data_8V1G
# 
_entry.id   8V1G 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   8V1G         pdb_00008v1g 10.2210/pdb8v1g/pdb 
WWPDB D_1000279336 ?            ?                   
EMDB  EMD-42885    ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-11-20 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8V1G 
_pdbx_database_status.recvd_initial_deposition_date   2023-11-20 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_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        'plasmodium falciparum Niemann-Pick type C1-related protein bound with MMV009108' 
_pdbx_database_related.db_id          EMD-42885 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              ewy5@case.edu 
_pdbx_contact_author.name_first         Edward 
_pdbx_contact_author.name_last          Yu 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-5912-1227 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Zhang, Z.' 1 0000-0003-0135-4970 
'Lyu, M.'   2 0000-0001-5795-0232 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'plasmodium falciparum Niemann-Pick type C1-related protein bound with MMV009108' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Zhang, Z.' 1 0000-0003-0135-4970 
primary 'Lyu, M.'   2 0000-0001-5795-0232 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Niemann-Pick type C1-related protein'   170505.406 1 ? ? ? ? 
2 non-polymer syn 2-acetamido-2-deoxy-beta-D-glucopyranose 221.208    2 ? ? ? ? 
3 non-polymer syn CHOLESTEROL                              386.654    1 ? ? ? ? 
4 non-polymer syn MMV009108                                415.572    1 ? ? ? ? 
# 
_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       
;MFVKNFIHKLKELKQKSLDKFANLLYDYGGYVYDRPCTFIICSLICCLLLTCGFYFKEHEKDIYKLYSISNSYAYETNET
INDFFYKSRRCFILVESNVNLLKPKILRELQKFEEGTKDIEVDLSEINECKTNSELPPEQSHVAKELYKTLIQRSEENLK
SGKINGSLFDYSDLDENGKSVLSLAGKENNDDTLIEGDNKNDEETSANNNNNEDDNNEDDNNEDDNNEDDNNENDNNNNN
EDDNNNDDDDDEDNEEEDEEKQKSLREKLYRKIYEMLKKKKENIVLDENNPNVNFTDYKDDVFYPYQYIPPMLIKADRCK
LQNVFGDKNLNIDLREASDGLKKQITYTLEDICEKKYGDCNFSSLFLYYEKGNGYIDYPIKVDNLDFYVNRRTYKEMMFK
GILGNMVYEKSGSKYIIKSANAIMTVIPLLNSHTYEPYALAYEKKLIDYVRFYNLDDIIQDEETNDDNDPFIRFHVFTDR
SLEDEVDRISKIDNLTRLLLLIGVLLIFMYALFNNVTSVLYRSKPLCAVMGIFCGFLGFLSGSGFLYFLGVKSVPPAETV
PFLVIGVGVDDVFVILNSYSLLFMVKDNKKRIQMCLKDSALAITVTTLTNIIAFLISAISPFYSICAFSLFTASSLFFGY
LMVLTFLLSFLCIEAKLEKKKRNIFTGTFHLFRSIFMKSSKKNKKENKENNIHDDGDNDNDEKKKDLSLEVKNNEDDYEN
ISIYEWIHNLYLFEESINKKKKNAALVYASNNGMSSNLNNVNEDGFPNPSKIVSMEDVKKRNIKKDDAYINKEDEEGGGY
YNKDDNKKKDILGKKQKKNNNNVTLVSKKGEDNELDVYYENLDEKTNDKYKMNNIKSSKLKYDNDKKDGAIINNRPSSDE
EYKEEKDKNKINILNDVFNDITIKPNENILLDRGDVIKSSGYDSSYNDLQSSSLPNPSSNEVLNKTTMVYNETDLKDNKK
EIKSSKKNVKDIKKSDMIHDDTYDIINSNNKNILLSSNEINNNSNNTNKFNNNSTELATKDTQQFINGHDKNIYLLSSHD
NALFYKYIYEEPKGNIGKYFRSLVKNYYVPFLSSRFGKTIVYIMFTIIIAMSIYGCTLMKKGIKYDKAFPVDSYVRRFTT
AKIKYFPDFGDFIEVYYFDKHFINKYRGLEKNTKEAASSFLYSDLTDRQIMNSPKINKNVHWENTNLQEELINMHNTLES
QEFVTSVANGFTFFLNKNKSSLRKENPQEFYEIFANWLKKDFVGNLFKNDFVFLNGKLVAWRFHYFQKNVDDSEISSKWL
KACKQITKLENHNVQMVCFHLSSIFNETDESIIEVTLINLGITILTILVVTAYIIKGFYSCVIIALIIFLIDLCIFGFMC
LCGITMNIISMVILVLSVGFSIDHTSHIVQAFSHSMGRTRDEKMKESLHLMIGPVLHSGLSTWFVISTLFFSNKDFTVIF
FQTLSLVLFFSITFSSMFLPVLLSSFGPLH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MFVKNFIHKLKELKQKSLDKFANLLYDYGGYVYDRPCTFIICSLICCLLLTCGFYFKEHEKDIYKLYSISNSYAYETNET
INDFFYKSRRCFILVESNVNLLKPKILRELQKFEEGTKDIEVDLSEINECKTNSELPPEQSHVAKELYKTLIQRSEENLK
SGKINGSLFDYSDLDENGKSVLSLAGKENNDDTLIEGDNKNDEETSANNNNNEDDNNEDDNNEDDNNEDDNNENDNNNNN
EDDNNNDDDDDEDNEEEDEEKQKSLREKLYRKIYEMLKKKKENIVLDENNPNVNFTDYKDDVFYPYQYIPPMLIKADRCK
LQNVFGDKNLNIDLREASDGLKKQITYTLEDICEKKYGDCNFSSLFLYYEKGNGYIDYPIKVDNLDFYVNRRTYKEMMFK
GILGNMVYEKSGSKYIIKSANAIMTVIPLLNSHTYEPYALAYEKKLIDYVRFYNLDDIIQDEETNDDNDPFIRFHVFTDR
SLEDEVDRISKIDNLTRLLLLIGVLLIFMYALFNNVTSVLYRSKPLCAVMGIFCGFLGFLSGSGFLYFLGVKSVPPAETV
PFLVIGVGVDDVFVILNSYSLLFMVKDNKKRIQMCLKDSALAITVTTLTNIIAFLISAISPFYSICAFSLFTASSLFFGY
LMVLTFLLSFLCIEAKLEKKKRNIFTGTFHLFRSIFMKSSKKNKKENKENNIHDDGDNDNDEKKKDLSLEVKNNEDDYEN
ISIYEWIHNLYLFEESINKKKKNAALVYASNNGMSSNLNNVNEDGFPNPSKIVSMEDVKKRNIKKDDAYINKEDEEGGGY
YNKDDNKKKDILGKKQKKNNNNVTLVSKKGEDNELDVYYENLDEKTNDKYKMNNIKSSKLKYDNDKKDGAIINNRPSSDE
EYKEEKDKNKINILNDVFNDITIKPNENILLDRGDVIKSSGYDSSYNDLQSSSLPNPSSNEVLNKTTMVYNETDLKDNKK
EIKSSKKNVKDIKKSDMIHDDTYDIINSNNKNILLSSNEINNNSNNTNKFNNNSTELATKDTQQFINGHDKNIYLLSSHD
NALFYKYIYEEPKGNIGKYFRSLVKNYYVPFLSSRFGKTIVYIMFTIIIAMSIYGCTLMKKGIKYDKAFPVDSYVRRFTT
AKIKYFPDFGDFIEVYYFDKHFINKYRGLEKNTKEAASSFLYSDLTDRQIMNSPKINKNVHWENTNLQEELINMHNTLES
QEFVTSVANGFTFFLNKNKSSLRKENPQEFYEIFANWLKKDFVGNLFKNDFVFLNGKLVAWRFHYFQKNVDDSEISSKWL
KACKQITKLENHNVQMVCFHLSSIFNETDESIIEVTLINLGITILTILVVTAYIIKGFYSCVIIALIIFLIDLCIFGFMC
LCGITMNIISMVILVLSVGFSIDHTSHIVQAFSHSMGRTRDEKMKESLHLMIGPVLHSGLSTWFVISTLFFSNKDFTVIF
FQTLSLVLFFSITFSSMFLPVLLSSFGPLH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 2-acetamido-2-deoxy-beta-D-glucopyranose NAG 
3 CHOLESTEROL                              CLR 
4 MMV009108                                Y6F 
# 
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    PHE n 
1 3    VAL n 
1 4    LYS n 
1 5    ASN n 
1 6    PHE n 
1 7    ILE n 
1 8    HIS n 
1 9    LYS n 
1 10   LEU n 
1 11   LYS n 
1 12   GLU n 
1 13   LEU n 
1 14   LYS n 
1 15   GLN n 
1 16   LYS n 
1 17   SER n 
1 18   LEU n 
1 19   ASP n 
1 20   LYS n 
1 21   PHE n 
1 22   ALA n 
1 23   ASN n 
1 24   LEU n 
1 25   LEU n 
1 26   TYR n 
1 27   ASP n 
1 28   TYR n 
1 29   GLY n 
1 30   GLY n 
1 31   TYR n 
1 32   VAL n 
1 33   TYR n 
1 34   ASP n 
1 35   ARG n 
1 36   PRO n 
1 37   CYS n 
1 38   THR n 
1 39   PHE n 
1 40   ILE n 
1 41   ILE n 
1 42   CYS n 
1 43   SER n 
1 44   LEU n 
1 45   ILE n 
1 46   CYS n 
1 47   CYS n 
1 48   LEU n 
1 49   LEU n 
1 50   LEU n 
1 51   THR n 
1 52   CYS n 
1 53   GLY n 
1 54   PHE n 
1 55   TYR n 
1 56   PHE n 
1 57   LYS n 
1 58   GLU n 
1 59   HIS n 
1 60   GLU n 
1 61   LYS n 
1 62   ASP n 
1 63   ILE n 
1 64   TYR n 
1 65   LYS n 
1 66   LEU n 
1 67   TYR n 
1 68   SER n 
1 69   ILE n 
1 70   SER n 
1 71   ASN n 
1 72   SER n 
1 73   TYR n 
1 74   ALA n 
1 75   TYR n 
1 76   GLU n 
1 77   THR n 
1 78   ASN n 
1 79   GLU n 
1 80   THR n 
1 81   ILE n 
1 82   ASN n 
1 83   ASP n 
1 84   PHE n 
1 85   PHE n 
1 86   TYR n 
1 87   LYS n 
1 88   SER n 
1 89   ARG n 
1 90   ARG n 
1 91   CYS n 
1 92   PHE n 
1 93   ILE n 
1 94   LEU n 
1 95   VAL n 
1 96   GLU n 
1 97   SER n 
1 98   ASN n 
1 99   VAL n 
1 100  ASN n 
1 101  LEU n 
1 102  LEU n 
1 103  LYS n 
1 104  PRO n 
1 105  LYS n 
1 106  ILE n 
1 107  LEU n 
1 108  ARG n 
1 109  GLU n 
1 110  LEU n 
1 111  GLN n 
1 112  LYS n 
1 113  PHE n 
1 114  GLU n 
1 115  GLU n 
1 116  GLY n 
1 117  THR n 
1 118  LYS n 
1 119  ASP n 
1 120  ILE n 
1 121  GLU n 
1 122  VAL n 
1 123  ASP n 
1 124  LEU n 
1 125  SER n 
1 126  GLU n 
1 127  ILE n 
1 128  ASN n 
1 129  GLU n 
1 130  CYS n 
1 131  LYS n 
1 132  THR n 
1 133  ASN n 
1 134  SER n 
1 135  GLU n 
1 136  LEU n 
1 137  PRO n 
1 138  PRO n 
1 139  GLU n 
1 140  GLN n 
1 141  SER n 
1 142  HIS n 
1 143  VAL n 
1 144  ALA n 
1 145  LYS n 
1 146  GLU n 
1 147  LEU n 
1 148  TYR n 
1 149  LYS n 
1 150  THR n 
1 151  LEU n 
1 152  ILE n 
1 153  GLN n 
1 154  ARG n 
1 155  SER n 
1 156  GLU n 
1 157  GLU n 
1 158  ASN n 
1 159  LEU n 
1 160  LYS n 
1 161  SER n 
1 162  GLY n 
1 163  LYS n 
1 164  ILE n 
1 165  ASN n 
1 166  GLY n 
1 167  SER n 
1 168  LEU n 
1 169  PHE n 
1 170  ASP n 
1 171  TYR n 
1 172  SER n 
1 173  ASP n 
1 174  LEU n 
1 175  ASP n 
1 176  GLU n 
1 177  ASN n 
1 178  GLY n 
1 179  LYS n 
1 180  SER n 
1 181  VAL n 
1 182  LEU n 
1 183  SER n 
1 184  LEU n 
1 185  ALA n 
1 186  GLY n 
1 187  LYS n 
1 188  GLU n 
1 189  ASN n 
1 190  ASN n 
1 191  ASP n 
1 192  ASP n 
1 193  THR n 
1 194  LEU n 
1 195  ILE n 
1 196  GLU n 
1 197  GLY n 
1 198  ASP n 
1 199  ASN n 
1 200  LYS n 
1 201  ASN n 
1 202  ASP n 
1 203  GLU n 
1 204  GLU n 
1 205  THR n 
1 206  SER n 
1 207  ALA n 
1 208  ASN n 
1 209  ASN n 
1 210  ASN n 
1 211  ASN n 
1 212  ASN n 
1 213  GLU n 
1 214  ASP n 
1 215  ASP n 
1 216  ASN n 
1 217  ASN n 
1 218  GLU n 
1 219  ASP n 
1 220  ASP n 
1 221  ASN n 
1 222  ASN n 
1 223  GLU n 
1 224  ASP n 
1 225  ASP n 
1 226  ASN n 
1 227  ASN n 
1 228  GLU n 
1 229  ASP n 
1 230  ASP n 
1 231  ASN n 
1 232  ASN n 
1 233  GLU n 
1 234  ASN n 
1 235  ASP n 
1 236  ASN n 
1 237  ASN n 
1 238  ASN n 
1 239  ASN n 
1 240  ASN n 
1 241  GLU n 
1 242  ASP n 
1 243  ASP n 
1 244  ASN n 
1 245  ASN n 
1 246  ASN n 
1 247  ASP n 
1 248  ASP n 
1 249  ASP n 
1 250  ASP n 
1 251  ASP n 
1 252  GLU n 
1 253  ASP n 
1 254  ASN n 
1 255  GLU n 
1 256  GLU n 
1 257  GLU n 
1 258  ASP n 
1 259  GLU n 
1 260  GLU n 
1 261  LYS n 
1 262  GLN n 
1 263  LYS n 
1 264  SER n 
1 265  LEU n 
1 266  ARG n 
1 267  GLU n 
1 268  LYS n 
1 269  LEU n 
1 270  TYR n 
1 271  ARG n 
1 272  LYS n 
1 273  ILE n 
1 274  TYR n 
1 275  GLU n 
1 276  MET n 
1 277  LEU n 
1 278  LYS n 
1 279  LYS n 
1 280  LYS n 
1 281  LYS n 
1 282  GLU n 
1 283  ASN n 
1 284  ILE n 
1 285  VAL n 
1 286  LEU n 
1 287  ASP n 
1 288  GLU n 
1 289  ASN n 
1 290  ASN n 
1 291  PRO n 
1 292  ASN n 
1 293  VAL n 
1 294  ASN n 
1 295  PHE n 
1 296  THR n 
1 297  ASP n 
1 298  TYR n 
1 299  LYS n 
1 300  ASP n 
1 301  ASP n 
1 302  VAL n 
1 303  PHE n 
1 304  TYR n 
1 305  PRO n 
1 306  TYR n 
1 307  GLN n 
1 308  TYR n 
1 309  ILE n 
1 310  PRO n 
1 311  PRO n 
1 312  MET n 
1 313  LEU n 
1 314  ILE n 
1 315  LYS n 
1 316  ALA n 
1 317  ASP n 
1 318  ARG n 
1 319  CYS n 
1 320  LYS n 
1 321  LEU n 
1 322  GLN n 
1 323  ASN n 
1 324  VAL n 
1 325  PHE n 
1 326  GLY n 
1 327  ASP n 
1 328  LYS n 
1 329  ASN n 
1 330  LEU n 
1 331  ASN n 
1 332  ILE n 
1 333  ASP n 
1 334  LEU n 
1 335  ARG n 
1 336  GLU n 
1 337  ALA n 
1 338  SER n 
1 339  ASP n 
1 340  GLY n 
1 341  LEU n 
1 342  LYS n 
1 343  LYS n 
1 344  GLN n 
1 345  ILE n 
1 346  THR n 
1 347  TYR n 
1 348  THR n 
1 349  LEU n 
1 350  GLU n 
1 351  ASP n 
1 352  ILE n 
1 353  CYS n 
1 354  GLU n 
1 355  LYS n 
1 356  LYS n 
1 357  TYR n 
1 358  GLY n 
1 359  ASP n 
1 360  CYS n 
1 361  ASN n 
1 362  PHE n 
1 363  SER n 
1 364  SER n 
1 365  LEU n 
1 366  PHE n 
1 367  LEU n 
1 368  TYR n 
1 369  TYR n 
1 370  GLU n 
1 371  LYS n 
1 372  GLY n 
1 373  ASN n 
1 374  GLY n 
1 375  TYR n 
1 376  ILE n 
1 377  ASP n 
1 378  TYR n 
1 379  PRO n 
1 380  ILE n 
1 381  LYS n 
1 382  VAL n 
1 383  ASP n 
1 384  ASN n 
1 385  LEU n 
1 386  ASP n 
1 387  PHE n 
1 388  TYR n 
1 389  VAL n 
1 390  ASN n 
1 391  ARG n 
1 392  ARG n 
1 393  THR n 
1 394  TYR n 
1 395  LYS n 
1 396  GLU n 
1 397  MET n 
1 398  MET n 
1 399  PHE n 
1 400  LYS n 
1 401  GLY n 
1 402  ILE n 
1 403  LEU n 
1 404  GLY n 
1 405  ASN n 
1 406  MET n 
1 407  VAL n 
1 408  TYR n 
1 409  GLU n 
1 410  LYS n 
1 411  SER n 
1 412  GLY n 
1 413  SER n 
1 414  LYS n 
1 415  TYR n 
1 416  ILE n 
1 417  ILE n 
1 418  LYS n 
1 419  SER n 
1 420  ALA n 
1 421  ASN n 
1 422  ALA n 
1 423  ILE n 
1 424  MET n 
1 425  THR n 
1 426  VAL n 
1 427  ILE n 
1 428  PRO n 
1 429  LEU n 
1 430  LEU n 
1 431  ASN n 
1 432  SER n 
1 433  HIS n 
1 434  THR n 
1 435  TYR n 
1 436  GLU n 
1 437  PRO n 
1 438  TYR n 
1 439  ALA n 
1 440  LEU n 
1 441  ALA n 
1 442  TYR n 
1 443  GLU n 
1 444  LYS n 
1 445  LYS n 
1 446  LEU n 
1 447  ILE n 
1 448  ASP n 
1 449  TYR n 
1 450  VAL n 
1 451  ARG n 
1 452  PHE n 
1 453  TYR n 
1 454  ASN n 
1 455  LEU n 
1 456  ASP n 
1 457  ASP n 
1 458  ILE n 
1 459  ILE n 
1 460  GLN n 
1 461  ASP n 
1 462  GLU n 
1 463  GLU n 
1 464  THR n 
1 465  ASN n 
1 466  ASP n 
1 467  ASP n 
1 468  ASN n 
1 469  ASP n 
1 470  PRO n 
1 471  PHE n 
1 472  ILE n 
1 473  ARG n 
1 474  PHE n 
1 475  HIS n 
1 476  VAL n 
1 477  PHE n 
1 478  THR n 
1 479  ASP n 
1 480  ARG n 
1 481  SER n 
1 482  LEU n 
1 483  GLU n 
1 484  ASP n 
1 485  GLU n 
1 486  VAL n 
1 487  ASP n 
1 488  ARG n 
1 489  ILE n 
1 490  SER n 
1 491  LYS n 
1 492  ILE n 
1 493  ASP n 
1 494  ASN n 
1 495  LEU n 
1 496  THR n 
1 497  ARG n 
1 498  LEU n 
1 499  LEU n 
1 500  LEU n 
1 501  LEU n 
1 502  ILE n 
1 503  GLY n 
1 504  VAL n 
1 505  LEU n 
1 506  LEU n 
1 507  ILE n 
1 508  PHE n 
1 509  MET n 
1 510  TYR n 
1 511  ALA n 
1 512  LEU n 
1 513  PHE n 
1 514  ASN n 
1 515  ASN n 
1 516  VAL n 
1 517  THR n 
1 518  SER n 
1 519  VAL n 
1 520  LEU n 
1 521  TYR n 
1 522  ARG n 
1 523  SER n 
1 524  LYS n 
1 525  PRO n 
1 526  LEU n 
1 527  CYS n 
1 528  ALA n 
1 529  VAL n 
1 530  MET n 
1 531  GLY n 
1 532  ILE n 
1 533  PHE n 
1 534  CYS n 
1 535  GLY n 
1 536  PHE n 
1 537  LEU n 
1 538  GLY n 
1 539  PHE n 
1 540  LEU n 
1 541  SER n 
1 542  GLY n 
1 543  SER n 
1 544  GLY n 
1 545  PHE n 
1 546  LEU n 
1 547  TYR n 
1 548  PHE n 
1 549  LEU n 
1 550  GLY n 
1 551  VAL n 
1 552  LYS n 
1 553  SER n 
1 554  VAL n 
1 555  PRO n 
1 556  PRO n 
1 557  ALA n 
1 558  GLU n 
1 559  THR n 
1 560  VAL n 
1 561  PRO n 
1 562  PHE n 
1 563  LEU n 
1 564  VAL n 
1 565  ILE n 
1 566  GLY n 
1 567  VAL n 
1 568  GLY n 
1 569  VAL n 
1 570  ASP n 
1 571  ASP n 
1 572  VAL n 
1 573  PHE n 
1 574  VAL n 
1 575  ILE n 
1 576  LEU n 
1 577  ASN n 
1 578  SER n 
1 579  TYR n 
1 580  SER n 
1 581  LEU n 
1 582  LEU n 
1 583  PHE n 
1 584  MET n 
1 585  VAL n 
1 586  LYS n 
1 587  ASP n 
1 588  ASN n 
1 589  LYS n 
1 590  LYS n 
1 591  ARG n 
1 592  ILE n 
1 593  GLN n 
1 594  MET n 
1 595  CYS n 
1 596  LEU n 
1 597  LYS n 
1 598  ASP n 
1 599  SER n 
1 600  ALA n 
1 601  LEU n 
1 602  ALA n 
1 603  ILE n 
1 604  THR n 
1 605  VAL n 
1 606  THR n 
1 607  THR n 
1 608  LEU n 
1 609  THR n 
1 610  ASN n 
1 611  ILE n 
1 612  ILE n 
1 613  ALA n 
1 614  PHE n 
1 615  LEU n 
1 616  ILE n 
1 617  SER n 
1 618  ALA n 
1 619  ILE n 
1 620  SER n 
1 621  PRO n 
1 622  PHE n 
1 623  TYR n 
1 624  SER n 
1 625  ILE n 
1 626  CYS n 
1 627  ALA n 
1 628  PHE n 
1 629  SER n 
1 630  LEU n 
1 631  PHE n 
1 632  THR n 
1 633  ALA n 
1 634  SER n 
1 635  SER n 
1 636  LEU n 
1 637  PHE n 
1 638  PHE n 
1 639  GLY n 
1 640  TYR n 
1 641  LEU n 
1 642  MET n 
1 643  VAL n 
1 644  LEU n 
1 645  THR n 
1 646  PHE n 
1 647  LEU n 
1 648  LEU n 
1 649  SER n 
1 650  PHE n 
1 651  LEU n 
1 652  CYS n 
1 653  ILE n 
1 654  GLU n 
1 655  ALA n 
1 656  LYS n 
1 657  LEU n 
1 658  GLU n 
1 659  LYS n 
1 660  LYS n 
1 661  LYS n 
1 662  ARG n 
1 663  ASN n 
1 664  ILE n 
1 665  PHE n 
1 666  THR n 
1 667  GLY n 
1 668  THR n 
1 669  PHE n 
1 670  HIS n 
1 671  LEU n 
1 672  PHE n 
1 673  ARG n 
1 674  SER n 
1 675  ILE n 
1 676  PHE n 
1 677  MET n 
1 678  LYS n 
1 679  SER n 
1 680  SER n 
1 681  LYS n 
1 682  LYS n 
1 683  ASN n 
1 684  LYS n 
1 685  LYS n 
1 686  GLU n 
1 687  ASN n 
1 688  LYS n 
1 689  GLU n 
1 690  ASN n 
1 691  ASN n 
1 692  ILE n 
1 693  HIS n 
1 694  ASP n 
1 695  ASP n 
1 696  GLY n 
1 697  ASP n 
1 698  ASN n 
1 699  ASP n 
1 700  ASN n 
1 701  ASP n 
1 702  GLU n 
1 703  LYS n 
1 704  LYS n 
1 705  LYS n 
1 706  ASP n 
1 707  LEU n 
1 708  SER n 
1 709  LEU n 
1 710  GLU n 
1 711  VAL n 
1 712  LYS n 
1 713  ASN n 
1 714  ASN n 
1 715  GLU n 
1 716  ASP n 
1 717  ASP n 
1 718  TYR n 
1 719  GLU n 
1 720  ASN n 
1 721  ILE n 
1 722  SER n 
1 723  ILE n 
1 724  TYR n 
1 725  GLU n 
1 726  TRP n 
1 727  ILE n 
1 728  HIS n 
1 729  ASN n 
1 730  LEU n 
1 731  TYR n 
1 732  LEU n 
1 733  PHE n 
1 734  GLU n 
1 735  GLU n 
1 736  SER n 
1 737  ILE n 
1 738  ASN n 
1 739  LYS n 
1 740  LYS n 
1 741  LYS n 
1 742  LYS n 
1 743  ASN n 
1 744  ALA n 
1 745  ALA n 
1 746  LEU n 
1 747  VAL n 
1 748  TYR n 
1 749  ALA n 
1 750  SER n 
1 751  ASN n 
1 752  ASN n 
1 753  GLY n 
1 754  MET n 
1 755  SER n 
1 756  SER n 
1 757  ASN n 
1 758  LEU n 
1 759  ASN n 
1 760  ASN n 
1 761  VAL n 
1 762  ASN n 
1 763  GLU n 
1 764  ASP n 
1 765  GLY n 
1 766  PHE n 
1 767  PRO n 
1 768  ASN n 
1 769  PRO n 
1 770  SER n 
1 771  LYS n 
1 772  ILE n 
1 773  VAL n 
1 774  SER n 
1 775  MET n 
1 776  GLU n 
1 777  ASP n 
1 778  VAL n 
1 779  LYS n 
1 780  LYS n 
1 781  ARG n 
1 782  ASN n 
1 783  ILE n 
1 784  LYS n 
1 785  LYS n 
1 786  ASP n 
1 787  ASP n 
1 788  ALA n 
1 789  TYR n 
1 790  ILE n 
1 791  ASN n 
1 792  LYS n 
1 793  GLU n 
1 794  ASP n 
1 795  GLU n 
1 796  GLU n 
1 797  GLY n 
1 798  GLY n 
1 799  GLY n 
1 800  TYR n 
1 801  TYR n 
1 802  ASN n 
1 803  LYS n 
1 804  ASP n 
1 805  ASP n 
1 806  ASN n 
1 807  LYS n 
1 808  LYS n 
1 809  LYS n 
1 810  ASP n 
1 811  ILE n 
1 812  LEU n 
1 813  GLY n 
1 814  LYS n 
1 815  LYS n 
1 816  GLN n 
1 817  LYS n 
1 818  LYS n 
1 819  ASN n 
1 820  ASN n 
1 821  ASN n 
1 822  ASN n 
1 823  VAL n 
1 824  THR n 
1 825  LEU n 
1 826  VAL n 
1 827  SER n 
1 828  LYS n 
1 829  LYS n 
1 830  GLY n 
1 831  GLU n 
1 832  ASP n 
1 833  ASN n 
1 834  GLU n 
1 835  LEU n 
1 836  ASP n 
1 837  VAL n 
1 838  TYR n 
1 839  TYR n 
1 840  GLU n 
1 841  ASN n 
1 842  LEU n 
1 843  ASP n 
1 844  GLU n 
1 845  LYS n 
1 846  THR n 
1 847  ASN n 
1 848  ASP n 
1 849  LYS n 
1 850  TYR n 
1 851  LYS n 
1 852  MET n 
1 853  ASN n 
1 854  ASN n 
1 855  ILE n 
1 856  LYS n 
1 857  SER n 
1 858  SER n 
1 859  LYS n 
1 860  LEU n 
1 861  LYS n 
1 862  TYR n 
1 863  ASP n 
1 864  ASN n 
1 865  ASP n 
1 866  LYS n 
1 867  LYS n 
1 868  ASP n 
1 869  GLY n 
1 870  ALA n 
1 871  ILE n 
1 872  ILE n 
1 873  ASN n 
1 874  ASN n 
1 875  ARG n 
1 876  PRO n 
1 877  SER n 
1 878  SER n 
1 879  ASP n 
1 880  GLU n 
1 881  GLU n 
1 882  TYR n 
1 883  LYS n 
1 884  GLU n 
1 885  GLU n 
1 886  LYS n 
1 887  ASP n 
1 888  LYS n 
1 889  ASN n 
1 890  LYS n 
1 891  ILE n 
1 892  ASN n 
1 893  ILE n 
1 894  LEU n 
1 895  ASN n 
1 896  ASP n 
1 897  VAL n 
1 898  PHE n 
1 899  ASN n 
1 900  ASP n 
1 901  ILE n 
1 902  THR n 
1 903  ILE n 
1 904  LYS n 
1 905  PRO n 
1 906  ASN n 
1 907  GLU n 
1 908  ASN n 
1 909  ILE n 
1 910  LEU n 
1 911  LEU n 
1 912  ASP n 
1 913  ARG n 
1 914  GLY n 
1 915  ASP n 
1 916  VAL n 
1 917  ILE n 
1 918  LYS n 
1 919  SER n 
1 920  SER n 
1 921  GLY n 
1 922  TYR n 
1 923  ASP n 
1 924  SER n 
1 925  SER n 
1 926  TYR n 
1 927  ASN n 
1 928  ASP n 
1 929  LEU n 
1 930  GLN n 
1 931  SER n 
1 932  SER n 
1 933  SER n 
1 934  LEU n 
1 935  PRO n 
1 936  ASN n 
1 937  PRO n 
1 938  SER n 
1 939  SER n 
1 940  ASN n 
1 941  GLU n 
1 942  VAL n 
1 943  LEU n 
1 944  ASN n 
1 945  LYS n 
1 946  THR n 
1 947  THR n 
1 948  MET n 
1 949  VAL n 
1 950  TYR n 
1 951  ASN n 
1 952  GLU n 
1 953  THR n 
1 954  ASP n 
1 955  LEU n 
1 956  LYS n 
1 957  ASP n 
1 958  ASN n 
1 959  LYS n 
1 960  LYS n 
1 961  GLU n 
1 962  ILE n 
1 963  LYS n 
1 964  SER n 
1 965  SER n 
1 966  LYS n 
1 967  LYS n 
1 968  ASN n 
1 969  VAL n 
1 970  LYS n 
1 971  ASP n 
1 972  ILE n 
1 973  LYS n 
1 974  LYS n 
1 975  SER n 
1 976  ASP n 
1 977  MET n 
1 978  ILE n 
1 979  HIS n 
1 980  ASP n 
1 981  ASP n 
1 982  THR n 
1 983  TYR n 
1 984  ASP n 
1 985  ILE n 
1 986  ILE n 
1 987  ASN n 
1 988  SER n 
1 989  ASN n 
1 990  ASN n 
1 991  LYS n 
1 992  ASN n 
1 993  ILE n 
1 994  LEU n 
1 995  LEU n 
1 996  SER n 
1 997  SER n 
1 998  ASN n 
1 999  GLU n 
1 1000 ILE n 
1 1001 ASN n 
1 1002 ASN n 
1 1003 ASN n 
1 1004 SER n 
1 1005 ASN n 
1 1006 ASN n 
1 1007 THR n 
1 1008 ASN n 
1 1009 LYS n 
1 1010 PHE n 
1 1011 ASN n 
1 1012 ASN n 
1 1013 ASN n 
1 1014 SER n 
1 1015 THR n 
1 1016 GLU n 
1 1017 LEU n 
1 1018 ALA n 
1 1019 THR n 
1 1020 LYS n 
1 1021 ASP n 
1 1022 THR n 
1 1023 GLN n 
1 1024 GLN n 
1 1025 PHE n 
1 1026 ILE n 
1 1027 ASN n 
1 1028 GLY n 
1 1029 HIS n 
1 1030 ASP n 
1 1031 LYS n 
1 1032 ASN n 
1 1033 ILE n 
1 1034 TYR n 
1 1035 LEU n 
1 1036 LEU n 
1 1037 SER n 
1 1038 SER n 
1 1039 HIS n 
1 1040 ASP n 
1 1041 ASN n 
1 1042 ALA n 
1 1043 LEU n 
1 1044 PHE n 
1 1045 TYR n 
1 1046 LYS n 
1 1047 TYR n 
1 1048 ILE n 
1 1049 TYR n 
1 1050 GLU n 
1 1051 GLU n 
1 1052 PRO n 
1 1053 LYS n 
1 1054 GLY n 
1 1055 ASN n 
1 1056 ILE n 
1 1057 GLY n 
1 1058 LYS n 
1 1059 TYR n 
1 1060 PHE n 
1 1061 ARG n 
1 1062 SER n 
1 1063 LEU n 
1 1064 VAL n 
1 1065 LYS n 
1 1066 ASN n 
1 1067 TYR n 
1 1068 TYR n 
1 1069 VAL n 
1 1070 PRO n 
1 1071 PHE n 
1 1072 LEU n 
1 1073 SER n 
1 1074 SER n 
1 1075 ARG n 
1 1076 PHE n 
1 1077 GLY n 
1 1078 LYS n 
1 1079 THR n 
1 1080 ILE n 
1 1081 VAL n 
1 1082 TYR n 
1 1083 ILE n 
1 1084 MET n 
1 1085 PHE n 
1 1086 THR n 
1 1087 ILE n 
1 1088 ILE n 
1 1089 ILE n 
1 1090 ALA n 
1 1091 MET n 
1 1092 SER n 
1 1093 ILE n 
1 1094 TYR n 
1 1095 GLY n 
1 1096 CYS n 
1 1097 THR n 
1 1098 LEU n 
1 1099 MET n 
1 1100 LYS n 
1 1101 LYS n 
1 1102 GLY n 
1 1103 ILE n 
1 1104 LYS n 
1 1105 TYR n 
1 1106 ASP n 
1 1107 LYS n 
1 1108 ALA n 
1 1109 PHE n 
1 1110 PRO n 
1 1111 VAL n 
1 1112 ASP n 
1 1113 SER n 
1 1114 TYR n 
1 1115 VAL n 
1 1116 ARG n 
1 1117 ARG n 
1 1118 PHE n 
1 1119 THR n 
1 1120 THR n 
1 1121 ALA n 
1 1122 LYS n 
1 1123 ILE n 
1 1124 LYS n 
1 1125 TYR n 
1 1126 PHE n 
1 1127 PRO n 
1 1128 ASP n 
1 1129 PHE n 
1 1130 GLY n 
1 1131 ASP n 
1 1132 PHE n 
1 1133 ILE n 
1 1134 GLU n 
1 1135 VAL n 
1 1136 TYR n 
1 1137 TYR n 
1 1138 PHE n 
1 1139 ASP n 
1 1140 LYS n 
1 1141 HIS n 
1 1142 PHE n 
1 1143 ILE n 
1 1144 ASN n 
1 1145 LYS n 
1 1146 TYR n 
1 1147 ARG n 
1 1148 GLY n 
1 1149 LEU n 
1 1150 GLU n 
1 1151 LYS n 
1 1152 ASN n 
1 1153 THR n 
1 1154 LYS n 
1 1155 GLU n 
1 1156 ALA n 
1 1157 ALA n 
1 1158 SER n 
1 1159 SER n 
1 1160 PHE n 
1 1161 LEU n 
1 1162 TYR n 
1 1163 SER n 
1 1164 ASP n 
1 1165 LEU n 
1 1166 THR n 
1 1167 ASP n 
1 1168 ARG n 
1 1169 GLN n 
1 1170 ILE n 
1 1171 MET n 
1 1172 ASN n 
1 1173 SER n 
1 1174 PRO n 
1 1175 LYS n 
1 1176 ILE n 
1 1177 ASN n 
1 1178 LYS n 
1 1179 ASN n 
1 1180 VAL n 
1 1181 HIS n 
1 1182 TRP n 
1 1183 GLU n 
1 1184 ASN n 
1 1185 THR n 
1 1186 ASN n 
1 1187 LEU n 
1 1188 GLN n 
1 1189 GLU n 
1 1190 GLU n 
1 1191 LEU n 
1 1192 ILE n 
1 1193 ASN n 
1 1194 MET n 
1 1195 HIS n 
1 1196 ASN n 
1 1197 THR n 
1 1198 LEU n 
1 1199 GLU n 
1 1200 SER n 
1 1201 GLN n 
1 1202 GLU n 
1 1203 PHE n 
1 1204 VAL n 
1 1205 THR n 
1 1206 SER n 
1 1207 VAL n 
1 1208 ALA n 
1 1209 ASN n 
1 1210 GLY n 
1 1211 PHE n 
1 1212 THR n 
1 1213 PHE n 
1 1214 PHE n 
1 1215 LEU n 
1 1216 ASN n 
1 1217 LYS n 
1 1218 ASN n 
1 1219 LYS n 
1 1220 SER n 
1 1221 SER n 
1 1222 LEU n 
1 1223 ARG n 
1 1224 LYS n 
1 1225 GLU n 
1 1226 ASN n 
1 1227 PRO n 
1 1228 GLN n 
1 1229 GLU n 
1 1230 PHE n 
1 1231 TYR n 
1 1232 GLU n 
1 1233 ILE n 
1 1234 PHE n 
1 1235 ALA n 
1 1236 ASN n 
1 1237 TRP n 
1 1238 LEU n 
1 1239 LYS n 
1 1240 LYS n 
1 1241 ASP n 
1 1242 PHE n 
1 1243 VAL n 
1 1244 GLY n 
1 1245 ASN n 
1 1246 LEU n 
1 1247 PHE n 
1 1248 LYS n 
1 1249 ASN n 
1 1250 ASP n 
1 1251 PHE n 
1 1252 VAL n 
1 1253 PHE n 
1 1254 LEU n 
1 1255 ASN n 
1 1256 GLY n 
1 1257 LYS n 
1 1258 LEU n 
1 1259 VAL n 
1 1260 ALA n 
1 1261 TRP n 
1 1262 ARG n 
1 1263 PHE n 
1 1264 HIS n 
1 1265 TYR n 
1 1266 PHE n 
1 1267 GLN n 
1 1268 LYS n 
1 1269 ASN n 
1 1270 VAL n 
1 1271 ASP n 
1 1272 ASP n 
1 1273 SER n 
1 1274 GLU n 
1 1275 ILE n 
1 1276 SER n 
1 1277 SER n 
1 1278 LYS n 
1 1279 TRP n 
1 1280 LEU n 
1 1281 LYS n 
1 1282 ALA n 
1 1283 CYS n 
1 1284 LYS n 
1 1285 GLN n 
1 1286 ILE n 
1 1287 THR n 
1 1288 LYS n 
1 1289 LEU n 
1 1290 GLU n 
1 1291 ASN n 
1 1292 HIS n 
1 1293 ASN n 
