 GLU A CB  1 
ATOM 2811 C CG  . GLU A 1 368 ? 120.551 114.751 106.718 1.00 49.85  ? 351 GLU A CG  1 
ATOM 2812 C CD  . GLU A 1 368 ? 121.163 116.117 106.949 1.00 49.85  ? 351 GLU A CD  1 
ATOM 2813 O OE1 . GLU A 1 368 ? 121.456 116.813 105.955 1.00 49.85  ? 351 GLU A OE1 1 
ATOM 2814 O OE2 . GLU A 1 368 ? 121.353 116.495 108.124 1.00 49.85  ? 351 GLU A OE2 1 
ATOM 2815 N N   . ASP A 1 369 ? 117.342 112.535 106.588 1.00 49.85  ? 352 ASP A N   1 
ATOM 2816 C CA  . ASP A 1 369 ? 116.821 111.725 107.685 1.00 49.85  ? 352 ASP A CA  1 
ATOM 2817 C C   . ASP A 1 369 ? 116.968 110.236 107.394 1.00 49.85  ? 352 ASP A C   1 
ATOM 2818 O O   . ASP A 1 369 ? 117.312 109.451 108.287 1.00 49.85  ? 352 ASP A O   1 
ATOM 2819 C CB  . ASP A 1 369 ? 115.358 112.080 107.948 1.00 49.85  ? 352 ASP A CB  1 
ATOM 2820 C CG  . ASP A 1 369 ? 114.764 111.284 109.090 1.00 49.85  ? 352 ASP A CG  1 
ATOM 2821 O OD1 . ASP A 1 369 ? 115.242 111.436 110.233 1.00 49.85  ? 352 ASP A OD1 1 
ATOM 2822 O OD2 . ASP A 1 369 ? 113.820 110.504 108.845 1.00 49.85  ? 352 ASP A OD2 1 
ATOM 2823 N N   . ASN A 1 370 ? 116.706 109.826 106.151 1.00 49.85  ? 353 ASN A N   1 
ATOM 2824 C CA  . ASN A 1 370 ? 116.871 108.422 105.789 1.00 49.85  ? 353 ASN A CA  1 
ATOM 2825 C C   . ASN A 1 370 ? 118.328 107.991 105.904 1.00 49.85  ? 353 ASN A C   1 
ATOM 2826 O O   . ASN A 1 370 ? 118.621 106.873 106.342 1.00 49.85  ? 353 ASN A O   1 
ATOM 2827 C CB  . ASN A 1 370 ? 116.346 108.180 104.375 1.00 49.85  ? 353 ASN A CB  1 
ATOM 2828 C CG  . ASN A 1 370 ? 114.843 108.001 104.335 1.00 49.85  ? 353 ASN A CG  1 
ATOM 2829 O OD1 . ASN A 1 370 ? 114.226 107.620 105.329 1.00 49.85  ? 353 ASN A OD1 1 
ATOM 2830 N ND2 . ASN A 1 370 ? 114.245 108.275 103.183 1.00 49.85  ? 353 ASN A ND2 1 
ATOM 2831 N N   . PHE A 1 371 ? 119.257 108.868 105.519 1.00 49.85  ? 354 PHE A N   1 
ATOM 2832 C CA  . PHE A 1 371 ? 120.673 108.544 105.656 1.00 49.85  ? 354 PHE A CA  1 
ATOM 2833 C C   . PHE A 1 371 ? 121.083 108.459 107.120 1.00 49.85  ? 354 PHE A C   1 
ATOM 2834 O O   . PHE A 1 371 ? 121.916 107.624 107.489 1.00 49.85  ? 354 PHE A O   1 
ATOM 2835 C CB  . PHE A 1 371 ? 121.522 109.574 104.914 1.00 49.85  ? 354 PHE A CB  1 
ATOM 2836 C CG  . PHE A 1 371 ? 121.741 109.243 103.469 1.00 49.85  ? 354 PHE A CG  1 
ATOM 2837 C CD1 . PHE A 1 371 ? 122.406 108.086 103.106 1.00 49.85  ? 354 PHE A CD1 1 
ATOM 2838 C CD2 . PHE A 1 371 ? 121.273 110.082 102.474 1.00 49.85  ? 354 PHE A CD2 1 
ATOM 2839 C CE1 . PHE A 1 371 ? 122.608 107.776 101.779 1.00 49.85  ? 354 PHE A CE1 1 
ATOM 2840 C CE2 . PHE A 1 371 ? 121.473 109.777 101.145 1.00 49.85  ? 354 PHE A CE2 1 
ATOM 2841 C CZ  . PHE A 1 371 ? 122.141 108.622 100.796 1.00 49.85  ? 354 PHE A CZ  1 
ATOM 2842 N N   . VAL A 1 372 ? 120.515 109.319 107.968 1.00 49.85  ? 355 VAL A N   1 
ATOM 2843 C CA  . VAL A 1 372 ? 120.782 109.234 109.401 1.00 49.85  ? 355 VAL A CA  1 
ATOM 2844 C C   . VAL A 1 372 ? 120.277 107.908 109.953 1.00 49.85  ? 355 VAL A C   1 
ATOM 2845 O O   . VAL A 1 372 ? 120.949 107.256 110.761 1.00 49.85  ? 355 VAL A O   1 
ATOM 2846 C CB  . VAL A 1 372 ? 120.154 110.434 110.134 1.00 49.85  ? 355 VAL A CB  1 
ATOM 2847 C CG1 . VAL A 1 372 ? 120.171 110.212 111.637 1.00 49.85  ? 355 VAL A CG1 1 
ATOM 2848 C CG2 . VAL A 1 372 ? 120.888 111.713 109.775 1.00 49.85  ? 355 VAL A CG2 1 
ATOM 2849 N N   . LYS A 1 373 ? 119.085 107.488 109.522 1.00 49.85  ? 356 LYS A N   1 
ATOM 2850 C CA  . LYS A 1 373 ? 118.553 106.199 109.955 1.00 49.85  ? 356 LYS A CA  1 
ATOM 2851 C C   . LYS A 1 373 ? 119.439 105.048 109.491 1.00 49.85  ? 356 LYS A C   1 
ATOM 2852 O O   . LYS A 1 373 ? 119.699 104.110 110.254 1.00 49.85  ? 356 LYS A O   1 
ATOM 2853 C CB  . LYS A 1 373 ? 117.128 106.014 109.433 1.00 49.85  ? 356 LYS A CB  1 
ATOM 2854 C CG  . LYS A 1 373 ? 116.087 106.871 110.129 1.00 49.85  ? 356 LYS A CG  1 
ATOM 2855 C CD  . LYS A 1 373 ? 114.685 106.485 109.688 1.00 49.85  ? 356 LYS A CD  1 
ATOM 2856 C CE  . LYS A 1 373 ? 113.638 107.381 110.325 1.00 49.85  ? 356 LYS A CE  1 
ATOM 2857 N NZ  . LYS A 1 373 ? 114.215 108.680 110.762 1.00 49.85  ? 356 LYS A NZ  1 
ATOM 2858 N N   . PHE A 1 374 ? 119.908 105.100 108.243 1.00 49.85  ? 357 PHE A N   1 
ATOM 2859 C CA  . PHE A 1 374 ? 120.702 103.999 107.705 1.00 49.85  ? 357 PHE A CA  1 
ATOM 2860 C C   . PHE A 1 374 ? 122.076 103.924 108.361 1.00 49.85  ? 357 PHE A C   1 
ATOM 2861 O O   . PHE A 1 374 ? 122.559 102.830 108.678 1.00 49.85  ? 357 PHE A O   1 
ATOM 2862 C CB  . PHE A 1 374 ? 120.837 104.140 106.190 1.00 49.85  ? 357 PHE A CB  1 
ATOM 2863 C CG  . PHE A 1 374 ? 119.843 103.326 105.417 1.00 49.85  ? 357 PHE A CG  1 
ATOM 2864 C CD1 . PHE A 1 374 ? 118.579 103.823 105.150 1.00 49.85  ? 357 PHE A CD1 1 
ATOM 2865 C CD2 . PHE A 1 374 ? 120.170 102.061 104.960 1.00 49.85  ? 357 PHE A CD2 1 
ATOM 2866 C CE1 . PHE A 1 374 ? 117.661 103.074 104.440 1.00 49.85  ? 357 PHE A CE1 1 
ATOM 2867 C CE2 . PHE A 1 374 ? 119.256 101.307 104.249 1.00 49.85  ? 357 PHE A CE2 1 
ATOM 2868 C CZ  . PHE A 1 374 ? 118.000 101.815 103.989 1.00 49.85  ? 357 PHE A CZ  1 
ATOM 2869 N N   . PHE A 1 375 ? 122.724 105.072 108.569 1.00 49.85  ? 358 PHE A N   1 
ATOM 2870 C CA  . PHE A 1 375 ? 124.037 105.084 109.205 1.00 49.85  ? 358 PHE A CA  1 
ATOM 2871 C C   . PHE A 1 375 ? 123.973 104.702 110.676 1.00 49.85  ? 358 PHE A C   1 
ATOM 2872 O O   . PHE A 1 375 ? 124.999 104.309 111.243 1.00 49.85  ? 358 PHE A O   1 
ATOM 2873 C CB  . PHE A 1 375 ? 124.683 106.465 109.070 1.00 49.85  ? 358 PHE A CB  1 
ATOM 2874 C CG  . PHE A 1 375 ? 125.039 106.840 107.661 1.00 49.85  ? 358 PHE A CG  1 
ATOM 2875 C CD1 . PHE A 1 375 ? 125.356 105.870 106.726 1.00 49.85  ? 358 PHE A CD1 1 
ATOM 2876 C CD2 . PHE A 1 375 ? 125.065 108.169 107.273 1.00 49.85  ? 358 PHE A CD2 1 
ATOM 2877 C CE1 . PHE A 1 375 ? 125.685 106.220 105.431 1.00 49.85  ? 358 PHE A CE1 1 
ATOM 2878 C CE2 . PHE A 1 375 ? 125.393 108.523 105.981 1.00 49.85  ? 358 PHE A CE2 1 
ATOM 2879 C CZ  . PHE A 1 375 ? 125.704 107.547 105.059 1.00 49.85  ? 358 PHE A CZ  1 
ATOM 2880 N N   . LYS A 1 376 ? 122.799 104.808 111.300 1.00 51.48  ? 359 LYS A N   1 
ATOM 2881 C CA  . LYS A 1 376 ? 122.630 104.593 112.736 1.00 51.48  ? 359 LYS A CA  1 
ATOM 2882 C C   . LYS A 1 376 ? 123.576 105.497 113.530 1.00 51.48  ? 359 LYS A C   1 
ATOM 2883 O O   . LYS A 1 376 ? 124.400 105.044 114.326 1.00 51.48  ? 359 LYS A O   1 
ATOM 2884 C CB  . LYS A 1 376 ? 122.826 103.118 113.103 1.00 51.48  ? 359 LYS A CB  1 
ATOM 2885 C CG  . LYS A 1 376 ? 122.022 102.156 112.246 1.00 51.48  ? 359 LYS A CG  1 
ATOM 2886 C CD  . LYS A 1 376 ? 121.480 101.005 113.075 1.00 51.48  ? 359 LYS A CD  1 
ATOM 2887 C CE  . LYS A 1 376 ? 120.434 101.487 114.067 1.00 51.48  ? 359 LYS A CE  1 
ATOM 2888 N NZ  . LYS A 1 376 ? 119.271 102.121 113.387 1.00 51.48  ? 359 LYS A NZ  1 
ATOM 2889 N N   . VAL A 1 377 ? 123.442 106.800 113.285 1.00 49.85  ? 360 VAL A N   1 
ATOM 2890 C CA  . VAL A 1 377 ? 124.251 107.814 113.945 1.00 49.85  ? 360 VAL A CA  1 
ATOM 2891 C C   . VAL A 1 377 ? 123.326 108.878 114.517 1.00 49.85  ? 360 VAL A C   1 
ATOM 2892 O O   . VAL A 1 377 ? 122.192 109.059 114.068 1.00 49.85  ? 360 VAL A O   1 
ATOM 2893 C CB  . VAL A 1 377 ? 125.281 108.454 112.990 1.00 49.85  ? 360 VAL A CB  1 
ATOM 2894 C CG1 . VAL A 1 377 ? 126.283 107.415 112.514 1.00 49.85  ? 360 VAL A CG1 1 
ATOM 2895 C CG2 . VAL A 1 377 ? 124.579 109.106 111.811 1.00 49.85  ? 360 VAL A CG2 1 
ATOM 2896 N N   . LEU A 1 378 ? 123.827 109.585 115.526 1.00 57.98  ? 361 LEU A N   1 
ATOM 2897 C CA  . LEU A 1 378 ? 123.058 110.642 116.165 1.00 57.98  ? 361 LEU A CA  1 
ATOM 2898 C C   . LEU A 1 378 ? 123.190 111.933 115.369 1.00 57.98  ? 361 LEU A C   1 
ATOM 2899 O O   . LEU A 1 378 ? 124.301 112.370 115.057 1.00 57.98  ? 361 LEU A O   1 
ATOM 2900 C CB  . LEU A 1 378 ? 123.532 110.853 117.602 1.00 57.98  ? 361 LEU A CB  1 
ATOM 2901 C CG  . LEU A 1 378 ? 122.806 110.048 118.682 1.00 57.98  ? 361 LEU A CG  1 
ATOM 2902 C CD1 . LEU A 1 378 ? 122.868 110.766 120.019 1.00 57.98  ? 361 LEU A CD1 1 
ATOM 2903 C CD2 . LEU A 1 378 ? 121.363 109.776 118.284 1.00 57.98  ? 361 LEU A CD2 1 
ATOM 2904 N N   . ASN A 1 379 ? 122.053 112.542 115.041 1.00 51.86  ? 362 ASN A N   1 
ATOM 2905 C CA  . ASN A 1 379 ? 122.047 113.757 114.243 1.00 51.86  ? 362 ASN A CA  1 
ATOM 2906 C C   . ASN A 1 379 ? 120.817 114.579 114.599 1.00 51.86  ? 362 ASN A C   1 
ATOM 2907 O O   . ASN A 1 379 ? 119.839 114.067 115.150 1.00 51.86  ? 362 ASN A O   1 
ATOM 2908 C CB  . ASN A 1 379 ? 122.078 113.440 112.743 1.00 51.86  ? 362 ASN A CB  1 
ATOM 2909 C CG  . ASN A 1 379 ? 122.387 114.656 111.891 1.00 51.86  ? 362 ASN A CG  1 
ATOM 2910 O OD1 . ASN A 1 379 ? 121.833 115.736 112.096 1.00 51.86  ? 362 ASN A OD1 1 
ATOM 2911 N ND2 . ASN A 1 379 ? 123.288 114.488 110.933 1.00 51.86  ? 362 ASN A ND2 1 
ATOM 2912 N N   . ALA A 1 380 ? 120.885 115.868 114.278 1.00 57.70  ? 363 ALA A N   1 
ATOM 2913 C CA  . ALA A 1 380 ? 119.768 116.767 114.526 1.00 57.70  ? 363 ALA A CA  1 
ATOM 2914 C C   . ALA A 1 380 ? 118.578 116.399 113.649 1.00 57.70  ? 363 ALA A C   1 
ATOM 2915 O O   . ALA A 1 380 ? 118.738 115.960 112.507 1.00 57.70  ? 363 ALA A O   1 
ATOM 2916 C CB  . ALA A 1 380 ? 120.185 118.212 114.264 1.00 57.70  ? 363 ALA A CB  1 
ATOM 2917 N N   . LYS A 1 381 ? 117.375 116.581 114.193 1.00 62.64  ? 364 LYS A N   1 
ATOM 2918 C CA  . LYS A 1 381 ? 116.153 116.281 113.456 1.00 62.64  ? 364 LYS A CA  1 
ATOM 2919 C C   . LYS A 1 381 ? 115.645 117.483 112.669 1.00 62.64  ? 364 LYS A C   1 
ATOM 2920 O O   . LYS A 1 381 ? 115.244 117.336 111.510 1.00 62.64  ? 364 LYS A O   1 
ATOM 2921 C CB  . LYS A 1 381 ? 115.071 115.783 114.416 1.00 62.64  ? 364 LYS A CB  1 
ATOM 2922 C CG  . LYS A 1 381 ? 115.600 114.882 115.521 1.00 62.64  ? 364 LYS A CG  1 
ATOM 2923 C CD  . LYS A 1 381 ? 115.492 113.415 115.139 1.00 62.64  ? 364 LYS A CD  1 
ATOM 2924 C CE  . LYS A 1 381 ? 115.823 112.512 116.316 1.00 62.64  ? 364 LYS A CE  1 
ATOM 2925 N NZ  . LYS A 1 381 ? 117.199 112.755 116.834 1.00 62.64  ? 364 LYS A NZ  1 
ATOM 2926 N N   . THR A 1 382 ? 115.650 118.665 113.275 1.00 55.10  ? 365 THR A N   1 
ATOM 2927 C CA  . THR A 1 382 ? 115.298 119.914 112.616 1.00 55.10  ? 365 THR A CA  1 
ATOM 2928 C C   . THR A 1 382 ? 116.515 120.830 112.579 1.00 55.10  ? 365 THR A C   1 
ATOM 2929 O O   . THR A 1 382 ? 117.524 120.585 113.243 1.00 55.10  ? 365 THR A O   1 
ATOM 2930 C CB  . THR A 1 382 ? 114.131 120.602 113.333 1.00 55.10  ? 365 THR A CB  1 
ATOM 2931 O OG1 . THR A 1 382 ? 113.787 121.810 112.643 1.00 55.10  ? 365 THR A OG1 1 
ATOM 2932 C CG2 . THR A 1 382 ? 114.509 120.933 114.768 1.00 55.10  ? 365 THR A CG2 1 
ATOM 2933 N N   . PHE A 1 383 ? 116.424 121.897 111.779 1.00 59.40  ? 366 PHE A N   1 
ATOM 2934 C CA  . PHE A 1 383 ? 117.554 122.815 111.694 1.00 59.40  ? 366 PHE A CA  1 
ATOM 2935 C C   . PHE A 1 383 ? 117.668 123.698 112.927 1.00 59.40  ? 366 PHE A C   1 
ATOM 2936 O O   . PHE A 1 383 ? 118.708 124.336 113.118 1.00 59.40  ? 366 PHE A O   1 
ATOM 2937 C CB  . PHE A 1 383 ? 117.454 123.725 110.467 1.00 59.40  ? 366 PHE A CB  1 
ATOM 2938 C CG  . PHE A 1 383 ? 116.052 124.113 110.100 1.00 59.40  ? 366 PHE A CG  1 
ATOM 2939 C CD1 . PHE A 1 383 ? 115.426 125.162 110.754 1.00 59.40  ? 366 PHE A CD1 1 
ATOM 2940 C CD2 . PHE A 1 383 ? 115.378 123.473 109.079 1.00 59.40  ? 366 PHE A CD2 1 
ATOM 2941 C CE1 . PHE A 1 383 ? 114.142 125.541 110.420 1.00 59.40  ? 366 PHE A CE1 1 
ATOM 2942 C CE2 . PHE A 1 383 ? 114.094 123.853 108.738 1.00 59.40  ? 366 PHE A CE2 1 
ATOM 2943 C CZ  . PHE A 1 383 ? 113.475 124.886 109.410 1.00 59.40  ? 366 PHE A CZ  1 
ATOM 2944 N N   . LEU A 1 384 ? 116.628 123.746 113.764 1.00 60.49  ? 367 LEU A N   1 
ATOM 2945 C CA  . LEU A 1 384 ? 116.554 124.763 114.808 1.00 60.49  ? 367 LEU A CA  1 
ATOM 2946 C C   . LEU A 1 384 ? 117.677 124.628 115.827 1.00 60.49  ? 367 LEU A C   1 
ATOM 2947 O O   . LEU A 1 384 ? 118.224 125.642 116.277 1.00 60.49  ? 367 LEU A O   1 
ATOM 2948 C CB  . LEU A 1 384 ? 115.194 124.702 115.500 1.00 60.49  ? 367 LEU A CB  1 
ATOM 2949 C CG  . LEU A 1 384 ? 114.021 125.044 114.582 1.00 60.49  ? 367 LEU A CG  1 
ATOM 2950 C CD1 . LEU A 1 384 ? 112.698 124.901 115.315 1.00 60.49  ? 367 LEU A CD1 1 
ATOM 2951 C CD2 . LEU A 1 384 ? 114.184 126.440 114.005 1.00 60.49  ? 367 LEU A CD2 1 
ATOM 2952 N N   . ASN A 1 385 ? 118.040 123.403 116.204 1.00 56.32  ? 368 ASN A N   1 
ATOM 2953 C CA  . ASN A 1 385 ? 119.172 123.191 117.105 1.00 56.32  ? 368 ASN A CA  1 
ATOM 2954 C C   . ASN A 1 385 ? 120.460 123.420 116.314 1.00 56.32  ? 368 ASN A C   1 
ATOM 2955 O O   . ASN A 1 385 ? 121.154 122.495 115.884 1.00 56.32  ? 368 ASN A O   1 
ATOM 2956 C CB  . ASN A 1 385 ? 119.103 121.809 117.752 1.00 56.32  ? 368 ASN A CB  1 
ATOM 2957 C CG  . ASN A 1 385 ? 119.182 120.678 116.748 1.00 56.32  ? 368 ASN A CG  1 
ATOM 2958 O OD1 . ASN A 1 385 ? 118.928 120.870 115.561 1.00 56.32  ? 368 ASN A OD1 1 
ATOM 2959 N ND2 . ASN A 1 385 ? 119.534 119.490 117.223 1.00 56.32  ? 368 ASN A ND2 1 
ATOM 2960 N N   . PHE A 1 386 ? 120.778 124.699 116.122 1.00 61.85  ? 369 PHE A N   1 
ATOM 2961 C CA  . PHE A 1 386 ? 121.949 125.099 115.360 1.00 61.85  ? 369 PHE A CA  1 
ATOM 2962 C C   . PHE A 1 386 ? 123.224 124.566 116.005 1.00 61.85  ? 369 PHE A C   1 
ATOM 2963 O O   . PHE A 1 386 ? 123.238 124.103 117.148 1.00 61.85  ? 369 PHE A O   1 
ATOM 2964 C CB  . PHE A 1 386 ? 122.018 126.620 115.249 1.00 61.85  ? 369 PHE A CB  1 
ATOM 2965 C CG  . PHE A 1 386 ? 120.821 127.232 114.593 1.00 61.85  ? 369 PHE A CG  1 
ATOM 2966 C CD1 . PHE A 1 386 ? 120.425 126.826 113.331 1.00 61.85  ? 369 PHE A CD1 1 
ATOM 2967 C CD2 . PHE A 1 386 ? 120.077 128.196 115.245 1.00 61.85  ? 369 PHE A CD2 1 
ATOM 2968 C CE1 . PHE A 1 386 ? 119.319 127.384 112.724 1.00 61.85  ? 369 PHE A CE1 1 
ATOM 2969 C CE2 . PHE A 1 386 ? 118.972 128.754 114.647 1.00 61.85  ? 369 PHE A CE2 1 
ATOM 2970 C CZ  . PHE A 1 386 ? 118.591 128.349 113.384 1.00 61.85  ? 369 PHE A CZ  1 
ATOM 2971 N N   . ASP A 1 387 ? 124.312 124.644 115.248 1.00 64.16  ? 370 ASP A N   1 
ATOM 2972 C CA  . ASP A 1 387 ? 125.576 124.119 115.727 1.00 64.16  ? 370 ASP A CA  1 
ATOM 2973 C C   . ASP A 1 387 ? 126.113 124.961 116.879 1.00 64.16  ? 370 ASP A C   1 
ATOM 2974 O O   . ASP A 1 387 ? 125.669 126.084 117.132 1.00 64.16  ? 370 ASP A O   1 
ATOM 2975 C CB  . ASP A 1 387 ? 126.611 124.083 114.609 1.00 64.16  ? 370 ASP A CB  1 
ATOM 2976 C CG  . ASP A 1 387 ? 127.569 122.934 114.764 1.00 64.16  ? 370 ASP A CG  1 
ATOM 2977 O OD1 . ASP A 1 387 ? 127.316 122.084 115.636 1.00 64.16  ? 370 ASP A OD1 1 
ATOM 2978 O OD2 . ASP A 1 387 ? 128.594 122.903 114.061 1.00 64.16  ? 370 ASP A OD2 1 
ATOM 2979 N N   . LYS A 1 388 ? 127.092 124.395 117.581 1.00 59.75  ? 371 LYS A N   1 
ATOM 2980 C CA  . LYS A 1 388 ? 127.772 125.095 118.659 1.00 59.75  ? 371 LYS A CA  1 
ATOM 2981 C C   . LYS A 1 388 ? 129.289 125.021 118.584 1.00 59.75  ? 371 LYS A C   1 
ATOM 2982 O O   . LYS A 1 388 ? 129.953 125.840 119.230 1.00 59.75  ? 371 LYS A O   1 
ATOM 2983 C CB  . LYS A 1 388 ? 127.314 124.556 120.024 1.00 59.75  ? 371 LYS A CB  1 
ATOM 2984 C CG  . LYS A 1 388 ? 127.386 125.574 121.154 1.00 59.75  ? 371 LYS A CG  1 
ATOM 2985 C CD  . LYS A 1 388 ? 126.568 126.821 120.843 1.00 59.75  ? 371 LYS A CD  1 
ATOM 2986 C CE  . LYS A 1 388 ? 125.102 126.488 120.606 1.00 59.75  ? 371 LYS A CE  1 
ATOM 2987 N NZ  . LYS A 1 388 ? 124.369 127.626 119.985 1.00 59.75  ? 371 LYS A NZ  1 
ATOM 2988 N N   . ALA A 1 389 ? 129.862 124.087 117.825 1.00 58.29  ? 372 ALA A N   1 
ATOM 2989 C CA  . ALA A 1 389 ? 131.310 124.006 117.706 1.00 58.29  ? 372 ALA A CA  1 
ATOM 2990 C C   . ALA A 1 389 ? 131.682 123.395 116.362 1.00 58.29  ? 372 ALA A C   1 
ATOM 2991 O O   . ALA A 1 389 ? 130.849 122.814 115.663 1.00 58.29  ? 372 ALA A O   1 
ATOM 2992 C CB  . ALA A 1 389 ? 131.920 123.196 118.854 1.00 58.29  ? 372 ALA A CB  1 
ATOM 2993 N N   . VAL A 1 390 ? 132.957 123.530 116.010 1.00 52.62  ? 373 VAL A N   1 
ATOM 2994 C CA  . VAL A 1 390 ? 133.535 122.874 114.845 1.00 52.62  ? 373 VAL A CA  1 
ATOM 2995 C C   . VAL A 1 390 ? 134.715 122.036 115.316 1.00 52.62  ? 373 VAL A C   1 
ATOM 2996 O O   . VAL A 1 390 ? 135.499 122.472 116.167 1.00 52.62  ? 373 VAL A O   1 
ATOM 2997 C CB  . VAL A 1 390 ? 133.955 123.889 113.759 1.00 52.62  ? 373 VAL A CB  1 
ATOM 2998 C CG1 . VAL A 1 390 ? 135.079 124.793 114.249 1.00 52.62  ? 373 VAL A CG1 1 
ATOM 2999 C CG2 . VAL A 1 390 ? 134.363 123.164 112.486 1.00 52.62  ? 373 VAL A CG2 1 
ATOM 3000 N N   . PHE A 1 391 ? 134.821 120.816 114.794 1.00 50.86  ? 374 PHE A N   1 
ATOM 3001 C CA  . PHE A 1 391 ? 135.800 119.850 115.272 1.00 50.86  ? 374 PHE A CA  1 
ATOM 3002 C C   . PHE A 1 391 ? 136.700 119.412 114.127 1.00 50.86  ? 374 PHE A C   1 
ATOM 3003 O O   . PHE A 1 391 ? 136.213 119.067 113.045 1.00 50.86  ? 374 PHE A O   1 
ATOM 3004 C CB  . PHE A 1 391 ? 135.108 118.633 115.891 1.00 50.86  ? 374 PHE A CB  1 
ATOM 3005 C CG  . PHE A 1 391 ? 134.495 118.904 117.233 1.00 50.86  ? 374 PHE A CG  1 
ATOM 3006 C CD1 . PHE A 1 391 ? 135.193 119.607 118.200 1.00 50.86  ? 374 PHE A CD1 1 
ATOM 3007 C CD2 . PHE A 1 391 ? 133.217 118.459 117.527 1.00 50.86  ? 374 PHE A CD2 1 
ATOM 3008 C CE1 . PHE A 1 391 ? 134.629 119.859 119.435 1.00 50.86  ? 374 PHE A CE1 1 
ATOM 3009 C CE2 . PHE A 1 391 ? 132.649 118.708 118.760 1.00 50.86  ? 374 PHE A CE2 1 
ATOM 3010 C CZ  . PHE A 1 391 ? 133.355 119.409 119.715 1.00 50.86  ? 374 PHE A CZ  1 
ATOM 3011 N N   . LYS A 1 392 ? 138.008 119.427 114.370 1.00 49.85  ? 375 LYS A N   1 
ATOM 3012 C CA  . LYS A 1 392 ? 138.983 118.907 113.421 1.00 49.85  ? 375 LYS A CA  1 
ATOM 3013 C C   . LYS A 1 392 ? 139.151 117.414 113.669 1.00 49.85  ? 375 LYS A C   1 
ATOM 3014 O O   . LYS A 1 392 ? 139.462 116.998 114.790 1.00 49.85  ? 375 LYS A O   1 
ATOM 3015 C CB  . LYS A 1 392 ? 140.320 119.634 113.560 1.00 49.85  ? 375 LYS A CB  1 
ATOM 3016 C CG  . LYS A 1 392 ? 141.527 118.834 113.091 1.00 49.85  ? 375 LYS A CG  1 
ATOM 3017 C CD  . LYS A 1 392 ? 141.534 118.665 111.581 1.00 49.85  ? 375 LYS A CD  1 
ATOM 3018 C CE  . LYS A 1 392 ? 142.952 118.554 111.047 1.00 49.85  ? 375 LYS A CE  1 
ATOM 3019 N NZ  . LYS A 1 392 ? 142.992 117.889 109.716 1.00 49.85  ? 375 LYS A NZ  1 
ATOM 3020 N N   . ILE A 1 393 ? 138.940 116.611 112.627 1.00 49.85  ? 376 ILE A N   1 
ATOM 3021 C CA  . ILE A 1 393 ? 138.974 115.161 112.739 1.00 49.85  ? 376 ILE A CA  1 
ATOM 3022 C C   . ILE A 1 393 ? 139.901 114.596 111.673 1.00 49.85  ? 376 ILE A C   1 
ATOM 3023 O O   . ILE A 1 393 ? 140.172 115.224 110.647 1.00 49.85  ? 376 ILE A O   1 
ATOM 3024 C CB  . ILE A 1 393 ? 137.566 114.533 112.616 1.00 49.85  ? 376 ILE A CB  1 
ATOM 3025 C CG1 . ILE A 1 393 ? 137.150 114.423 111.148 1.00 49.85  ? 376 ILE A CG1 1 
ATOM 3026 C CG2 . ILE A 1 393 ? 136.542 115.334 113.402 1.00 49.85  ? 376 ILE A CG2 1 
ATOM 3027 C CD1 . ILE A 1 393 ? 135.794 113.788 110.946 1.00 49.85  ? 376 ILE A CD1 1 
ATOM 3028 N N   . ASN A 1 394 ? 140.400 113.391 111.941 1.00 49.85  ? 377 ASN A N   1 
ATOM 3029 C CA  . ASN A 1 394 ? 141.184 112.624 110.981 1.00 49.85  ? 377 ASN A CA  1 
ATOM 3030 C C   . ASN A 1 394 ? 140.519 111.267 110.823 1.00 49.85  ? 377 ASN A C   1 
ATOM 3031 O O   . ASN A 1 394 ? 140.311 110.558 111.812 1.00 49.85  ? 377 ASN A O   1 
ATOM 3032 C CB  . ASN A 1 394 ? 142.637 112.468 111.438 1.00 49.85  ? 377 ASN A CB  1 
ATOM 3033 C CG  . ASN A 1 394 ? 143.505 111.791 110.396 1.00 49.85  ? 377 ASN A CG  1 
ATOM 3034 O OD1 . ASN A 1 394 ? 143.093 111.607 109.251 1.00 49.85  ? 377 ASN A OD1 1 
ATOM 3035 N ND2 . ASN A 1 394 ? 144.716 111.414 110.790 1.00 49.85  ? 377 ASN A ND2 1 
ATOM 3036 N N   . ILE A 1 395 ? 140.188 110.908 109.586 1.00 49.85  ? 378 ILE A N   1 
ATOM 3037 C CA  . ILE A 1 395 ? 139.392 109.715 109.327 1.00 49.85  ? 378 ILE A CA  1 
ATOM 3038 C C   . ILE A 1 395 ? 140.073 108.850 108.277 1.00 49.85  ? 378 ILE A C   1 
ATOM 3039 O O   . ILE A 1 395 ? 139.452 107.952 107.697 1.00 49.85  ? 378 ILE A O   1 
ATOM 3040 C CB  . ILE A 1 395 ? 137.969 110.101 108.892 1.00 49.85  ? 378 ILE A CB  1 
ATOM 3041 C CG1 . ILE A 1 395 ? 138.026 111.192 107.825 1.00 49.85  ? 378 ILE A CG1 1 
ATOM 3042 C CG2 . ILE A 1 395 ? 137.164 110.576 110.087 1.00 49.85  ? 378 ILE A CG2 1 
ATOM 3043 C CD1 . ILE A 1 395 ? 136.688 111.802 107.515 1.00 49.85  ? 378 ILE A CD1 1 
ATOM 3044 N N   . VAL A 1 396 ? 141.350 109.115 108.025 1.00 49.85  ? 379 VAL A N   1 
ATOM 3045 C CA  . VAL A 1 396 ? 142.135 108.313 107.089 1.00 49.85  ? 379 VAL A CA  1 
ATOM 3046 C C   . VAL A 1 396 ? 142.544 106.997 107.750 1.00 49.85  ? 379 VAL A C   1 
ATOM 3047 O O   . VAL A 1 396 ? 142.299 105.932 107.166 1.00 49.85  ? 379 VAL A O   1 
ATOM 3048 C CB  . VAL A 1 396 ? 143.352 109.095 106.566 1.00 49.85  ? 379 VAL A CB  1 
ATOM 3049 C CG1 . VAL A 1 396 ? 144.286 108.175 105.795 1.00 49.85  ? 379 VAL A CG1 1 
ATOM 3050 C CG2 . VAL A 1 396 ? 142.897 110.258 105.703 1.00 49.85  ? 379 VAL A CG2 1 
ATOM 3051 N N   . PRO A 1 397 ? 143.161 106.993 108.938 1.00 49.85  ? 380 PRO A N   1 
ATOM 3052 C CA  . PRO A 1 397 ? 143.492 105.711 109.570 1.00 49.85  ? 380 PRO A CA  1 
ATOM 3053 C C   . PRO A 1 397 ? 142.243 104.957 109.995 1.00 49.85  ? 380 PRO A C   1 
ATOM 3054 O O   . PRO A 1 397 ? 141.211 105.546 110.323 1.00 49.85  ? 380 PRO A O   1 
ATOM 3055 C CB  . PRO A 1 397 ? 144.338 106.115 110.786 1.00 49.85  ? 380 PRO A CB  1 
ATOM 3056 C CG  . PRO A 1 397 ? 144.753 107.522 110.525 1.00 49.85  ? 380 PRO A CG  1 
ATOM 3057 C CD  . PRO A 1 397 ? 143.611 108.116 109.780 1.00 49.85  ? 380 PRO A CD  1 
ATOM 3058 N N   . LYS A 1 398 ? 142.352 103.627 109.989 1.00 49.85  ? 381 LYS A N   1 
ATOM 3059 C CA  . LYS A 1 398 ? 141.224 102.785 110.370 1.00 49.85  ? 381 LYS A CA  1 
ATOM 3060 C C   . LYS A 1 398 ? 140.989 102.766 111.874 1.00 49.85  ? 381 LYS A C   1 
ATOM 3061 O O   . LYS A 1 398 ? 139.908 102.361 112.313 1.00 49.85  ? 381 LYS A O   1 
ATOM 3062 C CB  . LYS A 1 398 ? 141.438 101.360 109.862 1.00 49.85  ? 381 LYS A CB  1 
ATOM 3063 C CG  . LYS A 1 398 ? 141.257 101.205 108.362 1.00 49.85  ? 381 LYS A CG  1 
ATOM 3064 C CD  . LYS A 1 398 ? 140.962 99.762  107.983 1.00 49.85  ? 381 LYS A CD  1 
ATOM 3065 C CE  . LYS A 1 398 ? 140.024 99.101  108.983 1.00 49.85  ? 381 LYS A CE  1 
ATOM 3066 N NZ  . LYS A 1 398 ? 138.648 99.664  108.912 1.00 49.85  ? 381 LYS A NZ  1 
ATOM 3067 N N   . VAL A 1 399 ? 141.970 103.192 112.674 1.00 49.85  ? 382 VAL A N   1 
ATOM 3068 C CA  . VAL A 1 399 ? 141.808 103.199 114.123 1.00 49.85  ? 382 VAL A CA  1 
ATOM 3069 C C   . VAL A 1 399 ? 140.905 104.320 114.610 1.00 49.85  ? 382 VAL A C   1 
ATOM 3070 O O   . VAL A 1 399 ? 140.562 104.354 115.797 1.00 49.85  ? 382 VAL A O   1 
ATOM 3071 C CB  . VAL A 1 399 ? 143.179 103.301 114.823 1.00 49.85  ? 382 VAL A CB  1 
ATOM 3072 C CG1 . VAL A 1 399 ? 144.150 102.292 114.235 1.00 49.85  ? 382 VAL A CG1 1 
ATOM 3073 C CG2 . VAL A 1 399 ? 143.733 104.711 114.705 1.00 49.85  ? 382 VAL A CG2 1 
ATOM 3074 N N   . ASN A 1 400 ? 140.513 105.237 113.730 1.00 49.85  ? 383 ASN A N   1 
ATOM 3075 C CA  . ASN A 1 400 ? 139.635 106.340 114.092 1.00 49.85  ? 383 ASN A CA  1 
ATOM 3076 C C   . ASN A 1 400 ? 138.283 106.306 113.400 1.00 49.85  ? 383 ASN A C   1 
ATOM 3077 O O   . ASN A 1 400 ? 137.321 106.859 113.936 1.00 49.85  ? 383 ASN A O   1 
ATOM 3078 C CB  . ASN A 1 400 ? 140.305 107.687 113.778 1.00 49.85  ? 383 ASN A CB  1 
ATOM 3079 C CG  . ASN A 1 400 ? 141.801 107.663 114.008 1.00 49.85  ? 383 ASN A CG  1 
ATOM 3080 O OD1 . ASN A 1 400 ? 142.586 107.665 113.060 1.00 49.85  ? 383 ASN A OD1 1 
ATOM 3081 N ND2 . ASN A 1 400 ? 142.205 107.647 115.272 1.00 49.85  ? 383 ASN A ND2 1 
ATOM 3082 N N   . TYR A 1 401 ? 138.181 105.673 112.234 1.00 49.85  ? 384 TYR A N   1 
ATOM 3083 C CA  . TYR A 1 401 ? 136.960 105.735 111.436 1.00 49.85  ? 384 TYR A CA  1 
ATOM 3084 C C   . TYR A 1 401 ? 137.011 104.612 110.416 1.00 49.85  ? 384 TYR A C   1 
ATOM 3085 O O   . TYR A 1 401 ? 137.977 104.520 109.652 1.00 49.85  ? 384 TYR A O   1 
ATOM 3086 C CB  . TYR A 1 401 ? 136.846 107.095 110.750 1.00 49.85  ? 384 TYR A CB  1 
ATOM 3087 C CG  . TYR A 1 401 ? 135.514 107.392 110.100 1.00 49.85  ? 384 TYR A CG  1 
ATOM 3088 C CD1 . TYR A 1 401 ? 135.231 106.960 108.811 1.00 49.85  ? 384 TYR A CD1 1 
ATOM 3089 C CD2 . TYR A 1 401 ? 134.548 108.129 110.769 1.00 49.85  ? 384 TYR A CD2 1 
ATOM 3090 C CE1 . TYR A 1 401 ? 134.017 107.244 108.215 1.00 49.85  ? 384 TYR A CE1 1 
ATOM 3091 C CE2 . TYR A 1 401 ? 133.335 108.415 110.182 1.00 49.85  ? 384 TYR A CE2 1 
ATOM 3092 C CZ  . TYR A 1 401 ? 133.073 107.972 108.907 1.00 49.85  ? 384 TYR A CZ  1 
ATOM 3093 O OH  . TYR A 1 401 ? 131.860 108.264 108.330 1.00 49.85  ? 384 TYR A OH  1 
ATOM 3094 N N   . THR A 1 402 ? 135.986 103.769 110.396 1.00 49.85  ? 385 THR A N   1 
ATOM 3095 C CA  . THR A 1 402 ? 135.950 102.621 109.505 1.00 49.85  ? 385 THR A CA  1 
ATOM 3096 C C   . THR A 1 402 ? 134.856 102.794 108.459 1.00 49.85  ? 385 THR A C   1 
ATOM 3097 O O   . THR A 1 402 ? 133.946 103.615 108.603 1.00 49.85  ? 385 THR A O   1 
ATOM 3098 C CB  . THR A 1 402 ? 135.738 101.321 110.290 1.00 49.85  ? 385 THR A CB  1 
ATOM 3099 O OG1 . THR A 1 402 ? 136.281 100.219 109.551 1.00 49.85  ? 385 THR A OG1 1 
ATOM 3100 C CG2 . THR A 1 402 ? 134.263 101.078 110.546 1.00 49.85  ? 385 THR A CG2 1 
ATOM 3101 N N   . ILE A 1 403 ? 134.972 102.008 107.387 1.00 49.85  ? 386 ILE A N   1 
ATOM 3102 C CA  . ILE A 1 403 ? 134.050 102.127 106.260 1.00 49.85  ? 386 ILE A CA  1 
ATOM 3103 C C   . ILE A 1 403 ? 132.635 101.748 106.681 1.00 49.85  ? 386 ILE A C   1 
ATOM 3104 O O   . ILE A 1 403 ? 131.663 102.438 106.353 1.00 49.85  ? 386 ILE A O   1 
ATOM 3105 C CB  . ILE A 1 403 ? 134.536 101.266 105.081 1.00 49.85  ? 386 ILE A CB  1 
ATOM 3106 C CG1 . ILE A 1 403 ? 135.745 101.914 104.405 1.00 49.85  ? 386 ILE A CG1 1 
ATOM 3107 C CG2 . ILE A 1 403 ? 133.417 101.046 104.075 1.00 49.85  ? 386 ILE A CG2 1 
ATOM 3108 C CD1 . ILE A 1 403 ? 136.519 100.972 103.508 1.00 49.85  ? 386 ILE A CD1 1 
ATOM 3109 N N   . TYR A 1 404 ? 132.500 100.649 107.423 1.00 51.30  ? 387 TYR A N   1 
ATOM 3110 C CA  . TYR A 1 404 ? 131.179 100.081 107.673 1.00 51.30  ? 387 TYR A CA  1 
ATOM 3111 C C   . TYR A 1 404 ? 130.440 100.812 108.789 1.00 51.30  ? 387 TYR A C   1 
ATOM 3112 O O   . TYR A 1 404 ? 129.282 101.209 108.618 1.00 51.30  ? 387 TYR A O   1 
ATOM 3113 C CB  . TYR A 1 404 ? 131.309 98.593  108.004 1.00 51.30  ? 387 TYR A CB  1 
ATOM 3114 C CG  . TYR A 1 404 ? 131.793 97.750  106.848 1.00 51.30  ? 387 TYR A CG  1 
ATOM 3115 C CD1 . TYR A 1 404 ? 131.510 98.108  105.537 1.00 51.30  ? 387 TYR A CD1 1 
ATOM 3116 C CD2 . TYR A 1 404 ? 132.536 96.598  107.066 1.00 51.30  ? 387 TYR A CD2 1 
ATOM 3117 C CE1 . TYR A 1 404 ? 131.951 97.341  104.476 1.00 51.30  ? 387 TYR A CE1 1 
ATOM 3118 C CE2 . TYR A 1 404 ? 132.981 95.825  106.013 1.00 51.30  ? 387 TYR A CE2 1 
ATOM 3119 C CZ  . TYR A 1 404 ? 132.686 96.201  104.720 1.00 51.30  ? 387 TYR A CZ  1 
ATOM 3120 O OH  . TYR A 1 404 ? 133.127 95.434  103.666 1.00 51.30  ? 387 TYR A OH  1 
ATOM 3121 N N   . ASP A 1 405 ? 131.089 100.999 109.938 1.00 52.07  ? 388 ASP A N   1 
ATOM 3122 C CA  . ASP A 1 405 ? 130.414 101.520 111.119 1.00 52.07  ? 388 ASP A CA  1 
ATOM 3123 C C   . ASP A 1 405 ? 130.648 103.004 111.364 1.00 52.07  ? 388 ASP A C   1 
ATOM 3124 O O   . ASP A 1 405 ? 129.868 103.621 112.097 1.00 52.07  ? 388 ASP A O   1 
ATOM 3125 C CB  . ASP A 1 405 ? 130.852 100.742 112.366 1.00 52.07  ? 388 ASP A CB  1 
ATOM 3126 C CG  . ASP A 1 405 ? 130.739 99.242  112.187 1.00 52.07  ? 388 ASP A CG  1 
ATOM 3127 O OD1 . ASP A 1 405 ? 130.413 98.797  111.068 1.00 52.07  ? 388 ASP A OD1 1 
ATOM 3128 O OD2 . ASP A 1 405 ? 130.973 98.508  113.169 1.00 52.07  ? 388 ASP A OD2 1 
ATOM 3129 N N   . GLY A 1 406 ? 131.688 103.592 110.780 1.00 49.85  ? 389 GLY A N   1 
ATOM 3130 C CA  . GLY A 1 406 ? 131.980 104.986 111.052 1.00 49.85  ? 389 GLY A CA  1 
ATOM 3131 C C   . GLY A 1 406 ? 132.659 105.170 112.400 1.00 49.85  ? 389 GLY A C   1 
ATOM 3132 O O   . GLY A 1 406 ? 133.493 104.366 112.820 1.00 49.85  ? 389 GLY A O   1 
ATOM 3133 N N   . PHE A 1 407 ? 132.293 106.258 113.084 1.00 49.85  ? 390 PHE A N   1 
ATOM 3134 C CA  . PHE A 1 407 ? 132.884 106.539 114.388 1.00 49.85  ? 390 PHE A CA  1 
ATOM 3135 C C   . PHE A 1 407 ? 132.535 105.466 115.411 1.00 49.85  ? 390 PHE A C   1 
ATOM 3136 O O   . PHE A 1 407 ? 133.385 105.086 116.224 1.00 49.85  ? 390 PHE A O   1 
ATOM 3137 C CB  . PHE A 1 407 ? 132.431 107.909 114.894 1.00 49.85  ? 390 PHE A CB  1 
ATOM 3138 C CG  . PHE A 1 407 ? 133.098 109.060 114.204 1.00 49.85  ? 390 PHE A CG  1 
ATOM 3139 C CD1 . PHE A 1 407 ? 134.369 109.462 114.574 1.00 49.85  ? 390 PHE A CD1 1 
ATOM 3140 C CD2 . PHE A 1 407 ? 132.449 109.754 113.199 1.00 49.85  ? 390 PHE A CD2 1 
ATOM 3141 C CE1 . PHE A 1 407 ? 134.986 110.520 113.945 1.00 49.85  ? 390 PHE A CE1 1 
ATOM 3142 C CE2 . PHE A 1 407 ? 133.060 110.817 112.569 1.00 49.85  ? 390 PHE A CE2 1 
ATOM 3143 C CZ  . PHE A 1 407 ? 134.330 111.201 112.942 1.00 49.85  ? 390 PHE A CZ  1 
ATOM 3144 N N   . ASN A 1 408 ? 131.299 104.968 115.389 1.00 52.59  ? 391 ASN A N   1 
ATOM 3145 C CA  . ASN A 1 408 ? 130.848 103.959 116.348 1.00 52.59  ? 391 ASN A CA  1 
ATOM 3146 C C   . ASN A 1 408 ? 131.434 102.599 115.965 1.00 52.59  ? 391 ASN A C   1 
ATOM 3147 O O   . ASN A 1 408 ? 130.767 101.720 115.416 1.00 52.59  ? 391 ASN A O   1 
ATOM 3148 C CB  . ASN A 1 408 ? 129.327 103.924 116.406 1.00 52.59  ? 391 ASN A CB  1 
ATOM 3149 C CG  . ASN A 1 408 ? 128.741 105.169 117.038 1.00 52.59  ? 391 ASN A CG  1 
ATOM 3150 O OD1 . ASN A 1 408 ? 129.304 105.725 117.981 1.00 52.59  ? 391 ASN A OD1 1 
ATOM 3151 N ND2 . ASN A 1 408 ? 127.605 105.618 116.518 1.00 52.59  ? 391 ASN A ND2 1 
ATOM 3152 N N   . LEU A 1 409 ? 132.720 102.442 116.271 1.00 49.85  ? 392 LEU A N   1 
ATOM 3153 C CA  . LEU A 1 409 ? 133.424 101.209 115.949 1.00 49.85  ? 392 LEU A CA  1 
ATOM 3154 C C   . LEU A 1 409 ? 132.838 100.037 116.729 1.00 49.85  ? 392 LEU A C   1 
ATOM 3155 O O   . LEU A 1 409 ? 132.368 100.185 117.860 1.00 49.85  ? 392 LEU A O   1 
ATOM 3156 C CB  . LEU A 1 409 ? 134.915 101.357 116.257 1.00 49.85  ? 392 LEU A CB  1 
ATOM 3157 C CG  . LEU A 1 409 ? 135.861 101.376 115.055 1.00 49.85  ? 392 LEU A CG  1 
ATOM 3158 C CD1 . LEU A 1 409 ? 137.287 101.084 115.489 1.00 49.85  ? 392 LEU A CD1 1 
ATOM 3159 C CD2 . LEU A 1 409 ? 135.407 100.383 113.998 1.00 49.85  ? 392 LEU A CD2 1 
ATOM 3160 N N   . ARG A 1 410 ? 132.868 98.861  116.109 1.00 54.35  ? 393 ARG A N   1 
ATOM 3161 C CA  . ARG A 1 410 ? 132.288 97.675  116.717 1.00 54.35  ? 393 ARG A CA  1 
ATOM 3162 C C   . ARG A 1 410 ? 133.243 97.056  117.734 1.00 54.35  ? 393 ARG A C   1 
ATOM 3163 O O   . ARG A 1 410 ? 134.457 97.277  117.704 1.00 54.35  ? 393 ARG A O   1 
ATOM 3164 C CB  . ARG A 1 410 ? 131.932 96.639  115.651 1.00 54.35  ? 393 ARG A CB  1 
ATOM 3165 C CG  . ARG A 1 410 ? 133.003 96.446  114.593 1.00 54.35  ? 393 ARG A CG  1 
ATOM 3166 C CD  . ARG A 1 410 ? 132.684 95.256  113.703 1.00 54.35  ? 393 ARG A CD  1 
ATOM 3167 N NE  . ARG A 1 410 ? 131.550 95.516  112.825 1.00 54.35  ? 393 ARG A NE  1 
ATOM 3168 C CZ  . ARG A 1 410 ? 131.287 94.831  111.720 1.00 54.35  ? 393 ARG A CZ  1 
ATOM 3169 N NH1 . ARG A 1 410 ? 132.061 93.835  111.324 1.00 54.35  ? 393 ARG A NH1 1 
ATOM 3170 N NH2 . ARG A 1 410 ? 130.219 95.153  110.996 1.00 54.35  ? 393 ARG A NH2 1 
ATOM 3171 N N   . ASN A 1 411 ? 132.666 96.267  118.643 1.00 65.19  ? 394 ASN A N   1 
ATOM 3172 C CA  . ASN A 1 411 ? 133.414 95.505  119.644 1.00 65.19  ? 394 ASN A CA  1 
ATOM 3173 C C   . ASN A 1 411 ? 134.289 96.401  120.515 1.00 65.19  ? 394 ASN A C   1 
ATOM 3174 O O   . ASN A 1 411 ? 135.370 95.998  120.952 1.00 65.19  ? 394 ASN A O   1 
ATOM 3175 C CB  . ASN A 1 411 ? 134.260 94.410  118.987 1.00 65.19  ? 394 ASN A CB  1 
ATOM 3176 C CG  . ASN A 1 411 ? 133.432 93.468  118.136 1.00 65.19  ? 394 ASN A CG  1 
ATOM 3177 O OD1 . ASN A 1 411 ? 132.295 93.144  118.478 1.00 65.19  ? 394 ASN A OD1 1 
ATOM 3178 N ND2 . ASN A 1 411 ? 133.999 93.024  117.021 1.00 65.19  ? 394 ASN A ND2 1 
ATOM 3179 N N   . THR A 1 412 ? 133.832 97.625  120.774 1.00 59.60  ? 395 THR A N   1 
ATOM 3180 C CA  . THR A 1 412 ? 134.533 98.536  121.671 1.00 59.60  ? 395 THR A CA  1 
ATOM 3181 C C   . THR A 1 412 ? 133.550 99.158  122.654 1.00 59.60  ? 395 THR A C   1 
ATOM 3182 O O   . THR A 1 412 ? 132.372 98.788  122.679 1.00 59.60  ? 395 THR A O   1 
ATOM 3183 C CB  . THR A 1 412 ? 135.259 99.635  120.889 1.00 59.60  ? 395 THR A CB  1 
ATOM 3184 O OG1 . THR A 1 412 ? 134.298 100.474 120.236 1.00 59.60  ? 395 THR A OG1 1 
ATOM 3185 C CG2 . THR A 1 412 ? 136.206 99.041  119.853 1.00 59.60  ? 395 THR A CG2 1 
ATOM 3186 N N   . ASN A 1 413 ? 134.022 100.103 123.466 1.00 64.72  ? 396 ASN A N   1 
ATOM 3187 C CA  . ASN A 1 413 ? 133.140 100.817 124.378 1.00 64.72  ? 396 ASN A CA  1 
ATOM 3188 C C   . ASN A 1 413 ? 132.383 101.949 123.698 1.00 64.72  ? 396 ASN A C   1 
ATOM 3189 O O   . ASN A 1 413 ? 131.485 102.531 124.315 1.00 64.72  ? 396 ASN A O   1 
ATOM 3190 C CB  . ASN A 1 413 ? 133.939 101.373 125.560 1.00 64.72  ? 396 ASN A CB  1 
ATOM 3191 C CG  . ASN A 1 413 ? 134.830 102.533 125.166 1.00 64.72  ? 396 ASN A CG  1 
ATOM 3192 O OD1 . ASN A 1 413 ? 135.761 102.375 124.376 1.00 64.72  ? 396 ASN A OD1 1 
ATOM 3193 N ND2 . ASN A 1 413 ? 134.550 103.709 125.716 1.00 64.72  ? 396 ASN A ND2 1 
ATOM 3194 N N   . LEU A 1 414 ? 132.723 102.272 122.452 1.00 66.08  ? 397 LEU A N   1 
ATOM 3195 C CA  . LEU A 1 414 ? 132.057 103.326 121.701 1.00 66.08  ? 397 LEU A CA  1 
ATOM 3196 C C   . LEU A 1 414 ? 130.950 102.802 120.797 1.00 66.08  ? 397 LEU A C   1 
ATOM 3197 O O   . LEU A 1 414 ? 130.322 103.595 120.088 1.00 66.08  ? 397 LEU A O   1 
ATOM 3198 C CB  . LEU A 1 414 ? 133.079 104.107 120.865 1.00 66.08  ? 397 LEU A CB  1 
ATOM 3199 C CG  . LEU A 1 414 ? 134.443 104.422 121.490 1.00 66.08  ? 397 LEU A CG  1 
ATOM 3200 C CD1 . LEU A 1 414 ? 135.473 103.351 121.157 1.00 66.08  ? 397 LEU A CD1 1 
ATOM 3201 C CD2 . LEU A 1 414 ? 134.935 105.795 121.055 1.00 66.08  ? 397 LEU A CD2 1 
ATOM 3202 N N   . ALA A 1 415 ? 130.694 101.492 120.803 1.00 62.83  ? 398 ALA A N   1 
ATOM 3203 C CA  . ALA A 1 415 ? 129.671 100.934 119.924 1.00 62.83  ? 398 ALA A CA  1 
ATOM 3204 C C   . ALA A 1 415 ? 128.268 101.258 120.423 1.00 62.83  ? 398 ALA A C   1 
ATOM 3205 O O   . ALA A 1 415 ? 127.374 101.557 119.624 1.00 62.83  ? 398 ALA A O   1 
ATOM 3206 C CB  . ALA A 1 415 ? 129.857 99.422  119.796 1.00 62.83  ? 398 ALA A CB  1 
ATOM 3207 N N   . ALA A 1 416 ? 128.056 101.205 121.732 1.00 73.14  ? 399 ALA A N   1 
ATOM 3208 C CA  . ALA A 1 416 ? 126.745 101.425 122.322 1.00 73.14  ? 399 ALA A CA  1 
ATOM 3209 C C   . ALA A 1 416 ? 126.603 102.864 122.805 1.00 73.14  ? 399 ALA A C   1 
ATOM 3210 O O   . ALA A 1 416 ? 127.585 103.547 123.106 1.00 73.14  ? 399 ALA A O   1 
ATOM 3211 C CB  . ALA A 1 416 ? 126.505 100.457 123.483 1.00 73.14  ? 399 ALA A CB  1 
ATOM 3212 N N   . ASN A 1 417 ? 125.352 103.319 122.863 1.00 76.35  ? 400 ASN A N   1 
ATOM 3213 C CA  . ASN A 1 417 ? 124.966 104.645 123.339 1.00 76.35  ? 400 ASN A CA  1 
ATOM 3214 C C   . ASN A 1 417 ? 125.565 105.774 122.509 1.00 76.35  ? 400 ASN A C   1 
ATOM 3215 O O   . ASN A 1 417 ? 125.532 106.934 122.940 1.00 76.35  ? 400 ASN A O   1 
ATOM 3216 C CB  . ASN A 1 417 ? 125.330 104.838 124.817 1.00 76.35  ? 400 ASN A CB  1 
ATOM 3217 C CG  . ASN A 1 417 ? 124.753 103.755 125.706 1.00 76.35  ? 400 ASN A CG  1 
ATOM 3218 O OD1 . ASN A 1 417 ? 123.558 103.463 125.653 1.00 76.35  ? 400 ASN A OD1 1 
ATOM 3219 N ND2 . ASN A 1 417 ? 125.602 103.150 126.528 1.00 76.35  ? 400 ASN A ND2 1 
ATOM 3220 N N   . PHE A 1 418 ? 126.100 105.467 121.328 1.00 66.02  ? 401 PHE A N   1 
ATOM 3221 C CA  . PHE A 1 418 ? 126.723 106.456 120.449 1.00 66.02  ? 401 PHE A CA  1 
ATOM 3222 C C   . PHE A 1 418 ? 127.803 107.249 121.183 1.00 66.02  ? 401 PHE A C   1 
ATOM 3223 O O   . PHE A 1 418 ? 127.898 108.474 121.076 1.00 66.02  ? 401 PHE A O   1 
ATOM 3224 C CB  . PHE A 1 418 ? 125.673 107.386 119.839 1.00 66.02  ? 401 PHE A CB  1 
ATOM 3225 C CG  . PHE A 1 418 ? 124.534 106.663 119.181 1.00 66.02  ? 401 PHE A CG  1 
ATOM 3226 C CD1 . PHE A 1 418 ? 124.735 105.947 118.014 1.00 66.02  ? 401 PHE A CD1 1 
ATOM 3227 C CD2 . PHE A 1 418 ? 123.263 106.699 119.729 1.00 66.02  ? 401 PHE A CD2 1 
ATOM 3228 C CE1 . PHE A 1 418 ? 123.690 105.280 117.405 1.00 66.02  ? 401 PHE A CE1 1 
ATOM 3229 C CE2 . PHE A 1 418 ? 122.214 106.035 119.123 1.00 66.02  ? 401 PHE A CE2 1 
ATOM 3230 C CZ  . PHE A 1 418 ? 122.428 105.324 117.959 1.00 66.02  ? 401 PHE A CZ  1 
ATOM 3231 N N   . ASN A 1 419 ? 128.625 106.529 121.950 1.00 68.59  ? 402 ASN A N   1 
ATOM 3232 C CA  . ASN A 1 419 ? 129.761 107.157 122.614 1.00 68.59  ? 402 ASN A CA  1 
ATOM 3233 C C   . ASN A 1 419 ? 130.875 107.506 121.637 1.00 68.59  ? 402 ASN A C   1 
ATOM 3234 O O   . ASN A 1 419 ? 131.706 108.366 121.946 1.00 68.59  ? 402 ASN A O   1 
ATOM 3235 C CB  . ASN A 1 419 ? 130.300 106.245 123.716 1.00 68.59  ? 402 ASN A CB  1 
ATOM 3236 C CG  . ASN A 1 419 ? 129.509 106.357 125.004 1.00 68.59  ? 402 ASN A CG  1 
ATOM 3237 O OD1 . ASN A 1 419 ? 128.691 107.262 125.166 1.00 68.59  ? 402 ASN A OD1 1 
ATOM 3238 N ND2 . ASN A 1 419 ? 129.750 105.437 125.930 1.00 68.59  ? 402 ASN A ND2 1 
ATOM 3239 N N   . GLY A 1 420 ? 130.914 106.854 120.472 1.00 63.26  ? 403 GLY A N   1 
ATOM 3240 C CA  . GLY A 1 420 ? 131.936 107.164 119.488 1.00 63.26  ? 403 GLY A CA  1 
ATOM 3241 C C   . GLY A 1 420 ? 131.834 108.572 118.940 1.00 63.26  ? 403 GLY A C   1 
ATOM 3242 O O   . GLY A 1 420 ? 132.852 109.200 118.637 1.00 63.26  ? 403 GLY A O   1 
ATOM 3243 N N   . GLN A 1 421 ? 130.616 109.087 118.805 1.00 53.37  ? 404 GLN A N   1 
ATOM 3244 C CA  . GLN A 1 421 ? 130.393 110.433 118.299 1.00 53.37  ? 404 GLN A CA  1 
ATOM 3245 C C   . GLN A 1 421 ? 130.373 111.481 119.402 1.00 53.37  ? 404 GLN A C   1 
ATOM 3246 O O   . GLN A 1 421 ? 130.160 112.662 119.111 1.00 53.37  ? 404 GLN A O   1 
ATOM 3247 C CB  . GLN A 1 421 ? 129.081 110.484 117.511 1.00 53.37  ? 404 GLN A CB  1 
ATOM 3248 C CG  . GLN A 1 421 ? 129.136 109.737 116.191 1.00 53.37  ? 404 GLN A CG  1 
ATOM 3249 C CD  . GLN A 1 421 ? 127.762 109.438 115.634 1.00 53.37  ? 404 GLN A CD  1 
ATOM 3250 O OE1 . GLN A 1 421 ? 127.373 108.278 115.506 1.00 53.37  ? 404 GLN A OE1 1 
ATOM 3251 N NE2 . GLN A 1 421 ? 127.019 110.484 115.298 1.00 53.37  ? 404 GLN A NE2 1 
ATOM 3252 N N   . ASN A 1 422 ? 130.588 111.081 120.652 1.00 61.42  ? 405 ASN A N   1 
ATOM 3253 C CA  . ASN A 1 422 ? 130.636 112.028 121.755 1.00 61.42  ? 405 ASN A CA  1 
ATOM 3254 C C   . ASN A 1 422 ? 131.968 112.766 121.752 1.00 61.42  ? 405 ASN A C   1 
ATOM 3255 O O   . ASN A 1 422 ? 133.027 112.166 121.547 1.00 61.42  ? 405 ASN A O   1 
ATOM 3256 C CB  . ASN A 1 422 ? 130.434 111.303 123.086 1.00 61.42  ? 405 ASN A CB  1 
ATOM 3257 C CG  . ASN A 1 422 ? 130.128 112.251 124.233 1.00 61.42  ? 405 ASN A CG  1 
ATOM 3258 O OD1 . ASN A 1 422 ? 130.743 113.308 124.367 1.00 61.42  ? 405 ASN A OD1 1 
ATOM 3259 N ND2 . ASN A 1 422 ? 129.168 111.871 125.069 1.00 61.42  ? 405 ASN A ND2 1 
ATOM 3260 N N   . THR A 1 423 ? 131.910 114.077 121.977 1.00 67.37  ? 406 THR A N   1 
ATOM 3261 C CA  . THR A 1 423 ? 133.111 114.898 122.025 1.00 67.37  ? 406 THR A CA  1 
ATOM 3262 C C   . THR A 1 423 ? 133.754 114.934 123.404 1.00 67.37  ? 406 THR A C   1 
ATOM 3263 O O   . THR A 1 423 ? 134.840 115.506 123.547 1.00 67.37  ? 406 THR A O   1 
ATOM 3264 C CB  . THR A 1 423 ? 132.801 116.331 121.584 1.00 67.37  ? 406 THR A CB  1 
ATOM 3265 O OG1 . THR A 1 423 ? 133.948 117.159 121.813 1.00 67.37  ? 406 THR A OG1 1 
ATOM 3266 C CG2 . THR A 1 423 ? 131.631 116.883 122.375 1.00 67.37  ? 406 THR A CG2 1 
ATOM 3267 N N   . GLU A 1 424 ? 133.113 114.351 124.417 1.00 74.37  ? 407 GLU A N   1 
ATOM 3268 C CA  . GLU A 1 424 ? 133.678 114.299 125.758 1.00 74.37  ? 407 GLU A CA  1 
ATOM 3269 C C   . GLU A 1 424 ? 134.184 112.916 126.140 1.00 74.37  ? 407 GLU A C   1 
ATOM 3270 O O   . GLU A 1 424 ? 135.021 112.808 127.043 1.00 74.37  ? 407 GLU A O   1 
ATOM 3271 C CB  . GLU A 1 424 ? 132.642 114.760 126.790 1.00 74.37  ? 407 GLU A CB  1 
ATOM 3272 C CG  . GLU A 1 424 ? 132.272 116.230 126.679 1.00 74.37  ? 407 GLU A CG  1 
ATOM 3273 C CD  . GLU A 1 424 ? 132.031 116.875 128.030 1.00 74.37  ? 407 GLU A CD  1 
ATOM 3274 O OE1 . GLU A 1 424 ? 131.257 116.311 128.830 1.00 74.37  ? 407 GLU A OE1 1 
ATOM 3275 O OE2 . GLU A 1 424 ? 132.615 117.948 128.290 1.00 74.37  ? 407 GLU A OE2 1 
ATOM 3276 N N   . ILE A 1 425 ? 133.702 111.867 125.483 1.00 63.88  ? 408 ILE A N   1 
ATOM 3277 C CA  . ILE A 1 425 ? 134.173 110.506 125.715 1.00 63.88  ? 408 ILE A CA  1 
ATOM 3278 C C   . ILE A 1 425 ? 135.255 110.118 124.717 1.00 63.88  ? 408 ILE A C   1 
ATOM 3279 O O   . ILE A 1 425 ? 136.297 109.583 125.096 1.00 63.88  ? 408 ILE A O   1 
ATOM 3280 C CB  . ILE A 1 425 ? 132.988 109.517 125.672 1.00 63.88  ? 408 ILE A CB  1 
ATOM 3281 C CG1 . ILE A 1 425 ? 132.000 109.825 126.802 1.00 63.88  ? 408 ILE A CG1 1 
ATOM 3282 C CG2 . ILE A 1 425 ? 133.489 108.081 125.749 1.00 63.88  ? 408 ILE A CG2 1 
ATOM 3283 C CD1 . ILE A 1 425 ? 131.150 108.644 127.227 1.00 63.88  ? 408 ILE A CD1 1 
ATOM 3284 N N   . ASN A 1 426 ? 135.024 110.385 123.433 1.00 56.93  ? 409 ASN A N   1 
ATOM 3285 C CA  . ASN A 1 426 ? 136.020 110.133 122.392 1.00 56.93  ? 409 ASN A CA  1 
ATOM 3286 C C   . ASN A 1 426 ? 136.885 111.377 122.180 1.00 56.93  ? 409 ASN A C   1 
ATOM 3287 O O   . ASN A 1 426 ? 136.966 111.947 121.093 1.00 56.93  ? 409 ASN A O   1 
ATOM 3288 C CB  . ASN A 1 426 ? 135.334 109.700 121.101 1.00 56.93  ? 409 ASN A CB  1 
ATOM 3289 C CG  . ASN A 1 426 ? 136.277 108.997 120.146 1.00 56.93  ? 409 ASN A CG  1 
ATOM 3290 O OD1 . ASN A 1 426 ? 137.445 108.773 120.463 1.00 56.93  ? 409 ASN A OD1 1 
ATOM 3291 N ND2 . ASN A 1 426 ? 135.773 108.641 118.971 1.00 56.93  ? 409 ASN A ND2 1 
ATOM 3292 N N   . ASN A 1 427 ? 137.538 111.795 123.268 1.00 60.59  ? 410 ASN A N   1 
ATOM 3293 C CA  . ASN A 1 427 ? 138.324 113.026 123.244 1.00 60.59  ? 410 ASN A CA  1 
ATOM 3294 C C   . ASN A 1 427 ? 139.533 112.916 122.325 1.00 60.59  ? 410 ASN A C   1 
ATOM 3295 O O   . ASN A 1 427 ? 140.006 113.930 121.800 1.00 60.59  ? 410 ASN A O   1 
ATOM 3296 C CB  . ASN A 1 427 ? 138.775 113.386 124.660 1.00 60.59  ? 410 ASN A CB  1 
ATOM 3297 C CG  . ASN A 1 427 ? 137.634 113.870 125.532 1.00 60.59  ? 410 ASN A CG  1 
ATOM 3298 O OD1 . ASN A 1 427 ? 136.969 114.854 125.213 1.00 60.59  ? 410 ASN A OD1 1 