1 1294 VAL n 
1 1295 GLN n 
1 1296 MET n 
1 1297 VAL n 
1 1298 CYS n 
1 1299 PHE n 
1 1300 HIS n 
1 1301 LEU n 
1 1302 SER n 
1 1303 SER n 
1 1304 ILE n 
1 1305 PHE n 
1 1306 ASN n 
1 1307 GLU n 
1 1308 THR n 
1 1309 ASP n 
1 1310 GLU n 
1 1311 SER n 
1 1312 ILE n 
1 1313 ILE n 
1 1314 GLU n 
1 1315 VAL n 
1 1316 THR n 
1 1317 LEU n 
1 1318 ILE n 
1 1319 ASN n 
1 1320 LEU n 
1 1321 GLY n 
1 1322 ILE n 
1 1323 THR n 
1 1324 ILE n 
1 1325 LEU n 
1 1326 THR n 
1 1327 ILE n 
1 1328 LEU n 
1 1329 VAL n 
1 1330 VAL n 
1 1331 THR n 
1 1332 ALA n 
1 1333 TYR n 
1 1334 ILE n 
1 1335 ILE n 
1 1336 LYS n 
1 1337 GLY n 
1 1338 PHE n 
1 1339 TYR n 
1 1340 SER n 
1 1341 CYS n 
1 1342 VAL n 
1 1343 ILE n 
1 1344 ILE n 
1 1345 ALA n 
1 1346 LEU n 
1 1347 ILE n 
1 1348 ILE n 
1 1349 PHE n 
1 1350 LEU n 
1 1351 ILE n 
1 1352 ASP n 
1 1353 LEU n 
1 1354 CYS n 
1 1355 ILE n 
1 1356 PHE n 
1 1357 GLY n 
1 1358 PHE n 
1 1359 MET n 
1 1360 CYS n 
1 1361 LEU n 
1 1362 CYS n 
1 1363 GLY n 
1 1364 ILE n 
1 1365 THR n 
1 1366 MET n 
1 1367 ASN n 
1 1368 ILE n 
1 1369 ILE n 
1 1370 SER n 
1 1371 MET n 
1 1372 VAL n 
1 1373 ILE n 
1 1374 LEU n 
1 1375 VAL n 
1 1376 LEU n 
1 1377 SER n 
1 1378 VAL n 
1 1379 GLY n 
1 1380 PHE n 
1 1381 SER n 
1 1382 ILE n 
1 1383 ASP n 
1 1384 HIS n 
1 1385 THR n 
1 1386 SER n 
1 1387 HIS n 
1 1388 ILE n 
1 1389 VAL n 
1 1390 GLN n 
1 1391 ALA n 
1 1392 PHE n 
1 1393 SER n 
1 1394 HIS n 
1 1395 SER n 
1 1396 MET n 
1 1397 GLY n 
1 1398 ARG n 
1 1399 THR n 
1 1400 ARG n 
1 1401 ASP n 
1 1402 GLU n 
1 1403 LYS n 
1 1404 MET n 
1 1405 LYS n 
1 1406 GLU n 
1 1407 SER n 
1 1408 LEU n 
1 1409 HIS n 
1 1410 LEU n 
1 1411 MET n 
1 1412 ILE n 
1 1413 GLY n 
1 1414 PRO n 
1 1415 VAL n 
1 1416 LEU n 
1 1417 HIS n 
1 1418 SER n 
1 1419 GLY n 
1 1420 LEU n 
1 1421 SER n 
1 1422 THR n 
1 1423 TRP n 
1 1424 PHE n 
1 1425 VAL n 
1 1426 ILE n 
1 1427 SER n 
1 1428 THR n 
1 1429 LEU n 
1 1430 PHE n 
1 1431 PHE n 
1 1432 SER n 
1 1433 ASN n 
1 1434 LYS n 
1 1435 ASP n 
1 1436 PHE n 
1 1437 THR n 
1 1438 VAL n 
1 1439 ILE n 
1 1440 PHE n 
1 1441 PHE n 
1 1442 GLN n 
1 1443 THR n 
1 1444 LEU n 
1 1445 SER n 
1 1446 LEU n 
1 1447 VAL n 
1 1448 LEU n 
1 1449 PHE n 
1 1450 PHE n 
1 1451 SER n 
1 1452 ILE n 
1 1453 THR n 
1 1454 PHE n 
1 1455 SER n 
1 1456 SER n 
1 1457 MET n 
1 1458 PHE n 
1 1459 LEU n 
1 1460 PRO n 
1 1461 VAL n 
1 1462 LEU n 
1 1463 LEU n 
1 1464 SER n 
1 1465 SER n 
1 1466 PHE n 
1 1467 GLY n 
1 1468 PRO n 
1 1469 LEU n 
1 1470 HIS 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                   1470 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 PF3D7_0107500 
_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      'Plasmodium falciparum 3D7' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     36329 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     9606 
_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 
CLR non-polymer                  . CHOLESTEROL                              ? 'C27 H46 O'        386.654 
CYS 'L-peptide linking'          y CYSTEINE                                 ? 'C3 H7 N O2 S'     121.158 
GLN 'L-peptide linking'          y GLUTAMINE                                ? 'C5 H10 N2 O3'     146.144 
GLU 'L-peptide linking'          y 'GLUTAMIC ACID'                          ? 'C5 H9 N O4'       147.129 
GLY 'peptide linking'            y GLYCINE                                  ? 'C2 H5 N O2'       75.067  
HIS 'L-peptide linking'          y HISTIDINE                                ? 'C6 H10 N3 O2 1'   156.162 
ILE 'L-peptide linking'          y ISOLEUCINE                               ? 'C6 H13 N O2'      131.173 
LEU 'L-peptide linking'          y LEUCINE                                  ? 'C6 H13 N O2'      131.173 
LYS 'L-peptide linking'          y LYSINE                                   ? 'C6 H15 N2 O2 1'   147.195 
MET 'L-peptide linking'          y METHIONINE                               ? 'C5 H11 N O2 S'    149.211 
NAG 'D-saccharide, beta linking' . 2-acetamido-2-deoxy-beta-D-glucopyranose 
;N-acetyl-beta-D-glucosamine; 2-acetamido-2-deoxy-beta-D-glucose; 2-acetamido-2-deoxy-D-glucose; 2-acetamido-2-deoxy-glucose; N-ACETYL-D-GLUCOSAMINE
;
'C8 H15 N O6'      221.208 
PHE 'L-peptide linking'          y PHENYLALANINE                            ? 'C9 H11 N O2'      165.189 
PRO 'L-peptide linking'          y PROLINE                                  ? 'C5 H9 N O2'       115.130 
SER 'L-peptide linking'          y SERINE                                   ? 'C3 H7 N O3'       105.093 
THR 'L-peptide linking'          y THREONINE                                ? 'C4 H9 N O3'       119.119 
TRP 'L-peptide linking'          y TRYPTOPHAN                               ? 'C11 H12 N2 O2'    204.225 
TYR 'L-peptide linking'          y TYROSINE                                 ? 'C9 H11 N O3'      181.189 
VAL 'L-peptide linking'          y VALINE                                   ? 'C5 H11 N O2'      117.146 
Y6F non-polymer                  . MMV009108                                
'4-[2-(3,4-dimethylanilino)-1,3-thiazol-4-yl]-N,N-diethylbenzene-1-sulfonamide' 'C21 H25 N3 O2 S2' 415.572 
# 
loop_
_pdbx_chem_comp_identifier.comp_id 
_pdbx_chem_comp_identifier.type 
_pdbx_chem_comp_identifier.program 
_pdbx_chem_comp_identifier.program_version 
_pdbx_chem_comp_identifier.identifier 
NAG 'CONDENSED IUPAC CARBOHYDRATE SYMBOL' GMML     1.0 DGlcpNAcb                      
NAG 'COMMON NAME'                         GMML     1.0 N-acetyl-b-D-glucopyranosamine 
NAG 'IUPAC CARBOHYDRATE SYMBOL'           PDB-CARE 1.0 b-D-GlcpNAc                    
NAG 'SNFG CARBOHYDRATE SYMBOL'            GMML     1.0 GlcNAc                         
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1    MET 1    1    ?    ?   ?   A . n 
A 1 2    PHE 2    2    ?    ?   ?   A . n 
A 1 3    VAL 3    3    ?    ?   ?   A . n 
A 1 4    LYS 4    4    ?    ?   ?   A . n 
A 1 5    ASN 5    5    5    ASN ASN A . n 
A 1 6    PHE 6    6    6    PHE PHE A . n 
A 1 7    ILE 7    7    7    ILE ILE A . n 
A 1 8    HIS 8    8    8    HIS HIS A . n 
A 1 9    LYS 9    9    9    LYS LYS A . n 
A 1 10   LEU 10   10   10   LEU LEU A . n 
A 1 11   LYS 11   11   11   LYS LYS A . n 
A 1 12   GLU 12   12   12   GLU GLU A . n 
A 1 13   LEU 13   13   13   LEU LEU A . n 
A 1 14   LYS 14   14   14   LYS LYS A . n 
A 1 15   GLN 15   15   15   GLN GLN A . n 
A 1 16   LYS 16   16   16   LYS LYS A . n 
A 1 17   SER 17   17   17   SER SER A . n 
A 1 18   LEU 18   18   18   LEU LEU A . n 
A 1 19   ASP 19   19   19   ASP ASP A . n 
A 1 20   LYS 20   20   20   LYS LYS A . n 
A 1 21   PHE 21   21   21   PHE PHE A . n 
A 1 22   ALA 22   22   22   ALA ALA A . n 
A 1 23   ASN 23   23   23   ASN ASN A . n 
A 1 24   LEU 24   24   24   LEU LEU A . n 
A 1 25   LEU 25   25   25   LEU LEU A . n 
A 1 26   TYR 26   26   26   TYR TYR A . n 
A 1 27   ASP 27   27   27   ASP ASP A . n 
A 1 28   TYR 28   28   28   TYR TYR A . n 
A 1 29   GLY 29   29   29   GLY GLY A . n 
A 1 30   GLY 30   30   30   GLY GLY A . n 
A 1 31   TYR 31   31   31   TYR TYR A . n 
A 1 32   VAL 32   32   32   VAL VAL A . n 
A 1 33   TYR 33   33   33   TYR TYR A . n 
A 1 34   ASP 34   34   34   ASP ASP A . n 
A 1 35   ARG 35   35   35   ARG ARG A . n 
A 1 36   PRO 36   36   36   PRO PRO A . n 
A 1 37   CYS 37   37   37   CYS CYS A . n 
A 1 38   THR 38   38   38   THR THR A . n 
A 1 39   PHE 39   39   39   PHE PHE A . n 
A 1 40   ILE 40   40   40   ILE ILE A . n 
A 1 41   ILE 41   41   41   ILE ILE A . n 
A 1 42   CYS 42   42   42   CYS CYS A . n 
A 1 43   SER 43   43   43   SER SER A . n 
A 1 44   LEU 44   44   44   LEU LEU A . n 
A 1 45   ILE 45   45   45   ILE ILE A . n 
A 1 46   CYS 46   46   46   CYS CYS A . n 
A 1 47   CYS 47   47   47   CYS CYS A . n 
A 1 48   LEU 48   48   48   LEU LEU A . n 
A 1 49   LEU 49   49   49   LEU LEU A . n 
A 1 50   LEU 50   50   50   LEU LEU A . n 
A 1 51   THR 51   51   51   THR THR A . n 
A 1 52   CYS 52   52   52   CYS CYS A . n 
A 1 53   GLY 53   53   53   GLY GLY A . n 
A 1 54   PHE 54   54   54   PHE PHE A . n 
A 1 55   TYR 55   55   55   TYR TYR A . n 
A 1 56   PHE 56   56   56   PHE PHE A . n 
A 1 57   LYS 57   57   57   LYS LYS A . n 
A 1 58   GLU 58   58   58   GLU GLU A . n 
A 1 59   HIS 59   59   59   HIS HIS A . n 
A 1 60   GLU 60   60   60   GLU GLU A . n 
A 1 61   LYS 61   61   61   LYS LYS A . n 
A 1 62   ASP 62   62   62   ASP ASP A . n 
A 1 63   ILE 63   63   63   ILE ILE A . n 
A 1 64   TYR 64   64   64   TYR TYR A . n 
A 1 65   LYS 65   65   65   LYS LYS A . n 
A 1 66   LEU 66   66   66   LEU LEU A . n 
A 1 67   TYR 67   67   67   TYR TYR A . n 
A 1 68   SER 68   68   68   SER SER A . n 
A 1 69   ILE 69   69   69   ILE ILE A . n 
A 1 70   SER 70   70   70   SER SER A . n 
A 1 71   ASN 71   71   71   ASN ASN A . n 
A 1 72   SER 72   72   72   SER SER A . n 
A 1 73   TYR 73   73   73   TYR TYR A . n 
A 1 74   ALA 74   74   74   ALA ALA A . n 
A 1 75   TYR 75   75   75   TYR TYR A . n 
A 1 76   GLU 76   76   76   GLU GLU A . n 
A 1 77   THR 77   77   77   THR THR A . n 
A 1 78   ASN 78   78   78   ASN ASN A . n 
A 1 79   GLU 79   79   79   GLU GLU A . n 
A 1 80   THR 80   80   80   THR THR A . n 
A 1 81   ILE 81   81   81   ILE ILE A . n 
A 1 82   ASN 82   82   82   ASN ASN A . n 
A 1 83   ASP 83   83   83   ASP ASP A . n 
A 1 84   PHE 84   84   84   PHE PHE A . n 
A 1 85   PHE 85   85   85   PHE PHE A . n 
A 1 86   TYR 86   86   86   TYR TYR A . n 
A 1 87   LYS 87   87   87   LYS LYS A . n 
A 1 88   SER 88   88   88   SER SER A . n 
A 1 89   ARG 89   89   89   ARG ARG A . n 
A 1 90   ARG 90   90   90   ARG ARG A . n 
A 1 91   CYS 91   91   91   CYS CYS A . n 
A 1 92   PHE 92   92   92   PHE PHE A . n 
A 1 93   ILE 93   93   93   ILE ILE A . n 
A 1 94   LEU 94   94   94   LEU LEU A . n 
A 1 95   VAL 95   95   95   VAL VAL A . n 
A 1 96   GLU 96   96   96   GLU GLU A . n 
A 1 97   SER 97   97   97   SER SER A . n 
A 1 98   ASN 98   98   98   ASN ASN A . n 
A 1 99   VAL 99   99   99   VAL VAL A . n 
A 1 100  ASN 100  100  100  ASN ASN A . n 
A 1 101  LEU 101  101  101  LEU LEU A . n 
A 1 102  LEU 102  102  102  LEU LEU A . n 
A 1 103  LYS 103  103  103  LYS LYS A . n 
A 1 104  PRO 104  104  104  PRO PRO A . n 
A 1 105  LYS 105  105  105  LYS LYS A . n 
A 1 106  ILE 106  106  106  ILE ILE A . n 
A 1 107  LEU 107  107  107  LEU LEU A . n 
A 1 108  ARG 108  108  108  ARG ARG A . n 
A 1 109  GLU 109  109  109  GLU GLU A . n 
A 1 110  LEU 110  110  110  LEU LEU A . n 
A 1 111  GLN 111  111  111  GLN GLN A . n 
A 1 112  LYS 112  112  112  LYS LYS A . n 
A 1 113  PHE 113  113  113  PHE PHE A . n 
A 1 114  GLU 114  114  114  GLU GLU A . n 
A 1 115  GLU 115  115  115  GLU GLU A . n 
A 1 116  GLY 116  116  116  GLY GLY A . n 
A 1 117  THR 117  117  117  THR THR A . n 
A 1 118  LYS 118  118  118  LYS LYS A . n 
A 1 119  ASP 119  119  119  ASP ASP A . n 
A 1 120  ILE 120  120  120  ILE ILE A . n 
A 1 121  GLU 121  121  121  GLU GLU A . n 
A 1 122  VAL 122  122  122  VAL VAL A . n 
A 1 123  ASP 123  123  123  ASP ASP A . n 
A 1 124  LEU 124  124  124  LEU LEU A . n 
A 1 125  SER 125  125  125  SER SER A . n 
A 1 126  GLU 126  126  126  GLU GLU A . n 
A 1 127  ILE 127  127  127  ILE ILE A . n 
A 1 128  ASN 128  128  128  ASN ASN A . n 
A 1 129  GLU 129  129  129  GLU GLU A . n 
A 1 130  CYS 130  130  130  CYS CYS A . n 
A 1 131  LYS 131  131  131  LYS LYS A . n 
A 1 132  THR 132  132  132  THR THR A . n 
A 1 133  ASN 133  133  133  ASN ASN A . n 
A 1 134  SER 134  134  134  SER SER A . n 
A 1 135  GLU 135  135  135  GLU GLU A . n 
A 1 136  LEU 136  136  136  LEU LEU A . n 
A 1 137  PRO 137  137  137  PRO PRO A . n 
A 1 138  PRO 138  138  138  PRO PRO A . n 
A 1 139  GLU 139  139  139  GLU GLU A . n 
A 1 140  GLN 140  140  140  GLN GLN A . n 
A 1 141  SER 141  141  141  SER SER A . n 
A 1 142  HIS 142  142  142  HIS HIS A . n 
A 1 143  VAL 143  143  143  VAL VAL A . n 
A 1 144  ALA 144  144  144  ALA ALA A . n 
A 1 145  LYS 145  145  145  LYS LYS A . n 
A 1 146  GLU 146  146  146  GLU GLU A . n 
A 1 147  LEU 147  147  147  LEU LEU A . n 
A 1 148  TYR 148  148  148  TYR TYR A . n 
A 1 149  LYS 149  149  149  LYS LYS A . n 
A 1 150  THR 150  150  150  THR THR A . n 
A 1 151  LEU 151  151  151  LEU LEU A . n 
A 1 152  ILE 152  152  152  ILE ILE A . n 
A 1 153  GLN 153  153  153  GLN GLN A . n 
A 1 154  ARG 154  154  154  ARG ARG A . n 
A 1 155  SER 155  155  155  SER SER A . n 
A 1 156  GLU 156  156  156  GLU GLU A . n 
A 1 157  GLU 157  157  157  GLU GLU A . n 
A 1 158  ASN 158  158  158  ASN ASN A . n 
A 1 159  LEU 159  159  159  LEU LEU A . n 
A 1 160  LYS 160  160  160  LYS LYS A . n 
A 1 161  SER 161  161  161  SER SER A . n 
A 1 162  GLY 162  162  162  GLY GLY A . n 
A 1 163  LYS 163  163  163  LYS LYS A . n 
A 1 164  ILE 164  164  164  ILE ILE A . n 
A 1 165  ASN 165  165  165  ASN ASN A . n 
A 1 166  GLY 166  166  166  GLY GLY A . n 
A 1 167  SER 167  167  167  SER SER A . n 
A 1 168  LEU 168  168  168  LEU LEU A . n 
A 1 169  PHE 169  169  169  PHE PHE A . n 
A 1 170  ASP 170  170  170  ASP ASP A . n 
A 1 171  TYR 171  171  171  TYR TYR A . n 
A 1 172  SER 172  172  172  SER SER A . n 
A 1 173  ASP 173  173  173  ASP ASP A . n 
A 1 174  LEU 174  174  174  LEU LEU A . n 
A 1 175  ASP 175  175  175  ASP ASP A . n 
A 1 176  GLU 176  176  176  GLU GLU A . n 
A 1 177  ASN 177  177  177  ASN ASN A . n 
A 1 178  GLY 178  178  178  GLY GLY A . n 
A 1 179  LYS 179  179  179  LYS LYS A . n 
A 1 180  SER 180  180  180  SER SER A . n 
A 1 181  VAL 181  181  ?    ?   ?   A . n 
A 1 182  LEU 182  182  ?    ?   ?   A . n 
A 1 183  SER 183  183  ?    ?   ?   A . n 
A 1 184  LEU 184  184  ?    ?   ?   A . n 
A 1 185  ALA 185  185  ?    ?   ?   A . n 
A 1 186  GLY 186  186  ?    ?   ?   A . n 
A 1 187  LYS 187  187  ?    ?   ?   A . n 
A 1 188  GLU 188  188  ?    ?   ?   A . n 
A 1 189  ASN 189  189  ?    ?   ?   A . n 
A 1 190  ASN 190  190  ?    ?   ?   A . n 
A 1 191  ASP 191  191  ?    ?   ?   A . n 
A 1 192  ASP 192  192  ?    ?   ?   A . n 
A 1 193  THR 193  193  ?    ?   ?   A . n 
A 1 194  LEU 194  194  ?    ?   ?   A . n 
A 1 195  ILE 195  195  ?    ?   ?   A . n 
A 1 196  GLU 196  196  ?    ?   ?   A . n 
A 1 197  GLY 197  197  ?    ?   ?   A . n 
A 1 198  ASP 198  198  ?    ?   ?   A . n 
A 1 199  ASN 199  199  ?    ?   ?   A . n 
A 1 200  LYS 200  200  ?    ?   ?   A . n 
A 1 201  ASN 201  201  ?    ?   ?   A . n 
A 1 202  ASP 202  202  ?    ?   ?   A . n 
A 1 203  GLU 203  203  ?    ?   ?   A . n 
A 1 204  GLU 204  204  ?    ?   ?   A . n 
A 1 205  THR 205  205  ?    ?   ?   A . n 
A 1 206  SER 206  206  ?    ?   ?   A . n 
A 1 207  ALA 207  207  ?    ?   ?   A . n 
A 1 208  ASN 208  208  ?    ?   ?   A . n 
A 1 209  ASN 209  209  ?    ?   ?   A . n 
A 1 210  ASN 210  210  ?    ?   ?   A . n 
A 1 211  ASN 211  211  ?    ?   ?   A . n 
A 1 212  ASN 212  212  ?    ?   ?   A . n 
A 1 213  GLU 213  213  ?    ?   ?   A . n 
A 1 214  ASP 214  214  ?    ?   ?   A . n 
A 1 215  ASP 215  215  ?    ?   ?   A . n 
A 1 216  ASN 216  216  ?    ?   ?   A . n 
A 1 217  ASN 217  217  ?    ?   ?   A . n 
A 1 218  GLU 218  218  ?    ?   ?   A . n 
A 1 219  ASP 219  219  ?    ?   ?   A . n 
A 1 220  ASP 220  220  ?    ?   ?   A . n 
A 1 221  ASN 221  221  ?    ?   ?   A . n 
A 1 222  ASN 222  222  ?    ?   ?   A . n 
A 1 223  GLU 223  223  ?    ?   ?   A . n 
A 1 224  ASP 224  224  ?    ?   ?   A . n 
A 1 225  ASP 225  225  ?    ?   ?   A . n 
A 1 226  ASN 226  226  ?    ?   ?   A . n 
A 1 227  ASN 227  227  ?    ?   ?   A . n 
A 1 228  GLU 228  228  ?    ?   ?   A . n 
A 1 229  ASP 229  229  ?    ?   ?   A . n 
A 1 230  ASP 230  230  ?    ?   ?   A . n 
A 1 231  ASN 231  231  ?    ?   ?   A . n 
A 1 232  ASN 232  232  ?    ?   ?   A . n 
A 1 233  GLU 233  233  ?    ?   ?   A . n 
A 1 234  ASN 234  234  ?    ?   ?   A . n 
A 1 235  ASP 235  235  ?    ?   ?   A . n 
A 1 236  ASN 236  236  ?    ?   ?   A . n 
A 1 237  ASN 237  237  ?    ?   ?   A . n 
A 1 238  ASN 238  238  ?    ?   ?   A . n 
A 1 239  ASN 239  239  ?    ?   ?   A . n 
A 1 240  ASN 240  240  ?    ?   ?   A . n 
A 1 241  GLU 241  241  ?    ?   ?   A . n 
A 1 242  ASP 242  242  ?    ?   ?   A . n 
A 1 243  ASP 243  243  ?    ?   ?   A . n 
A 1 244  ASN 244  244  ?    ?   ?   A . n 
A 1 245  ASN 245  245  ?    ?   ?   A . n 
A 1 246  ASN 246  246  ?    ?   ?   A . n 
A 1 247  ASP 247  247  ?    ?   ?   A . n 
A 1 248  ASP 248  248  ?    ?   ?   A . n 
A 1 249  ASP 249  249  ?    ?   ?   A . n 
A 1 250  ASP 250  250  ?    ?   ?   A . n 
A 1 251  ASP 251  251  ?    ?   ?   A . n 
A 1 252  GLU 252  252  ?    ?   ?   A . n 
A 1 253  ASP 253  253  ?    ?   ?   A . n 
A 1 254  ASN 254  254  ?    ?   ?   A . n 
A 1 255  GLU 255  255  ?    ?   ?   A . n 
A 1 256  GLU 256  256  ?    ?   ?   A . n 
A 1 257  GLU 257  257  ?    ?   ?   A . n 
A 1 258  ASP 258  258  ?    ?   ?   A . n 
A 1 259  GLU 259  259  ?    ?   ?   A . n 
A 1 260  GLU 260  260  ?    ?   ?   A . n 
A 1 261  LYS 261  261  ?    ?   ?   A . n 
A 1 262  GLN 262  262  ?    ?   ?   A . n 
A 1 263  LYS 263  263  ?    ?   ?   A . n 
A 1 264  SER 264  264  ?    ?   ?   A . n 
A 1 265  LEU 265  265  ?    ?   ?   A . n 
A 1 266  ARG 266  266  ?    ?   ?   A . n 
A 1 267  GLU 267  267  ?    ?   ?   A . n 
A 1 268  LYS 268  268  ?    ?   ?   A . n 
A 1 269  LEU 269  269  ?    ?   ?   A . n 
A 1 270  TYR 270  270  ?    ?   ?   A . n 
A 1 271  ARG 271  271  ?    ?   ?   A . n 
A 1 272  LYS 272  272  ?    ?   ?   A . n 
A 1 273  ILE 273  273  ?    ?   ?   A . n 
A 1 274  TYR 274  274  ?    ?   ?   A . n 
A 1 275  GLU 275  275  ?    ?   ?   A . n 
A 1 276  MET 276  276  ?    ?   ?   A . n 
A 1 277  LEU 277  277  ?    ?   ?   A . n 
A 1 278  LYS 278  278  ?    ?   ?   A . n 
A 1 279  LYS 279  279  ?    ?   ?   A . n 
A 1 280  LYS 280  280  ?    ?   ?   A . n 
A 1 281  LYS 281  281  ?    ?   ?   A . n 
A 1 282  GLU 282  282  ?    ?   ?   A . n 
A 1 283  ASN 283  283  ?    ?   ?   A . n 
A 1 284  ILE 284  284  ?    ?   ?   A . n 
A 1 285  VAL 285  285  ?    ?   ?   A . n 
A 1 286  LEU 286  286  ?    ?   ?   A . n 
A 1 287  ASP 287  287  ?    ?   ?   A . n 
A 1 288  GLU 288  288  ?    ?   ?   A . n 
A 1 289  ASN 289  289  ?    ?   ?   A . n 
A 1 290  ASN 290  290  ?    ?   ?   A . n 
A 1 291  PRO 291  291  ?    ?   ?   A . n 
A 1 292  ASN 292  292  292  ASN ASN A . n 
A 1 293  VAL 293  293  293  VAL VAL A . n 
A 1 294  ASN 294  294  294  ASN ASN A . n 
A 1 295  PHE 295  295  295  PHE PHE A . n 
A 1 296  THR 296  296  296  THR THR A . n 
A 1 297  ASP 297  297  297  ASP ASP A . n 
A 1 298  TYR 298  298  298  TYR TYR A . n 
A 1 299  LYS 299  299  299  LYS LYS A . n 
A 1 300  ASP 300  300  300  ASP ASP A . n 
A 1 301  ASP 301  301  301  ASP ASP A . n 
A 1 302  VAL 302  302  302  VAL VAL A . n 
A 1 303  PHE 303  303  303  PHE PHE A . n 
A 1 304  TYR 304  304  304  TYR TYR A . n 
A 1 305  PRO 305  305  305  PRO PRO A . n 
A 1 306  TYR 306  306  306  TYR TYR A . n 
A 1 307  GLN 307  307  307  GLN GLN A . n 
A 1 308  TYR 308  308  308  TYR TYR A . n 
A 1 309  ILE 309  309  309  ILE ILE A . n 
A 1 310  PRO 310  310  310  PRO PRO A . n 
A 1 311  PRO 311  311  311  PRO PRO A . n 
A 1 312  MET 312  312  312  MET MET A . n 
A 1 313  LEU 313  313  313  LEU LEU A . n 
A 1 314  ILE 314  314  314  ILE ILE A . n 
A 1 315  LYS 315  315  315  LYS LYS A . n 
A 1 316  ALA 316  316  316  ALA ALA A . n 
A 1 317  ASP 317  317  317  ASP ASP A . n 
A 1 318  ARG 318  318  318  ARG ARG A . n 
A 1 319  CYS 319  319  319  CYS CYS A . n 
A 1 320  LYS 320  320  320  LYS LYS A . n 
A 1 321  LEU 321  321  321  LEU LEU A . n 
A 1 322  GLN 322  322  322  GLN GLN A . n 
A 1 323  ASN 323  323  323  ASN ASN A . n 
A 1 324  VAL 324  324  324  VAL VAL A . n 
A 1 325  PHE 325  325  325  PHE PHE A . n 
A 1 326  GLY 326  326  326  GLY GLY A . n 
A 1 327  ASP 327  327  327  ASP ASP A . n 
A 1 328  LYS 328  328  328  LYS LYS A . n 
A 1 329  ASN 329  329  329  ASN ASN A . n 
A 1 330  LEU 330  330  330  LEU LEU A . n 
A 1 331  ASN 331  331  331  ASN ASN A . n 
A 1 332  ILE 332  332  332  ILE ILE A . n 
A 1 333  ASP 333  333  333  ASP ASP A . n 
A 1 334  LEU 334  334  334  LEU LEU A . n 
A 1 335  ARG 335  335  335  ARG ARG A . n 
A 1 336  GLU 336  336  336  GLU GLU A . n 
A 1 337  ALA 337  337  337  ALA ALA A . n 
A 1 338  SER 338  338  338  SER SER A . n 
A 1 339  ASP 339  339  339  ASP ASP A . n 
A 1 340  GLY 340  340  340  GLY GLY A . n 
A 1 341  LEU 341  341  341  LEU LEU A . n 
A 1 342  LYS 342  342  342  LYS LYS A . n 
A 1 343  LYS 343  343  343  LYS LYS A . n 
A 1 344  GLN 344  344  344  GLN GLN A . n 
A 1 345  ILE 345  345  345  ILE ILE A . n 
A 1 346  THR 346  346  346  THR THR A . n 
A 1 347  TYR 347  347  347  TYR TYR A . n 
A 1 348  THR 348  348  348  THR THR A . n 
A 1 349  LEU 349  349  349  LEU LEU A . n 
A 1 350  GLU 350  350  350  GLU GLU A . n 
A 1 351  ASP 351  351  351  ASP ASP A . n 
A 1 352  ILE 352  352  352  ILE ILE A . n 
A 1 353  CYS 353  353  353  CYS CYS A . n 
A 1 354  GLU 354  354  354  GLU GLU A . n 
A 1 355  LYS 355  355  355  LYS LYS A . n 
A 1 356  LYS 356  356  356  LYS LYS A . n 
A 1 357  TYR 357  357  357  TYR TYR A . n 
A 1 358  GLY 358  358  358  GLY GLY A . n 
A 1 359  ASP 359  359  359  ASP ASP A . n 
A 1 360  CYS 360  360  360  CYS CYS A . n 
A 1 361  ASN 361  361  361  ASN ASN A . n 
A 1 362  PHE 362  362  362  PHE PHE A . n 
A 1 363  SER 363  363  363  SER SER A . n 
A 1 364  SER 364  364  364  SER SER A . n 
A 1 365  LEU 365  365  365  LEU LEU A . n 
A 1 366  PHE 366  366  366  PHE PHE A . n 
A 1 367  LEU 367  367  367  LEU LEU A . n 
A 1 368  TYR 368  368  368  TYR TYR A . n 
A 1 369  TYR 369  369  369  TYR TYR A . n 
A 1 370  GLU 370  370  370  GLU GLU A . n 
A 1 371  LYS 371  371  371  LYS LYS A . n 
A 1 372  GLY 372  372  372  GLY GLY A . n 
A 1 373  ASN 373  373  373  ASN ASN A . n 
A 1 374  GLY 374  374  374  GLY GLY A . n 
A 1 375  TYR 375  375  375  TYR TYR A . n 
A 1 376  ILE 376  376  376  ILE ILE A . n 
A 1 377  ASP 377  377  377  ASP ASP A . n 
A 1 378  TYR 378  378  378  TYR TYR A . n 
A 1 379  PRO 379  379  379  PRO PRO A . n 
A 1 380  ILE 380  380  380  ILE ILE A . n 
A 1 381  LYS 381  381  381  LYS LYS A . n 
A 1 382  VAL 382  382  382  VAL VAL A . n 
A 1 383  ASP 383  383  383  ASP ASP A . n 
A 1 384  ASN 384  384  384  ASN ASN A . n 
A 1 385  LEU 385  385  385  LEU LEU A . n 
A 1 386  ASP 386  386  386  ASP ASP A . n 
A 1 387  PHE 387  387  387  PHE PHE A . n 
A 1 388  TYR 388  388  388  TYR TYR A . n 
A 1 389  VAL 389  389  389  VAL VAL A . n 
A 1 390  ASN 390  390  390  ASN ASN A . n 
A 1 391  ARG 391  391  391  ARG ARG A . n 
A 1 392  ARG 392  392  392  ARG ARG A . n 
A 1 393  THR 393  393  393  THR THR A . n 
A 1 394  TYR 394  394  394  TYR TYR A . n 
A 1 395  LYS 395  395  395  LYS LYS A . n 
A 1 396  GLU 396  396  396  GLU GLU A . n 
A 1 397  MET 397  397  397  MET MET A . n 
A 1 398  MET 398  398  398  MET MET A . n 
A 1 399  PHE 399  399  399  PHE PHE A . n 
A 1 400  LYS 400  400  400  LYS LYS A . n 
A 1 401  GLY 401  401  401  GLY GLY A . n 
A 1 402  ILE 402  402  402  ILE ILE A . n 
A 1 403  LEU 403  403  403  LEU LEU A . n 
A 1 404  GLY 404  404  404  GLY GLY A . n 
A 1 405  ASN 405  405  405  ASN ASN A . n 
A 1 406  MET 406  406  406  MET MET A . n 
A 1 407  VAL 407  407  407  VAL VAL A . n 
A 1 408  TYR 408  408  408  TYR TYR A . n 
A 1 409  GLU 409  409  409  GLU GLU A . n 
A 1 410  LYS 410  410  410  LYS LYS A . n 
A 1 411  SER 411  411  411  SER SER A . n 
A 1 412  GLY 412  412  412  GLY GLY A . n 
A 1 413  SER 413  413  413  SER SER A . n 
A 1 414  LYS 414  414  414  LYS LYS A . n 
A 1 415  TYR 415  415  415  TYR TYR A . n 
A 1 416  ILE 416  416  416  ILE ILE A . n 
A 1 417  ILE 417  417  417  ILE ILE A . n 
A 1 418  LYS 418  418  418  LYS LYS A . n 
A 1 419  SER 419  419  419  SER SER A . n 
A 1 420  ALA 420  420  420  ALA ALA A . n 
A 1 421  ASN 421  421  421  ASN ASN A . n 
A 1 422  ALA 422  422  422  ALA ALA A . n 
A 1 423  ILE 423  423  423  ILE ILE A . n 
A 1 424  MET 424  424  424  MET MET A . n 
A 1 425  THR 425  425  425  THR THR A . n 
A 1 426  VAL 426  426  426  VAL VAL A . n 
A 1 427  ILE 427  427  427  ILE ILE A . n 
A 1 428  PRO 428  428  428  PRO PRO A . n 
A 1 429  LEU 429  429  429  LEU LEU A . n 
A 1 430  LEU 430  430  430  LEU LEU A . n 
A 1 431  ASN 431  431  431  ASN ASN A . n 
A 1 432  SER 432  432  432  SER SER A . n 
A 1 433  HIS 433  433  433  HIS HIS A . n 
A 1 434  THR 434  434  434  THR THR A . n 
A 1 435  TYR 435  435  435  TYR TYR A . n 
A 1 436  GLU 436  436  436  GLU GLU A . n 
A 1 437  PRO 437  437  437  PRO PRO A . n 
A 1 438  TYR 438  438  438  TYR TYR A . n 
A 1 439  ALA 439  439  439  ALA ALA A . n 
A 1 440  LEU 440  440  440  LEU LEU A . n 
A 1 441  ALA 441  441  441  ALA ALA A . n 
A 1 442  TYR 442  442  442  TYR TYR A . n 
A 1 443  GLU 443  443  443  GLU GLU A . n 
A 1 444  LYS 444  444  444  LYS LYS A . n 
A 1 445  LYS 445  445  445  LYS LYS A . n 
A 1 446  LEU 446  446  446  LEU LEU A . n 
A 1 447  ILE 447  447  447  ILE ILE A . n 
A 1 448  ASP 448  448  448  ASP ASP A . n 
A 1 449  TYR 449  449  449  TYR TYR A . n 
A 1 450  VAL 450  450  450  VAL VAL A . n 
A 1 451  ARG 451  451  451  ARG ARG A . n 
A 1 452  PHE 452  452  452  PHE PHE A . n 
A 1 453  TYR 453  453  453  TYR TYR A . n 
A 1 454  ASN 454  454  454  ASN ASN A . n 
A 1 455  LEU 455  455  455  LEU LEU A . n 
A 1 456  ASP 456  456  456  ASP ASP A . n 
A 1 457  ASP 457  457  457  ASP ASP A . n 
A 1 458  ILE 458  458  458  ILE ILE A . n 
A 1 459  ILE 459  459  459  ILE ILE A . n 
A 1 460  GLN 460  460  460  GLN GLN A . n 
A 1 461  ASP 461  461  461  ASP ASP A . n 
A 1 462  GLU 462  462  462  GLU GLU A . n 
A 1 463  GLU 463  463  463  GLU GLU A . n 
A 1 464  THR 464  464  464  THR THR A . n 
A 1 465  ASN 465  465  465  ASN ASN A . n 
A 1 466  ASP 466  466  466  ASP ASP A . n 
A 1 467  ASP 467  467  467  ASP ASP A . n 
A 1 468  ASN 468  468  468  ASN ASN A . n 
A 1 469  ASP 469  469  469  ASP ASP A . n 
A 1 470  PRO 470  470  470  PRO PRO A . n 
A 1 471  PHE 471  471  471  PHE PHE A . n 
A 1 472  ILE 472  472  472  ILE ILE A . n 
A 1 473  ARG 473  473  473  ARG ARG A . n 
A 1 474  PHE 474  474  474  PHE PHE A . n 
A 1 475  HIS 475  475  475  HIS HIS A . n 
A 1 476  VAL 476  476  476  VAL VAL A . n 
A 1 477  PHE 477  477  477  PHE PHE A . n 
A 1 478  THR 478  478  478  THR THR A . n 
A 1 479  ASP 479  479  479  ASP ASP A . n 
A 1 480  ARG 480  480  480  ARG ARG A . n 
A 1 481  SER 481  481  481  SER SER A . n 
A 1 482  LEU 482  482  482  LEU LEU A . n 
A 1 483  GLU 483  483  483  GLU GLU A . n 
A 1 484  ASP 484  484  484  ASP ASP A . n 
A 1 485  GLU 485  485  485  GLU GLU A . n 
A 1 486  VAL 486  486  486  VAL VAL A . n 
A 1 487  ASP 487  487  487  ASP ASP A . n 
A 1 488  ARG 488  488  488  ARG ARG A . n 
A 1 489  ILE 489  489  489  ILE ILE A . n 
A 1 490  SER 490  490  490  SER SER A . n 
A 1 491  LYS 491  491  491  LYS LYS A . n 
A 1 492  ILE 492  492  492  ILE ILE A . n 
A 1 493  ASP 493  493  493  ASP ASP A . n 
A 1 494  ASN 494  494  494  ASN ASN A . n 
A 1 495  LEU 495  495  495  LEU LEU A . n 
A 1 496  THR 496  496  496  THR THR A . n 
A 1 497  ARG 497  497  497  ARG ARG A . n 
A 1 498  LEU 498  498  498  LEU LEU A . n 
A 1 499  LEU 499  499  499  LEU LEU A . n 
A 1 500  LEU 500  500  500  LEU LEU A . n 
A 1 501  LEU 501  501  501  LEU LEU A . n 
A 1 502  ILE 502  502  502  ILE ILE A . n 
A 1 503  GLY 503  503  503  GLY GLY A . n 
A 1 504  VAL 504  504  504  VAL VAL A . n 
A 1 505  LEU 505  505  505  LEU LEU A . n 
A 1 506  LEU 506  506  506  LEU LEU A . n 
A 1 507  ILE 507  507  507  ILE ILE A . n 
A 1 508  PHE 508  508  508  PHE PHE A . n 
A 1 509  MET 509  509  509  MET MET A . n 
A 1 510  TYR 510  510  510  TYR TYR A . n 
A 1 511  ALA 511  511  511  ALA ALA A . n 
A 1 512  LEU 512  512  512  LEU LEU A . n 
A 1 513  PHE 513  513  513  PHE PHE A . n 
A 1 514  ASN 514  514  514  ASN ASN A . n 
A 1 515  ASN 515  515  515  ASN ASN A . n 
A 1 516  VAL 516  516  516  VAL VAL A . n 
A 1 517  THR 517  517  517  THR THR A . n 
A 1 518  SER 518  518  518  SER SER A . n 
A 1 519  VAL 519  519  519  VAL VAL A . n 
A 1 520  LEU 520  520  520  LEU LEU A . n 
A 1 521  TYR 521  521  521  TYR TYR A . n 
A 1 522  ARG 522  522  522  ARG ARG A . n 
A 1 523  SER 523  523  523  SER SER A . n 
A 1 524  LYS 524  524  524  LYS LYS A . n 
A 1 525  PRO 525  525  525  PRO PRO A . n 
A 1 526  LEU 526  526  526  LEU LEU A . n 
A 1 527  CYS 527  527  527  CYS CYS A . n 
A 1 528  ALA 528  528  528  ALA ALA A . n 
A 1 529  VAL 529  529  529  VAL VAL A . n 
A 1 530  MET 530  530  530  MET MET A . n 
A 1 531  GLY 531  531  531  GLY GLY A . n 
A 1 532  ILE 532  532  532  ILE ILE A . n 
A 1 533  PHE 533  533  533  PHE PHE A . n 
A 1 534  CYS 534  534  534  CYS CYS A . n 
A 1 535  GLY 535  535  535  GLY GLY A . n 
A 1 536  PHE 536  536  536  PHE PHE A . n 
A 1 537  LEU 537  537  537  LEU LEU A . n 
A 1 538  GLY 538  538  538  GLY GLY A . n 
A 1 539  PHE 539  539  539  PHE PHE A . n 
A 1 540  LEU 540  540  540  LEU LEU A . n 
A 1 541  SER 541  541  541  SER SER A . n 
A 1 542  GLY 542  542  542  GLY GLY A . n 
A 1 543  SER 543  543  543  SER SER A . n 
A 1 544  GLY 544  544  544  GLY GLY A . n 
A 1 545  PHE 545  545  545  PHE PHE A . n 
A 1 546  LEU 546  546  546  LEU LEU A . n 
A 1 547  TYR 547  547  547  TYR TYR A . n 
A 1 548  PHE 548  548  548  PHE PHE A . n 
A 1 549  LEU 549  549  549  LEU LEU A . n 
A 1 550  GLY 550  550  550  GLY GLY A . n 
A 1 551  VAL 551  551  551  VAL VAL A . n 
A 1 552  LYS 552  552  552  LYS LYS A . n 
A 1 553  SER 553  553  553  SER SER A . n 
A 1 554  VAL 554  554  554  VAL VAL A . n 
A 1 555  PRO 555  555  555  PRO PRO A . n 
A 1 556  PRO 556  556  556  PRO PRO A . n 
A 1 557  ALA 557  557  557  ALA ALA A . n 
A 1 558  GLU 558  558  558  GLU GLU A . n 
A 1 559  THR 559  559  559  THR THR A . n 
A 1 560  VAL 560  560  560  VAL VAL A . n 
A 1 561  PRO 561  561  561  PRO PRO A . n 
A 1 562  PHE 562  562  562  PHE PHE A . n 
A 1 563  LEU 563  563  563  LEU LEU A . n 
A 1 564  VAL 564  564  564  VAL VAL A . n 
A 1 565  ILE 565  565  565  ILE ILE A . n 
A 1 566  GLY 566  566  566  GLY GLY A . n 
A 1 567  VAL 567  567  567  VAL VAL A . n 
A 1 568  GLY 568  568  568  GLY GLY A . n 
A 1 569  VAL 569  569  569  VAL VAL A . n 
A 1 570  ASP 570  570  570  ASP ASP A . n 
A 1 571  ASP 571  571  571  ASP ASP A . n 
A 1 572  VAL 572  572  572  VAL VAL A . n 
A 1 573  PHE 573  573  573  PHE PHE A . n 
A 1 574  VAL 574  574  574  VAL VAL A . n 
A 1 575  ILE 575  575  575  ILE ILE A . n 
A 1 576  LEU 576  576  576  LEU LEU A . n 
A 1 577  ASN 577  577  577  ASN ASN A . n 
A 1 578  SER 578  578  578  SER SER A . n 
A 1 579  TYR 579  579  579  TYR TYR A . n 
A 1 580  SER 580  580  580  SER SER A . n 
A 1 581  LEU 581  581  581  LEU LEU A . n 
A 1 582  LEU 582  582  582  LEU LEU A . n 
A 1 583  PHE 583  583  583  PHE PHE A . n 
A 1 584  MET 584  584  584  MET MET A . n 
A 1 585  VAL 585  585  585  VAL VAL A . n 
A 1 586  LYS 586  586  586  LYS LYS A . n 
A 1 587  ASP 587  587  587  ASP ASP A . n 
A 1 588  ASN 588  588  588  ASN ASN A . n 
A 1 589  LYS 589  589  589  LYS LYS A . n 
A 1 590  LYS 590  590  590  LYS LYS A . n 
A 1 591  ARG 591  591  591  ARG ARG A . n 
A 1 592  ILE 592  592  592  ILE ILE A . n 
A 1 593  GLN 593  593  593  GLN GLN A . n 
A 1 594  MET 594  594  594  MET MET A . n 
A 1 595  CYS 595  595  595  CYS CYS A . n 
A 1 596  LEU 596  596  596  LEU LEU A . n 
A 1 597  LYS 597  597  597  LYS LYS A . n 
A 1 598  ASP 598  598  598  ASP ASP A . n 
A 1 599  SER 599  599  599  SER SER A . n 
A 1 600  ALA 600  600  600  ALA ALA A . n 
A 1 601  LEU 601  601  601  LEU LEU A . n 
A 1 602  ALA 602  602  602  ALA ALA A . n 
A 1 603  ILE 603  603  603  ILE ILE A . n 
A 1 604  THR 604  604  604  THR THR A . n 
A 1 605  VAL 605  605  605  VAL VAL A . n 
A 1 606  THR 606  606  606  THR THR A . n 
A 1 607  THR 607  607  607  THR THR A . n 
A 1 608  LEU 608  608  608  LEU LEU A . n 
A 1 609  THR 609  609  609  THR THR A . n 
A 1 610  ASN 610  610  610  ASN ASN A . n 
A 1 611  ILE 611  611  611  ILE ILE A . n 
A 1 612  ILE 612  612  612  ILE ILE A . n 
A 1 613  ALA 613  613  613  ALA ALA A . n 
A 1 614  PHE 614  614  614  PHE PHE A . n 
A 1 615  LEU 615  615  615  LEU LEU A . n 
A 1 616  ILE 616  616  616  ILE ILE A . n 
A 1 617  SER 617  617  617  SER SER A . n 
A 1 618  ALA 618  618  618  ALA ALA A . n 
A 1 619  ILE 619  619  619  ILE ILE A . n 
A 1 620  SER 620  620  620  SER SER A . n 
A 1 621  PRO 621  621  621  PRO PRO A . n 
A 1 622  PHE 622  622  622  PHE PHE A . n 
A 1 623  TYR 623  623  623  TYR TYR A . n 
A 1 624  SER 624  624  624  SER SER A . n 
A 1 625  ILE 625  625  625  ILE ILE A . n 
A 1 626  CYS 626  626  626  CYS CYS A . n 
A 1 627  ALA 627  627  627  ALA ALA A . n 
A 1 628  PHE 628  628  628  PHE PHE A . n 
A 1 629  SER 629  629  629  SER SER A . n 
A 1 630  LEU 630  630  630  LEU LEU A . n 
A 1 631  PHE 631  631  631  PHE PHE A . n 
A 1 632  THR 632  632  632  THR THR A . n 
A 1 633  ALA 633  633  633  ALA ALA A . n 
A 1 634  SER 634  634  634  SER SER A . n 
A 1 635  SER 635  635  635  SER SER A . n 
A 1 636  LEU 636  636  636  LEU LEU A . n 
A 1 637  PHE 637  637  637  PHE PHE A . n 
A 1 638  PHE 638  638  638  PHE PHE A . n 
A 1 639  GLY 639  639  639  GLY GLY A . n 
A 1 640  TYR 640  640  640  TYR TYR A . n 
A 1 641  LEU 641  641  641  LEU LEU A . n 
A 1 642  MET 642  642  642  MET MET A . n 
A 1 643  VAL 643  643  643  VAL VAL A . n 
A 1 644  LEU 644  644  644  LEU LEU A . n 
A 1 645  THR 645  645  645  THR THR A . n 
A 1 646  PHE 646  646  646  PHE PHE A . n 
A 1 647  LEU 647  647  647  LEU LEU A . n 
A 1 648  LEU 648  648  648  LEU LEU A . n 
A 1 649  SER 649  649  649  SER SER A . n 
A 1 650  PHE 650  650  650  PHE PHE A . n 
A 1 651  LEU 651  651  651  LEU LEU A . n 
A 1 652  CYS 652  652  652  CYS CYS A . n 
A 1 653  ILE 653  653  653  ILE ILE A . n 
A 1 654  GLU 654  654  654  GLU GLU A . n 
A 1 655  ALA 655  655  655  ALA ALA A . n 
A 1 656  LYS 656  656  656  LYS LYS A . n 
A 1 657  LEU 657  657  657  LEU LEU A . n 
A 1 658  GLU 658  658  658  GLU GLU A . n 
A 1 659  LYS 659  659  659  LYS LYS A . n 
A 1 660  LYS 660  660  660  LYS LYS A . n 
A 1 661  LYS 661  661  661  LYS LYS A . n 
A 1 662  ARG 662  662  662  ARG ARG A . n 
A 1 663  ASN 663  663  663  ASN ASN A . n 
A 1 664  ILE 664  664  664  ILE ILE A . n 
A 1 665  PHE 665  665  665  PHE PHE A . n 
A 1 666  THR 666  666  666  THR THR A . n 
A 1 667  GLY 667  667  667  GLY GLY A . n 
A 1 668  THR 668  668  668  THR THR A . n 
A 1 669  PHE 669  669  669  PHE PHE A . n 
A 1 670  HIS 670  670  670  HIS HIS A . n 
A 1 671  LEU 671  671  671  LEU LEU A . n 
A 1 672  PHE 672  672  672  PHE PHE A . n 
A 1 673  ARG 673  673  673  ARG ARG A . n 
A 1 674  SER 674  674  674  SER SER A . n 
A 1 675  ILE 675  675  ?    ?   ?   A . n 
A 1 676  PHE 676  676  ?    ?   ?   A . n 
A 1 677  MET 677  677  ?    ?   ?   A . n 
A 1 678  LYS 678  678  ?    ?   ?   A . n 
A 1 679  SER 679  679  ?    ?   ?   A . n 
A 1 680  SER 680  680  ?    ?   ?   A . n 
A 1 681  LYS 681  681  ?    ?   ?   A . n 
A 1 682  LYS 682  682  ?    ?   ?   A . n 
A 1 683  ASN 683  683  ?    ?   ?   A . n 
A 1 684  LYS 684  684  ?    ?   ?   A . n 
A 1 685  LYS 685  685  ?    ?   ?   A . n 
A 1 686  GLU 686  686  ?    ?   ?   A . n 
A 1 687  ASN 687  687  ?    ?   ?   A . n 
A 1 688  LYS 688  688  ?    ?   ?   A . n 
A 1 689  GLU 689  689  ?    ?   ?   A . n 
A 1 690  ASN 690  690  ?    ?   ?   A . n 
A 1 691  ASN 691  691  ?    ?   ?   A . n 
A 1 692  ILE 692  692  ?    ?   ?   A . n 
A 1 693  HIS 693  693  ?    ?   ?   A . n 
A 1 694  ASP 694  694  ?    ?   ?   A . n 
A 1 695  ASP 695  695  ?    ?   ?   A . n 
A 1 696  GLY 696  696  ?    ?   ?   A . n 
A 1 697  ASP 697  697  ?    ?   ?   A . n 
A 1 698  ASN 698  698  ?    ?   ?   A . n 
A 1 699  ASP 699  699  ?    ?   ?   A . n 
A 1 700  ASN 700  700  ?    ?   ?   A . n 
A 1 701  ASP 701  701  ?    ?   ?   A . n 
A 1 702  GLU 702  702  ?    ?   ?   A . n 
A 1 703  LYS 703  703  ?    ?   ?   A . n 
A 1 704  LYS 704  704  ?    ?   ?   A . n 
A 1 705  LYS 705  705  ?    ?   ?   A . n 
A 1 706  ASP 706  706  ?    ?   ?   A . n 
A 1 707  LEU 707  707  ?    ?   ?   A . n 
A 1 708  SER 708  708  ?    ?   ?   A . n 
A 1 709  LEU 709  709  ?    ?   ?   A . n 
A 1 710  GLU 710  710  ?    ?   ?   A . n 
A 1 711  VAL 711  711  ?    ?   ?   A . n 
A 1 712  LYS 712  712  ?    ?   ?   A . n 
A 1 713  ASN 713  713  ?    ?   ?   A . n 
A 1 714  ASN 714  714  ?    ?   ?   A . n 
A 1 715  GLU 715  715  ?    ?   ?   A . n 
A 1 716  ASP 716  716  ?    ?   ?   A . n 
A 1 717  ASP 717  717  ?    ?   ?   A . n 
A 1 718  TYR 718  718  ?    ?   ?   A . n 
A 1 719  GLU 719  719  ?    ?   ?   A . n 
A 1 720  ASN 720  720  ?    ?   ?   A . n 
A 1 721  ILE 721  721  721  ILE ILE A . n 
A 1 722  SER 722  722  722  SER SER A . n 
A 1 723  ILE 723  723  723  ILE ILE A . n 
A 1 724  TYR 724  724  724  TYR TYR A . n 
A 1 725  GLU 725  725  725  GLU GLU A . n 
A 1 726  TRP 726  726  726  TRP TRP A . n 
A 1 727  ILE 727  727  727  ILE ILE A . n 
A 1 728  HIS 728  728  728  HIS HIS A . n 
A 1 729  ASN 729  729  729  ASN ASN A . n 
A 1 730  LEU 730  730  730  LEU LEU A . n 
A 1 731  TYR 731  731  731  TYR TYR A . n 
A 1 732  LEU 732  732  732  LEU LEU A . n 
A 1 733  PHE 733  733  733  PHE PHE A . n 
A 1 734  GLU 734  734  734  GLU GLU A . n 
A 1 735  GLU 735  735  735  GLU GLU A . n 
A 1 736  SER 736  736  736  SER SER A . n 
A 1 737  ILE 737  737  ?    ?   ?   A . n 
A 1 738  ASN 738  738  ?    ?   ?   A . n 
A 1 739  LYS 739  739  ?    ?   ?   A . n 
A 1 740  LYS 740  740  ?    ?   ?   A . n 
A 1 741  LYS 741  741  ?    ?   ?   A . n 
A 1 742  LYS 742  742  ?    ?   ?   A . n 
A 1 743  ASN 743  743  ?    ?   ?   A . n 
A 1 744  ALA 744  744  ?    ?   ?   A . n 
A 1 745  ALA 745  745  ?    ?   ?   A . n 
A 1 746  LEU 746  746  ?    ?   ?   A . n 
A 1 747  VAL 747  747  ?    ?   ?   A . n 
A 1 748  TYR 748  748  ?    ?   ?   A . n 
A 1 749  ALA 749  749  ?    ?   ?   A . n 
A 1 750  SER 750  750  ?    ?   ?   A . n 
A 1 751  ASN 751  751  ?    ?   ?   A . n 
A 1 752  ASN 752  752  ?    ?   ?   A . n 
A 1 753  GLY 753  753  ?    ?   ?   A . n 
A 1 754  MET 754  754  ?    ?   ?   A . n 
A 1 755  SER 755  755  ?    ?   ?   A . n 
A 1 756  SER 756  756  ?    ?   ?   A . n 
A 1 757  ASN 757  757  ?    ?   ?   A . n 
A 1 758  LEU 758  758  ?    ?   ?   A . n 
A 1 759  ASN 759  759  ?    ?   ?   A . n 
A 1 760  ASN 760  760  ?    ?   ?   A . n 
A 1 761  VAL 761  761  ?    ?   ?   A . n 
A 1 762  ASN 762  762  ?    ?   ?   A . n 
A 1 763  GLU 763  763  ?    ?   ?   A . n 
A 1 764  ASP 764  764  ?    ?   ?   A . n 
A 1 765  GLY 765  765  ?    ?   ?   A . n 
A 1 766  PHE 766  766  ?    ?   ?   A . n 
A 1 767  PRO 767  767  ?    ?   ?   A . n 
A 1 768  ASN 768  768  ?    ?   ?   A . n 
A 1 769  PRO 769  769  ?    ?   ?   A . n 
A 1 770  SER 770  770  ?    ?   ?   A . n 
A 1 771  LYS 771  771  ?    ?   ?   A . n 
A 1 772  ILE 772  772  ?    ?   ?   A . n 
A 1 773  VAL 773  773  ?    ?   ?   A . n 
A 1 774  SER 774  774  ?    ?   ?   A . n 
A 1 775  MET 775  775  ?    ?   ?   A . n 
A 1 776  GLU 776  776  ?    ?   ?   A . n 
A 1 777  ASP 777  777  ?    ?   ?   A . n 
A 1 778  VAL 778  778  ?    ?   ?   A . n 
A 1 779  LYS 779  779  ?    ?   ?   A . n 
A 1 780  LYS 780  780  ?    ?   ?   A . n 
A 1 781  ARG 781  781  ?    ?   ?   A . n 
A 1 782  ASN 782  782  ?    ?   ?   A . n 
A 1 783  ILE 783  783  ?    ?   ?   A . n 
A 1 784  LYS 784  784  ?    ?   ?   A . n 
A 1 785  LYS 785  785  ?    ?   ?   A . n 
A 1 786  ASP 786  786  ?    ?   ?   A . n 
A 1 787  ASP 787  787  ?    ?   ?   A . n 
A 1 788  ALA 788  788  ?    ?   ?   A . n 
A 1 789  TYR 789  789  ?    ?   ?   A . n 
A 1 790  ILE 790  790  ?    ?   ?   A . n 
A 1 791  ASN 791  791  ?    ?   ?   A . n 
A 1 792  LYS 792  792  ?    ?   ?   A . n 
A 1 793  GLU 793  793  ?    ?   ?   A . n 
A 1 794  ASP 794  794  ?    ?   ?   A . n 
A 1 795  GLU 795  795  ?    ?   ?   A . n 
A 1 796  GLU 796  796  ?    ?   ?   A . n 
A 1 797  GLY 797  797  ?    ?   ?   A . n 
A 1 798  GLY 798  798  ?    ?   ?   A . n 
A 1 799  GLY 799  799  ?    ?   ?   A . n 
A 1 800  TYR 800  800  ?    ?   ?   A . n 
A 1 801  TYR 801  801  ?    ?   ?   A . n 
A 1 802  ASN 802  802  ?    ?   ?   A . n 
A 1 803  LYS 803  803  ?    ?   ?   A . n 
A 1 804  ASP 804  804  ?    ?   ?   A . n 
A 1 805  ASP 805  805  ?    ?   ?   A . n 
A 1 806  ASN 806  806  ?    ?   ?   A . n 
A 1 807  LYS 807  807  ?    ?   ?   A . n 
A 1 808  LYS 808  808  ?    ?   ?   A . n 
A 1 809  LYS 809  809  ?    ?   ?   A . n 
A 1 810  ASP 810  810  ?    ?   ?   A . n 
A 1 811  ILE 811  811  ?    ?   ?   A . n 
A 1 812  LEU 812  812  ?    ?   ?   A . n 
A 1 813  GLY 813  813  ?    ?   ?   A . n 
A 1 814  LYS 814  814  ?    ?   ?   A . n 
A 1 815  LYS 815  815  ?    ?   ?   A . n 
A 1 816  GLN 816  816  ?    ?   ?   A . n 
A 1 817  LYS 817  817  ?    ?   ?   A . n 
A 1 818  LYS 818  818  ?    ?   ?   A . n 
A 1 819  ASN 819  819  ?    ?   ?   A . n 
A 1 820  ASN 820  820  ?    ?   ?   A . n 
A 1 821  ASN 821  821  ?    ?   ?   A . n 
A 1 822  ASN 822  822  ?    ?   ?   A . n 
A 1 823  VAL 823  823  ?    ?   ?   A . n 
A 1 824  THR 824  824  ?    ?   ?   A . n 
A 1 825  LEU 825  825  ?    ?   ?   A . n 
A 1 826  VAL 826  826  ?    ?   ?   A . n 
A 1 827  SER 827  827  ?    ?   ?   A . n 
A 1 828  LYS 828  828  ?    ?   ?   A . n 
A 1 829  LYS 829  829  ?    ?   ?   A . n 
A 1 830  GLY 830  830  ?    ?   ?   A . n 
A 1 831  GLU 831  831  ?    ?   ?   A . n 
A 1 832  ASP 832  832  ?    ?   ?   A . n 
A 1 833  ASN 833  833  ?    ?   ?   A . n 
A 1 834  GLU 834  834  ?    ?   ?   A . n 
A 1 835  LEU 835  835  ?    ?   ?   A . n 
A 1 836  ASP 836  836  ?    ?   ?   A . n 
A 1 837  VAL 837  837  ?    ?   ?   A . n 
A 1 838  TYR 838  838  ?    ?   ?   A . n 
A 1 839  TYR 839  839  ?    ?   ?   A . n 
A 1 840  GLU 840  840  ?    ?   ?   A . n 
A 1 841  ASN 841  841  ?    ?   ?   A . n 
A 1 842  LEU 842  842  ?    ?   ?   A . n 
A 1 843  ASP 843  843  ?    ?   ?   A . n 
A 1 844  GLU 844  844  ?    ?   ?   A . n 
A 1 845  LYS 845  845  ?    ?   ?   A . n 
A 1 846  THR 846  846  ?    ?   ?   A . n 
A 1 847  ASN 847  847  ?    ?   ?   A . n 
A 1 848  ASP 848  848  ?    ?   ?   A . n 
A 1 849  LYS 849  849  ?    ?   ?   A . n 
A 1 850  TYR 850  850  ?    ?   ?   A . n 
A 1 851  LYS 851  851  ?    ?   ?   A . n 
A 1 852  MET 852  852  ?    ?   ?   A . n 
A 1 853  ASN 853  853  ?    ?   ?   A . n 
A 1 854  ASN 854  854  ?    ?   ?   A . n 
A 1 855  ILE 855  855  ?    ?   ?   A . n 
A 1 856  LYS 856  856  ?    ?   ?   A . n 
A 1 857  SER 857  857  ?    ?   ?   A . n 
A 1 858  SER 858  858  ?    ?   ?   A . n 
A 1 859  LYS 859  859  ?    ?   ?   A . n 
A 1 860  LEU 860  860  ?    ?   ?   A . n 
A 1 861  LYS 861  861  ?    ?   ?   A . n 
A 1 862  TYR 862  862  ?    ?   ?   A . n 
A 1 863  ASP 863  863  ?    ?   ?   A . n 
A 1 864  ASN 864  864  ?    ?   ?   A . n 
A 1 865  ASP 865  865  ?    ?   ?   A . n 
A 1 866  LYS 866  866  ?    ?   ?   A . n 
A 1 867  LYS 867  867  ?    ?   ?   A . n 
A 1 868  ASP 868  868  ?    ?   ?   A . n 
A 1 869  GLY 869  869  ?    ?   ?   A . n 
A 1 870  ALA 870  870  ?    ?   ?   A . n 
A 1 871  ILE 871  871  ?    ?   ?   A . n 
A 1 872  ILE 872  872  ?    ?   ?   A . n 
A 1 873  ASN 873  873  ?    ?   ?   A . n 
A 1 874  ASN 874  874  ?    ?   ?   A . n 
A 1 875  ARG 875  875  ?    ?   ?   A . n 
A 1 876  PRO 876  876  ?    ?   ?   A . n 
A 1 877  SER 877  877  ?    ?   ?   A . n 
A 1 878  SER 878  878  ?    ?   ?   A . n 
A 1 879  ASP 879  879  ?    ?   ?   A . n 
A 1 880  GLU 880  880  ?    ?   ?   A . n 
A 1 881  GLU 881  881  ?    ?   ?   A . n 
A 1 882  TYR 882  882  ?    ?   ?   A . n 
A 1 883  LYS 883  883  ?    ?   ?   A . n 
A 1 884  GLU 884  884  ?    ?   ?   A . n 
A 1 885  GLU 885  885  ?    ?   ?   A . n 
A 1 886  LYS 886  886  ?    ?   ?   A . n 
A 1 887  ASP 887  887  ?    ?   ?   A . n 
A 1 888  LYS 888  888  ?    ?   ?   A . n 
A 1 889  ASN 889  889  ?    ?   ?   A . n 
A 1 890  LYS 890  890  ?    ?   ?   A . n 
A 1 891  ILE 891  891  ?    ?   ?   A . n 
A 1 892  ASN 892  892  ?    ?   ?   A . n 
A 1 893  ILE 893  893  ?    ?   ?   A . n 
A 1 894  LEU 894  894  ?    ?   ?   A . n 
A 1 895  ASN 895  895  ?    ?   ?   A . n 
A 1 896  ASP 896  896  ?    ?   ?   A . n 
A 1 897  VAL 897  897  ?    ?   ?   A . n 
A 1 898  PHE 898  898  ?    ?   ?   A . n 
A 1 899  ASN 899  899  ?    ?   ?   A . n 
A 1 900  ASP 900  900  ?    ?   ?   A . n 
A 1 901  ILE 901  901  ?    ?   ?   A . n 
A 1 902  THR 902  902  ?    ?   ?   A . n 
A 1 903  ILE 903  903  ?    ?   ?   A . n 
A 1 904  LYS 904  904  ?    ?   ?   A . n 
A 1 905  PRO 905  905  ?    ?   ?   A . n 
A 1 906  ASN 906  906  ?    ?   ?   A . n 
A 1 907  GLU 907  907  ?    ?   ?   A . n 
A 1 908  ASN 908  908  ?    ?   ?   A . n 
A 1 909  ILE 909  909  ?    ?   ?   A . n 
A 1 910  LEU 910  910  ?    ?   ?   A . n 
A 1 911  LEU 911  911  ?    ?   ?   A . n 
A 1 912  ASP 912  912  ?    ?   ?   A . n 
A 1 913  ARG 913  913  ?    ?   ?   A . n 
A 1 914  GLY 914  914  ?    ?   ?   A . n 
A 1 915  ASP 915  915  ?    ?   ?   A . n 
A 1 916  VAL 916  916  ?    ?   ?   A . n 
A 1 917  ILE 917  917  ?    ?   ?   A . n 
A 1 918  LYS 918  918  ?    ?   ?   A . n 
A 1 919  SER 919  919  ?    ?   ?   A . n 
A 1 920  SER 920  920  ?    ?   ?   A . n 
A 1 921  GLY 921  921  ?    ?   ?   A . n 
A 1 922  TYR 922  922  ?    ?   ?   A . n 
A 1 923  ASP 923  923  ?    ?   ?   A . n 
A 1 924  SER 924  924  ?    ?   ?   A . n 
A 1 925  SER 925  925  ?    ?   ?   A . n 
A 1 926  TYR 926  926  ?    ?   ?   A . n 
A 1 927  ASN 927  927  ?    ?   ?   A . n 
A 1 928  ASP 928  928  ?    ?   ?   A . n 
A 1 929  LEU 929  929  ?    ?   ?   A . n 
A 1 930  GLN 930  930  ?    ?   ?   A . n 
A 1 931  SER 931  931  ?    ?   ?   A . n 
A 1 932  SER 932  932  ?    ?   ?   A . n 
A 1 933  SER 933  933  ?    ?   ?   A . n 
A 1 934  LEU 934  934  ?    ?   ?   A . n 
A 1 935  PRO 935  935  ?    ?   ?   A . n 
A 1 936  ASN 936  936  ?    ?   ?   A . n 
A 1 937  PRO 937  937  ?    ?   ?   A . n 
A 1 938  SER 938  938  ?    ?   ?   A . n 
A 1 939  SER 939  939  ?    ?   ?   A . n 