ATOM 3299 N ND2 . ASN A 1 427 ? 137.403 113.178 126.641 1.00 60.59  ? 410 ASN A ND2 1 
ATOM 3300 N N   . MET A 1 428 ? 140.049 111.703 122.118 1.00 59.65  ? 411 MET A N   1 
ATOM 3301 C CA  . MET A 1 428 ? 141.270 111.538 121.339 1.00 59.65  ? 411 MET A CA  1 
ATOM 3302 C C   . MET A 1 428 ? 141.055 111.782 119.851 1.00 59.65  ? 411 MET A C   1 
ATOM 3303 O O   . MET A 1 428 ? 142.021 112.083 119.141 1.00 59.65  ? 411 MET A O   1 
ATOM 3304 C CB  . MET A 1 428 ? 141.849 110.139 121.567 1.00 59.65  ? 411 MET A CB  1 
ATOM 3305 C CG  . MET A 1 428 ? 141.676 109.182 120.398 1.00 59.65  ? 411 MET A CG  1 
ATOM 3306 S SD  . MET A 1 428 ? 142.335 107.540 120.740 1.00 59.65  ? 411 MET A SD  1 
ATOM 3307 C CE  . MET A 1 428 ? 141.422 107.115 122.221 1.00 59.65  ? 411 MET A CE  1 
ATOM 3308 N N   . ASN A 1 429 ? 139.820 111.672 119.365 1.00 53.43  ? 412 ASN A N   1 
ATOM 3309 C CA  . ASN A 1 429 ? 139.540 111.797 117.942 1.00 53.43  ? 412 ASN A CA  1 
ATOM 3310 C C   . ASN A 1 429 ? 139.035 113.174 117.537 1.00 53.43  ? 412 ASN A C   1 
ATOM 3311 O O   . ASN A 1 429 ? 138.949 113.453 116.336 1.00 53.43  ? 412 ASN A O   1 
ATOM 3312 C CB  . ASN A 1 429 ? 138.514 110.741 117.512 1.00 53.43  ? 412 ASN A CB  1 
ATOM 3313 C CG  . ASN A 1 429 ? 139.071 109.776 116.493 1.00 53.43  ? 412 ASN A CG  1 
ATOM 3314 O OD1 . ASN A 1 429 ? 140.099 110.041 115.870 1.00 53.43  ? 412 ASN A OD1 1 
ATOM 3315 N ND2 . ASN A 1 429 ? 138.396 108.647 116.316 1.00 53.43  ? 412 ASN A ND2 1 
ATOM 3316 N N   . PHE A 1 430 ? 138.707 114.039 118.493 1.00 55.40  ? 413 PHE A N   1 
ATOM 3317 C CA  . PHE A 1 430 ? 138.139 115.344 118.196 1.00 55.40  ? 413 PHE A CA  1 
ATOM 3318 C C   . PHE A 1 430 ? 138.946 116.434 118.883 1.00 55.40  ? 413 PHE A C   1 
ATOM 3319 O O   . PHE A 1 430 ? 139.462 116.247 119.988 1.00 55.40  ? 413 PHE A O   1 
ATOM 3320 C CB  . PHE A 1 430 ? 136.672 115.429 118.638 1.00 55.40  ? 413 PHE A CB  1 
ATOM 3321 C CG  . PHE A 1 430 ? 135.793 114.383 118.019 1.00 55.40  ? 413 PHE A CG  1 
ATOM 3322 C CD1 . PHE A 1 430 ? 135.920 114.059 116.680 1.00 55.40  ? 413 PHE A CD1 1 
ATOM 3323 C CD2 . PHE A 1 430 ? 134.844 113.720 118.776 1.00 55.40  ? 413 PHE A CD2 1 
ATOM 3324 C CE1 . PHE A 1 430 ? 135.117 113.097 116.106 1.00 55.40  ? 413 PHE A CE1 1 
ATOM 3325 C CE2 . PHE A 1 430 ? 134.037 112.754 118.207 1.00 55.40  ? 413 PHE A CE2 1 
ATOM 3326 C CZ  . PHE A 1 430 ? 134.175 112.442 116.870 1.00 55.40  ? 413 PHE A CZ  1 
ATOM 3327 N N   . THR A 1 431 ? 139.047 117.578 118.212 1.00 49.85  ? 414 THR A N   1 
ATOM 3328 C CA  . THR A 1 431 ? 139.714 118.754 118.752 1.00 49.85  ? 414 THR A CA  1 
ATOM 3329 C C   . THR A 1 431 ? 138.826 119.965 118.515 1.00 49.85  ? 414 THR A C   1 
ATOM 3330 O O   . THR A 1 431 ? 138.381 120.199 117.387 1.00 49.85  ? 414 THR A O   1 
ATOM 3331 C CB  . THR A 1 431 ? 141.085 118.968 118.104 1.00 49.85  ? 414 THR A CB  1 
ATOM 3332 O OG1 . THR A 1 431 ? 141.826 117.741 118.134 1.00 49.85  ? 414 THR A OG1 1 
ATOM 3333 C CG2 . THR A 1 431 ? 141.863 120.042 118.849 1.00 49.85  ? 414 THR A CG2 1 
ATOM 3334 N N   . LYS A 1 432 ? 138.571 120.730 119.572 1.00 55.65  ? 415 LYS A N   1 
ATOM 3335 C CA  . LYS A 1 432 ? 137.702 121.898 119.479 1.00 55.65  ? 415 LYS A CA  1 
ATOM 3336 C C   . LYS A 1 432 ? 138.504 123.069 118.925 1.00 55.65  ? 415 LYS A C   1 
ATOM 3337 O O   . LYS A 1 432 ? 139.451 123.540 119.562 1.00 55.65  ? 415 LYS A O   1 
ATOM 3338 C CB  . LYS A 1 432 ? 137.107 122.233 120.844 1.00 55.65  ? 415 LYS A CB  1 
ATOM 3339 C CG  . LYS A 1 432 ? 135.978 123.250 120.792 1.00 55.65  ? 415 LYS A CG  1 
ATOM 3340 C CD  . LYS A 1 432 ? 135.508 123.626 122.187 1.00 55.65  ? 415 LYS A CD  1 
ATOM 3341 C CE  . LYS A 1 432 ? 134.036 124.003 122.190 1.00 55.65  ? 415 LYS A CE  1 
ATOM 3342 N NZ  . LYS A 1 432 ? 133.525 124.232 123.570 1.00 55.65  ? 415 LYS A NZ  1 
ATOM 3343 N N   . LEU A 1 433 ? 138.129 123.536 117.739 1.00 56.67  ? 416 LEU A N   1 
ATOM 3344 C CA  . LEU A 1 433 ? 138.791 124.669 117.116 1.00 56.67  ? 416 LEU A CA  1 
ATOM 3345 C C   . LEU A 1 433 ? 138.045 125.964 117.425 1.00 56.67  ? 416 LEU A C   1 
ATOM 3346 O O   . LEU A 1 433 ? 136.903 125.965 117.889 1.00 56.67  ? 416 LEU A O   1 
ATOM 3347 C CB  . LEU A 1 433 ? 138.895 124.470 115.604 1.00 56.67  ? 416 LEU A CB  1 
ATOM 3348 C CG  . LEU A 1 433 ? 139.239 123.070 115.098 1.00 56.67  ? 416 LEU A CG  1 
ATOM 3349 C CD1 . LEU A 1 433 ? 139.213 123.048 113.581 1.00 56.67  ? 416 LEU A CD1 1 
ATOM 3350 C CD2 . LEU A 1 433 ? 140.599 122.640 115.619 1.00 56.67  ? 416 LEU A CD2 1 
ATOM 3351 N N   . LYS A 1 434 ? 138.715 127.081 117.157 1.00 67.12  ? 417 LYS A N   1 
ATOM 3352 C CA  . LYS A 1 434 ? 138.114 128.393 117.344 1.00 67.12  ? 417 LYS A CA  1 
ATOM 3353 C C   . LYS A 1 434 ? 137.154 128.697 116.202 1.00 67.12  ? 417 LYS A C   1 
ATOM 3354 O O   . LYS A 1 434 ? 137.495 128.521 115.029 1.00 67.12  ? 417 LYS A O   1 
ATOM 3355 C CB  . LYS A 1 434 ? 139.196 129.469 117.418 1.00 67.12  ? 417 LYS A CB  1 
ATOM 3356 C CG  . LYS A 1 434 ? 138.743 130.764 118.069 1.00 67.12  ? 417 LYS A CG  1 
ATOM 3357 C CD  . LYS A 1 434 ? 139.834 131.820 117.999 1.00 67.12  ? 417 LYS A CD  1 
ATOM 3358 C CE  . LYS A 1 434 ? 139.256 133.189 117.680 1.00 67.12  ? 417 LYS A CE  1 
ATOM 3359 N NZ  . LYS A 1 434 ? 138.007 133.454 118.444 1.00 67.12  ? 417 LYS A NZ  1 
ATOM 3360 N N   . ASN A 1 435 ? 135.954 129.152 116.547 1.00 71.34  ? 418 ASN A N   1 
ATOM 3361 C CA  . ASN A 1 435 ? 134.995 129.628 115.562 1.00 71.34  ? 418 ASN A CA  1 
ATOM 3362 C C   . ASN A 1 435 ? 134.997 131.153 115.530 1.00 71.34  ? 418 ASN A C   1 
ATOM 3363 O O   . ASN A 1 435 ? 135.137 131.810 116.566 1.00 71.34  ? 418 ASN A O   1 
ATOM 3364 C CB  . ASN A 1 435 ? 133.594 129.055 115.827 1.00 71.34  ? 418 ASN A CB  1 
ATOM 3365 C CG  . ASN A 1 435 ? 133.028 129.418 117.200 1.00 71.34  ? 418 ASN A CG  1 
ATOM 3366 O OD1 . ASN A 1 435 ? 133.369 130.435 117.798 1.00 71.34  ? 418 ASN A OD1 1 
ATOM 3367 N ND2 . ASN A 1 435 ? 132.146 128.561 117.702 1.00 71.34  ? 418 ASN A ND2 1 
ATOM 3368 N N   . PHE A 1 436 ? 134.906 131.711 114.322 1.00 73.34  ? 419 PHE A N   1 
ATOM 3369 C CA  . PHE A 1 436 ? 135.083 133.151 114.168 1.00 73.34  ? 419 PHE A CA  1 
ATOM 3370 C C   . PHE A 1 436 ? 133.848 133.920 114.621 1.00 73.34  ? 419 PHE A C   1 
ATOM 3371 O O   . PHE A 1 436 ? 133.966 135.025 115.165 1.00 73.34  ? 419 PHE A O   1 
ATOM 3372 C CB  . PHE A 1 436 ? 135.429 133.485 112.718 1.00 73.34  ? 419 PHE A CB  1 
ATOM 3373 C CG  . PHE A 1 436 ? 136.882 133.794 112.505 1.00 73.34  ? 419 PHE A CG  1 
ATOM 3374 C CD1 . PHE A 1 436 ? 137.853 132.851 112.798 1.00 73.34  ? 419 PHE A CD1 1 
ATOM 3375 C CD2 . PHE A 1 436 ? 137.280 135.032 112.030 1.00 73.34  ? 419 PHE A CD2 1 
ATOM 3376 C CE1 . PHE A 1 436 ? 139.192 133.131 112.610 1.00 73.34  ? 419 PHE A CE1 1 
ATOM 3377 C CE2 . PHE A 1 436 ? 138.618 135.319 111.840 1.00 73.34  ? 419 PHE A CE2 1 
ATOM 3378 C CZ  . PHE A 1 436 ? 139.575 134.368 112.130 1.00 73.34  ? 419 PHE A CZ  1 
ATOM 3379 N N   . THR A 1 437 ? 132.660 133.361 114.404 1.00 69.98  ? 420 THR A N   1 
ATOM 3380 C CA  . THR A 1 437 ? 131.424 134.022 114.809 1.00 69.98  ? 420 THR A CA  1 
ATOM 3381 C C   . THR A 1 437 ? 131.373 134.106 116.328 1.00 69.98  ? 420 THR A C   1 
ATOM 3382 O O   . THR A 1 437 ? 131.303 133.080 117.013 1.00 69.98  ? 420 THR A O   1 
ATOM 3383 C CB  . THR A 1 437 ? 130.212 133.273 114.264 1.00 69.98  ? 420 THR A CB  1 
ATOM 3384 O OG1 . THR A 1 437 ? 130.228 131.920 114.736 1.00 69.98  ? 420 THR A OG1 1 
ATOM 3385 C CG2 . THR A 1 437 ? 130.228 133.280 112.747 1.00 69.98  ? 420 THR A CG2 1 
ATOM 3386 N N   . GLY A 1 438 ? 131.416 135.328 116.855 1.00 71.27  ? 421 GLY A N   1 
ATOM 3387 C CA  . GLY A 1 438 ? 131.378 135.505 118.293 1.00 71.27  ? 421 GLY A CA  1 
ATOM 3388 C C   . GLY A 1 438 ? 130.076 135.007 118.889 1.00 71.27  ? 421 GLY A C   1 
ATOM 3389 O O   . GLY A 1 438 ? 129.035 134.969 118.230 1.00 71.27  ? 421 GLY A O   1 
ATOM 3390 N N   . LEU A 1 439 ? 130.147 134.609 120.162 1.00 64.68  ? 422 LEU A N   1 
ATOM 3391 C CA  . LEU A 1 439 ? 128.967 134.089 120.843 1.00 64.68  ? 422 LEU A CA  1 
ATOM 3392 C C   . LEU A 1 439 ? 127.844 135.118 120.881 1.00 64.68  ? 422 LEU A C   1 
ATOM 3393 O O   . LEU A 1 439 ? 126.665 134.752 120.827 1.00 64.68  ? 422 LEU A O   1 
ATOM 3394 C CB  . LEU A 1 439 ? 129.339 133.636 122.256 1.00 64.68  ? 422 LEU A CB  1 
ATOM 3395 C CG  . LEU A 1 439 ? 128.275 132.906 123.076 1.00 64.68  ? 422 LEU A CG  1 
ATOM 3396 C CD1 . LEU A 1 439 ? 128.756 131.514 123.446 1.00 64.68  ? 422 LEU A CD1 1 
ATOM 3397 C CD2 . LEU A 1 439 ? 127.936 133.693 124.328 1.00 64.68  ? 422 LEU A CD2 1 
ATOM 3398 N N   . PHE A 1 440 ? 128.188 136.404 120.960 1.00 59.52  ? 423 PHE A N   1 
ATOM 3399 C CA  . PHE A 1 440 ? 127.216 137.491 120.935 1.00 59.52  ? 423 PHE A CA  1 
ATOM 3400 C C   . PHE A 1 440 ? 127.444 138.411 119.739 1.00 59.52  ? 423 PHE A C   1 
ATOM 3401 O O   . PHE A 1 440 ? 127.163 139.609 119.805 1.00 59.52  ? 423 PHE A O   1 
ATOM 3402 C CB  . PHE A 1 440 ? 127.264 138.285 122.240 1.00 59.52  ? 423 PHE A CB  1 
ATOM 3403 C CG  . PHE A 1 440 ? 126.361 137.747 123.314 1.00 59.52  ? 423 PHE A CG  1 
ATOM 3404 C CD1 . PHE A 1 440 ? 125.980 136.418 123.318 1.00 59.52  ? 423 PHE A CD1 1 
ATOM 3405 C CD2 . PHE A 1 440 ? 125.907 138.568 124.331 1.00 59.52  ? 423 PHE A CD2 1 
ATOM 3406 C CE1 . PHE A 1 440 ? 125.154 135.920 124.304 1.00 59.52  ? 423 PHE A CE1 1 
ATOM 3407 C CE2 . PHE A 1 440 ? 125.083 138.076 125.322 1.00 59.52  ? 423 PHE A CE2 1 
ATOM 3408 C CZ  . PHE A 1 440 ? 124.706 136.750 125.308 1.00 59.52  ? 423 PHE A CZ  1 
ATOM 3409 N N   . GLU A 1 441 ? 127.955 137.859 118.635 1.00 67.23  ? 424 GLU A N   1 
ATOM 3410 C CA  . GLU A 1 441 ? 128.228 138.674 117.455 1.00 67.23  ? 424 GLU A CA  1 
ATOM 3411 C C   . GLU A 1 441 ? 126.937 139.156 116.802 1.00 67.23  ? 424 GLU A C   1 
ATOM 3412 O O   . GLU A 1 441 ? 126.826 140.329 116.426 1.00 67.23  ? 424 GLU A O   1 
ATOM 3413 C CB  . GLU A 1 441 ? 129.075 137.883 116.459 1.00 67.23  ? 424 GLU A CB  1 
ATOM 3414 C CG  . GLU A 1 441 ? 129.164 138.508 115.077 1.00 67.23  ? 424 GLU A CG  1 
ATOM 3415 C CD  . GLU A 1 441 ? 129.956 139.800 115.070 1.00 67.23  ? 424 GLU A CD  1 
ATOM 3416 O OE1 . GLU A 1 441 ? 130.974 139.879 115.789 1.00 67.23  ? 424 GLU A OE1 1 
ATOM 3417 O OE2 . GLU A 1 441 ? 129.561 140.736 114.344 1.00 67.23  ? 424 GLU A OE2 1 
ATOM 3418 N N   . PHE A 1 442 ? 125.954 138.272 116.663 1.00 69.06  ? 425 PHE A N   1 
ATOM 3419 C CA  . PHE A 1 442 ? 124.632 138.621 116.159 1.00 69.06  ? 425 PHE A CA  1 
ATOM 3420 C C   . PHE A 1 442 ? 123.636 138.495 117.301 1.00 69.06  ? 425 PHE A C   1 
ATOM 3421 O O   . PHE A 1 442 ? 123.540 137.436 117.930 1.00 69.06  ? 425 PHE A O   1 
ATOM 3422 C CB  . PHE A 1 442 ? 124.230 137.719 114.993 1.00 69.06  ? 425 PHE A CB  1 
ATOM 3423 C CG  . PHE A 1 442 ? 125.357 137.417 114.054 1.00 69.06  ? 425 PHE A CG  1 
ATOM 3424 C CD1 . PHE A 1 442 ? 125.913 138.418 113.277 1.00 69.06  ? 425 PHE A CD1 1 
ATOM 3425 C CD2 . PHE A 1 442 ? 125.867 136.135 113.955 1.00 69.06  ? 425 PHE A CD2 1 
ATOM 3426 C CE1 . PHE A 1 442 ? 126.953 138.146 112.413 1.00 69.06  ? 425 PHE A CE1 1 
ATOM 3427 C CE2 . PHE A 1 442 ? 126.908 135.856 113.093 1.00 69.06  ? 425 PHE A CE2 1 
ATOM 3428 C CZ  . PHE A 1 442 ? 127.452 136.863 112.321 1.00 69.06  ? 425 PHE A CZ  1 
ATOM 3429 N N   . TYR A 1 443 ? 122.898 139.568 117.566 1.00 54.63  ? 426 TYR A N   1 
ATOM 3430 C CA  . TYR A 1 443 ? 122.168 139.671 118.818 1.00 54.63  ? 426 TYR A CA  1 
ATOM 3431 C C   . TYR A 1 443 ? 120.943 140.557 118.639 1.00 54.63  ? 426 TYR A C   1 
ATOM 3432 O O   . TYR A 1 443 ? 120.741 141.183 117.595 1.00 54.63  ? 426 TYR A O   1 
ATOM 3433 C CB  . TYR A 1 443 ? 123.056 140.238 119.930 1.00 54.63  ? 426 TYR A CB  1 
ATOM 3434 C CG  . TYR A 1 443 ? 123.722 141.554 119.580 1.00 54.63  ? 426 TYR A CG  1 
ATOM 3435 C CD1 . TYR A 1 443 ? 124.762 141.618 118.661 1.00 54.63  ? 426 TYR A CD1 1 
ATOM 3436 C CD2 . TYR A 1 443 ? 123.332 142.730 120.205 1.00 54.63  ? 426 TYR A CD2 1 
ATOM 3437 C CE1 . TYR A 1 443 ? 125.372 142.820 118.352 1.00 54.63  ? 426 TYR A CE1 1 
ATOM 3438 C CE2 . TYR A 1 443 ? 123.934 143.936 119.903 1.00 54.63  ? 426 TYR A CE2 1 
ATOM 3439 C CZ  . TYR A 1 443 ? 124.954 143.975 118.979 1.00 54.63  ? 426 TYR A CZ  1 
ATOM 3440 O OH  . TYR A 1 443 ? 125.558 145.175 118.680 1.00 54.63  ? 426 TYR A OH  1 
ATOM 3441 N N   . LYS A 1 444 ? 120.125 140.593 119.687 1.00 50.79  ? 427 LYS A N   1 
ATOM 3442 C CA  . LYS A 1 444 ? 119.042 141.551 119.844 1.00 50.79  ? 427 LYS A CA  1 
ATOM 3443 C C   . LYS A 1 444 ? 119.110 142.131 121.250 1.00 50.79  ? 427 LYS A C   1 
ATOM 3444 O O   . LYS A 1 444 ? 119.523 141.455 122.194 1.00 50.79  ? 427 LYS A O   1 
ATOM 3445 C CB  . LYS A 1 444 ? 117.671 140.909 119.606 1.00 50.79  ? 427 LYS A CB  1 
ATOM 3446 C CG  . LYS A 1 444 ? 117.426 140.453 118.179 1.00 50.79  ? 427 LYS A CG  1 
ATOM 3447 C CD  . LYS A 1 444 ? 116.009 139.928 118.021 1.00 50.79  ? 427 LYS A CD  1 
ATOM 3448 C CE  . LYS A 1 444 ? 115.529 140.031 116.585 1.00 50.79  ? 427 LYS A CE  1 
ATOM 3449 N NZ  . LYS A 1 444 ? 114.129 139.546 116.435 1.00 50.79  ? 427 LYS A NZ  1 
ATOM 3450 N N   . LEU A 1 445 ? 118.704 143.389 121.386 1.00 49.85  ? 428 LEU A N   1 
ATOM 3451 C CA  . LEU A 1 445 ? 118.782 144.113 122.655 1.00 49.85  ? 428 LEU A CA  1 
ATOM 3452 C C   . LEU A 1 445 ? 117.384 144.222 123.250 1.00 49.85  ? 428 LEU A C   1 
ATOM 3453 O O   . LEU A 1 445 ? 116.604 145.095 122.864 1.00 49.85  ? 428 LEU A O   1 
ATOM 3454 C CB  . LEU A 1 445 ? 119.403 145.493 122.458 1.00 49.85  ? 428 LEU A CB  1 
ATOM 3455 C CG  . LEU A 1 445 ? 120.854 145.560 121.989 1.00 49.85  ? 428 LEU A CG  1 
ATOM 3456 C CD1 . LEU A 1 445 ? 121.430 146.936 122.265 1.00 49.85  ? 428 LEU A CD1 1 
ATOM 3457 C CD2 . LEU A 1 445 ? 121.673 144.497 122.697 1.00 49.85  ? 428 LEU A CD2 1 
ATOM 3458 N N   . LEU A 1 446 ? 117.083 143.363 124.216 1.00 49.85  ? 429 LEU A N   1 
ATOM 3459 C CA  . LEU A 1 446 ? 115.777 143.362 124.860 1.00 49.85  ? 429 LEU A CA  1 
ATOM 3460 C C   . LEU A 1 446 ? 115.877 143.979 126.247 1.00 49.85  ? 429 LEU A C   1 
ATOM 3461 O O   . LEU A 1 446 ? 116.797 143.666 127.009 1.00 49.85  ? 429 LEU A O   1 
ATOM 3462 C CB  . LEU A 1 446 ? 115.216 141.943 124.968 1.00 49.85  ? 429 LEU A CB  1 
ATOM 3463 C CG  . LEU A 1 446 ? 115.566 140.944 123.865 1.00 49.85  ? 429 LEU A CG  1 
ATOM 3464 C CD1 . LEU A 1 446 ? 114.978 139.583 124.189 1.00 49.85  ? 429 LEU A CD1 1 
ATOM 3465 C CD2 . LEU A 1 446 ? 115.071 141.431 122.514 1.00 49.85  ? 429 LEU A CD2 1 
ATOM 3466 N N   . CYS A 1 447 ? 114.926 144.852 126.576 1.00 61.41  ? 430 CYS A N   1 
ATOM 3467 C CA  . CYS A 1 447 ? 114.872 145.399 127.925 1.00 61.41  ? 430 CYS A CA  1 
ATOM 3468 C C   . CYS A 1 447 ? 113.482 145.928 128.231 1.00 61.41  ? 430 CYS A C   1 
ATOM 3469 O O   . CYS A 1 447 ? 112.651 146.120 127.339 1.00 61.41  ? 430 CYS A O   1 
ATOM 3470 C CB  . CYS A 1 447 ? 115.932 146.481 128.144 1.00 61.41  ? 430 CYS A CB  1 
ATOM 3471 S SG  . CYS A 1 447 ? 116.134 147.728 126.845 1.00 61.41  ? 430 CYS A SG  1 
ATOM 3472 N N   . VAL A 1 448 ? 113.247 146.147 129.520 1.00 59.22  ? 431 VAL A N   1 
ATOM 3473 C CA  . VAL A 1 448 ? 111.957 146.579 130.024 1.00 59.22  ? 431 VAL A CA  1 
ATOM 3474 C C   . VAL A 1 448 ? 112.008 148.051 130.415 1.00 59.22  ? 431 VAL A C   1 
ATOM 3475 O O   . VAL A 1 448 ? 113.085 148.624 130.582 1.00 59.22  ? 431 VAL A O   1 
ATOM 3476 C CB  . VAL A 1 448 ? 111.520 145.709 131.214 1.00 59.22  ? 431 VAL A CB  1 
ATOM 3477 C CG1 . VAL A 1 448 ? 111.802 144.242 130.927 1.00 59.22  ? 431 VAL A CG1 1 
ATOM 3478 C CG2 . VAL A 1 448 ? 112.238 146.149 132.480 1.00 59.22  ? 431 VAL A CG2 1 
ATOM 3479 N N   . LEU A 1 470 ? 118.453 148.023 131.925 1.00 50.59  ? 453 LEU A N   1 
ATOM 3480 C CA  . LEU A 1 470 ? 119.171 146.756 131.857 1.00 50.59  ? 453 LEU A CA  1 
ATOM 3481 C C   . LEU A 1 470 ? 118.919 146.050 130.522 1.00 50.59  ? 453 LEU A C   1 
ATOM 3482 O O   . LEU A 1 470 ? 118.355 144.962 130.470 1.00 50.59  ? 453 LEU A O   1 
ATOM 3483 C CB  . LEU A 1 470 ? 118.790 145.872 133.058 1.00 50.59  ? 453 LEU A CB  1 
ATOM 3484 C CG  . LEU A 1 470 ? 117.332 145.527 133.399 1.00 50.59  ? 453 LEU A CG  1 
ATOM 3485 C CD1 . LEU A 1 470 ? 116.935 144.116 132.973 1.00 50.59  ? 453 LEU A CD1 1 
ATOM 3486 C CD2 . LEU A 1 470 ? 117.072 145.729 134.886 1.00 50.59  ? 453 LEU A CD2 1 
ATOM 3487 N N   . CYS A 1 471 ? 119.363 146.678 129.436 1.00 58.06  ? 454 CYS A N   1 
ATOM 3488 C CA  . CYS A 1 471 ? 119.145 146.147 128.094 1.00 58.06  ? 454 CYS A CA  1 
ATOM 3489 C C   . CYS A 1 471 ? 120.145 145.026 127.843 1.00 58.06  ? 454 CYS A C   1 
ATOM 3490 O O   . CYS A 1 471 ? 121.352 145.267 127.741 1.00 58.06  ? 454 CYS A O   1 
ATOM 3491 C CB  . CYS A 1 471 ? 119.254 147.252 127.044 1.00 58.06  ? 454 CYS A CB  1 
ATOM 3492 S SG  . CYS A 1 471 ? 117.944 148.529 127.125 1.00 58.06  ? 454 CYS A SG  1 
ATOM 3493 N N   . ILE A 1 472 ? 119.638 143.804 127.739 1.00 49.34  ? 455 ILE A N   1 
ATOM 3494 C CA  . ILE A 1 472 ? 120.471 142.632 127.632 1.00 49.34  ? 455 ILE A CA  1 
ATOM 3495 C C   . ILE A 1 472 ? 120.568 142.206 126.173 1.00 49.34  ? 455 ILE A C   1 
ATOM 3496 O O   . ILE A 1 472 ? 119.714 142.524 125.345 1.00 49.34  ? 455 ILE A O   1 
ATOM 3497 C CB  . ILE A 1 472 ? 119.951 141.474 128.513 1.00 49.34  ? 455 ILE A CB  1 
ATOM 3498 C CG1 . ILE A 1 472 ? 118.903 140.660 127.757 1.00 49.34  ? 455 ILE A CG1 1 
ATOM 3499 C CG2 . ILE A 1 472 ? 119.370 142.012 129.803 1.00 49.34  ? 455 ILE A CG2 1 
ATOM 3500 C CD1 . ILE A 1 472 ? 118.683 139.283 128.327 1.00 49.34  ? 455 ILE A CD1 1 
ATOM 3501 N N   . LYS A 1 473 ? 121.622 141.459 125.860 1.00 52.11  ? 456 LYS A N   1 
ATOM 3502 C CA  . LYS A 1 473 ? 121.929 140.991 124.517 1.00 52.11  ? 456 LYS A CA  1 
ATOM 3503 C C   . LYS A 1 473 ? 121.564 139.516 124.434 1.00 52.11  ? 456 LYS A C   1 
ATOM 3504 O O   . LYS A 1 473 ? 122.074 138.704 125.212 1.00 52.11  ? 456 LYS A O   1 
ATOM 3505 C CB  . LYS A 1 473 ? 123.412 141.202 124.211 1.00 52.11  ? 456 LYS A CB  1 
ATOM 3506 C CG  . LYS A 1 473 ? 123.959 142.511 124.772 1.00 52.11  ? 456 LYS A CG  1 
ATOM 3507 C CD  . LYS A 1 473 ? 125.478 142.624 124.666 1.00 52.11  ? 456 LYS A CD  1 
ATOM 3508 C CE  . LYS A 1 473 ? 126.045 141.922 123.445 1.00 52.11  ? 456 LYS A CE  1 
ATOM 3509 N NZ  . LYS A 1 473 ? 125.607 142.558 122.180 1.00 52.11  ? 456 LYS A NZ  1 
ATOM 3510 N N   . VAL A 1 474 ? 120.692 139.181 123.517 1.00 49.85  ? 457 VAL A N   1 
ATOM 3511 C CA  . VAL A 1 474 ? 120.234 137.809 123.340 1.00 49.85  ? 457 VAL A CA  1 
ATOM 3512 C C   . VAL A 1 474 ? 120.690 137.332 121.971 1.00 49.85  ? 457 VAL A C   1 
ATOM 3513 O O   . VAL A 1 474 ? 120.463 138.014 120.967 1.00 49.85  ? 457 VAL A O   1 
ATOM 3514 C CB  . VAL A 1 474 ? 118.705 137.698 123.478 1.00 49.85  ? 457 VAL A CB  1 
ATOM 3515 C CG1 . VAL A 1 474 ? 118.243 136.292 123.134 1.00 49.85  ? 457 VAL A CG1 1 
ATOM 3516 C CG2 . VAL A 1 474 ? 118.276 138.078 124.885 1.00 49.85  ? 457 VAL A CG2 1 
ATOM 3517 N N   . ASN A 1 475 ? 121.328 136.164 121.936 1.00 49.85  ? 458 ASN A N   1 
ATOM 3518 C CA  . ASN A 1 475 ? 121.911 135.657 120.701 1.00 49.85  ? 458 ASN A CA  1 
ATOM 3519 C C   . ASN A 1 475 ? 120.831 135.406 119.654 1.00 49.85  ? 458 ASN A C   1 
ATOM 3520 O O   . ASN A 1 475 ? 119.706 135.010 119.968 1.00 49.85  ? 458 ASN A O   1 
ATOM 3521 C CB  . ASN A 1 475 ? 122.692 134.369 120.973 1.00 49.85  ? 458 ASN A CB  1 
ATOM 3522 C CG  . ASN A 1 475 ? 123.416 133.855 119.744 1.00 49.85  ? 458 ASN A CG  1 
ATOM 3523 O OD1 . ASN A 1 475 ? 122.825 133.190 118.894 1.00 49.85  ? 458 ASN A OD1 1 
ATOM 3524 N ND2 . ASN A 1 475 ? 124.705 134.163 119.644 1.00 49.85  ? 458 ASN A ND2 1 
ATOM 3525 N N   . ASN A 1 476 ? 121.189 135.649 118.390 1.00 49.85  ? 459 ASN A N   1 
ATOM 3526 C CA  . ASN A 1 476 ? 120.228 135.504 117.300 1.00 49.85  ? 459 ASN A CA  1 
ATOM 3527 C C   . ASN A 1 476 ? 119.799 134.057 117.104 1.00 49.85  ? 459 ASN A C   1 
ATOM 3528 O O   . ASN A 1 476 ? 118.663 133.802 116.688 1.00 49.85  ? 459 ASN A O   1 
ATOM 3529 C CB  . ASN A 1 476 ? 120.819 136.062 116.006 1.00 49.85  ? 459 ASN A CB  1 
ATOM 3530 C CG  . ASN A 1 476 ? 119.933 135.808 114.805 1.00 49.85  ? 459 ASN A CG  1 
ATOM 3531 O OD1 . ASN A 1 476 ? 118.727 136.044 114.849 1.00 49.85  ? 459 ASN A OD1 1 
ATOM 3532 N ND2 . ASN A 1 476 ? 120.528 135.325 113.721 1.00 49.85  ? 459 ASN A ND2 1 
ATOM 3533 N N   . TRP A 1 477 ? 120.675 133.102 117.398 1.00 52.83  ? 460 TRP A N   1 
ATOM 3534 C CA  . TRP A 1 477 ? 120.366 131.691 117.214 1.00 52.83  ? 460 TRP A CA  1 
ATOM 3535 C C   . TRP A 1 477 ? 119.664 131.077 118.418 1.00 52.83  ? 460 TRP A C   1 
ATOM 3536 O O   . TRP A 1 477 ? 119.353 129.882 118.393 1.00 52.83  ? 460 TRP A O   1 
ATOM 3537 C CB  . TRP A 1 477 ? 121.645 130.906 116.904 1.00 52.83  ? 460 TRP A CB  1 
ATOM 3538 C CG  . TRP A 1 477 ? 122.506 131.550 115.858 1.00 52.83  ? 460 TRP A CG  1 
ATOM 3539 C CD1 . TRP A 1 477 ? 123.654 132.258 116.063 1.00 52.83  ? 460 TRP A CD1 1 
ATOM 3540 C CD2 . TRP A 1 477 ? 122.284 131.549 114.443 1.00 52.83  ? 460 TRP A CD2 1 
ATOM 3541 N NE1 . TRP A 1 477 ? 124.162 132.695 114.864 1.00 52.83  ? 460 TRP A NE1 1 
ATOM 3542 C CE2 . TRP A 1 477 ? 123.339 132.273 113.854 1.00 52.83  ? 460 TRP A CE2 1 
ATOM 3543 C CE3 . TRP A 1 477 ? 121.296 131.005 113.616 1.00 52.83  ? 460 TRP A CE3 1 
ATOM 3544 C CZ2 . TRP A 1 477 ? 123.434 132.467 112.478 1.00 52.83  ? 460 TRP A CZ2 1 
ATOM 3545 C CZ3 . TRP A 1 477 ? 121.392 131.198 112.251 1.00 52.83  ? 460 TRP A CZ3 1 
ATOM 3546 C CH2 . TRP A 1 477 ? 122.453 131.923 111.695 1.00 52.83  ? 460 TRP A CH2 1 
ATOM 3547 N N   . ASP A 1 478 ? 119.408 131.860 119.465 1.00 49.85  ? 461 ASP A N   1 
ATOM 3548 C CA  . ASP A 1 478 ? 118.711 131.388 120.653 1.00 49.85  ? 461 ASP A CA  1 
ATOM 3549 C C   . ASP A 1 478 ? 117.261 131.854 120.707 1.00 49.85  ? 461 ASP A C   1 
ATOM 3550 O O   . ASP A 1 478 ? 116.634 131.771 121.768 1.00 49.85  ? 461 ASP A O   1 
ATOM 3551 C CB  . ASP A 1 478 ? 119.450 131.843 121.913 1.00 49.85  ? 461 ASP A CB  1 
ATOM 3552 C CG  . ASP A 1 478 ? 120.450 130.816 122.405 1.00 49.85  ? 461 ASP A CG  1 
ATOM 3553 O OD1 . ASP A 1 478 ? 120.245 129.613 122.144 1.00 49.85  ? 461 ASP A OD1 1 
ATOM 3554 O OD2 . ASP A 1 478 ? 121.441 131.213 123.053 1.00 49.85  ? 461 ASP A OD2 1 
ATOM 3555 N N   . LEU A 1 479 ? 116.717 132.341 119.598 1.00 49.85  ? 462 LEU A N   1 
ATOM 3556 C CA  . LEU A 1 479 ? 115.373 132.895 119.561 1.00 49.85  ? 462 LEU A CA  1 
ATOM 3557 C C   . LEU A 1 479 ? 114.402 131.928 118.888 1.00 49.85  ? 462 LEU A C   1 
ATOM 3558 O O   . LEU A 1 479 ? 114.793 130.941 118.261 1.00 49.85  ? 462 LEU A O   1 
ATOM 3559 C CB  . LEU A 1 479 ? 115.375 134.246 118.841 1.00 49.85  ? 462 LEU A CB  1 
ATOM 3560 C CG  . LEU A 1 479 ? 116.220 135.328 119.515 1.00 49.85  ? 462 LEU A CG  1 
ATOM 3561 C CD1 . LEU A 1 479 ? 116.636 136.386 118.510 1.00 49.85  ? 462 LEU A CD1 1 
ATOM 3562 C CD2 . LEU A 1 479 ? 115.463 135.954 120.673 1.00 49.85  ? 462 LEU A CD2 1 
ATOM 3563 N N   . PHE A 1 480 ? 113.114 132.231 119.030 1.00 49.85  ? 463 PHE A N   1 
ATOM 3564 C CA  . PHE A 1 480 ? 112.064 131.355 118.535 1.00 49.85  ? 463 PHE A CA  1 
ATOM 3565 C C   . PHE A 1 480 ? 111.992 131.382 117.012 1.00 49.85  ? 463 PHE A C   1 
ATOM 3566 O O   . PHE A 1 480 ? 112.466 132.310 116.351 1.00 49.85  ? 463 PHE A O   1 
ATOM 3567 C CB  . PHE A 1 480 ? 110.710 131.753 119.122 1.00 49.85  ? 463 PHE A CB  1 
ATOM 3568 C CG  . PHE A 1 480 ? 110.475 131.233 120.508 1.00 49.85  ? 463 PHE A CG  1 
ATOM 3569 C CD1 . PHE A 1 480 ? 110.923 131.937 121.611 1.00 49.85  ? 463 PHE A CD1 1 
ATOM 3570 C CD2 . PHE A 1 480 ? 109.807 130.038 120.707 1.00 49.85  ? 463 PHE A CD2 1 
ATOM 3571 C CE1 . PHE A 1 480 ? 110.709 131.459 122.887 1.00 49.85  ? 463 PHE A CE1 1 
ATOM 3572 C CE2 . PHE A 1 480 ? 109.590 129.555 121.980 1.00 49.85  ? 463 PHE A CE2 1 
ATOM 3573 C CZ  . PHE A 1 480 ? 110.041 130.266 123.071 1.00 49.85  ? 463 PHE A CZ  1 
ATOM 3574 N N   . PHE A 1 481 ? 111.377 130.341 116.459 1.00 49.85  ? 464 PHE A N   1 
ATOM 3575 C CA  . PHE A 1 481 ? 111.160 130.204 115.023 1.00 49.85  ? 464 PHE A CA  1 
ATOM 3576 C C   . PHE A 1 481 ? 109.687 130.476 114.746 1.00 49.85  ? 464 PHE A C   1 
ATOM 3577 O O   . PHE A 1 481 ? 108.823 129.670 115.110 1.00 49.85  ? 464 PHE A O   1 
ATOM 3578 C CB  . PHE A 1 481 ? 111.567 128.812 114.546 1.00 49.85  ? 464 PHE A CB  1 
ATOM 3579 C CG  . PHE A 1 481 ? 111.268 128.552 113.099 1.00 49.85  ? 464 PHE A CG  1 
ATOM 3580 C CD1 . PHE A 1 481 ? 112.072 129.084 112.107 1.00 49.85  ? 464 PHE A CD1 1 
ATOM 3581 C CD2 . PHE A 1 481 ? 110.187 127.769 112.732 1.00 49.85  ? 464 PHE A CD2 1 
ATOM 3582 C CE1 . PHE A 1 481 ? 111.802 128.844 110.775 1.00 49.85  ? 464 PHE A CE1 1 
ATOM 3583 C CE2 . PHE A 1 481 ? 109.911 127.526 111.402 1.00 49.85  ? 464 PHE A CE2 1 
ATOM 3584 C CZ  . PHE A 1 481 ? 110.720 128.064 110.422 1.00 49.85  ? 464 PHE A CZ  1 
ATOM 3585 N N   . SER A 1 482 ? 109.402 131.605 114.104 1.00 49.85  ? 465 SER A N   1 
ATOM 3586 C CA  . SER A 1 482 ? 108.028 132.048 113.869 1.00 49.85  ? 465 SER A CA  1 
ATOM 3587 C C   . SER A 1 482 ? 107.745 132.112 112.377 1.00 49.85  ? 465 SER A C   1 
ATOM 3588 O O   . SER A 1 482 ? 108.077 133.116 111.722 1.00 49.85  ? 465 SER A O   1 
ATOM 3589 C CB  . SER A 1 482 ? 107.787 133.412 114.512 1.00 49.85  ? 465 SER A CB  1 
ATOM 3590 O OG  . SER A 1 482 ? 107.808 133.325 115.925 1.00 49.85  ? 465 SER A OG  1 
ATOM 3591 N N   . PRO A 1 483 ? 107.141 131.081 111.793 1.00 49.85  ? 466 PRO A N   1 
ATOM 3592 C CA  . PRO A 1 483 ? 106.770 131.155 110.377 1.00 49.85  ? 466 PRO A CA  1 
ATOM 3593 C C   . PRO A 1 483 ? 105.659 132.166 110.149 1.00 49.85  ? 466 PRO A C   1 
ATOM 3594 O O   . PRO A 1 483 ? 104.805 132.394 111.008 1.00 49.85  ? 466 PRO A O   1 
ATOM 3595 C CB  . PRO A 1 483 ? 106.303 129.732 110.055 1.00 49.85  ? 466 PRO A CB  1 
ATOM 3596 C CG  . PRO A 1 483 ? 105.864 129.178 111.364 1.00 49.85  ? 466 PRO A CG  1 
ATOM 3597 C CD  . PRO A 1 483 ? 106.744 129.804 112.408 1.00 49.85  ? 466 PRO A CD  1 
ATOM 3598 N N   . SER A 1 484 ? 105.682 132.777 108.969 1.00 49.85  ? 467 SER A N   1 
ATOM 3599 C CA  . SER A 1 484 ? 104.661 133.743 108.602 1.00 49.85  ? 467 SER A CA  1 
ATOM 3600 C C   . SER A 1 484 ? 103.378 133.031 108.183 1.00 49.85  ? 467 SER A C   1 
ATOM 3601 O O   . SER A 1 484 ? 103.358 131.825 107.925 1.00 49.85  ? 467 SER A O   1 
ATOM 3602 C CB  . SER A 1 484 ? 105.153 134.644 107.469 1.00 49.85  ? 467 SER A CB  1 
ATOM 3603 O OG  . SER A 1 484 ? 104.204 135.654 107.174 1.00 49.85  ? 467 SER A OG  1 
ATOM 3604 N N   . GLU A 1 485 ? 102.290 133.801 108.124 1.00 61.24  ? 468 GLU A N   1 
ATOM 3605 C CA  . GLU A 1 485 ? 101.019 133.248 107.673 1.00 61.24  ? 468 GLU A CA  1 
ATOM 3606 C C   . GLU A 1 485 ? 100.988 133.026 106.167 1.00 61.24  ? 468 GLU A C   1 
ATOM 3607 O O   . GLU A 1 485 ? 100.111 132.307 105.677 1.00 61.24  ? 468 GLU A O   1 
ATOM 3608 C CB  . GLU A 1 485 ? 99.869  134.167 108.089 1.00 61.24  ? 468 GLU A CB  1 
ATOM 3609 C CG  . GLU A 1 485 ? 99.903  134.580 109.553 1.00 61.24  ? 468 GLU A CG  1 
ATOM 3610 C CD  . GLU A 1 485 ? 99.275  135.940 109.791 1.00 61.24  ? 468 GLU A CD  1 
ATOM 3611 O OE1 . GLU A 1 485 ? 98.777  136.545 108.819 1.00 61.24  ? 468 GLU A OE1 1 
ATOM 3612 O OE2 . GLU A 1 485 ? 99.278  136.402 110.951 1.00 61.24  ? 468 GLU A OE2 1 
ATOM 3613 N N   . ASP A 1 486 ? 101.923 133.625 105.425 1.00 60.45  ? 469 ASP A N   1 
ATOM 3614 C CA  . ASP A 1 486 ? 101.932 133.493 103.973 1.00 60.45  ? 469 ASP A CA  1 
ATOM 3615 C C   . ASP A 1 486 ? 102.447 132.134 103.514 1.00 60.45  ? 469 ASP A C   1 
ATOM 3616 O O   . ASP A 1 486 ? 102.032 131.647 102.457 1.00 60.45  ? 469 ASP A O   1 
ATOM 3617 C CB  . ASP A 1 486 ? 102.778 134.605 103.350 1.00 60.45  ? 469 ASP A CB  1 
ATOM 3618 C CG  . ASP A 1 486 ? 102.588 135.939 104.044 1.00 60.45  ? 469 ASP A CG  1 
ATOM 3619 O OD1 . ASP A 1 486 ? 101.441 136.428 104.092 1.00 60.45  ? 469 ASP A OD1 1 
ATOM 3620 O OD2 . ASP A 1 486 ? 103.588 136.498 104.542 1.00 60.45  ? 469 ASP A OD2 1 
ATOM 3621 N N   . ASN A 1 487 ? 103.346 131.513 104.282 1.00 50.07  ? 470 ASN A N   1 
ATOM 3622 C CA  . ASN A 1 487 ? 103.936 130.246 103.862 1.00 50.07  ? 470 ASN A CA  1 
ATOM 3623 C C   . ASN A 1 487 ? 102.928 129.106 103.842 1.00 50.07  ? 470 ASN A C   1 
ATOM 3624 O O   . ASN A 1 487 ? 103.210 128.060 103.248 1.00 50.07  ? 470 ASN A O   1 
ATOM 3625 C CB  . ASN A 1 487 ? 105.106 129.876 104.773 1.00 50.07  ? 470 ASN A CB  1 
ATOM 3626 C CG  . ASN A 1 487 ? 105.867 131.087 105.264 1.00 50.07  ? 470 ASN A CG  1 
ATOM 3627 O OD1 . ASN A 1 487 ? 105.657 131.556 106.381 1.00 50.07  ? 470 ASN A OD1 1 
ATOM 3628 N ND2 . ASN A 1 487 ? 106.756 131.604 104.427 1.00 50.07  ? 470 ASN A ND2 1 
ATOM 3629 N N   . PHE A 1 488 ? 101.769 129.277 104.471 1.00 49.85  ? 471 PHE A N   1 
ATOM 3630 C CA  . PHE A 1 488 ? 100.745 128.241 104.535 1.00 49.85  ? 471 PHE A CA  1 
ATOM 3631 C C   . PHE A 1 488 ? 99.561  128.681 103.684 1.00 49.85  ? 471 PHE A C   1 
ATOM 3632 O O   . PHE A 1 488 ? 98.856  129.635 104.034 1.00 49.85  ? 471 PHE A O   1 
ATOM 3633 C CB  . PHE A 1 488 ? 100.326 127.981 105.980 1.00 49.85  ? 471 PHE A CB  1 
ATOM 3634 C CG  . PHE A 1 488 ? 101.481 127.715 106.900 1.00 49.85  ? 471 PHE A CG  1 
ATOM 3635 C CD1 . PHE A 1 488 ? 102.040 126.452 106.984 1.00 49.85  ? 471 PHE A CD1 1 
ATOM 3636 C CD2 . PHE A 1 488 ? 102.012 128.731 107.676 1.00 49.85  ? 471 PHE A CD2 1 
ATOM 3637 C CE1 . PHE A 1 488 ? 103.105 126.206 107.827 1.00 49.85  ? 471 PHE A CE1 1 
ATOM 3638 C CE2 . PHE A 1 488 ? 103.077 128.491 108.520 1.00 49.85  ? 471 PHE A CE2 1 
ATOM 3639 C CZ  . PHE A 1 488 ? 103.623 127.229 108.595 1.00 49.85  ? 471 PHE A CZ  1 
ATOM 3640 N N   . THR A 1 489 ? 99.345  127.985 102.572 1.00 64.10  ? 472 THR A N   1 
ATOM 3641 C CA  . THR A 1 489 ? 98.254  128.272 101.656 1.00 64.10  ? 472 THR A CA  1 
ATOM 3642 C C   . THR A 1 489 ? 97.412  127.020 101.462 1.00 64.10  ? 472 THR A C   1 
ATOM 3643 O O   . THR A 1 489 ? 97.915  125.895 101.538 1.00 64.10  ? 472 THR A O   1 
ATOM 3644 C CB  . THR A 1 489 ? 98.776  128.766 100.300 1.00 64.10  ? 472 THR A CB  1 
ATOM 3645 O OG1 . THR A 1 489 ? 99.628  127.769 99.721  1.00 64.10  ? 472 THR A OG1 1 
ATOM 3646 C CG2 . THR A 1 489 ? 99.559  130.060 100.469 1.00 64.10  ? 472 THR A CG2 1 
ATOM 3647 N N   . ASN A 1 490 ? 96.122  127.223 101.206 1.00 62.63  ? 473 ASN A N   1 
ATOM 3648 C CA  . ASN A 1 490 ? 95.175  126.123 101.124 1.00 62.63  ? 473 ASN A CA  1 
ATOM 3649 C C   . ASN A 1 490 ? 94.176  126.382 100.007 1.00 62.63  ? 473 ASN A C   1 
ATOM 3650 O O   . ASN A 1 490 ? 93.943  127.522 99.600  1.00 62.63  ? 473 ASN A O   1 
ATOM 3651 C CB  . ASN A 1 490 ? 94.430  125.924 102.450 1.00 62.63  ? 473 ASN A CB  1 
ATOM 3652 C CG  . ASN A 1 490 ? 93.442  127.039 102.734 1.00 62.63  ? 473 ASN A CG  1 
ATOM 3653 O OD1 . ASN A 1 490 ? 92.230  126.829 102.721 1.00 62.63  ? 473 ASN A OD1 1 
ATOM 3654 N ND2 . ASN A 1 490 ? 93.958  128.234 102.994 1.00 62.63  ? 473 ASN A ND2 1 
ATOM 3655 N N   . ASP A 1 491 ? 93.586  125.292 99.513  1.00 67.40  ? 474 ASP A N   1 
ATOM 3656 C CA  . ASP A 1 491 ? 92.512  125.344 98.530  1.00 67.40  ? 474 ASP A CA  1 
ATOM 3657 C C   . ASP A 1 491 ? 91.186  124.853 99.105  1.00 67.40  ? 474 ASP A C   1 
ATOM 3658 O O   . ASP A 1 491 ? 90.312  124.413 98.352  1.00 67.40  ? 474 ASP A O   1 
ATOM 3659 C CB  . ASP A 1 491 ? 92.892  124.540 97.285  1.00 67.40  ? 474 ASP A CB  1 
ATOM 3660 C CG  . ASP A 1 491 ? 93.161  123.073 97.587  1.00 67.40  ? 474 ASP A CG  1 
ATOM 3661 O OD1 . ASP A 1 491 ? 93.020  122.654 98.756  1.00 67.40  ? 474 ASP A OD1 1 
ATOM 3662 O OD2 . ASP A 1 491 ? 93.516  122.333 96.646  1.00 67.40  ? 474 ASP A OD2 1 
ATOM 3663 N N   . LEU A 1 492 ? 91.031  124.912 100.429 1.00 66.26  ? 475 LEU A N   1 
ATOM 3664 C CA  . LEU A 1 492 ? 89.823  124.399 101.068 1.00 66.26  ? 475 LEU A CA  1 
ATOM 3665 C C   . LEU A 1 492 ? 88.587  125.162 100.606 1.00 66.26  ? 475 LEU A C   1 
ATOM 3666 O O   . LEU A 1 492 ? 87.570  124.559 100.244 1.00 66.26  ? 475 LEU A O   1 
ATOM 3667 C CB  . LEU A 1 492 ? 89.969  124.477 102.589 1.00 66.26  ? 475 LEU A CB  1 
ATOM 3668 C CG  . LEU A 1 492 ? 91.208  123.805 103.186 1.00 66.26  ? 475 LEU A CG  1 
ATOM 3669 C CD1 . LEU A 1 492 ? 91.414  124.241 104.628 1.00 66.26  ? 475 LEU A CD1 1 
ATOM 3670 C CD2 . LEU A 1 492 ? 91.112  122.294 103.090 1.00 66.26  ? 475 LEU A CD2 1 
ATOM 3671 N N   . ASN A 1 493 ? 88.660  126.496 100.606 1.00 68.35  ? 476 ASN A N   1 
ATOM 3672 C CA  . ASN A 1 493 ? 87.513  127.305 100.211 1.00 68.35  ? 476 ASN A CA  1 
ATOM 3673 C C   . ASN A 1 493 ? 87.159  127.137 98.740  1.00 68.35  ? 476 ASN A C   1 
ATOM 3674 O O   . ASN A 1 493 ? 86.040  127.480 98.343  1.00 68.35  ? 476 ASN A O   1 
ATOM 3675 C CB  . ASN A 1 493 ? 87.779  128.780 100.521 1.00 68.35  ? 476 ASN A CB  1 
ATOM 3676 C CG  . ASN A 1 493 ? 89.186  129.209 100.154 1.00 68.35  ? 476 ASN A CG  1 
ATOM 3677 O OD1 . ASN A 1 493 ? 89.784  128.683 99.216  1.00 68.35  ? 476 ASN A OD1 1 
ATOM 3678 N ND2 . ASN A 1 493 ? 89.724  130.170 100.897 1.00 68.35  ? 476 ASN A ND2 1 
ATOM 3679 N N   . LYS A 1 494 ? 88.079  126.626 97.927  1.00 69.71  ? 477 LYS A N   1 
ATOM 3680 C CA  . LYS A 1 494 ? 87.789  126.392 96.520  1.00 69.71  ? 477 LYS A CA  1 
ATOM 3681 C C   . LYS A 1 494 ? 86.791  125.251 96.366  1.00 69.71  ? 477 LYS A C   1 
ATOM 3682 O O   . LYS A 1 494 ? 86.834  124.263 97.103  1.00 69.71  ? 477 LYS A O   1 
ATOM 3683 C CB  . LYS A 1 494 ? 89.077  126.075 95.760  1.00 69.71  ? 477 LYS A CB  1 
ATOM 3684 C CG  . LYS A 1 494 ? 88.884  125.818 94.273  1.00 69.71  ? 477 LYS A CG  1 
ATOM 3685 C CD  . LYS A 1 494 ? 90.214  125.606 93.568  1.00 69.71  ? 477 LYS A CD  1 
ATOM 3686 C CE  . LYS A 1 494 ? 91.227  126.669 93.959  1.00 69.71  ? 477 LYS A CE  1 
ATOM 3687 N NZ  . LYS A 1 494 ? 92.621  126.151 93.907  1.00 69.71  ? 477 LYS A NZ  1 
ATOM 3688 N N   . GLY A 1 495 ? 85.886  125.394 95.402  1.00 79.04  ? 478 GLY A N   1 
ATOM 3689 C CA  . GLY A 1 495 ? 84.906  124.362 95.143  1.00 79.04  ? 478 GLY A CA  1 
ATOM 3690 C C   . GLY A 1 495 ? 85.529  123.118 94.538  1.00 79.04  ? 478 GLY A C   1 
ATOM 3691 O O   . GLY A 1 495 ? 86.703  123.078 94.167  1.00 79.04  ? 478 GLY A O   1 
ATOM 3692 N N   . GLU A 1 496 ? 84.710  122.073 94.436  1.00 79.99  ? 479 GLU A N   1 
ATOM 3693 C CA  . GLU A 1 496 ? 85.183  120.788 93.939  1.00 79.99  ? 479 GLU A CA  1 
ATOM 3694 C C   . GLU A 1 496 ? 83.981  120.005 93.431  1.00 79.99  ? 479 GLU A C   1 
ATOM 3695 O O   . GLU A 1 496 ? 82.950  119.944 94.107  1.00 79.99  ? 479 GLU A O   1 
ATOM 3696 C CB  . GLU A 1 496 ? 85.941  120.037 95.045  1.00 79.99  ? 479 GLU A CB  1 
ATOM 3697 C CG  . GLU A 1 496 ? 86.657  118.760 94.625  1.00 79.99  ? 479 GLU A CG  1 
ATOM 3698 C CD  . GLU A 1 496 ? 85.724  117.587 94.453  1.00 79.99  ? 479 GLU A CD  1 
ATOM 3699 O OE1 . GLU A 1 496 ? 84.905  117.356 95.366  1.00 79.99  ? 479 GLU A OE1 1 
ATOM 3700 O OE2 . GLU A 1 496 ? 85.818  116.893 93.421  1.00 79.99  ? 479 GLU A OE2 1 
ATOM 3701 N N   . GLU A 1 497 ? 84.117  119.413 92.247  1.00 88.88  ? 480 GLU A N   1 
ATOM 3702 C CA  . GLU A 1 497 ? 83.003  118.838 91.506  1.00 88.88  ? 480 GLU A CA  1 
ATOM 3703 C C   . GLU A 1 497 ? 83.150  117.324 91.408  1.00 88.88  ? 480 GLU A C   1 
ATOM 3704 O O   . GLU A 1 497 ? 84.248  116.813 91.166  1.00 88.88  ? 480 GLU A O   1 
ATOM 3705 C CB  . GLU A 1 497 ? 82.924  119.450 90.105  1.00 88.88  ? 480 GLU A CB  1 
ATOM 3706 C CG  . GLU A 1 497 ? 81.745  118.996 89.267  1.00 88.88  ? 480 GLU A CG  1 
ATOM 3707 C CD  . GLU A 1 497 ? 81.754  119.620 87.885  1.00 88.88  ? 480 GLU A CD  1 
ATOM 3708 O OE1 . GLU A 1 497 ? 82.725  120.337 87.563  1.00 88.88  ? 480 GLU A OE1 1 
ATOM 3709 O OE2 . GLU A 1 497 ? 80.793  119.399 87.121  1.00 88.88  ? 480 GLU A OE2 1 
ATOM 3710 N N   . ILE A 1 498 ? 82.038  116.610 91.582  1.00 89.22  ? 481 ILE A N   1 
ATOM 3711 C CA  . ILE A 1 498 ? 82.027  115.150 91.605  1.00 89.22  ? 481 ILE A CA  1 
ATOM 3712 C C   . ILE A 1 498 ? 81.624  114.620 90.238  1.00 89.22  ? 481 ILE A C   1 
ATOM 3713 O O   . ILE A 1 498 ? 80.579  114.999 89.694  1.00 89.22  ? 481 ILE A O   1 
ATOM 3714 C CB  . ILE A 1 498 ? 81.082  114.613 92.695  1.00 89.22  ? 481 ILE A CB  1 
ATOM 3715 C CG1 . ILE A 1 498 ? 81.578  114.983 94.096  1.00 89.22  ? 481 ILE A CG1 1 
ATOM 3716 C CG2 . ILE A 1 498 ? 80.929  113.105 92.572  1.00 89.22  ? 481 ILE A CG2 1 
ATOM 3717 C CD1 . ILE A 1 498 ? 83.076  115.157 94.197  1.00 89.22  ? 481 ILE A CD1 1 
ATOM 3718 N N   . THR A 1 499 ? 82.454  113.743 89.686  1.00 97.17  ? 482 THR A N   1 
ATOM 3719 C CA  . THR A 1 499 ? 82.150  112.960 88.498  1.00 97.17  ? 482 THR A CA  1 
ATOM 3720 C C   . THR A 1 499 ? 82.333  111.480 88.825  1.00 97.17  ? 482 THR A C   1 
ATOM 3721 O O   . THR A 1 499 ? 82.571  111.099 89.973  1.00 97.17  ? 482 THR A O   1 
ATOM 3722 C CB  . THR A 1 499 ? 83.032  113.377 87.317  1.00 97.17  ? 482 THR A CB  1 
ATOM 3723 O OG1 . THR A 1 499 ? 84.413  113.273 87.686  1.00 97.17  ? 482 THR A OG1 1 
ATOM 3724 C CG2 . THR A 1 499 ? 82.726  114.808 86.900  1.00 97.17  ? 482 THR A CG2 1 
ATOM 3725 N N   . SER A 1 500 ? 82.219  110.642 87.801  1.00 97.55  ? 483 SER A N   1 
ATOM 3726 C CA  . SER A 1 500 ? 82.372  109.204 87.986  1.00 97.55  ? 483 SER A CA  1 
ATOM 3727 C C   . SER A 1 500 ? 83.650  108.693 87.329  1.00 97.55  ? 483 SER A C   1 
ATOM 3728 O O   . SER A 1 500 ? 84.218  107.688 87.757  1.00 97.55  ? 483 SER A O   1 
ATOM 3729 C CB  . SER A 1 500 ? 81.160  108.461 87.424  1.00 97.55  ? 483 SER A CB  1 
ATOM 3730 O OG  . SER A 1 500 ? 80.079  108.489 88.339  1.00 97.55  ? 483 SER A OG  1 
ATOM 3731 N N   . SER A 1 512 ? 109.446 104.720 106.082 1.00 127.46 ? 495 SER A N   1 
ATOM 3732 C CA  . SER A 1 512 ? 109.838 103.429 106.633 1.00 127.46 ? 495 SER A CA  1 
ATOM 3733 C C   . SER A 1 512 ? 110.888 102.755 105.757 1.00 127.46 ? 495 SER A C   1 
ATOM 3734 O O   . SER A 1 512 ? 111.021 103.073 104.576 1.00 127.46 ? 495 SER A O   1 
ATOM 3735 C CB  . SER A 1 512 ? 108.619 102.518 106.787 1.00 127.46 ? 495 SER A CB  1 
ATOM 3736 O OG  . SER A 1 512 ? 108.536 101.594 105.716 1.00 127.46 ? 495 SER A OG  1 
ATOM 3737 N N   . LEU A 1 513 ? 111.636 101.820 106.347 1.00 126.13 ? 496 LEU A N   1 
ATOM 3738 C CA  . LEU A 1 513 ? 112.671 101.113 105.603 1.00 126.13 ? 496 LEU A CA  1 
ATOM 3739 C C   . LEU A 1 513 ? 112.096 100.104 104.618 1.00 126.13 ? 496 LEU A C   1 
ATOM 3740 O O   . LEU A 1 513 ? 112.799 99.695  103.687 1.00 126.13 ? 496 LEU A O   1 
ATOM 3741 C CB  . LEU A 1 513 ? 113.623 100.409 106.571 1.00 126.13 ? 496 LEU A CB  1 
ATOM 3742 C CG  . LEU A 1 513 ? 114.293 101.284 107.634 1.00 126.13 ? 496 LEU A CG  1 
ATOM 3743 C CD1 . LEU A 1 513 ? 115.390 100.511 108.352 1.00 126.13 ? 496 LEU A CD1 1 
ATOM 3744 C CD2 . LEU A 1 513 ? 114.847 102.561 107.020 1.00 126.13 ? 496 LEU A CD2 1 
ATOM 3745 N N   . ASP A 1 514 ? 110.839 99.691  104.804 1.00 125.97 ? 497 ASP A N   1 
ATOM 3746 C CA  . ASP A 1 514 ? 110.248 98.687  103.924 1.00 125.97 ? 497 ASP A CA  1 
ATOM 3747 C C   . ASP A 1 514 ? 110.123 99.204  102.496 1.00 125.97 ? 497 ASP A C   1 
ATOM 3748 O O   . ASP A 1 514 ? 110.428 98.483  101.536 1.00 125.97 ? 497 ASP A O   1 
ATOM 3749 C CB  . ASP A 1 514 ? 108.883 98.259  104.462 1.00 125.97 ? 497 ASP A CB  1 
ATOM 3750 C CG  . ASP A 1 514 ? 108.970 97.638  105.842 1.00 125.97 ? 497 ASP A CG  1 
ATOM 3751 O OD1 . ASP A 1 514 ? 110.088 97.267  106.260 1.00 125.97 ? 497 ASP A OD1 1 
ATOM 3752 O OD2 . ASP A 1 514 ? 107.921 97.520  106.510 1.00 125.97 ? 497 ASP A OD2 1 
ATOM 3753 N N   . LEU A 1 515 ? 109.677 100.451 102.332 1.00 118.66 ? 498 LEU A N   1 
ATOM 3754 C CA  . LEU A 1 515 ? 109.566 101.013 100.991 1.00 118.66 ? 498 LEU A CA  1 
ATOM 3755 C C   . LEU A 1 515 ? 110.935 101.209 100.353 1.00 118.66 ? 498 LEU A C   1 
ATOM 3756 O O   . LEU A 1 515 ? 111.081 101.031 99.140  1.00 118.66 ? 498 LEU A O   1 
ATOM 3757 C CB  . LEU A 1 515 ? 108.767 102.321 101.030 1.00 118.66 ? 498 LEU A CB  1 
ATOM 3758 C CG  . LEU A 1 515 ? 109.156 103.491 101.942 1.00 118.66 ? 498 LEU A CG  1 
ATOM 3759 C CD1 . LEU A 1 515 ? 110.296 104.326 101.373 1.00 118.66 ? 498 LEU A CD1 1 
ATOM 3760 C CD2 . LEU A 1 515 ? 107.942 104.365 102.226 1.00 118.66 ? 498 LEU A CD2 1 
ATOM 3761 N N   . ILE A 1 516 ? 111.950 101.553 101.150 1.00 107.29 ? 499 ILE A N   1 
ATOM 3762 C CA  . ILE A 1 516 ? 113.306 101.665 100.617 1.00 107.29 ? 499 ILE A CA  1 
ATOM 3763 C C   . ILE A 1 516 ? 113.798 100.309 100.128 1.00 107.29 ? 499 ILE A C   1 
ATOM 3764 O O   . ILE A 1 516 ? 114.407 100.200 99.056  1.00 107.29 ? 499 ILE A O   1 
ATOM 3765 C CB  . ILE A 1 516 ? 114.249 102.264 101.677 1.00 107.29 ? 499 ILE A CB  1 
ATOM 3766 C CG1 . ILE A 1 516 ? 113.801 103.680 102.047 1.00 107.29 ? 499 ILE A CG1 1 
ATOM 3767 C CG2 . ILE A 1 516 ? 115.685 102.260 101.176 1.00 107.29 ? 499 ILE A CG2 1 
ATOM 3768 C CD1 . ILE A 1 516 ? 114.883 104.529 102.680 1.00 107.29 ? 499 ILE A CD1 1 
ATOM 3769 N N   . GLN A 1 517 ? 113.540 99.253  100.905 1.00 114.76 ? 500 GLN A N   1 
ATOM 3770 C CA  . GLN A 1 517 ? 113.935 97.911  100.484 1.00 114.76 ? 500 GLN A CA  1 
ATOM 3771 C C   . GLN A 1 517 ? 113.209 97.496  99.210  1.00 114.76 ? 500 GLN A C   1 
ATOM 3772 O O   . GLN A 1 517 ? 113.806 96.885  98.315  1.00 114.76 ? 500 GLN A O   1 
ATOM 3773 C CB  . GLN A 1 517 ? 113.665 96.910  101.608 1.00 114.76 ? 500 GLN A CB  1 
ATOM 3774 C CG  . GLN A 1 517 ? 114.599 97.046  102.798 1.00 114.76 ? 500 GLN A CG  1 
ATOM 3775 C CD  . GLN A 1 517 ? 116.060 96.953  102.407 1.00 114.76 ? 500 GLN A CD  1 
ATOM 3776 O OE1 . GLN A 1 517 ? 116.499 95.955  101.836 1.00 114.76 ? 500 GLN A OE1 1 
ATOM 3777 N NE2 . GLN A 1 517 ? 116.822 97.996  102.714 1.00 114.76 ? 500 GLN A NE2 1 
ATOM 3778 N N   . GLN A 1 518 ? 111.916 97.815  99.113  1.00 117.29 ? 501 GLN A N   1 
ATOM 3779 C CA  . GLN A 1 518 ? 111.165 97.488  97.904  1.00 117.29 ? 501 GLN A CA  1 
ATOM 3780 C C   . GLN A 1 518 ? 111.708 98.241  96.694  1.00 117.29 ? 501 GLN A C   1 
ATOM 3781 O O   . GLN A 1 518 ? 111.850 97.666  95.607  1.00 117.29 ? 501 GLN A O   1 
ATOM 3782 C CB  . GLN A 1 518 ? 109.681 97.793  98.110  1.00 117.29 ? 501 GLN A CB  1 
ATOM 3783 C CG  . GLN A 1 518 ? 108.932 96.713  98.875  1.00 117.29 ? 501 GLN A CG  1 
ATOM 3784 C CD  . GLN A 1 518 ? 107.604 97.197  99.421  1.00 117.29 ? 501 GLN A CD  1 
ATOM 3785 O OE1 . GLN A 1 518 ? 107.196 98.333  99.178  1.00 117.29 ? 501 GLN A OE1 1 
ATOM 3786 N NE2 . GLN A 1 518 ? 106.920 96.334  100.164 1.00 117.29 ? 501 GLN A NE2 1 
ATOM 3787 N N   . TYR A 1 519 ? 112.025 99.527  96.865  1.00 101.11 ? 502 TYR A N   1 