A 1 940  ASN 940  940  ?    ?   ?   A . n 
A 1 941  GLU 941  941  ?    ?   ?   A . n 
A 1 942  VAL 942  942  ?    ?   ?   A . n 
A 1 943  LEU 943  943  ?    ?   ?   A . n 
A 1 944  ASN 944  944  ?    ?   ?   A . n 
A 1 945  LYS 945  945  ?    ?   ?   A . n 
A 1 946  THR 946  946  ?    ?   ?   A . n 
A 1 947  THR 947  947  ?    ?   ?   A . n 
A 1 948  MET 948  948  ?    ?   ?   A . n 
A 1 949  VAL 949  949  ?    ?   ?   A . n 
A 1 950  TYR 950  950  ?    ?   ?   A . n 
A 1 951  ASN 951  951  ?    ?   ?   A . n 
A 1 952  GLU 952  952  ?    ?   ?   A . n 
A 1 953  THR 953  953  ?    ?   ?   A . n 
A 1 954  ASP 954  954  ?    ?   ?   A . n 
A 1 955  LEU 955  955  ?    ?   ?   A . n 
A 1 956  LYS 956  956  ?    ?   ?   A . n 
A 1 957  ASP 957  957  ?    ?   ?   A . n 
A 1 958  ASN 958  958  ?    ?   ?   A . n 
A 1 959  LYS 959  959  ?    ?   ?   A . n 
A 1 960  LYS 960  960  ?    ?   ?   A . n 
A 1 961  GLU 961  961  ?    ?   ?   A . n 
A 1 962  ILE 962  962  ?    ?   ?   A . n 
A 1 963  LYS 963  963  ?    ?   ?   A . n 
A 1 964  SER 964  964  ?    ?   ?   A . n 
A 1 965  SER 965  965  ?    ?   ?   A . n 
A 1 966  LYS 966  966  ?    ?   ?   A . n 
A 1 967  LYS 967  967  ?    ?   ?   A . n 
A 1 968  ASN 968  968  ?    ?   ?   A . n 
A 1 969  VAL 969  969  ?    ?   ?   A . n 
A 1 970  LYS 970  970  ?    ?   ?   A . n 
A 1 971  ASP 971  971  ?    ?   ?   A . n 
A 1 972  ILE 972  972  ?    ?   ?   A . n 
A 1 973  LYS 973  973  ?    ?   ?   A . n 
A 1 974  LYS 974  974  ?    ?   ?   A . n 
A 1 975  SER 975  975  ?    ?   ?   A . n 
A 1 976  ASP 976  976  ?    ?   ?   A . n 
A 1 977  MET 977  977  ?    ?   ?   A . n 
A 1 978  ILE 978  978  ?    ?   ?   A . n 
A 1 979  HIS 979  979  ?    ?   ?   A . n 
A 1 980  ASP 980  980  ?    ?   ?   A . n 
A 1 981  ASP 981  981  ?    ?   ?   A . n 
A 1 982  THR 982  982  ?    ?   ?   A . n 
A 1 983  TYR 983  983  ?    ?   ?   A . n 
A 1 984  ASP 984  984  ?    ?   ?   A . n 
A 1 985  ILE 985  985  ?    ?   ?   A . n 
A 1 986  ILE 986  986  ?    ?   ?   A . n 
A 1 987  ASN 987  987  ?    ?   ?   A . n 
A 1 988  SER 988  988  ?    ?   ?   A . n 
A 1 989  ASN 989  989  ?    ?   ?   A . n 
A 1 990  ASN 990  990  ?    ?   ?   A . n 
A 1 991  LYS 991  991  ?    ?   ?   A . n 
A 1 992  ASN 992  992  ?    ?   ?   A . n 
A 1 993  ILE 993  993  ?    ?   ?   A . n 
A 1 994  LEU 994  994  ?    ?   ?   A . n 
A 1 995  LEU 995  995  ?    ?   ?   A . n 
A 1 996  SER 996  996  ?    ?   ?   A . n 
A 1 997  SER 997  997  ?    ?   ?   A . n 
A 1 998  ASN 998  998  ?    ?   ?   A . n 
A 1 999  GLU 999  999  ?    ?   ?   A . n 
A 1 1000 ILE 1000 1000 ?    ?   ?   A . n 
A 1 1001 ASN 1001 1001 ?    ?   ?   A . n 
A 1 1002 ASN 1002 1002 ?    ?   ?   A . n 
A 1 1003 ASN 1003 1003 ?    ?   ?   A . n 
A 1 1004 SER 1004 1004 ?    ?   ?   A . n 
A 1 1005 ASN 1005 1005 ?    ?   ?   A . n 
A 1 1006 ASN 1006 1006 ?    ?   ?   A . n 
A 1 1007 THR 1007 1007 ?    ?   ?   A . n 
A 1 1008 ASN 1008 1008 ?    ?   ?   A . n 
A 1 1009 LYS 1009 1009 ?    ?   ?   A . n 
A 1 1010 PHE 1010 1010 ?    ?   ?   A . n 
A 1 1011 ASN 1011 1011 ?    ?   ?   A . n 
A 1 1012 ASN 1012 1012 ?    ?   ?   A . n 
A 1 1013 ASN 1013 1013 ?    ?   ?   A . n 
A 1 1014 SER 1014 1014 ?    ?   ?   A . n 
A 1 1015 THR 1015 1015 ?    ?   ?   A . n 
A 1 1016 GLU 1016 1016 ?    ?   ?   A . n 
A 1 1017 LEU 1017 1017 ?    ?   ?   A . n 
A 1 1018 ALA 1018 1018 ?    ?   ?   A . n 
A 1 1019 THR 1019 1019 ?    ?   ?   A . n 
A 1 1020 LYS 1020 1020 ?    ?   ?   A . n 
A 1 1021 ASP 1021 1021 ?    ?   ?   A . n 
A 1 1022 THR 1022 1022 ?    ?   ?   A . n 
A 1 1023 GLN 1023 1023 ?    ?   ?   A . n 
A 1 1024 GLN 1024 1024 ?    ?   ?   A . n 
A 1 1025 PHE 1025 1025 ?    ?   ?   A . n 
A 1 1026 ILE 1026 1026 ?    ?   ?   A . n 
A 1 1027 ASN 1027 1027 ?    ?   ?   A . n 
A 1 1028 GLY 1028 1028 ?    ?   ?   A . n 
A 1 1029 HIS 1029 1029 ?    ?   ?   A . n 
A 1 1030 ASP 1030 1030 ?    ?   ?   A . n 
A 1 1031 LYS 1031 1031 ?    ?   ?   A . n 
A 1 1032 ASN 1032 1032 ?    ?   ?   A . n 
A 1 1033 ILE 1033 1033 ?    ?   ?   A . n 
A 1 1034 TYR 1034 1034 ?    ?   ?   A . n 
A 1 1035 LEU 1035 1035 ?    ?   ?   A . n 
A 1 1036 LEU 1036 1036 ?    ?   ?   A . n 
A 1 1037 SER 1037 1037 ?    ?   ?   A . n 
A 1 1038 SER 1038 1038 ?    ?   ?   A . n 
A 1 1039 HIS 1039 1039 ?    ?   ?   A . n 
A 1 1040 ASP 1040 1040 ?    ?   ?   A . n 
A 1 1041 ASN 1041 1041 ?    ?   ?   A . n 
A 1 1042 ALA 1042 1042 ?    ?   ?   A . n 
A 1 1043 LEU 1043 1043 ?    ?   ?   A . n 
A 1 1044 PHE 1044 1044 ?    ?   ?   A . n 
A 1 1045 TYR 1045 1045 ?    ?   ?   A . n 
A 1 1046 LYS 1046 1046 ?    ?   ?   A . n 
A 1 1047 TYR 1047 1047 1047 TYR TYR A . n 
A 1 1048 ILE 1048 1048 1048 ILE ILE A . n 
A 1 1049 TYR 1049 1049 1049 TYR TYR A . n 
A 1 1050 GLU 1050 1050 1050 GLU GLU A . n 
A 1 1051 GLU 1051 1051 1051 GLU GLU A . n 
A 1 1052 PRO 1052 1052 1052 PRO PRO A . n 
A 1 1053 LYS 1053 1053 1053 LYS LYS A . n 
A 1 1054 GLY 1054 1054 1054 GLY GLY A . n 
A 1 1055 ASN 1055 1055 1055 ASN ASN A . n 
A 1 1056 ILE 1056 1056 1056 ILE ILE A . n 
A 1 1057 GLY 1057 1057 1057 GLY GLY A . n 
A 1 1058 LYS 1058 1058 1058 LYS LYS A . n 
A 1 1059 TYR 1059 1059 1059 TYR TYR A . n 
A 1 1060 PHE 1060 1060 1060 PHE PHE A . n 
A 1 1061 ARG 1061 1061 1061 ARG ARG A . n 
A 1 1062 SER 1062 1062 1062 SER SER A . n 
A 1 1063 LEU 1063 1063 1063 LEU LEU A . n 
A 1 1064 VAL 1064 1064 1064 VAL VAL A . n 
A 1 1065 LYS 1065 1065 1065 LYS LYS A . n 
A 1 1066 ASN 1066 1066 1066 ASN ASN A . n 
A 1 1067 TYR 1067 1067 1067 TYR TYR A . n 
A 1 1068 TYR 1068 1068 1068 TYR TYR A . n 
A 1 1069 VAL 1069 1069 1069 VAL VAL A . n 
A 1 1070 PRO 1070 1070 1070 PRO PRO A . n 
A 1 1071 PHE 1071 1071 1071 PHE PHE A . n 
A 1 1072 LEU 1072 1072 1072 LEU LEU A . n 
A 1 1073 SER 1073 1073 1073 SER SER A . n 
A 1 1074 SER 1074 1074 1074 SER SER A . n 
A 1 1075 ARG 1075 1075 1075 ARG ARG A . n 
A 1 1076 PHE 1076 1076 1076 PHE PHE A . n 
A 1 1077 GLY 1077 1077 1077 GLY GLY A . n 
A 1 1078 LYS 1078 1078 1078 LYS LYS A . n 
A 1 1079 THR 1079 1079 1079 THR THR A . n 
A 1 1080 ILE 1080 1080 1080 ILE ILE A . n 
A 1 1081 VAL 1081 1081 1081 VAL VAL A . n 
A 1 1082 TYR 1082 1082 1082 TYR TYR A . n 
A 1 1083 ILE 1083 1083 1083 ILE ILE A . n 
A 1 1084 MET 1084 1084 1084 MET MET A . n 
A 1 1085 PHE 1085 1085 1085 PHE PHE A . n 
A 1 1086 THR 1086 1086 1086 THR THR A . n 
A 1 1087 ILE 1087 1087 1087 ILE ILE A . n 
A 1 1088 ILE 1088 1088 1088 ILE ILE A . n 
A 1 1089 ILE 1089 1089 1089 ILE ILE A . n 
A 1 1090 ALA 1090 1090 1090 ALA ALA A . n 
A 1 1091 MET 1091 1091 1091 MET MET A . n 
A 1 1092 SER 1092 1092 1092 SER SER A . n 
A 1 1093 ILE 1093 1093 1093 ILE ILE A . n 
A 1 1094 TYR 1094 1094 1094 TYR TYR A . n 
A 1 1095 GLY 1095 1095 1095 GLY GLY A . n 
A 1 1096 CYS 1096 1096 1096 CYS CYS A . n 
A 1 1097 THR 1097 1097 1097 THR THR A . n 
A 1 1098 LEU 1098 1098 1098 LEU LEU A . n 
A 1 1099 MET 1099 1099 1099 MET MET A . n 
A 1 1100 LYS 1100 1100 1100 LYS LYS A . n 
A 1 1101 LYS 1101 1101 1101 LYS LYS A . n 
A 1 1102 GLY 1102 1102 1102 GLY GLY A . n 
A 1 1103 ILE 1103 1103 1103 ILE ILE A . n 
A 1 1104 LYS 1104 1104 1104 LYS LYS A . n 
A 1 1105 TYR 1105 1105 1105 TYR TYR A . n 
A 1 1106 ASP 1106 1106 1106 ASP ASP A . n 
A 1 1107 LYS 1107 1107 1107 LYS LYS A . n 
A 1 1108 ALA 1108 1108 1108 ALA ALA A . n 
A 1 1109 PHE 1109 1109 1109 PHE PHE A . n 
A 1 1110 PRO 1110 1110 1110 PRO PRO A . n 
A 1 1111 VAL 1111 1111 1111 VAL VAL A . n 
A 1 1112 ASP 1112 1112 1112 ASP ASP A . n 
A 1 1113 SER 1113 1113 1113 SER SER A . n 
A 1 1114 TYR 1114 1114 1114 TYR TYR A . n 
A 1 1115 VAL 1115 1115 1115 VAL VAL A . n 
A 1 1116 ARG 1116 1116 1116 ARG ARG A . n 
A 1 1117 ARG 1117 1117 1117 ARG ARG A . n 
A 1 1118 PHE 1118 1118 1118 PHE PHE A . n 
A 1 1119 THR 1119 1119 1119 THR THR A . n 
A 1 1120 THR 1120 1120 1120 THR THR A . n 
A 1 1121 ALA 1121 1121 1121 ALA ALA A . n 
A 1 1122 LYS 1122 1122 1122 LYS LYS A . n 
A 1 1123 ILE 1123 1123 1123 ILE ILE A . n 
A 1 1124 LYS 1124 1124 1124 LYS LYS A . n 
A 1 1125 TYR 1125 1125 1125 TYR TYR A . n 
A 1 1126 PHE 1126 1126 1126 PHE PHE A . n 
A 1 1127 PRO 1127 1127 1127 PRO PRO A . n 
A 1 1128 ASP 1128 1128 1128 ASP ASP A . n 
A 1 1129 PHE 1129 1129 1129 PHE PHE A . n 
A 1 1130 GLY 1130 1130 1130 GLY GLY A . n 
A 1 1131 ASP 1131 1131 1131 ASP ASP A . n 
A 1 1132 PHE 1132 1132 1132 PHE PHE A . n 
A 1 1133 ILE 1133 1133 1133 ILE ILE A . n 
A 1 1134 GLU 1134 1134 1134 GLU GLU A . n 
A 1 1135 VAL 1135 1135 1135 VAL VAL A . n 
A 1 1136 TYR 1136 1136 1136 TYR TYR A . n 
A 1 1137 TYR 1137 1137 1137 TYR TYR A . n 
A 1 1138 PHE 1138 1138 1138 PHE PHE A . n 
A 1 1139 ASP 1139 1139 1139 ASP ASP A . n 
A 1 1140 LYS 1140 1140 1140 LYS LYS A . n 
A 1 1141 HIS 1141 1141 1141 HIS HIS A . n 
A 1 1142 PHE 1142 1142 1142 PHE PHE A . n 
A 1 1143 ILE 1143 1143 1143 ILE ILE A . n 
A 1 1144 ASN 1144 1144 1144 ASN ASN A . n 
A 1 1145 LYS 1145 1145 1145 LYS LYS A . n 
A 1 1146 TYR 1146 1146 1146 TYR TYR A . n 
A 1 1147 ARG 1147 1147 1147 ARG ARG A . n 
A 1 1148 GLY 1148 1148 1148 GLY GLY A . n 
A 1 1149 LEU 1149 1149 1149 LEU LEU A . n 
A 1 1150 GLU 1150 1150 1150 GLU GLU A . n 
A 1 1151 LYS 1151 1151 1151 LYS LYS A . n 
A 1 1152 ASN 1152 1152 ?    ?   ?   A . n 
A 1 1153 THR 1153 1153 ?    ?   ?   A . n 
A 1 1154 LYS 1154 1154 ?    ?   ?   A . n 
A 1 1155 GLU 1155 1155 ?    ?   ?   A . n 
A 1 1156 ALA 1156 1156 ?    ?   ?   A . n 
A 1 1157 ALA 1157 1157 ?    ?   ?   A . n 
A 1 1158 SER 1158 1158 ?    ?   ?   A . n 
A 1 1159 SER 1159 1159 ?    ?   ?   A . n 
A 1 1160 PHE 1160 1160 ?    ?   ?   A . n 
A 1 1161 LEU 1161 1161 1161 LEU LEU A . n 
A 1 1162 TYR 1162 1162 1162 TYR TYR A . n 
A 1 1163 SER 1163 1163 1163 SER SER A . n 
A 1 1164 ASP 1164 1164 1164 ASP ASP A . n 
A 1 1165 LEU 1165 1165 1165 LEU LEU A . n 
A 1 1166 THR 1166 1166 1166 THR THR A . n 
A 1 1167 ASP 1167 1167 1167 ASP ASP A . n 
A 1 1168 ARG 1168 1168 1168 ARG ARG A . n 
A 1 1169 GLN 1169 1169 1169 GLN GLN A . n 
A 1 1170 ILE 1170 1170 1170 ILE ILE A . n 
A 1 1171 MET 1171 1171 1171 MET MET A . n 
A 1 1172 ASN 1172 1172 1172 ASN ASN A . n 
A 1 1173 SER 1173 1173 1173 SER SER A . n 
A 1 1174 PRO 1174 1174 1174 PRO PRO A . n 
A 1 1175 LYS 1175 1175 1175 LYS LYS A . n 
A 1 1176 ILE 1176 1176 1176 ILE ILE A . n 
A 1 1177 ASN 1177 1177 1177 ASN ASN A . n 
A 1 1178 LYS 1178 1178 1178 LYS LYS A . n 
A 1 1179 ASN 1179 1179 1179 ASN ASN A . n 
A 1 1180 VAL 1180 1180 1180 VAL VAL A . n 
A 1 1181 HIS 1181 1181 1181 HIS HIS A . n 
A 1 1182 TRP 1182 1182 1182 TRP TRP A . n 
A 1 1183 GLU 1183 1183 1183 GLU GLU A . n 
A 1 1184 ASN 1184 1184 1184 ASN ASN A . n 
A 1 1185 THR 1185 1185 1185 THR THR A . n 
A 1 1186 ASN 1186 1186 1186 ASN ASN A . n 
A 1 1187 LEU 1187 1187 1187 LEU LEU A . n 
A 1 1188 GLN 1188 1188 1188 GLN GLN A . n 
A 1 1189 GLU 1189 1189 1189 GLU GLU A . n 
A 1 1190 GLU 1190 1190 1190 GLU GLU A . n 
A 1 1191 LEU 1191 1191 1191 LEU LEU A . n 
A 1 1192 ILE 1192 1192 1192 ILE ILE A . n 
A 1 1193 ASN 1193 1193 1193 ASN ASN A . n 
A 1 1194 MET 1194 1194 1194 MET MET A . n 
A 1 1195 HIS 1195 1195 1195 HIS HIS A . n 
A 1 1196 ASN 1196 1196 1196 ASN ASN A . n 
A 1 1197 THR 1197 1197 1197 THR THR A . n 
A 1 1198 LEU 1198 1198 1198 LEU LEU A . n 
A 1 1199 GLU 1199 1199 1199 GLU GLU A . n 
A 1 1200 SER 1200 1200 1200 SER SER A . n 
A 1 1201 GLN 1201 1201 1201 GLN GLN A . n 
A 1 1202 GLU 1202 1202 1202 GLU GLU A . n 
A 1 1203 PHE 1203 1203 1203 PHE PHE A . n 
A 1 1204 VAL 1204 1204 1204 VAL VAL A . n 
A 1 1205 THR 1205 1205 1205 THR THR A . n 
A 1 1206 SER 1206 1206 1206 SER SER A . n 
A 1 1207 VAL 1207 1207 1207 VAL VAL A . n 
A 1 1208 ALA 1208 1208 1208 ALA ALA A . n 
A 1 1209 ASN 1209 1209 1209 ASN ASN A . n 
A 1 1210 GLY 1210 1210 1210 GLY GLY A . n 
A 1 1211 PHE 1211 1211 1211 PHE PHE A . n 
A 1 1212 THR 1212 1212 1212 THR THR A . n 
A 1 1213 PHE 1213 1213 1213 PHE PHE A . n 
A 1 1214 PHE 1214 1214 1214 PHE PHE A . n 
A 1 1215 LEU 1215 1215 1215 LEU LEU A . n 
A 1 1216 ASN 1216 1216 1216 ASN ASN A . n 
A 1 1217 LYS 1217 1217 1217 LYS LYS A . n 
A 1 1218 ASN 1218 1218 1218 ASN ASN A . n 
A 1 1219 LYS 1219 1219 1219 LYS LYS A . n 
A 1 1220 SER 1220 1220 1220 SER SER A . n 
A 1 1221 SER 1221 1221 1221 SER SER A . n 
A 1 1222 LEU 1222 1222 1222 LEU LEU A . n 
A 1 1223 ARG 1223 1223 1223 ARG ARG A . n 
A 1 1224 LYS 1224 1224 1224 LYS LYS A . n 
A 1 1225 GLU 1225 1225 1225 GLU GLU A . n 
A 1 1226 ASN 1226 1226 1226 ASN ASN A . n 
A 1 1227 PRO 1227 1227 1227 PRO PRO A . n 
A 1 1228 GLN 1228 1228 1228 GLN GLN A . n 
A 1 1229 GLU 1229 1229 1229 GLU GLU A . n 
A 1 1230 PHE 1230 1230 1230 PHE PHE A . n 
A 1 1231 TYR 1231 1231 1231 TYR TYR A . n 
A 1 1232 GLU 1232 1232 1232 GLU GLU A . n 
A 1 1233 ILE 1233 1233 1233 ILE ILE A . n 
A 1 1234 PHE 1234 1234 1234 PHE PHE A . n 
A 1 1235 ALA 1235 1235 1235 ALA ALA A . n 
A 1 1236 ASN 1236 1236 1236 ASN ASN A . n 
A 1 1237 TRP 1237 1237 1237 TRP TRP A . n 
A 1 1238 LEU 1238 1238 1238 LEU LEU A . n 
A 1 1239 LYS 1239 1239 1239 LYS LYS A . n 
A 1 1240 LYS 1240 1240 1240 LYS LYS A . n 
A 1 1241 ASP 1241 1241 1241 ASP ASP A . n 
A 1 1242 PHE 1242 1242 1242 PHE PHE A . n 
A 1 1243 VAL 1243 1243 1243 VAL VAL A . n 
A 1 1244 GLY 1244 1244 1244 GLY GLY A . n 
A 1 1245 ASN 1245 1245 1245 ASN ASN A . n 
A 1 1246 LEU 1246 1246 1246 LEU LEU A . n 
A 1 1247 PHE 1247 1247 1247 PHE PHE A . n 
A 1 1248 LYS 1248 1248 1248 LYS LYS A . n 
A 1 1249 ASN 1249 1249 1249 ASN ASN A . n 
A 1 1250 ASP 1250 1250 1250 ASP ASP A . n 
A 1 1251 PHE 1251 1251 1251 PHE PHE A . n 
A 1 1252 VAL 1252 1252 1252 VAL VAL A . n 
A 1 1253 PHE 1253 1253 1253 PHE PHE A . n 
A 1 1254 LEU 1254 1254 1254 LEU LEU A . n 
A 1 1255 ASN 1255 1255 1255 ASN ASN A . n 
A 1 1256 GLY 1256 1256 1256 GLY GLY A . n 
A 1 1257 LYS 1257 1257 1257 LYS LYS A . n 
A 1 1258 LEU 1258 1258 1258 LEU LEU A . n 
A 1 1259 VAL 1259 1259 1259 VAL VAL A . n 
A 1 1260 ALA 1260 1260 1260 ALA ALA A . n 
A 1 1261 TRP 1261 1261 1261 TRP TRP A . n 
A 1 1262 ARG 1262 1262 1262 ARG ARG A . n 
A 1 1263 PHE 1263 1263 1263 PHE PHE A . n 
A 1 1264 HIS 1264 1264 1264 HIS HIS A . n 
A 1 1265 TYR 1265 1265 1265 TYR TYR A . n 
A 1 1266 PHE 1266 1266 1266 PHE PHE A . n 
A 1 1267 GLN 1267 1267 1267 GLN GLN A . n 
A 1 1268 LYS 1268 1268 1268 LYS LYS A . n 
A 1 1269 ASN 1269 1269 1269 ASN ASN A . n 
A 1 1270 VAL 1270 1270 1270 VAL VAL A . n 
A 1 1271 ASP 1271 1271 1271 ASP ASP A . n 
A 1 1272 ASP 1272 1272 1272 ASP ASP A . n 
A 1 1273 SER 1273 1273 1273 SER SER A . n 
A 1 1274 GLU 1274 1274 1274 GLU GLU A . n 
A 1 1275 ILE 1275 1275 1275 ILE ILE A . n 
A 1 1276 SER 1276 1276 1276 SER SER A . n 
A 1 1277 SER 1277 1277 1277 SER SER A . n 
A 1 1278 LYS 1278 1278 1278 LYS LYS A . n 
A 1 1279 TRP 1279 1279 1279 TRP TRP A . n 
A 1 1280 LEU 1280 1280 1280 LEU LEU A . n 
A 1 1281 LYS 1281 1281 1281 LYS LYS A . n 
A 1 1282 ALA 1282 1282 1282 ALA ALA A . n 
A 1 1283 CYS 1283 1283 1283 CYS CYS A . n 
A 1 1284 LYS 1284 1284 1284 LYS LYS A . n 
A 1 1285 GLN 1285 1285 1285 GLN GLN A . n 
A 1 1286 ILE 1286 1286 1286 ILE ILE A . n 
A 1 1287 THR 1287 1287 1287 THR THR A . n 
A 1 1288 LYS 1288 1288 1288 LYS LYS A . n 
A 1 1289 LEU 1289 1289 1289 LEU LEU A . n 
A 1 1290 GLU 1290 1290 1290 GLU GLU A . n 
A 1 1291 ASN 1291 1291 1291 ASN ASN A . n 
A 1 1292 HIS 1292 1292 1292 HIS HIS A . n 
A 1 1293 ASN 1293 1293 1293 ASN ASN A . n 
A 1 1294 VAL 1294 1294 1294 VAL VAL A . n 
A 1 1295 GLN 1295 1295 1295 GLN GLN A . n 
A 1 1296 MET 1296 1296 1296 MET MET A . n 
A 1 1297 VAL 1297 1297 1297 VAL VAL A . n 
A 1 1298 CYS 1298 1298 1298 CYS CYS A . n 
A 1 1299 PHE 1299 1299 1299 PHE PHE A . n 
A 1 1300 HIS 1300 1300 1300 HIS HIS A . n 
A 1 1301 LEU 1301 1301 1301 LEU LEU A . n 
A 1 1302 SER 1302 1302 1302 SER SER A . n 
A 1 1303 SER 1303 1303 1303 SER SER A . n 
A 1 1304 ILE 1304 1304 1304 ILE ILE A . n 
A 1 1305 PHE 1305 1305 1305 PHE PHE A . n 
A 1 1306 ASN 1306 1306 1306 ASN ASN A . n 
A 1 1307 GLU 1307 1307 1307 GLU GLU A . n 
A 1 1308 THR 1308 1308 1308 THR THR A . n 
A 1 1309 ASP 1309 1309 1309 ASP ASP A . n 
A 1 1310 GLU 1310 1310 1310 GLU GLU A . n 
A 1 1311 SER 1311 1311 1311 SER SER A . n 
A 1 1312 ILE 1312 1312 1312 ILE ILE A . n 
A 1 1313 ILE 1313 1313 1313 ILE ILE A . n 
A 1 1314 GLU 1314 1314 1314 GLU GLU A . n 
A 1 1315 VAL 1315 1315 1315 VAL VAL A . n 
A 1 1316 THR 1316 1316 1316 THR THR A . n 
A 1 1317 LEU 1317 1317 1317 LEU LEU A . n 
A 1 1318 ILE 1318 1318 1318 ILE ILE A . n 
A 1 1319 ASN 1319 1319 1319 ASN ASN A . n 
A 1 1320 LEU 1320 1320 1320 LEU LEU A . n 
A 1 1321 GLY 1321 1321 1321 GLY GLY A . n 
A 1 1322 ILE 1322 1322 1322 ILE ILE A . n 
A 1 1323 THR 1323 1323 1323 THR THR A . n 
A 1 1324 ILE 1324 1324 1324 ILE ILE A . n 
A 1 1325 LEU 1325 1325 1325 LEU LEU A . n 
A 1 1326 THR 1326 1326 1326 THR THR A . n 
A 1 1327 ILE 1327 1327 1327 ILE ILE A . n 
A 1 1328 LEU 1328 1328 1328 LEU LEU A . n 
A 1 1329 VAL 1329 1329 1329 VAL VAL A . n 
A 1 1330 VAL 1330 1330 1330 VAL VAL A . n 
A 1 1331 THR 1331 1331 1331 THR THR A . n 
A 1 1332 ALA 1332 1332 1332 ALA ALA A . n 
A 1 1333 TYR 1333 1333 1333 TYR TYR A . n 
A 1 1334 ILE 1334 1334 1334 ILE ILE A . n 
A 1 1335 ILE 1335 1335 1335 ILE ILE A . n 
A 1 1336 LYS 1336 1336 1336 LYS LYS A . n 
A 1 1337 GLY 1337 1337 1337 GLY GLY A . n 
A 1 1338 PHE 1338 1338 1338 PHE PHE A . n 
A 1 1339 TYR 1339 1339 1339 TYR TYR A . n 
A 1 1340 SER 1340 1340 1340 SER SER A . n 
A 1 1341 CYS 1341 1341 1341 CYS CYS A . n 
A 1 1342 VAL 1342 1342 1342 VAL VAL A . n 
A 1 1343 ILE 1343 1343 1343 ILE ILE A . n 
A 1 1344 ILE 1344 1344 1344 ILE ILE A . n 
A 1 1345 ALA 1345 1345 1345 ALA ALA A . n 
A 1 1346 LEU 1346 1346 1346 LEU LEU A . n 
A 1 1347 ILE 1347 1347 1347 ILE ILE A . n 
A 1 1348 ILE 1348 1348 1348 ILE ILE A . n 
A 1 1349 PHE 1349 1349 1349 PHE PHE A . n 
A 1 1350 LEU 1350 1350 1350 LEU LEU A . n 
A 1 1351 ILE 1351 1351 1351 ILE ILE A . n 
A 1 1352 ASP 1352 1352 1352 ASP ASP A . n 
A 1 1353 LEU 1353 1353 1353 LEU LEU A . n 
A 1 1354 CYS 1354 1354 1354 CYS CYS A . n 
A 1 1355 ILE 1355 1355 1355 ILE ILE A . n 
A 1 1356 PHE 1356 1356 1356 PHE PHE A . n 
A 1 1357 GLY 1357 1357 1357 GLY GLY A . n 
A 1 1358 PHE 1358 1358 1358 PHE PHE A . n 
A 1 1359 MET 1359 1359 1359 MET MET A . n 
A 1 1360 CYS 1360 1360 1360 CYS CYS A . n 
A 1 1361 LEU 1361 1361 1361 LEU LEU A . n 
A 1 1362 CYS 1362 1362 1362 CYS CYS A . n 
A 1 1363 GLY 1363 1363 1363 GLY GLY A . n 
A 1 1364 ILE 1364 1364 1364 ILE ILE A . n 
A 1 1365 THR 1365 1365 1365 THR THR A . n 
A 1 1366 MET 1366 1366 1366 MET MET A . n 
A 1 1367 ASN 1367 1367 1367 ASN ASN A . n 
A 1 1368 ILE 1368 1368 1368 ILE ILE A . n 
A 1 1369 ILE 1369 1369 1369 ILE ILE A . n 
A 1 1370 SER 1370 1370 1370 SER SER A . n 
A 1 1371 MET 1371 1371 1371 MET MET A . n 
A 1 1372 VAL 1372 1372 1372 VAL VAL A . n 
A 1 1373 ILE 1373 1373 1373 ILE ILE A . n 
A 1 1374 LEU 1374 1374 1374 LEU LEU A . n 
A 1 1375 VAL 1375 1375 1375 VAL VAL A . n 
A 1 1376 LEU 1376 1376 1376 LEU LEU A . n 
A 1 1377 SER 1377 1377 1377 SER SER A . n 
A 1 1378 VAL 1378 1378 1378 VAL VAL A . n 
A 1 1379 GLY 1379 1379 1379 GLY GLY A . n 
A 1 1380 PHE 1380 1380 1380 PHE PHE A . n 
A 1 1381 SER 1381 1381 1381 SER SER A . n 
A 1 1382 ILE 1382 1382 1382 ILE ILE A . n 
A 1 1383 ASP 1383 1383 1383 ASP ASP A . n 
A 1 1384 HIS 1384 1384 1384 HIS HIS A . n 
A 1 1385 THR 1385 1385 1385 THR THR A . n 
A 1 1386 SER 1386 1386 1386 SER SER A . n 
A 1 1387 HIS 1387 1387 1387 HIS HIS A . n 
A 1 1388 ILE 1388 1388 1388 ILE ILE A . n 
A 1 1389 VAL 1389 1389 1389 VAL VAL A . n 
A 1 1390 GLN 1390 1390 1390 GLN GLN A . n 
A 1 1391 ALA 1391 1391 1391 ALA ALA A . n 
A 1 1392 PHE 1392 1392 1392 PHE PHE A . n 
A 1 1393 SER 1393 1393 1393 SER SER A . n 
A 1 1394 HIS 1394 1394 1394 HIS HIS A . n 
A 1 1395 SER 1395 1395 1395 SER SER A . n 
A 1 1396 MET 1396 1396 1396 MET MET A . n 
A 1 1397 GLY 1397 1397 1397 GLY GLY A . n 
A 1 1398 ARG 1398 1398 1398 ARG ARG A . n 
A 1 1399 THR 1399 1399 1399 THR THR A . n 
A 1 1400 ARG 1400 1400 1400 ARG ARG A . n 
A 1 1401 ASP 1401 1401 1401 ASP ASP A . n 
A 1 1402 GLU 1402 1402 1402 GLU GLU A . n 
A 1 1403 LYS 1403 1403 1403 LYS LYS A . n 
A 1 1404 MET 1404 1404 1404 MET MET A . n 
A 1 1405 LYS 1405 1405 1405 LYS LYS A . n 
A 1 1406 GLU 1406 1406 1406 GLU GLU A . n 
A 1 1407 SER 1407 1407 1407 SER SER A . n 
A 1 1408 LEU 1408 1408 1408 LEU LEU A . n 
A 1 1409 HIS 1409 1409 1409 HIS HIS A . n 
A 1 1410 LEU 1410 1410 1410 LEU LEU A . n 
A 1 1411 MET 1411 1411 1411 MET MET A . n 
A 1 1412 ILE 1412 1412 1412 ILE ILE A . n 
A 1 1413 GLY 1413 1413 1413 GLY GLY A . n 
A 1 1414 PRO 1414 1414 1414 PRO PRO A . n 
A 1 1415 VAL 1415 1415 1415 VAL VAL A . n 
A 1 1416 LEU 1416 1416 1416 LEU LEU A . n 
A 1 1417 HIS 1417 1417 1417 HIS HIS A . n 
A 1 1418 SER 1418 1418 1418 SER SER A . n 
A 1 1419 GLY 1419 1419 1419 GLY GLY A . n 
A 1 1420 LEU 1420 1420 1420 LEU LEU A . n 
A 1 1421 SER 1421 1421 1421 SER SER A . n 
A 1 1422 THR 1422 1422 1422 THR THR A . n 
A 1 1423 TRP 1423 1423 1423 TRP TRP A . n 
A 1 1424 PHE 1424 1424 1424 PHE PHE A . n 
A 1 1425 VAL 1425 1425 1425 VAL VAL A . n 
A 1 1426 ILE 1426 1426 1426 ILE ILE A . n 
A 1 1427 SER 1427 1427 1427 SER SER A . n 
A 1 1428 THR 1428 1428 1428 THR THR A . n 
A 1 1429 LEU 1429 1429 1429 LEU LEU A . n 
A 1 1430 PHE 1430 1430 1430 PHE PHE A . n 
A 1 1431 PHE 1431 1431 1431 PHE PHE A . n 
A 1 1432 SER 1432 1432 1432 SER SER A . n 
A 1 1433 ASN 1433 1433 1433 ASN ASN A . n 
A 1 1434 LYS 1434 1434 1434 LYS LYS A . n 
A 1 1435 ASP 1435 1435 1435 ASP ASP A . n 
A 1 1436 PHE 1436 1436 1436 PHE PHE A . n 
A 1 1437 THR 1437 1437 1437 THR THR A . n 
A 1 1438 VAL 1438 1438 1438 VAL VAL A . n 
A 1 1439 ILE 1439 1439 1439 ILE ILE A . n 
A 1 1440 PHE 1440 1440 1440 PHE PHE A . n 
A 1 1441 PHE 1441 1441 1441 PHE PHE A . n 
A 1 1442 GLN 1442 1442 1442 GLN GLN A . n 
A 1 1443 THR 1443 1443 1443 THR THR A . n 
A 1 1444 LEU 1444 1444 1444 LEU LEU A . n 
A 1 1445 SER 1445 1445 1445 SER SER A . n 
A 1 1446 LEU 1446 1446 1446 LEU LEU A . n 
A 1 1447 VAL 1447 1447 1447 VAL VAL A . n 
A 1 1448 LEU 1448 1448 1448 LEU LEU A . n 
A 1 1449 PHE 1449 1449 1449 PHE PHE A . n 
A 1 1450 PHE 1450 1450 1450 PHE PHE A . n 
A 1 1451 SER 1451 1451 1451 SER SER A . n 
A 1 1452 ILE 1452 1452 1452 ILE ILE A . n 
A 1 1453 THR 1453 1453 1453 THR THR A . n 
A 1 1454 PHE 1454 1454 1454 PHE PHE A . n 
A 1 1455 SER 1455 1455 1455 SER SER A . n 
A 1 1456 SER 1456 1456 1456 SER SER A . n 
A 1 1457 MET 1457 1457 1457 MET MET A . n 
A 1 1458 PHE 1458 1458 1458 PHE PHE A . n 
A 1 1459 LEU 1459 1459 1459 LEU LEU A . n 
A 1 1460 PRO 1460 1460 1460 PRO PRO A . n 
A 1 1461 VAL 1461 1461 1461 VAL VAL A . n 
A 1 1462 LEU 1462 1462 1462 LEU LEU A . n 
A 1 1463 LEU 1463 1463 1463 LEU LEU A . n 
A 1 1464 SER 1464 1464 1464 SER SER A . n 
A 1 1465 SER 1465 1465 1465 SER SER A . n 
A 1 1466 PHE 1466 1466 1466 PHE PHE A . n 
A 1 1467 GLY 1467 1467 1467 GLY GLY A . n 
A 1 1468 PRO 1468 1468 1468 PRO PRO A . n 
A 1 1469 LEU 1469 1469 1469 LEU LEU A . n 
A 1 1470 HIS 1470 1470 1470 HIS HIS A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        Y6F 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   Y6F 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 NAG 1 1501 1471 NAG NAG A . 
C 3 CLR 1 1502 1481 CLR CLR A . 
D 4 Y6F 1 1503 1472 Y6F MMV A . 
E 2 NAG 1 1504 1482 NAG NAG A . 
# 
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 LYS 131  ? CG  ? A LYS 131  CG  
2  1 Y 1 A LYS 131  ? CD  ? A LYS 131  CD  
3  1 Y 1 A LYS 131  ? CE  ? A LYS 131  CE  
4  1 Y 1 A LYS 131  ? NZ  ? A LYS 131  NZ  
5  1 Y 1 A LEU 136  ? CG  ? A LEU 136  CG  
6  1 Y 1 A LEU 136  ? CD1 ? A LEU 136  CD1 
7  1 Y 1 A LEU 136  ? CD2 ? A LEU 136  CD2 
8  1 Y 1 A LYS 491  ? CG  ? A LYS 491  CG  
9  1 Y 1 A LYS 491  ? CD  ? A LYS 491  CD  
10 1 Y 1 A LYS 491  ? CE  ? A LYS 491  CE  
11 1 Y 1 A LYS 491  ? NZ  ? A LYS 491  NZ  
12 1 Y 1 A LEU 671  ? CG  ? A LEU 671  CG  
13 1 Y 1 A LEU 671  ? CD1 ? A LEU 671  CD1 
14 1 Y 1 A LEU 671  ? CD2 ? A LEU 671  CD2 
15 1 Y 1 A PHE 672  ? CG  ? A PHE 672  CG  
16 1 Y 1 A PHE 672  ? CD1 ? A PHE 672  CD1 
17 1 Y 1 A PHE 672  ? CD2 ? A PHE 672  CD2 
18 1 Y 1 A PHE 672  ? CE1 ? A PHE 672  CE1 
19 1 Y 1 A PHE 672  ? CE2 ? A PHE 672  CE2 
20 1 Y 1 A PHE 672  ? CZ  ? A PHE 672  CZ  
21 1 Y 1 A ARG 673  ? CG  ? A ARG 673  CG  
22 1 Y 1 A ARG 673  ? CD  ? A ARG 673  CD  
23 1 Y 1 A ARG 673  ? NE  ? A ARG 673  NE  
24 1 Y 1 A ARG 673  ? CZ  ? A ARG 673  CZ  
25 1 Y 1 A ARG 673  ? NH1 ? A ARG 673  NH1 
26 1 Y 1 A ARG 673  ? NH2 ? A ARG 673  NH2 
27 1 Y 1 A TYR 1047 ? CG  ? A TYR 1047 CG  
28 1 Y 1 A TYR 1047 ? CD1 ? A TYR 1047 CD1 
29 1 Y 1 A TYR 1047 ? CD2 ? A TYR 1047 CD2 
30 1 Y 1 A TYR 1047 ? CE1 ? A TYR 1047 CE1 
31 1 Y 1 A TYR 1047 ? CE2 ? A TYR 1047 CE2 
32 1 Y 1 A TYR 1047 ? CZ  ? A TYR 1047 CZ  
33 1 Y 1 A TYR 1047 ? OH  ? A TYR 1047 OH  
# 
_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                     8V1G 
_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                         8V1G 
_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                   8V1G 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     8V1G 
_struct.title                        'plasmodium falciparum Niemann-Pick type C1-related protein bound with MMV009108' 
_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        8V1G 
_struct_keywords.text            
'Niemann-Pick type C1-related protein, NCR1, cholesterol transporter, plasmodium falciparum, MEMBRANE PROTEIN' 
_struct_keywords.pdbx_keywords   'MEMBRANE PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 2 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q8I266_PLAF7 
_struct_ref.pdbx_db_accession          Q8I266 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MFVKNFIHKLKELKQKSLDKFANLLYDYGGYVYDRPCTFIICSLICCLLLTCGFYFKEHEKDIYKLYSISNSYAYETNET
INDFFYKSRRCFILVESNVNLLKPKILRELQKFEEGTKDIEVDLSEINECKTNSELPPEQSHVAKELYKTLIQRSEENLK
SGKINGSLFDYSDLDENGKSVLSLAGKENNDDTLIEGDNKNDEETSANNNNNEDDNNEDDNNEDDNNEDDNNENDNNNNN
EDDNNNDDDDDEDNEEEDEEKQKSLREKLYRKIYEMLKKKKENIVLDENNPNVNFTDYKDDVFYPYQYIPPMLIKADRCK
LQNVFGDKNLNIDLREASDGLKKQITYTLEDICEKKYGDCNFSSLFLYYEKGNGYIDYPIKVDNLDFYVNRRTYKEMMFK
GILGNMVYEKSGSKYIIKSANAIMTVIPLLNSHTYEPYALAYEKKLIDYVRFYNLDDIIQDEETNDDNDPFIRFHVFTDR
SLEDEVDRISKIDNLTRLLLLIGVLLIFMYALFNNVTSVLYRSKPLCAVMGIFCGFLGFLSGSGFLYFLGVKSVPPAETV
PFLVIGVGVDDVFVILNSYSLLFMVKDNKKRIQMCLKDSALAITVTTLTNIIAFLISAISPFYSICAFSLFTASSLFFGY
LMVLTFLLSFLCIEAKLEKKKRNIFTGTFHLFRSIFMKSSKKNKKENKENNIHDDGDNDNDEKKKDLSLEVKNNEDDYEN
ISIYEWIHNLYLFEESINKKKKNAALVYASNNGMSSNLNNVNEDGFPNPSKIVSMEDVKKRNIKKDDAYINKEDEEGGGY
YNKDDNKKKDILGKKQKKNNNNVTLVSKKGEDNELDVYYENLDEKTNDKYKMNNIKSSKLKYDNDKKDGAIINNRPSSDE
EYKEEKDKNKINILNDVFNDITIKPNENILLDRGDVIKSSGYDSSYNDLQSSSLPNPSSNEVLNKTTMVYNETDLKDNKK
EIKSSKKNVKDIKKSDMIHDDTYDIINSNNKNILLSSNEINNNSNNTNKFNNNSTELATKDTQQFINGHDKNIYLLSSHD
NALFYKYIYEEPKGNIGKYFRSLVKNYYVPFLSSRFGKTIVYIMFTIIIAMSIYGCTLMKKGIKYDKAFPVDSYVRRFTT
AKIKYFPDFGDFIEVYYFDKHFINKYRGLEKNTKEAASSFLYSDLTDRQIMNSPKINKNVHWENTNLQEELINMHNTLES
QEFVTSVANGFTFFLNKNKSSLRKENPQEFYEIFANWLKKDFVGNLFKNDFVFLNGKLVAWRFHYFQKNVDDSEISSKWL
KACKQITKLENHNVQMVCFHLSSIFNETDESIIEVTLINLGITILTILVVTAYIIKGFYSCVIIALIIFLIDLCIFGFMC
LCGITMNIISMVILVLSVGFSIDHTSHIVQAFSHSMGRTRDEKMKESLHLMIGPVLHSGLSTWFVISTLFFSNKDFTVIF
FQTLSLVLFFSITFSSMFLPVLLSSFGPLH
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              8V1G 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 1470 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q8I266 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1470 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       1470 
# 
_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,B,C,D,E 
# 
_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 ASN A 5    ? ARG A 35   ? ASN A 5    ARG A 35   1 ? 31 
HELX_P HELX_P2  AA2 ARG A 35   ? CYS A 52   ? ARG A 35   CYS A 52   1 ? 18 
HELX_P HELX_P3  AA3 GLY A 53   ? LYS A 57   ? GLY A 53   LYS A 57   5 ? 5  
HELX_P HELX_P4  AA4 ASP A 62   ? SER A 68   ? ASP A 62   SER A 68   1 ? 7  
HELX_P HELX_P5  AA5 SER A 72   ? PHE A 85   ? SER A 72   PHE A 85   1 ? 14 
HELX_P HELX_P6  AA6 LYS A 103  ? ASP A 119  ? LYS A 103  ASP A 119  1 ? 17 
HELX_P HELX_P7  AA7 SER A 125  ? ILE A 127  ? SER A 125  ILE A 127  5 ? 3  
HELX_P HELX_P8  AA8 SER A 141  ? GLY A 162  ? SER A 141  GLY A 162  1 ? 22 
HELX_P HELX_P9  AA9 ASN A 294  ? LYS A 299  ? ASN A 294  LYS A 299  1 ? 6  
HELX_P HELX_P10 AB1 PRO A 310  ? ILE A 314  ? PRO A 310  ILE A 314  5 ? 5  
HELX_P HELX_P11 AB2 LYS A 320  ? PHE A 325  ? LYS A 320  PHE A 325  1 ? 6  
HELX_P HELX_P12 AB3 ASP A 333  ? ALA A 337  ? ASP A 333  ALA A 337  5 ? 5  
HELX_P HELX_P13 AB4 SER A 338  ? ILE A 345  ? SER A 338  ILE A 345  1 ? 8  
HELX_P HELX_P14 AB5 GLU A 350  ? ILE A 352  ? GLU A 350  ILE A 352  5 ? 3  
HELX_P HELX_P15 AB6 SER A 364  ? TYR A 368  ? SER A 364  TYR A 368  5 ? 5  
HELX_P HELX_P16 AB7 TYR A 369  ? ASN A 373  ? TYR A 369  ASN A 373  5 ? 5  
HELX_P HELX_P17 AB8 MET A 398  ? LEU A 403  ? MET A 398  LEU A 403  1 ? 6  
HELX_P HELX_P18 AB9 TYR A 435  ? ARG A 451  ? TYR A 435  ARG A 451  1 ? 17 
HELX_P HELX_P19 AC1 LEU A 455  ? GLN A 460  ? LEU A 455  GLN A 460  1 ? 6  
HELX_P HELX_P20 AC2 THR A 478  ? LYS A 491  ? THR A 478  LYS A 491  1 ? 14 
HELX_P HELX_P21 AC3 ASP A 493  ? VAL A 516  ? ASP A 493  VAL A 516  1 ? 24 
HELX_P HELX_P22 AC4 LYS A 524  ? GLY A 550  ? LYS A 524  GLY A 550  1 ? 27 
HELX_P HELX_P23 AC5 VAL A 554  ? GLU A 558  ? VAL A 554  GLU A 558  5 ? 5  
HELX_P HELX_P24 AC6 THR A 559  ? VAL A 569  ? THR A 559  VAL A 569  1 ? 11 
HELX_P HELX_P25 AC7 VAL A 569  ? LEU A 582  ? VAL A 569  LEU A 582  1 ? 14 
HELX_P HELX_P26 AC8 ASP A 587  ? ALA A 618  ? ASP A 587  ALA A 618  1 ? 32 
HELX_P HELX_P27 AC9 PHE A 622  ? LYS A 660  ? PHE A 622  LYS A 660  1 ? 39 
HELX_P HELX_P28 AD1 ASN A 663  ? SER A 674  ? ASN A 663  SER A 674  1 ? 12 
HELX_P HELX_P29 AD2 SER A 722  ? GLU A 735  ? SER A 722  GLU A 735  1 ? 14 
HELX_P HELX_P30 AD3 GLY A 1057 ? TYR A 1067 ? GLY A 1057 TYR A 1067 1 ? 11 
HELX_P HELX_P31 AD4 TYR A 1067 ? SER A 1074 ? TYR A 1067 SER A 1074 1 ? 8  
HELX_P HELX_P32 AD5 SER A 1074 ? LEU A 1098 ? SER A 1074 LEU A 1098 1 ? 25 
HELX_P HELX_P33 AD6 LYS A 1104 ? PHE A 1109 ? LYS A 1104 PHE A 1109 5 ? 6  
HELX_P HELX_P34 AD7 SER A 1113 ? PHE A 1126 ? SER A 1113 PHE A 1126 1 ? 14 
HELX_P HELX_P35 AD8 ASP A 1139 ? GLY A 1148 ? ASP A 1139 GLY A 1148 1 ? 10 
HELX_P HELX_P36 AD9 GLN A 1169 ? SER A 1173 ? GLN A 1169 SER A 1173 5 ? 5  
HELX_P HELX_P37 AE1 ASN A 1184 ? GLN A 1201 ? ASN A 1184 GLN A 1201 1 ? 18 
HELX_P HELX_P38 AE2 ASN A 1209 ? ASN A 1218 ? ASN A 1209 ASN A 1218 1 ? 10 
HELX_P HELX_P39 AE3 SER A 1220 ? GLU A 1225 ? SER A 1220 GLU A 1225 5 ? 6  
HELX_P HELX_P40 AE4 ASN A 1226 ? ASP A 1241 ? ASN A 1226 ASP A 1241 1 ? 16 
HELX_P HELX_P41 AE5 ASP A 1241 ? LYS A 1248 ? ASP A 1241 LYS A 1248 1 ? 8  
HELX_P HELX_P42 AE6 ASP A 1272 ? LYS A 1288 ? ASP A 1272 LYS A 1288 1 ? 17 
HELX_P HELX_P43 AE7 LEU A 1289 ? ASN A 1293 ? LEU A 1289 ASN A 1293 5 ? 5  
HELX_P HELX_P44 AE8 LEU A 1301 ? TYR A 1333 ? LEU A 1301 TYR A 1333 1 ? 33 
HELX_P HELX_P45 AE9 PHE A 1338 ? CYS A 1362 ? PHE A 1338 CYS A 1362 1 ? 25 
HELX_P HELX_P46 AF1 ASN A 1367 ? SER A 1395 ? ASN A 1367 SER A 1395 1 ? 29 
HELX_P HELX_P47 AF2 THR A 1399 ? SER A 1427 ? THR A 1399 SER A 1427 1 ? 29 
HELX_P HELX_P48 AF3 THR A 1428 ? SER A 1432 ? THR A 1428 SER A 1432 5 ? 5  
HELX_P HELX_P49 AF4 LYS A 1434 ? MET A 1457 ? LYS A 1434 MET A 1457 1 ? 24 
HELX_P HELX_P50 AF5 MET A 1457 ? GLY A 1467 ? MET A 1457 GLY A 1467 1 ? 11 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale one ? A ASN 165 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 165 A NAG 1501 1_555 ? ? ? ? ? ? ? 1.439 ? N-Glycosylation 
covale2 covale one ? A ASN 294 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 294 A NAG 1504 1_555 ? ? ? ? ? ? ? 1.444 ? N-Glycosylation 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 NAG B . ? ASN A 165 ? NAG A 1501 ? 1_555 ASN A 165 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate 
2 NAG E . ? ASN A 294 ? NAG A 1504 ? 1_555 ASN A 294 ? 1_555 C1 ND2 ASN 1 NAG N-Glycosylation Carbohydrate 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          TYR 
_struct_mon_prot_cis.label_seq_id           304 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           TYR 
_struct_mon_prot_cis.auth_seq_id            304 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    305 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     305 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       2.26 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 2 ? 
AA3 ? 4 ? 
AA4 ? 5 ? 
AA5 ? 2 ? 
AA6 ? 3 ? 
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 
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA7 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ALA A 422  ? LEU A 430  ? ALA A 422  LEU A 430  
AA1 2 SER A 88   ? SER A 97   ? SER A 88   SER A 97   
AA1 3 ILE A 472  ? PHE A 477  ? ILE A 472  PHE A 477  
AA2 1 GLU A 121  ? ASP A 123  ? GLU A 121  ASP A 123  
AA2 2 THR A 346  ? THR A 348  ? THR A 346  THR A 348  
AA3 1 PHE A 303  ? TYR A 304  ? PHE A 303  TYR A 304  
AA3 2 PHE A 1251 ? LEU A 1254 ? PHE A 1251 LEU A 1254 
AA3 3 LYS A 1257 ? GLN A 1267 ? LYS A 1257 GLN A 1267 
AA3 4 VAL A 1204 ? ALA A 1208 ? VAL A 1204 ALA A 1208 
AA4 1 PHE A 303  ? TYR A 304  ? PHE A 303  TYR A 304  
AA4 2 PHE A 1251 ? LEU A 1254 ? PHE A 1251 LEU A 1254 
AA4 3 LYS A 1257 ? GLN A 1267 ? LYS A 1257 GLN A 1267 
AA4 4 ASP A 1131 ? PHE A 1138 ? ASP A 1131 PHE A 1138 
AA4 5 VAL A 1297 ? PHE A 1299 ? VAL A 1297 PHE A 1299 
AA5 1 LYS A 355  ? LYS A 356  ? LYS A 355  LYS A 356  
AA5 2 ASP A 359  ? CYS A 360  ? ASP A 359  CYS A 360  
AA6 1 ILE A 380  ? VAL A 382  ? ILE A 380  VAL A 382  
AA6 2 TYR A 415  ? SER A 419  ? TYR A 415  SER A 419  
AA6 3 VAL A 407  ? TYR A 408  ? VAL A 407  TYR A 408  
AA7 1 TYR A 388  ? VAL A 389  ? TYR A 388  VAL A 389  
AA7 2 GLU A 396  ? MET A 397  ? GLU A 396  MET A 397  
# 
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 LEU A 429  ? O LEU A 429  N ARG A 89   ? N ARG A 89   
AA1 2 3 N LEU A 94   ? N LEU A 94   O HIS A 475  ? O HIS A 475  
AA2 1 2 N VAL A 122  ? N VAL A 122  O TYR A 347  ? O TYR A 347  
AA3 1 2 N TYR A 304  ? N TYR A 304  O PHE A 1253 ? O PHE A 1253 
AA3 2 3 N LEU A 1254 ? N LEU A 1254 O LYS A 1257 ? O LYS A 1257 
AA3 3 4 O HIS A 1264 ? O HIS A 1264 N ALA A 1208 ? N ALA A 1208 
AA4 1 2 N TYR A 304  ? N TYR A 304  O PHE A 1253 ? O PHE A 1253 
AA4 2 3 N LEU A 1254 ? N LEU A 1254 O LYS A 1257 ? O LYS A 1257 
AA4 3 4 O TRP A 1261 ? O TRP A 1261 N TYR A 1137 ? N TYR A 1137 
AA4 4 5 N TYR A 1136 ? N TYR A 1136 O VAL A 1297 ? O VAL A 1297 
AA5 1 2 N LYS A 356  ? N LYS A 356  O ASP A 359  ? O ASP A 359  
AA6 1 2 N VAL A 382  ? N VAL A 382  O TYR A 415  ? O TYR A 415  
AA6 2 3 O SER A 419  ? O SER A 419  N VAL A 407  ? N VAL A 407  
AA7 1 2 N TYR A 388  ? N TYR A 388  O MET A 397  ? O MET A 397  
# 
_pdbx_entry_details.entry_id                   8V1G 
_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     Y 
_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 THR A 132  ? ? 57.95   19.50   
2 1 ASN A 133  ? ? -140.95 23.02   
3 1 GLU A 135  ? ? -99.84  39.55   
4 1 THR A 517  ? ? -126.28 -169.44 
5 1 THR A 645  ? ? -106.44 -61.35  
6 1 ASN A 1179 ? ? 39.30   52.95   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          8V1G 
_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      ? 
# 
_em_3d_reconstruction.entry_id                    8V1G 
_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                  2.98 
_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               82204 
_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            7.5 
# 
_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                 'Niemann-Pick type C1-related protein' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        8V1G 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'FEI TITAN 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             800 
_em_imaging.nominal_defocus_max             1500 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           81000 
_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              8V1G 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              ? 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   ? 
_em_vitrification.instrument            ? 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                8V1G 
_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 1    ? A MET 1    
2   1 Y 1 A PHE 2    ? A PHE 2    
3   1 Y 1 A VAL 3    ? A VAL 3    
4   1 Y 1 A LYS 4    ? A LYS 4    
5   1 Y 1 A VAL 181  ? A VAL 181  
6   1 Y 1 A LEU 182  ? A LEU 182  
7   1 Y 1 A SER 183  ? A SER 183  
8   1 Y 1 A LEU 184  ? A LEU 184  
9   1 Y 1 A ALA 185  ? A ALA 185  
10  1 Y 1 A GLY 186  ? A GLY 186  
11  1 Y 1 A LYS 187  ? A LYS 187  
12  1 Y 1 A GLU 188  ? A GLU 188  
13  1 Y 1 A ASN 189  ? A ASN 189  
14  1 Y 1 A ASN 190  ? A ASN 190  
15  1 Y 1 A ASP 191  ? A ASP 191  
16  1 Y 1 A ASP 192  ? A ASP 192  
17  1 Y 1 A THR 193  ? A THR 193  
18  1 Y 1 A LEU 194  ? A LEU 194  
19  1 Y 1 A ILE 195  ? A ILE 195  
20  1 Y 1 A GLU 196  ? A GLU 196  
21  1 Y 1 A GLY 197  ? A GLY 197  
22  1 Y 1 A ASP 198  ? A ASP 198  
23  1 Y 1 A ASN 199  ? A ASN 199  
24  1 Y 1 A LYS 200  ? A LYS 200  
25  1 Y 1 A ASN 201  ? A ASN 201  
26  1 Y 1 A ASP 202  ? A ASP 202  
27  1 Y 1 A GLU 203  ? A GLU 203  
28  1 Y 1 A GLU 204  ? A GLU 204  
29  1 Y 1 A THR 205  ? A THR 205  
30  1 Y 1 A SER 206  ? A SER 206  
31  1 Y 1 A ALA 207  ? A ALA 207  
32  1 Y 1 A ASN 208  ? A ASN 208  
33  1 Y 1 A ASN 209  ? A ASN 209  
34  1 Y 1 A ASN 210  ? A ASN 210  
35  1 Y 1 A ASN 211  ? A ASN 211  
36  1 Y 1 A ASN 212  ? A ASN 212  
37  1 Y 1 A GLU 213  ? A GLU 213  
38  1 Y 1 A ASP 214  ? A ASP 214  
39  1 Y 1 A ASP 215  ? A ASP 215  
40  1 Y 1 A ASN 216  ? A ASN 216  
41  1 Y 1 A ASN 217  ? A ASN 217  
42  1 Y 1 A GLU 218  ? A GLU 218  
43  1 Y 1 A ASP 219  ? A ASP 219  
44  1 Y 1 A ASP 220  ? A ASP 220  
45  1 Y 1 A ASN 221  ? A ASN 221  
46  1 Y 1 A ASN 222  ? A ASN 222  
47  1 Y 1 A GLU 223  ? A GLU 223  
48  1 Y 1 A ASP 224  ? A ASP 224  
49  1 Y 1 A ASP 225  ? A ASP 225  
50  1 Y 1 A ASN 226  ? A ASN 226  
51  1 Y 1 A ASN 227  ? A ASN 227  
52  1 Y 1 A GLU 228  ? A GLU 228  
53  1 Y 1 A ASP 229  ? A ASP 229  
54  1 Y 1 A ASP 230  ? A ASP 230  
55  1 Y 1 A ASN 231  ? A ASN 231  
56  1 Y 1 A ASN 232  ? A ASN 232  
57  1 Y 1 A GLU 233  ? A GLU 233  
58  1 Y 1 A ASN 234  ? A ASN 234  
59  1 Y 1 A ASP 235  ? A ASP 235  
60  1 Y 1 A ASN 236  ? A ASN 236  
61  1 Y 1 A ASN 237  ? A ASN 237  
62  1 Y 1 A ASN 238  ? A ASN 238  
63  1 Y 1 A ASN 239  ? A ASN 239  
64  1 Y 1 A ASN 240  ? A ASN 240  
65  1 Y 1 A GLU 241  ? A GLU 241  
66  1 Y 1 A ASP 242  ? A ASP 242  
67  1 Y 1 A ASP 243  ? A ASP 243  
68  1 Y 1 A ASN 244  ? A ASN 244  
69  1 Y 1 A ASN 245  ? A ASN 245  
70  1 Y 1 A ASN 246  ? A ASN 246  
71  1 Y 1 A ASP 247  ? A ASP 247  
72  1 Y 1 A ASP 248  ? A ASP 248  
73  1 Y 1 A ASP 249  ? A ASP 249  
74  1 Y 1 A ASP 250  ? A ASP 250  
75  1 Y 1 A ASP 251  ? A ASP 251  
76  1 Y 1 A GLU 252  ? A GLU 252  
77  1 Y 1 A ASP 253  ? A ASP 253  
78  1 Y 1 A ASN 254  ? A ASN 254  
79  1 Y 1 A GLU 255  ? A GLU 255  
80  1 Y 1 A GLU 256  ? A GLU 256  
81  1 Y 1 A GLU 257  ? A GLU 257  
82  1 Y 1 A ASP 258  ? A ASP 258  
83  1 Y 1 A GLU 259  ? A GLU 259  
84  1 Y 1 A GLU 260  ? A GLU 260  
85  1 Y 1 A LYS 261  ? A LYS 261  
86  1 Y 1 A GLN 262  ? A GLN 262  
87  1 Y 1 A LYS 263  ? A LYS 263  
88  1 Y 1 A SER 264  ? A SER 264  
89  1 Y 1 A LEU 265  ? A LEU 265  
90  1 Y 1 A ARG 266  ? A ARG 266  
91  1 Y 1 A GLU 267  ? A GLU 267  
92  1 Y 1 A LYS 268  ? A LYS 268  
93  1 Y 1 A LEU 269  ? A LEU 269  
94  1 Y 1 A TYR 270  ? A TYR 270  
95  1 Y 1 A ARG 271  ? A ARG 271  
96  1 Y 1 A LYS 272  ? A LYS 272  
97  1 Y 1 A ILE 273  ? A ILE 273  
98  1 Y 1 A TYR 274  ? A TYR 274  
99  1 Y 1 A GLU 275  ? A GLU 275  
100 1 Y 1 A MET 276  ? A MET 276  
101 1 Y 1 A LEU 277  ? A LEU 277  
102 1 Y 1 A LYS 278  ? A LYS 278  
103 1 Y 1 A LYS 279  ? A LYS 279  
104 1 Y 1 A LYS 280  ? A LYS 280  
105 1 Y 1 A LYS 281  ? A LYS 281  
106 1 Y 1 A GLU 282  ? A GLU 282  
107 1 Y 1 A ASN 283  ? A ASN 283  
108 1 Y 1 A ILE 284  ? A ILE 284  
109 1 Y 1 A VAL 285  ? A VAL 285  
110 1 Y 1 A LEU 286  ? A LEU 286  
111 1 Y 1 A ASP 287  ? A ASP 287  
112 1 Y 1 A GLU 288  ? A GLU 288  
113 1 Y 1 A ASN 289  ? A ASN 289  
114 1 Y 1 A ASN 290  ? A ASN 290  
115 1 Y 1 A PRO 291  ? A PRO 291  
116 1 Y 1 A ILE 675  ? A ILE 675  
117 1 Y 1 A PHE 676  ? A PHE 676  
118 1 Y 1 A MET 677  ? A MET 677  
119 1 Y 1 A LYS 678  ? A LYS 678  
120 1 Y 1 A SER 679  ? A SER 679  
121 1 Y 1 A SER 680  ? A SER 680  
122 1 Y 1 A LYS 681  ? A LYS 681  
123 1 Y 1 A LYS 682  ? A LYS 682  
124 1 Y 1 A ASN 683  ? A ASN 683  
125 1 Y 1 A LYS 684  ? A LYS 684  
126 1 Y 1 A LYS 685  ? A LYS 685  
127 1 Y 1 A GLU 686  ? A GLU 686  
128 1 Y 1 A ASN 687  ? A ASN 687  
129 1 Y 1 A LYS 688  ? A LYS 688  
130 1 Y 1 A GLU 689  ? A GLU 689  
131 1 Y 1 A ASN 690  ? A ASN 690  
132 1 Y 1 A ASN 691  ? A ASN 691  
133 1 Y 1 A ILE 692  ? A ILE 692  
134 1 Y 1 A HIS 693  ? A HIS 693  
135 1 Y 1 A ASP 694  ? A ASP 694  
136 1 Y 1 A ASP 695  ? A ASP 695  
137 1 Y 1 A GLY 696  ? A GLY 696  
138 1 Y 1 A ASP 697  ? A ASP 697  
139 1 Y 1 A ASN 698  ? A ASN 698  
140 1 Y 1 A ASP 699  ? A ASP 699  
141 1 Y 1 A ASN 700  ? A ASN 700  
142 1 Y 1 A ASP 701  ? A ASP 701  
143 1 Y 1 A GLU 702  ? A GLU 702  
144 1 Y 1 A LYS 703  ? A LYS 703  
145 1 Y 1 A LYS 704  ? A LYS 704  
146 1 Y 1 A LYS 705  ? A LYS 705  
147 1 Y 1 A ASP 706  ? A ASP 706  
148 1 Y 1 A LEU 707  ? A LEU 707  
149 1 Y 1 A SER 708  ? A SER 708  
150 1 Y 1 A LEU 709  ? A LEU 709  
151 1 Y 1 A GLU 710  ? A GLU 710  
152 1 Y 1 A VAL 711  ? A VAL 711  
153 1 Y 1 A LYS 712  ? A LYS 712  
154 1 Y 1 A ASN 713  ? A ASN 713  
155 1 Y 1 A ASN 714  ? A ASN 714  
156 1 Y 1 A GLU 715  ? A GLU 715  
157 1 Y 1 A ASP 716  ? A ASP 716  
158 1 Y 1 A ASP 717  ? A ASP 717  
159 1 Y 1 A TYR 718  ? A TYR 718  
160 1 Y 1 A GLU 719  ? A GLU 719  
161 1 Y 1 A ASN 720  ? A ASN 720  
162 1 Y 1 A ILE 737  ? A ILE 737  
163 1 Y 1 A ASN 738  ? A ASN 738  
164 1 Y 1 A LYS 739  ? A LYS 739  
165 1 Y 1 A LYS 740  ? A LYS 740  
166 1 Y 1 A LYS 741  ? A LYS 741  
167 1 Y 1 A LYS 742  ? A LYS 742  
168 1 Y 1 A ASN 743  ? A ASN 743  
169 1 Y 1 A ALA 744  ? A ALA 744  
170 1 Y 1 A ALA 745  ? A ALA 745  
171 1 Y 1 A LEU 746  ? A LEU 746  
172 1 Y 1 A VAL 747  ? A VAL 747  
173 1 Y 1 A TYR 748  ? A TYR 748  
174 1 Y 1 A ALA 749  ? A ALA 749  
175 1 Y 1 A SER 750  ? A SER 750  
176 1 Y 1 A ASN 751  ? A ASN 751  
177 1 Y 1 A ASN 752  ? A ASN 752  
178 1 Y 1 A GLY 753  ? A GLY 753  
179 1 Y 1 A MET 754  ? A MET 754  
180 1 Y 1 A SER 755  ? A SER 755  
181 1 Y 1 A SER 756  ? A SER 756  
182 1 Y 1 A ASN 757  ? A ASN 757  
183 1 Y 1 A LEU 758  ? A LEU 758  
184 1 Y 1 A ASN 759  ? A ASN 759  
185 1 Y 1 A ASN 760  ? A ASN 760  
186 1 Y 1 A VAL 761  ? A VAL 761  
187 1 Y 1 A ASN 762  ? A ASN 762  
188 1 Y 1 A GLU 763  ? A GLU 763  
189 1 Y 1 A ASP 764  ? A ASP 764  
190 1 Y 1 A GLY 765  ? A GLY 765  
191 1 Y 1 A PHE 766  ? A PHE 766  
192 1 Y 1 A PRO 767  ? A PRO 767  
193 1 Y 1 A ASN 768  ? A ASN 768  
194 1 Y 1 A PRO 769  ? A PRO 769  
195 1 Y 1 A SER 770  ? A SER 770  
196 1 Y 1 A LYS 771  ? A LYS 771  
197 1 Y 1 A ILE 772  ? A ILE 772  
198 1 Y 1 A VAL 773  ? A VAL 773  
199 1 Y 1 A SER 774  ? A SER 774  
200 1 Y 1 A MET 775  ? A MET 775  
201 1 Y 1 A GLU 776  ? A GLU 776  
202 1 Y 1 A ASP 777  ? A ASP 777  
203 1 Y 1 A VAL 778  ? A VAL 778  
204 1 Y 1 A LYS 779  ? A LYS 779  
205 1 Y 1 A LYS 780  ? A LYS 780  
206 1 Y 1 A ARG 781  ? A ARG 781  
207 1 Y 1 A ASN 782  ? A ASN 782  
208 1 Y 1 A ILE 783  ? A ILE 783  
209 1 Y 1 A LYS 784  ? A LYS 784  
210 1 Y 1 A LYS 785  ? A LYS 785  
211 1 Y 1 A ASP 786  ? A ASP 786  
212 1 Y 1 A ASP 787  ? A ASP 787  
213 1 Y 1 A ALA 788  ? A ALA 788  
214 1 Y 1 A TYR 789  ? A TYR 789  
215 1 Y 1 A ILE 790  ? A ILE 790  
216 1 Y 1 A ASN 791  ? A ASN 791  
217 1 Y 1 A LYS 792  ? A LYS 792  
218 1 Y 1 A GLU 793  ? A GLU 793  
219 1 Y 1 A ASP 794  ? A ASP 794  
220 1 Y 1 A GLU 795  ? A GLU 795  
221 1 Y 1 A GLU 796  ? A GLU 796  
222 1 Y 1 A GLY 797  ? A GLY 797  
223 1 Y 1 A GLY 798  ? A GLY 798  
224 1 Y 1 A GLY 799  ? A GLY 799  
225 1 Y 1 A TYR 800  ? A TYR 800  
226 1 Y 1 A TYR 801  ? A TYR 801  
227 1 Y 1 A ASN 802  ? A ASN 802  
228 1 Y 1 A LYS 803  ? A LYS 803  
229 1 Y 1 A ASP 804  ? A ASP 804  
230 1 Y 1 A ASP 805  ? A ASP 805  
231 1 Y 1 A ASN 806  ? A ASN 806  
232 1 Y 1 A LYS 807  ? A LYS 807  
233 1 Y 1 A LYS 808  ? A LYS 808  
234 1 Y 1 A LYS 809  ? A LYS 809  
235 1 Y 1 A ASP 810  ? A ASP 810  
236 1 Y 1 A ILE 811  ? A ILE 811  
237 1 Y 1 A LEU 812  ? A LEU 812  
238 1 Y 1 A GLY 813  ? A GLY 813  
239 1 Y 1 A LYS 814  ? A LYS 814  
240 1 Y 1 A LYS 815  ? A LYS 815  
241 1 Y 1 A GLN 816  ? A GLN 816  
242 1 Y 1 A LYS 817  ? A LYS 817  
243 1 Y 1 A LYS 818  ? A LYS 818  
244 1 Y 1 A ASN 819  ? A ASN 819  
245 1 Y 1 A ASN 820  ? A ASN 820  
246 1 Y 1 A ASN 821  ? A ASN 821  
247 1 Y 1 A ASN 822  ? A ASN 822  
248 1 Y 1 A VAL 823  ? A VAL 823  
249 1 Y 1 A THR 824  ? A THR 824  
250 1 Y 1 A LEU 825  ? A LEU 825  
251 1 Y 1 A VAL 826  ? A VAL 826  
252 1 Y 1 A SER 827  ? A SER 827  
253 1 Y 1 A LYS 828  ? A LYS 828  
254 1 Y 1 A LYS 829  ? A LYS 829  
255 1 Y 1 A GLY 830  ? A GLY 830  
256 1 Y 1 A GLU 831  ? A GLU 831  
257 1 Y 1 A ASP 832  ? A ASP 832  
258 1 Y 1 A ASN 833  ? A ASN 833  
259 1 Y 1 A GLU 834  ? A GLU 834  
260 1 Y 1 A LEU 835  ? A LEU 835  
261 1 Y 1 A ASP 836  ? A ASP 836  
262 1 Y 1 A VAL 837  ? A VAL 837  
263 1 Y 1 A TYR 838  ? A TYR 838  
264 1 Y 1 A TYR 839  ? A TYR 839  
265 1 Y 1 A GLU 840  ? A GLU 840  
266 1 Y 1 A ASN 841  ? A ASN 841  
267 1 Y 1 A LEU 842  ? A LEU 842  
268 1 Y 1 A ASP 843  ? A ASP 843  
269 1 Y 1 A GLU 844  ? A GLU 844  
270 1 Y 1 A LYS 845  ? A LYS 845  
271 1 Y 1 A THR 846  ? A THR 846  
272 1 Y 1 A ASN 847  ? A ASN 847  
273 1 Y 1 A ASP 848  ? A ASP 848  
274 1 Y 1 A LYS 849  ? A LYS 849  
275 1 Y 1 A TYR 850  ? A TYR 850  
276 1 Y 1 A LYS 851  ? A LYS 851  
277 1 Y 1 A MET 852  ? A MET 852  
278 1 Y 1 A ASN 853  ? A ASN 853  
279 1 Y 1 A ASN 854  ? A ASN 854  
280 1 Y 1 A ILE 855  ? A ILE 855  
281 1 Y 1 A LYS 856  ? A LYS 856  
282 1 Y 1 A SER 857  ? A SER 857  
283 1 Y 1 A SER 858  ? A SER 858  
284 1 Y 1 A LYS 859  ? A LYS 859  
285 1 Y 1 A LEU 860  ? A LEU 860  
286 1 Y 1 A LYS 861  ? A LYS 861  
287 1 Y 1 A TYR 862  ? A TYR 862  
288 1 Y 1 A ASP 863  ? A ASP 863  
289 1 Y 1 A ASN 864  ? A ASN 864  