ATOM 3788 C CA  . TYR A 1 519 ? 112.601 100.299 95.769  1.00 101.11 ? 502 TYR A CA  1 
ATOM 3789 C C   . TYR A 1 519 ? 113.951 99.731  95.349  1.00 101.11 ? 502 TYR A C   1 
ATOM 3790 O O   . TYR A 1 519 ? 114.274 99.698  94.156  1.00 101.11 ? 502 TYR A O   1 
ATOM 3791 C CB  . TYR A 1 519 ? 112.733 101.767 96.175  1.00 101.11 ? 502 TYR A CB  1 
ATOM 3792 C CG  . TYR A 1 519 ? 111.530 102.613 95.820  1.00 101.11 ? 502 TYR A CG  1 
ATOM 3793 C CD1 . TYR A 1 519 ? 111.395 103.167 94.554  1.00 101.11 ? 502 TYR A CD1 1 
ATOM 3794 C CD2 . TYR A 1 519 ? 110.529 102.856 96.750  1.00 101.11 ? 502 TYR A CD2 1 
ATOM 3795 C CE1 . TYR A 1 519 ? 110.297 103.941 94.226  1.00 101.11 ? 502 TYR A CE1 1 
ATOM 3796 C CE2 . TYR A 1 519 ? 109.428 103.628 96.432  1.00 101.11 ? 502 TYR A CE2 1 
ATOM 3797 C CZ  . TYR A 1 519 ? 109.317 104.168 95.169  1.00 101.11 ? 502 TYR A CZ  1 
ATOM 3798 O OH  . TYR A 1 519 ? 108.222 104.936 94.850  1.00 101.11 ? 502 TYR A OH  1 
ATOM 3799 N N   . TYR A 1 520 ? 114.755 99.285  96.318  1.00 101.44 ? 503 TYR A N   1 
ATOM 3800 C CA  . TYR A 1 520 ? 116.011 98.616  95.990  1.00 101.44 ? 503 TYR A CA  1 
ATOM 3801 C C   . TYR A 1 520 ? 115.767 97.353  95.178  1.00 101.44 ? 503 TYR A C   1 
ATOM 3802 O O   . TYR A 1 520 ? 116.456 97.102  94.182  1.00 101.44 ? 503 TYR A O   1 
ATOM 3803 C CB  . TYR A 1 520 ? 116.782 98.284  97.266  1.00 101.44 ? 503 TYR A CB  1 
ATOM 3804 C CG  . TYR A 1 520 ? 118.021 97.451  97.028  1.00 101.44 ? 503 TYR A CG  1 
ATOM 3805 C CD1 . TYR A 1 520 ? 119.128 97.983  96.380  1.00 101.44 ? 503 TYR A CD1 1 
ATOM 3806 C CD2 . TYR A 1 520 ? 118.076 96.124  97.435  1.00 101.44 ? 503 TYR A CD2 1 
ATOM 3807 C CE1 . TYR A 1 520 ? 120.260 97.222  96.160  1.00 101.44 ? 503 TYR A CE1 1 
ATOM 3808 C CE2 . TYR A 1 520 ? 119.204 95.356  97.217  1.00 101.44 ? 503 TYR A CE2 1 
ATOM 3809 C CZ  . TYR A 1 520 ? 120.292 95.910  96.577  1.00 101.44 ? 503 TYR A CZ  1 
ATOM 3810 O OH  . TYR A 1 520 ? 121.417 95.149  96.356  1.00 101.44 ? 503 TYR A OH  1 
ATOM 3811 N N   . LEU A 1 521 ? 114.789 96.546  95.588  1.00 114.24 ? 504 LEU A N   1 
ATOM 3812 C CA  . LEU A 1 521 ? 114.471 95.336  94.842  1.00 114.24 ? 504 LEU A CA  1 
ATOM 3813 C C   . LEU A 1 521 ? 113.941 95.640  93.447  1.00 114.24 ? 504 LEU A C   1 
ATOM 3814 O O   . LEU A 1 521 ? 114.076 94.800  92.551  1.00 114.24 ? 504 LEU A O   1 
ATOM 3815 C CB  . LEU A 1 521 ? 113.462 94.487  95.617  1.00 114.24 ? 504 LEU A CB  1 
ATOM 3816 C CG  . LEU A 1 521 ? 114.047 93.355  96.467  1.00 114.24 ? 504 LEU A CG  1 
ATOM 3817 C CD1 . LEU A 1 521 ? 114.676 92.292  95.579  1.00 114.24 ? 504 LEU A CD1 1 
ATOM 3818 C CD2 . LEU A 1 521 ? 115.060 93.883  97.475  1.00 114.24 ? 504 LEU A CD2 1 
ATOM 3819 N N   . THR A 1 522 ? 113.347 96.815  93.241  1.00 113.49 ? 505 THR A N   1 
ATOM 3820 C CA  . THR A 1 522 ? 112.860 97.219  91.928  1.00 113.49 ? 505 THR A CA  1 
ATOM 3821 C C   . THR A 1 522 ? 113.821 98.137  91.179  1.00 113.49 ? 505 THR A C   1 
ATOM 3822 O O   . THR A 1 522 ? 113.469 98.629  90.103  1.00 113.49 ? 505 THR A O   1 
ATOM 3823 C CB  . THR A 1 522 ? 111.494 97.904  92.053  1.00 113.49 ? 505 THR A CB  1 
ATOM 3824 O OG1 . THR A 1 522 ? 111.639 99.145  92.756  1.00 113.49 ? 505 THR A OG1 1 
ATOM 3825 C CG2 . THR A 1 522 ? 110.508 97.009  92.788  1.00 113.49 ? 505 THR A CG2 1 
ATOM 3826 N N   . PHE A 1 523 ? 115.015 98.381  91.712  1.00 101.46 ? 506 PHE A N   1 
ATOM 3827 C CA  . PHE A 1 523 ? 115.973 99.266  91.066  1.00 101.46 ? 506 PHE A CA  1 
ATOM 3828 C C   . PHE A 1 523 ? 116.873 98.492  90.104  1.00 101.46 ? 506 PHE A C   1 
ATOM 3829 O O   . PHE A 1 523 ? 116.855 97.261  90.041  1.00 101.46 ? 506 PHE A O   1 
ATOM 3830 C CB  . PHE A 1 523 ? 116.819 99.996  92.110  1.00 101.46 ? 506 PHE A CB  1 
ATOM 3831 C CG  . PHE A 1 523 ? 117.072 101.443 91.785  1.00 101.46 ? 506 PHE A CG  1 
ATOM 3832 C CD1 . PHE A 1 523 ? 118.096 101.807 90.928  1.00 101.46 ? 506 PHE A CD1 1 
ATOM 3833 C CD2 . PHE A 1 523 ? 116.292 102.438 92.343  1.00 101.46 ? 506 PHE A CD2 1 
ATOM 3834 C CE1 . PHE A 1 523 ? 118.335 103.132 90.629  1.00 101.46 ? 506 PHE A CE1 1 
ATOM 3835 C CE2 . PHE A 1 523 ? 116.528 103.764 92.046  1.00 101.46 ? 506 PHE A CE2 1 
ATOM 3836 C CZ  . PHE A 1 523 ? 117.549 104.112 91.189  1.00 101.46 ? 506 PHE A CZ  1 
ATOM 3837 N N   . ASN A 1 524 ? 117.673 99.241  89.346  1.00 102.45 ? 507 ASN A N   1 
ATOM 3838 C CA  . ASN A 1 524 ? 118.628 98.678  88.401  1.00 102.45 ? 507 ASN A CA  1 
ATOM 3839 C C   . ASN A 1 524 ? 119.983 99.357  88.555  1.00 102.45 ? 507 ASN A C   1 
ATOM 3840 O O   . ASN A 1 524 ? 120.066 100.587 88.628  1.00 102.45 ? 507 ASN A O   1 
ATOM 3841 C CB  . ASN A 1 524 ? 118.114 98.801  86.957  1.00 102.45 ? 507 ASN A CB  1 
ATOM 3842 C CG  . ASN A 1 524 ? 117.633 100.205 86.611  1.00 102.45 ? 507 ASN A CG  1 
ATOM 3843 O OD1 . ASN A 1 524 ? 117.860 101.162 87.350  1.00 102.45 ? 507 ASN A OD1 1 
ATOM 3844 N ND2 . ASN A 1 524 ? 116.963 100.328 85.472  1.00 102.45 ? 507 ASN A ND2 1 
ATOM 3845 N N   . PHE A 1 525 ? 121.039 98.549  88.620  1.00 96.08  ? 508 PHE A N   1 
ATOM 3846 C CA  . PHE A 1 525 ? 122.424 99.008  88.664  1.00 96.08  ? 508 PHE A CA  1 
ATOM 3847 C C   . PHE A 1 525 ? 123.238 98.334  87.571  1.00 96.08  ? 508 PHE A C   1 
ATOM 3848 O O   . PHE A 1 525 ? 124.408 97.989  87.762  1.00 96.08  ? 508 PHE A O   1 
ATOM 3849 C CB  . PHE A 1 525 ? 123.054 98.744  90.030  1.00 96.08  ? 508 PHE A CB  1 
ATOM 3850 C CG  . PHE A 1 525 ? 122.209 99.178  91.191  1.00 96.08  ? 508 PHE A CG  1 
ATOM 3851 C CD1 . PHE A 1 525 ? 121.682 100.456 91.245  1.00 96.08  ? 508 PHE A CD1 1 
ATOM 3852 C CD2 . PHE A 1 525 ? 121.929 98.300  92.223  1.00 96.08  ? 508 PHE A CD2 1 
ATOM 3853 C CE1 . PHE A 1 525 ? 120.908 100.855 92.315  1.00 96.08  ? 508 PHE A CE1 1 
ATOM 3854 C CE2 . PHE A 1 525 ? 121.149 98.692  93.290  1.00 96.08  ? 508 PHE A CE2 1 
ATOM 3855 C CZ  . PHE A 1 525 ? 120.637 99.971  93.337  1.00 96.08  ? 508 PHE A CZ  1 
ATOM 3856 N N   . ASP A 1 526 ? 122.628 98.135  86.405  1.00 113.18 ? 509 ASP A N   1 
ATOM 3857 C CA  . ASP A 1 526 ? 123.243 97.345  85.346  1.00 113.18 ? 509 ASP A CA  1 
ATOM 3858 C C   . ASP A 1 526 ? 124.252 98.147  84.529  1.00 113.18 ? 509 ASP A C   1 
ATOM 3859 O O   . ASP A 1 526 ? 125.405 97.729  84.383  1.00 113.18 ? 509 ASP A O   1 
ATOM 3860 C CB  . ASP A 1 526 ? 122.159 96.771  84.429  1.00 113.18 ? 509 ASP A CB  1 
ATOM 3861 C CG  . ASP A 1 526 ? 121.194 95.864  85.166  1.00 113.18 ? 509 ASP A CG  1 
ATOM 3862 O OD1 . ASP A 1 526 ? 121.596 95.271  86.189  1.00 113.18 ? 509 ASP A OD1 1 
ATOM 3863 O OD2 . ASP A 1 526 ? 120.032 95.745  84.723  1.00 113.18 ? 509 ASP A OD2 1 
ATOM 3864 N N   . ASN A 1 527 ? 123.841 99.293  83.991  1.00 98.47  ? 510 ASN A N   1 
ATOM 3865 C CA  . ASN A 1 527 ? 124.671 100.059 83.072  1.00 98.47  ? 510 ASN A CA  1 
ATOM 3866 C C   . ASN A 1 527 ? 124.653 101.528 83.463  1.00 98.47  ? 510 ASN A C   1 
ATOM 3867 O O   . ASN A 1 527 ? 123.589 102.085 83.753  1.00 98.47  ? 510 ASN A O   1 
ATOM 3868 C CB  . ASN A 1 527 ? 124.186 99.883  81.627  1.00 98.47  ? 510 ASN A CB  1 
ATOM 3869 C CG  . ASN A 1 527 ? 125.237 100.270 80.605  1.00 98.47  ? 510 ASN A CG  1 
ATOM 3870 O OD1 . ASN A 1 527 ? 125.882 101.311 80.720  1.00 98.47  ? 510 ASN A OD1 1 
ATOM 3871 N ND2 . ASN A 1 527 ? 125.414 99.428  79.594  1.00 98.47  ? 510 ASN A ND2 1 
ATOM 3872 N N   . GLU A 1 528 ? 125.846 102.157 83.471  1.00 79.19  ? 511 GLU A N   1 
ATOM 3873 C CA  . GLU A 1 528 ? 126.077 103.571 83.719  1.00 79.19  ? 511 GLU A CA  1 
ATOM 3874 C C   . GLU A 1 528 ? 126.495 104.274 82.432  1.00 79.19  ? 511 GLU A C   1 
ATOM 3875 O O   . GLU A 1 528 ? 127.075 103.649 81.538  1.00 79.19  ? 511 GLU A O   1 
ATOM 3876 C CB  . GLU A 1 528 ? 127.165 103.764 84.780  1.00 79.19  ? 511 GLU A CB  1 
ATOM 3877 C CG  . GLU A 1 528 ? 126.941 102.974 86.058  1.00 79.19  ? 511 GLU A CG  1 
ATOM 3878 C CD  . GLU A 1 528 ? 128.051 103.177 87.070  1.00 79.19  ? 511 GLU A CD  1 
ATOM 3879 O OE1 . GLU A 1 528 ? 129.147 103.624 86.671  1.00 79.19  ? 511 GLU A OE1 1 
ATOM 3880 O OE2 . GLU A 1 528 ? 127.828 102.892 88.265  1.00 79.19  ? 511 GLU A OE2 1 
ATOM 3881 N N   . PRO A 1 529 ? 126.209 105.570 82.300  1.00 69.28  ? 512 PRO A N   1 
ATOM 3882 C CA  . PRO A 1 529 ? 126.591 106.285 81.075  1.00 69.28  ? 512 PRO A CA  1 
ATOM 3883 C C   . PRO A 1 529 ? 128.094 106.238 80.846  1.00 69.28  ? 512 PRO A C   1 
ATOM 3884 O O   . PRO A 1 529 ? 128.890 106.354 81.780  1.00 69.28  ? 512 PRO A O   1 
ATOM 3885 C CB  . PRO A 1 529 ? 126.105 107.715 81.333  1.00 69.28  ? 512 PRO A CB  1 
ATOM 3886 C CG  . PRO A 1 529 ? 125.023 107.569 82.348  1.00 69.28  ? 512 PRO A CG  1 
ATOM 3887 C CD  . PRO A 1 529 ? 125.440 106.425 83.221  1.00 69.28  ? 512 PRO A CD  1 
ATOM 3888 N N   . GLU A 1 530 ? 128.476 106.068 79.585  1.00 76.01  ? 513 GLU A N   1 
ATOM 3889 C CA  . GLU A 1 530 ? 129.876 105.967 79.206  1.00 76.01  ? 513 GLU A CA  1 
ATOM 3890 C C   . GLU A 1 530 ? 130.462 107.347 78.927  1.00 76.01  ? 513 GLU A C   1 
ATOM 3891 O O   . GLU A 1 530 ? 129.746 108.315 78.659  1.00 76.01  ? 513 GLU A O   1 
ATOM 3892 C CB  . GLU A 1 530 ? 130.038 105.074 77.975  1.00 76.01  ? 513 GLU A CB  1 
ATOM 3893 C CG  . GLU A 1 530 ? 129.696 103.614 78.215  1.00 76.01  ? 513 GLU A CG  1 
ATOM 3894 C CD  . GLU A 1 530 ? 129.843 102.771 76.964  1.00 76.01  ? 513 GLU A CD  1 
ATOM 3895 O OE1 . GLU A 1 530 ? 130.222 103.327 75.911  1.00 76.01  ? 513 GLU A OE1 1 
ATOM 3896 O OE2 . GLU A 1 530 ? 129.581 101.551 77.032  1.00 76.01  ? 513 GLU A OE2 1 
ATOM 3897 N N   . ASN A 1 531 ? 131.790 107.426 78.996  1.00 74.44  ? 514 ASN A N   1 
ATOM 3898 C CA  . ASN A 1 531 ? 132.516 108.655 78.675  1.00 74.44  ? 514 ASN A CA  1 
ATOM 3899 C C   . ASN A 1 531 ? 132.814 108.633 77.182  1.00 74.44  ? 514 ASN A C   1 
ATOM 3900 O O   . ASN A 1 531 ? 133.828 108.097 76.733  1.00 74.44  ? 514 ASN A O   1 
ATOM 3901 C CB  . ASN A 1 531 ? 133.785 108.769 79.510  1.00 74.44  ? 514 ASN A CB  1 
ATOM 3902 C CG  . ASN A 1 531 ? 134.639 109.957 79.114  1.00 74.44  ? 514 ASN A CG  1 
ATOM 3903 O OD1 . ASN A 1 531 ? 134.124 111.005 78.726  1.00 74.44  ? 514 ASN A OD1 1 
ATOM 3904 N ND2 . ASN A 1 531 ? 135.954 109.799 79.211  1.00 74.44  ? 514 ASN A ND2 1 
ATOM 3905 N N   . ILE A 1 532 ? 131.914 109.223 76.403  1.00 75.37  ? 515 ILE A N   1 
ATOM 3906 C CA  . ILE A 1 532 ? 132.027 109.207 74.949  1.00 75.37  ? 515 ILE A CA  1 
ATOM 3907 C C   . ILE A 1 532 ? 132.964 110.321 74.504  1.00 75.37  ? 515 ILE A C   1 
ATOM 3908 O O   . ILE A 1 532 ? 132.994 111.406 75.098  1.00 75.37  ? 515 ILE A O   1 
ATOM 3909 C CB  . ILE A 1 532 ? 130.635 109.338 74.302  1.00 75.37  ? 515 ILE A CB  1 
ATOM 3910 C CG1 . ILE A 1 532 ? 130.735 109.281 72.776  1.00 75.37  ? 515 ILE A CG1 1 
ATOM 3911 C CG2 . ILE A 1 532 ? 129.947 110.619 74.755  1.00 75.37  ? 515 ILE A CG2 1 
ATOM 3912 C CD1 . ILE A 1 532 ? 131.324 107.989 72.251  1.00 75.37  ? 515 ILE A CD1 1 
ATOM 3913 N N   . SER A 1 533 ? 133.752 110.046 73.467  1.00 70.71  ? 516 SER A N   1 
ATOM 3914 C CA  . SER A 1 533 ? 134.677 111.041 72.944  1.00 70.71  ? 516 SER A CA  1 
ATOM 3915 C C   . SER A 1 533 ? 133.918 112.246 72.402  1.00 70.71  ? 516 SER A C   1 
ATOM 3916 O O   . SER A 1 533 ? 132.890 112.106 71.735  1.00 70.71  ? 516 SER A O   1 
ATOM 3917 C CB  . SER A 1 533 ? 135.547 110.430 71.845  1.00 70.71  ? 516 SER A CB  1 
ATOM 3918 O OG  . SER A 1 533 ? 136.080 111.434 71.000  1.00 70.71  ? 516 SER A OG  1 
ATOM 3919 N N   . ILE A 1 534 ? 134.434 113.436 72.696  1.00 62.56  ? 517 ILE A N   1 
ATOM 3920 C CA  . ILE A 1 534 ? 133.812 114.692 72.296  1.00 62.56  ? 517 ILE A CA  1 
ATOM 3921 C C   . ILE A 1 534 ? 134.896 115.609 71.746  1.00 62.56  ? 517 ILE A C   1 
ATOM 3922 O O   . ILE A 1 534 ? 136.029 115.610 72.238  1.00 62.56  ? 517 ILE A O   1 
ATOM 3923 C CB  . ILE A 1 534 ? 133.060 115.347 73.476  1.00 62.56  ? 517 ILE A CB  1 
ATOM 3924 C CG1 . ILE A 1 534 ? 132.551 116.742 73.105  1.00 62.56  ? 517 ILE A CG1 1 
ATOM 3925 C CG2 . ILE A 1 534 ? 133.941 115.402 74.710  1.00 62.56  ? 517 ILE A CG2 1 
ATOM 3926 C CD1 . ILE A 1 534 ? 131.778 117.420 74.214  1.00 62.56  ? 517 ILE A CD1 1 
ATOM 3927 N N   . GLU A 1 535 ? 134.553 116.372 70.708  1.00 65.61  ? 518 GLU A N   1 
ATOM 3928 C CA  . GLU A 1 535 ? 135.506 117.296 70.107  1.00 65.61  ? 518 GLU A CA  1 
ATOM 3929 C C   . GLU A 1 535 ? 135.992 118.309 71.136  1.00 65.61  ? 518 GLU A C   1 
ATOM 3930 O O   . GLU A 1 535 ? 135.226 118.773 71.986  1.00 65.61  ? 518 GLU A O   1 
ATOM 3931 C CB  . GLU A 1 535 ? 134.871 118.018 68.919  1.00 65.61  ? 518 GLU A CB  1 
ATOM 3932 C CG  . GLU A 1 535 ? 134.858 117.210 67.631  1.00 65.61  ? 518 GLU A CG  1 
ATOM 3933 C CD  . GLU A 1 535 ? 136.087 117.450 66.777  1.00 65.61  ? 518 GLU A CD  1 
ATOM 3934 O OE1 . GLU A 1 535 ? 137.197 117.552 67.341  1.00 65.61  ? 518 GLU A OE1 1 
ATOM 3935 O OE2 . GLU A 1 535 ? 135.943 117.538 65.540  1.00 65.61  ? 518 GLU A OE2 1 
ATOM 3936 N N   . ASN A 1 536 ? 137.278 118.643 71.058  1.00 53.43  ? 519 ASN A N   1 
ATOM 3937 C CA  . ASN A 1 536 ? 137.888 119.521 72.046  1.00 53.43  ? 519 ASN A CA  1 
ATOM 3938 C C   . ASN A 1 536 ? 137.253 120.905 72.015  1.00 53.43  ? 519 ASN A C   1 
ATOM 3939 O O   . ASN A 1 536 ? 136.942 121.445 70.950  1.00 53.43  ? 519 ASN A O   1 
ATOM 3940 C CB  . ASN A 1 536 ? 139.393 119.627 71.800  1.00 53.43  ? 519 ASN A CB  1 
ATOM 3941 C CG  . ASN A 1 536 ? 139.742 119.643 70.327  1.00 53.43  ? 519 ASN A CG  1 
ATOM 3942 O OD1 . ASN A 1 536 ? 139.435 120.598 69.614  1.00 53.43  ? 519 ASN A OD1 1 
ATOM 3943 N ND2 . ASN A 1 536 ? 140.388 118.580 69.861  1.00 53.43  ? 519 ASN A ND2 1 
ATOM 3944 N N   . LEU A 1 537 ? 137.061 121.477 73.200  1.00 53.85  ? 520 LEU A N   1 
ATOM 3945 C CA  . LEU A 1 537 ? 136.485 122.803 73.351  1.00 53.85  ? 520 LEU A CA  1 
ATOM 3946 C C   . LEU A 1 537 ? 137.587 123.854 73.219  1.00 53.85  ? 520 LEU A C   1 
ATOM 3947 O O   . LEU A 1 537 ? 138.707 123.564 72.790  1.00 53.85  ? 520 LEU A O   1 
ATOM 3948 C CB  . LEU A 1 537 ? 135.751 122.908 74.686  1.00 53.85  ? 520 LEU A CB  1 
ATOM 3949 C CG  . LEU A 1 537 ? 134.234 122.710 74.658  1.00 53.85  ? 520 LEU A CG  1 
ATOM 3950 C CD1 . LEU A 1 537 ? 133.882 121.287 74.256  1.00 53.85  ? 520 LEU A CD1 1 
ATOM 3951 C CD2 . LEU A 1 537 ? 133.633 123.047 76.012  1.00 53.85  ? 520 LEU A CD2 1 
ATOM 3952 N N   . SER A 1 538 ? 137.275 125.093 73.586  1.00 58.63  ? 521 SER A N   1 
ATOM 3953 C CA  . SER A 1 538 ? 138.249 126.168 73.505  1.00 58.63  ? 521 SER A CA  1 
ATOM 3954 C C   . SER A 1 538 ? 139.333 125.989 74.567  1.00 58.63  ? 521 SER A C   1 
ATOM 3955 O O   . SER A 1 538 ? 139.216 125.178 75.490  1.00 58.63  ? 521 SER A O   1 
ATOM 3956 C CB  . SER A 1 538 ? 137.563 127.524 73.668  1.00 58.63  ? 521 SER A CB  1 
ATOM 3957 O OG  . SER A 1 538 ? 136.752 127.823 72.545  1.00 58.63  ? 521 SER A OG  1 
ATOM 3958 N N   . SER A 1 539 ? 140.410 126.767 74.420  1.00 58.93  ? 522 SER A N   1 
ATOM 3959 C CA  . SER A 1 539 ? 141.517 126.689 75.369  1.00 58.93  ? 522 SER A CA  1 
ATOM 3960 C C   . SER A 1 539 ? 141.066 127.061 76.776  1.00 58.93  ? 522 SER A C   1 
ATOM 3961 O O   . SER A 1 539 ? 141.426 126.390 77.750  1.00 58.93  ? 522 SER A O   1 
ATOM 3962 C CB  . SER A 1 539 ? 142.661 127.596 74.917  1.00 58.93  ? 522 SER A CB  1 
ATOM 3963 O OG  . SER A 1 539 ? 143.386 128.094 76.028  1.00 58.93  ? 522 SER A OG  1 
ATOM 3964 N N   . ASP A 1 540 ? 140.282 128.126 76.902  1.00 62.57  ? 523 ASP A N   1 
ATOM 3965 C CA  . ASP A 1 540 ? 139.710 128.541 78.174  1.00 62.57  ? 523 ASP A CA  1 
ATOM 3966 C C   . ASP A 1 540 ? 138.195 128.462 78.077  1.00 62.57  ? 523 ASP A C   1 
ATOM 3967 O O   . ASP A 1 540 ? 137.603 128.976 77.123  1.00 62.57  ? 523 ASP A O   1 
ATOM 3968 C CB  . ASP A 1 540 ? 140.150 129.960 78.545  1.00 62.57  ? 523 ASP A CB  1 
ATOM 3969 C CG  . ASP A 1 540 ? 140.065 130.919 77.376  1.00 62.57  ? 523 ASP A CG  1 
ATOM 3970 O OD1 . ASP A 1 540 ? 140.515 130.552 76.270  1.00 62.57  ? 523 ASP A OD1 1 
ATOM 3971 O OD2 . ASP A 1 540 ? 139.548 132.041 77.561  1.00 62.57  ? 523 ASP A OD2 1 
ATOM 3972 N N   . ILE A 1 541 ? 137.574 127.817 79.061  1.00 57.30  ? 524 ILE A N   1 
ATOM 3973 C CA  . ILE A 1 541 ? 136.124 127.664 79.096  1.00 57.30  ? 524 ILE A CA  1 
ATOM 3974 C C   . ILE A 1 541 ? 135.564 128.897 79.797  1.00 57.30  ? 524 ILE A C   1 
ATOM 3975 O O   . ILE A 1 541 ? 135.636 129.022 81.020  1.00 57.30  ? 524 ILE A O   1 
ATOM 3976 C CB  . ILE A 1 541 ? 135.707 126.371 79.798  1.00 57.30  ? 524 ILE A CB  1 
ATOM 3977 C CG1 . ILE A 1 541 ? 136.600 125.213 79.350  1.00 57.30  ? 524 ILE A CG1 1 
ATOM 3978 C CG2 . ILE A 1 541 ? 134.245 126.063 79.517  1.00 57.30  ? 524 ILE A CG2 1 
ATOM 3979 C CD1 . ILE A 1 541 ? 136.298 124.712 77.958  1.00 57.30  ? 524 ILE A CD1 1 
ATOM 3980 N N   . ILE A 1 542 ? 135.008 129.817 79.015  1.00 57.77  ? 525 ILE A N   1 
ATOM 3981 C CA  . ILE A 1 542 ? 134.448 131.047 79.564  1.00 57.77  ? 525 ILE A CA  1 
ATOM 3982 C C   . ILE A 1 542 ? 133.074 130.737 80.143  1.00 57.77  ? 525 ILE A C   1 
ATOM 3983 O O   . ILE A 1 542 ? 132.154 130.351 79.415  1.00 57.77  ? 525 ILE A O   1 
ATOM 3984 C CB  . ILE A 1 542 ? 134.364 132.144 78.494  1.00 57.77  ? 525 ILE A CB  1 
ATOM 3985 C CG1 . ILE A 1 542 ? 135.767 132.573 78.060  1.00 57.77  ? 525 ILE A CG1 1 
ATOM 3986 C CG2 . ILE A 1 542 ? 133.579 133.337 79.016  1.00 57.77  ? 525 ILE A CG2 1 
ATOM 3987 C CD1 . ILE A 1 542 ? 136.725 132.794 79.212  1.00 57.77  ? 525 ILE A CD1 1 
ATOM 3988 N N   . GLY A 1 543 ? 132.935 130.905 81.454  1.00 55.96  ? 526 GLY A N   1 
ATOM 3989 C CA  . GLY A 1 543 ? 131.676 130.623 82.117  1.00 55.96  ? 526 GLY A CA  1 
ATOM 3990 C C   . GLY A 1 543 ? 131.523 131.463 83.364  1.00 55.96  ? 526 GLY A C   1 
ATOM 3991 O O   . GLY A 1 543 ? 132.503 131.925 83.957  1.00 55.96  ? 526 GLY A O   1 
ATOM 3992 N N   . GLN A 1 544 ? 130.267 131.656 83.756  1.00 59.09  ? 527 GLN A N   1 
ATOM 3993 C CA  . GLN A 1 544 ? 129.918 132.451 84.923  1.00 59.09  ? 527 GLN A CA  1 
ATOM 3994 C C   . GLN A 1 544 ? 128.979 131.646 85.808  1.00 59.09  ? 527 GLN A C   1 
ATOM 3995 O O   . GLN A 1 544 ? 128.086 130.955 85.309  1.00 59.09  ? 527 GLN A O   1 
ATOM 3996 C CB  . GLN A 1 544 ? 129.268 133.779 84.508  1.00 59.09  ? 527 GLN A CB  1 
ATOM 3997 C CG  . GLN A 1 544 ? 128.522 134.499 85.614  1.00 59.09  ? 527 GLN A CG  1 
ATOM 3998 C CD  . GLN A 1 544 ? 127.723 135.678 85.098  1.00 59.09  ? 527 GLN A CD  1 
ATOM 3999 O OE1 . GLN A 1 544 ? 127.463 135.788 83.900  1.00 59.09  ? 527 GLN A OE1 1 
ATOM 4000 N NE2 . GLN A 1 544 ? 127.333 136.570 86.000  1.00 59.09  ? 527 GLN A NE2 1 
ATOM 4001 N N   . LEU A 1 545 ? 129.191 131.732 87.120  1.00 56.72  ? 528 LEU A N   1 
ATOM 4002 C CA  . LEU A 1 545 ? 128.383 130.968 88.058  1.00 56.72  ? 528 LEU A CA  1 
ATOM 4003 C C   . LEU A 1 545 ? 126.923 131.403 87.988  1.00 56.72  ? 528 LEU A C   1 
ATOM 4004 O O   . LEU A 1 545 ? 126.595 132.517 87.572  1.00 56.72  ? 528 LEU A O   1 
ATOM 4005 C CB  . LEU A 1 545 ? 128.903 131.143 89.484  1.00 56.72  ? 528 LEU A CB  1 
ATOM 4006 C CG  . LEU A 1 545 ? 130.268 130.542 89.814  1.00 56.72  ? 528 LEU A CG  1 
ATOM 4007 C CD1 . LEU A 1 545 ? 131.095 131.540 90.605  1.00 56.72  ? 528 LEU A CD1 1 
ATOM 4008 C CD2 . LEU A 1 545 ? 130.115 129.237 90.578  1.00 56.72  ? 528 LEU A CD2 1 
ATOM 4009 N N   . GLU A 1 546 ? 126.039 130.493 88.391  1.00 66.37  ? 529 GLU A N   1 
ATOM 4010 C CA  . GLU A 1 546 ? 124.618 130.807 88.447  1.00 66.37  ? 529 GLU A CA  1 
ATOM 4011 C C   . GLU A 1 546 ? 124.378 131.972 89.397  1.00 66.37  ? 529 GLU A C   1 
ATOM 4012 O O   . GLU A 1 546 ? 124.844 131.965 90.540  1.00 66.37  ? 529 GLU A O   1 
ATOM 4013 C CB  . GLU A 1 546 ? 123.824 129.582 88.898  1.00 66.37  ? 529 GLU A CB  1 
ATOM 4014 C CG  . GLU A 1 546 ? 122.352 129.617 88.521  1.00 66.37  ? 529 GLU A CG  1 
ATOM 4015 C CD  . GLU A 1 546 ? 122.122 129.404 87.038  1.00 66.37  ? 529 GLU A CD  1 
ATOM 4016 O OE1 . GLU A 1 546 ? 122.220 130.384 86.271  1.00 66.37  ? 529 GLU A OE1 1 
ATOM 4017 O OE2 . GLU A 1 546 ? 121.842 128.254 86.639  1.00 66.37  ? 529 GLU A OE2 1 
ATOM 4018 N N   . LEU A 1 547 ? 123.651 132.978 88.918  1.00 80.69  ? 530 LEU A N   1 
ATOM 4019 C CA  . LEU A 1 547 ? 123.386 134.156 89.729  1.00 80.69  ? 530 LEU A CA  1 
ATOM 4020 C C   . LEU A 1 547 ? 122.440 133.807 90.868  1.00 80.69  ? 530 LEU A C   1 
ATOM 4021 O O   . LEU A 1 547 ? 121.377 133.216 90.651  1.00 80.69  ? 530 LEU A O   1 
ATOM 4022 C CB  . LEU A 1 547 ? 122.795 135.271 88.869  1.00 80.69  ? 530 LEU A CB  1 
ATOM 4023 C CG  . LEU A 1 547 ? 123.659 135.737 87.696  1.00 80.69  ? 530 LEU A CG  1 
ATOM 4024 C CD1 . LEU A 1 547 ? 122.828 136.518 86.690  1.00 80.69  ? 530 LEU A CD1 1 
ATOM 4025 C CD2 . LEU A 1 547 ? 124.825 136.572 88.197  1.00 80.69  ? 530 LEU A CD2 1 
ATOM 4026 N N   . MET A 1 548 ? 122.823 134.170 92.073  1.00 92.38  ? 531 MET A N   1 
ATOM 4027 C CA  . MET A 1 548 ? 121.962 133.885 93.204  1.00 92.38  ? 531 MET A CA  1 
ATOM 4028 C C   . MET A 1 548 ? 121.222 135.144 93.638  1.00 92.38  ? 531 MET A C   1 
ATOM 4029 O O   . MET A 1 548 ? 121.757 136.253 93.535  1.00 92.38  ? 531 MET A O   1 
ATOM 4030 C CB  . MET A 1 548 ? 122.777 133.340 94.381  1.00 92.38  ? 531 MET A CB  1 
ATOM 4031 C CG  . MET A 1 548 ? 123.118 131.864 94.266  1.00 92.38  ? 531 MET A CG  1 
ATOM 4032 S SD  . MET A 1 548 ? 121.660 130.805 94.313  1.00 92.38  ? 531 MET A SD  1 
ATOM 4033 C CE  . MET A 1 548 ? 121.902 129.966 95.876  1.00 92.38  ? 531 MET A CE  1 
ATOM 4034 N N   . PRO A 1 549 ? 119.986 135.004 94.114  1.00 101.02 ? 532 PRO A N   1 
ATOM 4035 C CA  . PRO A 1 549 ? 119.245 136.179 94.585  1.00 101.02 ? 532 PRO A CA  1 
ATOM 4036 C C   . PRO A 1 549 ? 119.955 136.838 95.757  1.00 101.02 ? 532 PRO A C   1 
ATOM 4037 O O   . PRO A 1 549 ? 120.564 136.169 96.595  1.00 101.02 ? 532 PRO A O   1 
ATOM 4038 C CB  . PRO A 1 549 ? 117.886 135.602 94.997  1.00 101.02 ? 532 PRO A CB  1 
ATOM 4039 C CG  . PRO A 1 549 ? 118.147 134.155 95.250  1.00 101.02 ? 532 PRO A CG  1 
ATOM 4040 C CD  . PRO A 1 549 ? 119.214 133.761 94.276  1.00 101.02 ? 532 PRO A CD  1 
ATOM 4041 N N   . ASN A 1 550 ? 119.878 138.163 95.806  1.00 107.10 ? 533 ASN A N   1 
ATOM 4042 C CA  . ASN A 1 550 ? 120.551 138.919 96.851  1.00 107.10 ? 533 ASN A CA  1 
ATOM 4043 C C   . ASN A 1 550 ? 119.780 138.805 98.159  1.00 107.10 ? 533 ASN A C   1 
ATOM 4044 O O   . ASN A 1 550 ? 118.570 139.050 98.202  1.00 107.10 ? 533 ASN A O   1 
ATOM 4045 C CB  . ASN A 1 550 ? 120.692 140.386 96.444  1.00 107.10 ? 533 ASN A CB  1 
ATOM 4046 C CG  . ASN A 1 550 ? 121.324 140.555 95.075  1.00 107.10 ? 533 ASN A CG  1 
ATOM 4047 O OD1 . ASN A 1 550 ? 121.066 141.536 94.378  1.00 107.10 ? 533 ASN A OD1 1 
ATOM 4048 N ND2 . ASN A 1 550 ? 122.165 139.603 94.687  1.00 107.10 ? 533 ASN A ND2 1 
ATOM 4049 N N   . ILE A 1 551 ? 120.482 138.433 99.224  1.00 102.49 ? 534 ILE A N   1 
ATOM 4050 C CA  . ILE A 1 551 ? 119.911 138.364 100.563 1.00 102.49 ? 534 ILE A CA  1 
ATOM 4051 C C   . ILE A 1 551 ? 120.346 139.611 101.318 1.00 102.49 ? 534 ILE A C   1 
ATOM 4052 O O   . ILE A 1 551 ? 121.542 139.815 101.559 1.00 102.49 ? 534 ILE A O   1 
ATOM 4053 C CB  . ILE A 1 551 ? 120.346 137.089 101.302 1.00 102.49 ? 534 ILE A CB  1 
ATOM 4054 C CG1 . ILE A 1 551 ? 119.676 135.855 100.692 1.00 102.49 ? 534 ILE A CG1 1 
ATOM 4055 C CG2 . ILE A 1 551 ? 120.022 137.198 102.784 1.00 102.49 ? 534 ILE A CG2 1 
ATOM 4056 C CD1 . ILE A 1 551 ? 120.516 135.149 99.651  1.00 102.49 ? 534 ILE A CD1 1 
ATOM 4057 N N   . GLU A 1 552 ? 119.379 140.446 101.685 1.00 104.27 ? 535 GLU A N   1 
ATOM 4058 C CA  . GLU A 1 552 ? 119.687 141.681 102.390 1.00 104.27 ? 535 GLU A CA  1 
ATOM 4059 C C   . GLU A 1 552 ? 120.231 141.378 103.781 1.00 104.27 ? 535 GLU A C   1 
ATOM 4060 O O   . GLU A 1 552 ? 119.775 140.451 104.456 1.00 104.27 ? 535 GLU A O   1 
ATOM 4061 C CB  . GLU A 1 552 ? 118.440 142.562 102.489 1.00 104.27 ? 535 GLU A CB  1 
ATOM 4062 C CG  . GLU A 1 552 ? 117.796 143.028 101.159 1.00 104.27 ? 535 GLU A CG  1 
ATOM 4063 C CD  . GLU A 1 552 ? 118.735 143.698 100.144 1.00 104.27 ? 535 GLU A CD  1 
ATOM 4064 O OE1 . GLU A 1 552 ? 119.966 143.486 100.152 1.00 104.27 ? 535 GLU A OE1 1 
ATOM 4065 O OE2 . GLU A 1 552 ? 118.213 144.465 99.308  1.00 104.27 ? 535 GLU A OE2 1 
ATOM 4066 N N   . ARG A 1 553 ? 121.220 142.163 104.202 1.00 100.24 ? 536 ARG A N   1 
ATOM 4067 C CA  . ARG A 1 553 ? 121.818 141.984 105.518 1.00 100.24 ? 536 ARG A CA  1 
ATOM 4068 C C   . ARG A 1 553 ? 120.791 142.292 106.600 1.00 100.24 ? 536 ARG A C   1 
ATOM 4069 O O   . ARG A 1 553 ? 120.244 143.399 106.652 1.00 100.24 ? 536 ARG A O   1 
ATOM 4070 C CB  . ARG A 1 553 ? 123.043 142.882 105.671 1.00 100.24 ? 536 ARG A CB  1 
ATOM 4071 C CG  . ARG A 1 553 ? 124.053 142.754 104.545 1.00 100.24 ? 536 ARG A CG  1 
ATOM 4072 C CD  . ARG A 1 553 ? 125.182 141.815 104.933 1.00 100.24 ? 536 ARG A CD  1 
ATOM 4073 N NE  . ARG A 1 553 ? 125.728 142.139 106.246 1.00 100.24 ? 536 ARG A NE  1 
ATOM 4074 C CZ  . ARG A 1 553 ? 126.428 141.298 106.995 1.00 100.24 ? 536 ARG A CZ  1 
ATOM 4075 N NH1 . ARG A 1 553 ? 126.691 140.066 106.589 1.00 100.24 ? 536 ARG A NH1 1 
ATOM 4076 N NH2 . ARG A 1 553 ? 126.875 141.702 108.180 1.00 100.24 ? 536 ARG A NH2 1 
ATOM 4077 N N   . PHE A 1 554 ? 120.528 141.315 107.456 1.00 87.48  ? 537 PHE A N   1 
ATOM 4078 C CA  . PHE A 1 554 ? 119.573 141.510 108.539 1.00 87.48  ? 537 PHE A CA  1 
ATOM 4079 C C   . PHE A 1 554 ? 120.132 142.511 109.544 1.00 87.48  ? 537 PHE A C   1 
ATOM 4080 O O   . PHE A 1 554 ? 121.313 142.428 109.901 1.00 87.48  ? 537 PHE A O   1 
ATOM 4081 C CB  . PHE A 1 554 ? 119.267 140.182 109.225 1.00 87.48  ? 537 PHE A CB  1 
ATOM 4082 C CG  . PHE A 1 554 ? 118.754 139.123 108.291 1.00 87.48  ? 537 PHE A CG  1 
ATOM 4083 C CD1 . PHE A 1 554 ? 118.029 139.467 107.162 1.00 87.48  ? 537 PHE A CD1 1 
ATOM 4084 C CD2 . PHE A 1 554 ? 119.007 137.784 108.536 1.00 87.48  ? 537 PHE A CD2 1 
ATOM 4085 C CE1 . PHE A 1 554 ? 117.558 138.497 106.300 1.00 87.48  ? 537 PHE A CE1 1 
ATOM 4086 C CE2 . PHE A 1 554 ? 118.541 136.808 107.675 1.00 87.48  ? 537 PHE A CE2 1 
ATOM 4087 C CZ  . PHE A 1 554 ? 117.815 137.166 106.558 1.00 87.48  ? 537 PHE A CZ  1 
ATOM 4088 N N   . PRO A 1 555 ? 119.333 143.471 110.007 1.00 78.04  ? 538 PRO A N   1 
ATOM 4089 C CA  . PRO A 1 555 ? 119.837 144.434 110.993 1.00 78.04  ? 538 PRO A CA  1 
ATOM 4090 C C   . PRO A 1 555 ? 120.253 143.738 112.281 1.00 78.04  ? 538 PRO A C   1 
ATOM 4091 O O   . PRO A 1 555 ? 119.628 142.770 112.718 1.00 78.04  ? 538 PRO A O   1 
ATOM 4092 C CB  . PRO A 1 555 ? 118.646 145.373 111.215 1.00 78.04  ? 538 PRO A CB  1 
ATOM 4093 C CG  . PRO A 1 555 ? 117.451 144.578 110.804 1.00 78.04  ? 538 PRO A CG  1 
ATOM 4094 C CD  . PRO A 1 555 ? 117.913 143.691 109.688 1.00 78.04  ? 538 PRO A CD  1 
ATOM 4095 N N   . ASN A 1 556 ? 121.323 144.244 112.885 1.00 72.95  ? 539 ASN A N   1 
ATOM 4096 C CA  . ASN A 1 556 ? 121.878 143.687 114.109 1.00 72.95  ? 539 ASN A CA  1 
ATOM 4097 C C   . ASN A 1 556 ? 121.750 144.699 115.237 1.00 72.95  ? 539 ASN A C   1 
ATOM 4098 O O   . ASN A 1 556 ? 121.992 145.894 115.042 1.00 72.95  ? 539 ASN A O   1 
ATOM 4099 C CB  . ASN A 1 556 ? 123.347 143.294 113.922 1.00 72.95  ? 539 ASN A CB  1 
ATOM 4100 C CG  . ASN A 1 556 ? 123.509 141.908 113.332 1.00 72.95  ? 539 ASN A CG  1 
ATOM 4101 O OD1 . ASN A 1 556 ? 122.544 141.303 112.866 1.00 72.95  ? 539 ASN A OD1 1 
ATOM 4102 N ND2 . ASN A 1 556 ? 124.734 141.399 113.348 1.00 72.95  ? 539 ASN A ND2 1 
ATOM 4103 N N   . GLY A 1 557 ? 121.372 144.215 116.415 1.00 59.53  ? 540 GLY A N   1 
ATOM 4104 C CA  . GLY A 1 557 ? 121.239 145.085 117.565 1.00 59.53  ? 540 GLY A CA  1 
ATOM 4105 C C   . GLY A 1 557 ? 119.945 145.860 117.639 1.00 59.53  ? 540 GLY A C   1 
ATOM 4106 O O   . GLY A 1 557 ? 119.918 146.946 118.227 1.00 59.53  ? 540 GLY A O   1 
ATOM 4107 N N   . LYS A 1 558 ? 118.869 145.342 117.049 1.00 58.43  ? 541 LYS A N   1 
ATOM 4108 C CA  . LYS A 1 558 ? 117.570 145.989 117.175 1.00 58.43  ? 541 LYS A CA  1 
ATOM 4109 C C   . LYS A 1 558 ? 117.131 145.996 118.633 1.00 58.43  ? 541 LYS A C   1 
ATOM 4110 O O   . LYS A 1 558 ? 117.252 144.988 119.335 1.00 58.43  ? 541 LYS A O   1 
ATOM 4111 C CB  . LYS A 1 558 ? 116.529 145.273 116.314 1.00 58.43  ? 541 LYS A CB  1 
ATOM 4112 C CG  . LYS A 1 558 ? 117.100 144.545 115.110 1.00 58.43  ? 541 LYS A CG  1 
ATOM 4113 C CD  . LYS A 1 558 ? 115.991 143.928 114.271 1.00 58.43  ? 541 LYS A CD  1 
ATOM 4114 C CE  . LYS A 1 558 ? 116.382 142.553 113.757 1.00 58.43  ? 541 LYS A CE  1 
ATOM 4115 N NZ  . LYS A 1 558 ? 115.699 142.227 112.475 1.00 58.43  ? 541 LYS A NZ  1 
ATOM 4116 N N   . LYS A 1 559 ? 116.623 147.135 119.089 1.00 55.28  ? 542 LYS A N   1 
ATOM 4117 C CA  . LYS A 1 559 ? 116.239 147.310 120.481 1.00 55.28  ? 542 LYS A CA  1 
ATOM 4118 C C   . LYS A 1 559 ? 114.736 147.123 120.647 1.00 55.28  ? 542 LYS A C   1 
ATOM 4119 O O   . LYS A 1 559 ? 113.945 147.533 119.792 1.00 55.28  ? 542 LYS A O   1 
ATOM 4120 C CB  . LYS A 1 559 ? 116.666 148.687 120.999 1.00 55.28  ? 542 LYS A CB  1 
ATOM 4121 C CG  . LYS A 1 559 ? 115.835 149.854 120.491 1.00 55.28  ? 542 LYS A CG  1 
ATOM 4122 C CD  . LYS A 1 559 ? 116.682 151.106 120.338 1.00 55.28  ? 542 LYS A CD  1 
ATOM 4123 C CE  . LYS A 1 559 ? 115.908 152.217 119.647 1.00 55.28  ? 542 LYS A CE  1 
ATOM 4124 N NZ  . LYS A 1 559 ? 115.182 151.729 118.443 1.00 55.28  ? 542 LYS A NZ  1 
ATOM 4125 N N   . TYR A 1 560 ? 114.354 146.470 121.741 1.00 51.30  ? 543 TYR A N   1 
ATOM 4126 C CA  . TYR A 1 560 ? 112.958 146.250 122.089 1.00 51.30  ? 543 TYR A CA  1 
ATOM 4127 C C   . TYR A 1 560 ? 112.735 146.682 123.530 1.00 51.30  ? 543 TYR A C   1 
ATOM 4128 O O   . TYR A 1 560 ? 113.510 146.314 124.423 1.00 51.30  ? 543 TYR A O   1 
ATOM 4129 C CB  . TYR A 1 560 ? 112.554 144.783 121.901 1.00 51.30  ? 543 TYR A CB  1 
ATOM 4130 C CG  . TYR A 1 560 ? 112.670 144.285 120.476 1.00 51.30  ? 543 TYR A CG  1 
ATOM 4131 C CD1 . TYR A 1 560 ? 113.900 143.933 119.938 1.00 51.30  ? 543 TYR A CD1 1 
ATOM 4132 C CD2 . TYR A 1 560 ? 111.548 144.176 119.666 1.00 51.30  ? 543 TYR A CD2 1 
ATOM 4133 C CE1 . TYR A 1 560 ? 114.009 143.480 118.637 1.00 51.30  ? 543 TYR A CE1 1 
ATOM 4134 C CE2 . TYR A 1 560 ? 111.648 143.724 118.365 1.00 51.30  ? 543 TYR A CE2 1 
ATOM 4135 C CZ  . TYR A 1 560 ? 112.880 143.377 117.855 1.00 51.30  ? 543 TYR A CZ  1 
ATOM 4136 O OH  . TYR A 1 560 ? 112.983 142.928 116.560 1.00 51.30  ? 543 TYR A OH  1 
ATOM 4137 N N   . GLU A 1 561 ? 111.686 147.472 123.743 1.00 58.78  ? 544 GLU A N   1 
ATOM 4138 C CA  . GLU A 1 561 ? 111.301 147.965 125.057 1.00 58.78  ? 544 GLU A CA  1 
ATOM 4139 C C   . GLU A 1 561 ? 110.042 147.238 125.503 1.00 58.78  ? 544 GLU A C   1 
ATOM 4140 O O   . GLU A 1 561 ? 109.069 147.154 124.746 1.00 58.78  ? 544 GLU A O   1 
ATOM 4141 C CB  . GLU A 1 561 ? 111.059 149.477 125.026 1.00 58.78  ? 544 GLU A CB  1 
ATOM 4142 C CG  . GLU A 1 561 ? 112.124 150.281 124.285 1.00 58.78  ? 544 GLU A CG  1 
ATOM 4143 C CD  . GLU A 1 561 ? 113.397 150.491 125.091 1.00 58.78  ? 544 GLU A CD  1 
ATOM 4144 O OE1 . GLU A 1 561 ? 113.736 149.634 125.934 1.00 58.78  ? 544 GLU A OE1 1 
ATOM 4145 O OE2 . GLU A 1 561 ? 114.064 151.525 124.878 1.00 58.78  ? 544 GLU A OE2 1 
ATOM 4146 N N   . LEU A 1 562 ? 110.061 146.712 126.726 1.00 55.34  ? 545 LEU A N   1 
ATOM 4147 C CA  . LEU A 1 562 ? 108.945 145.909 127.211 1.00 55.34  ? 545 LEU A CA  1 
ATOM 4148 C C   . LEU A 1 562 ? 108.545 146.296 128.628 1.00 55.34  ? 545 LEU A C   1 
ATOM 4149 O O   . LEU A 1 562 ? 109.017 147.302 129.167 1.00 55.34  ? 545 LEU A O   1 
ATOM 4150 C CB  . LEU A 1 562 ? 109.298 144.421 127.158 1.00 55.34  ? 545 LEU A CB  1 
ATOM 4151 C CG  . LEU A 1 562 ? 109.800 143.869 125.823 1.00 55.34  ? 545 LEU A CG  1 
ATOM 4152 C CD1 . LEU A 1 562 ? 110.496 142.534 126.020 1.00 55.34  ? 545 LEU A CD1 1 
ATOM 4153 C CD2 . LEU A 1 562 ? 108.654 143.742 124.834 1.00 55.34  ? 545 LEU A CD2 1 
ATOM 4154 N N   . ASP A 1 563 ? 107.655 145.505 129.228 1.00 62.74  ? 546 ASP A N   1 
ATOM 4155 C CA  . ASP A 1 563 ? 107.284 145.660 130.626 1.00 62.74  ? 546 ASP A CA  1 
ATOM 4156 C C   . ASP A 1 563 ? 107.285 144.348 131.396 1.00 62.74  ? 546 ASP A C   1 
ATOM 4157 O O   . ASP A 1 563 ? 107.104 144.373 132.618 1.00 62.74  ? 546 ASP A O   1 
ATOM 4158 C CB  . ASP A 1 563 ? 105.896 146.309 130.752 1.00 62.74  ? 546 ASP A CB  1 
ATOM 4159 C CG  . ASP A 1 563 ? 105.905 147.780 130.386 1.00 62.74  ? 546 ASP A CG  1 
ATOM 4160 O OD1 . ASP A 1 563 ? 106.898 148.468 130.704 1.00 62.74  ? 546 ASP A OD1 1 
ATOM 4161 O OD2 . ASP A 1 563 ? 104.919 148.250 129.780 1.00 62.74  ? 546 ASP A OD2 1 
ATOM 4162 N N   . LYS A 1 564 ? 107.486 143.215 130.729 1.00 59.46  ? 547 LYS A N   1 
ATOM 4163 C CA  . LYS A 1 564 ? 107.516 141.908 131.365 1.00 59.46  ? 547 LYS A CA  1 
ATOM 4164 C C   . LYS A 1 564 ? 108.853 141.235 131.088 1.00 59.46  ? 547 LYS A C   1 
ATOM 4165 O O   . LYS A 1 564 ? 109.525 141.535 130.096 1.00 59.46  ? 547 LYS A O   1 
ATOM 4166 C CB  . LYS A 1 564 ? 106.373 141.016 130.863 1.00 59.46  ? 547 LYS A CB  1 
ATOM 4167 C CG  . LYS A 1 564 ? 106.518 140.589 129.410 1.00 59.46  ? 547 LYS A CG  1 
ATOM 4168 C CD  . LYS A 1 564 ? 105.654 139.380 129.099 1.00 59.46  ? 547 LYS A CD  1 
ATOM 4169 C CE  . LYS A 1 564 ? 106.033 138.756 127.769 1.00 59.46  ? 547 LYS A CE  1 
ATOM 4170 N NZ  . LYS A 1 564 ? 104.862 138.134 127.094 1.00 59.46  ? 547 LYS A NZ  1 
ATOM 4171 N N   . TYR A 1 565 ? 109.235 140.322 131.976 1.00 49.85  ? 548 TYR A N   1 
ATOM 4172 C CA  . TYR A 1 565 ? 110.504 139.615 131.850 1.00 49.85  ? 548 TYR A CA  1 
ATOM 4173 C C   . TYR A 1 565 ? 110.356 138.462 130.866 1.00 49.85  ? 548 TYR A C   1 
ATOM 4174 O O   . TYR A 1 565 ? 109.556 137.548 131.086 1.00 49.85  ? 548 TYR A O   1 
ATOM 4175 C CB  . TYR A 1 565 ? 110.968 139.102 133.211 1.00 49.85  ? 548 TYR A CB  1 
ATOM 4176 C CG  . TYR A 1 565 ? 111.683 140.129 134.062 1.00 49.85  ? 548 TYR A CG  1 
ATOM 4177 C CD1 . TYR A 1 565 ? 111.370 141.479 133.973 1.00 49.85  ? 548 TYR A CD1 1 
ATOM 4178 C CD2 . TYR A 1 565 ? 112.671 139.746 134.958 1.00 49.85  ? 548 TYR A CD2 1 
ATOM 4179 C CE1 . TYR A 1 565 ? 112.023 142.417 134.751 1.00 49.85  ? 548 TYR A CE1 1 
ATOM 4180 C CE2 . TYR A 1 565 ? 113.328 140.675 135.739 1.00 49.85  ? 548 TYR A CE2 1 
ATOM 4181 C CZ  . TYR A 1 565 ? 113.001 142.008 135.632 1.00 49.85  ? 548 TYR A CZ  1 
ATOM 4182 O OH  . TYR A 1 565 ? 113.655 142.936 136.410 1.00 49.85  ? 548 TYR A OH  1 
ATOM 4183 N N   . THR A 1 566 ? 111.122 138.506 129.780 1.00 49.85  ? 549 THR A N   1 
ATOM 4184 C CA  . THR A 1 566 ? 111.131 137.404 128.833 1.00 49.85  ? 549 THR A CA  1 
ATOM 4185 C C   . THR A 1 566 ? 111.828 136.189 129.438 1.00 49.85  ? 549 THR A C   1 
ATOM 4186 O O   . THR A 1 566 ? 112.572 136.289 130.417 1.00 49.85  ? 549 THR A O   1 
ATOM 4187 C CB  . THR A 1 566 ? 111.832 137.808 127.536 1.00 49.85  ? 549 THR A CB  1 
ATOM 4188 O OG1 . THR A 1 566 ? 113.230 138.000 127.786 1.00 49.85  ? 549 THR A OG1 1 
ATOM 4189 C CG2 . THR A 1 566 ? 111.240 139.095 126.991 1.00 49.85  ? 549 THR A CG2 1 
ATOM 4190 N N   . MET A 1 567 ? 111.572 135.023 128.840 1.00 49.85  ? 550 MET A N   1 
ATOM 4191 C CA  . MET A 1 567 ? 112.256 133.811 129.280 1.00 49.85  ? 550 MET A CA  1 
ATOM 4192 C C   . MET A 1 567 ? 113.761 133.920 129.077 1.00 49.85  ? 550 MET A C   1 
ATOM 4193 O O   . MET A 1 567 ? 114.534 133.270 129.791 1.00 49.85  ? 550 MET A O   1 
ATOM 4194 C CB  . MET A 1 567 ? 111.698 132.592 128.543 1.00 49.85  ? 550 MET A CB  1 
ATOM 4195 C CG  . MET A 1 567 ? 112.442 132.212 127.278 1.00 49.85  ? 550 MET A CG  1 
ATOM 4196 S SD  . MET A 1 567 ? 111.750 130.733 126.519 1.00 49.85  ? 550 MET A SD  1 
ATOM 4197 C CE  . MET A 1 567 ? 110.013 131.158 126.496 1.00 49.85  ? 550 MET A CE  1 
ATOM 4198 N N   . PHE A 1 568 ? 114.194 134.745 128.122 1.00 49.85  ? 551 PHE A N   1 
ATOM 4199 C CA  . PHE A 1 568 ? 115.622 134.943 127.908 1.00 49.85  ? 551 PHE A CA  1 
ATOM 4200 C C   . PHE A 1 568 ? 116.260 135.660 129.090 1.00 49.85  ? 551 PHE A C   1 
ATOM 4201 O O   . PHE A 1 568 ? 117.401 135.363 129.457 1.00 49.85  ? 551 PHE A O   1 
ATOM 4202 C CB  . PHE A 1 568 ? 115.852 135.717 126.611 1.00 49.85  ? 551 PHE A CB  1 
ATOM 4203 C CG  . PHE A 1 568 ? 115.073 135.182 125.444 1.00 49.85  ? 551 PHE A CG  1 
ATOM 4204 C CD1 . PHE A 1 568 ? 115.470 134.021 124.804 1.00 49.85  ? 551 PHE A CD1 1 
ATOM 4205 C CD2 . PHE A 1 568 ? 113.938 135.834 124.993 1.00 49.85  ? 551 PHE A CD2 1 
ATOM 4206 C CE1 . PHE A 1 568 ? 114.754 133.526 123.732 1.00 49.85  ? 551 PHE A CE1 1 
ATOM 4207 C CE2 . PHE A 1 568 ? 113.219 135.343 123.922 1.00 49.85  ? 551 PHE A CE2 1 
ATOM 4208 C CZ  . PHE A 1 568 ? 113.628 134.187 123.291 1.00 49.85  ? 551 PHE A CZ  1 
ATOM 4209 N N   . HIS A 1 569 ? 115.539 136.601 129.705 1.00 52.73  ? 552 HIS A N   1 
ATOM 4210 C CA  . HIS A 1 569 ? 116.062 137.278 130.888 1.00 52.73  ? 552 HIS A CA  1 
ATOM 4211 C C   . HIS A 1 569 ? 116.272 136.297 132.035 1.00 52.73  ? 552 HIS A C   1 
ATOM 4212 O O   . HIS A 1 569 ? 117.315 136.312 132.700 1.00 52.73  ? 552 HIS A O   1 
ATOM 4213 C CB  . HIS A 1 569 ? 115.118 138.403 131.310 1.00 52.73  ? 552 HIS A CB  1 
ATOM 4214 C CG  . HIS A 1 569 ? 115.346 139.691 130.583 1.00 52.73  ? 552 HIS A CG  1 
ATOM 4215 N ND1 . HIS A 1 569 ? 114.745 139.982 129.377 1.00 52.73  ? 552 HIS A ND1 1 
ATOM 4216 C CD2 . HIS A 1 569 ? 116.106 140.768 130.894 1.00 52.73  ? 552 HIS A CD2 1 
ATOM 4217 C CE1 . HIS A 1 569 ? 115.127 141.181 128.976 1.00 52.73  ? 552 HIS A CE1 1 
ATOM 4218 N NE2 . HIS A 1 569 ? 115.953 141.679 129.878 1.00 52.73  ? 552 HIS A NE2 1 
ATOM 4219 N N   . TYR A 1 570 ? 115.288 135.427 132.279 1.00 52.41  ? 553 TYR A N   1 
ATOM 4220 C CA  . TYR A 1 570 ? 115.428 134.440 133.345 1.00 52.41  ? 553 TYR A CA  1 
ATOM 4221 C C   . TYR A 1 570 ? 116.544 133.452 133.033 1.00 52.41  ? 553 TYR A C   1 
ATOM 4222 O O   . TYR A 1 570 ? 117.290 133.046 133.932 1.00 52.41  ? 553 TYR A O   1 
ATOM 4223 C CB  . TYR A 1 570 ? 114.111 133.699 133.568 1.00 52.41  ? 553 TYR A CB  1 
ATOM 4224 C CG  . TYR A 1 570 ? 113.169 134.383 134.533 1.00 52.41  ? 553 TYR A CG  1 
ATOM 4225 C CD1 . TYR A 1 570 ? 112.933 135.748 134.456 1.00 52.41  ? 553 TYR A CD1 1 
ATOM 4226 C CD2 . TYR A 1 570 ? 112.540 133.666 135.542 1.00 52.41  ? 553 TYR A CD2 1 
ATOM 4227 C CE1 . TYR A 1 570 ? 112.073 136.375 135.336 1.00 52.41  ? 553 TYR A CE1 1 
ATOM 4228 C CE2 . TYR A 1 570 ? 111.681 134.286 136.431 1.00 52.41  ? 553 TYR A CE2 1 
ATOM 4229 C CZ  . TYR A 1 570 ? 111.452 135.640 136.324 1.00 52.41  ? 553 TYR A CZ  1 
ATOM 4230 O OH  . TYR A 1 570 ? 110.601 136.263 137.208 1.00 52.41  ? 553 TYR A OH  1 
ATOM 4231 N N   . LEU A 1 571 ? 116.667 133.047 131.767 1.00 49.85  ? 554 LEU A N   1 
ATOM 4232 C CA  . LEU A 1 571 ? 117.746 132.144 131.382 1.00 49.85  ? 554 LEU A CA  1 
ATOM 4233 C C   . LEU A 1 571 ? 119.108 132.789 131.603 1.00 49.85  ? 554 LEU A C   1 
ATOM 4234 O O   . LEU A 1 571 ? 120.042 132.139 132.088 1.00 49.85  ? 554 LEU A O   1 
ATOM 4235 C CB  . LEU A 1 571 ? 117.581 131.729 129.921 1.00 49.85  ? 554 LEU A CB  1 
ATOM 4236 C CG  . LEU A 1 571 ? 117.937 130.284 129.578 1.00 49.85  ? 554 LEU A CG  1 
ATOM 4237 C CD1 . LEU A 1 571 ? 117.012 129.325 130.305 1.00 49.85  ? 554 LEU A CD1 1 
ATOM 4238 C CD2 . LEU A 1 571 ? 117.874 130.064 128.077 1.00 49.85  ? 554 LEU A CD2 1 
ATOM 4239 N N   . ARG A 1 572 ? 119.240 134.071 131.256 1.00 49.85  ? 555 ARG A N   1 
ATOM 4240 C CA  . ARG A 1 572 ? 120.501 134.776 131.455 1.00 49.85  ? 555 ARG A CA  1 
ATOM 4241 C C   . ARG A 1 572 ? 120.803 134.980 132.933 1.00 49.85  ? 555 ARG A C   1 
ATOM 4242 O O   . ARG A 1 572 ? 121.974 134.990 133.329 1.00 49.85  ? 555 ARG A O   1 
ATOM 4243 C CB  . ARG A 1 572 ? 120.463 136.120 130.727 1.00 49.85  ? 555 ARG A CB  1 
ATOM 4244 C CG  . ARG A 1 572 ? 121.724 136.955 130.871 1.00 49.85  ? 555 ARG A CG  1 
ATOM 4245 C CD  . ARG A 1 572 ? 122.907 136.295 130.185 1.00 49.85  ? 555 ARG A CD  1 
ATOM 4246 N NE  . ARG A 1 572 ? 122.508 135.572 128.984 1.00 49.85  ? 555 ARG A NE  1 
ATOM 4247 C CZ  . ARG A 1 572 ? 122.376 136.125 127.787 1.00 49.85  ? 555 ARG A CZ  1 
ATOM 4248 N NH1 . ARG A 1 572 ? 122.595 137.416 127.595 1.00 49.85  ? 555 ARG A NH1 1 
ATOM 4249 N NH2 . ARG A 1 572 ? 122.013 135.366 126.758 1.00 49.85  ? 555 ARG A NH2 1 
ATOM 4250 N N   . ALA A 1 573 ? 119.768 135.138 133.761 1.00 49.85  ? 556 ALA A N   1 
ATOM 4251 C CA  . ALA A 1 573 ? 119.977 135.329 135.190 1.00 49.85  ? 556 ALA A CA  1 
ATOM 4252 C C   . ALA A 1 573 ? 120.566 134.102 135.876 1.00 49.85  ? 556 ALA A C   1 
ATOM 4253 O O   . ALA A 1 573 ? 121.017 134.215 137.020 1.00 49.85  ? 556 ALA A O   1 
ATOM 4254 C CB  . ALA A 1 573 ? 118.660 135.714 135.865 1.00 49.85  ? 556 ALA A CB  1 
ATOM 4255 N N   . GLN A 1 574 ? 120.571 132.943 135.214 1.00 49.85  ? 557 GLN A N   1 
ATOM 4256 C CA  . GLN A 1 574 ? 121.163 131.725 135.753 1.00 49.85  ? 557 GLN A CA  1 
ATOM 4257 C C   . GLN A 1 574 ? 122.553 131.459 135.185 1.00 49.85  ? 557 GLN A C   1 
ATOM 4258 O O   . GLN A 1 574 ? 122.953 130.299 135.043 1.00 49.85  ? 557 GLN A O   1 
ATOM 4259 C CB  . GLN A 1 574 ? 120.250 130.528 135.488 1.00 49.85  ? 557 GLN A CB  1 
ATOM 4260 C CG  . GLN A 1 574 ? 118.872 130.645 136.111 1.00 49.85  ? 557 GLN A CG  1 
ATOM 4261 C CD  . GLN A 1 574 ? 117.886 129.654 135.530 1.00 49.85  ? 557 GLN A CD  1 
ATOM 4262 O OE1 . GLN A 1 574 ? 118.141 128.451 135.503 1.00 49.85  ? 557 GLN A OE1 1 
ATOM 4263 N NE2 . GLN A 1 574 ? 116.750 130.155 135.062 1.00 49.85  ? 557 GLN A NE2 1 
ATOM 4264 N N   . GLU A 1 575 ? 123.297 132.511 134.858 1.00 49.85  ? 558 GLU A N   1 
ATOM 4265 C CA  . GLU A 1 575 ? 124.604 132.389 134.229 1.00 49.85  ? 558 GLU A CA  1 
ATOM 4266 C C   . GLU A 1 575 ? 125.663 133.068 135.085 1.00 49.85  ? 558 GLU A C   1 
ATOM 4267 O O   . GLU A 1 575 ? 125.429 134.144 135.643 1.00 49.85  ? 558 GLU A O   1 
ATOM 4268 C CB  . GLU A 1 575 ? 124.599 133.003 132.825 1.00 49.85  ? 558 GLU A CB  1 
ATOM 4269 C CG  . GLU A 1 575 ? 123.691 132.293 131.835 1.00 49.85  ? 558 GLU A CG  1 
ATOM 4270 C CD  . GLU A 1 575 ? 124.401 131.184 131.083 1.00 49.85  ? 558 GLU A CD  1 
ATOM 4271 O OE1 . GLU A 1 575 ? 124.990 130.300 131.739 1.00 49.85  ? 558 GLU A OE1 1 
ATOM 4272 O OE2 . GLU A 1 575 ? 124.365 131.195 129.835 1.00 49.85  ? 558 GLU A OE2 1 
ATOM 4273 N N   . PHE A 1 576 ? 126.827 132.431 135.182 1.00 56.84  ? 559 PHE A N   1 
ATOM 4274 C CA  . PHE A 1 576 ? 127.970 132.964 135.908 1.00 56.84  ? 559 PHE A CA  1 
ATOM 4275 C C   . PHE A 1 576 ? 129.191 132.936 134.996 1.00 56.84  ? 559 PHE A C   1 