290 1 Y 1 A ASP 865  ? A ASP 865  
291 1 Y 1 A LYS 866  ? A LYS 866  
292 1 Y 1 A LYS 867  ? A LYS 867  
293 1 Y 1 A ASP 868  ? A ASP 868  
294 1 Y 1 A GLY 869  ? A GLY 869  
295 1 Y 1 A ALA 870  ? A ALA 870  
296 1 Y 1 A ILE 871  ? A ILE 871  
297 1 Y 1 A ILE 872  ? A ILE 872  
298 1 Y 1 A ASN 873  ? A ASN 873  
299 1 Y 1 A ASN 874  ? A ASN 874  
300 1 Y 1 A ARG 875  ? A ARG 875  
301 1 Y 1 A PRO 876  ? A PRO 876  
302 1 Y 1 A SER 877  ? A SER 877  
303 1 Y 1 A SER 878  ? A SER 878  
304 1 Y 1 A ASP 879  ? A ASP 879  
305 1 Y 1 A GLU 880  ? A GLU 880  
306 1 Y 1 A GLU 881  ? A GLU 881  
307 1 Y 1 A TYR 882  ? A TYR 882  
308 1 Y 1 A LYS 883  ? A LYS 883  
309 1 Y 1 A GLU 884  ? A GLU 884  
310 1 Y 1 A GLU 885  ? A GLU 885  
311 1 Y 1 A LYS 886  ? A LYS 886  
312 1 Y 1 A ASP 887  ? A ASP 887  
313 1 Y 1 A LYS 888  ? A LYS 888  
314 1 Y 1 A ASN 889  ? A ASN 889  
315 1 Y 1 A LYS 890  ? A LYS 890  
316 1 Y 1 A ILE 891  ? A ILE 891  
317 1 Y 1 A ASN 892  ? A ASN 892  
318 1 Y 1 A ILE 893  ? A ILE 893  
319 1 Y 1 A LEU 894  ? A LEU 894  
320 1 Y 1 A ASN 895  ? A ASN 895  
321 1 Y 1 A ASP 896  ? A ASP 896  
322 1 Y 1 A VAL 897  ? A VAL 897  
323 1 Y 1 A PHE 898  ? A PHE 898  
324 1 Y 1 A ASN 899  ? A ASN 899  
325 1 Y 1 A ASP 900  ? A ASP 900  
326 1 Y 1 A ILE 901  ? A ILE 901  
327 1 Y 1 A THR 902  ? A THR 902  
328 1 Y 1 A ILE 903  ? A ILE 903  
329 1 Y 1 A LYS 904  ? A LYS 904  
330 1 Y 1 A PRO 905  ? A PRO 905  
331 1 Y 1 A ASN 906  ? A ASN 906  
332 1 Y 1 A GLU 907  ? A GLU 907  
333 1 Y 1 A ASN 908  ? A ASN 908  
334 1 Y 1 A ILE 909  ? A ILE 909  
335 1 Y 1 A LEU 910  ? A LEU 910  
336 1 Y 1 A LEU 911  ? A LEU 911  
337 1 Y 1 A ASP 912  ? A ASP 912  
338 1 Y 1 A ARG 913  ? A ARG 913  
339 1 Y 1 A GLY 914  ? A GLY 914  
340 1 Y 1 A ASP 915  ? A ASP 915  
341 1 Y 1 A VAL 916  ? A VAL 916  
342 1 Y 1 A ILE 917  ? A ILE 917  
343 1 Y 1 A LYS 918  ? A LYS 918  
344 1 Y 1 A SER 919  ? A SER 919  
345 1 Y 1 A SER 920  ? A SER 920  
346 1 Y 1 A GLY 921  ? A GLY 921  
347 1 Y 1 A TYR 922  ? A TYR 922  
348 1 Y 1 A ASP 923  ? A ASP 923  
349 1 Y 1 A SER 924  ? A SER 924  
350 1 Y 1 A SER 925  ? A SER 925  
351 1 Y 1 A TYR 926  ? A TYR 926  
352 1 Y 1 A ASN 927  ? A ASN 927  
353 1 Y 1 A ASP 928  ? A ASP 928  
354 1 Y 1 A LEU 929  ? A LEU 929  
355 1 Y 1 A GLN 930  ? A GLN 930  
356 1 Y 1 A SER 931  ? A SER 931  
357 1 Y 1 A SER 932  ? A SER 932  
358 1 Y 1 A SER 933  ? A SER 933  
359 1 Y 1 A LEU 934  ? A LEU 934  
360 1 Y 1 A PRO 935  ? A PRO 935  
361 1 Y 1 A ASN 936  ? A ASN 936  
362 1 Y 1 A PRO 937  ? A PRO 937  
363 1 Y 1 A SER 938  ? A SER 938  
364 1 Y 1 A SER 939  ? A SER 939  
365 1 Y 1 A ASN 940  ? A ASN 940  
366 1 Y 1 A GLU 941  ? A GLU 941  
367 1 Y 1 A VAL 942  ? A VAL 942  
368 1 Y 1 A LEU 943  ? A LEU 943  
369 1 Y 1 A ASN 944  ? A ASN 944  
370 1 Y 1 A LYS 945  ? A LYS 945  
371 1 Y 1 A THR 946  ? A THR 946  
372 1 Y 1 A THR 947  ? A THR 947  
373 1 Y 1 A MET 948  ? A MET 948  
374 1 Y 1 A VAL 949  ? A VAL 949  
375 1 Y 1 A TYR 950  ? A TYR 950  
376 1 Y 1 A ASN 951  ? A ASN 951  
377 1 Y 1 A GLU 952  ? A GLU 952  
378 1 Y 1 A THR 953  ? A THR 953  
379 1 Y 1 A ASP 954  ? A ASP 954  
380 1 Y 1 A LEU 955  ? A LEU 955  
381 1 Y 1 A LYS 956  ? A LYS 956  
382 1 Y 1 A ASP 957  ? A ASP 957  
383 1 Y 1 A ASN 958  ? A ASN 958  
384 1 Y 1 A LYS 959  ? A LYS 959  
385 1 Y 1 A LYS 960  ? A LYS 960  
386 1 Y 1 A GLU 961  ? A GLU 961  
387 1 Y 1 A ILE 962  ? A ILE 962  
388 1 Y 1 A LYS 963  ? A LYS 963  
389 1 Y 1 A SER 964  ? A SER 964  
390 1 Y 1 A SER 965  ? A SER 965  
391 1 Y 1 A LYS 966  ? A LYS 966  
392 1 Y 1 A LYS 967  ? A LYS 967  
393 1 Y 1 A ASN 968  ? A ASN 968  
394 1 Y 1 A VAL 969  ? A VAL 969  
395 1 Y 1 A LYS 970  ? A LYS 970  
396 1 Y 1 A ASP 971  ? A ASP 971  
397 1 Y 1 A ILE 972  ? A ILE 972  
398 1 Y 1 A LYS 973  ? A LYS 973  
399 1 Y 1 A LYS 974  ? A LYS 974  
400 1 Y 1 A SER 975  ? A SER 975  
401 1 Y 1 A ASP 976  ? A ASP 976  
402 1 Y 1 A MET 977  ? A MET 977  
403 1 Y 1 A ILE 978  ? A ILE 978  
404 1 Y 1 A HIS 979  ? A HIS 979  
405 1 Y 1 A ASP 980  ? A ASP 980  
406 1 Y 1 A ASP 981  ? A ASP 981  
407 1 Y 1 A THR 982  ? A THR 982  
408 1 Y 1 A TYR 983  ? A TYR 983  
409 1 Y 1 A ASP 984  ? A ASP 984  
410 1 Y 1 A ILE 985  ? A ILE 985  
411 1 Y 1 A ILE 986  ? A ILE 986  
412 1 Y 1 A ASN 987  ? A ASN 987  
413 1 Y 1 A SER 988  ? A SER 988  
414 1 Y 1 A ASN 989  ? A ASN 989  
415 1 Y 1 A ASN 990  ? A ASN 990  
416 1 Y 1 A LYS 991  ? A LYS 991  
417 1 Y 1 A ASN 992  ? A ASN 992  
418 1 Y 1 A ILE 993  ? A ILE 993  
419 1 Y 1 A LEU 994  ? A LEU 994  
420 1 Y 1 A LEU 995  ? A LEU 995  
421 1 Y 1 A SER 996  ? A SER 996  
422 1 Y 1 A SER 997  ? A SER 997  
423 1 Y 1 A ASN 998  ? A ASN 998  
424 1 Y 1 A GLU 999  ? A GLU 999  
425 1 Y 1 A ILE 1000 ? A ILE 1000 
426 1 Y 1 A ASN 1001 ? A ASN 1001 
427 1 Y 1 A ASN 1002 ? A ASN 1002 
428 1 Y 1 A ASN 1003 ? A ASN 1003 
429 1 Y 1 A SER 1004 ? A SER 1004 
430 1 Y 1 A ASN 1005 ? A ASN 1005 
431 1 Y 1 A ASN 1006 ? A ASN 1006 
432 1 Y 1 A THR 1007 ? A THR 1007 
433 1 Y 1 A ASN 1008 ? A ASN 1008 
434 1 Y 1 A LYS 1009 ? A LYS 1009 
435 1 Y 1 A PHE 1010 ? A PHE 1010 
436 1 Y 1 A ASN 1011 ? A ASN 1011 
437 1 Y 1 A ASN 1012 ? A ASN 1012 
438 1 Y 1 A ASN 1013 ? A ASN 1013 
439 1 Y 1 A SER 1014 ? A SER 1014 
440 1 Y 1 A THR 1015 ? A THR 1015 
441 1 Y 1 A GLU 1016 ? A GLU 1016 
442 1 Y 1 A LEU 1017 ? A LEU 1017 
443 1 Y 1 A ALA 1018 ? A ALA 1018 
444 1 Y 1 A THR 1019 ? A THR 1019 
445 1 Y 1 A LYS 1020 ? A LYS 1020 
446 1 Y 1 A ASP 1021 ? A ASP 1021 
447 1 Y 1 A THR 1022 ? A THR 1022 
448 1 Y 1 A GLN 1023 ? A GLN 1023 
449 1 Y 1 A GLN 1024 ? A GLN 1024 
450 1 Y 1 A PHE 1025 ? A PHE 1025 
451 1 Y 1 A ILE 1026 ? A ILE 1026 
452 1 Y 1 A ASN 1027 ? A ASN 1027 
453 1 Y 1 A GLY 1028 ? A GLY 1028 
454 1 Y 1 A HIS 1029 ? A HIS 1029 
455 1 Y 1 A ASP 1030 ? A ASP 1030 
456 1 Y 1 A LYS 1031 ? A LYS 1031 
457 1 Y 1 A ASN 1032 ? A ASN 1032 
458 1 Y 1 A ILE 1033 ? A ILE 1033 
459 1 Y 1 A TYR 1034 ? A TYR 1034 
460 1 Y 1 A LEU 1035 ? A LEU 1035 
461 1 Y 1 A LEU 1036 ? A LEU 1036 
462 1 Y 1 A SER 1037 ? A SER 1037 
463 1 Y 1 A SER 1038 ? A SER 1038 
464 1 Y 1 A HIS 1039 ? A HIS 1039 
465 1 Y 1 A ASP 1040 ? A ASP 1040 
466 1 Y 1 A ASN 1041 ? A ASN 1041 
467 1 Y 1 A ALA 1042 ? A ALA 1042 
468 1 Y 1 A LEU 1043 ? A LEU 1043 
469 1 Y 1 A PHE 1044 ? A PHE 1044 
470 1 Y 1 A TYR 1045 ? A TYR 1045 
471 1 Y 1 A LYS 1046 ? A LYS 1046 
472 1 Y 1 A ASN 1152 ? A ASN 1152 
473 1 Y 1 A THR 1153 ? A THR 1153 
474 1 Y 1 A LYS 1154 ? A LYS 1154 
475 1 Y 1 A GLU 1155 ? A GLU 1155 
476 1 Y 1 A ALA 1156 ? A ALA 1156 
477 1 Y 1 A ALA 1157 ? A ALA 1157 
478 1 Y 1 A SER 1158 ? A SER 1158 
479 1 Y 1 A SER 1159 ? A SER 1159 
480 1 Y 1 A PHE 1160 ? A PHE 1160 
# 
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  
CLR C1   C N N 74  
CLR C2   C N N 75  
CLR C3   C N S 76  
CLR C4   C N N 77  
CLR C5   C N N 78  
CLR C6   C N N 79  
CLR C7   C N N 80  
CLR C8   C N S 81  
CLR C9   C N S 82  
CLR C10  C N R 83  
CLR C11  C N N 84  
CLR C12  C N N 85  
CLR C13  C N R 86  
CLR C14  C N S 87  
CLR C15  C N N 88  
CLR C16  C N N 89  
CLR C17  C N R 90  
CLR C18  C N N 91  
CLR C19  C N N 92  
CLR C20  C N R 93  
CLR C21  C N N 94  
CLR C22  C N N 95  
CLR C23  C N N 96  
CLR C24  C N N 97  
CLR C25  C N N 98  
CLR C26  C N N 99  
CLR C27  C N N 100 
CLR O1   O N N 101 
CLR H11  H N N 102 
CLR H12  H N N 103 
CLR H21  H N N 104 
CLR H22  H N N 105 
CLR H3   H N N 106 
CLR H41  H N N 107 
CLR H42  H N N 108 
CLR H6   H N N 109 
CLR H71  H N N 110 
CLR H72  H N N 111 
CLR H8   H N N 112 
CLR H9   H N N 113 
CLR H111 H N N 114 
CLR H112 H N N 115 
CLR H121 H N N 116 
CLR H122 H N N 117 
CLR H14  H N N 118 
CLR H151 H N N 119 
CLR H152 H N N 120 
CLR H161 H N N 121 
CLR H162 H N N 122 
CLR H17  H N N 123 
CLR H181 H N N 124 
CLR H182 H N N 125 
CLR H183 H N N 126 
CLR H191 H N N 127 
CLR H192 H N N 128 
CLR H193 H N N 129 
CLR H20  H N N 130 
CLR H211 H N N 131 
CLR H212 H N N 132 
CLR H213 H N N 133 
CLR H221 H N N 134 
CLR H222 H N N 135 
CLR H231 H N N 136 
CLR H232 H N N 137 
CLR H241 H N N 138 
CLR H242 H N N 139 
CLR H25  H N N 140 
CLR H261 H N N 141 
CLR H262 H N N 142 
CLR H263 H N N 143 
CLR H271 H N N 144 
CLR H272 H N N 145 
CLR H273 H N N 146 
CLR H1   H N N 147 
CYS N    N N N 148 
CYS CA   C N R 149 
CYS C    C N N 150 
CYS O    O N N 151 
CYS CB   C N N 152 
CYS SG   S N N 153 
CYS OXT  O N N 154 
CYS H    H N N 155 
CYS H2   H N N 156 
CYS HA   H N N 157 
CYS HB2  H N N 158 
CYS HB3  H N N 159 
CYS HG   H N N 160 
CYS HXT  H N N 161 
GLN N    N N N 162 
GLN CA   C N S 163 
GLN C    C N N 164 
GLN O    O N N 165 
GLN CB   C N N 166 
GLN CG   C N N 167 
GLN CD   C N N 168 
GLN OE1  O N N 169 
GLN NE2  N N N 170 
GLN OXT  O N N 171 
GLN H    H N N 172 
GLN H2   H N N 173 
GLN HA   H N N 174 
GLN HB2  H N N 175 
GLN HB3  H N N 176 
GLN HG2  H N N 177 
GLN HG3  H N N 178 
GLN HE21 H N N 179 
GLN HE22 H N N 180 
GLN HXT  H N N 181 
GLU N    N N N 182 
GLU CA   C N S 183 
GLU C    C N N 184 
GLU O    O N N 185 
GLU CB   C N N 186 
GLU CG   C N N 187 
GLU CD   C N N 188 
GLU OE1  O N N 189 
GLU OE2  O N N 190 
GLU OXT  O N N 191 
GLU H    H N N 192 
GLU H2   H N N 193 
GLU HA   H N N 194 
GLU HB2  H N N 195 
GLU HB3  H N N 196 
GLU HG2  H N N 197 
GLU HG3  H N N 198 
GLU HE2  H N N 199 
GLU HXT  H N N 200 
GLY N    N N N 201 
GLY CA   C N N 202 
GLY C    C N N 203 
GLY O    O N N 204 
GLY OXT  O N N 205 
GLY H    H N N 206 
GLY H2   H N N 207 
GLY HA2  H N N 208 
GLY HA3  H N N 209 
GLY HXT  H N N 210 
HIS N    N N N 211 
HIS CA   C N S 212 
HIS C    C N N 213 
HIS O    O N N 214 
HIS CB   C N N 215 
HIS CG   C Y N 216 
HIS ND1  N Y N 217 
HIS CD2  C Y N 218 
HIS CE1  C Y N 219 
HIS NE2  N Y N 220 
HIS OXT  O N N 221 
HIS H    H N N 222 
HIS H2   H N N 223 
HIS HA   H N N 224 
HIS HB2  H N N 225 
HIS HB3  H N N 226 
HIS HD1  H N N 227 
HIS HD2  H N N 228 
HIS HE1  H N N 229 
HIS HE2  H N N 230 
HIS HXT  H N N 231 
ILE N    N N N 232 
ILE CA   C N S 233 
ILE C    C N N 234 
ILE O    O N N 235 
ILE CB   C N S 236 
ILE CG1  C N N 237 
ILE CG2  C N N 238 
ILE CD1  C N N 239 
ILE OXT  O N N 240 
ILE H    H N N 241 
ILE H2   H N N 242 
ILE HA   H N N 243 
ILE HB   H N N 244 
ILE HG12 H N N 245 
ILE HG13 H N N 246 
ILE HG21 H N N 247 
ILE HG22 H N N 248 
ILE HG23 H N N 249 
ILE HD11 H N N 250 
ILE HD12 H N N 251 
ILE HD13 H N N 252 
ILE HXT  H N N 253 
LEU N    N N N 254 
LEU CA   C N S 255 
LEU C    C N N 256 
LEU O    O N N 257 
LEU CB   C N N 258 
LEU CG   C N N 259 
LEU CD1  C N N 260 
LEU CD2  C N N 261 
LEU OXT  O N N 262 
LEU H    H N N 263 
LEU H2   H N N 264 
LEU HA   H N N 265 
LEU HB2  H N N 266 
LEU HB3  H N N 267 
LEU HG   H N N 268 
LEU HD11 H N N 269 
LEU HD12 H N N 270 
LEU HD13 H N N 271 
LEU HD21 H N N 272 
LEU HD22 H N N 273 
LEU HD23 H N N 274 
LEU HXT  H N N 275 
LYS N    N N N 276 
LYS CA   C N S 277 
LYS C    C N N 278 
LYS O    O N N 279 
LYS CB   C N N 280 
LYS CG   C N N 281 
LYS CD   C N N 282 
LYS CE   C N N 283 
LYS NZ   N N N 284 
LYS OXT  O N N 285 
LYS H    H N N 286 
LYS H2   H N N 287 
LYS HA   H N N 288 
LYS HB2  H N N 289 
LYS HB3  H N N 290 
LYS HG2  H N N 291 
LYS HG3  H N N 292 
LYS HD2  H N N 293 
LYS HD3  H N N 294 
LYS HE2  H N N 295 
LYS HE3  H N N 296 
LYS HZ1  H N N 297 
LYS HZ2  H N N 298 
LYS HZ3  H N N 299 
LYS HXT  H N N 300 
MET N    N N N 301 
MET CA   C N S 302 
MET C    C N N 303 
MET O    O N N 304 
MET CB   C N N 305 
MET CG   C N N 306 
MET SD   S N N 307 
MET CE   C N N 308 
MET OXT  O N N 309 
MET H    H N N 310 
MET H2   H N N 311 
MET HA   H N N 312 
MET HB2  H N N 313 
MET HB3  H N N 314 
MET HG2  H N N 315 
MET HG3  H N N 316 
MET HE1  H N N 317 
MET HE2  H N N 318 
MET HE3  H N N 319 
MET HXT  H N N 320 
NAG C1   C N R 321 
NAG C2   C N R 322 
NAG C3   C N R 323 
NAG C4   C N S 324 
NAG C5   C N R 325 
NAG C6   C N N 326 
NAG C7   C N N 327 
NAG C8   C N N 328 
NAG N2   N N N 329 
NAG O1   O N N 330 
NAG O3   O N N 331 
NAG O4   O N N 332 
NAG O5   O N N 333 
NAG O6   O N N 334 
NAG O7   O N N 335 
NAG H1   H N N 336 
NAG H2   H N N 337 
NAG H3   H N N 338 
NAG H4   H N N 339 
NAG H5   H N N 340 
NAG H61  H N N 341 
NAG H62  H N N 342 
NAG H81  H N N 343 
NAG H82  H N N 344 
NAG H83  H N N 345 
NAG HN2  H N N 346 
NAG HO1  H N N 347 
NAG HO3  H N N 348 
NAG HO4  H N N 349 
NAG HO6  H N N 350 
PHE N    N N N 351 
PHE CA   C N S 352 
PHE C    C N N 353 
PHE O    O N N 354 
PHE CB   C N N 355 
PHE CG   C Y N 356 
PHE CD1  C Y N 357 
PHE CD2  C Y N 358 
PHE CE1  C Y N 359 
PHE CE2  C Y N 360 
PHE CZ   C Y N 361 
PHE OXT  O N N 362 
PHE H    H N N 363 
PHE H2   H N N 364 
PHE HA   H N N 365 
PHE HB2  H N N 366 
PHE HB3  H N N 367 
PHE HD1  H N N 368 
PHE HD2  H N N 369 
PHE HE1  H N N 370 
PHE HE2  H N N 371 
PHE HZ   H N N 372 
PHE HXT  H N N 373 
PRO N    N N N 374 
PRO CA   C N S 375 
PRO C    C N N 376 
PRO O    O N N 377 
PRO CB   C N N 378 
PRO CG   C N N 379 
PRO CD   C N N 380 
PRO OXT  O N N 381 
PRO H    H N N 382 
PRO HA   H N N 383 
PRO HB2  H N N 384 
PRO HB3  H N N 385 
PRO HG2  H N N 386 
PRO HG3  H N N 387 
PRO HD2  H N N 388 
PRO HD3  H N N 389 
PRO HXT  H N N 390 
SER N    N N N 391 
SER CA   C N S 392 
SER C    C N N 393 
SER O    O N N 394 
SER CB   C N N 395 
SER OG   O N N 396 
SER OXT  O N N 397 
SER H    H N N 398 
SER H2   H N N 399 
SER HA   H N N 400 
SER HB2  H N N 401 
SER HB3  H N N 402 
SER HG   H N N 403 
SER HXT  H N N 404 
THR N    N N N 405 
THR CA   C N S 406 
THR C    C N N 407 
THR O    O N N 408 
THR CB   C N R 409 
THR OG1  O N N 410 
THR CG2  C N N 411 
THR OXT  O N N 412 
THR H    H N N 413 
THR H2   H N N 414 
THR HA   H N N 415 
THR HB   H N N 416 
THR HG1  H N N 417 
THR HG21 H N N 418 
THR HG22 H N N 419 
THR HG23 H N N 420 
THR HXT  H N N 421 
TRP N    N N N 422 
TRP CA   C N S 423 
TRP C    C N N 424 
TRP O    O N N 425 
TRP CB   C N N 426 
TRP CG   C Y N 427 
TRP CD1  C Y N 428 
TRP CD2  C Y N 429 
TRP NE1  N Y N 430 
TRP CE2  C Y N 431 
TRP CE3  C Y N 432 
TRP CZ2  C Y N 433 
TRP CZ3  C Y N 434 
TRP CH2  C Y N 435 
TRP OXT  O N N 436 
TRP H    H N N 437 
TRP H2   H N N 438 
TRP HA   H N N 439 
TRP HB2  H N N 440 
TRP HB3  H N N 441 
TRP HD1  H N N 442 
TRP HE1  H N N 443 
TRP HE3  H N N 444 
TRP HZ2  H N N 445 
TRP HZ3  H N N 446 
TRP HH2  H N N 447 
TRP HXT  H N N 448 
TYR N    N N N 449 
TYR CA   C N S 450 
TYR C    C N N 451 
TYR O    O N N 452 
TYR CB   C N N 453 
TYR CG   C Y N 454 
TYR CD1  C Y N 455 
TYR CD2  C Y N 456 
TYR CE1  C Y N 457 
TYR CE2  C Y N 458 
TYR CZ   C Y N 459 
TYR OH   O N N 460 
TYR OXT  O N N 461 
TYR H    H N N 462 
TYR H2   H N N 463 
TYR HA   H N N 464 
TYR HB2  H N N 465 
TYR HB3  H N N 466 
TYR HD1  H N N 467 
TYR HD2  H N N 468 
TYR HE1  H N N 469 
TYR HE2  H N N 470 
TYR HH   H N N 471 
TYR HXT  H N N 472 
VAL N    N N N 473 
VAL CA   C N S 474 
VAL C    C N N 475 
VAL O    O N N 476 
VAL CB   C N N 477 
VAL CG1  C N N 478 
VAL CG2  C N N 479 
VAL OXT  O N N 480 
VAL H    H N N 481 
VAL H2   H N N 482 
VAL HA   H N N 483 
VAL HB   H N N 484 
VAL HG11 H N N 485 
VAL HG12 H N N 486 
VAL HG13 H N N 487 
VAL HG21 H N N 488 
VAL HG22 H N N 489 
VAL HG23 H N N 490 
VAL HXT  H N N 491 
Y6F C10  C Y N 492 
Y6F C12  C Y N 493 
Y6F C13  C Y N 494 
Y6F C14  C Y N 495 
Y6F C16  C N N 496 
Y6F C17  C Y N 497 
Y6F C18  C N N 498 
Y6F C19  C Y N 499 
Y6F C21  C Y N 500 
Y6F C22  C Y N 501 
Y6F C24  C N N 502 
Y6F C03  C Y N 503 
Y6F C04  C Y N 504 
Y6F C05  C Y N 505 
Y6F C06  C Y N 506 
Y6F C07  C Y N 507 
Y6F C08  C Y N 508 
Y6F C15  C Y N 509 
Y6F C25  C N N 510 
Y6F C26  C N N 511 
Y6F C27  C N N 512 
Y6F N11  N N N 513 
Y6F N20  N Y N 514 
Y6F N23  N N N 515 
Y6F O01  O N N 516 
Y6F O28  O N N 517 
Y6F S02  S N N 518 
Y6F S09  S Y N 519 
Y6F H1   H N N 520 
Y6F H2   H N N 521 
Y6F H3   H N N 522 
Y6F H4   H N N 523 
Y6F H5   H N N 524 
Y6F H6   H N N 525 
Y6F H7   H N N 526 
Y6F H8   H N N 527 
Y6F H9   H N N 528 
Y6F H10  H N N 529 
Y6F H11  H N N 530 
Y6F H12  H N N 531 
Y6F H13  H N N 532 
Y6F H14  H N N 533 
Y6F H15  H N N 534 
Y6F H16  H N N 535 
Y6F H17  H N N 536 
Y6F H18  H N N 537 
Y6F H19  H N N 538 
Y6F H20  H N N 539 
Y6F H21  H N N 540 
Y6F H22  H N N 541 
Y6F H23  H N N 542 
Y6F H24  H N N 543 
Y6F H25  H N N 544 
# 
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  
CLR C1  C2   sing N N 70  
CLR C1  C10  sing N N 71  
CLR C1  H11  sing N N 72  
CLR C1  H12  sing N N 73  
CLR C2  C3   sing N N 74  
CLR C2  H21  sing N N 75  
CLR C2  H22  sing N N 76  
CLR C3  C4   sing N N 77  
CLR C3  O1   sing N N 78  
CLR C3  H3   sing N N 79  
CLR C4  C5   sing N N 80  
CLR C4  H41  sing N N 81  
CLR C4  H42  sing N N 82  
CLR C5  C6   doub N N 83  
CLR C5  C10  sing N N 84  
CLR C6  C7   sing N N 85  
CLR C6  H6   sing N N 86  
CLR C7  C8   sing N N 87  
CLR C7  H71  sing N N 88  
CLR C7  H72  sing N N 89  
CLR C8  C9   sing N N 90  
CLR C8  C14  sing N N 91  
CLR C8  H8   sing N N 92  
CLR C9  C10  sing N N 93  
CLR C9  C11  sing N N 94  
CLR C9  H9   sing N N 95  
CLR C10 C19  sing N N 96  
CLR C11 C12  sing N N 97  
CLR C11 H111 sing N N 98  
CLR C11 H112 sing N N 99  
CLR C12 C13  sing N N 100 
CLR C12 H121 sing N N 101 
CLR C12 H122 sing N N 102 
CLR C13 C14  sing N N 103 
CLR C13 C17  sing N N 104 
CLR C13 C18  sing N N 105 
CLR C14 C15  sing N N 106 
CLR C14 H14  sing N N 107 
CLR C15 C16  sing N N 108 
CLR C15 H151 sing N N 109 
CLR C15 H152 sing N N 110 
CLR C16 C17  sing N N 111 
CLR C16 H161 sing N N 112 
CLR C16 H162 sing N N 113 
CLR C17 C20  sing N N 114 
CLR C17 H17  sing N N 115 
CLR C18 H181 sing N N 116 
CLR C18 H182 sing N N 117 
CLR C18 H183 sing N N 118 
CLR C19 H191 sing N N 119 
CLR C19 H192 sing N N 120 
CLR C19 H193 sing N N 121 
CLR C20 C21  sing N N 122 
CLR C20 C22  sing N N 123 
CLR C20 H20  sing N N 124 
CLR C21 H211 sing N N 125 
CLR C21 H212 sing N N 126 
CLR C21 H213 sing N N 127 
CLR C22 C23  sing N N 128 
CLR C22 H221 sing N N 129 
CLR C22 H222 sing N N 130 
CLR C23 C24  sing N N 131 
CLR C23 H231 sing N N 132 
CLR C23 H232 sing N N 133 
CLR C24 C25  sing N N 134 
CLR C24 H241 sing N N 135 
CLR C24 H242 sing N N 136 
CLR C25 C26  sing N N 137 
CLR C25 C27  sing N N 138 
CLR C25 H25  sing N N 139 
CLR C26 H261 sing N N 140 
CLR C26 H262 sing N N 141 
CLR C26 H263 sing N N 142 
CLR C27 H271 sing N N 143 
CLR C27 H272 sing N N 144 
CLR C27 H273 sing N N 145 
CLR O1  H1   sing N N 146 
CYS N   CA   sing N N 147 
CYS N   H    sing N N 148 
CYS N   H2   sing N N 149 
CYS CA  C    sing N N 150 
CYS CA  CB   sing N N 151 
CYS CA  HA   sing N N 152 
CYS C   O    doub N N 153 
CYS C   OXT  sing N N 154 
CYS CB  SG   sing N N 155 
CYS CB  HB2  sing N N 156 
CYS CB  HB3  sing N N 157 
CYS SG  HG   sing N N 158 
CYS OXT HXT  sing N N 159 
GLN N   CA   sing N N 160 
GLN N   H    sing N N 161 
GLN N   H2   sing N N 162 
GLN CA  C    sing N N 163 
GLN CA  CB   sing N N 164 
GLN CA  HA   sing N N 165 
GLN C   O    doub N N 166 
GLN C   OXT  sing N N 167 
GLN CB  CG   sing N N 168 
GLN CB  HB2  sing N N 169 
GLN CB  HB3  sing N N 170 
GLN CG  CD   sing N N 171 
GLN CG  HG2  sing N N 172 
GLN CG  HG3  sing N N 173 
GLN CD  OE1  doub N N 174 
GLN CD  NE2  sing N N 175 
GLN NE2 HE21 sing N N 176 
GLN NE2 HE22 sing N N 177 
GLN OXT HXT  sing N N 178 
GLU N   CA   sing N N 179 
GLU N   H    sing N N 180 
GLU N   H2   sing N N 181 
GLU CA  C    sing N N 182 
GLU CA  CB   sing N N 183 
GLU CA  HA   sing N N 184 
GLU C   O    doub N N 185 
GLU C   OXT  sing N N 186 
GLU CB  CG   sing N N 187 
GLU CB  HB2  sing N N 188 
GLU CB  HB3  sing N N 189 
GLU CG  CD   sing N N 190 
GLU CG  HG2  sing N N 191 
GLU CG  HG3  sing N N 192 
GLU CD  OE1  doub N N 193 
GLU CD  OE2  sing N N 194 
GLU OE2 HE2  sing N N 195 
GLU OXT HXT  sing N N 196 
GLY N   CA   sing N N 197 
GLY N   H    sing N N 198 
GLY N   H2   sing N N 199 
GLY CA  C    sing N N 200 
GLY CA  HA2  sing N N 201 
GLY CA  HA3  sing N N 202 
GLY C   O    doub N N 203 
GLY C   OXT  sing N N 204 
GLY OXT HXT  sing N N 205 
HIS N   CA   sing N N 206 
HIS N   H    sing N N 207 
HIS N   H2   sing N N 208 
HIS CA  C    sing N N 209 
HIS CA  CB   sing N N 210 
HIS CA  HA   sing N N 211 
HIS C   O    doub N N 212 
HIS C   OXT  sing N N 213 
HIS CB  CG   sing N N 214 
HIS CB  HB2  sing N N 215 
HIS CB  HB3  sing N N 216 
HIS CG  ND1  sing Y N 217 
HIS CG  CD2  doub Y N 218 
HIS ND1 CE1  doub Y N 219 
HIS ND1 HD1  sing N N 220 
HIS CD2 NE2  sing Y N 221 
HIS CD2 HD2  sing N N 222 
HIS CE1 NE2  sing Y N 223 
HIS CE1 HE1  sing N N 224 
HIS NE2 HE2  sing N N 225 
HIS OXT HXT  sing N N 226 
ILE N   CA   sing N N 227 
ILE N   H    sing N N 228 
ILE N   H2   sing N N 229 
ILE CA  C    sing N N 230 
ILE CA  CB   sing N N 231 
ILE CA  HA   sing N N 232 
ILE C   O    doub N N 233 
ILE C   OXT  sing N N 234 
ILE CB  CG1  sing N N 235 
ILE CB  CG2  sing N N 236 
ILE CB  HB   sing N N 237 
ILE CG1 CD1  sing N N 238 
ILE CG1 HG12 sing N N 239 
ILE CG1 HG13 sing N N 240 
ILE CG2 HG21 sing N N 241 
ILE CG2 HG22 sing N N 242 
ILE CG2 HG23 sing N N 243 
ILE CD1 HD11 sing N N 244 
ILE CD1 HD12 sing N N 245 
ILE CD1 HD13 sing N N 246 
ILE OXT HXT  sing N N 247 
LEU N   CA   sing N N 248 
LEU N   H    sing N N 249 
LEU N   H2   sing N N 250 
LEU CA  C    sing N N 251 
LEU CA  CB   sing N N 252 
LEU CA  HA   sing N N 253 
LEU C   O    doub N N 254 
LEU C   OXT  sing N N 255 
LEU CB  CG   sing N N 256 
LEU CB  HB2  sing N N 257 
LEU CB  HB3  sing N N 258 
LEU CG  CD1  sing N N 259 
LEU CG  CD2  sing N N 260 
LEU CG  HG   sing N N 261 
LEU CD1 HD11 sing N N 262 
LEU CD1 HD12 sing N N 263 
LEU CD1 HD13 sing N N 264 
LEU CD2 HD21 sing N N 265 
LEU CD2 HD22 sing N N 266 
LEU CD2 HD23 sing N N 267 
LEU OXT HXT  sing N N 268 
LYS N   CA   sing N N 269 
LYS N   H    sing N N 270 
LYS N   H2   sing N N 271 
LYS CA  C    sing N N 272 
LYS CA  CB   sing N N 273 
LYS CA  HA   sing N N 274 
LYS C   O    doub N N 275 
LYS C   OXT  sing N N 276 
LYS CB  CG   sing N N 277 
LYS CB  HB2  sing N N 278 
LYS CB  HB3  sing N N 279 
LYS CG  CD   sing N N 280 
LYS CG  HG2  sing N N 281 
LYS CG  HG3  sing N N 282 
LYS CD  CE   sing N N 283 
LYS CD  HD2  sing N N 284 
LYS CD  HD3  sing N N 285 
LYS CE  NZ   sing N N 286 
LYS CE  HE2  sing N N 287 
LYS CE  HE3  sing N N 288 
LYS NZ  HZ1  sing N N 289 
LYS NZ  HZ2  sing N N 290 
LYS NZ  HZ3  sing N N 291 
LYS OXT HXT  sing N N 292 
MET N   CA   sing N N 293 
MET N   H    sing N N 294 
MET N   H2   sing N N 295 
MET CA  C    sing N N 296 
MET CA  CB   sing N N 297 
MET CA  HA   sing N N 298 
MET C   O    doub N N 299 
MET C   OXT  sing N N 300 
MET CB  CG   sing N N 301 
MET CB  HB2  sing N N 302 
MET CB  HB3  sing N N 303 
MET CG  SD   sing N N 304 
MET CG  HG2  sing N N 305 
MET CG  HG3  sing N N 306 
MET SD  CE   sing N N 307 
MET CE  HE1  sing N N 308 
MET CE  HE2  sing N N 309 
MET CE  HE3  sing N N 310 
MET OXT HXT  sing N N 311 
NAG C1  C2   sing N N 312 
NAG C1  O1   sing N N 313 
NAG C1  O5   sing N N 314 
NAG C1  H1   sing N N 315 
NAG C2  C3   sing N N 316 
NAG C2  N2   sing N N 317 
NAG C2  H2   sing N N 318 
NAG C3  C4   sing N N 319 
NAG C3  O3   sing N N 320 
NAG C3  H3   sing N N 321 
NAG C4  C5   sing N N 322 
NAG C4  O4   sing N N 323 
NAG C4  H4   sing N N 324 
NAG C5  C6   sing N N 325 
NAG C5  O5   sing N N 326 
NAG C5  H5   sing N N 327 
NAG C6  O6   sing N N 328 
NAG C6  H61  sing N N 329 
NAG C6  H62  sing N N 330 
NAG C7  C8   sing N N 331 
NAG C7  N2   sing N N 332 
NAG C7  O7   doub N N 333 
NAG C8  H81  sing N N 334 
NAG C8  H82  sing N N 335 
NAG C8  H83  sing N N 336 
NAG N2  HN2  sing N N 337 
NAG O1  HO1  sing N N 338 
NAG O3  HO3  sing N N 339 
NAG O4  HO4  sing N N 340 
NAG O6  HO6  sing N N 341 
PHE N   CA   sing N N 342 
PHE N   H    sing N N 343 
PHE N   H2   sing N N 344 
PHE CA  C    sing N N 345 
PHE CA  CB   sing N N 346 
PHE CA  HA   sing N N 347 
PHE C   O    doub N N 348 
PHE C   OXT  sing N N 349 
PHE CB  CG   sing N N 350 
PHE CB  HB2  sing N N 351 
PHE CB  HB3  sing N N 352 
PHE CG  CD1  doub Y N 353 
PHE CG  CD2  sing Y N 354 
PHE CD1 CE1  sing Y N 355 
PHE CD1 HD1  sing N N 356 
PHE CD2 CE2  doub Y N 357 
PHE CD2 HD2  sing N N 358 
PHE CE1 CZ   doub Y N 359 
PHE CE1 HE1  sing N N 360 
PHE CE2 CZ   sing Y N 361 
PHE CE2 HE2  sing N N 362 
PHE CZ  HZ   sing N N 363 
PHE OXT HXT  sing N N 364 
PRO N   CA   sing N N 365 
PRO N   CD   sing N N 366 
PRO N   H    sing N N 367 
PRO CA  C    sing N N 368 
PRO CA  CB   sing N N 369 
PRO CA  HA   sing N N 370 
PRO C   O    doub N N 371 
PRO C   OXT  sing N N 372 
PRO CB  CG   sing N N 373 
PRO CB  HB2  sing N N 374 
PRO CB  HB3  sing N N 375 
PRO CG  CD   sing N N 376 
PRO CG  HG2  sing N N 377 
PRO CG  HG3  sing N N 378 
PRO CD  HD2  sing N N 379 
PRO CD  HD3  sing N N 380 
PRO OXT HXT  sing N N 381 
SER N   CA   sing N N 382 
SER N   H    sing N N 383 
SER N   H2   sing N N 384 
SER CA  C    sing N N 385 
SER CA  CB   sing N N 386 
SER CA  HA   sing N N 387 
SER C   O    doub N N 388 
SER C   OXT  sing N N 389 
SER CB  OG   sing N N 390 
SER CB  HB2  sing N N 391 
SER CB  HB3  sing N N 392 
SER OG  HG   sing N N 393 
SER OXT HXT  sing N N 394 
THR N   CA   sing N N 395 
THR N   H    sing N N 396 
THR N   H2   sing N N 397 
THR CA  C    sing N N 398 
THR CA  CB   sing N N 399 
THR CA  HA   sing N N 400 
THR C   O    doub N N 401 
THR C   OXT  sing N N 402 
THR CB  OG1  sing N N 403 
THR CB  CG2  sing N N 404 
THR CB  HB   sing N N 405 
THR OG1 HG1  sing N N 406 
THR CG2 HG21 sing N N 407 
THR CG2 HG22 sing N N 408 
THR CG2 HG23 sing N N 409 
THR OXT HXT  sing N N 410 
TRP N   CA   sing N N 411 
TRP N   H    sing N N 412 
TRP N   H2   sing N N 413 
TRP CA  C    sing N N 414 
TRP CA  CB   sing N N 415 
TRP CA  HA   sing N N 416 
TRP C   O    doub N N 417 
TRP C   OXT  sing N N 418 
TRP CB  CG   sing N N 419 
TRP CB  HB2  sing N N 420 
TRP CB  HB3  sing N N 421 
TRP CG  CD1  doub Y N 422 
TRP CG  CD2  sing Y N 423 
TRP CD1 NE1  sing Y N 424 
TRP CD1 HD1  sing N N 425 
TRP CD2 CE2  doub Y N 426 
TRP CD2 CE3  sing Y N 427 
TRP NE1 CE2  sing Y N 428 
TRP NE1 HE1  sing N N 429 
TRP CE2 CZ2  sing Y N 430 
TRP CE3 CZ3  doub Y N 431 
TRP CE3 HE3  sing N N 432 
TRP CZ2 CH2  doub Y N 433 
TRP CZ2 HZ2  sing N N 434 
TRP CZ3 CH2  sing Y N 435 
TRP CZ3 HZ3  sing N N 436 
TRP CH2 HH2  sing N N 437 
TRP OXT HXT  sing N N 438 
TYR N   CA   sing N N 439 
TYR N   H    sing N N 440 
TYR N   H2   sing N N 441 
TYR CA  C    sing N N 442 
TYR CA  CB   sing N N 443 
TYR CA  HA   sing N N 444 
TYR C   O    doub N N 445 
TYR C   OXT  sing N N 446 
TYR CB  CG   sing N N 447 
TYR CB  HB2  sing N N 448 
TYR CB  HB3  sing N N 449 
TYR CG  CD1  doub Y N 450 
TYR CG  CD2  sing Y N 451 
TYR CD1 CE1  sing Y N 452 
TYR CD1 HD1  sing N N 453 
TYR CD2 CE2  doub Y N 454 
TYR CD2 HD2  sing N N 455 
TYR CE1 CZ   doub Y N 456 
TYR CE1 HE1  sing N N 457 
TYR CE2 CZ   sing Y N 458 
TYR CE2 HE2  sing N N 459 
TYR CZ  OH   sing N N 460 
TYR OH  HH   sing N N 461 
TYR OXT HXT  sing N N 462 
VAL N   CA   sing N N 463 
VAL N   H    sing N N 464 
VAL N   H2   sing N N 465 
VAL CA  C    sing N N 466 
VAL CA  CB   sing N N 467 
VAL CA  HA   sing N N 468 
VAL C   O    doub N N 469 
VAL C   OXT  sing N N 470 
VAL CB  CG1  sing N N 471 
VAL CB  CG2  sing N N 472 
VAL CB  HB   sing N N 473 
VAL CG1 HG11 sing N N 474 
VAL CG1 HG12 sing N N 475 
VAL CG1 HG13 sing N N 476 
VAL CG2 HG21 sing N N 477 
VAL CG2 HG22 sing N N 478 
VAL CG2 HG23 sing N N 479 
VAL OXT HXT  sing N N 480 
Y6F C25 C24  sing N N 481 
Y6F C24 N23  sing N N 482 
Y6F C26 N23  sing N N 483 
Y6F C26 C27  sing N N 484 
Y6F N23 S02  sing N N 485 
Y6F O01 S02  doub N N 486 
Y6F O28 S02  doub N N 487 
Y6F S02 C03  sing N N 488 
Y6F C03 C22  doub Y N 489 
Y6F C03 C04  sing Y N 490 
Y6F C22 C21  sing Y N 491 
Y6F C04 C05  doub Y N 492 
Y6F C21 C06  doub Y N 493 
Y6F C05 C06  sing Y N 494 
Y6F C06 C07  sing N N 495 
Y6F C18 C17  sing N N 496 
Y6F C07 N20  sing Y N 497 
Y6F C07 C08  doub Y N 498 
Y6F N20 C10  doub Y N 499 
Y6F C08 S09  sing Y N 500 
Y6F C17 C19  doub Y N 501 
Y6F C17 C15  sing Y N 502 
Y6F C19 C12  sing Y N 503 
Y6F C10 S09  sing Y N 504 
Y6F C10 N11  sing N N 505 
Y6F C16 C15  sing N N 506 
Y6F C15 C14  doub Y N 507 
Y6F C12 N11  sing N N 508 
Y6F C12 C13  doub Y N 509 
Y6F C14 C13  sing Y N 510 
Y6F C13 H1   sing N N 511 
Y6F C14 H2   sing N N 512 
Y6F C16 H3   sing N N 513 
Y6F C16 H4   sing N N 514 
Y6F C16 H5   sing N N 515 
Y6F C18 H6   sing N N 516 
Y6F C18 H7   sing N N 517 
Y6F C18 H8   sing N N 518 
Y6F C19 H9   sing N N 519 
Y6F C21 H10  sing N N 520 
Y6F C22 H11  sing N N 521 
Y6F C24 H12  sing N N 522 
Y6F C24 H13  sing N N 523 
Y6F C04 H14  sing N N 524 
Y6F C05 H15  sing N N 525 
Y6F C08 H16  sing N N 526 
Y6F C25 H17  sing N N 527 
Y6F C25 H18  sing N N 528 
Y6F C25 H19  sing N N 529 
Y6F C26 H20  sing N N 530 
Y6F C26 H21  sing N N 531 
Y6F C27 H22  sing N N 532 
Y6F C27 H23  sing N N 533 
Y6F C27 H24  sing N N 534 
Y6F N11 H25  sing N N 535 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2023-11-20 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           8V1G 
_em_admin.last_update        2024-11-20 
_em_admin.map_release_date   2024-11-20 
_em_admin.title              'plasmodium falciparum Niemann-Pick type C1-related protein bound with MMV009108' 
# 
_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_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          36329 
_em_entity_assembly_naturalsource.organism             'Plasmodium falciparum 3D7' 
_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          9606 
_em_entity_assembly_recombinant.organism             'Homo sapiens' 
_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         40.5 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'GATAN K3 BIOQUANTUM (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                     ? 
# 
_em_particle_selection.details                  ? 
_em_particle_selection.id                       1 
_em_particle_selection.image_processing_id      1 
_em_particle_selection.method                   ? 
_em_particle_selection.num_particles_selected   5798543 
_em_particle_selection.reference_model          ? 
# 
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 
'PARTICLE SELECTION'            ? 1  1 ? ? ? ? 
'IMAGE ACQUISITION'             ? 2  ? ? 1 ? ? 
MASKING                         ? 3  ? ? ? ? ? 
'CTF CORRECTION'                ? 4  1 ? ? ? ? 
'LAYERLINE INDEXING'            ? 5  ? ? ? ? ? 
'DIFFRACTION INDEXING'          ? 6  ? ? ? ? ? 
'MODEL FITTING'                 ? 7  ? ? ? ? ? 
'MODEL REFINEMENT'              ? 8  ? ? ? ? ? 
OTHER                           ? 9  ? ? ? ? ? 
'INITIAL EULER ASSIGNMENT'      ? 10 1 ? ? ? ? 
'FINAL EULER ASSIGNMENT'        ? 11 1 ? ? ? ? 
CLASSIFICATION                  ? 12 1 ? ? ? ? 
RECONSTRUCTION                  ? 13 1 ? ? ? ? 
'VOLUME SELECTION'              ? 14 1 1 1 ? ? 
'SERIES ALIGNMENT'              ? 15 1 1 1 ? ? 
'MOLECULAR REPLACEMENT'         ? 16 1 1 1 ? ? 
'LATTICE DISTORTION CORRECTION' ? 17 1 1 1 ? ? 
'SYMMETRY DETERMINATION'        ? 18 1 1 1 ? ? 
'CRYSTALLOGRAPHY MERGING'       ? 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 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    8V1G 
_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   . ASN A 1 5    ? 193.685 120.137 162.143 1.00 138.50 ? 5    ASN A N   1 
ATOM   2    C CA  . ASN A 1 5    ? 194.660 121.216 162.046 1.00 141.42 ? 5    ASN A CA  1 
ATOM   3    C C   . ASN A 1 5    ? 193.970 122.573 161.968 1.00 141.64 ? 5    ASN A C   1 
ATOM   4    O O   . ASN A 1 5    ? 194.130 123.415 162.852 1.00 141.05 ? 5    ASN A O   1 
ATOM   5    C CB  . ASN A 1 5    ? 195.561 121.017 160.826 1.00 140.73 ? 5    ASN A CB  1 
ATOM   6    C CG  . ASN A 1 5    ? 196.579 122.130 160.663 1.00 140.93 ? 5    ASN A CG  1 
ATOM   7    O OD1 . ASN A 1 5    ? 197.003 122.748 161.640 1.00 140.12 ? 5    ASN A OD1 1 
ATOM   8    N ND2 . ASN A 1 5    ? 196.976 122.392 159.424 1.00 141.00 ? 5    ASN A ND2 1 
ATOM   9    N N   . PHE A 1 6    ? 193.204 122.774 160.894 1.00 138.74 ? 6    PHE A N   1 
ATOM   10   C CA  . PHE A 1 6    ? 192.528 124.050 160.690 1.00 138.86 ? 6    PHE A CA  1 
ATOM   11   C C   . PHE A 1 6    ? 191.518 124.326 161.797 1.00 137.89 ? 6    PHE A C   1 
ATOM   12   O O   . PHE A 1 6    ? 191.475 125.433 162.348 1.00 136.98 ? 6    PHE A O   1 
ATOM   13   C CB  . PHE A 1 6    ? 191.846 124.055 159.322 1.00 139.48 ? 6    PHE A CB  1 
ATOM   14   C CG  . PHE A 1 6    ? 191.339 125.402 158.897 1.00 139.91 ? 6    PHE A CG  1 
ATOM   15   C CD1 . PHE A 1 6    ? 192.177 126.301 158.258 1.00 138.37 ? 6    PHE A CD1 1 
ATOM   16   C CD2 . PHE A 1 6    ? 190.022 125.765 159.122 1.00 138.96 ? 6    PHE A CD2 1 
ATOM   17   C CE1 . PHE A 1 6    ? 191.713 127.540 157.859 1.00 138.03 ? 6    PHE A CE1 1 
ATOM   18   C CE2 . PHE A 1 6    ? 189.551 127.003 158.726 1.00 137.93 ? 6    PHE A CE2 1 
ATOM   19   C CZ  . PHE A 1 6    ? 190.399 127.892 158.094 1.00 139.33 ? 6    PHE A CZ  1 
ATOM   20   N N   . ILE A 1 7    ? 190.713 123.321 162.150 1.00 138.05 ? 7    ILE A N   1 
ATOM   21   C CA  . ILE A 1 7    ? 189.674 123.507 163.160 1.00 139.55 ? 7    ILE A CA  1 
ATOM   22   C C   . ILE A 1 7    ? 190.292 123.861 164.506 1.00 139.94 ? 7    ILE A C   1 
ATOM   23   O O   . ILE A 1 7    ? 189.829 124.776 165.197 1.00 139.24 ? 7    ILE A O   1 
ATOM   24   C CB  . ILE A 1 7    ? 188.794 122.247 163.258 1.00 138.96 ? 7    ILE A CB  1 
ATOM   25   C CG1 . ILE A 1 7    ? 188.083 121.985 161.928 1.00 138.46 ? 7    ILE A CG1 1 
ATOM   26   C CG2 . ILE A 1 7    ? 187.786 122.383 164.389 1.00 137.76 ? 7    ILE A CG2 1 
ATOM   27   C CD1 . ILE A 1 7    ? 187.217 120.742 161.933 1.00 137.83 ? 7    ILE A CD1 1 
ATOM   28   N N   . HIS A 1 8    ? 191.344 123.143 164.900 1.00 135.82 ? 8    HIS A N   1 
ATOM   29   C CA  . HIS A 1 8    ? 191.979 123.412 166.185 1.00 133.83 ? 8    HIS A CA  1 
ATOM   30   C C   . HIS A 1 8    ? 192.649 124.781 166.200 1.00 134.30 ? 8    HIS A C   1 
ATOM   31   O O   . HIS A 1 8    ? 192.415 125.583 167.113 1.00 135.31 ? 8    HIS A O   1 
ATOM   32   C CB  . HIS A 1 8    ? 192.994 122.315 166.505 1.00 132.07 ? 8    HIS A CB  1 
ATOM   33   C CG  . HIS A 1 8    ? 193.762 122.551 167.767 1.00 132.96 ? 8    HIS A CG  1 
ATOM   34   N ND1 . HIS A 1 8    ? 193.230 122.317 169.017 1.00 133.53 ? 8    HIS A ND1 1 
ATOM   35   C CD2 . HIS A 1 8    ? 195.022 123.002 167.973 1.00 133.31 ? 8    HIS A CD2 1 
ATOM   36   C CE1 . HIS A 1 8    ? 194.130 122.612 169.938 1.00 133.69 ? 8    HIS A CE1 1 
ATOM   37   N NE2 . HIS A 1 8    ? 195.226 123.030 169.331 1.00 133.25 ? 8    HIS A NE2 1 
ATOM   38   N N   . LYS A 1 9    ? 193.469 125.073 165.189 1.00 126.68 ? 9    LYS A N   1 
ATOM   39   C CA  . LYS A 1 9    ? 194.271 126.292 165.198 1.00 127.07 ? 9    LYS A CA  1 
ATOM   40   C C   . LYS A 1 9    ? 193.407 127.542 165.070 1.00 127.40 ? 9    LYS A C   1 
ATOM   41   O O   . LYS A 1 9    ? 193.606 128.521 165.798 1.00 126.32 ? 9    LYS A O   1 
ATOM   42   C CB  . LYS A 1 9    ? 195.315 126.243 164.080 1.00 125.88 ? 9    LYS A CB  1 
ATOM   43   C CG  . LYS A 1 9    ? 196.411 125.220 164.318 1.00 126.40 ? 9    LYS A CG  1 
ATOM   44   C CD  . LYS A 1 9    ? 197.071 125.436 165.670 1.00 126.71 ? 9    LYS A CD  1 
ATOM   45   C CE  . LYS A 1 9    ? 198.098 124.356 165.964 1.00 126.33 ? 9    LYS A CE  1 
ATOM   46   N NZ  . LYS A 1 9    ? 198.722 124.537 167.303 1.00 126.79 ? 9    LYS A NZ  1 
ATOM   47   N N   . LEU A 1 10   ? 192.449 127.534 164.138 1.00 119.36 ? 10   LEU A N   1 
ATOM   48   C CA  . LEU A 1 10   ? 191.608 128.712 163.957 1.00 118.54 ? 10   LEU A CA  1 
ATOM   49   C C   . LEU A 1 10   ? 190.788 129.000 165.206 1.00 116.42 ? 10   LEU A C   1 
ATOM   50   O O   . LEU A 1 10   ? 190.673 130.155 165.631 1.00 116.26 ? 10   LEU A O   1 
ATOM   51   C CB  . LEU A 1 10   ? 190.693 128.529 162.747 1.00 118.71 ? 10   LEU A CB  1 
ATOM   52   C CG  . LEU A 1 10   ? 189.822 129.744 162.423 1.00 118.33 ? 10   LEU A CG  1 
ATOM   53   C CD1 . LEU A 1 10   ? 190.690 130.962 162.154 1.00 118.22 ? 10   LEU A CD1 1 
ATOM   54   C CD2 . LEU A 1 10   ? 188.913 129.460 161.240 1.00 118.66 ? 10   LEU A CD2 1 
ATOM   55   N N   . LYS A 1 11   ? 190.220 127.958 165.817 1.00 112.20 ? 11   LYS A N   1 
ATOM   56   C CA  . LYS A 1 11   ? 189.435 128.158 167.030 1.00 113.41 ? 11   LYS A CA  1 
ATOM   57   C C   . LYS A 1 11   ? 190.309 128.633 168.184 1.00 114.39 ? 11   LYS A C   1 
ATOM   58   O O   . LYS A 1 11   ? 189.889 129.484 168.977 1.00 115.58 ? 11   LYS A O   1 
ATOM   59   C CB  . LYS A 1 11   ? 188.696 126.873 167.402 1.00 112.73 ? 11   LYS A CB  1 
ATOM   60   C CG  . LYS A 1 11   ? 187.484 126.591 166.530 1.00 111.56 ? 11   LYS A CG  1 
ATOM   61   C CD  . LYS A 1 11   ? 186.620 125.487 167.114 1.00 112.53 ? 11   LYS A CD  1 
ATOM   62   C CE  . LYS A 1 11   ? 185.341 125.306 166.311 1.00 112.67 ? 11   LYS A CE  1 
ATOM   63   N NZ  . LYS A 1 11   ? 184.446 124.276 166.907 1.00 112.19 ? 11   LYS A NZ  1 
ATOM   64   N N   . GLU A 1 12   ? 191.527 128.096 168.299 1.00 116.03 ? 12   GLU A N   1 
ATOM   65   C CA  . GLU A 1 12   ? 192.426 128.549 169.355 1.00 116.29 ? 12   GLU A CA  1 
ATOM   66   C C   . GLU A 1 12   ? 192.782 130.019 169.180 1.00 115.67 ? 12   GLU A C   1 
ATOM   67   O O   . GLU A 1 12   ? 192.767 130.790 170.148 1.00 113.25 ? 12   GLU A O   1 
ATOM   68   C CB  . GLU A 1 12   ? 193.689 127.689 169.372 1.00 115.92 ? 12   GLU A CB  1 
ATOM   69   C CG  . GLU A 1 12   ? 194.563 127.892 170.599 1.00 118.25 ? 12   GLU A CG  1 
ATOM   70   C CD  . GLU A 1 12   ? 193.946 127.314 171.859 1.00 117.53 ? 12   GLU A CD  1 
ATOM   71   O OE1 . GLU A 1 12   ? 193.021 126.483 171.746 1.00 117.18 ? 12   GLU A OE1 1 
ATOM   72   O OE2 . GLU A 1 12   ? 194.388 127.692 172.964 1.00 115.94 ? 12   GLU A OE2 1 
ATOM   73   N N   . LEU A 1 13   ? 193.094 130.428 167.947 1.00 106.03 ? 13   LEU A N   1 
ATOM   74   C CA  . LEU A 1 13   ? 193.400 131.831 167.689 1.00 104.77 ? 13   LEU A CA  1 
ATOM   75   C C   . LEU A 1 13   ? 192.199 132.719 167.985 1.00 105.27 ? 13   LEU A C   1 
ATOM   76   O O   . LEU A 1 13   ? 192.344 133.799 168.571 1.00 106.98 ? 13   LEU A O   1 
ATOM   77   C CB  . LEU A 1 13   ? 193.853 132.011 166.241 1.00 106.00 ? 13   LEU A CB  1 
ATOM   78   C CG  . LEU A 1 13   ? 195.158 131.324 165.840 1.00 109.66 ? 13   LEU A CG  1 
ATOM   79   C CD1 . LEU A 1 13   ? 195.418 131.500 164.352 1.00 107.21 ? 13   LEU A CD1 1 
ATOM   80   C CD2 . LEU A 1 13   ? 196.321 131.861 166.659 1.00 108.36 ? 13   LEU A CD2 1 
ATOM   81   N N   . LYS A 1 14   ? 191.004 132.281 167.584 1.00 90.47  ? 14   LYS A N   1 
ATOM   82   C CA  . LYS A 1 14   ? 189.798 133.058 167.843 1.00 88.22  ? 14   LYS A CA  1 
ATOM   83   C C   . LYS A 1 14   ? 189.568 133.239 169.338 1.00 90.98  ? 14   LYS A C   1 
ATOM   84   O O   . LYS A 1 14   ? 189.295 134.354 169.805 1.00 92.68  ? 14   LYS A O   1 
ATOM   85   C CB  . LYS A 1 14   ? 188.601 132.367 167.190 1.00 86.01  ? 14   LYS A CB  1 
ATOM   86   C CG  . LYS A 1 14   ? 187.278 133.073 167.374 1.00 89.17  ? 14   LYS A CG  1 
ATOM   87   C CD  . LYS A 1 14   ? 186.156 132.295 166.707 1.00 86.47  ? 14   LYS A CD  1 
ATOM   88   C CE  . LYS A 1 14   ? 185.915 130.966 167.393 1.00 85.06  ? 14   LYS A CE  1 
ATOM   89   N NZ  . LYS A 1 14   ? 184.783 130.228 166.767 1.00 85.91  ? 14   LYS A NZ  1 
ATOM   90   N N   . GLN A 1 15   ? 189.686 132.153 170.105 1.00 90.22  ? 15   GLN A N   1 
ATOM   91   C CA  . GLN A 1 15   ? 189.488 132.241 171.547 1.00 87.63  ? 15   GLN A CA  1 
ATOM   92   C C   . GLN A 1 15   ? 190.535 133.133 172.195 1.00 87.33  ? 15   GLN A C   1 
ATOM   93   O O   . GLN A 1 15   ? 190.215 133.929 173.085 1.00 87.37  ? 15   GLN A O   1 
ATOM   94   C CB  . GLN A 1 15   ? 189.514 130.845 172.166 1.00 91.61  ? 15   GLN A CB  1 
ATOM   95   C CG  . GLN A 1 15   ? 188.224 130.064 171.985 1.00 94.20  ? 15   GLN A CG  1 
ATOM   96   C CD  . GLN A 1 15   ? 187.072 130.654 172.775 1.00 93.50  ? 15   GLN A CD  1 
ATOM   97   O OE1 . GLN A 1 15   ? 186.377 131.554 172.305 1.00 91.39  ? 15   GLN A OE1 1 
ATOM   98   N NE2 . GLN A 1 15   ? 186.865 130.148 173.984 1.00 91.79  ? 15   GLN A NE2 1 
ATOM   99   N N   . LYS A 1 16   ? 191.794 133.016 171.766 1.00 91.18  ? 16   LYS A N   1 
ATOM   100  C CA  . LYS A 1 16   ? 192.840 133.855 172.337 1.00 92.79  ? 16   LYS A CA  1 
ATOM   101  C C   . LYS A 1 16   ? 192.588 135.328 172.042 1.00 93.91  ? 16   LYS A C   1 
ATOM   102  O O   . LYS A 1 16   ? 192.762 136.183 172.918 1.00 91.84  ? 16   LYS A O   1 
ATOM   103  C CB  . LYS A 1 16   ? 194.207 133.423 171.808 1.00 93.51  ? 16   LYS A CB  1 
ATOM   104  C CG  . LYS A 1 16   ? 195.376 134.140 172.458 1.00 92.54  ? 16   LYS A CG  1 
ATOM   105  C CD  . LYS A 1 16   ? 196.699 133.537 172.021 1.00 93.54  ? 16   LYS A CD  1 
ATOM   106  C CE  . LYS A 1 16   ? 196.780 132.065 172.392 1.00 93.18  ? 16   LYS A CE  1 
ATOM   107  N NZ  . LYS A 1 16   ? 198.069 131.453 171.966 1.00 92.86  ? 16   LYS A NZ  1 
ATOM   108  N N   . SER A 1 17   ? 192.166 135.643 170.815 1.00 86.21  ? 17   SER A N   1 
ATOM   109  C CA  . SER A 1 17   ? 191.876 137.031 170.471 1.00 81.08  ? 17   SER A CA  1 
ATOM   110  C C   . SER A 1 17   ? 190.718 137.575 171.296 1.00 82.73  ? 17   SER A C   1 
ATOM   111  O O   . SER A 1 17   ? 190.786 138.700 171.810 1.00 81.86  ? 17   SER A O   1 
ATOM   112  C CB  . SER A 1 17   ? 191.568 137.146 168.979 1.00 81.50  ? 17   SER A CB  1 
ATOM   113  O OG  . SER A 1 17   ? 190.460 136.338 168.628 1.00 82.91  ? 17   SER A OG  1 
ATOM   114  N N   . LEU A 1 18   ? 189.645 136.793 171.436 1.00 81.52  ? 18   LEU A N   1 
ATOM   115  C CA  . LEU A 1 18   ? 188.502 137.255 172.220 1.00 77.58  ? 18   LEU A CA  1 
ATOM   116  C C   . LEU A 1 18   ? 188.882 137.463 173.681 1.00 80.57  ? 18   LEU A C   1 
ATOM   117  O O   . LEU A 1 18   ? 188.483 138.459 174.299 1.00 82.54  ? 18   LEU A O   1 
ATOM   118  C CB  . LEU A 1 18   ? 187.345 136.265 172.099 1.00 77.46  ? 18   LEU A CB  1 
ATOM   119  C CG  . LEU A 1 18   ? 186.730 136.132 170.706 1.00 79.14  ? 18   LEU A CG  1 
ATOM   120  C CD1 . LEU A 1 18   ? 185.559 135.166 170.726 1.00 79.60  ? 18   LEU A CD1 1 
ATOM   121  C CD2 . LEU A 1 18   ? 186.299 137.489 170.181 1.00 77.25  ? 18   LEU A CD2 1 
ATOM   122  N N   . ASP A 1 19   ? 189.656 136.536 174.250 1.00 84.32  ? 19   ASP A N   1 
ATOM   123  C CA  . ASP A 1 19   ? 190.079 136.680 175.638 1.00 80.70  ? 19   ASP A CA  1 
ATOM   124  C C   . ASP A 1 19   ? 190.973 137.898 175.820 1.00 84.31  ? 19   ASP A C   1 
ATOM   125  O O   . ASP A 1 19   ? 190.855 138.621 176.817 1.00 89.01  ? 19   ASP A O   1 
ATOM   126  C CB  . ASP A 1 19   ? 190.793 135.414 176.102 1.00 84.90  ? 19   ASP A CB  1 
ATOM   127  C CG  . ASP A 1 19   ? 189.885 134.204 176.104 1.00 91.18  ? 19   ASP A CG  1 
ATOM   128  O OD1 . ASP A 1 19   ? 188.673 134.373 176.353 1.00 92.76  ? 19   ASP A OD1 1 
ATOM   129  O OD2 . ASP A 1 19   ? 190.380 133.085 175.853 1.00 90.49  ? 19   ASP A OD2 1 
ATOM   130  N N   . LYS A 1 20   ? 191.881 138.140 174.872 1.00 78.20  ? 20   LYS A N   1 
ATOM   131  C CA  . LYS A 1 20   ? 192.742 139.312 174.973 1.00 80.59  ? 20   LYS A CA  1 
ATOM   132  C C   . LYS A 1 20   ? 191.929 140.595 174.891 1.00 78.25  ? 20   LYS A C   1 
ATOM   133  O O   . LYS A 1 20   ? 192.199 141.553 175.622 1.00 77.31  ? 20   LYS A O   1 
ATOM   134  C CB  . LYS A 1 20   ? 193.813 139.285 173.886 1.00 81.49  ? 20   LYS A CB  1 
ATOM   135  C CG  . LYS A 1 20   ? 194.838 140.400 174.023 1.00 77.81  ? 20   LYS A CG  1 
ATOM   136  C CD  . LYS A 1 20   ? 195.847 140.379 172.889 1.00 83.05  ? 20   LYS A CD  1 
ATOM   137  C CE  . LYS A 1 20   ? 196.857 141.505 173.035 1.00 82.69  ? 20   LYS A CE  1 
ATOM   138  N NZ  . LYS A 1 20   ? 197.808 141.553 171.892 1.00 79.72  ? 20   LYS A NZ  1 
ATOM   139  N N   . PHE A 1 21   ? 190.929 140.636 174.008 1.00 66.38  ? 21   PHE A N   1 
ATOM   140  C CA  . PHE A 1 21   ? 190.077 141.819 173.926 1.00 64.88  ? 21   PHE A CA  1 
ATOM   141  C C   . PHE A 1 21   ? 189.312 142.038 175.225 1.00 69.35  ? 21   PHE A C   1 
ATOM   142  O O   . PHE A 1 21   ? 189.199 143.173 175.710 1.00 71.31  ? 21   PHE A O   1 
ATOM   143  C CB  . PHE A 1 21   ? 189.110 141.691 172.751 1.00 58.81  ? 21   PHE A CB  1 
ATOM   144  C CG  . PHE A 1 21   ? 188.209 142.878 172.578 1.00 61.44  ? 21   PHE A CG  1 
ATOM   145  C CD1 . PHE A 1 21   ? 188.648 144.004 171.910 1.00 61.07  ? 21   PHE A CD1 1 
ATOM   146  C CD2 . PHE A 1 21   ? 186.923 142.866 173.081 1.00 66.54  ? 21   PHE A CD2 1 
ATOM   147  C CE1 . PHE A 1 21   ? 187.824 145.096 171.750 1.00 59.90  ? 21   PHE A CE1 1 
ATOM   148  C CE2 . PHE A 1 21   ? 186.094 143.956 172.924 1.00 63.72  ? 21   PHE A CE2 1 
ATOM   149  C CZ  . PHE A 1 21   ? 186.546 145.071 172.257 1.00 58.99  ? 21   PHE A CZ  1 
ATOM   150  N N   . ALA A 1 22   ? 188.780 140.960 175.805 1.00 69.16  ? 22   ALA A N   1 
ATOM   151  C CA  . ALA A 1 22   ? 188.057 141.088 177.065 1.00 60.53  ? 22   ALA A CA  1 
ATOM   152  C C   . ALA A 1 22   ? 188.969 141.595 178.173 1.00 64.11  ? 22   ALA A C   1 
ATOM   153  O O   . ALA A 1 22   ? 188.575 142.458 178.964 1.00 69.26  ? 22   ALA A O   1 
ATOM   154  C CB  . ALA A 1 22   ? 187.433 139.749 177.452 1.00 60.02  ? 22   ALA A CB  1 
ATOM   155  N N   . ASN A 1 23   ? 190.196 141.077 178.243 1.00 66.12  ? 23   ASN A N   1 
ATOM   156  C CA  . ASN A 1 23   ? 191.128 141.534 179.269 1.00 66.25  ? 23   ASN A CA  1 
ATOM   157  C C   . ASN A 1 23   ? 191.538 142.984 179.042 1.00 70.39  ? 23   ASN A C   1 
ATOM   158  O O   . ASN A 1 23   ? 191.719 143.744 180.003 1.00 77.97  ? 23   ASN A O   1 
ATOM   159  C CB  . ASN A 1 23   ? 192.352 140.624 179.305 1.00 69.55  ? 23   ASN A CB  1 
ATOM   160  C CG  . ASN A 1 23   ? 191.998 139.194 179.653 1.00 72.90  ? 23   ASN A CG  1 
ATOM   161  O OD1 . ASN A 1 23   ? 191.062 138.942 180.411 1.00 72.18  ? 23   ASN A OD1 1 
ATOM   162  N ND2 . ASN A 1 23   ? 192.743 138.248 179.095 1.00 73.01  ? 23   ASN A ND2 1 
ATOM   163  N N   . LEU A 1 24   ? 191.698 143.386 177.779 1.00 64.92  ? 24   LEU A N   1 
ATOM   164  C CA  . LEU A 1 24   ? 192.013 144.778 177.485 1.00 63.46  ? 24   LEU A CA  1 
ATOM   165  C C   . LEU A 1 24   ? 190.897 145.699 177.949 1.00 62.53  ? 24   LEU A C   1 
ATOM   166  O O   . LEU A 1 24   ? 191.158 146.753 178.535 1.00 62.62  ? 24   LEU A O   1 
ATOM   167  C CB  . LEU A 1 24   ? 192.266 144.963 175.991 1.00 63.22  ? 24   LEU A CB  1 
ATOM   168  C CG  . LEU A 1 24   ? 193.587 144.422 175.450 1.00 68.65  ? 24   LEU A CG  1 
ATOM   169  C CD1 . LEU A 1 24   ? 193.709 144.713 173.965 1.00 68.22  ? 24   LEU A CD1 1 
ATOM   170  C CD2 . LEU A 1 24   ? 194.757 145.012 176.217 1.00 67.81  ? 24   LEU A CD2 1 