ATOM 4276 O O   . PHE A 1 576 ? 129.134 132.459 133.858 1.00 56.84  ? 559 PHE A O   1 
ATOM 4277 C CB  . PHE A 1 576 ? 128.226 132.188 137.209 1.00 56.84  ? 559 PHE A CB  1 
ATOM 4278 C CG  . PHE A 1 576 ? 128.515 130.724 137.009 1.00 56.84  ? 559 PHE A CG  1 
ATOM 4279 C CD1 . PHE A 1 576 ? 127.517 129.847 136.616 1.00 56.84  ? 559 PHE A CD1 1 
ATOM 4280 C CD2 . PHE A 1 576 ? 129.788 130.225 137.225 1.00 56.84  ? 559 PHE A CD2 1 
ATOM 4281 C CE1 . PHE A 1 576 ? 127.785 128.504 136.437 1.00 56.84  ? 559 PHE A CE1 1 
ATOM 4282 C CE2 . PHE A 1 576 ? 130.062 128.883 137.049 1.00 56.84  ? 559 PHE A CE2 1 
ATOM 4283 C CZ  . PHE A 1 576 ? 129.059 128.022 136.654 1.00 56.84  ? 559 PHE A CZ  1 
ATOM 4284 N N   . GLU A 1 577 ? 130.310 133.456 135.503 1.00 65.97  ? 560 GLU A N   1 
ATOM 4285 C CA  . GLU A 1 577 ? 131.522 133.633 134.710 1.00 65.97  ? 560 GLU A CA  1 
ATOM 4286 C C   . GLU A 1 577 ? 132.697 132.823 135.249 1.00 65.97  ? 560 GLU A C   1 
ATOM 4287 O O   . GLU A 1 577 ? 133.850 133.110 134.908 1.00 65.97  ? 560 GLU A O   1 
ATOM 4288 C CB  . GLU A 1 577 ? 131.891 135.118 134.631 1.00 65.97  ? 560 GLU A CB  1 
ATOM 4289 C CG  . GLU A 1 577 ? 132.497 135.712 135.906 1.00 65.97  ? 560 GLU A CG  1 
ATOM 4290 C CD  . GLU A 1 577 ? 131.550 135.693 137.095 1.00 65.97  ? 560 GLU A CD  1 
ATOM 4291 O OE1 . GLU A 1 577 ? 130.325 135.562 136.889 1.00 65.97  ? 560 GLU A OE1 1 
ATOM 4292 O OE2 . GLU A 1 577 ? 132.035 135.805 138.240 1.00 65.97  ? 560 GLU A OE2 1 
ATOM 4293 N N   . HIS A 1 578 ? 132.427 131.804 136.069 1.00 66.80  ? 561 HIS A N   1 
ATOM 4294 C CA  . HIS A 1 578 ? 133.473 131.005 136.714 1.00 66.80  ? 561 HIS A CA  1 
ATOM 4295 C C   . HIS A 1 578 ? 134.411 131.888 137.534 1.00 66.80  ? 561 HIS A C   1 
ATOM 4296 O O   . HIS A 1 578 ? 135.624 131.673 137.571 1.00 66.80  ? 561 HIS A O   1 
ATOM 4297 C CB  . HIS A 1 578 ? 134.260 130.180 135.692 1.00 66.80  ? 561 HIS A CB  1 
ATOM 4298 C CG  . HIS A 1 578 ? 133.484 129.045 135.102 1.00 66.80  ? 561 HIS A CG  1 
ATOM 4299 N ND1 . HIS A 1 578 ? 133.065 127.963 135.846 1.00 66.80  ? 561 HIS A ND1 1 
ATOM 4300 C CD2 . HIS A 1 578 ? 133.054 128.821 133.837 1.00 66.80  ? 561 HIS A CD2 1 
ATOM 4301 C CE1 . HIS A 1 578 ? 132.410 127.122 135.066 1.00 66.80  ? 561 HIS A CE1 1 
ATOM 4302 N NE2 . HIS A 1 578 ? 132.389 127.619 133.842 1.00 66.80  ? 561 HIS A NE2 1 
ATOM 4303 N N   . GLY A 1 579 ? 133.842 132.893 138.196 1.00 74.65  ? 562 GLY A N   1 
ATOM 4304 C CA  . GLY A 1 579 ? 134.649 133.798 138.988 1.00 74.65  ? 562 GLY A CA  1 
ATOM 4305 C C   . GLY A 1 579 ? 135.213 133.129 140.227 1.00 74.65  ? 562 GLY A C   1 
ATOM 4306 O O   . GLY A 1 579 ? 134.640 132.188 140.777 1.00 74.65  ? 562 GLY A O   1 
ATOM 4307 N N   . LYS A 1 580 ? 136.368 133.631 140.669 1.00 77.03  ? 563 LYS A N   1 
ATOM 4308 C CA  . LYS A 1 580 ? 137.006 133.092 141.864 1.00 77.03  ? 563 LYS A CA  1 
ATOM 4309 C C   . LYS A 1 580 ? 136.274 133.485 143.139 1.00 77.03  ? 563 LYS A C   1 
ATOM 4310 O O   . LYS A 1 580 ? 136.426 132.807 144.160 1.00 77.03  ? 563 LYS A O   1 
ATOM 4311 C CB  . LYS A 1 580 ? 138.464 133.550 141.934 1.00 77.03  ? 563 LYS A CB  1 
ATOM 4312 C CG  . LYS A 1 580 ? 139.263 133.290 140.665 1.00 77.03  ? 563 LYS A CG  1 
ATOM 4313 C CD  . LYS A 1 580 ? 139.063 131.868 140.161 1.00 77.03  ? 563 LYS A CD  1 
ATOM 4314 C CE  . LYS A 1 580 ? 139.461 131.737 138.700 1.00 77.03  ? 563 LYS A CE  1 
ATOM 4315 N NZ  . LYS A 1 580 ? 139.072 130.414 138.137 1.00 77.03  ? 563 LYS A NZ  1 
ATOM 4316 N N   . SER A 1 581 ? 135.490 134.559 143.104 1.00 74.57  ? 564 SER A N   1 
ATOM 4317 C CA  . SER A 1 581 ? 134.714 134.961 144.266 1.00 74.57  ? 564 SER A CA  1 
ATOM 4318 C C   . SER A 1 581 ? 133.566 133.984 144.505 1.00 74.57  ? 564 SER A C   1 
ATOM 4319 O O   . SER A 1 581 ? 133.160 133.228 143.618 1.00 74.57  ? 564 SER A O   1 
ATOM 4320 C CB  . SER A 1 581 ? 134.171 136.379 144.085 1.00 74.57  ? 564 SER A CB  1 
ATOM 4321 O OG  . SER A 1 581 ? 133.329 136.742 145.165 1.00 74.57  ? 564 SER A OG  1 
ATOM 4322 N N   . ARG A 1 582 ? 133.049 134.002 145.731 1.00 65.54  ? 565 ARG A N   1 
ATOM 4323 C CA  . ARG A 1 582 ? 131.975 133.090 146.099 1.00 65.54  ? 565 ARG A CA  1 
ATOM 4324 C C   . ARG A 1 582 ? 130.710 133.399 145.308 1.00 65.54  ? 565 ARG A C   1 
ATOM 4325 O O   . ARG A 1 582 ? 130.330 134.560 145.134 1.00 65.54  ? 565 ARG A O   1 
ATOM 4326 C CB  . ARG A 1 582 ? 131.694 133.178 147.599 1.00 65.54  ? 565 ARG A CB  1 
ATOM 4327 C CG  . ARG A 1 582 ? 131.605 134.592 148.143 1.00 65.54  ? 565 ARG A CG  1 
ATOM 4328 C CD  . ARG A 1 582 ? 130.916 134.604 149.497 1.00 65.54  ? 565 ARG A CD  1 
ATOM 4329 N NE  . ARG A 1 582 ? 129.690 133.816 149.490 1.00 65.54  ? 565 ARG A NE  1 
ATOM 4330 C CZ  . ARG A 1 582 ? 128.998 133.496 150.575 1.00 65.54  ? 565 ARG A CZ  1 
ATOM 4331 N NH1 . ARG A 1 582 ? 129.386 133.881 151.780 1.00 65.54  ? 565 ARG A NH1 1 
ATOM 4332 N NH2 . ARG A 1 582 ? 127.891 132.770 150.449 1.00 65.54  ? 565 ARG A NH2 1 
ATOM 4333 N N   . ILE A 1 583 ? 130.059 132.346 144.824 1.00 51.53  ? 566 ILE A N   1 
ATOM 4334 C CA  . ILE A 1 583 ? 128.825 132.473 144.060 1.00 51.53  ? 566 ILE A CA  1 
ATOM 4335 C C   . ILE A 1 583 ? 127.646 132.266 145.000 1.00 51.53  ? 566 ILE A C   1 
ATOM 4336 O O   . ILE A 1 583 ? 127.594 131.275 145.738 1.00 51.53  ? 566 ILE A O   1 
ATOM 4337 C CB  . ILE A 1 583 ? 128.791 131.464 142.900 1.00 51.53  ? 566 ILE A CB  1 
ATOM 4338 C CG1 . ILE A 1 583 ? 129.978 131.693 141.965 1.00 51.53  ? 566 ILE A CG1 1 
ATOM 4339 C CG2 . ILE A 1 583 ? 127.481 131.574 142.137 1.00 51.53  ? 566 ILE A CG2 1 
ATOM 4340 C CD1 . ILE A 1 583 ? 129.932 130.858 140.707 1.00 51.53  ? 566 ILE A CD1 1 
ATOM 4341 N N   . ALA A 1 584 ? 126.701 133.200 144.978 1.00 54.97  ? 567 ALA A N   1 
ATOM 4342 C CA  . ALA A 1 584 ? 125.539 133.166 145.854 1.00 54.97  ? 567 ALA A CA  1 
ATOM 4343 C C   . ALA A 1 584 ? 124.274 132.983 145.028 1.00 54.97  ? 567 ALA A C   1 
ATOM 4344 O O   . ALA A 1 584 ? 124.075 133.676 144.024 1.00 54.97  ? 567 ALA A O   1 
ATOM 4345 C CB  . ALA A 1 584 ? 125.445 134.445 146.689 1.00 54.97  ? 567 ALA A CB  1 
ATOM 4346 N N   . LEU A 1 585 ? 123.426 132.055 145.455 1.00 49.85  ? 568 LEU A N   1 
ATOM 4347 C CA  . LEU A 1 585 ? 122.161 131.798 144.787 1.00 49.85  ? 568 LEU A CA  1 
ATOM 4348 C C   . LEU A 1 585 ? 121.079 132.723 145.331 1.00 49.85  ? 568 LEU A C   1 
ATOM 4349 O O   . LEU A 1 585 ? 121.112 133.135 146.493 1.00 49.85  ? 568 LEU A O   1 
ATOM 4350 C CB  . LEU A 1 585 ? 121.745 130.338 144.966 1.00 49.85  ? 568 LEU A CB  1 
ATOM 4351 C CG  . LEU A 1 585 ? 122.376 129.332 144.002 1.00 49.85  ? 568 LEU A CG  1 
ATOM 4352 C CD1 . LEU A 1 585 ? 121.500 128.098 143.859 1.00 49.85  ? 568 LEU A CD1 1 
ATOM 4353 C CD2 . LEU A 1 585 ? 122.636 129.966 142.646 1.00 49.85  ? 568 LEU A CD2 1 
ATOM 4354 N N   . THR A 1 586 ? 120.117 133.048 144.471 1.00 49.85  ? 569 THR A N   1 
ATOM 4355 C CA  . THR A 1 586 ? 119.025 133.935 144.847 1.00 49.85  ? 569 THR A CA  1 
ATOM 4356 C C   . THR A 1 586 ? 117.807 133.615 143.994 1.00 49.85  ? 569 THR A C   1 
ATOM 4357 O O   . THR A 1 586 ? 117.901 132.930 142.973 1.00 49.85  ? 569 THR A O   1 
ATOM 4358 C CB  . THR A 1 586 ? 119.412 135.411 144.692 1.00 49.85  ? 569 THR A CB  1 
ATOM 4359 O OG1 . THR A 1 586 ? 118.452 136.232 145.368 1.00 49.85  ? 569 THR A OG1 1 
ATOM 4360 C CG2 . THR A 1 586 ? 119.457 135.798 143.223 1.00 49.85  ? 569 THR A CG2 1 
ATOM 4361 N N   . ASN A 1 587 ? 116.653 134.116 144.434 1.00 49.85  ? 570 ASN A N   1 
ATOM 4362 C CA  . ASN A 1 587 ? 115.395 133.890 143.739 1.00 49.85  ? 570 ASN A CA  1 
ATOM 4363 C C   . ASN A 1 587 ? 114.890 135.111 142.984 1.00 49.85  ? 570 ASN A C   1 
ATOM 4364 O O   . ASN A 1 587 ? 113.950 134.980 142.192 1.00 49.85  ? 570 ASN A O   1 
ATOM 4365 C CB  . ASN A 1 587 ? 114.317 133.426 144.730 1.00 49.85  ? 570 ASN A CB  1 
ATOM 4366 C CG  . ASN A 1 587 ? 114.597 132.046 145.289 1.00 49.85  ? 570 ASN A CG  1 
ATOM 4367 O OD1 . ASN A 1 587 ? 114.780 131.876 146.494 1.00 49.85  ? 570 ASN A OD1 1 
ATOM 4368 N ND2 . ASN A 1 587 ? 114.633 131.049 144.412 1.00 49.85  ? 570 ASN A ND2 1 
ATOM 4369 N N   . SER A 1 588 ? 115.479 136.283 143.201 1.00 54.32  ? 571 SER A N   1 
ATOM 4370 C CA  . SER A 1 588 ? 115.085 137.492 142.492 1.00 54.32  ? 571 SER A CA  1 
ATOM 4371 C C   . SER A 1 588 ? 115.904 137.610 141.213 1.00 54.32  ? 571 SER A C   1 
ATOM 4372 O O   . SER A 1 588 ? 117.133 137.734 141.265 1.00 54.32  ? 571 SER A O   1 
ATOM 4373 C CB  . SER A 1 588 ? 115.277 138.725 143.374 1.00 54.32  ? 571 SER A CB  1 
ATOM 4374 O OG  . SER A 1 588 ? 115.131 139.916 142.622 1.00 54.32  ? 571 SER A OG  1 
ATOM 4375 N N   . VAL A 1 589 ? 115.222 137.568 140.067 1.00 49.85  ? 572 VAL A N   1 
ATOM 4376 C CA  . VAL A 1 589 ? 115.909 137.636 138.781 1.00 49.85  ? 572 VAL A CA  1 
ATOM 4377 C C   . VAL A 1 589 ? 116.572 138.996 138.595 1.00 49.85  ? 572 VAL A C   1 
ATOM 4378 O O   . VAL A 1 589 ? 117.652 139.098 138.000 1.00 49.85  ? 572 VAL A O   1 
ATOM 4379 C CB  . VAL A 1 589 ? 114.925 137.312 137.644 1.00 49.85  ? 572 VAL A CB  1 
ATOM 4380 C CG1 . VAL A 1 589 ? 115.526 137.646 136.288 1.00 49.85  ? 572 VAL A CG1 1 
ATOM 4381 C CG2 . VAL A 1 589 ? 114.546 135.848 137.705 1.00 49.85  ? 572 VAL A CG2 1 
ATOM 4382 N N   . ASN A 1 590 ? 115.940 140.058 139.099 1.00 53.60  ? 573 ASN A N   1 
ATOM 4383 C CA  . ASN A 1 590 ? 116.536 141.387 139.011 1.00 53.60  ? 573 ASN A CA  1 
ATOM 4384 C C   . ASN A 1 590 ? 117.883 141.425 139.725 1.00 53.60  ? 573 ASN A C   1 
ATOM 4385 O O   . ASN A 1 590 ? 118.862 141.974 139.200 1.00 53.60  ? 573 ASN A O   1 
ATOM 4386 C CB  . ASN A 1 590 ? 115.568 142.419 139.597 1.00 53.60  ? 573 ASN A CB  1 
ATOM 4387 C CG  . ASN A 1 590 ? 116.252 143.704 140.033 1.00 53.60  ? 573 ASN A CG  1 
ATOM 4388 O OD1 . ASN A 1 590 ? 117.187 144.179 139.389 1.00 53.60  ? 573 ASN A OD1 1 
ATOM 4389 N ND2 . ASN A 1 590 ? 115.784 144.271 141.138 1.00 53.60  ? 573 ASN A ND2 1 
ATOM 4390 N N   . GLU A 1 591 ? 117.956 140.826 140.917 1.00 49.85  ? 574 GLU A N   1 
ATOM 4391 C CA  . GLU A 1 591 ? 119.215 140.775 141.652 1.00 49.85  ? 574 GLU A CA  1 
ATOM 4392 C C   . GLU A 1 591 ? 120.283 140.020 140.871 1.00 49.85  ? 574 GLU A C   1 
ATOM 4393 O O   . GLU A 1 591 ? 121.445 140.440 140.829 1.00 49.85  ? 574 GLU A O   1 
ATOM 4394 C CB  . GLU A 1 591 ? 118.995 140.125 143.018 1.00 49.85  ? 574 GLU A CB  1 
ATOM 4395 C CG  . GLU A 1 591 ? 120.212 140.147 143.926 1.00 49.85  ? 574 GLU A CG  1 
ATOM 4396 C CD  . GLU A 1 591 ? 119.920 139.576 145.300 1.00 49.85  ? 574 GLU A CD  1 
ATOM 4397 O OE1 . GLU A 1 591 ? 118.769 139.156 145.537 1.00 49.85  ? 574 GLU A OE1 1 
ATOM 4398 O OE2 . GLU A 1 591 ? 120.843 139.545 146.140 1.00 49.85  ? 574 GLU A OE2 1 
ATOM 4399 N N   . ALA A 1 592 ? 119.908 138.900 140.250 1.00 49.85  ? 575 ALA A N   1 
ATOM 4400 C CA  . ALA A 1 592 ? 120.872 138.129 139.472 1.00 49.85  ? 575 ALA A CA  1 
ATOM 4401 C C   . ALA A 1 592 ? 121.372 138.918 138.269 1.00 49.85  ? 575 ALA A C   1 
ATOM 4402 O O   . ALA A 1 592 ? 122.572 138.911 137.967 1.00 49.85  ? 575 ALA A O   1 
ATOM 4403 C CB  . ALA A 1 592 ? 120.249 136.808 139.026 1.00 49.85  ? 575 ALA A CB  1 
ATOM 4404 N N   . LEU A 1 593 ? 120.468 139.603 137.567 1.00 49.85  ? 576 LEU A N   1 
ATOM 4405 C CA  . LEU A 1 593 ? 120.861 140.338 136.371 1.00 49.85  ? 576 LEU A CA  1 
ATOM 4406 C C   . LEU A 1 593 ? 121.648 141.601 136.695 1.00 49.85  ? 576 LEU A C   1 
ATOM 4407 O O   . LEU A 1 593 ? 122.411 142.071 135.844 1.00 49.85  ? 576 LEU A O   1 
ATOM 4408 C CB  . LEU A 1 593 ? 119.627 140.687 135.538 1.00 49.85  ? 576 LEU A CB  1 
ATOM 4409 C CG  . LEU A 1 593 ? 119.036 139.527 134.734 1.00 49.85  ? 576 LEU A CG  1 
ATOM 4410 C CD1 . LEU A 1 593 ? 117.795 139.970 133.978 1.00 49.85  ? 576 LEU A CD1 1 
ATOM 4411 C CD2 . LEU A 1 593 ? 120.069 138.952 133.780 1.00 49.85  ? 576 LEU A CD2 1 
ATOM 4412 N N   . LEU A 1 594 ? 121.485 142.163 137.894 1.00 53.35  ? 577 LEU A N   1 
ATOM 4413 C CA  . LEU A 1 594 ? 122.297 143.316 138.277 1.00 53.35  ? 577 LEU A CA  1 
ATOM 4414 C C   . LEU A 1 594 ? 123.678 142.885 138.759 1.00 53.35  ? 577 LEU A C   1 
ATOM 4415 O O   . LEU A 1 594 ? 124.699 143.260 138.173 1.00 53.35  ? 577 LEU A O   1 
ATOM 4416 C CB  . LEU A 1 594 ? 121.585 144.134 139.358 1.00 53.35  ? 577 LEU A CB  1 
ATOM 4417 C CG  . LEU A 1 594 ? 120.306 144.865 138.953 1.00 53.35  ? 577 LEU A CG  1 
ATOM 4418 C CD1 . LEU A 1 594 ? 119.894 145.848 140.039 1.00 53.35  ? 577 LEU A CD1 1 
ATOM 4419 C CD2 . LEU A 1 594 ? 120.490 145.576 137.622 1.00 53.35  ? 577 LEU A CD2 1 
ATOM 4420 N N   . ASN A 1 595 ? 123.726 142.094 139.828 1.00 53.42  ? 578 ASN A N   1 
ATOM 4421 C CA  . ASN A 1 595 ? 124.989 141.626 140.382 1.00 53.42  ? 578 ASN A CA  1 
ATOM 4422 C C   . ASN A 1 595 ? 125.397 140.341 139.676 1.00 53.42  ? 578 ASN A C   1 
ATOM 4423 O O   . ASN A 1 595 ? 124.689 139.332 139.797 1.00 53.42  ? 578 ASN A O   1 
ATOM 4424 C CB  . ASN A 1 595 ? 124.849 141.386 141.879 1.00 53.42  ? 578 ASN A CB  1 
ATOM 4425 C CG  . ASN A 1 595 ? 126.169 141.065 142.558 1.00 53.42  ? 578 ASN A CG  1 
ATOM 4426 O OD1 . ASN A 1 595 ? 127.224 141.044 141.928 1.00 53.42  ? 578 ASN A OD1 1 
ATOM 4427 N ND2 . ASN A 1 595 ? 126.111 140.814 143.860 1.00 53.42  ? 578 ASN A ND2 1 
ATOM 4428 N N   . PRO A 1 596 ? 126.515 140.319 138.942 1.00 55.73  ? 579 PRO A N   1 
ATOM 4429 C CA  . PRO A 1 596 ? 126.898 139.093 138.228 1.00 55.73  ? 579 PRO A CA  1 
ATOM 4430 C C   . PRO A 1 596 ? 127.439 137.996 139.127 1.00 55.73  ? 579 PRO A C   1 
ATOM 4431 O O   . PRO A 1 596 ? 127.540 136.847 138.674 1.00 55.73  ? 579 PRO A O   1 
ATOM 4432 C CB  . PRO A 1 596 ? 127.969 139.579 137.236 1.00 55.73  ? 579 PRO A CB  1 
ATOM 4433 C CG  . PRO A 1 596 ? 128.388 140.946 137.702 1.00 55.73  ? 579 PRO A CG  1 
ATOM 4434 C CD  . PRO A 1 596 ? 127.568 141.345 138.890 1.00 55.73  ? 579 PRO A CD  1 
ATOM 4435 N N   . SER A 1 597 ? 127.793 138.303 140.376 1.00 54.92  ? 580 SER A N   1 
ATOM 4436 C CA  . SER A 1 597 ? 128.174 137.248 141.308 1.00 54.92  ? 580 SER A CA  1 
ATOM 4437 C C   . SER A 1 597 ? 126.966 136.409 141.707 1.00 54.92  ? 580 SER A C   1 
ATOM 4438 O O   . SER A 1 597 ? 127.067 135.182 141.826 1.00 54.92  ? 580 SER A O   1 
ATOM 4439 C CB  . SER A 1 597 ? 128.843 137.851 142.543 1.00 54.92  ? 580 SER A CB  1 
ATOM 4440 O OG  . SER A 1 597 ? 127.920 138.610 143.303 1.00 54.92  ? 580 SER A OG  1 
ATOM 4441 N N   . ARG A 1 598 ? 125.820 137.050 141.916 1.00 50.33  ? 581 ARG A N   1 
ATOM 4442 C CA  . ARG A 1 598 ? 124.601 136.328 142.247 1.00 50.33  ? 581 ARG A CA  1 
ATOM 4443 C C   . ARG A 1 598 ? 124.073 135.580 141.029 1.00 50.33  ? 581 ARG A C   1 
ATOM 4444 O O   . ARG A 1 598 ? 124.246 136.005 139.884 1.00 50.33  ? 581 ARG A O   1 
ATOM 4445 C CB  . ARG A 1 598 ? 123.534 137.290 142.769 1.00 50.33  ? 581 ARG A CB  1 
ATOM 4446 C CG  . ARG A 1 598 ? 123.952 138.088 143.995 1.00 50.33  ? 581 ARG A CG  1 
ATOM 4447 C CD  . ARG A 1 598 ? 123.623 137.341 145.278 1.00 50.33  ? 581 ARG A CD  1 
ATOM 4448 N NE  . ARG A 1 598 ? 124.106 138.035 146.466 1.00 50.33  ? 581 ARG A NE  1 
ATOM 4449 C CZ  . ARG A 1 598 ? 125.382 138.130 146.819 1.00 50.33  ? 581 ARG A CZ  1 
ATOM 4450 N NH1 . ARG A 1 598 ? 126.343 137.579 146.096 1.00 50.33  ? 581 ARG A NH1 1 
ATOM 4451 N NH2 . ARG A 1 598 ? 125.700 138.791 147.928 1.00 50.33  ? 581 ARG A NH2 1 
ATOM 4452 N N   . VAL A 1 599 ? 123.423 134.448 141.288 1.00 49.85  ? 582 VAL A N   1 
ATOM 4453 C CA  . VAL A 1 599 ? 122.820 133.630 140.242 1.00 49.85  ? 582 VAL A CA  1 
ATOM 4454 C C   . VAL A 1 599 ? 121.393 133.299 140.653 1.00 49.85  ? 582 VAL A C   1 
ATOM 4455 O O   . VAL A 1 599 ? 121.157 132.847 141.778 1.00 49.85  ? 582 VAL A O   1 
ATOM 4456 C CB  . VAL A 1 599 ? 123.625 132.341 139.987 1.00 49.85  ? 582 VAL A CB  1 
ATOM 4457 C CG1 . VAL A 1 599 ? 122.819 131.367 139.141 1.00 49.85  ? 582 VAL A CG1 1 
ATOM 4458 C CG2 . VAL A 1 599 ? 124.947 132.669 139.314 1.00 49.85  ? 582 VAL A CG2 1 
ATOM 4459 N N   . TYR A 1 600 ? 120.446 133.529 139.747 1.00 50.06  ? 583 TYR A N   1 
ATOM 4460 C CA  . TYR A 1 600 ? 119.051 133.236 140.042 1.00 50.06  ? 583 TYR A CA  1 
ATOM 4461 C C   . TYR A 1 600 ? 118.815 131.732 140.072 1.00 50.06  ? 583 TYR A C   1 
ATOM 4462 O O   . TYR A 1 600 ? 119.354 130.985 139.251 1.00 50.06  ? 583 TYR A O   1 
ATOM 4463 C CB  . TYR A 1 600 ? 118.135 133.883 139.005 1.00 50.06  ? 583 TYR A CB  1 
ATOM 4464 C CG  . TYR A 1 600 ? 116.761 133.255 138.931 1.00 50.06  ? 583 TYR A CG  1 
ATOM 4465 C CD1 . TYR A 1 600 ? 115.829 133.460 139.939 1.00 50.06  ? 583 TYR A CD1 1 
ATOM 4466 C CD2 . TYR A 1 600 ? 116.397 132.455 137.855 1.00 50.06  ? 583 TYR A CD2 1 
ATOM 4467 C CE1 . TYR A 1 600 ? 114.573 132.889 139.877 1.00 50.06  ? 583 TYR A CE1 1 
ATOM 4468 C CE2 . TYR A 1 600 ? 115.144 131.879 137.786 1.00 50.06  ? 583 TYR A CE2 1 
ATOM 4469 C CZ  . TYR A 1 600 ? 114.236 132.099 138.800 1.00 50.06  ? 583 TYR A CZ  1 
ATOM 4470 O OH  . TYR A 1 600 ? 112.986 131.529 138.737 1.00 50.06  ? 583 TYR A OH  1 
ATOM 4471 N N   . THR A 1 601 ? 118.005 131.287 141.029 1.00 49.85  ? 584 THR A N   1 
ATOM 4472 C CA  . THR A 1 601 ? 117.605 129.893 141.122 1.00 49.85  ? 584 THR A CA  1 
ATOM 4473 C C   . THR A 1 601 ? 116.102 129.809 141.343 1.00 49.85  ? 584 THR A C   1 
ATOM 4474 O O   . THR A 1 601 ? 115.498 130.685 141.968 1.00 49.85  ? 584 THR A O   1 
ATOM 4475 C CB  . THR A 1 601 ? 118.349 129.157 142.249 1.00 49.85  ? 584 THR A CB  1 
ATOM 4476 O OG1 . THR A 1 601 ? 117.988 127.771 142.239 1.00 49.85  ? 584 THR A OG1 1 
ATOM 4477 C CG2 . THR A 1 601 ? 118.011 129.756 143.602 1.00 49.85  ? 584 THR A CG2 1 
ATOM 4478 N N   . PHE A 1 602 ? 115.501 128.746 140.808 1.00 49.85  ? 585 PHE A N   1 
ATOM 4479 C CA  . PHE A 1 602 ? 114.067 128.515 140.919 1.00 49.85  ? 585 PHE A CA  1 
ATOM 4480 C C   . PHE A 1 602 ? 113.738 127.389 141.893 1.00 49.85  ? 585 PHE A C   1 
ATOM 4481 O O   . PHE A 1 602 ? 112.644 126.818 141.831 1.00 49.85  ? 585 PHE A O   1 
ATOM 4482 C CB  . PHE A 1 602 ? 113.463 128.225 139.543 1.00 49.85  ? 585 PHE A CB  1 
ATOM 4483 C CG  . PHE A 1 602 ? 114.042 127.017 138.861 1.00 49.85  ? 585 PHE A CG  1 
ATOM 4484 C CD1 . PHE A 1 602 ? 115.271 127.081 138.226 1.00 49.85  ? 585 PHE A CD1 1 
ATOM 4485 C CD2 . PHE A 1 602 ? 113.350 125.819 138.847 1.00 49.85  ? 585 PHE A CD2 1 
ATOM 4486 C CE1 . PHE A 1 602 ? 115.800 125.972 137.596 1.00 49.85  ? 585 PHE A CE1 1 
ATOM 4487 C CE2 . PHE A 1 602 ? 113.874 124.707 138.219 1.00 49.85  ? 585 PHE A CE2 1 
ATOM 4488 C CZ  . PHE A 1 602 ? 115.101 124.784 137.593 1.00 49.85  ? 585 PHE A CZ  1 
ATOM 4489 N N   . PHE A 1 603 ? 114.661 127.059 142.789 1.00 49.85  ? 586 PHE A N   1 
ATOM 4490 C CA  . PHE A 1 603 ? 114.431 126.049 143.808 1.00 49.85  ? 586 PHE A CA  1 
ATOM 4491 C C   . PHE A 1 603 ? 113.827 126.683 145.059 1.00 49.85  ? 586 PHE A C   1 
ATOM 4492 O O   . PHE A 1 603 ? 113.684 127.903 145.165 1.00 49.85  ? 586 PHE A O   1 
ATOM 4493 C CB  . PHE A 1 603 ? 115.733 125.325 144.147 1.00 49.85  ? 586 PHE A CB  1 
ATOM 4494 C CG  . PHE A 1 603 ? 116.196 124.375 143.079 1.00 49.85  ? 586 PHE A CG  1 
ATOM 4495 C CD1 . PHE A 1 603 ? 115.335 123.967 142.074 1.00 49.85  ? 586 PHE A CD1 1 
ATOM 4496 C CD2 . PHE A 1 603 ? 117.493 123.892 143.078 1.00 49.85  ? 586 PHE A CD2 1 
ATOM 4497 C CE1 . PHE A 1 603 ? 115.759 123.093 141.091 1.00 49.85  ? 586 PHE A CE1 1 
ATOM 4498 C CE2 . PHE A 1 603 ? 117.923 123.019 142.097 1.00 49.85  ? 586 PHE A CE2 1 
ATOM 4499 C CZ  . PHE A 1 603 ? 117.054 122.620 141.102 1.00 49.85  ? 586 PHE A CZ  1 
ATOM 4500 N N   . SER A 1 604 ? 113.467 125.832 146.015 1.00 55.05  ? 587 SER A N   1 
ATOM 4501 C CA  . SER A 1 604 ? 112.902 126.310 147.266 1.00 55.05  ? 587 SER A CA  1 
ATOM 4502 C C   . SER A 1 604 ? 113.965 127.023 148.098 1.00 55.05  ? 587 SER A C   1 
ATOM 4503 O O   . SER A 1 604 ? 115.170 126.888 147.867 1.00 55.05  ? 587 SER A O   1 
ATOM 4504 C CB  . SER A 1 604 ? 112.302 125.152 148.061 1.00 55.05  ? 587 SER A CB  1 
ATOM 4505 O OG  . SER A 1 604 ? 112.070 125.526 149.408 1.00 55.05  ? 587 SER A OG  1 
ATOM 4506 N N   . SER A 1 605 ? 113.498 127.797 149.081 1.00 55.34  ? 588 SER A N   1 
ATOM 4507 C CA  . SER A 1 605 ? 114.408 128.549 149.938 1.00 55.34  ? 588 SER A CA  1 
ATOM 4508 C C   . SER A 1 605 ? 115.325 127.643 150.748 1.00 55.34  ? 588 SER A C   1 
ATOM 4509 O O   . SER A 1 605 ? 116.401 128.085 151.169 1.00 55.34  ? 588 SER A O   1 
ATOM 4510 C CB  . SER A 1 605 ? 113.616 129.458 150.878 1.00 55.34  ? 588 SER A CB  1 
ATOM 4511 O OG  . SER A 1 605 ? 113.038 128.714 151.936 1.00 55.34  ? 588 SER A OG  1 
ATOM 4512 N N   . ASP A 1 606 ? 114.925 126.390 150.977 1.00 58.93  ? 589 ASP A N   1 
ATOM 4513 C CA  . ASP A 1 606 ? 115.791 125.458 151.691 1.00 58.93  ? 589 ASP A CA  1 
ATOM 4514 C C   . ASP A 1 606 ? 117.085 125.218 150.926 1.00 58.93  ? 589 ASP A C   1 
ATOM 4515 O O   . ASP A 1 606 ? 118.164 125.159 151.524 1.00 58.93  ? 589 ASP A O   1 
ATOM 4516 C CB  . ASP A 1 606 ? 115.059 124.139 151.935 1.00 58.93  ? 589 ASP A CB  1 
ATOM 4517 C CG  . ASP A 1 606 ? 114.203 124.170 153.185 1.00 58.93  ? 589 ASP A CG  1 
ATOM 4518 O OD1 . ASP A 1 606 ? 114.453 125.029 154.057 1.00 58.93  ? 589 ASP A OD1 1 
ATOM 4519 O OD2 . ASP A 1 606 ? 113.283 123.333 153.298 1.00 58.93  ? 589 ASP A OD2 1 
ATOM 4520 N N   . TYR A 1 607 ? 116.996 125.079 149.602 1.00 54.50  ? 590 TYR A N   1 
ATOM 4521 C CA  . TYR A 1 607 ? 118.195 124.888 148.791 1.00 54.50  ? 590 TYR A CA  1 
ATOM 4522 C C   . TYR A 1 607 ? 119.117 126.098 148.881 1.00 54.50  ? 590 TYR A C   1 
ATOM 4523 O O   . TYR A 1 607 ? 120.341 125.951 148.999 1.00 54.50  ? 590 TYR A O   1 
ATOM 4524 C CB  . TYR A 1 607 ? 117.794 124.616 147.341 1.00 54.50  ? 590 TYR A CB  1 
ATOM 4525 C CG  . TYR A 1 607 ? 118.814 123.845 146.535 1.00 54.50  ? 590 TYR A CG  1 
ATOM 4526 C CD1 . TYR A 1 607 ? 120.021 124.421 146.166 1.00 54.50  ? 590 TYR A CD1 1 
ATOM 4527 C CD2 . TYR A 1 607 ? 118.566 122.537 146.139 1.00 54.50  ? 590 TYR A CD2 1 
ATOM 4528 C CE1 . TYR A 1 607 ? 120.950 123.718 145.426 1.00 54.50  ? 590 TYR A CE1 1 
ATOM 4529 C CE2 . TYR A 1 607 ? 119.491 121.827 145.399 1.00 54.50  ? 590 TYR A CE2 1 
ATOM 4530 C CZ  . TYR A 1 607 ? 120.681 122.423 145.047 1.00 54.50  ? 590 TYR A CZ  1 
ATOM 4531 O OH  . TYR A 1 607 ? 121.608 121.722 144.313 1.00 54.50  ? 590 TYR A OH  1 
ATOM 4532 N N   . VAL A 1 608 ? 118.546 127.304 148.831 1.00 55.45  ? 591 VAL A N   1 
ATOM 4533 C CA  . VAL A 1 608 ? 119.349 128.520 148.926 1.00 55.45  ? 591 VAL A CA  1 
ATOM 4534 C C   . VAL A 1 608 ? 120.037 128.599 150.282 1.00 55.45  ? 591 VAL A C   1 
ATOM 4535 O O   . VAL A 1 608 ? 121.225 128.933 150.375 1.00 55.45  ? 591 VAL A O   1 
ATOM 4536 C CB  . VAL A 1 608 ? 118.472 129.758 148.664 1.00 55.45  ? 591 VAL A CB  1 
ATOM 4537 C CG1 . VAL A 1 608 ? 119.228 131.032 149.006 1.00 55.45  ? 591 VAL A CG1 1 
ATOM 4538 C CG2 . VAL A 1 608 ? 118.007 129.779 147.221 1.00 55.45  ? 591 VAL A CG2 1 
ATOM 4539 N N   . LYS A 1 609 ? 119.303 128.291 151.354 1.00 60.27  ? 592 LYS A N   1 
ATOM 4540 C CA  . LYS A 1 609 ? 119.897 128.300 152.687 1.00 60.27  ? 592 LYS A CA  1 
ATOM 4541 C C   . LYS A 1 609 ? 121.022 127.273 152.780 1.00 60.27  ? 592 LYS A C   1 
ATOM 4542 O O   . LYS A 1 609 ? 122.096 127.560 153.322 1.00 60.27  ? 592 LYS A O   1 
ATOM 4543 C CB  . LYS A 1 609 ? 118.810 128.020 153.730 1.00 60.27  ? 592 LYS A CB  1 
ATOM 4544 C CG  . LYS A 1 609 ? 119.207 128.092 155.213 1.00 60.27  ? 592 LYS A CG  1 
ATOM 4545 C CD  . LYS A 1 609 ? 120.444 128.936 155.488 1.00 60.27  ? 592 LYS A CD  1 
ATOM 4546 C CE  . LYS A 1 609 ? 120.491 129.389 156.938 1.00 60.27  ? 592 LYS A CE  1 
ATOM 4547 N NZ  . LYS A 1 609 ? 119.214 130.025 157.360 1.00 60.27  ? 592 LYS A NZ  1 
ATOM 4548 N N   . LYS A 1 610 ? 120.801 126.077 152.230 1.00 57.20  ? 593 LYS A N   1 
ATOM 4549 C CA  . LYS A 1 610 ? 121.793 125.012 152.325 1.00 57.20  ? 593 LYS A CA  1 
ATOM 4550 C C   . LYS A 1 610 ? 123.064 125.361 151.560 1.00 57.20  ? 593 LYS A C   1 
ATOM 4551 O O   . LYS A 1 610 ? 124.171 125.053 152.016 1.00 57.20  ? 593 LYS A O   1 
ATOM 4552 C CB  . LYS A 1 610 ? 121.195 123.701 151.815 1.00 57.20  ? 593 LYS A CB  1 
ATOM 4553 C CG  . LYS A 1 610 ? 120.181 123.083 152.765 1.00 57.20  ? 593 LYS A CG  1 
ATOM 4554 C CD  . LYS A 1 610 ? 120.194 121.568 152.706 1.00 57.20  ? 593 LYS A CD  1 
ATOM 4555 C CE  . LYS A 1 610 ? 120.888 120.971 153.914 1.00 57.20  ? 593 LYS A CE  1 
ATOM 4556 N NZ  . LYS A 1 610 ? 121.076 119.504 153.761 1.00 57.20  ? 593 LYS A NZ  1 
ATOM 4557 N N   . VAL A 1 611 ? 122.931 125.997 150.392 1.00 52.28  ? 594 VAL A N   1 
ATOM 4558 C CA  . VAL A 1 611 ? 124.118 126.355 149.615 1.00 52.28  ? 594 VAL A CA  1 
ATOM 4559 C C   . VAL A 1 611 ? 124.751 127.668 150.044 1.00 52.28  ? 594 VAL A C   1 
ATOM 4560 O O   . VAL A 1 611 ? 125.891 127.946 149.653 1.00 52.28  ? 594 VAL A O   1 
ATOM 4561 C CB  . VAL A 1 611 ? 123.814 126.436 148.108 1.00 52.28  ? 594 VAL A CB  1 
ATOM 4562 C CG1 . VAL A 1 611 ? 123.139 125.165 147.642 1.00 52.28  ? 594 VAL A CG1 1 
ATOM 4563 C CG2 . VAL A 1 611 ? 122.953 127.651 147.801 1.00 52.28  ? 594 VAL A CG2 1 
ATOM 4564 N N   . ASN A 1 612 ? 124.055 128.487 150.832 1.00 64.25  ? 595 ASN A N   1 
ATOM 4565 C CA  . ASN A 1 612 ? 124.586 129.774 151.259 1.00 64.25  ? 595 ASN A CA  1 
ATOM 4566 C C   . ASN A 1 612 ? 125.217 129.739 152.645 1.00 64.25  ? 595 ASN A C   1 
ATOM 4567 O O   . ASN A 1 612 ? 125.649 130.786 153.137 1.00 64.25  ? 595 ASN A O   1 
ATOM 4568 C CB  . ASN A 1 612 ? 123.485 130.838 151.221 1.00 64.25  ? 595 ASN A CB  1 
ATOM 4569 C CG  . ASN A 1 612 ? 123.394 131.533 149.877 1.00 64.25  ? 595 ASN A CG  1 
ATOM 4570 O OD1 . ASN A 1 612 ? 124.257 131.357 149.016 1.00 64.25  ? 595 ASN A OD1 1 
ATOM 4571 N ND2 . ASN A 1 612 ? 122.348 132.328 149.690 1.00 64.25  ? 595 ASN A ND2 1 
ATOM 4572 N N   . LYS A 1 613 ? 125.284 128.574 153.285 1.00 71.53  ? 596 LYS A N   1 
ATOM 4573 C CA  . LYS A 1 613 ? 125.914 128.462 154.590 1.00 71.53  ? 596 LYS A CA  1 
ATOM 4574 C C   . LYS A 1 613 ? 127.405 128.171 154.425 1.00 71.53  ? 596 LYS A C   1 
ATOM 4575 O O   . LYS A 1 613 ? 127.932 128.094 153.313 1.00 71.53  ? 596 LYS A O   1 
ATOM 4576 C CB  . LYS A 1 613 ? 125.221 127.389 155.430 1.00 71.53  ? 596 LYS A CB  1 
ATOM 4577 C CG  . LYS A 1 613 ? 125.323 125.979 154.876 1.00 71.53  ? 596 LYS A CG  1 
ATOM 4578 C CD  . LYS A 1 613 ? 124.704 124.972 155.836 1.00 71.53  ? 596 LYS A CD  1 
ATOM 4579 C CE  . LYS A 1 613 ? 124.617 123.585 155.220 1.00 71.53  ? 596 LYS A CE  1 
ATOM 4580 N NZ  . LYS A 1 613 ? 125.954 123.055 154.839 1.00 71.53  ? 596 LYS A NZ  1 
ATOM 4581 N N   . ALA A 1 614 ? 128.103 128.033 155.551 1.00 82.49  ? 597 ALA A N   1 
ATOM 4582 C CA  . ALA A 1 614 ? 129.531 127.741 155.559 1.00 82.49  ? 597 ALA A CA  1 
ATOM 4583 C C   . ALA A 1 614 ? 129.815 126.649 156.578 1.00 82.49  ? 597 ALA A C   1 
ATOM 4584 O O   . ALA A 1 614 ? 129.292 126.689 157.697 1.00 82.49  ? 597 ALA A O   1 
ATOM 4585 C CB  . ALA A 1 614 ? 130.352 128.994 155.880 1.00 82.49  ? 597 ALA A CB  1 
ATOM 4586 N N   . THR A 1 615 ? 130.642 125.679 156.192 1.00 94.73  ? 598 THR A N   1 
ATOM 4587 C CA  . THR A 1 615 ? 130.996 124.574 157.072 1.00 94.73  ? 598 THR A CA  1 
ATOM 4588 C C   . THR A 1 615 ? 132.413 124.120 156.750 1.00 94.73  ? 598 THR A C   1 
ATOM 4589 O O   . THR A 1 615 ? 132.815 124.100 155.584 1.00 94.73  ? 598 THR A O   1 
ATOM 4590 C CB  . THR A 1 615 ? 130.009 123.407 156.923 1.00 94.73  ? 598 THR A CB  1 
ATOM 4591 O OG1 . THR A 1 615 ? 128.701 123.832 157.327 1.00 94.73  ? 598 THR A OG1 1 
ATOM 4592 C CG2 . THR A 1 615 ? 130.429 122.222 157.776 1.00 94.73  ? 598 THR A CG2 1 
ATOM 4593 N N   . GLU A 1 616 ? 133.162 123.758 157.790 1.00 98.78  ? 599 GLU A N   1 
ATOM 4594 C CA  . GLU A 1 616 ? 134.528 123.287 157.625 1.00 98.78  ? 599 GLU A CA  1 
ATOM 4595 C C   . GLU A 1 616 ? 134.537 121.885 157.015 1.00 98.78  ? 599 GLU A C   1 
ATOM 4596 O O   . GLU A 1 616 ? 133.499 121.314 156.666 1.00 98.78  ? 599 GLU A O   1 
ATOM 4597 C CB  . GLU A 1 616 ? 135.258 123.303 158.966 1.00 98.78  ? 599 GLU A CB  1 
ATOM 4598 C CG  . GLU A 1 616 ? 135.528 124.697 159.514 1.00 98.78  ? 599 GLU A CG  1 
ATOM 4599 C CD  . GLU A 1 616 ? 134.388 125.227 160.363 1.00 98.78  ? 599 GLU A CD  1 
ATOM 4600 O OE1 . GLU A 1 616 ? 133.214 125.025 159.987 1.00 98.78  ? 599 GLU A OE1 1 
ATOM 4601 O OE2 . GLU A 1 616 ? 134.666 125.846 161.411 1.00 98.78  ? 599 GLU A OE2 1 
ATOM 4602 N N   . ALA A 1 617 ? 135.740 121.320 156.891 1.00 98.97  ? 600 ALA A N   1 
ATOM 4603 C CA  . ALA A 1 617 ? 135.914 120.008 156.279 1.00 98.97  ? 600 ALA A CA  1 
ATOM 4604 C C   . ALA A 1 617 ? 135.347 118.875 157.123 1.00 98.97  ? 600 ALA A C   1 
ATOM 4605 O O   . ALA A 1 617 ? 135.265 117.745 156.629 1.00 98.97  ? 600 ALA A O   1 
ATOM 4606 C CB  . ALA A 1 617 ? 137.396 119.748 156.005 1.00 98.97  ? 600 ALA A CB  1 
ATOM 4607 N N   . ALA A 1 618 ? 134.968 119.141 158.375 1.00 95.51  ? 601 ALA A N   1 
ATOM 4608 C CA  . ALA A 1 618 ? 134.422 118.087 159.224 1.00 95.51  ? 601 ALA A CA  1 
ATOM 4609 C C   . ALA A 1 618 ? 133.123 117.532 158.653 1.00 95.51  ? 601 ALA A C   1 
ATOM 4610 O O   . ALA A 1 618 ? 132.899 116.316 158.668 1.00 95.51  ? 601 ALA A O   1 
ATOM 4611 C CB  . ALA A 1 618 ? 134.201 118.615 160.641 1.00 95.51  ? 601 ALA A CB  1 
ATOM 4612 N N   . MET A 1 619 ? 132.190 118.404 158.140 1.00 90.51  ? 602 MET A N   1 
ATOM 4613 C CA  . MET A 1 619 ? 130.892 117.999 157.617 1.00 90.51  ? 602 MET A CA  1 
ATOM 4614 C C   . MET A 1 619 ? 130.755 118.229 156.116 1.00 90.51  ? 602 MET A C   1 
ATOM 4615 O O   . MET A 1 619 ? 129.643 118.149 155.590 1.00 90.51  ? 602 MET A O   1 
ATOM 4616 C CB  . MET A 1 619 ? 129.771 118.723 158.366 1.00 90.51  ? 602 MET A CB  1 
ATOM 4617 C CG  . MET A 1 619 ? 130.150 119.171 159.769 1.00 90.51  ? 602 MET A CG  1 
ATOM 4618 S SD  . MET A 1 619 ? 128.981 120.353 160.466 1.00 90.51  ? 602 MET A SD  1 
ATOM 4619 C CE  . MET A 1 619 ? 129.979 121.100 161.752 1.00 90.51  ? 602 MET A CE  1 
ATOM 4620 N N   . PHE A 1 620 ? 131.853 118.509 155.411 1.00 78.80  ? 603 PHE A N   1 
ATOM 4621 C CA  . PHE A 1 620 ? 131.778 118.653 153.960 1.00 78.80  ? 603 PHE A CA  1 
ATOM 4622 C C   . PHE A 1 620 ? 131.445 117.325 153.288 1.00 78.80  ? 603 PHE A C   1 
ATOM 4623 O O   . PHE A 1 620 ? 130.756 117.298 152.255 1.00 78.80  ? 603 PHE A O   1 
ATOM 4624 C CB  . PHE A 1 620 ? 133.098 119.217 153.432 1.00 78.80  ? 603 PHE A CB  1 
ATOM 4625 C CG  . PHE A 1 620 ? 133.161 119.336 151.938 1.00 78.80  ? 603 PHE A CG  1 
ATOM 4626 C CD1 . PHE A 1 620 ? 132.123 119.913 151.230 1.00 78.80  ? 603 PHE A CD1 1 
ATOM 4627 C CD2 . PHE A 1 620 ? 134.264 118.878 151.242 1.00 78.80  ? 603 PHE A CD2 1 
ATOM 4628 C CE1 . PHE A 1 620 ? 132.183 120.025 149.858 1.00 78.80  ? 603 PHE A CE1 1 
ATOM 4629 C CE2 . PHE A 1 620 ? 134.328 118.986 149.869 1.00 78.80  ? 603 PHE A CE2 1 
ATOM 4630 C CZ  . PHE A 1 620 ? 133.286 119.560 149.176 1.00 78.80  ? 603 PHE A CZ  1 
ATOM 4631 N N   . LEU A 1 621 ? 131.929 116.219 153.860 1.00 80.93  ? 604 LEU A N   1 
ATOM 4632 C CA  . LEU A 1 621 ? 131.596 114.897 153.346 1.00 80.93  ? 604 LEU A CA  1 
ATOM 4633 C C   . LEU A 1 621 ? 130.100 114.634 153.424 1.00 80.93  ? 604 LEU A C   1 
ATOM 4634 O O   . LEU A 1 621 ? 129.555 113.888 152.602 1.00 80.93  ? 604 LEU A O   1 
ATOM 4635 C CB  . LEU A 1 621 ? 132.364 113.827 154.122 1.00 80.93  ? 604 LEU A CB  1 
ATOM 4636 C CG  . LEU A 1 621 ? 133.889 113.933 154.101 1.00 80.93  ? 604 LEU A CG  1 
ATOM 4637 C CD1 . LEU A 1 621 ? 134.502 113.097 155.214 1.00 80.93  ? 604 LEU A CD1 1 
ATOM 4638 C CD2 . LEU A 1 621 ? 134.432 113.509 152.748 1.00 80.93  ? 604 LEU A CD2 1 
ATOM 4639 N N   . GLY A 1 622 ? 129.425 115.212 154.412 1.00 76.90  ? 605 GLY A N   1 
ATOM 4640 C CA  . GLY A 1 622 ? 127.981 115.147 154.467 1.00 76.90  ? 605 GLY A CA  1 
ATOM 4641 C C   . GLY A 1 622 ? 127.347 116.150 153.528 1.00 76.90  ? 605 GLY A C   1 
ATOM 4642 O O   . GLY A 1 622 ? 126.324 115.862 152.903 1.00 76.90  ? 605 GLY A O   1 
ATOM 4643 N N   . TRP A 1 623 ? 127.963 117.331 153.427 1.00 71.53  ? 606 TRP A N   1 
ATOM 4644 C CA  . TRP A 1 623 ? 127.436 118.401 152.586 1.00 71.53  ? 606 TRP A CA  1 
ATOM 4645 C C   . TRP A 1 623 ? 127.263 117.945 151.147 1.00 71.53  ? 606 TRP A C   1 
ATOM 4646 O O   . TRP A 1 623 ? 126.242 118.239 150.513 1.00 71.53  ? 606 TRP A O   1 
ATOM 4647 C CB  . TRP A 1 623 ? 128.372 119.610 152.641 1.00 71.53  ? 606 TRP A CB  1 
ATOM 4648 C CG  . TRP A 1 623 ? 127.795 120.883 152.092 1.00 71.53  ? 606 TRP A CG  1 
ATOM 4649 C CD1 . TRP A 1 623 ? 126.958 121.014 151.025 1.00 71.53  ? 606 TRP A CD1 1 
ATOM 4650 C CD2 . TRP A 1 623 ? 128.059 122.211 152.555 1.00 71.53  ? 606 TRP A CD2 1 
ATOM 4651 N NE1 . TRP A 1 623 ? 126.661 122.334 150.812 1.00 71.53  ? 606 TRP A NE1 1 
ATOM 4652 C CE2 . TRP A 1 623 ? 127.327 123.091 151.737 1.00 71.53  ? 606 TRP A CE2 1 
ATOM 4653 C CE3 . TRP A 1 623 ? 128.834 122.740 153.588 1.00 71.53  ? 606 TRP A CE3 1 
ATOM 4654 C CZ2 . TRP A 1 623 ? 127.347 124.469 151.919 1.00 71.53  ? 606 TRP A CZ2 1 
ATOM 4655 C CZ3 . TRP A 1 623 ? 128.852 124.108 153.766 1.00 71.53  ? 606 TRP A CZ3 1 
ATOM 4656 C CH2 . TRP A 1 623 ? 128.113 124.956 152.938 1.00 71.53  ? 606 TRP A CH2 1 
ATOM 4657 N N   . VAL A 1 624 ? 128.262 117.249 150.605 1.00 71.12  ? 607 VAL A N   1 
ATOM 4658 C CA  . VAL A 1 624 ? 128.200 116.860 149.196 1.00 71.12  ? 607 VAL A CA  1 
ATOM 4659 C C   . VAL A 1 624 ? 126.989 115.965 148.943 1.00 71.12  ? 607 VAL A C   1 
ATOM 4660 O O   . VAL A 1 624 ? 126.230 116.168 147.983 1.00 71.12  ? 607 VAL A O   1 
ATOM 4661 C CB  . VAL A 1 624 ? 129.511 116.182 148.756 1.00 71.12  ? 607 VAL A CB  1 
ATOM 4662 C CG1 . VAL A 1 624 ? 130.569 117.228 148.458 1.00 71.12  ? 607 VAL A CG1 1 
ATOM 4663 C CG2 . VAL A 1 624 ? 130.003 115.220 149.818 1.00 71.12  ? 607 VAL A CG2 1 
ATOM 4664 N N   . GLU A 1 625 ? 126.774 114.975 149.814 1.00 69.04  ? 608 GLU A N   1 
ATOM 4665 C CA  . GLU A 1 625 ? 125.658 114.061 149.598 1.00 69.04  ? 608 GLU A CA  1 
ATOM 4666 C C   . GLU A 1 625 ? 124.317 114.729 149.881 1.00 69.04  ? 608 GLU A C   1 
ATOM 4667 O O   . GLU A 1 625 ? 123.336 114.443 149.186 1.00 69.04  ? 608 GLU A O   1 
ATOM 4668 C CB  . GLU A 1 625 ? 125.837 112.786 150.429 1.00 69.04  ? 608 GLU A CB  1 
ATOM 4669 C CG  . GLU A 1 625 ? 126.079 112.983 151.911 1.00 69.04  ? 608 GLU A CG  1 
ATOM 4670 C CD  . GLU A 1 625 ? 124.795 113.133 152.699 1.00 69.04  ? 608 GLU A CD  1 
ATOM 4671 O OE1 . GLU A 1 625 ? 123.723 112.776 152.166 1.00 69.04  ? 608 GLU A OE1 1 
ATOM 4672 O OE2 . GLU A 1 625 ? 124.857 113.598 153.855 1.00 69.04  ? 608 GLU A OE2 1 
ATOM 4673 N N   . GLN A 1 626 ? 124.251 115.637 150.861 1.00 68.45  ? 609 GLN A N   1 
ATOM 4674 C CA  . GLN A 1 626 ? 123.009 116.382 151.064 1.00 68.45  ? 609 GLN A CA  1 
ATOM 4675 C C   . GLN A 1 626 ? 122.664 117.220 149.841 1.00 68.45  ? 609 GLN A C   1 
ATOM 4676 O O   . GLN A 1 626 ? 121.502 117.266 149.422 1.00 68.45  ? 609 GLN A O   1 
ATOM 4677 C CB  . GLN A 1 626 ? 123.089 117.271 152.306 1.00 68.45  ? 609 GLN A CB  1 
ATOM 4678 C CG  . GLN A 1 626 ? 123.585 116.588 153.560 1.00 68.45  ? 609 GLN A CG  1 
ATOM 4679 C CD  . GLN A 1 626 ? 123.607 117.513 154.761 1.00 68.45  ? 609 GLN A CD  1 
ATOM 4680 O OE1 . GLN A 1 626 ? 122.703 118.325 154.950 1.00 68.45  ? 609 GLN A OE1 1 
ATOM 4681 N NE2 . GLN A 1 626 ? 124.649 117.399 155.577 1.00 68.45  ? 609 GLN A NE2 1 
ATOM 4682 N N   . LEU A 1 627 ? 123.656 117.889 149.252 1.00 61.94  ? 610 LEU A N   1 
ATOM 4683 C CA  . LEU A 1 627 ? 123.381 118.710 148.079 1.00 61.94  ? 610 LEU A CA  1 
ATOM 4684 C C   . LEU A 1 627 ? 122.953 117.862 146.890 1.00 61.94  ? 610 LEU A C   1 
ATOM 4685 O O   . LEU A 1 627 ? 122.006 118.221 146.182 1.00 61.94  ? 610 LEU A O   1 
ATOM 4686 C CB  . LEU A 1 627 ? 124.596 119.559 147.718 1.00 61.94  ? 610 LEU A CB  1 
ATOM 4687 C CG  . LEU A 1 627 ? 124.715 120.879 148.478 1.00 61.94  ? 610 LEU A CG  1 
ATOM 4688 C CD1 . LEU A 1 627 ? 125.617 121.840 147.729 1.00 61.94  ? 610 LEU A CD1 1 
ATOM 4689 C CD2 . LEU A 1 627 ? 123.346 121.495 148.710 1.00 61.94  ? 610 LEU A CD2 1 
ATOM 4690 N N   . VAL A 1 628 ? 123.631 116.735 146.649 1.00 61.94  ? 611 VAL A N   1 
ATOM 4691 C CA  . VAL A 1 628 ? 123.242 115.913 145.505 1.00 61.94  ? 611 VAL A CA  1 
ATOM 4692 C C   . VAL A 1 628 ? 121.849 115.328 145.720 1.00 61.94  ? 611 VAL A C   1 
ATOM 4693 O O   . VAL A 1 628 ? 121.037 115.272 144.788 1.00 61.94  ? 611 VAL A O   1 
ATOM 4694 C CB  . VAL A 1 628 ? 124.296 114.825 145.213 1.00 61.94  ? 611 VAL A CB  1 
ATOM 4695 C CG1 . VAL A 1 628 ? 124.367 113.795 146.319 1.00 61.94  ? 611 VAL A CG1 1 
ATOM 4696 C CG2 . VAL A 1 628 ? 124.005 114.152 143.879 1.00 61.94  ? 611 VAL A CG2 1 
ATOM 4697 N N   . TYR A 1 629 ? 121.515 114.940 146.992 1.00 58.71  ? 612 TYR A N   1 
ATOM 4698 C CA  . TYR A 1 629 ? 120.188 114.405 147.275 1.00 58.71  ? 612 TYR A CA  1 
ATOM 4699 C C   . TYR A 1 629 ? 119.112 115.470 147.100 1.00 58.71  ? 612 TYR A C   1 
ATOM 4700 O O   . TYR A 1 629 ? 118.060 115.204 146.508 1.00 58.71  ? 612 TYR A O   1 
ATOM 4701 C CB  . TYR A 1 629 ? 120.158 113.822 148.689 1.00 58.71  ? 612 TYR A CB  1 
ATOM 4702 C CG  . TYR A 1 629 ? 118.854 114.026 149.425 1.00 58.71  ? 612 TYR A CG  1 
ATOM 4703 C CD1 . TYR A 1 629 ? 117.734 113.262 149.124 1.00 58.71  ? 612 TYR A CD1 1 
ATOM 4704 C CD2 . TYR A 1 629 ? 118.747 114.980 150.428 1.00 58.71  ? 612 TYR A CD2 1 
ATOM 4705 C CE1 . TYR A 1 629 ? 116.542 113.448 149.797 1.00 58.71  ? 612 TYR A CE1 1 
ATOM 4706 C CE2 . TYR A 1 629 ? 117.561 115.172 151.106 1.00 58.71  ? 612 TYR A CE2 1 
ATOM 4707 C CZ  . TYR A 1 629 ? 116.462 114.404 150.787 1.00 58.71  ? 612 TYR A CZ  1 
ATOM 4708 O OH  . TYR A 1 629 ? 115.277 114.592 151.461 1.00 58.71  ? 612 TYR A OH  1 
ATOM 4709 N N   . ASP A 1 630 ? 119.358 116.684 147.601 1.00 59.81  ? 613 ASP A N   1 
ATOM 4710 C CA  . ASP A 1 630 ? 118.376 117.755 147.462 1.00 59.81  ? 613 ASP A CA  1 
ATOM 4711 C C   . ASP A 1 630 ? 118.183 118.150 146.003 1.00 59.81  ? 613 ASP A C   1 
ATOM 4712 O O   . ASP A 1 630 ? 117.052 118.398 145.570 1.00 59.81  ? 613 ASP A O   1 
ATOM 4713 C CB  . ASP A 1 630 ? 118.795 118.967 148.293 1.00 59.81  ? 613 ASP A CB  1 
ATOM 4714 C CG  . ASP A 1 630 ? 118.259 118.914 149.708 1.00 59.81  ? 613 ASP A CG  1 
ATOM 4715 O OD1 . ASP A 1 630 ? 117.241 118.228 149.935 1.00 59.81  ? 613 ASP A OD1 1 
ATOM 4716 O OD2 . ASP A 1 630 ? 118.854 119.560 150.594 1.00 59.81  ? 613 ASP A OD2 1 
ATOM 4717 N N   . PHE A 1 631 ? 119.271 118.227 145.234 1.00 50.72  ? 614 PHE A N   1 
ATOM 4718 C CA  . PHE A 1 631 ? 119.147 118.552 143.817 1.00 50.72  ? 614 PHE A CA  1 
ATOM 4719 C C   . PHE A 1 631 ? 118.370 117.473 143.074 1.00 50.72  ? 614 PHE A C   1 
ATOM 4720 O O   . PHE A 1 631 ? 117.490 117.781 142.261 1.00 50.72  ? 614 PHE A O   1 
ATOM 4721 C CB  . PHE A 1 631 ? 120.534 118.748 143.204 1.00 50.72  ? 614 PHE A CB  1 
ATOM 4722 C CG  . PHE A 1 631 ? 120.514 119.339 141.824 1.00 50.72  ? 614 PHE A CG  1 
ATOM 4723 C CD1 . PHE A 1 631 ? 120.540 120.710 141.640 1.00 50.72  ? 614 PHE A CD1 1 
ATOM 4724 C CD2 . PHE A 1 631 ? 120.465 118.521 140.708 1.00 50.72  ? 614 PHE A CD2 1 
ATOM 4725 C CE1 . PHE A 1 631 ? 120.521 121.253 140.371 1.00 50.72  ? 614 PHE A CE1 1 
ATOM 4726 C CE2 . PHE A 1 631 ? 120.449 119.058 139.440 1.00 50.72  ? 614 PHE A CE2 1 
ATOM 4727 C CZ  . PHE A 1 631 ? 120.475 120.425 139.270 1.00 50.72  ? 614 PHE A CZ  1 
ATOM 4728 N N   . THR A 1 632 ? 118.665 116.201 143.356 1.00 54.57  ? 615 THR A N   1 
ATOM 4729 C CA  . THR A 1 632 ? 117.932 115.117 142.713 1.00 54.57  ? 615 THR A CA  1 
ATOM 4730 C C   . THR A 1 632 ? 116.457 115.150 143.092 1.00 54.57  ? 615 THR A C   1 
ATOM 4731 O O   . THR A 1 632 ? 115.587 114.896 142.251 1.00 54.57  ? 615 THR A O   1 
ATOM 4732 C CB  . THR A 1 632 ? 118.554 113.771 143.086 1.00 54.57  ? 615 THR A CB  1 
ATOM 4733 O OG1 . THR A 1 632 ? 119.962 113.805 142.820 1.00 54.57  ? 615 THR A OG1 1 
ATOM 4734 C CG2 . THR A 1 632 ? 117.922 112.647 142.278 1.00 54.57  ? 615 THR A CG2 1 
ATOM 4735 N N   . ASP A 1 633 ? 116.156 115.467 144.352 1.00 54.16  ? 616 ASP A N   1 
ATOM 4736 C CA  . ASP A 1 633 ? 114.766 115.515 144.794 1.00 54.16  ? 616 ASP A CA  1 
ATOM 4737 C C   . ASP A 1 633 ? 114.012 116.661 144.130 1.00 54.16  ? 616 ASP A C   1 
ATOM 4738 O O   . ASP A 1 633 ? 112.903 116.471 143.617 1.00 54.16  ? 616 ASP A O   1 
ATOM 4739 C CB  . ASP A 1 633 ? 114.708 115.642 146.316 1.00 54.16  ? 616 ASP A CB  1 
ATOM 4740 C CG  . ASP A 1 633 ? 113.390 116.211 146.803 1.00 54.16  ? 616 ASP A CG  1 
ATOM 4741 O OD1 . ASP A 1 633 ? 112.330 115.664 146.433 1.00 54.16  ? 616 ASP A OD1 1 
ATOM 4742 O OD2 . ASP A 1 633 ? 113.414 117.207 147.556 1.00 54.16  ? 616 ASP A OD2 1 
ATOM 4743 N N   . GLU A 1 634 ? 114.597 117.862 144.131 1.00 52.25  ? 617 GLU A N   1 
ATOM 4744 C CA  . GLU A 1 634 ? 113.896 119.021 143.588 1.00 52.25  ? 617 GLU A CA  1 
ATOM 4745 C C   . GLU A 1 634 ? 113.747 118.929 142.076 1.00 52.25  ? 617 GLU A C   1 
ATOM 4746 O O   . GLU A 1 634 ? 112.710 119.317 141.527 1.00 52.25  ? 617 GLU A O   1 
ATOM 4747 C CB  . GLU A 1 634 ? 114.618 120.310 143.978 1.00 52.25  ? 617 GLU A CB  1 
ATOM 4748 C CG  . GLU A 1 634 ? 114.712 120.532 145.475 1.00 52.25  ? 617 GLU A CG  1 
ATOM 4749 C CD  . GLU A 1 634 ? 113.807 121.648 145.951 1.00 52.25  ? 617 GLU A CD  1 
ATOM 4750 O OE1 . GLU A 1 634 ? 112.952 122.096 145.160 1.00 52.25  ? 617 GLU A OE1 1 
ATOM 4751 O OE2 . GLU A 1 634 ? 113.948 122.074 147.116 1.00 52.25  ? 617 GLU A OE2 1 
ATOM 4752 N N   . THR A 1 635 ? 114.767 118.421 141.382 1.00 54.69  ? 618 THR A N   1 
ATOM 4753 C CA  . THR A 1 635 ? 114.657 118.284 139.935 1.00 54.69  ? 618 THR A CA  1 
ATOM 4754 C C   . THR A 1 635 ? 113.676 117.192 139.529 1.00 54.69  ? 618 THR A C   1 
ATOM 4755 O O   . THR A 1 635 ? 113.088 117.278 138.445 1.00 54.69  ? 618 THR A O   1 
ATOM 4756 C CB  . THR A 1 635 ? 116.031 118.007 139.323 1.00 54.69  ? 618 THR A CB  1 
ATOM 4757 O OG1 . THR A 1 635 ? 116.645 116.899 139.994 1.00 54.69  ? 618 THR A OG1 1 
ATOM 4758 C CG2 . THR A 1 635 ? 116.921 119.234 139.441 1.00 54.69  ? 618 THR A CG2 1 
ATOM 4759 N N   . SER A 1 636 ? 113.467 116.185 140.375 1.00 54.09  ? 619 SER A N   1 
ATOM 4760 C CA  . SER A 1 636 ? 112.581 115.072 140.065 1.00 54.09  ? 619 SER A CA  1 
ATOM 4761 C C   . SER A 1 636 ? 111.200 115.225 140.687 1.00 54.09  ? 619 SER A C   1 
ATOM 4762 O O   . SER A 1 636 ? 110.412 114.274 140.657 1.00 54.09  ? 619 SER A O   1 
ATOM 4763 C CB  . SER A 1 636 ? 113.209 113.756 140.523 1.00 54.09  ? 619 SER A CB  1 
ATOM 4764 O OG  . SER A 1 636 ? 114.159 113.299 139.581 1.00 54.09  ? 619 SER A OG  1 
ATOM 4765 N N   . GLU A 1 637 ? 110.889 116.389 141.249 1.00 57.49  ? 620 GLU A N   1 
ATOM 4766 C CA  . GLU A 1 637 ? 109.587 116.591 141.866 1.00 57.49  ? 620 GLU A CA  1 
ATOM 4767 C C   . GLU A 1 637 ? 108.489 116.587 140.807 1.00 57.49  ? 620 GLU A C   1 
ATOM 4768 O O   . GLU A 1 637 ? 108.719 116.906 139.637 1.00 57.49  ? 620 GLU A O   1 
ATOM 4769 C CB  . GLU A 1 637 ? 109.567 117.899 142.657 1.00 57.49  ? 620 GLU A CB  1 
ATOM 4770 C CG  . GLU A 1 637 ? 109.089 119.109 141.876 1.00 57.49  ? 620 GLU A CG  1 
ATOM 4771 C CD  . GLU A 1 637 ? 108.844 120.312 142.764 1.00 57.49  ? 620 GLU A CD  1 
ATOM 4772 O OE1 . GLU A 1 637 ? 109.666 120.559 143.671 1.00 57.49  ? 620 GLU A OE1 1 
ATOM 4773 O OE2 . GLU A 1 637 ? 107.830 121.009 142.558 1.00 57.49  ? 620 GLU A OE2 1 
ATOM 4774 N N   . VAL A 1 638 ? 107.285 116.206 141.229 1.00 58.00  ? 621 VAL A N   1 
ATOM 4775 C CA  . VAL A 1 638 ? 106.162 116.045 140.316 1.00 58.00  ? 621 VAL A CA  1 
ATOM 4776 C C   . VAL A 1 638 ? 104.871 116.299 141.079 1.00 58.00  ? 621 VAL A C   1 
ATOM 4777 O O   . VAL A 1 638 ? 104.806 116.135 142.301 1.00 58.00  ? 621 VAL A O   1 
ATOM 4778 C CB  . VAL A 1 638 ? 106.163 114.641 139.661 1.00 58.00  ? 621 VAL A CB  1 
ATOM 4779 C CG1 . VAL A 1 638 ? 105.476 113.622 140.558 1.00 58.00  ? 621 VAL A CG1 1 
ATOM 4780 C CG2 . VAL A 1 638 ? 105.497 114.687 138.300 1.00 58.00  ? 621 VAL A CG2 1 
ATOM 4781 N N   . SER A 1 639 ? 103.845 116.726 140.349 1.00 64.91  ? 622 SER A N   1 
ATOM 4782 C CA  . SER A 1 639 ? 102.509 116.915 140.896 1.00 64.91  ? 622 SER A CA  1 
ATOM 4783 C C   . SER A 1 639 ? 101.506 116.269 139.953 1.00 64.91  ? 622 SER A C   1 
ATOM 4784 O O   . SER A 1 639 ? 101.533 116.523 138.745 1.00 64.91  ? 622 SER A O   1 
ATOM 4785 C CB  . SER A 1 639 ? 102.190 118.402 141.087 1.00 64.91  ? 622 SER A CB  1 
ATOM 4786 O OG  . SER A 1 639 ? 100.808 118.601 141.325 1.00 64.91  ? 622 SER A OG  1 
ATOM 4787 N N   . THR A 1 640 ? 100.629 115.435 140.504 1.00 78.21  ? 623 THR A N   1 
ATOM 4788 C CA  . THR A 1 640 ? 99.650  114.694 139.720 1.00 78.21  ? 623 THR A CA  1 
ATOM 4789 C C   . THR A 1 640 ? 98.278  115.336 139.873 1.00 78.21  ? 623 THR A C   1 
ATOM 4790 O O   . THR A 1 640 ? 97.853  115.646 140.991 1.00 78.21  ? 623 THR A O   1 
ATOM 4791 C CB  . THR A 1 640 ? 99.596  113.230 140.156 1.00 78.21  ? 623 THR A CB  1 
ATOM 4792 O OG1 . THR A 1 640 ? 98.711  113.096 141.276 1.00 78.21  ? 623 THR A OG1 1 
ATOM 4793 C CG2 . THR A 1 640 ? 100.981 112.742 140.552 1.00 78.21  ? 623 THR A CG2 1 
ATOM 4794 N N   . THR A 1 641 ? 97.591  115.532 138.750 1.00 83.09  ? 624 THR A N   1 
ATOM 4795 C CA  . THR A 1 641 ? 96.270  116.142 138.761 1.00 83.09  ? 624 THR A CA  1 
ATOM 4796 C C   . THR A 1 641 ? 95.460  115.601 137.593 1.00 83.09  ? 624 THR A C   1 
ATOM 4797 O O   . THR A 1 641 ? 96.006  115.067 136.624 1.00 83.09  ? 624 THR A O   1 
ATOM 4798 C CB  . THR A 1 641 ? 96.351  117.672 138.692 1.00 83.09  ? 624 THR A CB  1 
ATOM 4799 O OG1 . THR A 1 641 ? 95.060  118.234 138.956 1.00 83.09  ? 624 THR A OG1 1 
ATOM 4800 C CG2 . THR A 1 641 ? 96.822  118.123 137.317 1.00 83.09  ? 624 THR A CG2 1 
ATOM 4801 N N   . ASP A 1 642 ? 94.136  115.741 137.703 1.00 90.75  ? 625 ASP A N   1 
ATOM 4802 C CA  . ASP A 1 642 ? 93.218  115.316 136.653 1.00 90.75  ? 625 ASP A CA  1 
ATOM 4803 C C   . ASP A 1 642 ? 92.185  116.392 136.337 1.00 90.75  ? 625 ASP A C   1 
ATOM 4804 O O   . ASP A 1 642 ? 91.177  116.104 135.684 1.00 90.75  ? 625 ASP A O   1 
ATOM 4805 C CB  . ASP A 1 642 ? 92.518  114.009 137.037 1.00 90.75  ? 625 ASP A CB  1 
ATOM 4806 C CG  . ASP A 1 642 ? 92.035  114.006 138.474 1.00 90.75  ? 625 ASP A CG  1 
ATOM 4807 O OD1 . ASP A 1 642 ? 91.086  114.756 138.786 1.00 90.75  ? 625 ASP A OD1 1 
ATOM 4808 O OD2 . ASP A 1 642 ? 92.604  113.253 139.292 1.00 90.75  ? 625 ASP A OD2 1 
ATOM 4809 N N   . LYS A 1 643 ? 92.415  117.624 136.788 1.00 82.50  ? 626 LYS A N   1 
ATOM 4810 C CA  . LYS A 1 643 ? 91.502  118.729 136.529 1.00 82.50  ? 626 LYS A CA  1 
ATOM 4811 C C   . LYS A 1 643 ? 91.753  119.402 135.187 1.00 82.50  ? 626 LYS A C   1 
ATOM 4812 O O   . LYS A 1 643 ? 91.024  120.335 134.833 1.00 82.50  ? 626 LYS A O   1 
ATOM 4813 C CB  . LYS A 1 643 ? 91.602  119.762 137.655 1.00 82.50  ? 626 LYS A CB  1 
ATOM 4814 C CG  . LYS A 1 643 ? 91.401  119.175 139.043 1.00 82.50  ? 626 LYS A CG  1 
ATOM 4815 C CD  . LYS A 1 643 ? 92.361  119.785 140.052 1.00 82.50  ? 626 LYS A CD  1 
ATOM 4816 C CE  . LYS A 1 643 ? 92.105  121.271 140.231 1.00 82.50  ? 626 LYS A CE  1 
ATOM 4817 N NZ  . LYS A 1 643 ? 90.875  121.531 141.029 1.00 82.50  ? 626 LYS A NZ  1 
ATOM 4818 N N   . ILE A 1 644 ? 92.760  118.957 134.439 1.00 74.27  ? 627 ILE A N   1 
ATOM 4819 C CA  . ILE A 1 644 ? 93.064  119.478 133.112 1.00 74.27  ? 627 ILE A CA  1 
ATOM 4820 C C   . ILE A 1 644 ? 93.141  118.292 132.159 1.00 74.27  ? 627 ILE A C   1 
ATOM 4821 O O   . ILE A 1 644 ? 93.803  117.292 132.457 1.00 74.27  ? 627 ILE A O   1 
ATOM 4822 C CB  . ILE A 1 644 ? 94.377  120.287 133.107 1.00 74.27  ? 627 ILE A CB  1 
ATOM 4823 C CG1 . ILE A 1 644 ? 94.829  120.624 131.681 1.00 74.27  ? 627 ILE A CG1 1 
ATOM 4824 C CG2 . ILE A 1 644 ? 95.466  119.555 133.883 1.00 74.27  ? 627 ILE A CG2 1 
ATOM 4825 C CD1 . ILE A 1 644 ? 93.779  121.328 130.839 1.00 74.27  ? 627 ILE A CD1 1 
ATOM 4826 N N   . ALA A 1 645 ? 92.454  118.398 131.025 1.00 62.86  ? 628 ALA A N   1 
ATOM 4827 C CA  . ALA A 1 645 ? 92.364  117.282 130.094 1.00 62.86  ? 628 ALA A CA  1 
ATOM 4828 C C   . ALA A 1 645 ? 93.719  116.974 129.469 1.00 62.86  ? 628 ALA A C   1 
ATOM 4829 O O   . ALA A 1 645 ? 94.468  117.878 129.087 1.00 62.86  ? 628 ALA A O   1 
ATOM 4830 C CB  . ALA A 1 645 ? 91.342  117.588 128.999 1.00 62.86  ? 628 ALA A CB  1 
ATOM 4831 N N   . ASP A 1 646 ? 94.033  115.681 129.382 1.00 58.28  ? 629 ASP A N   1 
ATOM 4832 C CA  . ASP A 1 646 ? 95.218  115.143 128.716 1.00 58.28  ? 629 ASP A CA  1 
ATOM 4833 C C   . ASP A 1 646 ? 96.525  115.582 129.368 1.00 58.28  ? 629 ASP A C   1 
ATOM 4834 O O   . ASP A 1 646 ? 97.603  115.301 128.831 1.00 58.28  ? 629 ASP A O   1 
ATOM 4835 C CB  . ASP A 1 646 ? 95.234  115.505 127.224 1.00 58.28  ? 629 ASP A CB  1 
ATOM 4836 C CG  . ASP A 1 646 ? 95.824  114.404 126.362 1.00 58.28  ? 629 ASP A CG  1 
ATOM 4837 O OD1 . ASP A 1 646 ? 96.589  113.572 126.892 1.00 58.28  ? 629 ASP A OD1 1 
ATOM 4838 O OD2 . ASP A 1 646 ? 95.522  114.370 125.151 1.00 58.28  ? 629 ASP A OD2 1 
ATOM 4839 N N   . ILE A 1 647 ? 96.467  116.261 130.507 1.00 54.56  ? 630 ILE A N   1 
ATOM 4840 C CA  . ILE A 1 647 ? 97.660  116.729 131.209 1.00 54.56  ? 630 ILE A CA  1 
ATOM 4841 C C   . ILE A 1 647 ? 97.677  116.025 132.562 1.00 54.56  ? 630 ILE A C   1 
ATOM 4842 O O   . ILE A 1 647 ? 97.070  116.482 133.534 1.00 54.56  ? 630 ILE A O   1 
ATOM 4843 C CB  . ILE A 1 647 ? 97.687  118.252 131.363 1.00 54.56  ? 630 ILE A CB  1 
ATOM 4844 C CG1 . ILE A 1 647 ? 97.694  118.922 129.990 1.00 54.56  ? 630 ILE A CG1 1 
ATOM 4845 C CG2 . ILE A 1 647 ? 98.904  118.687 132.160 1.00 54.56  ? 630 ILE A CG2 1 
ATOM 4846 C CD1 . ILE A 1 647 ? 98.801  118.436 129.089 1.00 54.56  ? 630 ILE A CD1 1 
ATOM 4847 N N   . THR A 1 648 ? 98.375  114.892 132.629 1.00 57.01  ? 631 THR A N   1 
ATOM 4848 C CA  . THR A 1 648 ? 98.498  114.131 133.865 1.00 57.01  ? 631 THR A CA  1 
ATOM 4849 C C   . THR A 1 648 ? 99.697  114.546 134.707 1.00 57.01  ? 631 THR A C   1 
ATOM 4850 O O   . THR A 1 648 ? 99.805  114.110 135.859 1.00 57.01  ? 631 THR A O   1 
ATOM 4851 C CB  . THR A 1 648 ? 98.594  112.633 133.556 1.00 57.01  ? 631 THR A CB  1 
ATOM 4852 O OG1 . THR A 1 648 ? 99.554  112.419 132.514 1.00 57.01  ? 631 THR A OG1 1 
ATOM 4853 C CG2 . THR A 1 648 ? 97.244  112.093 133.111 1.00 57.01  ? 631 THR A CG2 1 
ATOM 4854 N N   . ILE A 1 649 ? 100.591 115.372 134.169 1.00 49.85  ? 632 ILE A N   1 
ATOM 4855 C CA  . ILE A 1 649 ? 101.761 115.861 134.887 1.00 49.85  ? 632 ILE A CA  1 
ATOM 4856 C C   . ILE A 1 649 ? 101.791 117.376 134.755 1.00 49.85  ? 632 ILE A C   1 
ATOM 4857 O O   . ILE A 1 649 ? 101.655 117.908 133.649 1.00 49.85  ? 632 ILE A O   1 
ATOM 4858 C CB  . ILE A 1 649 ? 103.064 115.238 134.352 1.00 49.85  ? 632 ILE A CB  1 
ATOM 4859 C CG1 . ILE A 1 649 ? 103.016 113.715 134.483 1.00 49.85  ? 632 ILE A CG1 1 
ATOM 4860 C CG2 . ILE A 1 649 ? 104.257 115.789 135.093 1.00 49.85  ? 632 ILE A CG2 1 
ATOM 4861 C CD1 . ILE A 1 649 ? 104.183 113.018 133.838 1.00 49.85  ? 632 ILE A CD1 1 
ATOM 4862 N N   . ILE A 1 650 ? 101.932 118.067 135.883 1.00 58.66  ? 633 ILE A N   1 
ATOM 4863 C CA  . ILE A 1 650 ? 101.742 119.513 135.923 1.00 58.66  ? 633 ILE A CA  1 
ATOM 4864 C C   . ILE A 1 650 ? 102.954 120.216 136.539 1.00 58.66  ? 633 ILE A C   1 
ATOM 4865 O O   . ILE A 1 650 ? 102.809 121.204 137.268 1.00 58.66  ? 633 ILE A O   1 
ATOM 4866 C CB  . ILE A 1 650 ? 100.410 119.848 136.629 1.00 58.66  ? 633 ILE A CB  1 
ATOM 4867 C CG1 . ILE A 1 650 ? 99.966  121.275 136.301 1.00 58.66  ? 633 ILE A CG1 1 
ATOM 4868 C CG2 . ILE A 1 650 ? 100.474 119.561 138.132 1.00 58.66  ? 633 ILE A CG2 1 
ATOM 4869 C CD1 . ILE A 1 650 ? 98.507  121.522 136.539 1.00 58.66  ? 633 ILE A CD1 1 
ATOM 4870 N N   . ILE A 1 651 ? 104.153 119.719 136.229 1.00 49.85  ? 634 ILE A N   1 
ATOM 4871 C CA  . ILE A 1 651 ? 105.421 120.075 136.877 1.00 49.85  ? 634 ILE A CA  1 
ATOM 4872 C C   . ILE A 1 651 ? 105.479 121.544 137.283 1.00 49.85  ? 634 ILE A C   1 
ATOM 4873 O O   . ILE A 1 651 ? 105.392 122.434 136.425 1.00 49.85  ? 634 ILE A O   1 
ATOM 4874 C CB  . ILE A 1 651 ? 106.609 119.759 135.954 1.00 49.85  ? 634 ILE A CB  1 
ATOM 4875 C CG1 . ILE A 1 651 ? 106.666 118.268 135.619 1.00 49.85  ? 634 ILE A CG1 1 
ATOM 4876 C CG2 . ILE A 1 651 ? 107.907 120.242 136.572 1.00 49.85  ? 634 ILE A CG2 1 
ATOM 4877 C CD1 . ILE A 1 651 ? 107.320 117.424 136.684 1.00 49.85  ? 634 ILE A CD1 1 
ATOM 4878 N N   . PRO A 1 652 ? 105.627 121.839 138.579 1.00 56.63  ? 635 PRO A N   1 
ATOM 4879 C CA  . PRO A 1 652 ? 105.517 123.242 139.018 1.00 56.63  ? 635 PRO A CA  1 
ATOM 4880 C C   . PRO A 1 652 ? 106.748 124.082 138.727 1.00 56.63  ? 635 PRO A C   1 
ATOM 4881 O O   . PRO A 1 652 ? 106.608 125.263 138.387 1.00 56.63  ? 635 PRO A O   1 
ATOM 4882 C CB  . PRO A 1 652 ? 105.267 123.136 140.531 1.00 56.63  ? 635 PRO A CB  1 
ATOM 4883 C CG  . PRO A 1 652 ? 105.172 121.702 140.863 1.00 56.63  ? 635 PRO A CG  1 
ATOM 4884 C CD  . PRO A 1 652 ? 105.477 120.866 139.673 1.00 56.63  ? 635 PRO A CD  1 
ATOM 4885 N N   . TYR A 1 653 ? 107.955 123.520 138.851 1.00 51.62  ? 636 TYR A N   1 
ATOM 4886 C CA  . TYR A 1 653 ? 109.146 124.363 138.813 1.00 51.62  ? 636 TYR A CA  1 
ATOM 4887 C C   . TYR A 1 653 ? 109.442 124.922 137.427 1.00 51.62  ? 636 TYR A C   1 
ATOM 4888 O O   . TYR A 1 653 ? 110.336 125.765 137.303 1.00 51.62  ? 636 TYR A O   1 
ATOM 4889 C CB  . TYR A 1 653 ? 110.372 123.613 139.351 1.00 51.62  ? 636 TYR A CB  1 
ATOM 4890 C CG  . TYR A 1 653 ? 110.711 122.309 138.665 1.00 51.62  ? 636 TYR A CG  1 
ATOM 4891 C CD1 . TYR A 1 653 ? 111.454 122.288 137.495 1.00 51.62  ? 636 TYR A CD1 1 
ATOM 4892 C CD2 . TYR A 1 653 ? 110.328 121.095 139.216 1.00 51.62  ? 636 TYR A CD2 1 
ATOM 4893 C CE1 . TYR A 1 653 ? 111.779 121.099 136.874 1.00 51.62  ? 636 TYR A CE1 1 
ATOM 4894 C CE2 . TYR A 1 653 ? 110.653 119.898 138.605 1.00 51.62  ? 636 TYR A CE2 1 
ATOM 4895 C CZ  . TYR A 1 653 ? 111.376 119.907 137.433 1.00 51.62  ? 636 TYR A CZ  1 
ATOM 4896 O OH  . TYR A 1 653 ? 111.701 118.721 136.818 1.00 51.62  ? 636 TYR A OH  1 
ATOM 4897 N N   . ILE A 1 654 ? 108.729 124.478 136.390 1.00 49.85  ? 637 ILE A N   1 
ATOM 4898 C CA  . ILE A 1 654 ? 108.830 125.138 135.091 1.00 49.85  ? 637 ILE A CA  1 
ATOM 4899 C C   . ILE A 1 654 ? 108.316 126.569 135.186 1.00 49.85  ? 637 ILE A C   1 
ATOM 4900 O O   . ILE A 1 654 ? 108.843 127.480 134.535 1.00 49.85  ? 637 ILE A O   1 
ATOM 4901 C CB  . ILE A 1 654 ? 108.082 124.324 134.017 1.00 49.85  ? 637 ILE A CB  1 
ATOM 4902 C CG1 . ILE A 1 654 ? 109.011 123.269 133.417 1.00 49.85  ? 637 ILE A CG1 1 
ATOM 4903 C CG2 . ILE A 1 654 ? 107.523 125.225 132.925 1.00 49.85  ? 637 ILE A CG2 1 
ATOM 4904 C CD1 . ILE A 1 654 ? 108.366 122.416 132.360 1.00 49.85  ? 637 ILE A CD1 1 
ATOM 4905 N N   . GLY A 1 655 ? 107.290 126.787 136.009 1.00 51.30  ? 638 GLY A N   1 
ATOM 4906 C CA  . GLY A 1 655 ? 106.689 128.086 136.210 1.00 51.30  ? 638 GLY A CA  1 
ATOM 4907 C C   . GLY A 1 655 ? 107.673 129.228 136.380 1.00 51.30  ? 638 GLY A C   1 
ATOM 4908 O O   . GLY A 1 655 ? 107.708 130.160 135.573 1.00 51.30  ? 638 GLY A O   1 
ATOM 4909 N N   . PRO A 1 656 ? 108.491 129.188 137.437 1.00 49.85  ? 639 PRO A N   1 
ATOM 4910 C CA  . PRO A 1 656 ? 109.472 130.257 137.651 1.00 49.85  ? 639 PRO A CA  1 
ATOM 4911 C C   . PRO A 1 656 ? 110.831 130.033 137.005 1.00 49.85  ? 639 PRO A C   1 
ATOM 4912 O O   . PRO A 1 656 ? 111.665 130.947 137.049 1.00 49.85  ? 639 PRO A O   1 
ATOM 4913 C CB  . PRO A 1 656 ? 109.597 130.296 139.184 1.00 49.85  ? 639 PRO A CB  1 
ATOM 4914 C CG  . PRO A 1 656 ? 109.140 128.928 139.664 1.00 49.85  ? 639 PRO A CG  1 
ATOM 4915 C CD  . PRO A 1 656 ? 108.580 128.165 138.491 1.00 49.85  ? 639 PRO A CD  1 
ATOM 4916 N N   . ALA A 1 657 ? 111.084 128.865 136.410 1.00 49.85  ? 640 ALA A N   1 
ATOM 4917 C CA  . ALA A 1 657 ? 112.376 128.630 135.772 1.00 49.85  ? 640 ALA A CA  1 
ATOM 4918 C C   . ALA A 1 657 ? 112.509 129.447 134.493 1.00 49.85  ? 640 ALA A C   1 
ATOM 4919 O O   . ALA A 1 657 ? 113.390 130.306 134.378 1.00 49.85  ? 640 ALA A O   1 
ATOM 4920 C CB  . ALA A 1 657 ? 112.558 127.140 135.482 1.00 49.85  ? 640 ALA A CB  1 
ATOM 4921 N N   . LEU A 1 658 ? 111.639 129.194 133.519 1.00 49.85  ? 641 LEU A N   1 
ATOM 4922 C CA  . LEU A 1 658 ? 111.616 129.955 132.279 1.00 49.85  ? 641 LEU A CA  1 
ATOM 4923 C C   . LEU A 1 658 ? 110.620 131.105 132.314 1.00 49.85  ? 641 LEU A C   1 
ATOM 4924 O O   . LEU A 1 658 ? 110.479 131.812 131.313 1.00 49.85  ? 641 LEU A O   1 
ATOM 4925 C CB  . LEU A 1 658 ? 111.300 129.033 131.096 1.00 49.85  ? 641 LEU A CB  1 
ATOM 4926 C CG  . LEU A 1 658 ? 111.856 127.611 131.159 1.00 49.85  ? 641 LEU A CG  1 
ATOM 4927 C CD1 . LEU A 1 658 ? 111.412 126.823 129.943 1.00 49.85  ? 641 LEU A CD1 1 
ATOM 4928 C CD2 . LEU A 1 658 ? 113.374 127.632 131.247 1.00 49.85  ? 641 LEU A CD2 1 
ATOM 4929 N N   . ASN A 1 659 ? 109.937 131.305 133.440 1.00 50.30  ? 642 ASN A N   1 
ATOM 4930 C CA  . ASN A 1 659 ? 108.978 132.392 133.620 1.00 50.30  ? 642 ASN A CA  1 
ATOM 4931 C C   . ASN A 1 659 ? 107.934 132.351 132.500 1.00 50.30  ? 642 ASN A C   1 
ATOM 4932 O O   . ASN A 1 659 ? 107.629 133.348 131.842 1.00 50.30  ? 642 ASN A O   1 
ATOM 4933 C CB  . ASN A 1 659 ? 109.709 133.739 133.692 1.00 50.30  ? 642 ASN A CB  1 
ATOM 4934 C CG  . ASN A 1 659 ? 108.775 134.931 133.741 1.00 50.30  ? 642 ASN A CG  1 
ATOM 4935 O OD1 . ASN A 1 659 ? 109.131 136.031 133.322 1.00 50.30  ? 642 ASN A OD1 1 
ATOM 4936 N ND2 . ASN A 1 659 ? 107.592 134.729 134.301 1.00 50.30  ? 642 ASN A ND2 1 
ATOM 4937 N N   . ILE A 1 660 ? 107.406 131.151 132.259 1.00 52.68  ? 643 ILE A N   1 
ATOM 4938 C CA  . ILE A 1 660 ? 106.433 130.971 131.187 1.00 52.68  ? 643 ILE A CA  1 
ATOM 4939 C C   . ILE A 1 660 ? 105.126 131.682 131.519 1.00 52.68  ? 643 ILE A C   1 
ATOM 4940 O O   . ILE A 1 660 ? 104.515 132.323 130.655 1.00 52.68  ? 643 ILE A O   1 
ATOM 4941 C CB  . ILE A 1 660 ? 106.221 129.471 130.911 1.00 52.68  ? 643 ILE A CB  1 
ATOM 4942 C CG1 . ILE A 1 660 ? 107.293 128.956 129.950 1.00 52.68  ? 643 ILE A CG1 1 
ATOM 4943 C CG2 . ILE A 1 660 ? 104.832 129.213 130.351 1.00 52.68  ? 643 ILE A CG2 1 
ATOM 4944 C CD1 . ILE A 1 660 ? 107.116 127.506 129.551 1.00 52.68  ? 643 ILE A CD1 1 
ATOM 4945 N N   . GLY A 1 661 ? 104.685 131.600 132.773 1.00 75.71  ? 644 GLY A N   1 
ATOM 4946 C CA  . GLY A 1 661 ? 103.414 132.165 133.179 1.00 75.71  ? 644 GLY A CA  1 
ATOM 4947 C C   . GLY A 1 661 ? 103.397 133.650 133.461 1.00 75.71  ? 644 GLY A C   1 
ATOM 4948 O O   . GLY A 1 661 ? 102.336 134.181 133.804 1.00 75.71  ? 644 GLY A O   1 
ATOM 4949 N N   . ASN A 1 662 ? 104.539 134.334 133.324 1.00 86.61  ? 645 ASN A N   1 
ATOM 4950 C CA  . ASN A 1 662 ? 104.661 135.761 133.642 1.00 86.61  ? 645 ASN A CA  1 
ATOM 4951 C C   . ASN A 1 662 ? 104.225 136.047 135.074 1.00 86.61  ? 645 ASN A C   1 
ATOM 4952 O O   . ASN A 1 662 ? 103.653 137.098 135.369 1.00 86.61  ? 645 ASN A O   1 
ATOM 4953 C CB  . ASN A 1 662 ? 103.868 136.618 132.651 1.00 86.61  ? 645 ASN A CB  1 
ATOM 4954 C CG  . ASN A 1 662 ? 104.408 138.027 132.535 1.00 86.61  ? 645 ASN A CG  1 
ATOM 4955 O OD1 . ASN A 1 662 ? 105.391 138.389 133.183 1.00 86.61  ? 645 ASN A OD1 1 
ATOM 4956 N ND2 . ASN A 1 662 ? 103.768 138.833 131.698 1.00 86.61  ? 645 ASN A ND2 1 
ATOM 4957 N N   . MET A 1 663 ? 104.512 135.112 135.978 1.00 100.39 ? 646 MET A N   1 
ATOM 4958 C CA  . MET A 1 663 ? 103.849 135.066 137.273 1.00 100.39 ? 646 MET A CA  1 
ATOM 4959 C C   . MET A 1 663 ? 104.667 134.216 138.236 1.00 100.39 ? 646 MET A C   1 
ATOM 4960 O O   . MET A 1 663 ? 105.041 133.088 137.907 1.00 100.39 ? 646 MET A O   1 
ATOM 4961 C CB  . MET A 1 663 ? 102.431 134.532 137.070 1.00 100.39 ? 646 MET A CB  1 
ATOM 4962 C CG  . MET A 1 663 ? 101.718 133.906 138.226 1.00 100.39 ? 646 MET A CG  1 
ATOM 4963 S SD  . MET A 1 663 ? 99.990  133.996 137.722 1.00 100.39 ? 646 MET A SD  1 
ATOM 4964 C CE  . MET A 1 663 ? 99.498  132.290 137.838 1.00 100.39 ? 646 MET A CE  1 
ATOM 4965 N N   . LEU A 1 664 ? 104.934 134.766 139.424 1.00 113.26 ? 647 LEU A N   1 
ATOM 4966 C CA  . LEU A 1 664 ? 106.019 134.264 140.264 1.00 113.26 ? 647 LEU A CA  1 
ATOM 4967 C C   . LEU A 1 664 ? 105.707 132.897 140.862 1.00 113.26 ? 647 LEU A C   1 
ATOM 4968 O O   . LEU A 1 664 ? 106.534 131.979 140.799 1.00 113.26 ? 647 LEU A O   1 
ATOM 4969 C CB  . LEU A 1 664 ? 106.321 135.267 141.378 1.00 113.26 ? 647 LEU A CB  1 
ATOM 4970 N N   . TYR A 1 665 ? 104.530 132.744 141.464 1.00 105.53 ? 648 TYR A N   1 
ATOM 4971 C CA  . TYR A 1 665 ? 104.259 131.554 142.260 1.00 105.53 ? 648 TYR A CA  1 
ATOM 4972 C C   . TYR A 1 665 ? 104.140 130.319 141.376 1.00 105.53 ? 648 TYR A C   1 
ATOM 4973 O O   . TYR A 1 665 ? 103.479 130.346 140.333 1.00 105.53 ? 648 TYR A O   1 
ATOM 4974 C CB  . TYR A 1 665 ? 102.986 131.736 143.085 1.00 105.53 ? 648 TYR A CB  1 
ATOM 4975 C CG  . TYR A 1 665 ? 102.674 133.167 143.444 1.00 105.53 ? 648 TYR A CG  1 
ATOM 4976 C CD1 . TYR A 1 665 ? 103.395 133.825 144.431 1.00 105.53 ? 648 TYR A CD1 1 
ATOM 4977 C CD2 . TYR A 1 665 ? 101.656 133.858 142.804 1.00 105.53 ? 648 TYR A CD2 1 
ATOM 4978 C CE1 . TYR A 1 665 ? 103.116 135.131 144.767 1.00 105.53 ? 648 TYR A CE1 1 
ATOM 4979 C CE2 . TYR A 1 665 ? 101.368 135.165 143.132 1.00 105.53 ? 648 TYR A CE2 1 
ATOM 4980 C CZ  . TYR A 1 665 ? 102.102 135.797 144.115 1.00 105.53 ? 648 TYR A CZ  1 
ATOM 4981 O OH  . TYR A 1 665 ? 101.825 137.101 144.451 1.00 105.53 ? 648 TYR A OH  1 
ATOM 4982 N N   . LYS A 1 666 ? 104.790 129.232 141.800 1.00 90.56  ? 649 LYS A N   1 
ATOM 4983 C CA  . LYS A 1 666 ? 104.713 127.984 141.048 1.00 90.56  ? 649 LYS A CA  1 
ATOM 4984 C C   . LYS A 1 666 ? 103.371 127.292 141.260 1.00 90.56  ? 649 LYS A C   1 
ATOM 4985 O O   . LYS A 1 666 ? 102.809 126.718 140.320 1.00 90.56  ? 649 LYS A O   1 
ATOM 4986 C CB  . LYS A 1 666 ? 105.874 127.065 141.433 1.00 90.56  ? 649 LYS A CB  1 
ATOM 4987 C CG  . LYS A 1 666 ? 105.942 126.694 142.908 1.00 90.56  ? 649 LYS A CG  1 
ATOM 4988 C CD  . LYS A 1 666 ? 107.302 126.105 143.260 1.00 90.56  ? 649 LYS A CD  1 
ATOM 4989 C CE  . LYS A 1 666 ? 107.317 125.513 144.660 1.00 90.56  ? 649 LYS A CE  1 
ATOM 4990 N NZ  . LYS A 1 666 ? 108.639 124.911 144.995 1.00 90.56  ? 649 LYS A NZ  1 
ATOM 4991 N N   . ASP A 1 667 ? 102.841 127.331 142.485 1.00 92.19  ? 650 ASP A N   1 
ATOM 4992 C CA  . ASP A 1 667 ? 101.505 126.792 142.724 1.00 92.19  ? 650 ASP A CA  1 
ATOM 4993 C C   . ASP A 1 667 ? 100.452 127.574 141.955 1.00 92.19  ? 650 ASP A C   1 
ATOM 4994 O O   . ASP A 1 667 ? 99.499  126.990 141.417 1.00 92.19  ? 650 ASP A O   1 
ATOM 4995 C CB  . ASP A 1 667 ? 101.197 126.796 144.220 1.00 92.19  ? 650 ASP A CB  1 
ATOM 4996 C CG  . ASP A 1 667 ? 102.280 126.121 145.038 1.00 92.19  ? 650 ASP A CG  1 
ATOM 4997 O OD1 . ASP A 1 667 ? 102.527 124.916 144.815 1.00 92.19  ? 650 ASP A OD1 1 
ATOM 4998 O OD2 . ASP A 1 667 ? 102.890 126.794 145.895 1.00 92.19  ? 650 ASP A OD2 1 
ATOM 4999 N N   . ASP A 1 668 ? 100.609 128.894 141.879 1.00 92.29  ? 651 ASP A N   1 
ATOM 5000 C CA  . ASP A 1 668 ? 99.724  129.670 141.027 1.00 92.29  ? 651 ASP A CA  1 
ATOM 5001 C C   . ASP A 1 668 ? 99.921  129.307 139.558 1.00 92.29  ? 651 ASP A C   1 
ATOM 5002 O O   . ASP A 1 668 ? 98.981  129.417 138.769 1.00 92.29  ? 651 ASP A O   1 
ATOM 5003 C CB  . ASP A 1 668 ? 99.945  131.163 141.266 1.00 92.29  ? 651 ASP A CB  1 
ATOM 5004 C CG  . ASP A 1 668 ? 98.723  131.994 140.927 1.00 92.29  ? 651 ASP A CG  1 
ATOM 5005 O OD1 . ASP A 1 668 ? 97.732  131.428 140.417 1.00 92.29  ? 651 ASP A OD1 1 
ATOM 5006 O OD2 . ASP A 1 668 ? 98.763  133.222 141.151 1.00 92.29  ? 651 ASP A OD2 1 
ATOM 5007 N N   . PHE A 1 669 ? 101.119 128.847 139.176 1.00 76.35  ? 652 PHE A N   1 
ATOM 5008 C CA  . PHE A 1 669 ? 101.309 128.316 137.826 1.00 76.35  ? 652 PHE A CA  1 
ATOM 5009 C C   . PHE A 1 669 ? 100.519 127.027 137.619 1.00 76.35  ? 652 PHE A C   1 
ATOM 5010 O O   . PHE A 1 669 ? 99.948  126.812 136.544 1.00 76.35  ? 652 PHE A O   1 
ATOM 5011 C CB  . PHE A 1 669 ? 102.792 128.076 137.544 1.00 76.35  ? 652 PHE A CB  1 
ATOM 5012 C CG  . PHE A 1 669 ? 103.054 127.399 136.229 1.00 76.35  ? 652 PHE A CG  1 
ATOM 5013 C CD1 . PHE A 1 669 ? 102.709 128.014 135.039 1.00 76.35  ? 652 PHE A CD1 1 
ATOM 5014 C CD2 . PHE A 1 669 ? 103.618 126.135 136.184 1.00 76.35  ? 652 PHE A CD2 1 
ATOM 5015 C CE1 . PHE A 1 669 ? 102.940 127.394 133.830 1.00 76.35  ? 652 PHE A CE1 1 
ATOM 5016 C CE2 . PHE A 1 669 ? 103.848 125.508 134.975 1.00 76.35  ? 652 PHE A CE2 1 
ATOM 5017 C CZ  . PHE A 1 669 ? 103.508 126.139 133.797 1.00 76.35  ? 652 PHE A CZ  1 
ATOM 5018 N N   . VAL A 1 670 ? 100.493 126.149 138.627 1.00 76.39  ? 653 VAL A N   1 
ATOM 5019 C CA  . VAL A 1 670 ? 99.623  124.972 138.571 1.00 76.39  ? 653 VAL A CA  1 
ATOM 5020 C C   . VAL A 1 670 ? 98.180  125.397 138.337 1.00 76.39  ? 653 VAL A C   1 
ATOM 5021 O O   . VAL A 1 670 ? 97.478  124.846 137.473 1.00 76.39  ? 653 VAL A O   1 
ATOM 5022 C CB  . VAL A 1 670 ? 99.760  124.139 139.861 1.00 76.39  ? 653 VAL A CB  1 
ATOM 5023 C CG1 . VAL A 1 670 ? 99.322  122.710 139.640 1.00 76.39  ? 653 VAL A CG1 1 
ATOM 5024 C CG2 . VAL A 1 670 ? 101.189 124.141 140.334 1.00 76.39  ? 653 VAL A CG2 1 
ATOM 5025 N N   . GLY A 1 671 ? 97.723  126.390 139.101 1.00 77.84  ? 654 GLY A N   1 
ATOM 5026 C CA  . GLY A 1 671 ? 96.363  126.880 138.932 1.00 77.84  ? 654 GLY A CA  1 
ATOM 5027 C C   . GLY A 1 671 ? 96.111  127.459 137.550 1.00 77.84  ? 654 GLY A C   1 
ATOM 5028 O O   . GLY A 1 671 ? 95.078  127.188 136.931 1.00 77.84  ? 654 GLY A O   1 
ATOM 5029 N N   . ALA A 1 672 ? 97.055  128.252 137.043 1.00 74.57  ? 655 ALA A N   1 
ATOM 5030 C CA  . ALA A 1 672 ? 96.896  128.853 135.723 1.00 74.57  ? 655 ALA A CA  1 
ATOM 5031 C C   . ALA A 1 672 ? 96.869  127.792 134.632 1.00 74.57  ? 655 ALA A C   1 
ATOM 5032 O O   . ALA A 1 672 ? 96.130  127.925 133.649 1.00 74.57  ? 655 ALA A O   1 
ATOM 5033 C CB  . ALA A 1 672 ? 98.014  129.861 135.466 1.00 74.57  ? 655 ALA A CB  1 
ATOM 5034 N N   . LEU A 1 673 ? 97.673  126.738 134.777 1.00 68.24  ? 656 LEU A N   1 
ATOM 5035 C CA  . LEU A 1 673 ? 97.661  125.669 133.786 1.00 68.24  ? 656 LEU A CA  1 
ATOM 5036 C C   . LEU A 1 673 ? 96.323  124.941 133.791 1.00 68.24  ? 656 LEU A C   1 
ATOM 5037 O O   . LEU A 1 673 ? 95.691  124.785 132.740 1.00 68.24  ? 656 LEU A O   1 
ATOM 5038 C CB  . LEU A 1 673 ? 98.819  124.700 134.029 1.00 68.24  ? 656 LEU A CB  1 
ATOM 5039 C CG  . LEU A 1 673 ? 98.946  123.564 133.010 1.00 68.24  ? 656 LEU A CG  1 
ATOM 5040 C CD1 . LEU A 1 673 ? 98.894  124.114 131.604 1.00 68.24  ? 656 LEU A CD1 1 
ATOM 5041 C CD2 . LEU A 1 673 ? 100.244 122.810 133.205 1.00 68.24  ? 656 LEU A CD2 1 
ATOM 5042 N N   . ILE A 1 674 ? 95.850  124.523 134.972 1.00 70.18  ? 657 ILE A N   1 
ATOM 5043 C CA  . ILE A 1 674 ? 94.552  123.848 135.007 1.00 70.18  ? 657 ILE A CA  1 
ATOM 5044 C C   . ILE A 1 674 ? 93.424  124.784 134.591 1.00 70.18  ? 657 ILE A C   1 
ATOM 5045 O O   . ILE A 1 674 ? 92.342  124.317 134.218 1.00 70.18  ? 657 ILE A O   1 
ATOM 5046 C CB  . ILE A 1 674 ? 94.229  123.240 136.388 1.00 70.18  ? 657 ILE A CB  1 
ATOM 5047 C CG1 . ILE A 1 674 ? 94.449  124.255 137.508 1.00 70.18  ? 657 ILE A CG1 1 
ATOM 5048 C CG2 . ILE A 1 674 ? 95.022  121.965 136.616 1.00 70.18  ? 657 ILE A CG2 1 
ATOM 5049 C CD1 . ILE A 1 674 ? 94.507  123.646 138.892 1.00 70.18  ? 657 ILE A CD1 1 
ATOM 5050 N N   . PHE A 1 675 ? 93.646  126.098 134.644 1.00 70.48  ? 658 PHE A N   1 
ATOM 5051 C CA  . PHE A 1 675 ? 92.622  127.041 134.213 1.00 70.48  ? 658 PHE A CA  1 
ATOM 5052 C C   . PHE A 1 675 ? 92.595  127.195 132.695 1.00 70.48  ? 658 PHE A C   1 
ATOM 5053 O O   . PHE A 1 675 ? 91.525  127.139 132.080 1.00 70.48  ? 658 PHE A O   1 
ATOM 5054 C CB  . PHE A 1 675 ? 92.853  128.397 134.885 1.00 70.48  ? 658 PHE A CB  1 
ATOM 5055 C CG  . PHE A 1 675 ? 91.816  129.433 134.547 1.00 70.48  ? 658 PHE A CG  1 
ATOM 5056 C CD1 . PHE A 1 675 ? 90.492  129.076 134.347 1.00 70.48  ? 658 PHE A CD1 1 
ATOM 5057 C CD2 . PHE A 1 675 ? 92.170  130.766 134.424 1.00 70.48  ? 658 PHE A CD2 1 
ATOM 5058 C CE1 . PHE A 1 675 ? 89.542  130.030 134.035 1.00 70.48  ? 658 PHE A CE1 1 
ATOM 5059 C CE2 . PHE A 1 675 ? 91.225  131.724 134.112 1.00 70.48  ? 658 PHE A CE2 1 
ATOM 5060 C CZ  . PHE A 1 675 ? 89.909  131.356 133.917 1.00 70.48  ? 658 PHE A CZ  1 
ATOM 5061 N N   . SER A 1 676 ? 93.761  127.385 132.070 1.00 61.07  ? 659 SER A N   1 
ATOM 5062 C CA  . SER A 1 676 ? 93.815  127.858 130.689 1.00 61.07  ? 659 SER A CA  1 
ATOM 5063 C C   . SER A 1 676 ? 94.492  126.882 129.729 1.00 61.07  ? 659 SER A C   1 
ATOM 5064 O O   . SER A 1 676 ? 94.814  127.269 128.602 1.00 61.07  ? 659 SER A O   1 
ATOM 5065 C CB  . SER A 1 676 ? 94.515  129.217 130.627 1.00 61.07  ? 659 SER A CB  1 
ATOM 5066 O OG  . SER A 1 676 ? 93.799  130.192 131.364 1.00 61.07  ? 659 SER A OG  1 
ATOM 5067 N N   . GLY A 1 677 ? 94.710  125.628 130.129 1.00 51.80  ? 660 GLY A N   1 
ATOM 5068 C CA  . GLY A 1 677 ? 95.253  124.705 129.150 1.00 51.80  ? 660 GLY A CA  1 
ATOM 5069 C C   . GLY A 1 677 ? 96.696  125.022 128.778 1.00 51.80  ? 660 GLY A C   1 
ATOM 5070 O O   . GLY A 1 677 ? 97.392  125.796 129.439 1.00 51.80  ? 660 GLY A O   1 
ATOM 5071 N N   . ALA A 1 678 ? 97.133  124.424 127.669 1.00 49.85  ? 661 ALA A N   1 
ATOM 5072 C CA  . ALA A 1 678 ? 98.508  124.536 127.202 1.00 49.85  ? 661 ALA A CA  1 
ATOM 5073 C C   . ALA A 1 678 ? 98.777  125.834 126.444 1.00 49.85  ? 661 ALA A C   1 
ATOM 5074 O O   . ALA A 1 678 ? 99.794  125.936 125.750 1.00 49.85  ? 661 ALA A O   1 
ATOM 5075 C CB  . ALA A 1 678 ? 98.865  123.335 126.324 1.00 49.85  ? 661 ALA A CB  1 
ATOM 5076 N N   . VAL A 1 679 ? 97.887  126.822 126.559 1.00 49.85  ? 662 VAL A N   1 
ATOM 5077 C CA  . VAL A 1 679 ? 98.108  128.108 125.904 1.00 49.85  ? 662 VAL A CA  1 
ATOM 5078 C C   . VAL A 1 679 ? 99.281  128.847 126.540 1.00 49.85  ? 662 VAL A C   1 
ATOM 5079 O O   . VAL A 1 679 ? 100.035 129.544 125.848 1.00 49.85  ? 662 VAL A O   1 
ATOM 5080 C CB  . VAL A 1 679 ? 96.813  128.943 125.945 1.00 49.85  ? 662 VAL A CB  1 
ATOM 5081 C CG1 . VAL A 1 679 ? 97.109  130.431 125.806 1.00 49.85  ? 662 VAL A CG1 1 
ATOM 5082 C CG2 . VAL A 1 679 ? 95.851  128.484 124.859 1.00 49.85  ? 662 VAL A CG2 1 
ATOM 5083 N N   . ILE A 1 680 ? 99.470  128.689 127.853 1.00 49.85  ? 663 ILE A N   1 
ATOM 5084 C CA  . ILE A 1 680 ? 100.447 129.494 128.583 1.00 49.85  ? 663 ILE A CA  1 
ATOM 5085 C C   . ILE A 1 680 ? 101.859 129.251 128.063 1.00 49.85  ? 663 ILE A C   1 
ATOM 5086 O O   . ILE A 1 680 ? 102.678 130.177 128.000 1.00 49.85  ? 663 ILE A O   1 
ATOM 5087 C CB  . ILE A 1 680 ? 100.347 129.209 130.093 1.00 49.85  ? 663 ILE A CB  1 
ATOM 5088 C CG1 . ILE A 1 680 ? 98.888  129.240 130.546 1.00 49.85  ? 663 ILE A CG1 1 
ATOM 5089 C CG2 . ILE A 1 680 ? 101.167 130.217 130.881 1.00 49.85  ? 663 ILE A CG2 1 
ATOM 5090 C CD1 . ILE A 1 680 ? 98.233  130.596 130.405 1.00 49.85  ? 663 ILE A CD1 1 
ATOM 5091 N N   . LEU A 1 681 ? 102.172 128.007 127.691 1.00 49.85  ? 664 LEU A N   1 
ATOM 5092 C CA  . LEU A 1 681 ? 103.533 127.685 127.269 1.00 49.85  ? 664 LEU A CA  1 
ATOM 5093 C C   . LEU A 1 681 ? 103.933 128.457 126.017 1.00 49.85  ? 664 LEU A C   1 
ATOM 5094 O O   . LEU A 1 681 ? 105.052 128.977 125.933 1.00 49.85  ? 664 LEU A O   1 
ATOM 5095 C CB  . LEU A 1 681 ? 103.674 126.181 127.032 1.00 49.85  ? 664 LEU A CB  1 
ATOM 5096 C CG  . LEU A 1 681 ? 103.306 125.248 128.184 1.00 49.85  ? 664 LEU A CG  1 
ATOM 5097 C CD1 . LEU A 1 681 ? 103.798 123.845 127.888 1.00 49.85  ? 664 LEU A CD1 1 
ATOM 5098 C CD2 . LEU A 1 681 ? 103.880 125.749 129.497 1.00 49.85  ? 664 LEU A CD2 1 
ATOM 5099 N N   . LEU A 1 682 ? 103.038 128.545 125.038 1.00 49.85  ? 665 LEU A N   1 
ATOM 5100 C CA  . LEU A 1 682 ? 103.370 129.196 123.778 1.00 49.85  ? 665 LEU A CA  1 
ATOM 5101 C C   . LEU A 1 682 ? 103.591 130.689 123.989 1.00 49.85  ? 665 LEU A C   1 
ATOM 5102 O O   . LEU A 1 682 ? 102.776 131.365 124.623 1.00 49.85  ? 665 LEU A O   1 
ATOM 5103 C CB  . LEU A 1 682 ? 102.260 128.967 122.756 1.00 49.85  ? 665 LEU A CB  1 
ATOM 5104 C CG  . LEU A 1 682 ? 101.665 127.559 122.709 1.00 49.85  ? 665 LEU A CG  1 
ATOM 5105 C CD1 . LEU A 1 682 ? 100.511 127.514 121.730 1.00 49.85  ? 665 LEU A CD1 1 
ATOM 5106 C CD2 . LEU A 1 682 ? 102.724 126.535 122.339 1.00 49.85  ? 665 LEU A CD2 1 
ATOM 5107 N N   . GLU A 1 683 ? 104.703 131.200 123.456 1.00 49.85  ? 666 GLU A N   1 
ATOM 5108 C CA  . GLU A 1 683 ? 104.994 132.626 123.577 1.00 49.85  ? 666 GLU A CA  1 
ATOM 5109 C C   . GLU A 1 683 ? 104.016 133.460 122.760 1.00 49.85  ? 666 GLU A C   1 
ATOM 5110 O O   . GLU A 1 683 ? 103.537 134.500 123.227 1.00 49.85  ? 666 GLU A O   1 
ATOM 5111 C CB  . GLU A 1 683 ? 106.434 132.905 123.146 1.00 49.85  ? 666 GLU A CB  1 
ATOM 5112 C CG  . GLU A 1 683 ? 107.107 134.051 123.892 1.00 49.85  ? 666 GLU A CG  1 
ATOM 5113 C CD  . GLU A 1 683 ? 107.453 133.709 125.331 1.00 49.85  ? 666 GLU A CD  1 
ATOM 5114 O OE1 . GLU A 1 683 ? 107.201 132.564 125.760 1.00 49.85  ? 666 GLU A OE1 1 
ATOM 5115 O OE2 . GLU A 1 683 ? 107.983 134.591 126.037 1.00 49.85  ? 666 GLU A OE2 1 
ATOM 5116 N N   . PHE A 1 684 ? 103.710 133.024 121.540 1.00 49.85  ? 667 PHE A N   1 
ATOM 5117 C CA  . PHE A 1 684 ? 102.749 133.698 120.679 1.00 49.85  ? 667 PHE A CA  1 
ATOM 5118 C C   . PHE A 1 684 ? 101.701 132.689 120.240 1.00 49.85  ? 667 PHE A C   1 
ATOM 5119 O O   . PHE A 1 684 ? 102.042 131.582 119.811 1.00 49.85  ? 667 PHE A O   1 
ATOM 5120 C CB  . PHE A 1 684 ? 103.431 134.333 119.460 1.00 49.85  ? 667 PHE A CB  1 
ATOM 5121 C CG  . PHE A 1 684 ? 104.138 133.346 118.571 1.00 49.85  ? 667 PHE A CG  1 
ATOM 5122 C CD1 . PHE A 1 684 ? 105.396 132.869 118.901 1.00 49.85  ? 667 PHE A CD1 1 
ATOM 5123 C CD2 . PHE A 1 684 ? 103.547 132.903 117.399 1.00 49.85  ? 667 PHE A CD2 1 
ATOM 5124 C CE1 . PHE A 1 684 ? 106.045 131.964 118.085 1.00 49.85  ? 667 PHE A CE1 1 
ATOM 5125 C CE2 . PHE A 1 684 ? 104.193 131.999 116.579 1.00 49.85  ? 667 PHE A CE2 1 
ATOM 5126 C CZ  . PHE A 1 684 ? 105.443 131.529 116.922 1.00 49.85  ? 667 PHE A CZ  1 
ATOM 5127 N N   . ILE A 1 685 ? 100.432 133.065 120.356 1.00 49.85  ? 668 ILE A N   1 
ATOM 5128 C CA  . ILE A 1 685 ? 99.335  132.173 119.992 1.00 49.85  ? 668 ILE A CA  1 
ATOM 5129 C C   . ILE A 1 685 ? 99.271  132.068 118.473 1.00 49.85  ? 668 ILE A C   1 
ATOM 5130 O O   . ILE A 1 685 ? 99.109  133.088 117.788 1.00 49.85  ? 668 ILE A O   1 
ATOM 5131 C CB  . ILE A 1 685 ? 98.000  132.663 120.572 1.00 49.85  ? 668 ILE A CB  1 
ATOM 5132 C CG1 . ILE A 1 685 ? 98.082  132.743 122.097 1.00 49.85  ? 668 ILE A CG1 1 
ATOM 5133 C CG2 . ILE A 1 685 ? 96.867  131.744 120.144 1.00 49.85  ? 668 ILE A CG2 1 
ATOM 5134 C CD1 . ILE A 1 685 ? 97.049  133.658 122.716 1.00 49.85  ? 668 ILE A CD1 1 
ATOM 5135 N N   . PRO A 1 686 ? 99.400  130.871 117.908 1.00 49.85  ? 669 PRO A N   1 
ATOM 5136 C CA  . PRO A 1 686 ? 99.299  130.729 116.452 1.00 49.85  ? 669 PRO A CA  1 
ATOM 5137 C C   . PRO A 1 686 ? 97.903  131.066 115.955 1.00 49.85  ? 669 PRO A C   1 
ATOM 5138 O O   . PRO A 1 686 ? 96.901  130.842 116.638 1.00 49.85  ? 669 PRO A O   1 
ATOM 5139 C CB  . PRO A 1 686 ? 99.632  129.253 116.217 1.00 49.85  ? 669 PRO A CB  1 
ATOM 5140 C CG  . PRO A 1 686 ? 99.293  128.588 117.507 1.00 49.85  ? 669 PRO A CG  1 
ATOM 5141 C CD  . PRO A 1 686 ? 99.638  129.581 118.574 1.00 49.85  ? 669 PRO A CD  1 
ATOM 5142 N N   . GLU A 1 687 ? 97.849  131.613 114.744 1.00 50.96  ? 670 GLU A N   1 
ATOM 5143 C CA  . GLU A 1 687 ? 96.592  132.027 114.123 1.00 50.96  ? 670 GLU A CA  1 
ATOM 5144 C C   . GLU A 1 687 ? 96.157  130.932 113.155 1.00 50.96  ? 670 GLU A C   1 
ATOM 5145 O O   . GLU A 1 687 ? 96.534  130.924 111.983 1.00 50.96  ? 670 GLU A O   1 
ATOM 5146 C CB  . GLU A 1 687 ? 96.749  133.372 113.422 1.00 50.96  ? 670 GLU A CB  1 
ATOM 5147 C CG  . GLU A 1 687 ? 96.392  134.567 114.289 1.00 50.96  ? 670 GLU A CG  1 
ATOM 5148 C CD  . GLU A 1 687 ? 97.612  135.234 114.892 1.00 50.96  ? 670 GLU A CD  1 
ATOM 5149 O OE1 . GLU A 1 687 ? 98.596  134.523 115.186 1.00 50.96  ? 670 GLU A OE1 1 
ATOM 5150 O OE2 . GLU A 1 687 ? 97.588  136.469 115.071 1.00 50.96  ? 670 GLU A OE2 1 
ATOM 5151 N N   . ILE A 1 688 ? 95.354  130.001 113.656 1.00 51.81  ? 671 ILE A N   1 
ATOM 5152 C CA  . ILE A 1 688 ? 94.783  128.941 112.836 1.00 51.81  ? 671 ILE A CA  1 
ATOM 5153 C C   . ILE A 1 688 ? 93.408  129.390 112.360 1.00 51.81  ? 671 ILE A C   1 
ATOM 5154 O O   . ILE A 1 688 ? 92.570  129.819 113.163 1.00 51.81  ? 671 ILE A O   1 
ATOM 5155 C CB  . ILE A 1 688 ? 94.702  127.620 113.620 1.00 51.81  ? 671 ILE A CB  1 
ATOM 5156 C CG1 . ILE A 1 688 ? 93.873  126.585 112.855 1.00 51.81  ? 671 ILE A CG1 1 
ATOM 5157 C CG2 . ILE A 1 688 ? 94.146  127.852 115.020 1.00 51.81  ? 671 ILE A CG2 1 
ATOM 5158 C CD1 . ILE A 1 688 ? 94.467  126.191 111.521 1.00 51.81  ? 671 ILE A CD1 1 
ATOM 5159 N N   . ALA A 1 689 ? 93.178  129.308 111.052 1.00 55.33  ? 672 ALA A N   1 
ATOM 5160 C CA  . ALA A 1 689 ? 91.933  129.785 110.456 1.00 55.33  ? 672 ALA A CA  1 
ATOM 5161 C C   . ALA A 1 689 ? 91.550  128.855 109.314 1.00 55.33  ? 672 ALA A C   1 
ATOM 5162 O O   . ALA A 1 689 ? 92.247  128.798 108.296 1.00 55.33  ? 672 ALA A O   1 
ATOM 5163 C CB  . ALA A 1 689 ? 92.073  131.225 109.962 1.00 55.33  ? 672 ALA A CB  1 
ATOM 5164 N N   . ILE A 1 690 ? 90.449  128.133 109.485 1.00 55.32  ? 673 ILE A N   1 
ATOM 5165 C CA  . ILE A 1 690 ? 89.883  127.274 108.453 1.00 55.32  ? 673 ILE A CA  1 
ATOM 5166 C C   . ILE A 1 690 ? 88.620  127.955 107.929 1.00 55.32  ? 673 ILE A C   1 
ATOM 5167 O O   . ILE A 1 690 ? 87.621  128.048 108.657 1.00 55.32  ? 673 ILE A O   1 
ATOM 5168 C CB  . ILE A 1 690 ? 89.576  125.869 108.986 1.00 55.32  ? 673 ILE A CB  1 
ATOM 5169 C CG1 . ILE A 1 690 ? 90.858  125.196 109.486 1.00 55.32  ? 673 ILE A CG1 1 
ATOM 5170 C CG2 . ILE A 1 690 ? 88.884  125.031 107.916 1.00 55.32  ? 673 ILE A CG2 1 
ATOM 5171 C CD1 . ILE A 1 690 ? 91.527  124.299 108.466 1.00 55.32  ? 673 ILE A CD1 1 
ATOM 5172 N N   . PRO A 1 691 ? 88.611  128.443 106.690 1.00 58.33  ? 674 PRO A N   1 
ATOM 5173 C CA  . PRO A 1 691 ? 87.404  129.093 106.165 1.00 58.33  ? 674 PRO A CA  1 
ATOM 5174 C C   . PRO A 1 691 ? 86.316  128.088 105.830 1.00 58.33  ? 674 PRO A C   1 
ATOM 5175 O O   . PRO A 1 691 ? 86.469  126.890 106.089 1.00 58.33  ? 674 PRO A O   1 
ATOM 5176 C CB  . PRO A 1 691 ? 87.918  129.812 104.914 1.00 58.33  ? 674 PRO A CB  1 
ATOM 5177 C CG  . PRO A 1 691 ? 89.042  128.952 104.445 1.00 58.33  ? 674 PRO A CG  1 
ATOM 5178 C CD  . PRO A 1 691 ? 89.692  128.391 105.690 1.00 58.33  ? 674 PRO A CD  1 
ATOM 5179 N N   . VAL A 1 692 ? 85.208  128.565 105.257 1.00 58.44  ? 675 VAL A N   1 
ATOM 5180 C CA  . VAL A 1 692 ? 84.116  127.670 104.900 1.00 58.44  ? 675 VAL A CA  1 
ATOM 5181 C C   . VAL A 1 692 ? 84.582  126.714 103.814 1.00 58.44  ? 675 VAL A C   1 
ATOM 5182 O O   . VAL A 1 692 ? 85.119  127.132 102.780 1.00 58.44  ? 675 VAL A O   1 
ATOM 5183 C CB  . VAL A 1 692 ? 82.888  128.475 104.451 1.00 58.44  ? 675 VAL A CB  1 
ATOM 5184 C CG1 . VAL A 1 692 ? 81.654  127.587 104.427 1.00 58.44  ? 675 VAL A CG1 1 
ATOM 5185 C CG2 . VAL A 1 692 ? 82.677  129.671 105.366 1.00 58.44  ? 675 VAL A CG2 1 
ATOM 5186 N N   . LEU A 1 693 ? 84.381  125.420 104.045 1.00 54.96  ? 676 LEU A N   1 
ATOM 5187 C CA  . LEU A 1 693 ? 84.812  124.416 103.086 1.00 54.96  ? 676 LEU A CA  1 
ATOM 5188 C C   . LEU A 1 693 ? 83.954  124.474 101.829 1.00 54.96  ? 676 LEU A C   1 
ATOM 5189 O O   . LEU A 1 693 ? 82.772  124.827 101.869 1.00 54.96  ? 676 LEU A O   1 
ATOM 5190 C CB  . LEU A 1 693 ? 84.744  123.020 103.705 1.00 54.96  ? 676 LEU A CB  1 
ATOM 5191 C CG  . LEU A 1 693 ? 85.424  122.844 105.064 1.00 54.96  ? 676 LEU A CG  1 
ATOM 5192 C CD1 . LEU A 1 693 ? 85.351  121.394 105.512 1.00 54.96  ? 676 LEU A CD1 1 
ATOM 5193 C CD2 . LEU A 1 693 ? 86.867  123.318 105.011 1.00 54.96  ? 676 LEU A CD2 1 
ATOM 5194 N N   . GLY A 1 694 ? 84.566  124.123 100.700 1.00 60.81  ? 677 GLY A N   1 
ATOM 5195 C CA  . GLY A 1 694 ? 83.868  124.157 99.431  1.00 60.81  ? 677 GLY A CA  1 
ATOM 5196 C C   . GLY A 1 694 ? 82.782  123.103 99.383  1.00 60.81  ? 677 GLY A C   1 
ATOM 5197 O O   . GLY A 1 694 ? 83.072  121.899 99.485  1.00 60.81  ? 677 GLY A O   1 
ATOM 5198 N N   . THR A 1 695 ? 81.530  123.529 99.236  1.00 65.60  ? 678 THR A N   1 
ATOM 5199 C CA  . THR A 1 695 ? 80.426  122.584 99.157  1.00 65.60  ? 678 THR A CA  1 
ATOM 5200 C C   . THR A 1 695 ? 80.546  121.734 97.899  1.00 65.60  ? 678 THR A C   1 
ATOM 5201 O O   . THR A 1 695 ? 80.890  122.229 96.823  1.00 65.60  ? 678 THR A O   1 
ATOM 5202 C CB  . THR A 1 695 ? 79.087  123.322 99.169  1.00 65.60  ? 678 THR A CB  1 
ATOM 5203 O OG1 . THR A 1 695 ? 79.180  124.501 98.360  1.00 65.60  ? 678 THR A OG1 1 
ATOM 5204 C CG2 . THR A 1 695 ? 78.707  123.714 100.590 1.00 65.60  ? 678 THR A CG2 1 
ATOM 5205 N N   . PHE A 1 696 ? 80.262  120.444 98.044  1.00 67.17  ? 679 PHE A N   1 
ATOM 5206 C CA  . PHE A 1 696 ? 80.382  119.522 96.925  1.00 67.17  ? 679 PHE A CA  1 
ATOM 5207 C C   . PHE A 1 696 ? 79.322  119.801 95.869  1.00 67.17  ? 679 PHE A C   1 
ATOM 5208 O O   . PHE A 1 696 ? 78.189  120.178 96.181  1.00 67.17  ? 679 PHE A O   1 
ATOM 5209 C CB  . PHE A 1 696 ? 80.273  118.080 97.418  1.00 67.17  ? 679 PHE A CB  1 
ATOM 5210 C CG  . PHE A 1 696 ? 81.571  117.514 97.909  1.00 67.17  ? 679 PHE A CG  1 
ATOM 5211 C CD1 . PHE A 1 696 ? 82.236  118.089 98.978  1.00 67.17  ? 679 PHE A CD1 1 
ATOM 5212 C CD2 . PHE A 1 696 ? 82.123  116.402 97.305  1.00 67.17  ? 679 PHE A CD2 1 
ATOM 5213 C CE1 . PHE A 1 696 ? 83.433  117.568 99.426  1.00 67.17  ? 679 PHE A CE1 1 
ATOM 5214 C CE2 . PHE A 1 696 ? 83.314  115.876 97.750  1.00 67.17  ? 679 PHE A CE2 1 
ATOM 5215 C CZ  . PHE A 1 696 ? 83.971  116.458 98.812  1.00 67.17  ? 679 PHE A CZ  1 
ATOM 5216 N N   . ALA A 1 697 ? 79.702  119.609 94.609  1.00 80.59  ? 680 ALA A N   1 
ATOM 5217 C CA  . ALA A 1 697 ? 78.820  119.796 93.461  1.00 80.59  ? 680 ALA A CA  1 
ATOM 5218 C C   . ALA A 1 697 ? 78.687  118.441 92.772  1.00 80.59  ? 680 ALA A C   1 
ATOM 5219 O O   . ALA A 1 697 ? 79.534  118.057 91.962  1.00 80.59  ? 680 ALA A O   1 
ATOM 5220 C CB  . ALA A 1 697 ? 79.360  120.864 92.512  1.00 80.59  ? 680 ALA A CB  1 
ATOM 5221 N N   . LEU A 1 698 ? 77.639  117.705 93.132  1.00 84.79  ? 681 LEU A N   1 
ATOM 5222 C CA  . LEU A 1 698 ? 77.360  116.432 92.484  1.00 84.79  ? 681 LEU A CA  1 
ATOM 5223 C C   . LEU A 1 698 ? 76.663  116.667 91.151  1.00 84.79  ? 681 LEU A C   1 
ATOM 5224 O O   . LEU A 1 698 ? 75.699  117.432 91.062  1.00 84.79  ? 681 LEU A O   1 
ATOM 5225 C CB  . LEU A 1 698 ? 76.491  115.551 93.384  1.00 84.79  ? 681 LEU A CB  1 
ATOM 5226 C CG  . LEU A 1 698 ? 76.609  115.709 94.902  1.00 84.79  ? 681 LEU A CG  1 
ATOM 5227 C CD1 . LEU A 1 698 ? 75.643  114.768 95.604  1.00 84.79  ? 681 LEU A CD1 1 
ATOM 5228 C CD2 . LEU A 1 698 ? 78.032  115.447 95.374  1.00 84.79  ? 681 LEU A CD2 1 
ATOM 5229 N N   . VAL A 1 699 ? 77.152  116.002 90.111  1.00 95.08  ? 682 VAL A N   1 
ATOM 5230 C CA  . VAL A 1 699 ? 76.618  116.171 88.765  1.00 95.08  ? 682 VAL A CA  1 
ATOM 5231 C C   . VAL A 1 699 ? 75.465  115.193 88.580  1.00 95.08  ? 682 VAL A C   1 
ATOM 5232 O O   . VAL A 1 699 ? 75.617  113.988 88.807  1.00 95.08  ? 682 VAL A O   1 
ATOM 5233 C CB  . VAL A 1 699 ? 77.706  115.959 87.702  1.00 95.08  ? 682 VAL A CB  1 
ATOM 5234 C CG1 . VAL A 1 699 ? 77.097  115.465 86.400  1.00 95.08  ? 682 VAL A CG1 1 
ATOM 5235 C CG2 . VAL A 1 699 ? 78.475  117.247 87.475  1.00 95.08  ? 682 VAL A CG2 1 
ATOM 5236 N N   . SER A 1 700 ? 74.309  115.715 88.180  1.00 100.76 ? 683 SER A N   1 
ATOM 5237 C CA  . SER A 1 700 ? 73.130  114.881 87.999  1.00 100.76 ? 683 SER A CA  1 
ATOM 5238 C C   . SER A 1 700 ? 73.298  113.957 86.800  1.00 100.76 ? 683 SER A C   1 
ATOM 5239 O O   . SER A 1 700 ? 73.880  114.332 85.778  1.00 100.76 ? 683 SER A O   1 
ATOM 5240 C CB  . SER A 1 700 ? 71.887  115.752 87.818  1.00 100.76 ? 683 SER A CB  1 
ATOM 5241 O OG  . SER A 1 700 ? 70.757  114.965 87.487  1.00 100.76 ? 683 SER A OG  1 
ATOM 5242 N N   . TYR A 1 701 ? 72.780  112.735 86.933  1.00 105.19 ? 684 TYR A N   1 
ATOM 5243 C CA  . TYR A 1 701 ? 72.799  111.736 85.860  1.00 105.19 ? 684 TYR A CA  1 
ATOM 5244 C C   . TYR A 1 701 ? 71.428  111.061 85.854  1.00 105.19 ? 684 TYR A C   1 
ATOM 5245 O O   . TYR A 1 701 ? 71.198  110.087 86.576  1.00 105.19 ? 684 TYR A O   1 
ATOM 5246 C CB  . TYR A 1 701 ? 73.929  110.735 86.053  1.00 105.19 ? 684 TYR A CB  1 
ATOM 5247 C CG  . TYR A 1 701 ? 75.304  111.304 85.778  1.00 105.19 ? 684 TYR A CG  1 
ATOM 5248 C CD1 . TYR A 1 701 ? 75.634  111.796 84.522  1.00 105.19 ? 684 TYR A CD1 1 
ATOM 5249 C CD2 . TYR A 1 701 ? 76.271  111.350 86.774  1.00 105.19 ? 684 TYR A CD2 1 
ATOM 5250 C CE1 . TYR A 1 701 ? 76.889  112.313 84.264  1.00 105.19 ? 684 TYR A CE1 1 
ATOM 5251 C CE2 . TYR A 1 701 ? 77.529  111.865 86.525  1.00 105.19 ? 684 TYR A CE2 1 
ATOM 5252 C CZ  . TYR A 1 701 ? 77.833  112.345 85.268  1.00 105.19 ? 684 TYR A CZ  1 
ATOM 5253 O OH  . TYR A 1 701 ? 79.083  112.862 85.016  1.00 105.19 ? 684 TYR A OH  1 
ATOM 5254 N N   . ILE A 1 702 ? 70.521  111.591 85.032  1.00 109.64 ? 685 ILE A N   1 
ATOM 5255 C CA  . ILE A 1 702 ? 69.145  111.111 85.015  1.00 109.64 ? 685 ILE A CA  1 
ATOM 5256 C C   . ILE A 1 702 ? 69.072  109.760 84.316  1.00 109.64 ? 685 ILE A C   1 
ATOM 5257 O O   . ILE A 1 702 ? 69.723  109.533 83.286  1.00 109.64 ? 685 ILE A O   1 
ATOM 5258 C CB  . ILE A 1 702 ? 68.230  112.147 84.339  1.00 109.64 ? 685 ILE A CB  1 
ATOM 5259 C CG1 . ILE A 1 702 ? 66.814  111.592 84.165  1.00 109.64 ? 685 ILE A CG1 1 
ATOM 5260 C CG2 . ILE A 1 702 ? 68.810  112.587 83.000  1.00 109.64 ? 685 ILE A CG2 1 
ATOM 5261 C CD1 . ILE A 1 702 ? 66.084  111.364 85.471  1.00 109.64 ? 685 ILE A CD1 1 
ATOM 5262 N N   . ALA A 1 703 ? 68.296  108.843 84.897  1.00 110.15 ? 686 ALA A N   1 
ATOM 5263 C CA  . ALA A 1 703 ? 67.964  107.521 84.372  1.00 110.15 ? 686 ALA A CA  1 
ATOM 5264 C C   . ALA A 1 703 ? 69.148  106.562 84.358  1.00 110.15 ? 686 ALA A C   1 
ATOM 5265 O O   . ALA A 1 703 ? 68.977  105.400 83.969  1.00 110.15 ? 686 ALA A O   1 
ATOM 5266 C CB  . ALA A 1 703 ? 67.363  107.583 82.959  1.00 110.15 ? 686 ALA A CB  1 
ATOM 5267 N N   . ASN A 1 704 ? 70.336  106.997 84.767  1.00 109.91 ? 687 ASN A N   1 
ATOM 5268 C CA  . ASN A 1 704 ? 71.507  106.125 84.855  1.00 109.91 ? 687 ASN A CA  1 
ATOM 5269 C C   . ASN A 1 704 ? 71.721  105.811 86.332  1.00 109.91 ? 687 ASN A C   1 
ATOM 5270 O O   . ASN A 1 704 ? 72.459  106.502 87.035  1.00 109.91 ? 687 ASN A O   1 
ATOM 5271 C CB  . ASN A 1 704 ? 72.725  106.782 84.220  1.00 109.91 ? 687 ASN A CB  1 
ATOM 5272 C CG  . ASN A 1 704 ? 72.943  106.342 82.786  1.00 109.91 ? 687 ASN A CG  1 
ATOM 5273 O OD1 . ASN A 1 704 ? 73.535  105.294 82.529  1.00 109.91 ? 687 ASN A OD1 1 
ATOM 5274 N ND2 . ASN A 1 704 ? 72.459  107.142 81.842  1.00 109.91 ? 687 ASN A ND2 1 
ATOM 5275 N N   . LYS A 1 705 ? 71.054  104.754 86.802  1.00 104.25 ? 688 LYS A N   1 
ATOM 5276 C CA  . LYS A 1 705 ? 71.052  104.444 88.228  1.00 104.25 ? 688 LYS A CA  1 
ATOM 5277 C C   . LYS A 1 705 ? 72.449  104.090 88.724  1.00 104.25 ? 688 LYS A C   1 
ATOM 5278 O O   . LYS A 1 705 ? 72.889  104.577 89.772  1.00 104.25 ? 688 LYS A O   1 
ATOM 5279 C CB  . LYS A 1 705 ? 70.074  103.303 88.509  1.00 104.25 ? 688 LYS A CB  1 
ATOM 5280 C CG  . LYS A 1 705 ? 68.662  103.564 88.010  1.00 104.25 ? 688 LYS A CG  1 
ATOM 5281 C CD  . LYS A 1 705 ? 68.114  104.873 88.552  1.00 104.25 ? 688 LYS A CD  1 
ATOM 5282 C CE  . LYS A 1 705 ? 66.690  105.110 88.078  1.00 104.25 ? 688 LYS A CE  1 
ATOM 5283 N NZ  . LYS A 1 705 ? 66.584  105.045 86.594  1.00 104.25 ? 688 LYS A NZ  1 
ATOM 5284 N N   . VAL A 1 706 ? 73.166  103.245 87.980  1.00 108.83 ? 689 VAL A N   1 
ATOM 5285 C CA  . VAL A 1 706 ? 74.504  102.849 88.410  1.00 108.83 ? 689 VAL A CA  1 
ATOM 5286 C C   . VAL A 1 706 ? 75.454  104.042 88.371  1.00 108.83 ? 689 VAL A C   1 
ATOM 5287 O O   . VAL A 1 706 ? 76.372  104.142 89.196  1.00 108.83 ? 689 VAL A O   1 
ATOM 5288 C CB  . VAL A 1 706 ? 75.010  101.661 87.565  1.00 108.83 ? 689 VAL A CB  1 
ATOM 5289 C CG1 . VAL A 1 706 ? 75.533  102.119 86.207  1.00 108.83 ? 689 VAL A CG1 1 
ATOM 5290 C CG2 . VAL A 1 706 ? 76.067  100.873 88.328  1.00 108.83 ? 689 VAL A CG2 1 
ATOM 5291 N N   . LEU A 1 707 ? 75.246  104.968 87.433  1.00 103.98 ? 690 LEU A N   1 
ATOM 5292 C CA  . LEU A 1 707 ? 76.013  106.209 87.425  1.00 103.98 ? 690 LEU A CA  1 
ATOM 5293 C C   . LEU A 1 707 ? 75.753  107.005 88.698  1.00 103.98 ? 690 LEU A C   1 
ATOM 5294 O O   . LEU A 1 707 ? 76.675  107.577 89.293  1.00 103.98 ? 690 LEU A O   1 
ATOM 5295 C CB  . LEU A 1 707 ? 75.651  107.025 86.183  1.00 103.98 ? 690 LEU A CB  1 
ATOM 5296 C CG  . LEU A 1 707 ? 76.613  108.081 85.638  1.00 103.98 ? 690 LEU A CG  1 
ATOM 5297 C CD1 . LEU A 1 707 ? 78.055  107.656 85.810  1.00 103.98 ? 690 LEU A CD1 1 
ATOM 5298 C CD2 . LEU A 1 707 ? 76.312  108.355 84.173  1.00 103.98 ? 690 LEU A CD2 1 
ATOM 5299 N N   . THR A 1 708 ? 74.493  107.038 89.138  1.00 103.74 ? 691 THR A N   1 
ATOM 5300 C CA  . THR A 1 708 ? 74.155  107.691 90.398  1.00 103.74 ? 691 THR A CA  1 
ATOM 5301 C C   . THR A 1 708 ? 74.854  107.008 91.570  1.00 103.74 ? 691 THR A C   1 
ATOM 5302 O O   . THR A 1 708 ? 75.318  107.671 92.504  1.00 103.74 ? 691 THR A O   1 
ATOM 5303 C CB  . THR A 1 708 ? 72.637  107.698 90.591  1.00 103.74 ? 691 THR A CB  1 
ATOM 5304 O OG1 . THR A 1 708 ? 72.046  108.649 89.696  1.00 103.74 ? 691 THR A OG1 1 
ATOM 5305 C CG2 . THR A 1 708 ? 72.269  108.069 92.021  1.00 103.74 ? 691 THR A CG2 1 
ATOM 5306 N N   . VAL A 1 709 ? 74.931  105.674 91.540  1.00 103.26 ? 692 VAL A N   1 
ATOM 5307 C CA  . VAL A 1 709 ? 75.633  104.950 92.601  1.00 103.26 ? 692 VAL A CA  1 
ATOM 5308 C C   . VAL A 1 709 ? 77.113  105.315 92.621  1.00 103.26 ? 692 VAL A C   1 
ATOM 5309 O O   . VAL A 1 709 ? 77.706  105.505 93.691  1.00 103.26 ? 692 VAL A O   1 
ATOM 5310 C CB  . VAL A 1 709 ? 75.429  103.431 92.450  1.00 103.26 ? 692 VAL A CB  1 
ATOM 5311 C CG1 . VAL A 1 709 ? 75.976  102.708 93.668  1.00 103.26 ? 692 VAL A CG1 1 
ATOM 5312 C CG2 . VAL A 1 709 ? 73.957  103.109 92.282  1.00 103.26 ? 692 VAL A CG2 1 
ATOM 5313 N N   . GLN A 1 710 ? 77.740  105.404 91.446  1.00 103.79 ? 693 GLN A N   1 
ATOM 5314 C CA  . GLN A 1 710 ? 79.145  105.808 91.418  1.00 103.79 ? 693 GLN A CA  1 
ATOM 5315 C C   . GLN A 1 710 ? 79.319  107.229 91.940  1.00 103.79 ? 693 GLN A C   1 
ATOM 5316 O O   . GLN A 1 710 ? 80.302  107.531 92.625  1.00 103.79 ? 693 GLN A O   1 
ATOM 5317 C CB  . GLN A 1 710 ? 79.750  105.671 90.018  1.00 103.79 ? 693 GLN A CB  1 
ATOM 5318 C CG  . GLN A 1 710 ? 79.721  104.271 89.426  1.00 103.79 ? 693 GLN A CG  1 
ATOM 5319 C CD  . GLN A 1 710 ? 79.056  104.218 88.070  1.00 103.79 ? 693 GLN A CD  1 
ATOM 5320 O OE1 . GLN A 1 710 ? 79.213  105.125 87.255  1.00 103.79 ? 693 GLN A OE1 1 
ATOM 5321 N NE2 . GLN A 1 710 ? 78.328  103.143 87.810  1.00 103.79 ? 693 GLN A NE2 1 
ATOM 5322 N N   . THR A 1 711 ? 78.380  108.123 91.619  1.00 99.23  ? 694 THR A N   1 
ATOM 5323 C CA  . THR A 1 711 ? 78.456  109.477 92.165  1.00 99.23  ? 694 THR A CA  1 
ATOM 5324 C C   . THR A 1 711 ? 78.338  109.469 93.686  1.00 99.23  ? 694 THR A C   1 
ATOM 5325 O O   . THR A 1 711 ? 79.090  110.165 94.378  1.00 99.23  ? 694 THR A O   1 
ATOM 5326 C CB  . THR A 1 711 ? 77.374  110.371 91.559  1.00 99.23  ? 694 THR A CB  1 
ATOM 5327 O OG1 . THR A 1 711 ? 76.082  109.804 91.808  1.00 99.23  ? 694 THR A OG1 1 
ATOM 5328 C CG2 . THR A 1 711 ? 77.585  110.528 90.061  1.00 99.23  ? 694 THR A CG2 1 
ATOM 5329 N N   . ILE A 1 712 ? 77.402  108.682 94.225  1.00 95.44  ? 695 ILE A N   1 
ATOM 5330 C CA  . ILE A 1 712 ? 77.204  108.639 95.670  1.00 95.44  ? 695 ILE A CA  1 
ATOM 5331 C C   . ILE A 1 712 ? 78.375  107.970 96.377  1.00 95.44  ? 695 ILE A C   1 
ATOM 5332 O O   . ILE A 1 712 ? 78.612  108.236 97.561  1.00 95.44  ? 695 ILE A O   1 
ATOM 5333 C CB  . ILE A 1 712 ? 75.878  107.934 96.024  1.00 95.44  ? 695 ILE A CB  1 
ATOM 5334 C CG1 . ILE A 1 712 ? 75.320  108.468 97.342  1.00 95.44  ? 695 ILE A CG1 1 
ATOM 5335 C CG2 . ILE A 1 712 ? 76.059  106.431 96.137  1.00 95.44  ? 695 ILE A CG2 1 
ATOM 5336 C CD1 . ILE A 1 712 ? 73.881  108.073 97.590  1.00 95.44  ? 695 ILE A CD1 1 
ATOM 5337 N N   . ASP A 1 713 ? 79.117  107.106 95.685  1.00 97.05  ? 696 ASP A N   1 
ATOM 5338 C CA  . ASP A 1 713 ? 80.309  106.505 96.270  1.00 97.05  ? 696 ASP A CA  1 
ATOM 5339 C C   . ASP A 1 713 ? 81.511  107.440 96.201  1.00 97.05  ? 696 ASP A C   1 
ATOM 5340 O O   . ASP A 1 713 ? 82.288  107.528 97.161  1.00 97.05  ? 696 ASP A O   1 
ATOM 5341 C CB  . ASP A 1 713 ? 80.630  105.184 95.567  1.00 97.05  ? 696 ASP A CB  1 
ATOM 5342 C CG  . ASP A 1 713 ? 79.809  104.027 96.100  1.00 97.05  ? 696 ASP A CG  1 
ATOM 5343 O OD1 . ASP A 1 713 ? 78.564  104.137 96.112  1.00 97.05  ? 696 ASP A OD1 1 
ATOM 5344 O OD2 . ASP A 1 713 ? 80.406  103.009 96.508  1.00 97.05  ? 696 ASP A OD2 1 
ATOM 5345 N N   . ASN A 1 714 ? 81.671  108.145 95.079  1.00 93.91  ? 697 ASN A N   1 
ATOM 5346 C CA  . ASN A 1 714 ? 82.739  109.130 94.964  1.00 93.91  ? 697 ASN A CA  1 
ATOM 5347 C C   . ASN A 1 714 ? 82.536  110.270 95.951  1.00 93.91  ? 697 ASN A C   1 
ATOM 5348 O O   . ASN A 1 714 ? 83.509  110.819 96.479  1.00 93.91  ? 697 ASN A O   1 
ATOM 5349 C CB  . ASN A 1 714 ? 82.810  109.662 93.534  1.00 93.91  ? 697 ASN A CB  1 
ATOM 5350 C CG  . ASN A 1 714 ? 83.620  108.766 92.619  1.00 93.91  ? 697 ASN A CG  1 
ATOM 5351 O OD1 . ASN A 1 714 ? 84.040  107.677 93.011  1.00 93.91  ? 697 ASN A OD1 1 
ATOM 5352 N ND2 . ASN A 1 714 ? 83.842  109.220 91.391  1.00 93.91  ? 697 ASN A ND2 1 
ATOM 5353 N N   . ALA A 1 715 ? 81.280  110.637 96.215  1.00 80.24  ? 698 ALA A N   1 
ATOM 5354 C CA  . ALA A 1 715 ? 81.005  111.666 97.211  1.00 80.24  ? 698 ALA A CA  1 
ATOM 5355 C C   . ALA A 1 715 ? 81.509  111.242 98.584  1.00 80.24  ? 698 ALA A C   1 
ATOM 5356 O O   . ALA A 1 715 ? 82.156  112.023 99.288  1.00 80.24  ? 698 ALA A O   1 
ATOM 5357 C CB  . ALA A 1 715 ? 79.507  111.967 97.254  1.00 80.24  ? 698 ALA A CB  1 
ATOM 5358 N N   . LEU A 1 716 ? 81.241  109.993 98.972  1.00 80.36  ? 699 LEU A N   1 
ATOM 5359 C CA  . LEU A 1 716 ? 81.704  109.501 100.266 1.00 80.36  ? 699 LEU A CA  1 
ATOM 5360 C C   . LEU A 1 716 ? 83.225  109.414 100.312 1.00 80.36  ? 699 LEU A C   1 
ATOM 5361 O O   . LEU A 1 716 ? 83.852  109.781 101.318 1.00 80.36  ? 699 LEU A O   1 
ATOM 5362 C CB  . LEU A 1 716 ? 81.081  108.136 100.554 1.00 80.36  ? 699 LEU A CB  1 
ATOM 5363 C CG  . LEU A 1 716 ? 79.624  108.136 101.020 1.00 80.36  ? 699 LEU A CG  1 
ATOM 5364 C CD1 . LEU A 1 716 ? 79.270  106.812 101.681 1.00 80.36  ? 699 LEU A CD1 1 
ATOM 5365 C CD2 . LEU A 1 716 ? 79.343  109.306 101.950 1.00 80.36  ? 699 LEU A CD2 1 
ATOM 5366 N N   . SER A 1 717 ? 83.836  108.921 99.232  1.00 82.09  ? 700 SER A N   1 
ATOM 5367 C CA  . SER A 1 717 ? 85.291  108.807 99.195  1.00 82.09  ? 700 SER A CA  1 
ATOM 5368 C C   . SER A 1 717 ? 85.953  110.173 99.315  1.00 82.09  ? 700 SER A C   1 
ATOM 5369 O O   . SER A 1 717 ? 86.914  110.343 100.076 1.00 82.09  ? 700 SER A O   1 
ATOM 5370 C CB  . SER A 1 717 ? 85.731  108.110 97.908  1.00 82.09  ? 700 SER A CB  1 
ATOM 5371 O OG  . SER A 1 717 ? 85.784  109.025 96.828  1.00 82.09  ? 700 SER A OG  1 
ATOM 5372 N N   . LYS A 1 718 ? 85.440  111.169 98.589  1.00 74.72  ? 701 LYS A N   1 
ATOM 5373 C CA  . LYS A 1 718 ? 86.023  112.501 98.663  1.00 74.72  ? 701 LYS A CA  1 
ATOM 5374 C C   . LYS A 1 718 ? 85.682  113.190 99.978  1.00 74.72  ? 701 LYS A C   1 
ATOM 5375 O O   . LYS A 1 718 ? 86.436  114.051 100.429 1.00 74.72  ? 701 LYS A O   1 
ATOM 5376 C CB  . LYS A 1 718 ? 85.564  113.345 97.476  1.00 74.72  ? 701 LYS A CB  1 
ATOM 5377 C CG  . LYS A 1 718 ? 86.517  114.476 97.124  1.00 74.72  ? 701 LYS A CG  1 
ATOM 5378 C CD  . LYS A 1 718 ? 87.938  113.965 96.950  1.00 74.72  ? 701 LYS A CD  1 
ATOM 5379 C CE  . LYS A 1 718 ? 88.934  115.110 96.872  1.00 74.72  ? 701 LYS A CE  1 
ATOM 5380 N NZ  . LYS A 1 718 ? 89.143  115.753 98.198  1.00 74.72  ? 701 LYS A NZ  1 
ATOM 5381 N N   . ARG A 1 719 ? 84.568  112.820 100.611 1.00 68.12  ? 702 ARG A N   1 
ATOM 5382 C CA  . ARG A 1 719 ? 84.283  113.284 101.966 1.00 68.12  ? 702 ARG A CA  1 
ATOM 5383 C C   . ARG A 1 719 ? 85.357  112.808 102.937 1.00 68.12  ? 702 ARG A C   1 
ATOM 5384 O O   . ARG A 1 719 ? 85.907  113.596 103.721 1.00 68.12  ? 702 ARG A O   1 
ATOM 5385 C CB  . ARG A 1 719 ? 82.892  112.788 102.373 1.00 68.12  ? 702 ARG A CB  1 
ATOM 5386 C CG  . ARG A 1 719 ? 82.651  112.495 103.848 1.00 68.12  ? 702 ARG A CG  1 
ATOM 5387 C CD  . ARG A 1 719 ? 82.759  113.716 104.744 1.00 68.12  ? 702 ARG A CD  1 
ATOM 5388 N NE  . ARG A 1 719 ? 81.995  113.554 105.978 1.00 68.12  ? 702 ARG A NE  1 
ATOM 5389 C CZ  . ARG A 1 719 ? 82.233  112.640 106.911 1.00 68.12  ? 702 ARG A CZ  1 
ATOM 5390 N NH1 . ARG A 1 719 ? 83.244  111.791 106.811 1.00 68.12  ? 702 ARG A NH1 1 
ATOM 5391 N NH2 . ARG A 1 719 ? 81.442  112.582 107.978 1.00 68.12  ? 702 ARG A NH2 1 
ATOM 5392 N N   . ASN A 1 720 ? 85.682  111.515 102.881 1.00 72.14  ? 703 ASN A N   1 
ATOM 5393 C CA  . ASN A 1 720 ? 86.743  110.984 103.734 1.00 72.14  ? 703 ASN A CA  1 
ATOM 5394 C C   . ASN A 1 720 ? 88.086  111.630 103.407 1.00 72.14  ? 703 ASN A C   1 
ATOM 5395 O O   . ASN A 1 720 ? 88.867  111.957 104.310 1.00 72.14  ? 703 ASN A O   1 
ATOM 5396 C CB  . ASN A 1 720 ? 86.824  109.465 103.586 1.00 72.14  ? 703 ASN A CB  1 
ATOM 5397 C CG  . ASN A 1 720 ? 85.638  108.756 104.212 1.00 72.14  ? 703 ASN A CG  1 
ATOM 5398 O OD1 . ASN A 1 720 ? 84.556  109.327 104.342 1.00 72.14  ? 703 ASN A OD1 1 
ATOM 5399 N ND2 . ASN A 1 720 ? 85.838  107.503 104.602 1.00 72.14  ? 703 ASN A ND2 1 
ATOM 5400 N N   . GLU A 1 721 ? 88.368  111.825 102.116 1.00 69.38  ? 704 GLU A N   1 
ATOM 5401 C CA  . GLU A 1 721 ? 89.627  112.445 101.718 1.00 69.38  ? 704 GLU A CA  1 
ATOM 5402 C C   . GLU A 1 721 ? 89.705  113.897 102.178 1.00 69.38  ? 704 GLU A C   1 
ATOM 5403 O O   . GLU A 1 721 ? 90.778  114.373 102.558 1.00 69.38  ? 704 GLU A O   1 
ATOM 5404 C CB  . GLU A 1 721 ? 89.804  112.348 100.203 1.00 69.38  ? 704 GLU A CB  1 
ATOM 5405 C CG  . GLU A 1 721 ? 91.126  112.901 99.701  1.00 69.38  ? 704 GLU A CG  1 
ATOM 5406 C CD  . GLU A 1 721 ? 92.186  111.827 99.549  1.00 69.38  ? 704 GLU A CD  1 
ATOM 5407 O OE1 . GLU A 1 721 ? 92.035  110.750 100.163 1.00 69.38  ? 704 GLU A OE1 1 
ATOM 5408 O OE2 . GLU A 1 721 ? 93.172  112.063 98.820  1.00 69.38  ? 704 GLU A OE2 1 
ATOM 5409 N N   . LYS A 1 722 ? 88.583  114.619 102.138 1.00 59.35  ? 705 LYS A N   1 
ATOM 5410 C CA  . LYS A 1 722 ? 88.545  115.987 102.640 1.00 59.35  ? 705 LYS A CA  1 
ATOM 5411 C C   . LYS A 1 722 ? 88.810  116.025 104.137 1.00 59.35  ? 705 LYS A C   1 
ATOM 5412 O O   . LYS A 1 722 ? 89.558  116.884 104.624 1.00 59.35  ? 705 LYS A O   1 
ATOM 5413 C CB  . LYS A 1 722 ? 87.189  116.615 102.318 1.00 59.35  ? 705 LYS A CB  1 
ATOM 5414 C CG  . LYS A 1 722 ? 87.078  118.097 102.623 1.00 59.35  ? 705 LYS A CG  1 
ATOM 5415 C CD  . LYS A 1 722 ? 86.993  118.912 101.343 1.00 59.35  ? 705 LYS A CD  1 
ATOM 5416 C CE  . LYS A 1 722 ? 87.065  120.400 101.629 1.00 59.35  ? 705 LYS A CE  1 
ATOM 5417 N NZ  . LYS A 1 722 ? 88.438  120.826 101.997 1.00 59.35  ? 705 LYS A NZ  1 
ATOM 5418 N N   . TRP A 1 723 ? 88.198  115.103 104.885 1.00 56.37  ? 706 TRP A N   1 
ATOM 5419 C CA  . TRP A 1 723 ? 88.491  114.996 106.312 1.00 56.37  ? 706 TRP A CA  1 
ATOM 5420 C C   . TRP A 1 723 ? 89.980  114.777 106.544 1.00 56.37  ? 706 TRP A C   1 
ATOM 5421 O O   . TRP A 1 723 ? 90.605  115.464 107.363 1.00 56.37  ? 706 TRP A O   1 
ATOM 5422 C CB  . TRP A 1 723 ? 87.681  113.856 106.928 1.00 56.37  ? 706 TRP A CB  1 
ATOM 5423 C CG  . TRP A 1 723 ? 86.416  114.283 107.607 1.00 56.37  ? 706 TRP A CG  1 
ATOM 5424 C CD1 . TRP A 1 723 ? 85.156  114.221 107.095 1.00 56.37  ? 706 TRP A CD1 1 
ATOM 5425 C CD2 . TRP A 1 723 ? 86.284  114.805 108.935 1.00 56.37  ? 706 TRP A CD2 1 
ATOM 5426 N NE1 . TRP A 1 723 ? 84.247  114.687 108.013 1.00 56.37  ? 706 TRP A NE1 1 
ATOM 5427 C CE2 . TRP A 1 723 ? 84.914  115.052 109.151 1.00 56.37  ? 706 TRP A CE2 1 
ATOM 5428 C CE3 . TRP A 1 723 ? 87.191  115.099 109.957 1.00 56.37  ? 706 TRP A CE3 1 
ATOM 5429 C CZ2 . TRP A 1 723 ? 84.429  115.572 110.348 1.00 56.37  ? 706 TRP A CZ2 1 
ATOM 5430 C CZ3 . TRP A 1 723 ? 86.706  115.618 111.144 1.00 56.37  ? 706 TRP A CZ3 1 
ATOM 5431 C CH2 . TRP A 1 723 ? 85.339  115.849 111.329 1.00 56.37  ? 706 TRP A CH2 1 
ATOM 5432 N N   . ASP A 1 724 ? 90.567  113.827 105.811 1.00 63.24  ? 707 ASP A N   1 
ATOM 5433 C CA  . ASP A 1 724 ? 91.984  113.521 105.981 1.00 63.24  ? 707 ASP A CA  1 
ATOM 5434 C C   . ASP A 1 724 ? 92.863  114.714 105.623 1.00 63.24  ? 707 ASP A C   1 
ATOM 5435 O O   . ASP A 1 724 ? 93.852  114.992 106.309 1.00 63.24  ? 707 ASP A O   1 
ATOM 5436 C CB  . ASP A 1 724 ? 92.360  112.305 105.135 1.00 63.24  ? 707 ASP A CB  1 
ATOM 5437 C CG  . ASP A 1 724 ? 93.807  111.898 105.316 1.00 63.24  ? 707 ASP A CG  1 
ATOM 5438 O OD1 . ASP A 1 724 ? 94.663  112.414 104.568 1.00 63.24  ? 707 ASP A OD1 1 
ATOM 5439 O OD2 . ASP A 1 724 ? 94.089  111.073 106.210 1.00 63.24  ? 707 ASP A OD2 1 
ATOM 5440 N N   . GLU A 1 725 ? 92.521  115.427 104.549 1.00 54.64  ? 708 GLU A N   1 
ATOM 5441 C CA  . GLU A 1 725 ? 93.339  116.548 104.102 1.00 54.64  ? 708 GLU A CA  1 
ATOM 5442 C C   . GLU A 1 725 ? 93.268  117.699 105.097 1.00 54.64  ? 708 GLU A C   1 
ATOM 5443 O O   . GLU A 1 725 ? 94.289  118.334 105.390 1.00 54.64  ? 708 GLU A O   1 
ATOM 5444 C CB  . GLU A 1 725 ? 92.899  116.953 102.683 1.00 54.64  ? 708 GLU A CB  1 
ATOM 5445 C CG  . GLU A 1 725 ? 93.780  117.941 101.868 1.00 54.64  ? 708 GLU A CG  1 
ATOM 5446 C CD  . GLU A 1 725 ? 93.908  119.361 102.410 1.00 54.64  ? 708 GLU A CD  1 
ATOM 5447 O OE1 . GLU A 1 725 ? 93.176  119.747 103.340 1.00 54.64  ? 708 GLU A OE1 1 
ATOM 5448 O OE2 . GLU A 1 725 ? 94.774  120.102 101.897 1.00 54.64  ? 708 GLU A OE2 1 
ATOM 5449 N N   . VAL A 1 726 ? 92.080  117.978 105.642 1.00 49.85  ? 709 VAL A N   1 
ATOM 5450 C CA  . VAL A 1 726 ? 91.972  119.025 106.655 1.00 49.85  ? 709 VAL A CA  1 
ATOM 5451 C C   . VAL A 1 726 ? 92.745  118.628 107.907 1.00 49.85  ? 709 VAL A C   1 
ATOM 5452 O O   . VAL A 1 726 ? 93.430  119.457 108.524 1.00 49.85  ? 709 VAL A O   1 
ATOM 5453 C CB  . VAL A 1 726 ? 90.496  119.324 106.970 1.00 49.85  ? 709 VAL A CB  1 
ATOM 5454 C CG1 . VAL A 1 726 ? 90.386  120.144 108.243 1.00 49.85  ? 709 VAL A CG1 1 
ATOM 5455 C CG2 . VAL A 1 726 ? 89.847  120.054 105.810 1.00 49.85  ? 709 VAL A CG2 1 
ATOM 5456 N N   . TYR A 1 727 ? 92.650  117.355 108.301 1.00 51.23  ? 710 TYR A N   1 
ATOM 5457 C CA  . TYR A 1 727 ? 93.432  116.867 109.432 1.00 51.23  ? 710 TYR A CA  1 
ATOM 5458 C C   . TYR A 1 727 ? 94.923  117.074 109.194 1.00 51.23  ? 710 TYR A C   1 
ATOM 5459 O O   . TYR A 1 727 ? 95.652  117.521 110.086 1.00 51.23  ? 710 TYR A O   1 
ATOM 5460 C CB  . TYR A 1 727 ? 93.132  115.388 109.670 1.00 51.23  ? 710 TYR A CB  1 
ATOM 5461 C CG  . TYR A 1 727 ? 91.945  115.097 110.559 1.00 51.23  ? 710 TYR A CG  1 
ATOM 5462 C CD1 . TYR A 1 727 ? 91.260  116.117 111.204 1.00 51.23  ? 710 TYR A CD1 1 
ATOM 5463 C CD2 . TYR A 1 727 ? 91.524  113.790 110.767 1.00 51.23  ? 710 TYR A CD2 1 
ATOM 5464 C CE1 . TYR A 1 727 ? 90.178  115.841 112.022 1.00 51.23  ? 710 TYR A CE1 1 
ATOM 5465 C CE2 . TYR A 1 727 ? 90.449  113.506 111.581 1.00 51.23  ? 710 TYR A CE2 1 
ATOM 5466 C CZ  . TYR A 1 727 ? 89.779  114.533 112.207 1.00 51.23  ? 710 TYR A CZ  1 
ATOM 5467 O OH  . TYR A 1 727 ? 88.707  114.246 113.020 1.00 51.23  ? 710 TYR A OH  1 
ATOM 5468 N N   . LYS A 1 728 ? 95.392  116.747 107.987 1.00 49.85  ? 711 LYS A N   1 
ATOM 5469 C CA  . LYS A 1 728 ? 96.806  116.901 107.660 1.00 49.85  ? 711 LYS A CA  1 
ATOM 5470 C C   . LYS A 1 728 ? 97.216  118.368 107.713 1.00 49.85  ? 711 LYS A C   1 
ATOM 5471 O O   . LYS A 1 728 ? 98.291  118.702 108.223 1.00 49.85  ? 711 LYS A O   1 
ATOM 5472 C CB  . LYS A 1 728 ? 97.073  116.285 106.279 1.00 49.85  ? 711 LYS A CB  1 
ATOM 5473 C CG  . LYS A 1 728 ? 98.535  115.982 105.884 1.00 49.85  ? 711 LYS A CG  1 
ATOM 5474 C CD  . LYS A 1 728 ? 99.457  117.190 105.815 1.00 49.85  ? 711 LYS A CD  1 
ATOM 5475 C CE  . LYS A 1 728 ? 100.907 116.771 105.650 1.00 49.85  ? 711 LYS A CE  1 
ATOM 5476 N NZ  . LYS A 1 728 ? 101.831 117.937 105.699 1.00 49.85  ? 711 LYS A NZ  1 
ATOM 5477 N N   . TYR A 1 729 ? 96.371  119.257 107.189 1.00 49.85  ? 712 TYR A N   1 
ATOM 5478 C CA  . TYR A 1 729 ? 96.690  120.682 107.207 1.00 49.85  ? 712 TYR A CA  1 
ATOM 5479 C C   . TYR A 1 729 ? 96.789  121.204 108.636 1.00 49.85  ? 712 TYR A C   1 
ATOM 5480 O O   . TYR A 1 729 ? 97.707  121.966 108.968 1.00 49.85  ? 712 TYR A O   1 
ATOM 5481 C CB  . TYR A 1 729 ? 95.639  121.459 106.414 1.00 49.85  ? 712 TYR A CB  1 
ATOM 5482 C CG  . TYR A 1 729 ? 95.765  122.962 106.514 1.00 49.85  ? 712 TYR A CG  1 
ATOM 5483 C CD1 . TYR A 1 729 ? 96.903  123.614 106.061 1.00 49.85  ? 712 TYR A CD1 1 
ATOM 5484 C CD2 . TYR A 1 729 ? 94.742  123.728 107.054 1.00 49.85  ? 712 TYR A CD2 1 
ATOM 5485 C CE1 . TYR A 1 729 ? 97.020  124.988 106.146 1.00 49.85  ? 712 TYR A CE1 1 
ATOM 5486 C CE2 . TYR A 1 729 ? 94.851  125.103 107.145 1.00 49.85  ? 712 TYR A CE2 1 
ATOM 5487 C CZ  . TYR A 1 729 ? 95.992  125.727 106.691 1.00 49.85  ? 712 TYR A CZ  1 
ATOM 5488 O OH  . TYR A 1 729 ? 96.103  127.096 106.779 1.00 49.85  ? 712 TYR A OH  1 
ATOM 5489 N N   . ILE A 1 730 ? 95.861  120.789 109.502 1.00 49.85  ? 713 ILE A N   1 
ATOM 5490 C CA  . ILE A 1 730 ? 95.900  121.235 110.892 1.00 49.85  ? 713 ILE A CA  1 
ATOM 5491 C C   . ILE A 1 730 ? 97.120  120.662 111.606 1.00 49.85  ? 713 ILE A C   1 
ATOM 5492 O O   . ILE A 1 730 ? 97.748  121.338 112.430 1.00 49.85  ? 713 ILE A O   1 
ATOM 5493 C CB  . ILE A 1 730 ? 94.590  120.865 111.610 1.00 49.85  ? 713 ILE A CB  1 
ATOM 5494 C CG1 . ILE A 1 730 ? 93.416  121.621 110.986 1.00 49.85  ? 713 ILE A CG1 1 
ATOM 5495 C CG2 . ILE A 1 730 ? 94.682  121.182 113.093 1.00 49.85  ? 713 ILE A CG2 1 
ATOM 5496 C CD1 . ILE A 1 730 ? 92.063  121.099 111.407 1.00 49.85  ? 713 ILE A CD1 1 
ATOM 5497 N N   . VAL A 1 731 ? 97.481  119.414 111.298 1.00 49.85  ? 714 VAL A N   1 
ATOM 5498 C CA  . VAL A 1 731 ? 98.672  118.812 111.893 1.00 49.85  ? 714 VAL A CA  1 
ATOM 5499 C C   . VAL A 1 731 ? 99.923  119.569 111.465 1.00 49.85  ? 714 VAL A C   1 
ATOM 5500 O O   . VAL A 1 731 ? 100.826 119.812 112.275 1.00 49.85  ? 714 VAL A O   1 
ATOM 5501 C CB  . VAL A 1 731 ? 98.753  117.318 111.525 1.00 49.85  ? 714 VAL A CB  1 
ATOM 5502 C CG1 . VAL A 1 731 ? 100.180 116.806 111.646 1.00 49.85  ? 714 VAL A CG1 1 
ATOM 5503 C CG2 . VAL A 1 731 ? 97.824  116.510 112.413 1.00 49.85  ? 714 VAL A CG2 1 
ATOM 5504 N N   . THR A 1 732 ? 100.002 119.943 110.186 1.00 49.85  ? 715 THR A N   1 
ATOM 5505 C CA  . THR A 1 732 ? 101.142 120.718 109.707 1.00 49.85  ? 715 THR A CA  1 
ATOM 5506 C C   . THR A 1 732 ? 101.212 122.075 110.396 1.00 49.85  ? 715 THR A C   1 
ATOM 5507 O O   . THR A 1 732 ? 102.296 122.530 110.783 1.00 49.85  ? 715 THR A O   1 
ATOM 5508 C CB  . THR A 1 732 ? 101.061 120.886 108.188 1.00 49.85  ? 715 THR A CB  1 
ATOM 5509 O OG1 . THR A 1 732 ? 101.494 119.679 107.549 1.00 49.85  ? 715 THR A OG1 1 
ATOM 5510 C CG2 . THR A 1 732 ? 101.940 122.038 107.722 1.00 49.85  ? 715 THR A CG2 1 
ATOM 5511 N N   . ASN A 1 733 ? 100.061 122.734 110.564 1.00 49.85  ? 716 ASN A N   1 
ATOM 5512 C CA  . ASN A 1 733 ? 100.040 124.002 111.288 1.00 49.85  ? 716 ASN A CA  1 
ATOM 5513 C C   . ASN A 1 733 ? 100.532 123.827 112.719 1.00 49.85  ? 716 ASN A C   1 
ATOM 5514 O O   . ASN A 1 733 ? 101.318 124.641 113.218 1.00 49.85  ? 716 ASN A O   1 
ATOM 5515 C CB  . ASN A 1 733 ? 98.631  124.593 111.277 1.00 49.85  ? 716 ASN A CB  1 
ATOM 5516 C CG  . ASN A 1 733 ? 98.474  125.700 110.260 1.00 49.85  ? 716 ASN A CG  1 
ATOM 5517 O OD1 . ASN A 1 733 ? 98.564  126.882 110.592 1.00 49.85  ? 716 ASN A OD1 1 
ATOM 5518 N ND2 . ASN A 1 733 ? 98.240  125.325 109.011 1.00 49.85  ? 716 ASN A ND2 1 
ATOM 5519 N N   . TRP A 1 734 ? 100.078 122.769 113.394 1.00 49.85  ? 717 TRP A N   1 
ATOM 5520 C CA  . TRP A 1 734 ? 100.507 122.518 114.766 1.00 49.85  ? 717 TRP A CA  1 
ATOM 5521 C C   . TRP A 1 734 ? 102.006 122.259 114.839 1.00 49.85  ? 717 TRP A C   1 
ATOM 5522 O O   . TRP A 1 734 ? 102.688 122.759 115.741 1.00 49.85  ? 717 TRP A O   1 
ATOM 5523 C CB  . TRP A 1 734 ? 99.730  121.337 115.346 1.00 49.85  ? 717 TRP A CB  1 
ATOM 5524 C CG  . TRP A 1 734 ? 100.365 120.734 116.557 1.00 49.85  ? 717 TRP A CG  1 
ATOM 5525 C CD1 . TRP A 1 734 ? 100.550 121.333 117.766 1.00 49.85  ? 717 TRP A CD1 1 
ATOM 5526 C CD2 . TRP A 1 734 ? 100.898 119.410 116.679 1.00 49.85  ? 717 TRP A CD2 1 
ATOM 5527 N NE1 . TRP A 1 734 ? 101.167 120.466 118.635 1.00 49.85  ? 717 TRP A NE1 1 
ATOM 5528 C CE2 . TRP A 1 734 ? 101.392 119.278 117.992 1.00 49.85  ? 717 TRP A CE2 1 
ATOM 5529 C CE3 . TRP A 1 734 ? 101.007 118.323 115.807 1.00 49.85  ? 717 TRP A CE3 1 
ATOM 5530 C CZ2 . TRP A 1 734 ? 101.984 118.106 118.453 1.00 49.85  ? 717 TRP A CZ2 1 
ATOM 5531 C CZ3 . TRP A 1 734 ? 101.595 117.160 116.266 1.00 49.85  ? 717 TRP A CZ3 1 
ATOM 5532 C CH2 . TRP A 1 734 ? 102.076 117.060 117.576 1.00 49.85  ? 717 TRP A CH2 1 
ATOM 5533 N N   . LEU A 1 735 ? 102.535 121.472 113.899 1.00 49.85  ? 718 LEU A N   1 
ATOM 5534 C CA  . LEU A 1 735 ? 103.965 121.180 113.887 1.00 49.85  ? 718 LEU A CA  1 
ATOM 5535 C C   . LEU A 1 735 ? 104.788 122.438 113.648 1.00 49.85  ? 718 LEU A C   1 
ATOM 5536 O O   . LEU A 1 735 ? 105.813 122.654 114.305 1.00 49.85  ? 718 LEU A O   1 
ATOM 5537 C CB  . LEU A 1 735 ? 104.277 120.132 112.819 1.00 49.85  ? 718 LEU A CB  1 
ATOM 5538 C CG  . LEU A 1 735 ? 103.993 118.670 113.163 1.00 49.85  ? 718 LEU A CG  1 
ATOM 5539 C CD1 . LEU A 1 735 ? 104.645 117.751 112.145 1.00 49.85  ? 718 LEU A CD1 1 
ATOM 5540 C CD2 . LEU A 1 735 ? 104.485 118.349 114.563 1.00 49.85  ? 718 LEU A CD2 1 
ATOM 5541 N N   . ALA A 1 736 ? 104.358 123.281 112.709 1.00 49.85  ? 719 ALA A N   1 
ATOM 5542 C CA  . ALA A 1 736 ? 105.162 124.438 112.335 1.00 49.85  ? 719 ALA A CA  1 
ATOM 5543 C C   . ALA A 1 736 ? 105.076 125.558 113.365 1.00 49.85  ? 719 ALA A C   1 
ATOM 5544 O O   . ALA A 1 736 ? 106.081 126.221 113.644 1.00 49.85  ? 719 ALA A O   1 
ATOM 5545 C CB  . ALA A 1 736 ? 104.735 124.948 110.960 1.00 49.85  ? 719 ALA A CB  1 
ATOM 5546 N N   . LYS A 1 737 ? 103.896 125.789 113.942 1.00 49.85  ? 720 LYS A N   1 
ATOM 5547 C CA  . LYS A 1 737 ? 103.685 126.968 114.772 1.00 49.85  ? 720 LYS A CA  1 
ATOM 5548 C C   . LYS A 1 737 ? 103.727 126.692 116.269 1.00 49.85  ? 720 LYS A C   1 
ATOM 5549 O O   . LYS A 1 737 ? 103.888 127.639 117.047 1.00 49.85  ? 720 LYS A O   1 
ATOM 5550 C CB  . LYS A 1 737 ? 102.343 127.623 114.429 1.00 49.85  ? 720 LYS A CB  1 
ATOM 5551 C CG  . LYS A 1 737 ? 102.367 128.466 113.167 1.00 49.85  ? 720 LYS A CG  1 
ATOM 5552 C CD  . LYS A 1 737 ? 100.992 128.530 112.526 1.00 49.85  ? 720 LYS A CD  1 
ATOM 5553 C CE  . LYS A 1 737 ? 101.010 129.370 111.262 1.00 49.85  ? 720 LYS A CE  1 
ATOM 5554 N NZ  . LYS A 1 737 ? 99.712  129.307 110.536 1.00 49.85  ? 720 LYS A NZ  1 
ATOM 5555 N N   . VAL A 1 738 ? 103.587 125.437 116.699 1.00 49.85  ? 721 VAL A N   1 
ATOM 5556 C CA  . VAL A 1 738 ? 103.521 125.100 118.113 1.00 49.85  ? 721 VAL A CA  1 
ATOM 5557 C C   . VAL A 1 738 ? 104.652 124.170 118.532 1.00 49.85  ? 721 VAL A C   1 
ATOM 5558 O O   . VAL A 1 738 ? 105.280 124.381 119.576 1.00 49.85  ? 721 VAL A O   1 
ATOM 5559 C CB  . VAL A 1 738 ? 102.150 124.486 118.474 1.00 49.85  ? 721 VAL A CB  1 
ATOM 5560 C CG1 . VAL A 1 738 ? 102.269 123.552 119.671 1.00 49.85  ? 721 VAL A CG1 1 
ATOM 5561 C CG2 . VAL A 1 738 ? 101.135 125.581 118.741 1.00 49.85  ? 721 VAL A CG2 1 
ATOM 5562 N N   . ASN A 1 739 ? 104.938 123.141 117.729 1.00 49.85  ? 722 ASN A N   1 
ATOM 5563 C CA  . ASN A 1 739 ? 105.939 122.152 118.117 1.00 49.85  ? 722 ASN A CA  1 
ATOM 5564 C C   . ASN A 1 739 ? 107.319 122.782 118.267 1.00 49.85  ? 722 ASN A C   1 
ATOM 5565 O O   . ASN A 1 739 ? 108.090 122.396 119.152 1.00 49.85  ? 722 ASN A O   1 
ATOM 5566 C CB  . ASN A 1 739 ? 105.976 121.016 117.097 1.00 49.85  ? 722 ASN A CB  1 
ATOM 5567 C CG  . ASN A 1 739 ? 106.467 119.714 117.695 1.00 49.85  ? 722 ASN A CG  1 
ATOM 5568 O OD1 . ASN A 1 739 ? 105.909 119.219 118.674 1.00 49.85  ? 722 ASN A OD1 1 
ATOM 5569 N ND2 . ASN A 1 739 ? 107.516 119.150 117.108 1.00 49.85  ? 722 ASN A ND2 1 
ATOM 5570 N N   . THR A 1 740 ? 107.652 123.747 117.406 1.00 49.85  ? 723 THR A N   1 
ATOM 5571 C CA  . THR A 1 740 ? 108.949 124.410 117.505 1.00 49.85  ? 723 THR A CA  1 
ATOM 5572 C C   . THR A 1 740 ? 109.078 125.188 118.809 1.00 49.85  ? 723 THR A C   1 
ATOM 5573 O O   . THR A 1 740 ? 110.147 125.196 119.432 1.00 49.85  ? 723 THR A O   1 
ATOM 5574 C CB  . THR A 1 740 ? 109.160 125.336 116.309 1.00 49.85  ? 723 THR A CB  1 
ATOM 5575 O OG1 . THR A 1 740 ? 108.240 126.432 116.383 1.00 49.85  ? 723 THR A OG1 1 
ATOM 5576 C CG2 . THR A 1 740 ? 108.935 124.581 115.009 1.00 49.85  ? 723 THR A CG2 1 
ATOM 5577 N N   . GLN A 1 741 ? 108.002 125.856 119.233 1.00 49.85  ? 724 GLN A N   1 
ATOM 5578 C CA  . GLN A 1 741 ? 108.035 126.593 120.492 1.00 49.85  ? 724 GLN A CA  1 
ATOM 5579 C C   . GLN A 1 741 ? 108.273 125.656 121.669 1.00 49.85  ? 724 GLN A C   1 
ATOM 5580 O O   . GLN A 1 741 ? 109.079 125.954 122.559 1.00 49.85  ? 724 GLN A O   1 
ATOM 5581 C CB  . GLN A 1 741 ? 106.730 127.364 120.678 1.00 49.85  ? 724 GLN A CB  1 
ATOM 5582 C CG  . GLN A 1 741 ? 106.507 128.467 119.661 1.00 49.85  ? 724 GLN A CG  1 
ATOM 5583 C CD  . GLN A 1 741 ? 105.233 129.244 119.919 1.00 49.85  ? 724 GLN A CD  1 
ATOM 5584 O OE1 . GLN A 1 741 ? 105.049 129.818 120.992 1.00 49.85  ? 724 GLN A OE1 1 
ATOM 5585 N NE2 . GLN A 1 741 ? 104.341 129.261 118.936 1.00 49.85  ? 724 GLN A NE2 1 
ATOM 5586 N N   . ILE A 1 742 ? 107.588 124.511 121.683 1.00 49.85  ? 725 ILE A N   1 
ATOM 5587 C CA  . ILE A 1 742 ? 107.768 123.548 122.763 1.00 49.85  ? 725 ILE A CA  1 
ATOM 5588 C C   . ILE A 1 742 ? 109.174 122.963 122.727 1.00 49.85  ? 725 ILE A C   1 
ATOM 5589 O O   . ILE A 1 742 ? 109.789 122.728 123.772 1.00 49.85  ? 725 ILE A O   1 
ATOM 5590 C CB  . ILE A 1 742 ? 106.688 122.453 122.684 1.00 49.85  ? 725 ILE A CB  1 
ATOM 5591 C CG1 . ILE A 1 742 ? 105.302 123.060 122.904 1.00 49.85  ? 725 ILE A CG1 1 
ATOM 5592 C CG2 . ILE A 1 742 ? 106.949 121.362 123.706 1.00 49.85  ? 725 ILE A CG2 1 
ATOM 5593 C CD1 . ILE A 1 742 ? 105.112 123.669 124.275 1.00 49.85  ? 725 ILE A CD1 1 
ATOM 5594 N N   . ASP A 1 743 ? 109.709 122.724 121.527 1.00 49.85  ? 726 ASP A N   1 
ATOM 5595 C CA  . ASP A 1 743 ? 111.072 122.211 121.413 1.00 49.85  ? 726 ASP A CA  1 
ATOM 5596 C C   . ASP A 1 743 ? 112.083 123.202 121.974 1.00 49.85  ? 726 ASP A C   1 
ATOM 5597 O O   . ASP A 1 743 ? 113.001 122.819 122.713 1.00 49.85  ? 726 ASP A O   1 
ATOM 5598 C CB  . ASP A 1 743 ? 111.390 121.896 119.952 1.00 49.85  ? 726 ASP A CB  1 
ATOM 5599 C CG  . ASP A 1 743 ? 111.027 120.477 119.568 1.00 49.85  ? 726 ASP A CG  1 
ATOM 5600 O OD1 . ASP A 1 743 ? 110.307 119.817 120.345 1.00 49.85  ? 726 ASP A OD1 1 
ATOM 5601 O OD2 . ASP A 1 743 ? 111.462 120.022 118.489 1.00 49.85  ? 726 ASP A OD2 1 
ATOM 5602 N N   . LEU A 1 744 ? 111.932 124.484 121.634 1.00 49.85  ? 727 LEU A N   1 
ATOM 5603 C CA  . LEU A 1 744 ? 112.843 125.495 122.161 1.00 49.85  ? 727 LEU A CA  1 
ATOM 5604 C C   . LEU A 1 744 ? 112.699 125.629 123.671 1.00 49.85  ? 727 LEU A C   1 
ATOM 5605 O O   . LEU A 1 744 ? 113.693 125.820 124.381 1.00 49.85  ? 727 LEU A O   1 
ATOM 5606 C CB  . LEU A 1 744 ? 112.603 126.840 121.478 1.00 49.85  ? 727 LEU A CB  1 
ATOM 5607 C CG  . LEU A 1 744 ? 113.552 127.949 121.934 1.00 49.85  ? 727 LEU A CG  1 
ATOM 5608 C CD1 . LEU A 1 744 ? 115.000 127.519 121.759 1.00 49.85  ? 727 LEU A CD1 1 
ATOM 5609 C CD2 . LEU A 1 744 ? 113.284 129.237 121.186 1.00 49.85  ? 727 LEU A CD2 1 
ATOM 5610 N N   . ILE A 1 745 ? 111.469 125.534 124.180 1.00 49.85  ? 728 ILE A N   1 
ATOM 5611 C CA  . ILE A 1 745 ? 111.256 125.596 125.623 1.00 49.85  ? 728 ILE A CA  1 
ATOM 5612 C C   . ILE A 1 745 ? 111.935 124.419 126.312 1.00 49.85  ? 728 ILE A C   1 
ATOM 5613 O O   . ILE A 1 745 ? 112.547 124.572 127.376 1.00 49.85  ? 728 ILE A O   1 
ATOM 5614 C CB  . ILE A 1 745 ? 109.748 125.653 125.934 1.00 49.85  ? 728 ILE A CB  1 
ATOM 5615 C CG1 . ILE A 1 745 ? 109.217 127.069 125.707 1.00 49.85  ? 728 ILE A CG1 1 
ATOM 5616 C CG2 . ILE A 1 745 ? 109.466 125.196 127.356 1.00 49.85  ? 728 ILE A CG2 1 
ATOM 5617 C CD1 . ILE A 1 745 ? 107.714 127.146 125.599 1.00 49.85  ? 728 ILE A CD1 1 
ATOM 5618 N N   . ARG A 1 746 ? 111.847 123.231 125.713 1.00 49.85  ? 729 ARG A N   1 
ATOM 5619 C CA  . ARG A 1 746 ? 112.510 122.055 126.270 1.00 49.85  ? 729 ARG A CA  1 
ATOM 5620 C C   . ARG A 1 746 ? 114.022 122.238 126.297 1.00 49.85  ? 729 ARG A C   1 
ATOM 5621 O O   . ARG A 1 746 ? 114.682 121.945 127.304 1.00 49.85  ? 729 ARG A O   1 
ATOM 5622 C CB  . ARG A 1 746 ? 112.131 120.821 125.450 1.00 49.85  ? 729 ARG A CB  1 
ATOM 5623 C CG  . ARG A 1 746 ? 112.084 119.528 126.234 1.00 49.85  ? 729 ARG A CG  1 
ATOM 5624 C CD  . ARG A 1 746 ? 110.911 118.671 125.786 1.00 49.85  ? 729 ARG A CD  1 
ATOM 5625 N NE  . ARG A 1 746 ? 110.540 118.922 124.399 1.00 49.85  ? 729 ARG A NE  1 
ATOM 5626 C CZ  . ARG A 1 746 ? 110.854 118.126 123.385 1.00 49.85  ? 729 ARG A CZ  1 
ATOM 5627 N NH1 . ARG A 1 746 ? 111.557 117.021 123.566 1.00 49.85  ? 729 ARG A NH1 1 
ATOM 5628 N NH2 . ARG A 1 746 ? 110.450 118.448 122.160 1.00 49.85  ? 729 ARG A NH2 1 
ATOM 5629 N N   . LYS A 1 747 ? 114.587 122.730 125.192 1.00 49.85  ? 730 LYS A N   1 
ATOM 5630 C CA  . LYS A 1 747 ? 116.029 122.947 125.132 1.00 49.85  ? 730 LYS A CA  1 
ATOM 5631 C C   . LYS A 1 747 ? 116.474 123.980 126.159 1.00 49.85  ? 730 LYS A C   1 
ATOM 5632 O O   . LYS A 1 747 ? 117.504 123.808 126.822 1.00 49.85  ? 730 LYS A O   1 
ATOM 5633 C CB  . LYS A 1 747 ? 116.436 123.380 123.725 1.00 49.85  ? 730 LYS A CB  1 
ATOM 5634 C CG  . LYS A 1 747 ? 116.647 122.230 122.756 1.00 49.85  ? 730 LYS A CG  1 
ATOM 5635 C CD  . LYS A 1 747 ? 117.145 122.733 121.413 1.00 49.85  ? 730 LYS A CD  1 
ATOM 5636 C CE  . LYS A 1 747 ? 116.069 122.606 120.348 1.00 49.85  ? 730 LYS A CE  1 
ATOM 5637 N NZ  . LYS A 1 747 ? 116.438 123.320 119.096 1.00 49.85  ? 730 LYS A NZ  1 
ATOM 5638 N N   . LYS A 1 748 ? 115.702 125.058 126.315 1.00 49.85  ? 731 LYS A N   1 
ATOM 5639 C CA  . LYS A 1 748 ? 116.070 126.093 127.273 1.00 49.85  ? 731 LYS A CA  1 
ATOM 5640 C C   . LYS A 1 748 ? 115.910 125.615 128.709 1.00 49.85  ? 731 LYS A C   1 
ATOM 5641 O O   . LYS A 1 748 ? 116.687 126.017 129.580 1.00 49.85  ? 731 LYS A O   1 
ATOM 5642 C CB  . LYS A 1 748 ? 115.244 127.352 127.022 1.00 49.85  ? 731 LYS A CB  1 
ATOM 5643 C CG  . LYS A 1 748 ? 115.741 128.153 125.834 1.00 49.85  ? 731 LYS A CG  1 
ATOM 5644 C CD  . LYS A 1 748 ? 114.986 129.453 125.672 1.00 49.85  ? 731 LYS A CD  1 
ATOM 5645 C CE  . LYS A 1 748 ? 115.392 130.152 124.388 1.00 49.85  ? 731 LYS A CE  1 
ATOM 5646 N NZ  . LYS A 1 748 ? 116.872 130.200 124.229 1.00 49.85  ? 731 LYS A NZ  1 
ATOM 5647 N N   . MET A 1 749 ? 114.924 124.758 128.981 1.00 49.85  ? 732 MET A N   1 
ATOM 5648 C CA  . MET A 1 749 ? 114.812 124.170 130.311 1.00 49.85  ? 732 MET A CA  1 
ATOM 5649 C C   . MET A 1 749 ? 115.997 123.262 130.613 1.00 49.85  ? 732 MET A C   1 
ATOM 5650 O O   . MET A 1 749 ? 116.524 123.270 131.733 1.00 49.85  ? 732 MET A O   1 
ATOM 5651 C CB  . MET A 1 749 ? 113.499 123.401 130.441 1.00 49.85  ? 732 MET A CB  1 
ATOM 5652 C CG  . MET A 1 749 ? 113.186 123.001 131.867 1.00 49.85  ? 732 MET A CG  1 
ATOM 5653 S SD  . MET A 1 749 ? 112.525 124.372 132.824 1.00 49.85  ? 732 MET A SD  1 
ATOM 5654 C CE  . MET A 1 749 ? 112.436 123.622 134.443 1.00 49.85  ? 732 MET A CE  1 
ATOM 5655 N N   . LYS A 1 750 ? 116.427 122.470 129.628 1.00 49.85  ? 733 LYS A N   1 
ATOM 5656 C CA  . LYS A 1 750 ? 117.627 121.659 129.812 1.00 49.85  ? 733 LYS A CA  1 
ATOM 5657 C C   . LYS A 1 750 ? 118.843 122.538 130.078 1.00 49.85  ? 733 LYS A C   1 
ATOM 5658 O O   . LYS A 1 750 ? 119.664 122.235 130.956 1.00 49.85  ? 733 LYS A O   1 
ATOM 5659 C CB  . LYS A 1 750 ? 117.856 120.778 128.584 1.00 49.85  ? 733 LYS A CB  1 
ATOM 5660 C CG  . LYS A 1 750 ? 119.234 120.142 128.516 1.00 49.85  ? 733 LYS A CG  1 
ATOM 5661 C CD  . LYS A 1 750 ? 119.406 119.077 129.585 1.00 49.85  ? 733 LYS A CD  1 
ATOM 5662 C CE  . LYS A 1 750 ? 120.774 118.422 129.491 1.00 49.85  ? 733 LYS A CE  1 
ATOM 5663 N NZ  . LYS A 1 750 ? 120.956 117.704 128.200 1.00 49.85  ? 733 LYS A NZ  1 
ATOM 5664 N N   . GLU A 1 751 ? 118.967 123.640 129.334 1.00 50.43  ? 734 GLU A N   1 
ATOM 5665 C CA  . GLU A 1 751 ? 120.076 124.564 129.547 1.00 50.43  ? 734 GLU A CA  1 
ATOM 5666 C C   . GLU A 1 751 ? 120.030 125.173 130.943 1.00 50.43  ? 734 GLU A C   1 
ATOM 5667 O O   . GLU A 1 751 ? 121.067 125.311 131.600 1.00 50.43  ? 734 GLU A O   1 
ATOM 5668 C CB  . GLU A 1 751 ? 120.056 125.659 128.479 1.00 50.43  ? 734 GLU A CB  1 
ATOM 5669 C CG  . GLU A 1 751 ? 120.785 126.933 128.873 1.00 50.43  ? 734 GLU A CG  1 
ATOM 5670 C CD  . GLU A 1 751 ? 121.164 127.782 127.676 1.00 50.43  ? 734 GLU A CD  1 
ATOM 5671 O OE1 . GLU A 1 751 ? 120.781 127.421 126.543 1.00 50.43  ? 734 GLU A OE1 1 
ATOM 5672 O OE2 . GLU A 1 751 ? 121.846 128.811 127.867 1.00 50.43  ? 734 GLU A OE2 1 
ATOM 5673 N N   . ALA A 1 752 ? 118.837 125.543 131.413 1.00 49.85  ? 735 ALA A N   1 
ATOM 5674 C CA  . ALA A 1 752 ? 118.706 126.119 132.749 1.00 49.85  ? 735 ALA A CA  1 
ATOM 5675 C C   . ALA A 1 752 ? 119.067 125.107 133.830 1.00 49.85  ? 735 ALA A C   1 
ATOM 5676 O O   . ALA A 1 752 ? 119.724 125.455 134.821 1.00 49.85  ? 735 ALA A O   1 
ATOM 5677 C CB  . ALA A 1 752 ? 117.285 126.642 132.955 1.00 49.85  ? 735 ALA A CB  1 
ATOM 5678 N N   . LEU A 1 753 ? 118.638 123.854 133.667 1.00 49.85  ? 736 LEU A N   1 
ATOM 5679 C CA  . LEU A 1 753 ? 119.000 122.823 134.636 1.00 49.85  ? 736 LEU A CA  1 
ATOM 5680 C C   . LEU A 1 753 ? 120.508 122.600 134.663 1.00 49.85  ? 736 LEU A C   1 
ATOM 5681 O O   . LEU A 1 753 ? 121.111 122.485 135.741 1.00 49.85  ? 736 LEU A O   1 
ATOM 5682 C CB  . LEU A 1 753 ? 118.269 121.520 134.312 1.00 49.85  ? 736 LEU A CB  1 
ATOM 5683 C CG  . LEU A 1 753 ? 116.818 121.427 134.784 1.00 49.85  ? 736 LEU A CG  1 
ATOM 5684 C CD1 . LEU A 1 753 ? 116.182 120.130 134.311 1.00 49.85  ? 736 LEU A CD1 1 
ATOM 5685 C CD2 . LEU A 1 753 ? 116.744 121.547 136.297 1.00 49.85  ? 736 LEU A CD2 1 
ATOM 5686 N N   . GLU A 1 754 ? 121.137 122.547 133.486 1.00 49.94  ? 737 GLU A N   1 
ATOM 5687 C CA  . GLU A 1 754 ? 122.587 122.398 133.435 1.00 49.94  ? 737 GLU A CA  1 
ATOM 5688 C C   . GLU A 1 754 ? 123.284 123.600 134.061 1.00 49.94  ? 737 GLU A C   1 
ATOM 5689 O O   . GLU A 1 754 ? 124.319 123.453 134.719 1.00 49.94  ? 737 GLU A O   1 
ATOM 5690 C CB  . GLU A 1 754 ? 123.046 122.200 131.991 1.00 49.94  ? 737 GLU A CB  1 
ATOM 5691 C CG  . GLU A 1 754 ? 122.900 120.774 131.489 1.00 49.94  ? 737 GLU A CG  1 
ATOM 5692 C CD  . GLU A 1 754 ? 123.483 120.582 130.103 1.00 49.94  ? 737 GLU A CD  1 
ATOM 5693 O OE1 . GLU A 1 754 ? 123.463 121.547 129.310 1.00 49.94  ? 737 GLU A OE1 1 
ATOM 5694 O OE2 . GLU A 1 754 ? 123.959 119.467 129.806 1.00 49.94  ? 737 GLU A OE2 1 
ATOM 5695 N N   . ASN A 1 755 ? 122.730 124.798 133.864 1.00 49.85  ? 738 ASN A N   1 
ATOM 5696 C CA  . ASN A 1 755 ? 123.302 125.996 134.467 1.00 49.85  ? 738 ASN A CA  1 
ATOM 5697 C C   . ASN A 1 755 ? 123.226 125.937 135.986 1.00 49.85  ? 738 ASN A C   1 
ATOM 5698 O O   . ASN A 1 755 ? 124.183 126.304 136.677 1.00 49.85  ? 738 ASN A O   1 
ATOM 5699 C CB  . ASN A 1 755 ? 122.579 127.236 133.945 1.00 49.85  ? 738 ASN A CB  1 
ATOM 5700 C CG  . ASN A 1 755 ? 123.222 127.805 132.699 1.00 49.85  ? 738 ASN A CG  1 
ATOM 5701 O OD1 . ASN A 1 755 ? 124.217 127.277 132.203 1.00 49.85  ? 738 ASN A OD1 1 
ATOM 5702 N ND2 . ASN A 1 755 ? 122.650 128.883 132.178 1.00 49.85  ? 738 ASN A ND2 1 
ATOM 5703 N N   . GLN A 1 756 ? 122.091 125.487 136.524 1.00 49.85  ? 739 GLN A N   1 
ATOM 5704 C CA  . GLN A 1 756 ? 121.965 125.347 137.973 1.00 49.85  ? 739 GLN A CA  1 
ATOM 5705 C C   . GLN A 1 756 ? 122.955 124.322 138.513 1.00 49.85  ? 739 GLN A C   1 
ATOM 5706 O O   . GLN A 1 756 ? 123.580 124.537 139.563 1.00 49.85  ? 739 GLN A O   1 
ATOM 5707 C CB  . GLN A 1 756 ? 120.534 124.957 138.340 1.00 49.85  ? 739 GLN A CB  1 
ATOM 5708 C CG  . GLN A 1 756 ? 119.606 126.136 138.569 1.00 49.85  ? 739 GLN A CG  1 
ATOM 5709 C CD  . GLN A 1 756 ? 119.936 126.899 139.834 1.00 49.85  ? 739 GLN A CD  1 
ATOM 5710 O OE1 . GLN A 1 756 ? 120.231 128.092 139.793 1.00 49.85  ? 739 GLN A OE1 1 
ATOM 5711 N NE2 . GLN A 1 756 ? 119.892 126.211 140.968 1.00 49.85  ? 739 GLN A NE2 1 
ATOM 5712 N N   . ALA A 1 757 ? 123.103 123.194 137.811 1.00 49.85  ? 740 ALA A N   1 
ATOM 5713 C CA  . ALA A 1 757 ? 124.070 122.185 138.231 1.00 49.85  ? 740 ALA A CA  1 
ATOM 5714 C C   . ALA A 1 757 ? 125.487 122.743 138.216 1.00 49.85  ? 740 ALA A C   1 
ATOM 5715 O O   . ALA A 1 757 ? 126.265 122.514 139.150 1.00 49.85  ? 740 ALA A O   1 
ATOM 5716 C CB  . ALA A 1 757 ? 123.966 120.952 137.334 1.00 49.85  ? 740 ALA A CB  1 
ATOM 5717 N N   . GLU A 1 758 ? 125.837 123.489 137.166 1.00 60.31  ? 741 GLU A N   1 
ATOM 5718 C CA  . GLU A 1 758 ? 127.159 124.099 137.095 1.00 60.31  ? 741 GLU A CA  1 
ATOM 5719 C C   . GLU A 1 758 ? 127.362 125.105 138.220 1.00 60.31  ? 741 GLU A C   1 
ATOM 5720 O O   . GLU A 1 758 ? 128.454 125.197 138.788 1.00 60.31  ? 741 GLU A O   1 
ATOM 5721 C CB  . GLU A 1 758 ? 127.355 124.768 135.734 1.00 60.31  ? 741 GLU A CB  1 
ATOM 5722 C CG  . GLU A 1 758 ? 128.717 124.517 135.107 1.00 60.31  ? 741 GLU A CG  1 
ATOM 5723 C CD  . GLU A 1 758 ? 129.047 125.516 134.015 1.00 60.31  ? 741 GLU A CD  1 
ATOM 5724 O OE1 . GLU A 1 758 ? 128.226 126.426 133.772 1.00 60.31  ? 741 GLU A OE1 1 
ATOM 5725 O OE2 . GLU A 1 758 ? 130.127 125.393 133.400 1.00 60.31  ? 741 GLU A OE2 1 
ATOM 5726 N N   . ALA A 1 759 ? 126.318 125.865 138.558 1.00 50.64  ? 742 ALA A N   1 
ATOM 5727 C CA  . ALA A 1 759 ? 126.434 126.856 139.623 1.00 50.64  ? 742 ALA A CA  1 
ATOM 5728 C C   . ALA A 1 759 ? 126.698 126.192 140.970 1.00 50.64  ? 742 ALA A C   1 
ATOM 5729 O O   . ALA A 1 759 ? 127.612 126.592 141.704 1.00 50.64  ? 742 ALA A O   1 
ATOM 5730 C CB  . ALA A 1 759 ? 125.171 127.713 139.681 1.00 50.64  ? 742 ALA A CB  1 
ATOM 5731 N N   . THR A 1 760 ? 125.910 125.169 141.316 1.00 49.85  ? 743 THR A N   1 
ATOM 5732 C CA  . THR A 1 760 ? 126.132 124.512 142.604 1.00 49.85  ? 743 THR A CA  1 
ATOM 5733 C C   . THR A 1 760 ? 127.474 123.787 142.624 1.00 49.85  ? 743 THR A C   1 
ATOM 5734 O O   . THR A 1 760 ? 128.151 123.746 143.663 1.00 49.85  ? 743 THR A O   1 
ATOM 5735 C CB  . THR A 1 760 ? 124.988 123.550 142.940 1.00 49.85  ? 743 THR A CB  1 
ATOM 5736 O OG1 . THR A 1 760 ? 125.347 122.768 144.085 1.00 49.85  ? 743 THR A OG1 1 
ATOM 5737 C CG2 . THR A 1 760 ? 124.698 122.616 141.790 1.00 49.85  ? 743 THR A CG2 1 
ATOM 5738 N N   . LYS A 1 761 ? 127.887 123.226 141.481 1.00 54.03  ? 744 LYS A N   1 
ATOM 5739 C CA  . LYS A 1 761 ? 129.203 122.603 141.398 1.00 54.03  ? 744 LYS A CA  1 
ATOM 5740 C C   . LYS A 1 761 ? 130.307 123.625 141.628 1.00 54.03  ? 744 LYS A C   1 
ATOM 5741 O O   . LYS A 1 761 ? 131.294 123.340 142.315 1.00 54.03  ? 744 LYS A O   1 
ATOM 5742 C CB  . LYS A 1 761 ? 129.370 121.922 140.041 1.00 54.03  ? 744 LYS A CB  1 
ATOM 5743 C CG  . LYS A 1 761 ? 128.847 120.500 140.006 1.00 54.03  ? 744 LYS A CG  1 
ATOM 5744 C CD  . LYS A 1 761 ? 129.307 119.768 138.762 1.00 54.03  ? 744 LYS A CD  1 
ATOM 5745 C CE  . LYS A 1 761 ? 128.518 120.201 137.540 1.00 54.03  ? 744 LYS A CE  1 
ATOM 5746 N NZ  . LYS A 1 761 ? 128.817 119.343 136.360 1.00 54.03  ? 744 LYS A NZ  1 
ATOM 5747 N N   . ALA A 1 762 ? 130.156 124.825 141.065 1.00 50.17  ? 745 ALA A N   1 
ATOM 5748 C CA  . ALA A 1 762 ? 131.136 125.879 141.293 1.00 50.17  ? 745 ALA A CA  1 
ATOM 5749 C C   . ALA A 1 762 ? 131.174 126.284 142.760 1.00 50.17  ? 745 ALA A C   1 
ATOM 5750 O O   . ALA A 1 762 ? 132.251 126.536 143.312 1.00 50.17  ? 745 ALA A O   1 
ATOM 5751 C CB  . ALA A 1 762 ? 130.827 127.086 140.409 1.00 50.17  ? 745 ALA A CB  1 
ATOM 5752 N N   . ILE A 1 763 ? 130.009 126.354 143.409 1.00 51.67  ? 746 ILE A N   1 
ATOM 5753 C CA  . ILE A 1 763 ? 129.980 126.723 144.825 1.00 51.67  ? 746 ILE A CA  1 
ATOM 5754 C C   . ILE A 1 763 ? 130.729 125.693 145.664 1.00 51.67  ? 746 ILE A C   1 
ATOM 5755 O O   . ILE A 1 763 ? 131.561 126.042 146.514 1.00 51.67  ? 746 ILE A O   1 
ATOM 5756 C CB  . ILE A 1 763 ? 128.532 126.901 145.318 1.00 51.67  ? 746 ILE A CB  1 
ATOM 5757 C CG1 . ILE A 1 763 ? 127.796 127.945 144.480 1.00 51.67  ? 746 ILE A CG1 1 
ATOM 5758 C CG2 . ILE A 1 763 ? 128.517 127.302 146.785 1.00 51.67  ? 746 ILE A CG2 1 
ATOM 5759 C CD1 . ILE A 1 763 ? 126.300 127.729 144.419 1.00 51.67  ? 746 ILE A CD1 1 
ATOM 5760 N N   . ILE A 1 764 ? 130.447 124.405 145.443 1.00 58.05  ? 747 ILE A N   1 
ATOM 5761 C CA  . ILE A 1 764 ? 131.120 123.395 146.258 1.00 58.05  ? 747 ILE A CA  1 
ATOM 5762 C C   . ILE A 1 764 ? 132.605 123.324 145.921 1.00 58.05  ? 747 ILE A C   1 
ATOM 5763 O O   . ILE A 1 764 ? 133.431 123.066 146.803 1.00 58.05  ? 747 ILE A O   1 
ATOM 5764 C CB  . ILE A 1 764 ? 130.448 122.015 146.133 1.00 58.05  ? 747 ILE A CB  1 
ATOM 5765 C CG1 . ILE A 1 764 ? 130.216 121.639 144.674 1.00 58.05  ? 747 ILE A CG1 1 
ATOM 5766 C CG2 . ILE A 1 764 ? 129.148 121.988 146.920 1.00 58.05  ? 747 ILE A CG2 1 
ATOM 5767 C CD1 . ILE A 1 764 ? 129.281 120.473 144.496 1.00 58.05  ? 747 ILE A CD1 1 
ATOM 5768 N N   . ASN A 1 765 ? 132.977 123.547 144.656 1.00 70.80  ? 748 ASN A N   1 
ATOM 5769 C CA  . ASN A 1 765 ? 134.393 123.588 144.305 1.00 70.80  ? 748 ASN A CA  1 
ATOM 5770 C C   . ASN A 1 765 ? 135.101 124.738 145.009 1.00 70.80  ? 748 ASN A C   1 
ATOM 5771 O O   . ASN A 1 765 ? 136.225 124.577 145.497 1.00 70.80  ? 748 ASN A O   1 
ATOM 5772 C CB  . ASN A 1 765 ? 134.560 123.710 142.791 1.00 70.80  ? 748 ASN A CB  1 
ATOM 5773 C CG  . ASN A 1 765 ? 135.897 123.182 142.308 1.00 70.80  ? 748 ASN A CG  1 
ATOM 5774 O OD1 . ASN A 1 765 ? 136.919 123.343 142.974 1.00 70.80  ? 748 ASN A OD1 1 
ATOM 5775 N ND2 . ASN A 1 765 ? 135.899 122.557 141.136 1.00 70.80  ? 748 ASN A ND2 1 
ATOM 5776 N N   . TYR A 1 766 ? 134.461 125.908 145.065 1.00 72.63  ? 749 TYR A N   1 
ATOM 5777 C CA  . TYR A 1 766 ? 135.051 127.038 145.773 1.00 72.63  ? 749 TYR A CA  1 
ATOM 5778 C C   . TYR A 1 766 ? 135.199 126.734 147.257 1.00 72.63  ? 749 TYR A C   1 
ATOM 5779 O O   . TYR A 1 766 ? 136.213 127.085 147.872 1.00 72.63  ? 749 TYR A O   1 
ATOM 5780 C CB  . TYR A 1 766 ? 134.203 128.292 145.569 1.00 72.63  ? 749 TYR A CB  1 
ATOM 5781 C CG  . TYR A 1 766 ? 134.433 129.350 146.624 1.00 72.63  ? 749 TYR A CG  1 
ATOM 5782 C CD1 . TYR A 1 766 ? 135.594 130.110 146.630 1.00 72.63  ? 749 TYR A CD1 1 
ATOM 5783 C CD2 . TYR A 1 766 ? 133.495 129.579 147.621 1.00 72.63  ? 749 TYR A CD2 1 
ATOM 5784 C CE1 . TYR A 1 766 ? 135.811 131.075 147.595 1.00 72.63  ? 749 TYR A CE1 1 
ATOM 5785 C CE2 . TYR A 1 766 ? 133.704 130.540 148.591 1.00 72.63  ? 749 TYR A CE2 1 
ATOM 5786 C CZ  . TYR A 1 766 ? 134.863 131.286 148.572 1.00 72.63  ? 749 TYR A CZ  1 
ATOM 5787 O OH  . TYR A 1 766 ? 135.075 132.246 149.535 1.00 72.63  ? 749 TYR A OH  1 
ATOM 5788 N N   . GLN A 1 767 ? 134.192 126.091 147.853 1.00 78.80  ? 750 GLN A N   1 
ATOM 5789 C CA  . GLN A 1 767 ? 134.295 125.721 149.262 1.00 78.80  ? 750 GLN A CA  1 
ATOM 5790 C C   . GLN A 1 767 ? 135.434 124.734 149.493 1.00 78.80  ? 750 GLN A C   1 
ATOM 5791 O O   . GLN A 1 767 ? 136.182 124.855 150.470 1.00 78.80  ? 750 GLN A O   1 
ATOM 5792 C CB  . GLN A 1 767 ? 132.969 125.139 149.754 1.00 78.80  ? 750 GLN A CB  1 
ATOM 5793 C CG  . GLN A 1 767 ? 132.974 124.681 151.213 1.00 78.80  ? 750 GLN A CG  1 
ATOM 5794 C CD  . GLN A 1 767 ? 133.234 125.802 152.211 1.00 78.80  ? 750 GLN A CD  1 
ATOM 5795 O OE1 . GLN A 1 767 ? 133.296 126.978 151.852 1.00 78.80  ? 750 GLN A OE1 1 
ATOM 5796 N NE2 . GLN A 1 767 ? 133.391 125.433 153.476 1.00 78.80  ? 750 GLN A NE2 1 
ATOM 5797 N N   . TYR A 1 768 ? 135.578 123.750 148.603 1.00 86.64  ? 751 TYR A N   1 
ATOM 5798 C CA  . TYR A 1 768 ? 136.644 122.763 148.745 1.00 86.64  ? 751 TYR A CA  1 
ATOM 5799 C C   . TYR A 1 768 ? 138.017 123.404 148.585 1.00 86.64  ? 751 TYR A C   1 
ATOM 5800 O O   . TYR A 1 768 ? 138.966 123.041 149.289 1.00 86.64  ? 751 TYR A O   1 
ATOM 5801 C CB  . TYR A 1 768 ? 136.448 121.640 147.726 1.00 86.64  ? 751 TYR A CB  1 
ATOM 5802 C CG  . TYR A 1 768 ? 137.576 120.634 147.672 1.00 86.64  ? 751 TYR A CG  1 
ATOM 5803 C CD1 . TYR A 1 768 ? 138.038 120.013 148.825 1.00 86.64  ? 751 TYR A CD1 1 
ATOM 5804 C CD2 . TYR A 1 768 ? 138.173 120.299 146.464 1.00 86.64  ? 751 TYR A CD2 1 
ATOM 5805 C CE1 . TYR A 1 768 ? 139.066 119.090 148.776 1.00 86.64  ? 751 TYR A CE1 1 
ATOM 5806 C CE2 . TYR A 1 768 ? 139.200 119.378 146.406 1.00 86.64  ? 751 TYR A CE2 1 
ATOM 5807 C CZ  . TYR A 1 768 ? 139.643 118.777 147.563 1.00 86.64  ? 751 TYR A CZ  1 
ATOM 5808 O OH  . TYR A 1 768 ? 140.665 117.859 147.505 1.00 86.64  ? 751 TYR A OH  1 
ATOM 5809 N N   . ASN A 1 769 ? 138.142 124.358 147.659 1.00 86.42  ? 752 ASN A N   1 
ATOM 5810 C CA  . ASN A 1 769 ? 139.415 125.036 147.434 1.00 86.42  ? 752 ASN A CA  1 
ATOM 5811 C C   . ASN A 1 769 ? 139.878 125.820 148.657 1.00 86.42  ? 752 ASN A C   1 
ATOM 5812 O O   . ASN A 1 769 ? 141.078 126.083 148.796 1.00 86.42  ? 752 ASN A O   1 
ATOM 5813 C CB  . ASN A 1 769 ? 139.294 125.956 146.214 1.00 86.42  ? 752 ASN A CB  1 
ATOM 5814 C CG  . ASN A 1 769 ? 140.285 127.104 146.239 1.00 86.42  ? 752 ASN A CG  1 
ATOM 5815 O OD1 . ASN A 1 769 ? 139.932 128.237 146.568 1.00 86.42  ? 752 ASN A OD1 1 
ATOM 5816 N ND2 . ASN A 1 769 ? 141.534 126.816 145.894 1.00 86.42  ? 752 ASN A ND2 1 
ATOM 5817 N N   . GLN A 1 770 ? 138.966 126.159 149.566 1.00 87.94  ? 753 GLN A N   1 
ATOM 5818 C CA  . GLN A 1 770 ? 139.274 126.968 150.736 1.00 87.94  ? 753 GLN A CA  1 
ATOM 5819 C C   . GLN A 1 770 ? 139.999 126.166 151.819 1.00 87.94  ? 753 GLN A C   1 
ATOM 5820 O O   . GLN A 1 770 ? 140.570 126.756 152.741 1.00 87.94  ? 753 GLN A O   1 
ATOM 5821 C CB  . GLN A 1 770 ? 137.970 127.601 151.253 1.00 87.94  ? 753 GLN A CB  1 
ATOM 5822 C CG  . GLN A 1 770 ? 138.054 128.782 152.241 1.00 87.94  ? 753 GLN A CG  1 
ATOM 5823 C CD  . GLN A 1 770 ? 138.508 128.411 153.641 1.00 87.94  ? 753 GLN A CD  1 
ATOM 5824 O OE1 . GLN A 1 770 ? 138.354 127.270 154.077 1.00 87.94  ? 753 GLN A OE1 1 
ATOM 5825 N NE2 . GLN A 1 770 ? 139.080 129.376 154.351 1.00 87.94  ? 753 GLN A NE2 1 
ATOM 5826 N N   . TYR A 1 771 ? 140.091 124.850 151.663 1.00 95.76  ? 754 TYR A N   1 
ATOM 5827 C CA  . TYR A 1 771 ? 140.634 123.967 152.684 1.00 95.76  ? 754 TYR A CA  1 
ATOM 5828 C C   . TYR A 1 771 ? 142.159 123.946 152.604 1.00 95.76  ? 754 TYR A C   1 
ATOM 5829 O O   . TYR A 1 771 ? 142.779 124.659 151.810 1.00 95.76  ? 754 TYR A O   1 
ATOM 5830 C CB  . TYR A 1 771 ? 140.068 122.554 152.528 1.00 95.76  ? 754 TYR A CB  1 
ATOM 5831 C CG  . TYR A 1 771 ? 138.599 122.434 152.856 1.00 95.76  ? 754 TYR A CG  1 
ATOM 5832 C CD1 . TYR A 1 771 ? 138.068 123.015 154.000 1.00 95.76  ? 754 TYR A CD1 1 
ATOM 5833 C CD2 . TYR A 1 771 ? 137.741 121.730 152.021 1.00 95.76  ? 754 TYR A CD2 1 
ATOM 5834 C CE1 . TYR A 1 771 ? 136.723 122.904 154.297 1.00 95.76  ? 754 TYR A CE1 1 
ATOM 5835 C CE2 . TYR A 1 771 ? 136.398 121.612 152.311 1.00 95.76  ? 754 TYR A CE2 1 
ATOM 5836 C CZ  . TYR A 1 771 ? 135.893 122.199 153.449 1.00 95.76  ? 754 TYR A CZ  1 
ATOM 5837 O OH  . TYR A 1 771 ? 134.553 122.081 153.736 1.00 95.76  ? 754 TYR A OH  1 
ATOM 5838 N N   . THR A 1 772 ? 142.762 123.113 153.448 1.00 114.40 ? 755 THR A N   1 
ATOM 5839 C CA  . THR A 1 772 ? 144.202 122.905 153.475 1.00 114.40 ? 755 THR A CA  1 
ATOM 5840 C C   . THR A 1 772 ? 144.572 121.654 152.684 1.00 114.40 ? 755 THR A C   1 
ATOM 5841 O O   . THR A 1 772 ? 143.729 120.805 152.388 1.00 114.40 ? 755 THR A O   1 
ATOM 5842 C CB  . THR A 1 772 ? 144.711 122.782 154.914 1.00 114.40 ? 755 THR A CB  1 
ATOM 5843 O OG1 . THR A 1 772 ? 144.519 121.440 155.378 1.00 114.40 ? 755 THR A OG1 1 
ATOM 5844 C CG2 . THR A 1 772 ? 143.967 123.745 155.828 1.00 114.40 ? 755 THR A CG2 1 
ATOM 5845 N N   . GLU A 1 773 ? 145.862 121.549 152.350 1.00 120.65 ? 756 GLU A N   1 
ATOM 5846 C CA  . GLU A 1 773 ? 146.317 120.467 151.481 1.00 120.65 ? 756 GLU A CA  1 
ATOM 5847 C C   . GLU A 1 773 ? 146.144 119.101 152.140 1.00 120.65 ? 756 GLU A C   1 
ATOM 5848 O O   . GLU A 1 773 ? 145.808 118.121 151.464 1.00 120.65 ? 756 GLU A O   1 
ATOM 5849 C CB  . GLU A 1 773 ? 147.774 120.703 151.065 1.00 120.65 ? 756 GLU A CB  1 
ATOM 5850 C CG  . GLU A 1 773 ? 148.840 120.268 152.071 1.00 120.65 ? 756 GLU A CG  1 
ATOM 5851 C CD  . GLU A 1 773 ? 148.996 121.229 153.240 1.00 120.65 ? 756 GLU A CD  1 
ATOM 5852 O OE1 . GLU A 1 773 ? 148.097 122.067 153.464 1.00 120.65 ? 756 GLU A OE1 1 
ATOM 5853 O OE2 . GLU A 1 773 ? 150.026 121.142 153.941 1.00 120.65 ? 756 GLU A OE2 1 
ATOM 5854 N N   . GLU A 1 774 ? 146.369 119.012 153.454 1.00 119.32 ? 757 GLU A N   1 
ATOM 5855 C CA  . GLU A 1 774 ? 146.181 117.739 154.144 1.00 119.32 ? 757 GLU A CA  1 
ATOM 5856 C C   . GLU A 1 774 ? 144.720 117.312 154.115 1.00 119.32 ? 757 GLU A C   1 
ATOM 5857 O O   . GLU A 1 774 ? 144.412 116.137 153.883 1.00 119.32 ? 757 GLU A O   1 
ATOM 5858 C CB  . GLU A 1 774 ? 146.687 117.840 155.583 1.00 119.32 ? 757 GLU A CB  1 
ATOM 5859 C CG  . GLU A 1 774 ? 146.390 116.613 156.431 1.00 119.32 ? 757 GLU A CG  1 
ATOM 5860 C CD  . GLU A 1 774 ? 146.592 116.863 157.912 1.00 119.32 ? 757 GLU A CD  1 
ATOM 5861 O OE1 . GLU A 1 774 ? 147.725 116.667 158.400 1.00 119.32 ? 757 GLU A OE1 1 
ATOM 5862 O OE2 . GLU A 1 774 ? 145.618 117.255 158.589 1.00 119.32 ? 757 GLU A OE2 1 
ATOM 5863 N N   . GLU A 1 775 ? 143.805 118.256 154.345 1.00 113.14 ? 758 GLU A N   1 
ATOM 5864 C CA  . GLU A 1 775 ? 142.382 117.947 154.259 1.00 113.14 ? 758 GLU A CA  1 
ATOM 5865 C C   . GLU A 1 775 ? 141.994 117.540 152.844 1.00 113.14 ? 758 GLU A C   1 
ATOM 5866 O O   . GLU A 1 775 ? 141.186 116.624 152.653 1.00 113.14 ? 758 GLU A O   1 
ATOM 5867 C CB  . GLU A 1 775 ? 141.555 119.148 154.718 1.00 113.14 ? 758 GLU A CB  1 
ATOM 5868 C CG  . GLU A 1 775 ? 141.805 119.560 156.159 1.00 113.14 ? 758 GLU A CG  1 
ATOM 5869 C CD  . GLU A 1 775 ? 141.314 120.962 156.457 1.00 113.14 ? 758 GLU A CD  1 
ATOM 5870 O OE1 . GLU A 1 775 ? 141.312 121.801 155.532 1.00 113.14 ? 758 GLU A OE1 1 
ATOM 5871 O OE2 . GLU A 1 775 ? 140.930 121.226 157.616 1.00 113.14 ? 758 GLU A OE2 1 
ATOM 5872 N N   . LYS A 1 776 ? 142.555 118.217 151.838 1.00 111.13 ? 759 LYS A N   1 
ATOM 5873 C CA  . LYS A 1 776 ? 142.265 117.862 150.452 1.00 111.13 ? 759 LYS A CA  1 
ATOM 5874 C C   . LYS A 1 776 ? 142.731 116.447 150.135 1.00 111.13 ? 759 LYS A C   1 
ATOM 5875 O O   . LYS A 1 776 ? 142.018 115.684 149.472 1.00 111.13 ? 759 LYS A O   1 
ATOM 5876 C CB  . LYS A 1 776 ? 142.921 118.868 149.506 1.00 111.13 ? 759 LYS A CB  1 
ATOM 5877 C CG  . LYS A 1 776 ? 142.357 120.276 149.603 1.00 111.13 ? 759 LYS A CG  1 
ATOM 5878 C CD  . LYS A 1 776 ? 143.014 121.206 148.596 1.00 111.13 ? 759 LYS A CD  1 
ATOM 5879 C CE  . LYS A 1 776 ? 142.683 122.661 148.889 1.00 111.13 ? 759 LYS A CE  1 
ATOM 5880 N NZ  . LYS A 1 776 ? 142.981 123.544 147.729 1.00 111.13 ? 759 LYS A NZ  1 
ATOM 5881 N N   . ASN A 1 777 ? 143.929 116.079 150.595 1.00 115.37 ? 760 ASN A N   1 
ATOM 5882 C CA  . ASN A 1 777 ? 144.431 114.730 150.352 1.00 115.37 ? 760 ASN A CA  1 
ATOM 5883 C C   . ASN A 1 777 ? 143.608 113.686 151.098 1.00 115.37 ? 760 ASN A C   1 
ATOM 5884 O O   . ASN A 1 777 ? 143.320 112.612 150.556 1.00 115.37 ? 760 ASN A O   1 
ATOM 5885 C CB  . ASN A 1 777 ? 145.904 114.637 150.746 1.00 115.37 ? 760 ASN A CB  1 
ATOM 5886 C CG  . ASN A 1 777 ? 146.817 115.335 149.757 1.00 115.37 ? 760 ASN A CG  1 
ATOM 5887 O OD1 . ASN A 1 777 ? 146.414 115.644 148.635 1.00 115.37 ? 760 ASN A OD1 1 
ATOM 5888 N ND2 . ASN A 1 777 ? 148.054 115.585 150.168 1.00 115.37 ? 760 ASN A ND2 1 
ATOM 5889 N N   . ASN A 1 778 ? 143.228 113.977 152.345 1.00 112.09 ? 761 ASN A N   1 
ATOM 5890 C CA  . ASN A 1 778 ? 142.449 113.021 153.126 1.00 112.09 ? 761 ASN A CA  1 
ATOM 5891 C C   . ASN A 1 778 ? 141.069 112.804 152.516 1.00 112.09 ? 761 ASN A C   1 
ATOM 5892 O O   . ASN A 1 778 ? 140.609 111.663 152.385 1.00 112.09 ? 761 ASN A O   1 
ATOM 5893 C CB  . ASN A 1 778 ? 142.332 113.503 154.573 1.00 112.09 ? 761 ASN A CB  1 
ATOM 5894 C CG  . ASN A 1 778 ? 141.585 112.523 155.457 1.00 112.09 ? 761 ASN A CG  1 
ATOM 5895 O OD1 . ASN A 1 778 ? 140.355 112.468 155.444 1.00 112.09 ? 761 ASN A OD1 1 
ATOM 5896 N ND2 . ASN A 1 778 ? 142.328 111.743 156.234 1.00 112.09 ? 761 ASN A ND2 1 
ATOM 5897 N N   . ILE A 1 779 ? 140.391 113.890 152.140 1.00 105.08 ? 762 ILE A N   1 
ATOM 5898 C CA  . ILE A 1 779 ? 139.060 113.769 151.554 1.00 105.08 ? 762 ILE A CA  1 
ATOM 5899 C C   . ILE A 1 779 ? 139.141 113.165 150.158 1.00 105.08 ? 762 ILE A C   1 
ATOM 5900 O O   . ILE A 1 779 ? 138.349 112.282 149.804 1.00 105.08 ? 762 ILE A O   1 
ATOM 5901 C CB  . ILE A 1 779 ? 138.358 115.139 151.542 1.00 105.08 ? 762 ILE A CB  1 
ATOM 5902 C CG1 . ILE A 1 779 ? 138.074 115.602 152.971 1.00 105.08 ? 762 ILE A CG1 1 
ATOM 5903 C CG2 . ILE A 1 779 ? 137.074 115.078 150.732 1.00 105.08 ? 762 ILE A CG2 1 
ATOM 5904 C CD1 . ILE A 1 779 ? 137.457 116.979 153.056 1.00 105.08 ? 762 ILE A CD1 1 
ATOM 5905 N N   . ASN A 1 780 ? 140.103 113.617 149.353 1.00 108.54 ? 763 ASN A N   1 
ATOM 5906 C CA  . ASN A 1 780 ? 140.253 113.181 147.964 1.00 108.54 ? 763 ASN A CA  1 
ATOM 5907 C C   . ASN A 1 780 ? 138.950 113.379 147.190 1.00 108.54 ? 763 ASN A C   1 
ATOM 5908 O O   . ASN A 1 780 ? 138.475 112.494 146.476 1.00 108.54 ? 763 ASN A O   1 
ATOM 5909 C CB  . ASN A 1 780 ? 140.726 111.727 147.891 1.00 108.54 ? 763 ASN A CB  1 
ATOM 5910 C CG  . ASN A 1 780 ? 141.273 111.359 146.525 1.00 108.54 ? 763 ASN A CG  1 
ATOM 5911 O OD1 . ASN A 1 780 ? 141.042 110.257 146.027 1.00 108.54 ? 763 ASN A OD1 1 
ATOM 5912 N ND2 . ASN A 1 780 ? 142.003 112.283 145.911 1.00 108.54 ? 763 ASN A ND2 1 
ATOM 5913 N N   . PHE A 1 781 ? 138.365 114.564 147.351 1.00 96.32  ? 764 PHE A N   1 
ATOM 5914 C CA  . PHE A 1 781 ? 137.096 114.890 146.709 1.00 96.32  ? 764 PHE A CA  1 
ATOM 5915 C C   . PHE A 1 781 ? 137.298 114.974 145.201 1.00 96.32  ? 764 PHE A C   1 
ATOM 5916 O O   . PHE A 1 781 ? 137.968 115.886 144.705 1.00 96.32  ? 764 PHE A O   1 
ATOM 5917 C CB  . PHE A 1 781 ? 136.550 116.202 147.265 1.00 96.32  ? 764 PHE A CB  1 
ATOM 5918 C CG  . PHE A 1 781 ? 135.443 116.798 146.443 1.00 96.32  ? 764 PHE A CG  1 
ATOM 5919 C CD1 . PHE A 1 781 ? 134.323 116.051 146.116 1.00 96.32  ? 764 PHE A CD1 1 
ATOM 5920 C CD2 . PHE A 1 781 ? 135.520 118.108 146.001 1.00 96.32  ? 764 PHE A CD2 1 
ATOM 5921 C CE1 . PHE A 1 781 ? 133.304 116.598 145.361 1.00 96.32  ? 764 PHE A CE1 1 
ATOM 5922 C CE2 . PHE A 1 781 ? 134.503 118.660 145.247 1.00 96.32  ? 764 PHE A CE2 1 
ATOM 5923 C CZ  . PHE A 1 781 ? 133.394 117.904 144.927 1.00 96.32  ? 764 PHE A CZ  1 
ATOM 5924 N N   . ASN A 1 782 ? 136.718 114.026 144.471 1.00 106.57 ? 765 ASN A N   1 
ATOM 5925 C CA  . ASN A 1 782 ? 136.797 113.988 143.013 1.00 106.57 ? 765 ASN A CA  1 
ATOM 5926 C C   . ASN A 1 782 ? 135.517 114.605 142.461 1.00 106.57 ? 765 ASN A C   1 
ATOM 5927 O O   . ASN A 1 782 ? 134.460 113.969 142.450 1.00 106.57 ? 765 ASN A O   1 
ATOM 5928 C CB  . ASN A 1 782 ? 136.996 112.560 142.515 1.00 106.57 ? 765 ASN A CB  1 
ATOM 5929 C CG  . ASN A 1 782 ? 136.114 111.561 143.238 1.00 106.57 ? 765 ASN A CG  1 
ATOM 5930 O OD1 . ASN A 1 782 ? 135.408 111.909 144.185 1.00 106.57 ? 765 ASN A OD1 1 
ATOM 5931 N ND2 . ASN A 1 782 ? 136.149 110.311 142.793 1.00 106.57 ? 765 ASN A ND2 1 
ATOM 5932 N N   . ILE A 1 783 ? 135.614 115.855 142.001 1.00 102.00 ? 766 ILE A N   1 
ATOM 5933 C CA  . ILE A 1 783 ? 134.443 116.563 141.499 1.00 102.00 ? 766 ILE A CA  1 
ATOM 5934 C C   . ILE A 1 783 ? 133.922 115.991 140.190 1.00 102.00 ? 766 ILE A C   1 
ATOM 5935 O O   . ILE A 1 783 ? 132.791 116.297 139.805 1.00 102.00 ? 766 ILE A O   1 
ATOM 5936 C CB  . ILE A 1 783 ? 134.743 118.067 141.340 1.00 102.00 ? 766 ILE A CB  1 
ATOM 5937 C CG1 . ILE A 1 783 ? 133.460 118.881 141.517 1.00 102.00 ? 766 ILE A CG1 1 
ATOM 5938 C CG2 . ILE A 1 783 ? 135.388 118.352 139.992 1.00 102.00 ? 766 ILE A CG2 1 
ATOM 5939 C CD1 . ILE A 1 783 ? 133.689 120.297 141.970 1.00 102.00 ? 766 ILE A CD1 1 
ATOM 5940 N N   . ASP A 1 784 ? 134.714 115.175 139.492 1.00 103.71 ? 767 ASP A N   1 
ATOM 5941 C CA  . ASP A 1 784 ? 134.211 114.520 138.288 1.00 103.71 ? 767 ASP A CA  1 
ATOM 5942 C C   . ASP A 1 784 ? 133.097 113.533 138.621 1.00 103.71 ? 767 ASP A C   1 
ATOM 5943 O O   . ASP A 1 784 ? 132.103 113.438 137.891 1.00 103.71 ? 767 ASP A O   1 
ATOM 5944 C CB  . ASP A 1 784 ? 135.355 113.819 137.556 1.00 103.71 ? 767 ASP A CB  1 
ATOM 5945 C CG  . ASP A 1 784 ? 136.234 114.787 136.787 1.00 103.71 ? 767 ASP A CG  1 
ATOM 5946 O OD1 . ASP A 1 784 ? 135.776 115.916 136.510 1.00 103.71 ? 767 ASP A OD1 1 
ATOM 5947 O OD2 . ASP A 1 784 ? 137.382 114.420 136.459 1.00 103.71 ? 767 ASP A OD2 1 
ATOM 5948 N N   . ASP A 1 785 ? 133.249 112.790 139.720 1.00 101.11 ? 768 ASP A N   1 
ATOM 5949 C CA  . ASP A 1 785 ? 132.210 111.853 140.138 1.00 101.11 ? 768 ASP A CA  1 
ATOM 5950 C C   . ASP A 1 785 ? 130.918 112.591 140.473 1.00 101.11 ? 768 ASP A C   1 
ATOM 5951 O O   . ASP A 1 785 ? 129.825 112.173 140.072 1.00 101.11 ? 768 ASP A O   1 
ATOM 5952 C CB  . ASP A 1 785 ? 132.703 111.041 141.338 1.00 101.11 ? 768 ASP A CB  1 
ATOM 5953 C CG  . ASP A 1 785 ? 131.570 110.430 142.146 1.00 101.11 ? 768 ASP A CG  1 
ATOM 5954 O OD1 . ASP A 1 785 ? 130.602 109.919 141.544 1.00 101.11 ? 768 ASP A OD1 1 
ATOM 5955 O OD2 . ASP A 1 785 ? 131.650 110.464 143.392 1.00 101.11 ? 768 ASP A OD2 1 
ATOM 5956 N N   . LEU A 1 786 ? 131.028 113.701 141.205 1.00 89.13  ? 769 LEU A N   1 
ATOM 5957 C CA  . LEU A 1 786 ? 129.843 114.487 141.527 1.00 89.13  ? 769 LEU A CA  1 
ATOM 5958 C C   . LEU A 1 786 ? 129.238 115.116 140.279 1.00 89.13  ? 769 LEU A C   1 
ATOM 5959 O O   . LEU A 1 786 ? 128.013 115.244 140.185 1.00 89.13  ? 769 LEU A O   1 
ATOM 5960 C CB  . LEU A 1 786 ? 130.190 115.559 142.561 1.00 89.13  ? 769 LEU A CB  1 
ATOM 5961 C CG  . LEU A 1 786 ? 129.037 116.411 143.092 1.00 89.13  ? 769 LEU A CG  1 
ATOM 5962 C CD1 . LEU A 1 786 ? 129.224 116.689 144.574 1.00 89.13  ? 769 LEU A CD1 1 
ATOM 5963 C CD2 . LEU A 1 786 ? 128.924 117.711 142.318 1.00 89.13  ? 769 LEU A CD2 1 
ATOM 5964 N N   . SER A 1 787 ? 130.075 115.520 139.321 1.00 91.68  ? 770 SER A N   1 
ATOM 5965 C CA  . SER A 1 787 ? 129.564 116.035 138.056 1.00 91.68  ? 770 SER A CA  1 
ATOM 5966 C C   . SER A 1 787 ? 128.752 114.974 137.327 1.00 91.68  ? 770 SER A C   1 
ATOM 5967 O O   . SER A 1 787 ? 127.668 115.259 136.804 1.00 91.68  ? 770 SER A O   1 
ATOM 5968 C CB  . SER A 1 787 ? 130.721 116.513 137.178 1.00 91.68  ? 770 SER A CB  1 
ATOM 5969 O OG  . SER A 1 787 ? 131.369 117.639 137.741 1.00 91.68  ? 770 SER A OG  1 
ATOM 5970 N N   . SER A 1 788 ? 129.263 113.742 137.286 1.00 89.74  ? 771 SER A N   1 
ATOM 5971 C CA  . SER A 1 788 ? 128.523 112.653 136.657 1.00 89.74  ? 771 SER A CA  1 
ATOM 5972 C C   . SER A 1 788 ? 127.214 112.382 137.390 1.00 89.74  ? 771 SER A C   1 
ATOM 5973 O O   . SER A 1 788 ? 126.176 112.149 136.758 1.00 89.74  ? 771 SER A O   1 
ATOM 5974 C CB  . SER A 1 788 ? 129.385 111.392 136.610 1.00 89.74  ? 771 SER A CB  1 
ATOM 5975 O OG  . SER A 1 788 ? 130.473 111.550 135.716 1.00 89.74  ? 771 SER A OG  1 
ATOM 5976 N N   . LYS A 1 789 ? 127.245 112.411 138.724 1.00 86.21  ? 772 LYS A N   1 
ATOM 5977 C CA  . LYS A 1 789 ? 126.028 112.185 139.499 1.00 86.21  ? 772 LYS A CA  1 
ATOM 5978 C C   . LYS A 1 789 ? 124.985 113.261 139.220 1.00 86.21  ? 772 LYS A C   1 
ATOM 5979 O O   . LYS A 1 789 ? 123.799 112.959 139.031 1.00 86.21  ? 772 LYS A O   1 
ATOM 5980 C CB  . LYS A 1 789 ? 126.361 112.138 140.991 1.00 86.21  ? 772 LYS A CB  1 
ATOM 5981 C CG  . LYS A 1 789 ? 127.072 110.870 141.432 1.00 86.21  ? 772 LYS A CG  1 
ATOM 5982 C CD  . LYS A 1 789 ? 126.161 109.659 141.339 1.00 86.21  ? 772 LYS A CD  1 
ATOM 5983 C CE  . LYS A 1 789 ? 126.821 108.430 141.942 1.00 86.21  ? 772 LYS A CE  1 
ATOM 5984 N NZ  . LYS A 1 789 ? 126.568 108.325 143.405 1.00 86.21  ? 772 LYS A NZ  1 
ATOM 5985 N N   . LEU A 1 790 ? 125.409 114.526 139.179 1.00 71.05  ? 773 LEU A N   1 
ATOM 5986 C CA  . LEU A 1 790 ? 124.470 115.611 138.925 1.00 71.05  ? 773 LEU A CA  1 
ATOM 5987 C C   . LEU A 1 790 ? 123.948 115.571 137.494 1.00 71.05  ? 773 LEU A C   1 
ATOM 5988 O O   . LEU A 1 790 ? 122.786 115.903 137.247 1.00 71.05  ? 773 LEU A O   1 
ATOM 5989 C CB  . LEU A 1 790 ? 125.123 116.959 139.227 1.00 71.05  ? 773 LEU A CB  1 
ATOM 5990 C CG  . LEU A 1 790 ? 125.228 117.313 140.712 1.00 71.05  ? 773 LEU A CG  1 
ATOM 5991 C CD1 . LEU A 1 790 ? 125.688 118.750 140.893 1.00 71.05  ? 773 LEU A CD1 1 
ATOM 5992 C CD2 . LEU A 1 790 ? 123.903 117.077 141.417 1.00 71.05  ? 773 LEU A CD2 1 
ATOM 5993 N N   . ASN A 1 791 ? 124.784 115.162 136.537 1.00 78.25  ? 774 ASN A N   1 
ATOM 5994 C CA  . ASN A 1 791 ? 124.309 115.021 135.164 1.00 78.25  ? 774 ASN A CA  1 
ATOM 5995 C C   . ASN A 1 791 ? 123.294 113.889 135.046 1.00 78.25  ? 774 ASN A C   1 
ATOM 5996 O O   . ASN A 1 791 ? 122.315 113.994 134.296 1.00 78.25  ? 774 ASN A O   1 
ATOM 5997 C CB  . ASN A 1 791 ? 125.490 114.794 134.221 1.00 78.25  ? 774 ASN A CB  1 
ATOM 5998 C CG  . ASN A 1 791 ? 126.353 116.031 134.064 1.00 78.25  ? 774 ASN A CG  1 
ATOM 5999 O OD1 . ASN A 1 791 ? 125.855 117.157 134.089 1.00 78.25  ? 774 ASN A OD1 1 
ATOM 6000 N ND2 . ASN A 1 791 ? 127.655 115.828 133.904 1.00 78.25  ? 774 ASN A ND2 1 
ATOM 6001 N N   . GLU A 1 792 ? 123.509 112.796 135.781 1.00 76.96  ? 775 GLU A N   1 
ATOM 6002 C CA  . GLU A 1 792 ? 122.521 111.723 135.794 1.00 76.96  ? 775 GLU A CA  1 
ATOM 6003 C C   . GLU A 1 792 ? 121.218 112.173 136.444 1.00 76.96  ? 775 GLU A C   1 
ATOM 6004 O O   . GLU A 1 792 ? 120.133 111.791 135.989 1.00 76.96  ? 775 GLU A O   1 
ATOM 6005 C CB  . GLU A 1 792 ? 123.092 110.497 136.505 1.00 76.96  ? 775 GLU A CB  1 
ATOM 6006 C CG  . GLU A 1 792 ? 123.716 109.484 135.557 1.00 76.96  ? 775 GLU A CG  1 
ATOM 6007 C CD  . GLU A 1 792 ? 124.940 108.810 136.142 1.00 76.96  ? 775 GLU A CD  1 
ATOM 6008 O OE1 . GLU A 1 792 ? 124.992 108.635 137.377 1.00 76.96  ? 775 GLU A OE1 1 
ATOM 6009 O OE2 . GLU A 1 792 ? 125.852 108.457 135.365 1.00 76.96  ? 775 GLU A OE2 1 
ATOM 6010 N N   . SER A 1 793 ? 121.302 112.989 137.497 1.00 65.31  ? 776 SER A N   1 
ATOM 6011 C CA  . SER A 1 793 ? 120.092 113.575 138.071 1.00 65.31  ? 776 SER A CA  1 
ATOM 6012 C C   . SER A 1 793 ? 119.402 114.497 137.070 1.00 65.31  ? 776 SER A C   1 
ATOM 6013 O O   . SER A 1 793 ? 118.167 114.551 137.007 1.00 65.31  ? 776 SER A O   1 
ATOM 6014 C CB  . SER A 1 793 ? 120.433 114.330 139.355 1.00 65.31  ? 776 SER A CB  1 
ATOM 6015 O OG  . SER A 1 793 ? 120.653 113.432 140.429 1.00 65.31  ? 776 SER A OG  1 
ATOM 6016 N N   . ILE A 1 794 ? 120.189 115.230 136.279 1.00 59.18  ? 777 ILE A N   1 
ATOM 6017 C CA  . ILE A 1 794 ? 119.630 116.070 135.224 1.00 59.18  ? 777 ILE A CA  1 
ATOM 6018 C C   . ILE A 1 794 ? 118.865 115.221 134.220 1.00 59.18  ? 777 ILE A C   1 
ATOM 6019 O O   . ILE A 1 794 ? 117.773 115.589 133.785 1.00 59.18  ? 777 ILE A O   1 
ATOM 6020 C CB  . ILE A 1 794 ? 120.744 116.888 134.542 1.00 59.18  ? 777 ILE A CB  1 
ATOM 6021 C CG1 . ILE A 1 794 ? 121.159 118.069 135.419 1.00 59.18  ? 777 ILE A CG1 1 
ATOM 6022 C CG2 . ILE A 1 794 ? 120.293 117.379 133.177 1.00 59.18  ? 777 ILE A CG2 1 
ATOM 6023 C CD1 . ILE A 1 794 ? 119.996 118.811 136.025 1.00 59.18  ? 777 ILE A CD1 1 
ATOM 6024 N N   . ASN A 1 795 ? 119.429 114.075 133.833 1.00 71.46  ? 778 ASN A N   1 
ATOM 6025 C CA  . ASN A 1 795 ? 118.731 113.171 132.918 1.00 71.46  ? 778 ASN A CA  1 
ATOM 6026 C C   . ASN A 1 795 ? 117.446 112.630 133.543 1.00 71.46  ? 778 ASN A C   1 
ATOM 6027 O O   . ASN A 1 795 ? 116.406 112.519 132.871 1.00 71.46  ? 778 ASN A O   1 
ATOM 6028 C CB  . ASN A 1 795 ? 119.665 112.024 132.522 1.00 71.46  ? 778 ASN A CB  1 
ATOM 6029 C CG  . ASN A 1 795 ? 119.170 111.245 131.315 1.00 71.46  ? 778 ASN A CG  1 
ATOM 6030 O OD1 . ASN A 1 795 ? 117.969 111.074 131.112 1.00 71.46  ? 778 ASN A OD1 1 
ATOM 6031 N ND2 . ASN A 1 795 ? 120.106 110.763 130.506 1.00 71.46  ? 778 ASN A ND2 1 
ATOM 6032 N N   . LYS A 1 796 ? 117.506 112.272 134.828 1.00 59.52  ? 779 LYS A N   1 
ATOM 6033 C CA  . LYS A 1 796 ? 116.341 111.720 135.510 1.00 59.52  ? 779 LYS A CA  1 
ATOM 6034 C C   . LYS A 1 796 ? 115.231 112.757 135.648 1.00 59.52  ? 779 LYS A C   1 
ATOM 6035 O O   . LYS A 1 796 ? 114.048 112.399 135.696 1.00 59.52  ? 779 LYS A O   1 
ATOM 6036 C CB  . LYS A 1 796 ? 116.767 111.165 136.873 1.00 59.52  ? 779 LYS A CB  1 
ATOM 6037 C CG  . LYS A 1 796 ? 115.702 111.169 137.951 1.00 59.52  ? 779 LYS A CG  1 
ATOM 6038 C CD  . LYS A 1 796 ? 116.182 110.439 139.196 1.00 59.52  ? 779 LYS A CD  1 
ATOM 6039 C CE  . LYS A 1 796 ? 115.045 110.213 140.180 1.00 59.52  ? 779 LYS A CE  1 
ATOM 6040 N NZ  . LYS A 1 796 ? 115.529 110.160 141.587 1.00 59.52  ? 779 LYS A NZ  1 
ATOM 6041 N N   . ALA A 1 797 ? 115.587 114.040 135.726 1.00 50.67  ? 780 ALA A N   1 
ATOM 6042 C CA  . ALA A 1 797 ? 114.586 115.099 135.629 1.00 50.67  ? 780 ALA A CA  1 
ATOM 6043 C C   . ALA A 1 797 ? 114.152 115.345 134.187 1.00 50.67  ? 780 ALA A C   1 
ATOM 6044 O O   . ALA A 1 797 ? 112.996 115.714 133.936 1.00 50.67  ? 780 ALA A O   1 
ATOM 6045 C CB  . ALA A 1 797 ? 115.130 116.393 136.232 1.00 50.67  ? 780 ALA A CB  1 
ATOM 6046 N N   . MET A 1 798 ? 115.070 115.151 133.240 1.00 53.89  ? 781 MET A N   1 
ATOM 6047 C CA  . MET A 1 798 ? 114.815 115.463 131.842 1.00 53.89  ? 781 MET A CA  1 
ATOM 6048 C C   . MET A 1 798 ? 113.774 114.532 131.248 1.00 53.89  ? 781 MET A C   1 
ATOM 6049 O O   . MET A 1 798 ? 112.999 114.950 130.384 1.00 53.89  ? 781 MET A O   1 
ATOM 6050 C CB  . MET A 1 798 ? 116.120 115.372 131.049 1.00 53.89  ? 781 MET A CB  1 
ATOM 6051 C CG  . MET A 1 798 ? 116.809 116.706 130.793 1.00 53.89  ? 781 MET A CG  1 
ATOM 6052 S SD  . MET A 1 798 ? 115.706 118.022 130.257 1.00 53.89  ? 781 MET A SD  1 
ATOM 6053 C CE  . MET A 1 798 ? 115.108 117.343 128.714 1.00 53.89  ? 781 MET A CE  1 
ATOM 6054 N N   . ILE A 1 799 ? 113.747 113.272 131.684 1.00 49.85  ? 782 ILE A N   1 
ATOM 6055 C CA  . ILE A 1 799 ? 112.718 112.362 131.179 1.00 49.85  ? 782 ILE A CA  1 
ATOM 6056 C C   . ILE A 1 799 ? 111.329 112.862 131.571 1.00 49.85  ? 782 ILE A C   1 
ATOM 6057 O O   . ILE A 1 799 ? 110.405 112.894 130.744 1.00 49.85  ? 782 ILE A O   1 
ATOM 6058 C CB  . ILE A 1 799 ? 112.965 110.923 131.669 1.00 49.85  ? 782 ILE A CB  1 
ATOM 6059 C CG1 . ILE A 1 799 ? 113.393 110.908 133.133 1.00 49.85  ? 782 ILE A CG1 1 
ATOM 6060 C CG2 . ILE A 1 799 ? 114.017 110.243 130.809 1.00 49.85  ? 782 ILE A CG2 1 
ATOM 6061 C CD1 . ILE A 1 799 ? 113.415 109.525 133.747 1.00 49.85  ? 782 ILE A CD1 1 
ATOM 6062 N N   . ASN A 1 800 ? 111.165 113.280 132.829 1.00 49.85  ? 783 ASN A N   1 
ATOM 6063 C CA  . ASN A 1 800 ? 109.881 113.813 133.278 1.00 49.85  ? 783 ASN A CA  1 
ATOM 6064 C C   . ASN A 1 800 ? 109.529 115.103 132.547 1.00 49.85  ? 783 ASN A C   1 
ATOM 6065 O O   . ASN A 1 800 ? 108.367 115.321 132.179 1.00 49.85  ? 783 ASN A O   1 
ATOM 6066 C CB  . ASN A 1 800 ? 109.908 114.047 134.788 1.00 49.85  ? 783 ASN A CB  1 
ATOM 6067 C CG  . ASN A 1 800 ? 109.791 112.761 135.581 1.00 49.85  ? 783 ASN A CG  1 
ATOM 6068 O OD1 . ASN A 1 800 ? 109.488 111.704 135.029 1.00 49.85  ? 783 ASN A OD1 1 
ATOM 6069 N ND2 . ASN A 1 800 ? 110.028 112.846 136.884 1.00 49.85  ? 783 ASN A ND2 1 
ATOM 6070 N N   . ILE A 1 801 ? 110.516 115.979 132.341 1.00 49.85  ? 784 ILE A N   1 
ATOM 6071 C CA  . ILE A 1 801 ? 110.255 117.231 131.636 1.00 49.85  ? 784 ILE A CA  1 
ATOM 6072 C C   . ILE A 1 801 ? 109.820 116.956 130.200 1.00 49.85  ? 784 ILE A C   1 
ATOM 6073 O O   . ILE A 1 801 ? 108.889 117.590 129.685 1.00 49.85  ? 784 ILE A O   1 
ATOM 6074 C CB  . ILE A 1 801 ? 111.494 118.144 131.691 1.00 49.85  ? 784 ILE A CB  1 
ATOM 6075 C CG1 . ILE A 1 801 ? 111.581 118.839 133.051 1.00 49.85  ? 784 ILE A CG1 1 
ATOM 6076 C CG2 . ILE A 1 801 ? 111.458 119.174 130.573 1.00 49.85  ? 784 ILE A CG2 1 
ATOM 6077 C CD1 . ILE A 1 801 ? 110.263 119.397 133.540 1.00 49.85  ? 784 ILE A CD1 1 
ATOM 6078 N N   . ASN A 1 802 ? 110.485 116.009 129.534 1.00 49.85  ? 785 ASN A N   1 
ATOM 6079 C CA  . ASN A 1 802 ? 110.093 115.626 128.184 1.00 49.85  ? 785 ASN A CA  1 
ATOM 6080 C C   . ASN A 1 802 ? 108.674 115.084 128.160 1.00 49.85  ? 785 ASN A C   1 
ATOM 6081 O O   . ASN A 1 802 ? 107.890 115.423 127.268 1.00 49.85  ? 785 ASN A O   1 
ATOM 6082 C CB  . ASN A 1 802 ? 111.063 114.583 127.629 1.00 49.85  ? 785 ASN A CB  1 
ATOM 6083 C CG  . ASN A 1 802 ? 112.411 115.168 127.281 1.00 49.85  ? 785 ASN A CG  1 
ATOM 6084 O OD1 . ASN A 1 802 ? 112.554 116.380 127.141 1.00 49.85  ? 785 ASN A OD1 1 
ATOM 6085 N ND2 . ASN A 1 802 ? 113.412 114.309 127.141 1.00 49.85  ? 785 ASN A ND2 1 
ATOM 6086 N N   . LYS A 1 803 ? 108.324 114.240 129.133 1.00 49.85  ? 786 LYS A N   1 
ATOM 6087 C CA  . LYS A 1 803 ? 106.970 113.697 129.168 1.00 49.85  ? 786 LYS A CA  1 
ATOM 6088 C C   . LYS A 1 803 ? 105.936 114.804 129.349 1.00 49.85  ? 786 LYS A C   1 
ATOM 6089 O O   . LYS A 1 803 ? 104.915 114.829 128.650 1.00 49.85  ? 786 LYS A O   1 
ATOM 6090 C CB  . LYS A 1 803 ? 106.851 112.655 130.279 1.00 49.85  ? 786 LYS A CB  1 
ATOM 6091 C CG  . LYS A 1 803 ? 105.522 111.921 130.299 1.00 49.85  ? 786 LYS A CG  1 
ATOM 6092 C CD  . LYS A 1 803 ? 105.507 110.838 131.364 1.00 49.85  ? 786 LYS A CD  1 
ATOM 6093 C CE  . LYS A 1 803 ? 104.207 110.050 131.333 1.00 49.85  ? 786 LYS A CE  1 
ATOM 6094 N NZ  . LYS A 1 803 ? 103.997 109.278 132.589 1.00 49.85  ? 786 LYS A NZ  1 
ATOM 6095 N N   . PHE A 1 804 ? 106.200 115.745 130.260 1.00 49.85  ? 787 PHE A N   1 
ATOM 6096 C CA  . PHE A 1 804 ? 105.256 116.835 130.495 1.00 49.85  ? 787 PHE A CA  1 
ATOM 6097 C C   . PHE A 1 804 ? 105.093 117.710 129.258 1.00 49.85  ? 787 PHE A C   1 
ATOM 6098 O O   . PHE A 1 804 ? 103.970 118.063 128.874 1.00 49.85  ? 787 PHE A O   1 
ATOM 6099 C CB  . PHE A 1 804 ? 105.710 117.680 131.685 1.00 49.85  ? 787 PHE A CB  1 
ATOM 6100 C CG  . PHE A 1 804 ? 105.000 119.001 131.796 1.00 49.85  ? 787 PHE A CG  1 
ATOM 6101 C CD1 . PHE A 1 804 ? 103.619 119.062 131.822 1.00 49.85  ? 787 PHE A CD1 1 
ATOM 6102 C CD2 . PHE A 1 804 ? 105.715 120.182 131.870 1.00 49.85  ? 787 PHE A CD2 1 
ATOM 6103 C CE1 . PHE A 1 804 ? 102.965 120.274 131.923 1.00 49.85  ? 787 PHE A CE1 1 
ATOM 6104 C CE2 . PHE A 1 804 ? 105.066 121.397 131.971 1.00 49.85  ? 787 PHE A CE2 1 
ATOM 6105 C CZ  . PHE A 1 804 ? 103.690 121.442 131.997 1.00 49.85  ? 787 PHE A CZ  1 
ATOM 6106 N N   . LEU A 1 805 ? 106.206 118.079 128.621 1.00 49.85  ? 788 LEU A N   1 
ATOM 6107 C CA  . LEU A 1 805 ? 106.114 118.978 127.476 1.00 49.85  ? 788 LEU A CA  1 
ATOM 6108 C C   . LEU A 1 805 ? 105.491 118.280 126.275 1.00 49.85  ? 788 LEU A C   1 
ATOM 6109 O O   . LEU A 1 805 ? 104.756 118.906 125.503 1.00 49.85  ? 788 LEU A O   1 
ATOM 6110 C CB  . LEU A 1 805 ? 107.491 119.544 127.136 1.00 49.85  ? 788 LEU A CB  1 
ATOM 6111 C CG  . LEU A 1 805 ? 107.935 120.636 128.114 1.00 49.85  ? 788 LEU A CG  1 
ATOM 6112 C CD1 . LEU A 1 805 ? 109.237 121.275 127.680 1.00 49.85  ? 788 LEU A CD1 1 
ATOM 6113 C CD2 . LEU A 1 805 ? 106.849 121.689 128.267 1.00 49.85  ? 788 LEU A CD2 1 
ATOM 6114 N N   . ASN A 1 806 ? 105.754 116.982 126.107 1.00 49.85  ? 789 ASN A N   1 
ATOM 6115 C CA  . ASN A 1 806 ? 105.081 116.222 125.062 1.00 49.85  ? 789 ASN A CA  1 
ATOM 6116 C C   . ASN A 1 806 ? 103.579 116.173 125.305 1.00 49.85  ? 789 ASN A C   1 
ATOM 6117 O O   . ASN A 1 806 ? 102.782 116.357 124.374 1.00 49.85  ? 789 ASN A O   1 
ATOM 6118 C CB  . ASN A 1 806 ? 105.662 114.811 124.999 1.00 49.85  ? 789 ASN A CB  1 
ATOM 6119 C CG  . ASN A 1 806 ? 106.994 114.760 124.282 1.00 49.85  ? 789 ASN A CG  1 
ATOM 6120 O OD1 . ASN A 1 806 ? 107.281 115.590 123.419 1.00 49.85  ? 789 ASN A OD1 1 
ATOM 6121 N ND2 . ASN A 1 806 ? 107.823 113.790 124.647 1.00 49.85  ? 789 ASN A ND2 1 
ATOM 6122 N N   . GLN A 1 807 ? 103.173 115.943 126.559 1.00 49.85  ? 790 GLN A N   1 
ATOM 6123 C CA  . GLN A 1 807 ? 101.751 115.937 126.882 1.00 49.85  ? 790 GLN A CA  1 
ATOM 6124 C C   . GLN A 1 807 ? 101.114 117.285 126.580 1.00 49.85  ? 790 GLN A C   1 
ATOM 6125 O O   . GLN A 1 807 ? 100.019 117.345 126.013 1.00 49.85  ? 790 GLN A O   1 
ATOM 6126 C CB  . GLN A 1 807 ? 101.541 115.566 128.350 1.00 49.85  ? 790 GLN A CB  1 
ATOM 6127 C CG  . GLN A 1 807 ? 101.526 114.072 128.625 1.00 49.85  ? 790 GLN A CG  1 
ATOM 6128 C CD  . GLN A 1 807 ? 100.906 113.732 129.965 1.00 49.85  ? 790 GLN A CD  1 
ATOM 6129 O OE1 . GLN A 1 807 ? 100.240 114.562 130.583 1.00 49.85  ? 790 GLN A OE1 1 
ATOM 6130 N NE2 . GLN A 1 807 ? 101.119 112.503 130.421 1.00 49.85  ? 790 GLN A NE2 1 
ATOM 6131 N N   . CYS A 1 808 ? 101.785 118.379 126.946 1.00 49.85  ? 791 CYS A N   1 
ATOM 6132 C CA  . CYS A 1 808 ? 101.225 119.705 126.688 1.00 49.85  ? 791 CYS A CA  1 
ATOM 6133 C C   . CYS A 1 808 ? 101.132 119.997 125.193 1.00 49.85  ? 791 CYS A C   1 
ATOM 6134 O O   . CYS A 1 808 ? 100.118 120.531 124.720 1.00 49.85  ? 791 CYS A O   1 
ATOM 6135 C CB  . CYS A 1 808 ? 102.058 120.773 127.392 1.00 49.85  ? 791 CYS A CB  1 
ATOM 6136 S SG  . CYS A 1 808 ? 101.382 121.307 128.978 1.00 49.85  ? 791 CYS A SG  1 
ATOM 6137 N N   . SER A 1 809 ? 102.174 119.654 124.432 1.00 49.85  ? 792 SER A N   1 
ATOM 6138 C CA  . SER A 1 809 ? 102.173 119.928 123.001 1.00 49.85  ? 792 SER A CA  1 
ATOM 6139 C C   . SER A 1 809 ? 101.167 119.071 122.247 1.00 49.85  ? 792 SER A C   1 
ATOM 6140 O O   . SER A 1 809 ? 100.698 119.486 121.183 1.00 49.85  ? 792 SER A O   1 
ATOM 6141 C CB  . SER A 1 809 ? 103.573 119.718 122.423 1.00 49.85  ? 792 SER A CB  1 
ATOM 6142 O OG  . SER A 1 809 ? 103.605 120.032 121.042 1.00 49.85  ? 792 SER A OG  1 
ATOM 6143 N N   . VAL A 1 810 ? 100.828 117.889 122.764 1.00 49.85  ? 793 VAL A N   1 
ATOM 6144 C CA  . VAL A 1 810 ? 99.783  117.098 122.122 1.00 49.85  ? 793 VAL A CA  1 
ATOM 6145 C C   . VAL A 1 810 ? 98.401  117.560 122.576 1.00 49.85  ? 793 VAL A C   1 
ATOM 6146 O O   . VAL A 1 810 ? 97.445  117.569 121.790 1.00 49.85  ? 793 VAL A O   1 
ATOM 6147 C CB  . VAL A 1 810 ? 100.012 115.600 122.394 1.00 49.85  ? 793 VAL A CB  1 
ATOM 6148 C CG1 . VAL A 1 810 ? 98.796  114.784 121.988 1.00 49.85  ? 793 VAL A CG1 1 
ATOM 6149 C CG2 . VAL A 1 810 ? 101.241 115.120 121.645 1.00 49.85  ? 793 VAL A CG2 1 
ATOM 6150 N N   . SER A 1 811 ? 98.275  117.976 123.839 1.00 49.85  ? 794 SER A N   1 
ATOM 6151 C CA  . SER A 1 811 ? 96.992  118.451 124.338 1.00 49.85  ? 794 SER A CA  1 
ATOM 6152 C C   . SER A 1 811 ? 96.571  119.748 123.666 1.00 49.85  ? 794 SER A C   1 
ATOM 6153 O O   . SER A 1 811 ? 95.374  119.974 123.466 1.00 49.85  ? 794 SER A O   1 
ATOM 6154 C CB  . SER A 1 811 ? 97.050  118.637 125.853 1.00 49.85  ? 794 SER A CB  1 
ATOM 6155 O OG  . SER A 1 811 ? 95.853  119.218 126.338 1.00 49.85  ? 794 SER A OG  1 
ATOM 6156 N N   . TYR A 1 812 ? 97.526  120.613 123.315 1.00 49.85  ? 795 TYR A N   1 
ATOM 6157 C CA  . TYR A 1 812 ? 97.156  121.817 122.577 1.00 49.85  ? 795 TYR A CA  1 
ATOM 6158 C C   . TYR A 1 812 ? 96.537  121.465 121.230 1.00 49.85  ? 795 TYR A C   1 
ATOM 6159 O O   . TYR A 1 812 ? 95.533  122.062 120.826 1.00 49.85  ? 795 TYR A O   1 
ATOM 6160 C CB  . TYR A 1 812 ? 98.362  122.734 122.387 1.00 49.85  ? 795 TYR A CB  1 
ATOM 6161 C CG  . TYR A 1 812 ? 97.968  124.116 121.912 1.00 49.85  ? 795 TYR A CG  1 
ATOM 6162 C CD1 . TYR A 1 812 ? 97.649  125.119 122.817 1.00 49.85  ? 795 TYR A CD1 1 
ATOM 6163 C CD2 . TYR A 1 812 ? 97.886  124.408 120.556 1.00 49.85  ? 795 TYR A CD2 1 
ATOM 6164 C CE1 . TYR A 1 812 ? 97.276  126.378 122.385 1.00 49.85  ? 795 TYR A CE1 1 
ATOM 6165 C CE2 . TYR A 1 812 ? 97.516  125.664 120.116 1.00 49.85  ? 795 TYR A CE2 1 
ATOM 6166 C CZ  . TYR A 1 812 ? 97.212  126.645 121.035 1.00 49.85  ? 795 TYR A CZ  1 
ATOM 6167 O OH  . TYR A 1 812 ? 96.842  127.897 120.600 1.00 49.85  ? 795 TYR A OH  1 
ATOM 6168 N N   . LEU A 1 813 ? 97.119  120.493 120.524 1.00 58.29  ? 796 LEU A N   1 
ATOM 6169 C CA  . LEU A 1 813 ? 96.535  120.048 119.263 1.00 58.29  ? 796 LEU A CA  1 
ATOM 6170 C C   . LEU A 1 813 ? 95.160  119.428 119.480 1.00 58.29  ? 796 LEU A C   1 
ATOM 6171 O O   . LEU A 1 813 ? 94.234  119.661 118.694 1.00 58.29  ? 796 LEU A O   1 
ATOM 6172 C CB  . LEU A 1 813 ? 97.472  119.056 118.574 1.00 58.29  ? 796 LEU A CB  1 
ATOM 6173 C CG  . LEU A 1 813 ? 96.865  118.147 117.505 1.00 58.29  ? 796 LEU A CG  1 
ATOM 6174 C CD1 . LEU A 1 813 ? 96.449  118.955 116.288 1.00 58.29  ? 796 LEU A CD1 1 
ATOM 6175 C CD2 . LEU A 1 813 ? 97.840  117.050 117.114 1.00 58.29  ? 796 LEU A CD2 1 
ATOM 6176 N N   . MET A 1 814 ? 95.007  118.636 120.543 1.00 49.85  ? 797 MET A N   1 
ATOM 6177 C CA  . MET A 1 814 ? 93.732  117.967 120.790 1.00 49.85  ? 797 MET A CA  1 
ATOM 6178 C C   . MET A 1 814 ? 92.644  118.911 121.288 1.00 49.85  ? 797 MET A C   1 
ATOM 6179 O O   . MET A 1 814 ? 91.460  118.574 121.181 1.00 49.85  ? 797 MET A O   1 
ATOM 6180 C CB  . MET A 1 814 ? 93.915  116.832 121.799 1.00 49.85  ? 797 MET A CB  1 
ATOM 6181 C CG  . MET A 1 814 ? 94.908  115.767 121.377 1.00 49.85  ? 797 MET A CG  1 
ATOM 6182 S SD  . MET A 1 814 ? 94.885  115.480 119.601 1.00 49.85  ? 797 MET A SD  1 
ATOM 6183 C CE  . MET A 1 814 ? 93.489  114.366 119.479 1.00 49.85  ? 797 MET A CE  1 
ATOM 6184 N N   . ASN A 1 815 ? 93.003  120.074 121.828 1.00 49.85  ? 798 ASN A N   1 
ATOM 6185 C CA  . ASN A 1 815 ? 92.026  120.935 122.481 1.00 49.85  ? 798 ASN A CA  1 
ATOM 6186 C C   . ASN A 1 815 ? 91.773  122.264 121.784 1.00 49.85  ? 798 ASN A C   1 
ATOM 6187 O O   . ASN A 1 815 ? 90.660  122.784 121.885 1.00 49.85  ? 798 ASN A O   1 
ATOM 6188 C CB  . ASN A 1 815 ? 92.457  121.222 123.928 1.00 49.85  ? 798 ASN A CB  1 
ATOM 6189 C CG  . ASN A 1 815 ? 91.299  121.162 124.904 1.00 49.85  ? 798 ASN A CG  1 
ATOM 6190 O OD1 . ASN A 1 815 ? 90.172  121.527 124.571 1.00 49.85  ? 798 ASN A OD1 1 
ATOM 6191 N ND2 . ASN A 1 815 ? 91.572  120.699 126.118 1.00 49.85  ? 798 ASN A ND2 1 
ATOM 6192 N N   . SER A 1 816 ? 92.757  122.835 121.087 1.00 49.85  ? 799 SER A N   1 
ATOM 6193 C CA  . SER A 1 816 ? 92.604  124.170 120.530 1.00 49.85  ? 799 SER A CA  1 
ATOM 6194 C C   . SER A 1 816 ? 92.850  124.253 119.030 1.00 49.85  ? 799 SER A C   1 
ATOM 6195 O O   . SER A 1 816 ? 92.697  125.338 118.459 1.00 49.85  ? 799 SER A O   1 
ATOM 6196 C CB  . SER A 1 816 ? 93.541  125.155 121.245 1.00 49.85  ? 799 SER A CB  1 
ATOM 6197 O OG  . SER A 1 816 ? 93.390  125.069 122.651 1.00 49.85  ? 799 SER A OG  1 
ATOM 6198 N N   . MET A 1 817 ? 93.222  123.156 118.377 1.00 49.85  ? 800 MET A N   1 
ATOM 6199 C CA  . MET A 1 817 ? 93.409  123.141 116.932 1.00 49.85  ? 800 MET A CA  1 
ATOM 6200 C C   . MET A 1 817 ? 92.453  122.190 116.233 1.00 49.85  ? 800 MET A C   1 
ATOM 6201 O O   . MET A 1 817 ? 91.808  122.576 115.251 1.00 49.85  ? 800 MET A O   1 
ATOM 6202 C CB  . MET A 1 817 ? 94.859  122.768 116.587 1.00 49.85  ? 800 MET A CB  1 
ATOM 6203 C CG  . MET A 1 817 ? 95.888  123.802 117.006 1.00 49.85  ? 800 MET A CG  1 
ATOM 6204 S SD  . MET A 1 817 ? 97.238  123.923 115.819 1.00 49.85  ? 800 MET A SD  1 
ATOM 6205 C CE  . MET A 1 817 ? 98.018  125.443 116.345 1.00 49.85  ? 800 MET A CE  1 
ATOM 6206 N N   . ILE A 1 818 ? 92.349  120.948 116.711 1.00 49.85  ? 801 ILE A N   1 
ATOM 6207 C CA  . ILE A 1 818 ? 91.435  119.989 116.086 1.00 49.85  ? 801 ILE A CA  1 
ATOM 6208 C C   . ILE A 1 818 ? 89.981  120.430 116.185 1.00 49.85  ? 801 ILE A C   1 
ATOM 6209 O O   . ILE A 1 818 ? 89.264  120.332 115.179 1.00 49.85  ? 801 ILE A O   1 
ATOM 6210 C CB  . ILE A 1 818 ? 91.685  118.581 116.642 1.00 49.85  ? 801 ILE A CB  1 
ATOM 6211 C CG1 . ILE A 1 818 ? 92.763  117.876 115.818 1.00 49.85  ? 801 ILE A CG1 1 
ATOM 6212 C CG2 . ILE A 1 818 ? 90.402  117.762 116.652 1.00 49.85  ? 801 ILE A CG2 1 
ATOM 6213 C CD1 . ILE A 1 818 ? 92.304  117.457 114.442 1.00 49.85  ? 801 ILE A CD1 1 
ATOM 6214 N N   . PRO A 1 819 ? 89.469  120.905 117.330 1.00 49.85  ? 802 PRO A N   1 
ATOM 6215 C CA  . PRO A 1 819 ? 88.055  121.321 117.368 1.00 49.85  ? 802 PRO A CA  1 
ATOM 6216 C C   . PRO A 1 819 ? 87.697  122.398 116.359 1.00 49.85  ? 802 PRO A C   1 
ATOM 6217 O O   . PRO A 1 819 ? 86.570  122.393 115.844 1.00 49.85  ? 802 PRO A O   1 
ATOM 6218 C CB  . PRO A 1 819 ? 87.882  121.819 118.807 1.00 49.85  ? 802 PRO A CB  1 
ATOM 6219 C CG  . PRO A 1 819 ? 88.857  121.026 119.581 1.00 49.85  ? 802 PRO A CG  1 
ATOM 6220 C CD  . PRO A 1 819 ? 90.055  120.893 118.684 1.00 49.85  ? 802 PRO A CD  1 
ATOM 6221 N N   . TYR A 1 820 ? 88.613  123.323 116.060 1.00 49.85  ? 803 TYR A N   1 
ATOM 6222 C CA  . TYR A 1 820 ? 88.321  124.349 115.063 1.00 49.85  ? 803 TYR A CA  1 
ATOM 6223 C C   . TYR A 1 820 ? 88.032  123.725 113.704 1.00 49.85  ? 803 TYR A C   1 
ATOM 6224 O O   . TYR A 1 820 ? 87.086  124.126 113.016 1.00 49.85  ? 803 TYR A O   1 
ATOM 6225 C CB  . TYR A 1 820 ? 89.487  125.333 114.957 1.00 49.85  ? 803 TYR A CB  1 
ATOM 6226 C CG  . TYR A 1 820 ? 89.566  126.333 116.088 1.00 49.85  ? 803 TYR A CG  1 
ATOM 6227 C CD1 . TYR A 1 820 ? 88.534  126.457 117.008 1.00 49.85  ? 803 TYR A CD1 1 
ATOM 6228 C CD2 . TYR A 1 820 ? 90.674  127.158 116.231 1.00 49.85  ? 803 TYR A CD2 1 
ATOM 6229 C CE1 . TYR A 1 820 ? 88.605  127.372 118.041 1.00 49.85  ? 803 TYR A CE1 1 
ATOM 6230 C CE2 . TYR A 1 820 ? 90.754  128.075 117.260 1.00 49.85  ? 803 TYR A CE2 1 
ATOM 6231 C CZ  . TYR A 1 820 ? 89.717  128.179 118.162 1.00 49.85  ? 803 TYR A CZ  1 
ATOM 6232 O OH  . TYR A 1 820 ? 89.793  129.092 119.189 1.00 49.85  ? 803 TYR A OH  1 
ATOM 6233 N N   . GLY A 1 821 ? 88.837  122.742 113.302 1.00 49.85  ? 804 GLY A N   1 
ATOM 6234 C CA  . GLY A 1 821 ? 88.560  122.036 112.062 1.00 49.85  ? 804 GLY A CA  1 
ATOM 6235 C C   . GLY A 1 821 ? 87.304  121.188 112.144 1.00 49.85  ? 804 GLY A C   1 
ATOM 6236 O O   . GLY A 1 821 ? 86.526  121.119 111.188 1.00 49.85  ? 804 GLY A O   1 
ATOM 6237 N N   . VAL A 1 822 ? 87.100  120.520 113.283 1.00 49.85  ? 805 VAL A N   1 
ATOM 6238 C CA  . VAL A 1 822 ? 85.974  119.603 113.430 1.00 49.85  ? 805 VAL A CA  1 
ATOM 6239 C C   . VAL A 1 822 ? 84.653  120.352 113.316 1.00 49.85  ? 805 VAL A C   1 
ATOM 6240 O O   . VAL A 1 822 ? 83.690  119.852 112.726 1.00 49.85  ? 805 VAL A O   1 
ATOM 6241 C CB  . VAL A 1 822 ? 86.082  118.833 114.760 1.00 49.85  ? 805 VAL A CB  1 
ATOM 6242 C CG1 . VAL A 1 822 ? 84.785  118.104 115.068 1.00 49.85  ? 805 VAL A CG1 1 
ATOM 6243 C CG2 . VAL A 1 822 ? 87.237  117.849 114.702 1.00 49.85  ? 805 VAL A CG2 1 
ATOM 6244 N N   . LYS A 1 823 ? 84.587  121.562 113.873 1.00 56.90  ? 806 LYS A N   1 
ATOM 6245 C CA  . LYS A 1 823 ? 83.387  122.381 113.726 1.00 56.90  ? 806 LYS A CA  1 
ATOM 6246 C C   . LYS A 1 823 ? 83.102  122.672 112.256 1.00 56.90  ? 806 LYS A C   1 
ATOM 6247 O O   . LYS A 1 823 ? 81.963  122.532 111.786 1.00 56.90  ? 806 LYS A O   1 
ATOM 6248 C CB  . LYS A 1 823 ? 83.553  123.679 114.518 1.00 56.90  ? 806 LYS A CB  1 
ATOM 6249 C CG  . LYS A 1 823 ? 82.514  124.752 114.237 1.00 56.90  ? 806 LYS A CG  1 
ATOM 6250 C CD  . LYS A 1 823 ? 81.142  124.350 114.748 1.00 56.90  ? 806 LYS A CD  1 
ATOM 6251 C CE  . LYS A 1 823 ? 80.167  125.515 114.672 1.00 56.90  ? 806 LYS A CE  1 
ATOM 6252 N NZ  . LYS A 1 823 ? 79.924  125.960 113.274 1.00 56.90  ? 806 LYS A NZ  1 
ATOM 6253 N N   . ARG A 1 824 ? 84.139  123.059 111.508 1.00 56.94  ? 807 ARG A N   1 
ATOM 6254 C CA  . ARG A 1 824 ? 83.962  123.371 110.094 1.00 56.94  ? 807 ARG A CA  1 
ATOM 6255 C C   . ARG A 1 824 ? 83.511  122.149 109.306 1.00 56.94  ? 807 ARG A C   1 
ATOM 6256 O O   . ARG A 1 824 ? 82.611  122.245 108.466 1.00 56.94  ? 807 ARG A O   1 
ATOM 6257 C CB  . ARG A 1 824 ? 85.258  123.935 109.513 1.00 56.94  ? 807 ARG A CB  1 
ATOM 6258 C CG  . ARG A 1 824 ? 85.551  125.365 109.927 1.00 56.94  ? 807 ARG A CG  1 
ATOM 6259 C CD  . ARG A 1 824 ? 84.618  126.337 109.225 1.00 56.94  ? 807 ARG A CD  1 
ATOM 6260 N NE  . ARG A 1 824 ? 85.224  127.652 109.056 1.00 56.94  ? 807 ARG A NE  1 
ATOM 6261 C CZ  . ARG A 1 824 ? 84.548  128.793 109.054 1.00 56.94  ? 807 ARG A CZ  1 
ATOM 6262 N NH1 . ARG A 1 824 ? 83.235  128.819 109.210 1.00 56.94  ? 807 ARG A NH1 1 
ATOM 6263 N NH2 . ARG A 1 824 ? 85.207  129.937 108.892 1.00 56.94  ? 807 ARG A NH2 1 
ATOM 6264 N N   . LEU A 1 825 ? 84.114  120.987 109.565 1.00 53.82  ? 808 LEU A N   1 
ATOM 6265 C CA  . LEU A 1 825 ? 83.701  119.805 108.814 1.00 53.82  ? 808 LEU A CA  1 
ATOM 6266 C C   . LEU A 1 825 ? 82.339  119.280 109.250 1.00 53.82  ? 808 LEU A C   1 
ATOM 6267 O O   . LEU A 1 825 ? 81.648  118.661 108.439 1.00 53.82  ? 808 LEU A O   1 
ATOM 6268 C CB  . LEU A 1 825 ? 84.729  118.674 108.894 1.00 53.82  ? 808 LEU A CB  1 
ATOM 6269 C CG  . LEU A 1 825 ? 86.100  118.864 108.239 1.00 53.82  ? 808 LEU A CG  1 
ATOM 6270 C CD1 . LEU A 1 825 ? 87.212  118.970 109.258 1.00 53.82  ? 808 LEU A CD1 1 
ATOM 6271 C CD2 . LEU A 1 825 ? 86.377  117.758 107.238 1.00 53.82  ? 808 LEU A CD2 1 
ATOM 6272 N N   . GLU A 1 826 ? 81.925  119.515 110.496 1.00 63.44  ? 809 GLU A N   1 
ATOM 6273 C CA  . GLU A 1 826 ? 80.563  119.161 110.876 1.00 63.44  ? 809 GLU A CA  1 
ATOM 6274 C C   . GLU A 1 826 ? 79.553  120.055 110.169 1.00 63.44  ? 809 GLU A C   1 
ATOM 6275 O O   . GLU A 1 826 ? 78.504  119.580 109.716 1.00 63.44  ? 809 GLU A O   1 
ATOM 6276 C CB  . GLU A 1 826 ? 80.398  119.239 112.393 1.00 63.44  ? 809 GLU A CB  1 
ATOM 6277 C CG  . GLU A 1 826 ? 80.909  118.007 113.122 1.00 63.44  ? 809 GLU A CG  1 
ATOM 6278 C CD  . GLU A 1 826 ? 80.022  117.602 114.281 1.00 63.44  ? 809 GLU A CD  1 
ATOM 6279 O OE1 . GLU A 1 826 ? 79.129  118.392 114.652 1.00 63.44  ? 809 GLU A OE1 1 
ATOM 6280 O OE2 . GLU A 1 826 ? 80.216  116.492 114.820 1.00 63.44  ? 809 GLU A OE2 1 
ATOM 6281 N N   . ASP A 1 827 ? 79.860  121.349 110.047 1.00 61.76  ? 810 ASP A N   1 
ATOM 6282 C CA  . ASP A 1 827 ? 79.015  122.223 109.236 1.00 61.76  ? 810 ASP A CA  1 
ATOM 6283 C C   . ASP A 1 827 ? 79.002  121.773 107.779 1.00 61.76  ? 810 ASP A C   1 
ATOM 6284 O O   . ASP A 1 827 ? 77.961  121.825 107.111 1.00 61.76  ? 810 ASP A O   1 
ATOM 6285 C CB  . ASP A 1 827 ? 79.489  123.670 109.350 1.00 61.76  ? 810 ASP A CB  1 
ATOM 6286 C CG  . ASP A 1 827 ? 79.585  124.139 110.785 1.00 61.76  ? 810 ASP A CG  1 
ATOM 6287 O OD1 . ASP A 1 827 ? 79.239  123.354 111.693 1.00 61.76  ? 810 ASP A OD1 1 
ATOM 6288 O OD2 . ASP A 1 827 ? 80.008  125.293 111.008 1.00 61.76  ? 810 ASP A OD2 1 
ATOM 6289 N N   . PHE A 1 828 ? 80.154  121.333 107.270 1.00 60.37  ? 811 PHE A N   1 
ATOM 6290 C CA  . PHE A 1 828 ? 80.229  120.823 105.904 1.00 60.37  ? 811 PHE A CA  1 
ATOM 6291 C C   . PHE A 1 828 ? 79.357  119.585 105.728 1.00 60.37  ? 811 PHE A C   1 
ATOM 6292 O O   . PHE A 1 828 ? 78.651  119.452 104.724 1.00 60.37  ? 811 PHE A O   1 
ATOM 6293 C CB  . PHE A 1 828 ? 81.688  120.521 105.552 1.00 60.37  ? 811 PHE A CB  1 
ATOM 6294 C CG  . PHE A 1 828 ? 81.859  119.485 104.481 1.00 60.37  ? 811 PHE A CG  1 
ATOM 6295 C CD1 . PHE A 1 828 ? 81.332  119.673 103.214 1.00 60.37  ? 811 PHE A CD1 1 
ATOM 6296 C CD2 . PHE A 1 828 ? 82.551  118.317 104.745 1.00 60.37  ? 811 PHE A CD2 1 
ATOM 6297 C CE1 . PHE A 1 828 ? 81.492  118.714 102.237 1.00 60.37  ? 811 PHE A CE1 1 
ATOM 6298 C CE2 . PHE A 1 828 ? 82.715  117.356 103.771 1.00 60.37  ? 811 PHE A CE2 1 
ATOM 6299 C CZ  . PHE A 1 828 ? 82.184  117.554 102.516 1.00 60.37  ? 811 PHE A CZ  1 
ATOM 6300 N N   . ASP A 1 829 ? 79.395  118.666 106.695 1.00 66.18  ? 812 ASP A N   1 
ATOM 6301 C CA  . ASP A 1 829 ? 78.540  117.485 106.635 1.00 66.18  ? 812 ASP A CA  1 
ATOM 6302 C C   . ASP A 1 829 ? 77.069  117.872 106.685 1.00 66.18  ? 812 ASP A C   1 
ATOM 6303 O O   . ASP A 1 829 ? 76.238  117.281 105.984 1.00 66.18  ? 812 ASP A O   1 
ATOM 6304 C CB  . ASP A 1 829 ? 78.882  116.530 107.778 1.00 66.18  ? 812 ASP A CB  1 
ATOM 6305 C CG  . ASP A 1 829 ? 79.822  115.420 107.352 1.00 66.18  ? 812 ASP A CG  1 
ATOM 6306 O OD1 . ASP A 1 829 ? 80.180  115.368 106.157 1.00 66.18  ? 812 ASP A OD1 1 
ATOM 6307 O OD2 . ASP A 1 829 ? 80.203  114.599 108.213 1.00 66.18  ? 812 ASP A OD2 1 
ATOM 6308 N N   . ALA A 1 830 ? 76.727  118.854 107.523 1.00 67.99  ? 813 ALA A N   1 
ATOM 6309 C CA  . ALA A 1 830 ? 75.347  119.321 107.594 1.00 67.99  ? 813 ALA A CA  1 
ATOM 6310 C C   . ALA A 1 830 ? 74.892  119.901 106.261 1.00 67.99  ? 813 ALA A C   1 
ATOM 6311 O O   . ALA A 1 830 ? 73.759  119.666 105.827 1.00 67.99  ? 813 ALA A O   1 
ATOM 6312 C CB  . ALA A 1 830 ? 75.198  120.354 108.710 1.00 67.99  ? 813 ALA A CB  1 
ATOM 6313 N N   . SER A 1 831 ? 75.762  120.666 105.600 1.00 67.62  ? 814 SER A N   1 
ATOM 6314 C CA  . SER A 1 831 ? 75.432  121.235 104.299 1.00 67.62  ? 814 SER A CA  1 
ATOM 6315 C C   . SER A 1 831 ? 75.463  120.205 103.177 1.00 67.62  ? 814 SER A C   1 
ATOM 6316 O O   . SER A 1 831 ? 74.873  120.443 102.118 1.00 67.62  ? 814 SER A O   1 
ATOM 6317 C CB  . SER A 1 831 ? 76.392  122.379 103.966 1.00 67.62  ? 814 SER A CB  1 
ATOM 6318 O OG  . SER A 1 831 ? 77.741  121.962 104.081 1.00 67.62  ? 814 SER A OG  1 
ATOM 6319 N N   . LEU A 1 832 ? 76.141  119.077 103.379 1.00 65.91  ? 815 LEU A N   1 
ATOM 6320 C CA  . LEU A 1 832 ? 76.257  118.060 102.342 1.00 65.91  ? 815 LEU A CA  1 
ATOM 6321 C C   . LEU A 1 832 ? 75.150  117.015 102.401 1.00 65.91  ? 815 LEU A C   1 
ATOM 6322 O O   . LEU A 1 832 ? 74.719  116.527 101.350 1.00 65.91  ? 815 LEU A O   1 
ATOM 6323 C CB  . LEU A 1 832 ? 77.622  117.371 102.442 1.00 65.91  ? 815 LEU A CB  1 
ATOM 6324 C CG  . LEU A 1 832 ? 77.770  115.937 101.926 1.00 65.91  ? 815 LEU A CG  1 
ATOM 6325 C CD1 . LEU A 1 832 ? 77.815  115.908 100.406 1.00 65.91  ? 815 LEU A CD1 1 
ATOM 6326 C CD2 . LEU A 1 832 ? 79.009  115.280 102.514 1.00 65.91  ? 815 LEU A CD2 1 
ATOM 6327 N N   . LYS A 1 833 ? 74.685  116.653 103.600 1.00 74.77  ? 816 LYS A N   1 
ATOM 6328 C CA  . LYS A 1 833 ? 73.684  115.593 103.707 1.00 74.77  ? 816 LYS A CA  1 
ATOM 6329 C C   . LYS A 1 833 ? 72.371  115.996 103.042 1.00 74.77  ? 816 LYS A C   1 
ATOM 6330 O O   . LYS A 1 833 ? 71.763  115.202 102.315 1.00 74.77  ? 816 LYS A O   1 
ATOM 6331 C CB  . LYS A 1 833 ? 73.457  115.209 105.173 1.00 74.77  ? 816 LYS A CB  1 
ATOM 6332 C CG  . LYS A 1 833 ? 73.102  116.355 106.106 1.00 74.77  ? 816 LYS A CG  1 
ATOM 6333 C CD  . LYS A 1 833 ? 73.095  115.893 107.559 1.00 74.77  ? 816 LYS A CD  1 
ATOM 6334 C CE  . LYS A 1 833 ? 74.494  115.842 108.147 1.00 74.77  ? 816 LYS A CE  1 
ATOM 6335 N NZ  . LYS A 1 833 ? 74.488  116.028 109.624 1.00 74.77  ? 816 LYS A NZ  1 
ATOM 6336 N N   . ASP A 1 834 ? 71.919  117.232 103.273 1.00 79.71  ? 817 ASP A N   1 
ATOM 6337 C CA  . ASP A 1 834 ? 70.672  117.683 102.661 1.00 79.71  ? 817 ASP A CA  1 
ATOM 6338 C C   . ASP A 1 834 ? 70.813  117.803 101.149 1.00 79.71  ? 817 ASP A C   1 
ATOM 6339 O O   . ASP A 1 834 ? 69.881  117.477 100.404 1.00 79.71  ? 817 ASP A O   1 
ATOM 6340 C CB  . ASP A 1 834 ? 70.237  119.016 103.266 1.00 79.71  ? 817 ASP A CB  1 
ATOM 6341 C CG  . ASP A 1 834 ? 71.368  120.017 103.336 1.00 79.71  ? 817 ASP A CG  1 
ATOM 6342 O OD1 . ASP A 1 834 ? 72.536  119.582 103.351 1.00 79.71  ? 817 ASP A OD1 1 
ATOM 6343 O OD2 . ASP A 1 834 ? 71.090  121.234 103.373 1.00 79.71  ? 817 ASP A OD2 1 
ATOM 6344 N N   . ALA A 1 835 ? 71.970  118.275 100.677 1.00 78.04  ? 818 ALA A N   1 
ATOM 6345 C CA  . ALA A 1 835 ? 72.201  118.354 99.240  1.00 78.04  ? 818 ALA A CA  1 
ATOM 6346 C C   . ALA A 1 835 ? 72.168  116.972 98.604  1.00 78.04  ? 818 ALA A C   1 
ATOM 6347 O O   . ALA A 1 835 ? 71.578  116.786 97.534  1.00 78.04  ? 818 ALA A O   1 
ATOM 6348 C CB  . ALA A 1 835 ? 73.535  119.045 98.958  1.00 78.04  ? 818 ALA A CB  1 
ATOM 6349 N N   . LEU A 1 836 ? 72.783  115.984 99.255  1.00 80.02  ? 819 LEU A N   1 
ATOM 6350 C CA  . LEU A 1 836 ? 72.751  114.625 98.726  1.00 80.02  ? 819 LEU A CA  1 
ATOM 6351 C C   . LEU A 1 836 ? 71.335  114.059 98.753  1.00 80.02  ? 819 LEU A C   1 
ATOM 6352 O O   . LEU A 1 836 ? 70.919  113.362 97.819  1.00 80.02  ? 819 LEU A O   1 
ATOM 6353 C CB  . LEU A 1 836 ? 73.713  113.737 99.516  1.00 80.02  ? 819 LEU A CB  1 
ATOM 6354 C CG  . LEU A 1 836 ? 74.482  112.655 98.751  1.00 80.02  ? 819 LEU A CG  1 
ATOM 6355 C CD1 . LEU A 1 836 ? 75.537  112.021 99.644  1.00 80.02  ? 819 LEU A CD1 1 
ATOM 6356 C CD2 . LEU A 1 836 ? 73.551  111.593 98.192  1.00 80.02  ? 819 LEU A CD2 1 
ATOM 6357 N N   . LEU A 1 837 ? 70.577  114.354 99.814  1.00 81.89  ? 820 LEU A N   1 
ATOM 6358 C CA  . LEU A 1 837 ? 69.195  113.890 99.891  1.00 81.89  ? 820 LEU A CA  1 
ATOM 6359 C C   . LEU A 1 837 ? 68.355  114.489 98.769  1.00 81.89  ? 820 LEU A C   1 
ATOM 6360 O O   . LEU A 1 837 ? 67.485  113.816 98.206  1.00 81.89  ? 820 LEU A O   1 
ATOM 6361 C CB  . LEU A 1 837 ? 68.603  114.235 101.258 1.00 81.89  ? 820 LEU A CB  1 
ATOM 6362 C CG  . LEU A 1 837 ? 67.433  113.384 101.760 1.00 81.89  ? 820 LEU A CG  1 
ATOM 6363 C CD1 . LEU A 1 837 ? 67.428  113.339 103.280 1.00 81.89  ? 820 LEU A CD1 1 
ATOM 6364 C CD2 . LEU A 1 837 ? 66.102  113.907 101.239 1.00 81.89  ? 820 LEU A CD2 1 
ATOM 6365 N N   . LYS A 1 838 ? 68.591  115.760 98.444  1.00 85.04  ? 821 LYS A N   1 
ATOM 6366 C CA  . LYS A 1 838 ? 67.952  116.354 97.274  1.00 85.04  ? 821 LYS A CA  1 
ATOM 6367 C C   . LYS A 1 838 ? 68.415  115.668 95.993  1.00 85.04  ? 821 LYS A C   1 
ATOM 6368 O O   . LYS A 1 838 ? 67.625  115.473 95.061  1.00 85.04  ? 821 LYS A O   1 
ATOM 6369 C CB  . LYS A 1 838 ? 68.247  117.854 97.222  1.00 85.04  ? 821 LYS A CB  1 
ATOM 6370 C CG  . LYS A 1 838 ? 67.960  118.507 95.880  1.00 85.04  ? 821 LYS A CG  1 
ATOM 6371 C CD  . LYS A 1 838 ? 68.214  120.005 95.929  1.00 85.04  ? 821 LYS A CD  1 
ATOM 6372 C CE  . LYS A 1 838 ? 67.892  120.664 94.598  1.00 85.04  ? 821 LYS A CE  1 
ATOM 6373 N NZ  . LYS A 1 838 ? 66.475  120.442 94.197  1.00 85.04  ? 821 LYS A NZ  1 
ATOM 6374 N N   . TYR A 1 839 ? 69.695  115.293 95.935  1.00 86.28  ? 822 TYR A N   1 
ATOM 6375 C CA  . TYR A 1 839 ? 70.239  114.644 94.745  1.00 86.28  ? 822 TYR A CA  1 
ATOM 6376 C C   . TYR A 1 839 ? 69.563  113.307 94.472  1.00 86.28  ? 822 TYR A C   1 
ATOM 6377 O O   . TYR A 1 839 ? 69.273  112.977 93.316  1.00 86.28  ? 822 TYR A O   1 
ATOM 6378 C CB  . TYR A 1 839 ? 71.748  114.457 94.896  1.00 86.28  ? 822 TYR A CB  1 
ATOM 6379 C CG  . TYR A 1 839 ? 72.358  113.525 93.873  1.00 86.28  ? 822 TYR A CG  1 
ATOM 6380 C CD1 . TYR A 1 839 ? 72.518  113.919 92.552  1.00 86.28  ? 822 TYR A CD1 1 
ATOM 6381 C CD2 . TYR A 1 839 ? 72.780  112.252 94.232  1.00 86.28  ? 822 TYR A CD2 1 
ATOM 6382 C CE1 . TYR A 1 839 ? 73.077  113.070 91.616  1.00 86.28  ? 822 TYR A CE1 1 
ATOM 6383 C CE2 . TYR A 1 839 ? 73.340  111.396 93.303  1.00 86.28  ? 822 TYR A CE2 1 
ATOM 6384 C CZ  . TYR A 1 839 ? 73.486  111.810 91.997  1.00 86.28  ? 822 TYR A CZ  1 
ATOM 6385 O OH  . TYR A 1 839 ? 74.043  110.961 91.069  1.00 86.28  ? 822 TYR A OH  1 
ATOM 6386 N N   . ILE A 1 840 ? 69.311  112.515 95.519  1.00 84.48  ? 823 ILE A N   1 
ATOM 6387 C CA  . ILE A 1 840 ? 68.696  111.208 95.303  1.00 84.48  ? 823 ILE A CA  1 
ATOM 6388 C C   . ILE A 1 840 ? 67.268  111.330 94.785  1.00 84.48  ? 823 ILE A C   1 
ATOM 6389 O O   . ILE A 1 840 ? 66.741  110.373 94.205  1.00 84.48  ? 823 ILE A O   1 
ATOM 6390 C CB  . ILE A 1 840 ? 68.724  110.347 96.583  1.00 84.48  ? 823 ILE A CB  1 
ATOM 6391 C CG1 . ILE A 1 840 ? 67.591  110.742 97.531  1.00 84.48  ? 823 ILE A CG1 1 
ATOM 6392 C CG2 . ILE A 1 840 ? 70.080  110.429 97.264  1.00 84.48  ? 823 ILE A CG2 1 
ATOM 6393 C CD1 . ILE A 1 840 ? 67.254  109.681 98.551  1.00 84.48  ? 823 ILE A CD1 1 
ATOM 6394 N N   . TYR A 1 841 ? 66.625  112.478 94.972  1.00 86.17  ? 824 TYR A N   1 
ATOM 6395 C CA  . TYR A 1 841 ? 65.272  112.681 94.470  1.00 86.17  ? 824 TYR A CA  1 
ATOM 6396 C C   . TYR A 1 841 ? 65.302  113.212 93.040  1.00 86.17  ? 824 TYR A C   1 
ATOM 6397 O O   . TYR A 1 841 ? 65.942  112.630 92.165  1.00 86.17  ? 824 TYR A O   1 
ATOM 6398 C CB  . TYR A 1 841 ? 64.499  113.642 95.377  1.00 86.17  ? 824 TYR A CB  1 
ATOM 6399 C CG  . TYR A 1 841 ? 63.027  113.318 95.504  1.00 86.17  ? 824 TYR A CG  1 
ATOM 6400 C CD1 . TYR A 1 841 ? 62.342  112.682 94.476  1.00 86.17  ? 824 TYR A CD1 1 
ATOM 6401 C CD2 . TYR A 1 841 ? 62.322  113.646 96.655  1.00 86.17  ? 824 TYR A CD2 1 
ATOM 6402 C CE1 . TYR A 1 841 ? 60.998  112.385 94.590  1.00 86.17  ? 824 TYR A CE1 1 
ATOM 6403 C CE2 . TYR A 1 841 ? 60.978  113.352 96.777  1.00 86.17  ? 824 TYR A CE2 1 
ATOM 6404 C CZ  . TYR A 1 841 ? 60.321  112.721 95.742  1.00 86.17  ? 824 TYR A CZ  1 
ATOM 6405 O OH  . TYR A 1 841 ? 58.982  112.427 95.859  1.00 86.17  ? 824 TYR A OH  1 
ATOM 6406 N N   . ILE A 1 848 ? 66.230  106.866 91.055  1.00 90.43  ? 831 ILE A N   1 
ATOM 6407 C CA  . ILE A 1 848 ? 65.146  106.023 91.541  1.00 90.43  ? 831 ILE A CA  1 
ATOM 6408 C C   . ILE A 1 848 ? 65.659  104.613 91.802  1.00 90.43  ? 831 ILE A C   1 
ATOM 6409 O O   . ILE A 1 848 ? 66.743  104.245 91.353  1.00 90.43  ? 831 ILE A O   1 
ATOM 6410 C CB  . ILE A 1 848 ? 63.971  106.000 90.549  1.00 90.43  ? 831 ILE A CB  1 
ATOM 6411 N N   . GLY A 1 849 ? 64.877  103.826 92.536  1.00 93.02  ? 832 GLY A N   1 
ATOM 6412 C CA  . GLY A 1 849 ? 65.258  102.459 92.824  1.00 93.02  ? 832 GLY A CA  1 
ATOM 6413 C C   . GLY A 1 849 ? 65.556  102.218 94.289  1.00 93.02  ? 832 GLY A C   1 
ATOM 6414 O O   . GLY A 1 849 ? 64.651  102.247 95.128  1.00 93.02  ? 832 GLY A O   1 
ATOM 6415 N N   . GLN A 1 850 ? 66.828  101.979 94.608  1.00 100.26 ? 833 GLN A N   1 
ATOM 6416 C CA  . GLN A 1 850 ? 67.247  101.702 95.981  1.00 100.26 ? 833 GLN A CA  1 
ATOM 6417 C C   . GLN A 1 850 ? 67.364  103.005 96.776  1.00 100.26 ? 833 GLN A C   1 
ATOM 6418 O O   . GLN A 1 850 ? 68.435  103.406 97.230  1.00 100.26 ? 833 GLN A O   1 
ATOM 6419 C CB  . GLN A 1 850 ? 68.562  100.933 95.986  1.00 100.26 ? 833 GLN A CB  1 
ATOM 6420 C CG  . GLN A 1 850 ? 68.481  99.553  95.355  1.00 100.26 ? 833 GLN A CG  1 
ATOM 6421 C CD  . GLN A 1 850 ? 69.100  99.511  93.972  1.00 100.26 ? 833 GLN A CD  1 
ATOM 6422 O OE1 . GLN A 1 850 ? 70.286  99.794  93.802  1.00 100.26 ? 833 GLN A OE1 1 
ATOM 6423 N NE2 . GLN A 1 850 ? 68.296  99.164  92.973  1.00 100.26 ? 833 GLN A NE2 1 
ATOM 6424 N N   . VAL A 1 851 ? 66.223  103.679 96.926  1.00 101.79 ? 834 VAL A N   1 
ATOM 6425 C CA  . VAL A 1 851 ? 66.197  104.932 97.674  1.00 101.79 ? 834 VAL A CA  1 
ATOM 6426 C C   . VAL A 1 851 ? 66.484  104.677 99.148  1.00 101.79 ? 834 VAL A C   1 
ATOM 6427 O O   . VAL A 1 851 ? 67.333  105.341 99.760  1.00 101.79 ? 834 VAL A O   1 
ATOM 6428 C CB  . VAL A 1 851 ? 64.845  105.643 97.478  1.00 101.79 ? 834 VAL A CB  1 
ATOM 6429 C CG1 . VAL A 1 851 ? 64.770  106.899 98.334  1.00 101.79 ? 834 VAL A CG1 1 
ATOM 6430 C CG2 . VAL A 1 851 ? 64.633  105.980 96.008  1.00 101.79 ? 834 VAL A CG2 1 
ATOM 6431 N N   . ASP A 1 852 ? 65.793  103.694 99.733  1.00 102.21 ? 835 ASP A N   1 
ATOM 6432 C CA  . ASP A 1 852 ? 65.929  103.437 101.161 1.00 102.21 ? 835 ASP A CA  1 
ATOM 6433 C C   . ASP A 1 852 ? 67.358  103.057 101.517 1.00 102.21 ? 835 ASP A C   1 
ATOM 6434 O O   . ASP A 1 852 ? 67.940  103.621 102.451 1.00 102.21 ? 835 ASP A O   1 
ATOM 6435 C CB  . ASP A 1 852 ? 64.956  102.336 101.584 1.00 102.21 ? 835 ASP A CB  1 
ATOM 6436 C CG  . ASP A 1 852 ? 63.580  102.513 100.971 1.00 102.21 ? 835 ASP A CG  1 
ATOM 6437 O OD1 . ASP A 1 852 ? 63.177  103.676 100.749 1.00 102.21 ? 835 ASP A OD1 1 
ATOM 6438 O OD2 . ASP A 1 852 ? 62.907  101.492 100.706 1.00 102.21 ? 835 ASP A OD2 1 
ATOM 6439 N N   . ARG A 1 853 ? 67.947  102.128 100.757 1.00 104.56 ? 836 ARG A N   1 
ATOM 6440 C CA  . ARG A 1 853 ? 69.302  101.666 101.045 1.00 104.56 ? 836 ARG A CA  1 
ATOM 6441 C C   . ARG A 1 853 ? 70.310  102.802 100.936 1.00 104.56 ? 836 ARG A C   1 
ATOM 6442 O O   . ARG A 1 853 ? 71.207  102.928 101.779 1.00 104.56 ? 836 ARG A O   1 
ATOM 6443 C CB  . ARG A 1 853 ? 69.676  100.524 100.101 1.00 104.56 ? 836 ARG A CB  1 
ATOM 6444 C CG  . ARG A 1 853 ? 71.047  99.930  100.375 1.00 104.56 ? 836 ARG A CG  1 
ATOM 6445 C CD  . ARG A 1 853 ? 71.607  99.224  99.149  1.00 104.56 ? 836 ARG A CD  1 
ATOM 6446 N NE  . ARG A 1 853 ? 71.617  100.086 97.973  1.00 104.56 ? 836 ARG A NE  1 
ATOM 6447 C CZ  . ARG A 1 853 ? 72.715  100.517 97.366  1.00 104.56 ? 836 ARG A CZ  1 
ATOM 6448 N NH1 . ARG A 1 853 ? 73.920  100.174 97.791  1.00 104.56 ? 836 ARG A NH1 1 
ATOM 6449 N NH2 . ARG A 1 853 ? 72.600  101.314 96.308  1.00 104.56 ? 836 ARG A NH2 1 
ATOM 6450 N N   . LEU A 1 854 ? 70.176  103.641 99.906  1.00 101.09 ? 837 LEU A N   1 
ATOM 6451 C CA  . LEU A 1 854 ? 71.060  104.793 99.775  1.00 101.09 ? 837 LEU A CA  1 
ATOM 6452 C C   . LEU A 1 854 ? 70.920  105.727 100.969 1.00 101.09 ? 837 LEU A C   1 
ATOM 6453 O O   . LEU A 1 854 ? 71.921  106.251 101.476 1.00 101.09 ? 837 LEU A O   1 
ATOM 6454 C CB  . LEU A 1 854 ? 70.768  105.539 98.472  1.00 101.09 ? 837 LEU A CB  1 
ATOM 6455 C CG  . LEU A 1 854 ? 71.352  104.953 97.184  1.00 101.09 ? 837 LEU A CG  1 
ATOM 6456 C CD1 . LEU A 1 854 ? 71.252  105.956 96.043  1.00 101.09 ? 837 LEU A CD1 1 
ATOM 6457 C CD2 . LEU A 1 854 ? 72.796  104.526 97.400  1.00 101.09 ? 837 LEU A CD2 1 
ATOM 6458 N N   . LYS A 1 855 ? 69.685  105.951 101.429 1.00 96.40  ? 838 LYS A N   1 
ATOM 6459 C CA  . LYS A 1 855 ? 69.476  106.826 102.579 1.00 96.40  ? 838 LYS A CA  1 
ATOM 6460 C C   . LYS A 1 855 ? 70.137  106.265 103.833 1.00 96.40  ? 838 LYS A C   1 
ATOM 6461 O O   . LYS A 1 855 ? 70.810  106.996 104.571 1.00 96.40  ? 838 LYS A O   1 
ATOM 6462 C CB  . LYS A 1 855 ? 67.982  107.056 102.808 1.00 96.40  ? 838 LYS A CB  1 
ATOM 6463 C CG  . LYS A 1 855 ? 67.307  107.806 101.676 1.00 96.40  ? 838 LYS A CG  1 
ATOM 6464 C CD  . LYS A 1 855 ? 65.797  107.823 101.825 1.00 96.40  ? 838 LYS A CD  1 
ATOM 6465 C CE  . LYS A 1 855 ? 65.384  108.502 103.119 1.00 96.40  ? 838 LYS A CE  1 
ATOM 6466 N NZ  . LYS A 1 855 ? 63.906  108.511 103.286 1.00 96.40  ? 838 LYS A NZ  1 
ATOM 6467 N N   . ASP A 1 856 ? 69.959  104.966 104.099 1.00 99.83  ? 839 ASP A N   1 
ATOM 6468 C CA  . ASP A 1 856 ? 70.623  104.403 105.274 1.00 99.83  ? 839 ASP A CA  1 
ATOM 6469 C C   . ASP A 1 856 ? 72.135  104.496 105.139 1.00 99.83  ? 839 ASP A C   1 
ATOM 6470 O O   . ASP A 1 856 ? 72.829  104.816 106.110 1.00 99.83  ? 839 ASP A O   1 
ATOM 6471 C CB  . ASP A 1 856 ? 70.214  102.952 105.559 1.00 99.83  ? 839 ASP A CB  1 
ATOM 6472 C CG  . ASP A 1 856 ? 68.770  102.653 105.236 1.00 99.83  ? 839 ASP A CG  1 
ATOM 6473 O OD1 . ASP A 1 856 ? 67.884  103.095 106.000 1.00 99.83  ? 839 ASP A OD1 1 
ATOM 6474 O OD2 . ASP A 1 856 ? 68.520  101.962 104.230 1.00 99.83  ? 839 ASP A OD2 1 
ATOM 6475 N N   . LYS A 1 857 ? 72.666  104.232 103.943 1.00 95.65  ? 840 LYS A N   1 
ATOM 6476 C CA  . LYS A 1 857 ? 74.111  104.294 103.758 1.00 95.65  ? 840 LYS A CA  1 
ATOM 6477 C C   . LYS A 1 857 ? 74.644  105.694 104.043 1.00 95.65  ? 840 LYS A C   1 
ATOM 6478 O O   . LYS A 1 857 ? 75.614  105.860 104.792 1.00 95.65  ? 840 LYS A O   1 
ATOM 6479 C CB  . LYS A 1 857 ? 74.480  103.852 102.342 1.00 95.65  ? 840 LYS A CB  1 
ATOM 6480 C CG  . LYS A 1 857 ? 75.976  103.727 102.114 1.00 95.65  ? 840 LYS A CG  1 
ATOM 6481 C CD  . LYS A 1 857 ? 76.287  103.284 100.697 1.00 95.65  ? 840 LYS A CD  1 
ATOM 6482 C CE  . LYS A 1 857 ? 77.757  102.924 100.549 1.00 95.65  ? 840 LYS A CE  1 
ATOM 6483 N NZ  . LYS A 1 857 ? 78.157  101.794 101.433 1.00 95.65  ? 840 LYS A NZ  1 
ATOM 6484 N N   . VAL A 1 858 ? 74.003  106.721 103.476 1.00 91.01  ? 841 VAL A N   1 
ATOM 6485 C CA  . VAL A 1 858 ? 74.520  108.076 103.648 1.00 91.01  ? 841 VAL A CA  1 
ATOM 6486 C C   . VAL A 1 858 ? 74.362  108.531 105.096 1.00 91.01  ? 841 VAL A C   1 
ATOM 6487 O O   . VAL A 1 858 ? 75.284  109.123 105.677 1.00 91.01  ? 841 VAL A O   1 
ATOM 6488 C CB  . VAL A 1 858 ? 73.855  109.055 102.658 1.00 91.01  ? 841 VAL A CB  1 
ATOM 6489 C CG1 . VAL A 1 858 ? 72.343  109.022 102.760 1.00 91.01  ? 841 VAL A CG1 1 
ATOM 6490 C CG2 . VAL A 1 858 ? 74.368  110.462 102.882 1.00 91.01  ? 841 VAL A CG2 1 
ATOM 6491 N N   . ASN A 1 859 ? 73.208  108.248 105.712 1.00 90.14  ? 842 ASN A N   1 
ATOM 6492 C CA  . ASN A 1 859 ? 73.002  108.654 107.098 1.00 90.14  ? 842 ASN A CA  1 
ATOM 6493 C C   . ASN A 1 859 ? 73.981  107.954 108.030 1.00 90.14  ? 842 ASN A C   1 
ATOM 6494 O O   . ASN A 1 859 ? 74.500  108.568 108.968 1.00 90.14  ? 842 ASN A O   1 
ATOM 6495 C CB  . ASN A 1 859 ? 71.560  108.380 107.525 1.00 90.14  ? 842 ASN A CB  1 
ATOM 6496 C CG  . ASN A 1 859 ? 70.564  109.297 106.840 1.00 90.14  ? 842 ASN A CG  1 
ATOM 6497 O OD1 . ASN A 1 859 ? 69.636  108.841 106.172 1.00 90.14  ? 842 ASN A OD1 1 
ATOM 6498 N ND2 . ASN A 1 859 ? 70.753  110.601 107.003 1.00 90.14  ? 842 ASN A ND2 1 
ATOM 6499 N N   . ASN A 1 860 ? 74.249  106.668 107.789 1.00 91.60  ? 843 ASN A N   1 
ATOM 6500 C CA  . ASN A 1 860 ? 75.223  105.949 108.602 1.00 91.60  ? 843 ASN A CA  1 
ATOM 6501 C C   . ASN A 1 860 ? 76.625  106.511 108.407 1.00 91.60  ? 843 ASN A C   1 
ATOM 6502 O O   . ASN A 1 860 ? 77.395  106.622 109.369 1.00 91.60  ? 843 ASN A O   1 
ATOM 6503 C CB  . ASN A 1 860 ? 75.181  104.457 108.263 1.00 91.60  ? 843 ASN A CB  1 
ATOM 6504 C CG  . ASN A 1 860 ? 76.403  103.705 108.759 1.00 91.60  ? 843 ASN A CG  1 
ATOM 6505 O OD1 . ASN A 1 860 ? 77.447  103.686 108.106 1.00 91.60  ? 843 ASN A OD1 1 
ATOM 6506 N ND2 . ASN A 1 860 ? 76.276  103.076 109.922 1.00 91.60  ? 843 ASN A ND2 1 
ATOM 6507 N N   . THR A 1 861 ? 76.977  106.873 107.170 1.00 86.51  ? 844 THR A N   1 
ATOM 6508 C CA  . THR A 1 861 ? 78.341  107.321 106.907 1.00 86.51  ? 844 THR A CA  1 
ATOM 6509 C C   . THR A 1 861 ? 78.608  108.699 107.504 1.00 86.51  ? 844 THR A C   1 
ATOM 6510 O O   . THR A 1 861 ? 79.653  108.913 108.129 1.00 86.51  ? 844 THR A O   1 
ATOM 6511 C CB  . THR A 1 861 ? 78.618  107.328 105.405 1.00 86.51  ? 844 THR A CB  1 
ATOM 6512 O OG1 . THR A 1 861 ? 78.461  106.002 104.885 1.00 86.51  ? 844 THR A OG1 1 
ATOM 6513 C CG2 . THR A 1 861 ? 80.039  107.798 105.139 1.00 86.51  ? 844 THR A CG2 1 
ATOM 6514 N N   . LEU A 1 862 ? 77.684  109.645 107.333 1.00 83.85  ? 845 LEU A N   1 
ATOM 6515 C CA  . LEU A 1 862 ? 77.926  111.000 107.821 1.00 83.85  ? 845 LEU A CA  1 
ATOM 6516 C C   . LEU A 1 862 ? 77.451  111.227 109.252 1.00 83.85  ? 845 LEU A C   1 
ATOM 6517 O O   . LEU A 1 862 ? 77.502  112.365 109.728 1.00 83.85  ? 845 LEU A O   1 
ATOM 6518 C CB  . LEU A 1 862 ? 77.273  112.038 106.902 1.00 83.85  ? 845 LEU A CB  1 
ATOM 6519 C CG  . LEU A 1 862 ? 77.117  111.730 105.415 1.00 83.85  ? 845 LEU A CG  1 
ATOM 6520 C CD1 . LEU A 1 862 ? 76.243  112.790 104.769 1.00 83.85  ? 845 LEU A CD1 1 
ATOM 6521 C CD2 . LEU A 1 862 ? 78.471  111.657 104.730 1.00 83.85  ? 845 LEU A CD2 1 
ATOM 6522 N N   . SER A 1 863 ? 76.992  110.185 109.948 1.00 83.87  ? 846 SER A N   1 
ATOM 6523 C CA  . SER A 1 863 ? 76.532  110.369 111.320 1.00 83.87  ? 846 SER A CA  1 
ATOM 6524 C C   . SER A 1 863 ? 77.687  110.605 112.286 1.00 83.87  ? 846 SER A C   1 
ATOM 6525 O O   . SER A 1 863 ? 77.532  111.346 113.263 1.00 83.87  ? 846 SER A O   1 
ATOM 6526 C CB  . SER A 1 863 ? 75.715  109.159 111.771 1.00 83.87  ? 846 SER A CB  1 
ATOM 6527 O OG  . SER A 1 863 ? 76.218  107.964 111.199 1.00 83.87  ? 846 SER A OG  1 
ATOM 6528 N N   . THR A 1 864 ? 78.844  109.997 112.034 1.00 78.58  ? 847 THR A N   1 
ATOM 6529 C CA  . THR A 1 864 ? 79.964  110.027 112.964 1.00 78.58  ? 847 THR A CA  1 
ATOM 6530 C C   . THR A 1 864 ? 81.191  110.627 112.291 1.00 78.58  ? 847 THR A C   1 
ATOM 6531 O O   . THR A 1 864 ? 81.464  110.355 111.118 1.00 78.58  ? 847 THR A O   1 
ATOM 6532 C CB  . THR A 1 864 ? 80.290  108.619 113.477 1.00 78.58  ? 847 THR A CB  1 
ATOM 6533 O OG1 . THR A 1 864 ? 79.082  107.966 113.886 1.00 78.58  ? 847 THR A OG1 1 
ATOM 6534 C CG2 . THR A 1 864 ? 81.244  108.686 114.661 1.00 78.58  ? 847 THR A CG2 1 
ATOM 6535 N N   . ASP A 1 865 ? 81.923  111.444 113.043 1.00 70.48  ? 848 ASP A N   1 
ATOM 6536 C CA  . ASP A 1 865 ? 83.149  112.042 112.536 1.00 70.48  ? 848 ASP A CA  1 
ATOM 6537 C C   . ASP A 1 865 ? 84.244  110.989 112.396 1.00 70.48  ? 848 ASP A C   1 
ATOM 6538 O O   . ASP A 1 865 ? 84.292  110.005 113.139 1.00 70.48  ? 848 ASP A O   1 
ATOM 6539 C CB  . ASP A 1 865 ? 83.622  113.160 113.465 1.00 70.48  ? 848 ASP A CB  1 
ATOM 6540 C CG  . ASP A 1 865 ? 82.516  114.136 113.813 1.00 70.48  ? 848 ASP A CG  1 
ATOM 6541 O OD1 . ASP A 1 865 ? 81.412  114.015 113.242 1.00 70.48  ? 848 ASP A OD1 1 
ATOM 6542 O OD2 . ASP A 1 865 ? 82.749  115.022 114.661 1.00 70.48  ? 848 ASP A OD2 1 
ATOM 6543 N N   . ILE A 1 866 ? 85.125  111.204 111.428 1.00 64.68  ? 849 ILE A N   1 
ATOM 6544 C CA  . ILE A 1 866 ? 86.264  110.300 111.233 1.00 64.68  ? 849 ILE A CA  1 
ATOM 6545 C C   . ILE A 1 866 ? 87.227  110.451 112.406 1.00 64.68  ? 849 ILE A C   1 
ATOM 6546 O O   . ILE A 1 866 ? 87.591  111.587 112.761 1.00 64.68  ? 849 ILE A O   1 
ATOM 6547 C CB  . ILE A 1 866 ? 86.960  110.600 109.904 1.00 64.68  ? 849 ILE A CB  1 
ATOM 6548 C CG1 . ILE A 1 866 ? 86.135  110.055 108.737 1.00 64.68  ? 849 ILE A CG1 1 
ATOM 6549 C CG2 . ILE A 1 866 ? 88.363  110.012 109.885 1.00 64.68  ? 849 ILE A CG2 1 
ATOM 6550 C CD1 . ILE A 1 866 ? 86.861  110.083 107.409 1.00 64.68  ? 849 ILE A CD1 1 
ATOM 6551 N N   . PRO A 1 867 ? 87.656  109.360 113.041 1.00 65.20  ? 850 PRO A N   1 
ATOM 6552 C CA  . PRO A 1 867 ? 88.565  109.486 114.186 1.00 65.20  ? 850 PRO A CA  1 
ATOM 6553 C C   . PRO A 1 867 ? 89.905  110.079 113.778 1.00 65.20  ? 850 PRO A C   1 
ATOM 6554 O O   . PRO A 1 867 ? 90.395  109.866 112.667 1.00 65.20  ? 850 PRO A O   1 
ATOM 6555 C CB  . PRO A 1 867 ? 88.720  108.042 114.678 1.00 65.20  ? 850 PRO A CB  1 
ATOM 6556 C CG  . PRO A 1 867 ? 88.406  107.201 113.491 1.00 65.20  ? 850 PRO A CG  1 
ATOM 6557 C CD  . PRO A 1 867 ? 87.372  107.954 112.706 1.00 65.20  ? 850 PRO A CD  1 
ATOM 6558 N N   . PHE A 1 868 ? 90.498  110.834 114.700 1.00 54.63  ? 851 PHE A N   1 
ATOM 6559 C CA  . PHE A 1 868 ? 91.794  111.461 114.478 1.00 54.63  ? 851 PHE A CA  1 
ATOM 6560 C C   . PHE A 1 868 ? 92.892  110.485 114.886 1.00 54.63  ? 851 PHE A C   1 
ATOM 6561 O O   . PHE A 1 868 ? 93.011  110.134 116.065 1.00 54.63  ? 851 PHE A O   1 
ATOM 6562 C CB  . PHE A 1 868 ? 91.905  112.763 115.270 1.00 54.63  ? 851 PHE A CB  1 
ATOM 6563 C CG  . PHE A 1 868 ? 93.192  113.511 115.045 1.00 54.63  ? 851 PHE A CG  1 
ATOM 6564 C CD1 . PHE A 1 868 ? 93.911  113.355 113.872 1.00 54.63  ? 851 PHE A CD1 1 
ATOM 6565 C CD2 . PHE A 1 868 ? 93.680  114.372 116.011 1.00 54.63  ? 851 PHE A CD2 1 
ATOM 6566 C CE1 . PHE A 1 868 ? 95.091  114.044 113.670 1.00 54.63  ? 851 PHE A CE1 1 
ATOM 6567 C CE2 . PHE A 1 868 ? 94.859  115.062 115.815 1.00 54.63  ? 851 PHE A CE2 1 
ATOM 6568 C CZ  . PHE A 1 868 ? 95.565  114.898 114.643 1.00 54.63  ? 851 PHE A CZ  1 
ATOM 6569 N N   . GLN A 1 869 ? 93.690  110.053 113.915 1.00 58.68  ? 852 GLN A N   1 
ATOM 6570 C CA  . GLN A 1 869 ? 94.795  109.126 114.145 1.00 58.68  ? 852 GLN A CA  1 
ATOM 6571 C C   . GLN A 1 869 ? 96.096  109.878 113.883 1.00 58.68  ? 852 GLN A C   1 
ATOM 6572 O O   . GLN A 1 869 ? 96.472  110.106 112.730 1.00 58.68  ? 852 GLN A O   1 
ATOM 6573 C CB  . GLN A 1 869 ? 94.665  107.893 113.256 1.00 58.68  ? 852 GLN A CB  1 
ATOM 6574 C CG  . GLN A 1 869 ? 95.609  106.762 113.623 1.00 58.68  ? 852 GLN A CG  1 
ATOM 6575 C CD  . GLN A 1 869 ? 94.910  105.644 114.373 1.00 58.68  ? 852 GLN A CD  1 
ATOM 6576 O OE1 . GLN A 1 869 ? 93.687  105.645 114.514 1.00 58.68  ? 852 GLN A OE1 1 
ATOM 6577 N NE2 . GLN A 1 869 ? 95.686  104.684 114.861 1.00 58.68  ? 852 GLN A NE2 1 
ATOM 6578 N N   . LEU A 1 870 ? 96.781  110.261 114.962 1.00 51.77  ? 853 LEU A N   1 
ATOM 6579 C CA  . LEU A 1 870 ? 98.005  111.045 114.844 1.00 51.77  ? 853 LEU A CA  1 
ATOM 6580 C C   . LEU A 1 870 ? 99.157  110.244 114.247 1.00 51.77  ? 853 LEU A C   1 
ATOM 6581 O O   . LEU A 1 870 ? 100.153 110.839 113.823 1.00 51.77  ? 853 LEU A O   1 
ATOM 6582 C CB  . LEU A 1 870 ? 98.397  111.591 116.219 1.00 51.77  ? 853 LEU A CB  1 
ATOM 6583 C CG  . LEU A 1 870 ? 99.484  112.663 116.312 1.00 51.77  ? 853 LEU A CG  1 
ATOM 6584 C CD1 . LEU A 1 870 ? 99.150  113.844 115.418 1.00 51.77  ? 853 LEU A CD1 1 
ATOM 6585 C CD2 . LEU A 1 870 ? 99.669  113.116 117.751 1.00 51.77  ? 853 LEU A CD2 1 
ATOM 6586 N N   . SER A 1 871 ? 99.041  108.915 114.200 1.00 60.48  ? 854 SER A N   1 
ATOM 6587 C CA  . SER A 1 871 ? 100.146 108.087 113.723 1.00 60.48  ? 854 SER A CA  1 
ATOM 6588 C C   . SER A 1 871 ? 100.436 108.323 112.246 1.00 60.48  ? 854 SER A C   1 
ATOM 6589 O O   . SER A 1 871 ? 101.602 108.400 111.843 1.00 60.48  ? 854 SER A O   1 
ATOM 6590 C CB  . SER A 1 871 ? 99.839  106.611 113.975 1.00 60.48  ? 854 SER A CB  1 
ATOM 6591 O OG  . SER A 1 871 ? 100.890 105.786 113.503 1.00 60.48  ? 854 SER A OG  1 
ATOM 6592 N N   . LYS A 1 872 ? 99.393  108.442 111.424 1.00 59.56  ? 855 LYS A N   1 
ATOM 6593 C CA  . LYS A 1 872 ? 99.579  108.550 109.983 1.00 59.56  ? 855 LYS A CA  1 
ATOM 6594 C C   . LYS A 1 872 ? 100.147 109.895 109.550 1.00 59.56  ? 855 LYS A C   1 
ATOM 6595 O O   . LYS A 1 872 ? 100.598 110.016 108.406 1.00 59.56  ? 855 LYS A O   1 
ATOM 6596 C CB  . LYS A 1 872 ? 98.250  108.312 109.266 1.00 59.56  ? 855 LYS A CB  1 
ATOM 6597 C CG  . LYS A 1 872 ? 97.668  106.924 109.469 1.00 59.56  ? 855 LYS A CG  1 
ATOM 6598 C CD  . LYS A 1 872 ? 96.442  106.709 108.596 1.00 59.56  ? 855 LYS A CD  1 
ATOM 6599 C CE  . LYS A 1 872 ? 95.502  107.903 108.656 1.00 59.56  ? 855 LYS A CE  1 
ATOM 6600 N NZ  . LYS A 1 872 ? 94.704  107.917 109.912 1.00 59.56  ? 855 LYS A NZ  1 
ATOM 6601 N N   . TYR A 1 873 ? 100.140 110.897 110.424 1.00 55.30  ? 856 TYR A N   1 
ATOM 6602 C CA  . TYR A 1 873 ? 100.477 112.267 110.054 1.00 55.30  ? 856 TYR A CA  1 
ATOM 6603 C C   . TYR A 1 873 ? 101.845 112.708 110.546 1.00 55.30  ? 856 TYR A C   1 
ATOM 6604 O O   . TYR A 1 873 ? 102.537 113.449 109.844 1.00 55.30  ? 856 TYR A O   1 
ATOM 6605 C CB  . TYR A 1 873 ? 99.412  113.232 110.591 1.00 55.30  ? 856 TYR A CB  1 
ATOM 6606 C CG  . TYR A 1 873 ? 97.993  112.934 110.141 1.00 55.30  ? 856 TYR A CG  1 
ATOM 6607 C CD1 . TYR A 1 873 ? 97.728  111.995 109.149 1.00 55.30  ? 856 TYR A CD1 1 
ATOM 6608 C CD2 . TYR A 1 873 ? 96.915  113.564 110.740 1.00 55.30  ? 856 TYR A CD2 1 
ATOM 6609 C CE1 . TYR A 1 873 ? 96.439  111.717 108.751 1.00 55.30  ? 856 TYR A CE1 1 
ATOM 6610 C CE2 . TYR A 1 873 ? 95.623  113.288 110.352 1.00 55.30  ? 856 TYR A CE2 1 
ATOM 6611 C CZ  . TYR A 1 873 ? 95.389  112.366 109.356 1.00 55.30  ? 856 TYR A CZ  1 
ATOM 6612 O OH  . TYR A 1 873 ? 94.099  112.091 108.966 1.00 55.30  ? 856 TYR A OH  1 
ATOM 6613 N N   . VAL A 1 874 ? 102.254 112.274 111.734 1.00 55.60  ? 857 VAL A N   1 
ATOM 6614 C CA  . VAL A 1 874 ? 103.562 112.598 112.286 1.00 55.60  ? 857 VAL A CA  1 
ATOM 6615 C C   . VAL A 1 874 ? 104.213 111.306 112.762 1.00 55.60  ? 857 VAL A C   1 
ATOM 6616 O O   . VAL A 1 874 ? 103.553 110.449 113.361 1.00 55.60  ? 857 VAL A O   1 
ATOM 6617 C CB  . VAL A 1 874 ? 103.462 113.637 113.427 1.00 55.60  ? 857 VAL A CB  1 
ATOM 6618 C CG1 . VAL A 1 874 ? 102.646 113.099 114.589 1.00 55.60  ? 857 VAL A CG1 1 
ATOM 6619 C CG2 . VAL A 1 874 ? 104.844 114.063 113.889 1.00 55.60  ? 857 VAL A CG2 1 
ATOM 6620 N N   . ASP A 1 875 ? 105.500 111.153 112.466 1.00 66.45  ? 858 ASP A N   1 
ATOM 6621 C CA  . ASP A 1 875 ? 106.252 109.942 112.787 1.00 66.45  ? 858 ASP A CA  1 
ATOM 6622 C C   . ASP A 1 875 ? 107.369 110.317 113.757 1.00 66.45  ? 858 ASP A C   1 
ATOM 6623 O O   . ASP A 1 875 ? 108.479 110.660 113.343 1.00 66.45  ? 858 ASP A O   1 
ATOM 6624 C CB  . ASP A 1 875 ? 106.800 109.289 111.521 1.00 66.45  ? 858 ASP A CB  1 
ATOM 6625 C CG  . ASP A 1 875 ? 105.703 108.815 110.590 1.00 66.45  ? 858 ASP A CG  1 
ATOM 6626 O OD1 . ASP A 1 875 ? 105.211 109.633 109.784 1.00 66.45  ? 858 ASP A OD1 1 
ATOM 6627 O OD2 . ASP A 1 875 ? 105.331 107.625 110.664 1.00 66.45  ? 858 ASP A OD2 1 
ATOM 6628 N N   . ASN A 1 876 ? 107.070 110.245 115.051 1.00 61.14  ? 859 ASN A N   1 
ATOM 6629 C CA  . ASN A 1 876 ? 108.054 110.515 116.088 1.00 61.14  ? 859 ASN A CA  1 
ATOM 6630 C C   . ASN A 1 876 ? 107.716 109.664 117.301 1.00 61.14  ? 859 ASN A C   1 
ATOM 6631 O O   . ASN A 1 876 ? 106.541 109.488 117.635 1.00 61.14  ? 859 ASN A O   1 
ATOM 6632 C CB  . ASN A 1 876 ? 108.084 112.002 116.464 1.00 61.14  ? 859 ASN A CB  1 
ATOM 6633 C CG  . ASN A 1 876 ? 109.175 112.329 117.465 1.00 61.14  ? 859 ASN A CG  1 
ATOM 6634 O OD1 . ASN A 1 876 ? 110.098 111.543 117.674 1.00 61.14  ? 859 ASN A OD1 1 
ATOM 6635 N ND2 . ASN A 1 876 ? 109.074 113.497 118.088 1.00 61.14  ? 859 ASN A ND2 1 
ATOM 6636 N N   . GLN A 1 877 ? 108.754 109.130 117.948 1.00 72.02  ? 860 GLN A N   1 
ATOM 6637 C CA  . GLN A 1 877 ? 108.537 108.242 119.086 1.00 72.02  ? 860 GLN A CA  1 
ATOM 6638 C C   . GLN A 1 877 ? 107.884 108.974 120.253 1.00 72.02  ? 860 GLN A C   1 
ATOM 6639 O O   . GLN A 1 877 ? 106.942 108.457 120.865 1.00 72.02  ? 860 GLN A O   1 
ATOM 6640 C CB  . GLN A 1 877 ? 109.862 107.613 119.519 1.00 72.02  ? 860 GLN A CB  1 
ATOM 6641 C CG  . GLN A 1 877 ? 111.011 108.602 119.649 1.00 72.02  ? 860 GLN A CG  1 
ATOM 6642 C CD  . GLN A 1 877 ? 112.150 108.068 120.494 1.00 72.02  ? 860 GLN A CD  1 
ATOM 6643 O OE1 . GLN A 1 877 ? 113.303 108.050 120.062 1.00 72.02  ? 860 GLN A OE1 1 
ATOM 6644 N NE2 . GLN A 1 877 ? 111.833 107.629 121.706 1.00 72.02  ? 860 GLN A NE2 1 
ATOM 6645 N N   . ARG A 1 878 ? 108.356 110.182 120.565 1.00 58.95  ? 861 ARG A N   1 
ATOM 6646 C CA  . ARG A 1 878 ? 107.886 110.881 121.758 1.00 58.95  ? 861 ARG A CA  1 
ATOM 6647 C C   . ARG A 1 878 ? 106.433 111.321 121.613 1.00 58.95  ? 861 ARG A C   1 
ATOM 6648 O O   . ARG A 1 878 ? 105.621 111.124 122.526 1.00 58.95  ? 861 ARG A O   1 
ATOM 6649 C CB  . ARG A 1 878 ? 108.788 112.081 122.046 1.00 58.95  ? 861 ARG A CB  1 
ATOM 6650 N N   . LEU A 1 879 ? 106.090 111.931 120.475 1.00 54.54  ? 862 LEU A N   1 
ATOM 6651 C CA  . LEU A 1 879 ? 104.733 112.438 120.289 1.00 54.54  ? 862 LEU A CA  1 
ATOM 6652 C C   . LEU A 1 879 ? 103.715 111.305 120.265 1.00 54.54  ? 862 LEU A C   1 
ATOM 6653 O O   . LEU A 1 879 ? 102.659 111.396 120.902 1.00 54.54  ? 862 LEU A O   1 
ATOM 6654 C CB  . LEU A 1 879 ? 104.655 113.265 119.008 1.00 54.54  ? 862 LEU A CB  1 
ATOM 6655 C CG  . LEU A 1 879 ? 105.760 114.308 118.833 1.00 54.54  ? 862 LEU A CG  1 
ATOM 6656 C CD1 . LEU A 1 879 ? 105.844 114.772 117.389 1.00 54.54  ? 862 LEU A CD1 1 
ATOM 6657 C CD2 . LEU A 1 879 ? 105.537 115.488 119.766 1.00 54.54  ? 862 LEU A CD2 1 
ATOM 6658 N N   . LEU A 1 880 ? 104.014 110.224 119.544 1.00 55.00  ? 863 LEU A N   1 
ATOM 6659 C CA  . LEU A 1 880 ? 103.114 109.075 119.537 1.00 55.00  ? 863 LEU A CA  1 
ATOM 6660 C C   . LEU A 1 880 ? 103.020 108.440 120.919 1.00 55.00  ? 863 LEU A C   1 
ATOM 6661 O O   . LEU A 1 880 ? 101.932 108.044 121.359 1.00 55.00  ? 863 LEU A O   1 
ATOM 6662 C CB  . LEU A 1 880 ? 103.576 108.045 118.506 1.00 55.00  ? 863 LEU A CB  1 
ATOM 6663 C CG  . LEU A 1 880 ? 103.104 108.187 117.057 1.00 55.00  ? 863 LEU A CG  1 
ATOM 6664 C CD1 . LEU A 1 880 ? 101.755 107.511 116.905 1.00 55.00  ? 863 LEU A CD1 1 
ATOM 6665 C CD2 . LEU A 1 880 ? 103.033 109.637 116.598 1.00 55.00  ? 863 LEU A CD2 1 
ATOM 6666 N N   . SER A 1 881 ? 104.153 108.340 121.620 1.00 62.18  ? 864 SER A N   1 
ATOM 6667 C CA  . SER A 1 881 ? 104.156 107.735 122.946 1.00 62.18  ? 864 SER A CA  1 
ATOM 6668 C C   . SER A 1 881 ? 103.283 108.520 123.915 1.00 62.18  ? 864 SER A C   1 
ATOM 6669 O O   . SER A 1 881 ? 102.541 107.929 124.706 1.00 62.18  ? 864 SER A O   1 
ATOM 6670 C CB  . SER A 1 881 ? 105.587 107.634 123.473 1.00 62.18  ? 864 SER A CB  1 
ATOM 6671 O OG  . SER A 1 881 ? 105.942 108.789 124.212 1.00 62.18  ? 864 SER A OG  1 
ATOM 6672 N N   . THR A 1 882 ? 103.363 109.853 123.880 1.00 54.10  ? 865 THR A N   1 
ATOM 6673 C CA  . THR A 1 882 ? 102.525 110.650 124.770 1.00 54.10  ? 865 THR A CA  1 
ATOM 6674 C C   . THR A 1 882 ? 101.078 110.723 124.295 1.00 54.10  ? 865 THR A C   1 
ATOM 6675 O O   . THR A 1 882 ? 100.182 110.937 125.118 1.00 54.10  ? 865 THR A O   1 
ATOM 6676 C CB  . THR A 1 882 ? 103.085 112.065 124.932 1.00 54.10  ? 865 THR A CB  1 
ATOM 6677 O OG1 . THR A 1 882 ? 102.227 112.816 125.799 1.00 54.10  ? 865 THR A OG1 1 
ATOM 6678 C CG2 . THR A 1 882 ? 103.149 112.770 123.600 1.00 54.10  ? 865 THR A CG2 1 
ATOM 6679 N N   . PHE A 1 883 ? 100.827 110.559 122.994 1.00 56.04  ? 866 PHE A N   1 
ATOM 6680 C CA  . PHE A 1 883 ? 99.454  110.533 122.505 1.00 56.04  ? 866 PHE A CA  1 
ATOM 6681 C C   . PHE A 1 883 ? 98.765  109.209 122.803 1.00 56.04  ? 866 PHE A C   1 
ATOM 6682 O O   . PHE A 1 883 ? 97.530  109.146 122.801 1.00 56.04  ? 866 PHE A O   1 
ATOM 6683 C CB  . PHE A 1 883 ? 99.426  110.807 121.000 1.00 56.04  ? 866 PHE A CB  1 
ATOM 6684 C CG  . PHE A 1 883 ? 98.041  110.871 120.422 1.00 56.04  ? 866 PHE A CG  1 
ATOM 6685 C CD1 . PHE A 1 883 ? 97.090  111.719 120.961 1.00 56.04  ? 866 PHE A CD1 1 
ATOM 6686 C CD2 . PHE A 1 883 ? 97.689  110.074 119.346 1.00 56.04  ? 866 PHE A CD2 1 
ATOM 6687 C CE1 . PHE A 1 883 ? 95.815  111.778 120.433 1.00 56.04  ? 866 PHE A CE1 1 
ATOM 6688 C CE2 . PHE A 1 883 ? 96.416  110.128 118.813 1.00 56.04  ? 866 PHE A CE2 1 
ATOM 6689 C CZ  . PHE A 1 883 ? 95.478  110.981 119.358 1.00 56.04  ? 866 PHE A CZ  1 
ATOM 6690 N N   . THR A 1 884 ? 99.537  108.148 123.053 1.00 63.81  ? 867 THR A N   1 
ATOM 6691 C CA  . THR A 1 884 ? 98.939  106.831 123.256 1.00 63.81  ? 867 THR A CA  1 
ATOM 6692 C C   . THR A 1 884 ? 98.014  106.811 124.470 1.00 63.81  ? 867 THR A C   1 
ATOM 6693 O O   . THR A 1 884 ? 96.892  106.296 124.393 1.00 63.81  ? 867 THR A O   1 
ATOM 6694 C CB  . THR A 1 884 ? 100.034 105.774 123.399 1.00 63.81  ? 867 THR A CB  1 
ATOM 6695 O OG1 . THR A 1 884 ? 100.794 105.704 122.186 1.00 63.81  ? 867 THR A OG1 1 
ATOM 6696 C CG2 . THR A 1 884 ? 99.424  104.409 123.683 1.00 63.81  ? 867 THR A CG2 1 
ATOM 6697 N N   . GLU A 1 885 ? 98.457  107.371 125.597 1.00 65.70  ? 868 GLU A N   1 
ATOM 6698 C CA  . GLU A 1 885 ? 97.651  107.373 126.821 1.00 65.70  ? 868 GLU A CA  1 
ATOM 6699 C C   . GLU A 1 885 ? 96.841  108.664 126.858 1.00 65.70  ? 868 GLU A C   1 
ATOM 6700 O O   . GLU A 1 885 ? 97.380  109.772 126.859 1.00 65.70  ? 868 GLU A O   1 
ATOM 6701 C CB  . GLU A 1 885 ? 98.522  107.191 128.064 1.00 65.70  ? 868 GLU A CB  1 
ATOM 6702 C CG  . GLU A 1 885 ? 99.429  108.356 128.496 1.00 65.70  ? 868 GLU A CG  1 
ATOM 6703 C CD  . GLU A 1 885 ? 100.366 108.861 127.414 1.00 65.70  ? 868 GLU A CD  1 
ATOM 6704 O OE1 . GLU A 1 885 ? 100.506 108.195 126.370 1.00 65.70  ? 868 GLU A OE1 1 
ATOM 6705 O OE2 . GLU A 1 885 ? 100.987 109.924 127.624 1.00 65.70  ? 868 GLU A OE2 1 
ATOM 6706 N N   . TYR A 1 886 ? 95.521  108.512 126.853 1.00 70.12  ? 869 TYR A N   1 
ATOM 6707 C CA  . TYR A 1 886 ? 94.603  109.646 126.857 1.00 70.12  ? 869 TYR A CA  1 
ATOM 6708 C C   . TYR A 1 886 ? 93.192  109.198 127.219 1.00 70.12  ? 869 TYR A C   1 
ATOM 6709 O O   . TYR A 1 886 ? 92.340  110.017 127.564 1.00 70.12  ? 869 TYR A O   1 
ATOM 6710 C CB  . TYR A 1 886 ? 94.627  110.353 125.495 1.00 70.12  ? 869 TYR A CB  1 
ATOM 6711 C CG  . TYR A 1 886 ? 93.783  109.702 124.418 1.00 70.12  ? 869 TYR A CG  1 
ATOM 6712 C CD1 . TYR A 1 886 ? 92.433  110.002 124.274 1.00 70.12  ? 869 TYR A CD1 1 
ATOM 6713 C CD2 . TYR A 1 886 ? 94.344  108.780 123.544 1.00 70.12  ? 869 TYR A CD2 1 
ATOM 6714 C CE1 . TYR A 1 886 ? 91.670  109.403 123.288 1.00 70.12  ? 869 TYR A CE1 1 
ATOM 6715 C CE2 . TYR A 1 886 ? 93.590  108.177 122.558 1.00 70.12  ? 869 TYR A CE2 1 
ATOM 6716 C CZ  . TYR A 1 886 ? 92.255  108.491 122.434 1.00 70.12  ? 869 TYR A CZ  1 
ATOM 6717 O OH  . TYR A 1 886 ? 91.504  107.890 121.451 1.00 70.12  ? 869 TYR A OH  1 
# 