ATOM   171  N N   . LEU A 1 25   ? 189.643 145.315 177.705 1.00 61.70  ? 25   LEU A N   1 
ATOM   172  C CA  . LEU A 1 25   ? 188.534 146.142 178.171 1.00 56.61  ? 25   LEU A CA  1 
ATOM   173  C C   . LEU A 1 25   ? 188.428 146.124 179.691 1.00 56.82  ? 25   LEU A C   1 
ATOM   174  O O   . LEU A 1 25   ? 188.037 147.123 180.303 1.00 62.97  ? 25   LEU A O   1 
ATOM   175  C CB  . LEU A 1 25   ? 187.229 145.688 177.528 1.00 56.60  ? 25   LEU A CB  1 
ATOM   176  C CG  . LEU A 1 25   ? 186.783 146.578 176.369 1.00 55.13  ? 25   LEU A CG  1 
ATOM   177  C CD1 . LEU A 1 25   ? 186.522 147.985 176.860 1.00 48.06  ? 25   LEU A CD1 1 
ATOM   178  C CD2 . LEU A 1 25   ? 187.822 146.585 175.269 1.00 55.51  ? 25   LEU A CD2 1 
ATOM   179  N N   . TYR A 1 26   ? 188.774 144.999 180.317 1.00 60.12  ? 26   TYR A N   1 
ATOM   180  C CA  . TYR A 1 26   ? 188.837 144.934 181.774 1.00 58.95  ? 26   TYR A CA  1 
ATOM   181  C C   . TYR A 1 26   ? 189.817 145.965 182.321 1.00 60.85  ? 26   TYR A C   1 
ATOM   182  O O   . TYR A 1 26   ? 189.482 146.758 183.213 1.00 70.44  ? 26   TYR A O   1 
ATOM   183  C CB  . TYR A 1 26   ? 189.241 143.517 182.188 1.00 60.60  ? 26   TYR A CB  1 
ATOM   184  C CG  . TYR A 1 26   ? 189.354 143.258 183.673 1.00 63.08  ? 26   TYR A CG  1 
ATOM   185  C CD1 . TYR A 1 26   ? 190.519 143.552 184.364 1.00 63.71  ? 26   TYR A CD1 1 
ATOM   186  C CD2 . TYR A 1 26   ? 188.307 142.682 184.375 1.00 63.02  ? 26   TYR A CD2 1 
ATOM   187  C CE1 . TYR A 1 26   ? 190.629 143.303 185.715 1.00 59.16  ? 26   TYR A CE1 1 
ATOM   188  C CE2 . TYR A 1 26   ? 188.409 142.426 185.725 1.00 63.49  ? 26   TYR A CE2 1 
ATOM   189  C CZ  . TYR A 1 26   ? 189.571 142.741 186.389 1.00 61.06  ? 26   TYR A CZ  1 
ATOM   190  O OH  . TYR A 1 26   ? 189.677 142.489 187.736 1.00 67.16  ? 26   TYR A OH  1 
ATOM   191  N N   . ASP A 1 27   ? 191.033 145.980 181.777 1.00 57.05  ? 27   ASP A N   1 
ATOM   192  C CA  . ASP A 1 27   ? 192.031 146.940 182.233 1.00 54.03  ? 27   ASP A CA  1 
ATOM   193  C C   . ASP A 1 27   ? 191.624 148.367 181.890 1.00 60.74  ? 27   ASP A C   1 
ATOM   194  O O   . ASP A 1 27   ? 191.919 149.301 182.644 1.00 65.41  ? 27   ASP A O   1 
ATOM   195  C CB  . ASP A 1 27   ? 193.392 146.606 181.632 1.00 57.24  ? 27   ASP A CB  1 
ATOM   196  C CG  . ASP A 1 27   ? 193.926 145.276 182.114 1.00 68.65  ? 27   ASP A CG  1 
ATOM   197  O OD1 . ASP A 1 27   ? 193.653 144.915 183.277 1.00 69.29  ? 27   ASP A OD1 1 
ATOM   198  O OD2 . ASP A 1 27   ? 194.617 144.591 181.331 1.00 70.04  ? 27   ASP A OD2 1 
ATOM   199  N N   . TYR A 1 28   ? 190.950 148.558 180.755 1.00 55.14  ? 28   TYR A N   1 
ATOM   200  C CA  . TYR A 1 28   ? 190.490 149.893 180.391 1.00 51.02  ? 28   TYR A CA  1 
ATOM   201  C C   . TYR A 1 28   ? 189.456 150.408 181.380 1.00 51.97  ? 28   TYR A C   1 
ATOM   202  O O   . TYR A 1 28   ? 189.488 151.579 181.767 1.00 58.97  ? 28   TYR A O   1 
ATOM   203  C CB  . TYR A 1 28   ? 189.921 149.885 178.976 1.00 50.65  ? 28   TYR A CB  1 
ATOM   204  C CG  . TYR A 1 28   ? 189.195 151.154 178.612 1.00 42.36  ? 28   TYR A CG  1 
ATOM   205  C CD1 . TYR A 1 28   ? 189.893 152.313 178.317 1.00 49.41  ? 28   TYR A CD1 1 
ATOM   206  C CD2 . TYR A 1 28   ? 187.812 151.192 178.561 1.00 46.40  ? 28   TYR A CD2 1 
ATOM   207  C CE1 . TYR A 1 28   ? 189.233 153.474 177.983 1.00 54.44  ? 28   TYR A CE1 1 
ATOM   208  C CE2 . TYR A 1 28   ? 187.144 152.346 178.228 1.00 52.16  ? 28   TYR A CE2 1 
ATOM   209  C CZ  . TYR A 1 28   ? 187.858 153.484 177.939 1.00 58.05  ? 28   TYR A CZ  1 
ATOM   210  O OH  . TYR A 1 28   ? 187.193 154.638 177.609 1.00 60.77  ? 28   TYR A OH  1 
ATOM   211  N N   . GLY A 1 29   ? 188.523 149.551 181.791 1.00 56.66  ? 29   GLY A N   1 
ATOM   212  C CA  . GLY A 1 29   ? 187.581 149.945 182.824 1.00 50.32  ? 29   GLY A CA  1 
ATOM   213  C C   . GLY A 1 29   ? 188.270 150.244 184.139 1.00 50.43  ? 29   GLY A C   1 
ATOM   214  O O   . GLY A 1 29   ? 187.900 151.185 184.848 1.00 58.26  ? 29   GLY A O   1 
ATOM   215  N N   . GLY A 1 30   ? 189.283 149.448 184.481 1.00 53.59  ? 30   GLY A N   1 
ATOM   216  C CA  . GLY A 1 30   ? 190.053 149.734 185.681 1.00 54.05  ? 30   GLY A CA  1 
ATOM   217  C C   . GLY A 1 30   ? 190.724 151.092 185.630 1.00 59.70  ? 30   GLY A C   1 
ATOM   218  O O   . GLY A 1 30   ? 190.769 151.813 186.629 1.00 62.66  ? 30   GLY A O   1 
ATOM   219  N N   . TYR A 1 31   ? 191.258 151.457 184.464 1.00 64.64  ? 31   TYR A N   1 
ATOM   220  C CA  . TYR A 1 31   ? 191.893 152.762 184.312 1.00 63.33  ? 31   TYR A CA  1 
ATOM   221  C C   . TYR A 1 31   ? 190.867 153.888 184.347 1.00 62.09  ? 31   TYR A C   1 
ATOM   222  O O   . TYR A 1 31   ? 191.124 154.951 184.921 1.00 67.06  ? 31   TYR A O   1 
ATOM   223  C CB  . TYR A 1 31   ? 192.693 152.803 183.012 1.00 60.45  ? 31   TYR A CB  1 
ATOM   224  C CG  . TYR A 1 31   ? 193.489 154.071 182.814 1.00 65.67  ? 31   TYR A CG  1 
ATOM   225  C CD1 . TYR A 1 31   ? 194.737 154.229 183.400 1.00 68.71  ? 31   TYR A CD1 1 
ATOM   226  C CD2 . TYR A 1 31   ? 192.999 155.107 182.032 1.00 67.99  ? 31   TYR A CD2 1 
ATOM   227  C CE1 . TYR A 1 31   ? 195.470 155.384 183.219 1.00 66.00  ? 31   TYR A CE1 1 
ATOM   228  C CE2 . TYR A 1 31   ? 193.725 156.265 181.846 1.00 69.52  ? 31   TYR A CE2 1 
ATOM   229  C CZ  . TYR A 1 31   ? 194.959 156.398 182.441 1.00 68.08  ? 31   TYR A CZ  1 
ATOM   230  O OH  . TYR A 1 31   ? 195.688 157.549 182.258 1.00 66.57  ? 31   TYR A OH  1 
ATOM   231  N N   . VAL A 1 32   ? 189.703 153.673 183.733 1.00 49.47  ? 32   VAL A N   1 
ATOM   232  C CA  . VAL A 1 32   ? 188.664 154.698 183.709 1.00 45.60  ? 32   VAL A CA  1 
ATOM   233  C C   . VAL A 1 32   ? 188.123 154.959 185.106 1.00 58.44  ? 32   VAL A C   1 
ATOM   234  O O   . VAL A 1 32   ? 187.824 156.107 185.457 1.00 67.89  ? 32   VAL A O   1 
ATOM   235  C CB  . VAL A 1 32   ? 187.540 154.291 182.738 1.00 43.19  ? 32   VAL A CB  1 
ATOM   236  C CG1 . VAL A 1 32   ? 186.315 155.156 182.942 1.00 49.87  ? 32   VAL A CG1 1 
ATOM   237  C CG2 . VAL A 1 32   ? 188.019 154.401 181.309 1.00 53.58  ? 32   VAL A CG2 1 
ATOM   238  N N   . TYR A 1 33   ? 187.998 153.914 185.928 1.00 62.33  ? 33   TYR A N   1 
ATOM   239  C CA  . TYR A 1 33   ? 187.400 154.077 187.250 1.00 60.49  ? 33   TYR A CA  1 
ATOM   240  C C   . TYR A 1 33   ? 188.148 155.097 188.098 1.00 63.50  ? 33   TYR A C   1 
ATOM   241  O O   . TYR A 1 33   ? 187.544 155.744 188.960 1.00 67.16  ? 33   TYR A O   1 
ATOM   242  C CB  . TYR A 1 33   ? 187.349 152.732 187.971 1.00 62.92  ? 33   TYR A CB  1 
ATOM   243  C CG  . TYR A 1 33   ? 186.806 152.813 189.378 1.00 60.72  ? 33   TYR A CG  1 
ATOM   244  C CD1 . TYR A 1 33   ? 185.443 152.825 189.614 1.00 61.15  ? 33   TYR A CD1 1 
ATOM   245  C CD2 . TYR A 1 33   ? 187.658 152.871 190.470 1.00 61.35  ? 33   TYR A CD2 1 
ATOM   246  C CE1 . TYR A 1 33   ? 184.941 152.895 190.894 1.00 67.59  ? 33   TYR A CE1 1 
ATOM   247  C CE2 . TYR A 1 33   ? 187.166 152.942 191.754 1.00 61.99  ? 33   TYR A CE2 1 
ATOM   248  C CZ  . TYR A 1 33   ? 185.806 152.953 191.961 1.00 65.67  ? 33   TYR A CZ  1 
ATOM   249  O OH  . TYR A 1 33   ? 185.307 153.024 193.240 1.00 64.86  ? 33   TYR A OH  1 
ATOM   250  N N   . ASP A 1 34   ? 189.449 155.258 187.877 1.00 64.16  ? 34   ASP A N   1 
ATOM   251  C CA  . ASP A 1 34   ? 190.236 156.198 188.661 1.00 66.23  ? 34   ASP A CA  1 
ATOM   252  C C   . ASP A 1 34   ? 190.112 157.639 188.188 1.00 67.29  ? 34   ASP A C   1 
ATOM   253  O O   . ASP A 1 34   ? 190.400 158.553 188.967 1.00 68.45  ? 34   ASP A O   1 
ATOM   254  C CB  . ASP A 1 34   ? 191.711 155.791 188.647 1.00 63.73  ? 34   ASP A CB  1 
ATOM   255  C CG  . ASP A 1 34   ? 191.993 154.608 189.543 1.00 71.25  ? 34   ASP A CG  1 
ATOM   256  O OD1 . ASP A 1 34   ? 191.430 154.561 190.656 1.00 78.14  ? 34   ASP A OD1 1 
ATOM   257  O OD2 . ASP A 1 34   ? 192.774 153.723 189.138 1.00 71.05  ? 34   ASP A OD2 1 
ATOM   258  N N   . ARG A 1 35   ? 189.700 157.872 186.944 1.00 70.95  ? 35   ARG A N   1 
ATOM   259  C CA  . ARG A 1 35   ? 189.629 159.218 186.373 1.00 69.66  ? 35   ARG A CA  1 
ATOM   260  C C   . ARG A 1 35   ? 188.307 159.419 185.641 1.00 67.54  ? 35   ARG A C   1 
ATOM   261  O O   . ARG A 1 35   ? 188.275 159.540 184.414 1.00 77.27  ? 35   ARG A O   1 
ATOM   262  C CB  . ARG A 1 35   ? 190.811 159.459 185.436 1.00 72.40  ? 35   ARG A CB  1 
ATOM   263  C CG  . ARG A 1 35   ? 192.167 159.253 186.085 1.00 73.75  ? 35   ARG A CG  1 
ATOM   264  C CD  . ARG A 1 35   ? 193.255 159.046 185.050 1.00 69.50  ? 35   ARG A CD  1 
ATOM   265  N NE  . ARG A 1 35   ? 194.538 158.751 185.675 1.00 77.94  ? 35   ARG A NE  1 
ATOM   266  C CZ  . ARG A 1 35   ? 194.911 157.546 186.081 1.00 76.80  ? 35   ARG A CZ  1 
ATOM   267  N NH1 . ARG A 1 35   ? 194.118 156.496 185.946 1.00 74.46  ? 35   ARG A NH1 1 
ATOM   268  N NH2 . ARG A 1 35   ? 196.108 157.390 186.639 1.00 75.07  ? 35   ARG A NH2 1 
ATOM   269  N N   . PRO A 1 36   ? 187.191 159.463 186.364 1.00 58.06  ? 36   PRO A N   1 
ATOM   270  C CA  . PRO A 1 36   ? 185.897 159.634 185.692 1.00 57.74  ? 36   PRO A CA  1 
ATOM   271  C C   . PRO A 1 36   ? 185.689 161.041 185.153 1.00 59.32  ? 36   PRO A C   1 
ATOM   272  O O   . PRO A 1 36   ? 185.245 161.218 184.013 1.00 62.51  ? 36   PRO A O   1 
ATOM   273  C CB  . PRO A 1 36   ? 184.888 159.298 186.794 1.00 61.05  ? 36   PRO A CB  1 
ATOM   274  C CG  . PRO A 1 36   ? 185.592 159.636 188.056 1.00 65.05  ? 36   PRO A CG  1 
ATOM   275  C CD  . PRO A 1 36   ? 187.048 159.350 187.826 1.00 63.41  ? 36   PRO A CD  1 
ATOM   276  N N   . CYS A 1 37   ? 186.009 162.050 185.967 1.00 65.23  ? 37   CYS A N   1 
ATOM   277  C CA  . CYS A 1 37   ? 185.797 163.434 185.556 1.00 63.27  ? 37   CYS A CA  1 
ATOM   278  C C   . CYS A 1 37   ? 186.677 163.802 184.370 1.00 65.12  ? 37   CYS A C   1 
ATOM   279  O O   . CYS A 1 37   ? 186.247 164.534 183.470 1.00 61.26  ? 37   CYS A O   1 
ATOM   280  C CB  . CYS A 1 37   ? 186.061 164.374 186.731 1.00 61.49  ? 37   CYS A CB  1 
ATOM   281  S SG  . CYS A 1 37   ? 185.050 164.044 188.187 1.00 78.18  ? 37   CYS A SG  1 
ATOM   282  N N   . THR A 1 38   ? 187.921 163.319 184.361 1.00 59.59  ? 38   THR A N   1 
ATOM   283  C CA  . THR A 1 38   ? 188.815 163.592 183.243 1.00 53.78  ? 38   THR A CA  1 
ATOM   284  C C   . THR A 1 38   ? 188.245 163.038 181.945 1.00 52.42  ? 38   THR A C   1 
ATOM   285  O O   . THR A 1 38   ? 188.230 163.724 180.917 1.00 57.70  ? 38   THR A O   1 
ATOM   286  C CB  . THR A 1 38   ? 190.194 162.997 183.519 1.00 53.73  ? 38   THR A CB  1 
ATOM   287  O OG1 . THR A 1 38   ? 190.817 163.710 184.593 1.00 61.59  ? 38   THR A OG1 1 
ATOM   288  C CG2 . THR A 1 38   ? 191.068 163.085 182.284 1.00 48.19  ? 38   THR A CG2 1 
ATOM   289  N N   . PHE A 1 39   ? 187.762 161.796 181.976 1.00 52.80  ? 39   PHE A N   1 
ATOM   290  C CA  . PHE A 1 39   ? 187.164 161.216 180.781 1.00 46.03  ? 39   PHE A CA  1 
ATOM   291  C C   . PHE A 1 39   ? 185.915 161.978 180.365 1.00 51.73  ? 39   PHE A C   1 
ATOM   292  O O   . PHE A 1 39   ? 185.701 162.222 179.173 1.00 62.95  ? 39   PHE A O   1 
ATOM   293  C CB  . PHE A 1 39   ? 186.849 159.740 181.011 1.00 39.84  ? 39   PHE A CB  1 
ATOM   294  C CG  . PHE A 1 39   ? 187.988 158.825 180.680 1.00 51.22  ? 39   PHE A CG  1 
ATOM   295  C CD1 . PHE A 1 39   ? 189.045 158.669 181.554 1.00 57.17  ? 39   PHE A CD1 1 
ATOM   296  C CD2 . PHE A 1 39   ? 188.006 158.130 179.487 1.00 52.72  ? 39   PHE A CD2 1 
ATOM   297  C CE1 . PHE A 1 39   ? 190.095 157.832 181.249 1.00 60.01  ? 39   PHE A CE1 1 
ATOM   298  C CE2 . PHE A 1 39   ? 189.053 157.290 179.178 1.00 54.78  ? 39   PHE A CE2 1 
ATOM   299  C CZ  . PHE A 1 39   ? 190.098 157.143 180.059 1.00 55.59  ? 39   PHE A CZ  1 
ATOM   300  N N   . ILE A 1 40   ? 185.088 162.381 181.332 1.00 55.40  ? 40   ILE A N   1 
ATOM   301  C CA  . ILE A 1 40   ? 183.882 163.138 181.004 1.00 52.87  ? 40   ILE A CA  1 
ATOM   302  C C   . ILE A 1 40   ? 184.243 164.423 180.273 1.00 56.27  ? 40   ILE A C   1 
ATOM   303  O O   . ILE A 1 40   ? 183.708 164.718 179.198 1.00 63.60  ? 40   ILE A O   1 
ATOM   304  C CB  . ILE A 1 40   ? 183.066 163.434 182.273 1.00 55.94  ? 40   ILE A CB  1 
ATOM   305  C CG1 . ILE A 1 40   ? 182.368 162.175 182.773 1.00 58.64  ? 40   ILE A CG1 1 
ATOM   306  C CG2 . ILE A 1 40   ? 182.046 164.523 182.003 1.00 50.59  ? 40   ILE A CG2 1 
ATOM   307  C CD1 . ILE A 1 40   ? 181.583 162.385 184.042 1.00 54.15  ? 40   ILE A CD1 1 
ATOM   308  N N   . ILE A 1 41   ? 185.171 165.199 180.836 1.00 55.71  ? 41   ILE A N   1 
ATOM   309  C CA  . ILE A 1 41   ? 185.470 166.504 180.257 1.00 52.77  ? 41   ILE A CA  1 
ATOM   310  C C   . ILE A 1 41   ? 186.179 166.351 178.918 1.00 56.15  ? 41   ILE A C   1 
ATOM   311  O O   . ILE A 1 41   ? 185.904 167.100 177.975 1.00 61.55  ? 41   ILE A O   1 
ATOM   312  C CB  . ILE A 1 41   ? 186.274 167.376 181.239 1.00 51.31  ? 41   ILE A CB  1 
ATOM   313  C CG1 . ILE A 1 41   ? 187.617 166.739 181.585 1.00 60.75  ? 41   ILE A CG1 1 
ATOM   314  C CG2 . ILE A 1 41   ? 185.470 167.629 182.500 1.00 59.88  ? 41   ILE A CG2 1 
ATOM   315  C CD1 . ILE A 1 41   ? 188.474 167.591 182.493 1.00 59.83  ? 41   ILE A CD1 1 
ATOM   316  N N   . CYS A 1 42   ? 187.089 165.380 178.798 1.00 57.84  ? 42   CYS A N   1 
ATOM   317  C CA  . CYS A 1 42   ? 187.782 165.188 177.528 1.00 52.70  ? 42   CYS A CA  1 
ATOM   318  C C   . CYS A 1 42   ? 186.821 164.747 176.432 1.00 61.74  ? 42   CYS A C   1 
ATOM   319  O O   . CYS A 1 42   ? 186.871 165.264 175.308 1.00 69.60  ? 42   CYS A O   1 
ATOM   320  C CB  . CYS A 1 42   ? 188.912 164.176 177.695 1.00 54.95  ? 42   CYS A CB  1 
ATOM   321  S SG  . CYS A 1 42   ? 190.274 164.763 178.721 1.00 75.62  ? 42   CYS A SG  1 
ATOM   322  N N   . SER A 1 43   ? 185.934 163.795 176.737 1.00 53.03  ? 43   SER A N   1 
ATOM   323  C CA  . SER A 1 43   ? 184.960 163.355 175.747 1.00 48.98  ? 43   SER A CA  1 
ATOM   324  C C   . SER A 1 43   ? 184.025 164.488 175.356 1.00 50.66  ? 43   SER A C   1 
ATOM   325  O O   . SER A 1 43   ? 183.702 164.653 174.175 1.00 54.86  ? 43   SER A O   1 
ATOM   326  C CB  . SER A 1 43   ? 184.166 162.169 176.288 1.00 51.40  ? 43   SER A CB  1 
ATOM   327  O OG  . SER A 1 43   ? 183.514 162.512 177.496 1.00 55.35  ? 43   SER A OG  1 
ATOM   328  N N   . LEU A 1 44   ? 183.580 165.283 176.331 1.00 57.05  ? 44   LEU A N   1 
ATOM   329  C CA  . LEU A 1 44   ? 182.693 166.397 176.020 1.00 60.12  ? 44   LEU A CA  1 
ATOM   330  C C   . LEU A 1 44   ? 183.392 167.434 175.150 1.00 70.23  ? 44   LEU A C   1 
ATOM   331  O O   . LEU A 1 44   ? 182.797 167.966 174.206 1.00 72.60  ? 44   LEU A O   1 
ATOM   332  C CB  . LEU A 1 44   ? 182.180 167.028 177.312 1.00 57.75  ? 44   LEU A CB  1 
ATOM   333  C CG  . LEU A 1 44   ? 180.963 167.939 177.174 1.00 61.26  ? 44   LEU A CG  1 
ATOM   334  C CD1 . LEU A 1 44   ? 179.833 167.193 176.498 1.00 63.43  ? 44   LEU A CD1 1 
ATOM   335  C CD2 . LEU A 1 44   ? 180.528 168.448 178.534 1.00 62.21  ? 44   LEU A CD2 1 
ATOM   336  N N   . ILE A 1 45   ? 184.660 167.731 175.445 1.00 66.27  ? 45   ILE A N   1 
ATOM   337  C CA  . ILE A 1 45   ? 185.405 168.697 174.644 1.00 55.45  ? 45   ILE A CA  1 
ATOM   338  C C   . ILE A 1 45   ? 185.579 168.191 173.220 1.00 60.28  ? 45   ILE A C   1 
ATOM   339  O O   . ILE A 1 45   ? 185.395 168.942 172.253 1.00 68.71  ? 45   ILE A O   1 
ATOM   340  C CB  . ILE A 1 45   ? 186.760 169.004 175.306 1.00 56.13  ? 45   ILE A CB  1 
ATOM   341  C CG1 . ILE A 1 45   ? 186.567 169.908 176.523 1.00 59.53  ? 45   ILE A CG1 1 
ATOM   342  C CG2 . ILE A 1 45   ? 187.709 169.643 174.312 1.00 64.05  ? 45   ILE A CG2 1 
ATOM   343  C CD1 . ILE A 1 45   ? 187.860 170.292 177.203 1.00 62.91  ? 45   ILE A CD1 1 
ATOM   344  N N   . CYS A 1 46   ? 185.940 166.915 173.063 1.00 61.67  ? 46   CYS A N   1 
ATOM   345  C CA  . CYS A 1 46   ? 186.093 166.362 171.721 1.00 60.76  ? 46   CYS A CA  1 
ATOM   346  C C   . CYS A 1 46   ? 184.773 166.382 170.963 1.00 61.39  ? 46   CYS A C   1 
ATOM   347  O O   . CYS A 1 46   ? 184.735 166.708 169.769 1.00 69.49  ? 46   CYS A O   1 
ATOM   348  C CB  . CYS A 1 46   ? 186.650 164.943 171.796 1.00 69.88  ? 46   CYS A CB  1 
ATOM   349  S SG  . CYS A 1 46   ? 188.373 164.847 172.330 1.00 85.05  ? 46   CYS A SG  1 
ATOM   350  N N   . CYS A 1 47   ? 183.676 166.043 171.642 1.00 57.81  ? 47   CYS A N   1 
ATOM   351  C CA  . CYS A 1 47   ? 182.372 166.060 170.992 1.00 59.48  ? 47   CYS A CA  1 
ATOM   352  C C   . CYS A 1 47   ? 181.991 167.467 170.553 1.00 56.02  ? 47   CYS A C   1 
ATOM   353  O O   . CYS A 1 47   ? 181.451 167.654 169.460 1.00 58.89  ? 47   CYS A O   1 
ATOM   354  C CB  . CYS A 1 47   ? 181.311 165.486 171.927 1.00 61.48  ? 47   CYS A CB  1 
ATOM   355  S SG  . CYS A 1 47   ? 179.647 165.498 171.236 1.00 75.37  ? 47   CYS A SG  1 
ATOM   356  N N   . LEU A 1 48   ? 182.257 168.470 171.392 1.00 57.66  ? 48   LEU A N   1 
ATOM   357  C CA  . LEU A 1 48   ? 181.956 169.846 171.006 1.00 59.99  ? 48   LEU A CA  1 
ATOM   358  C C   . LEU A 1 48   ? 182.821 170.298 169.835 1.00 59.27  ? 48   LEU A C   1 
ATOM   359  O O   . LEU A 1 48   ? 182.338 170.986 168.927 1.00 61.13  ? 48   LEU A O   1 
ATOM   360  C CB  . LEU A 1 48   ? 182.135 170.780 172.201 1.00 61.04  ? 48   LEU A CB  1 
ATOM   361  C CG  . LEU A 1 48   ? 181.158 170.561 173.358 1.00 66.25  ? 48   LEU A CG  1 
ATOM   362  C CD1 . LEU A 1 48   ? 181.332 171.630 174.423 1.00 62.38  ? 48   LEU A CD1 1 
ATOM   363  C CD2 . LEU A 1 48   ? 179.724 170.527 172.855 1.00 65.04  ? 48   LEU A CD2 1 
ATOM   364  N N   . LEU A 1 49   ? 184.103 169.925 169.839 1.00 59.69  ? 49   LEU A N   1 
ATOM   365  C CA  . LEU A 1 49   ? 184.973 170.289 168.726 1.00 54.23  ? 49   LEU A CA  1 
ATOM   366  C C   . LEU A 1 49   ? 184.484 169.674 167.423 1.00 59.41  ? 49   LEU A C   1 
ATOM   367  O O   . LEU A 1 49   ? 184.505 170.327 166.374 1.00 67.34  ? 49   LEU A O   1 
ATOM   368  C CB  . LEU A 1 49   ? 186.411 169.862 169.014 1.00 55.54  ? 49   LEU A CB  1 
ATOM   369  C CG  . LEU A 1 49   ? 187.142 170.660 170.093 1.00 61.04  ? 49   LEU A CG  1 
ATOM   370  C CD1 . LEU A 1 49   ? 188.597 170.235 170.174 1.00 58.02  ? 49   LEU A CD1 1 
ATOM   371  C CD2 . LEU A 1 49   ? 187.029 172.148 169.820 1.00 62.40  ? 49   LEU A CD2 1 
ATOM   372  N N   . LEU A 1 50   ? 184.043 168.415 167.467 1.00 62.60  ? 50   LEU A N   1 
ATOM   373  C CA  . LEU A 1 50   ? 183.477 167.802 166.269 1.00 57.46  ? 50   LEU A CA  1 
ATOM   374  C C   . LEU A 1 50   ? 182.158 168.461 165.878 1.00 57.30  ? 50   LEU A C   1 
ATOM   375  O O   . LEU A 1 50   ? 181.884 168.650 164.688 1.00 63.24  ? 50   LEU A O   1 
ATOM   376  C CB  . LEU A 1 50   ? 183.289 166.301 166.479 1.00 56.57  ? 50   LEU A CB  1 
ATOM   377  C CG  . LEU A 1 50   ? 184.446 165.421 166.002 1.00 55.02  ? 50   LEU A CG  1 
ATOM   378  C CD1 . LEU A 1 50   ? 184.734 165.686 164.539 1.00 56.22  ? 50   LEU A CD1 1 
ATOM   379  C CD2 . LEU A 1 50   ? 185.693 165.644 166.835 1.00 53.22  ? 50   LEU A CD2 1 
ATOM   380  N N   . THR A 1 51   ? 181.331 168.818 166.864 1.00 56.85  ? 51   THR A N   1 
ATOM   381  C CA  . THR A 1 51   ? 180.053 169.460 166.577 1.00 56.95  ? 51   THR A CA  1 
ATOM   382  C C   . THR A 1 51   ? 180.248 170.807 165.902 1.00 62.00  ? 51   THR A C   1 
ATOM   383  O O   . THR A 1 51   ? 179.403 171.232 165.106 1.00 71.34  ? 51   THR A O   1 
ATOM   384  C CB  . THR A 1 51   ? 179.251 169.631 167.868 1.00 64.45  ? 51   THR A CB  1 
ATOM   385  O OG1 . THR A 1 51   ? 179.182 168.378 168.558 1.00 75.26  ? 51   THR A OG1 1 
ATOM   386  C CG2 . THR A 1 51   ? 177.840 170.109 167.568 1.00 56.40  ? 51   THR A CG2 1 
ATOM   387  N N   . CYS A 1 52   ? 181.356 171.489 166.201 1.00 64.98  ? 52   CYS A N   1 
ATOM   388  C CA  . CYS A 1 52   ? 181.651 172.759 165.544 1.00 63.01  ? 52   CYS A CA  1 
ATOM   389  C C   . CYS A 1 52   ? 181.671 172.636 164.026 1.00 63.26  ? 52   CYS A C   1 
ATOM   390  O O   . CYS A 1 52   ? 181.626 173.657 163.333 1.00 62.53  ? 52   CYS A O   1 
ATOM   391  C CB  . CYS A 1 52   ? 182.988 173.313 166.034 1.00 64.64  ? 52   CYS A CB  1 
ATOM   392  S SG  . CYS A 1 52   ? 182.959 173.937 167.729 1.00 82.68  ? 52   CYS A SG  1 
ATOM   393  N N   . GLY A 1 53   ? 181.731 171.417 163.493 1.00 66.34  ? 53   GLY A N   1 
ATOM   394  C CA  . GLY A 1 53   ? 181.655 171.206 162.061 1.00 67.04  ? 53   GLY A CA  1 
ATOM   395  C C   . GLY A 1 53   ? 180.309 171.523 161.448 1.00 66.58  ? 53   GLY A C   1 
ATOM   396  O O   . GLY A 1 53   ? 180.208 171.572 160.218 1.00 73.22  ? 53   GLY A O   1 
ATOM   397  N N   . PHE A 1 54   ? 179.277 171.736 162.267 1.00 57.88  ? 54   PHE A N   1 
ATOM   398  C CA  . PHE A 1 54   ? 177.974 172.114 161.734 1.00 53.50  ? 54   PHE A CA  1 
ATOM   399  C C   . PHE A 1 54   ? 178.016 173.448 161.009 1.00 57.79  ? 54   PHE A C   1 
ATOM   400  O O   . PHE A 1 54   ? 177.125 173.731 160.203 1.00 55.66  ? 54   PHE A O   1 
ATOM   401  C CB  . PHE A 1 54   ? 176.938 172.172 162.854 1.00 53.51  ? 54   PHE A CB  1 
ATOM   402  C CG  . PHE A 1 54   ? 176.231 170.874 163.093 1.00 56.52  ? 54   PHE A CG  1 
ATOM   403  C CD1 . PHE A 1 54   ? 176.755 169.933 163.956 1.00 59.94  ? 54   PHE A CD1 1 
ATOM   404  C CD2 . PHE A 1 54   ? 175.035 170.598 162.457 1.00 59.18  ? 54   PHE A CD2 1 
ATOM   405  C CE1 . PHE A 1 54   ? 176.102 168.740 164.177 1.00 62.44  ? 54   PHE A CE1 1 
ATOM   406  C CE2 . PHE A 1 54   ? 174.378 169.407 162.675 1.00 53.47  ? 54   PHE A CE2 1 
ATOM   407  C CZ  . PHE A 1 54   ? 174.912 168.478 163.537 1.00 54.26  ? 54   PHE A CZ  1 
ATOM   408  N N   . TYR A 1 55   ? 179.026 174.277 161.280 1.00 80.29  ? 55   TYR A N   1 
ATOM   409  C CA  . TYR A 1 55   ? 179.155 175.548 160.580 1.00 79.78  ? 55   TYR A CA  1 
ATOM   410  C C   . TYR A 1 55   ? 179.374 175.358 159.087 1.00 82.14  ? 55   TYR A C   1 
ATOM   411  O O   . TYR A 1 55   ? 179.090 176.274 158.309 1.00 82.70  ? 55   TYR A O   1 
ATOM   412  C CB  . TYR A 1 55   ? 180.303 176.360 161.182 1.00 76.54  ? 55   TYR A CB  1 
ATOM   413  C CG  . TYR A 1 55   ? 180.421 177.758 160.623 1.00 80.49  ? 55   TYR A CG  1 
ATOM   414  C CD1 . TYR A 1 55   ? 179.588 178.774 161.068 1.00 81.82  ? 55   TYR A CD1 1 
ATOM   415  C CD2 . TYR A 1 55   ? 181.366 178.062 159.655 1.00 79.90  ? 55   TYR A CD2 1 
ATOM   416  C CE1 . TYR A 1 55   ? 179.691 180.054 160.561 1.00 82.71  ? 55   TYR A CE1 1 
ATOM   417  C CE2 . TYR A 1 55   ? 181.476 179.339 159.142 1.00 82.89  ? 55   TYR A CE2 1 
ATOM   418  C CZ  . TYR A 1 55   ? 180.636 180.330 159.599 1.00 85.45  ? 55   TYR A CZ  1 
ATOM   419  O OH  . TYR A 1 55   ? 180.742 181.605 159.092 1.00 87.03  ? 55   TYR A OH  1 
ATOM   420  N N   . PHE A 1 56   ? 179.867 174.192 158.669 1.00 74.13  ? 56   PHE A N   1 
ATOM   421  C CA  . PHE A 1 56   ? 180.084 173.883 157.262 1.00 65.25  ? 56   PHE A CA  1 
ATOM   422  C C   . PHE A 1 56   ? 178.984 172.998 156.690 1.00 63.45  ? 56   PHE A C   1 
ATOM   423  O O   . PHE A 1 56   ? 179.220 172.255 155.733 1.00 63.15  ? 56   PHE A O   1 
ATOM   424  C CB  . PHE A 1 56   ? 181.447 173.222 157.073 1.00 63.48  ? 56   PHE A CB  1 
ATOM   425  C CG  . PHE A 1 56   ? 182.594 174.051 157.562 1.00 68.66  ? 56   PHE A CG  1 
ATOM   426  C CD1 . PHE A 1 56   ? 182.543 175.430 157.506 1.00 72.23  ? 56   PHE A CD1 1 
ATOM   427  C CD2 . PHE A 1 56   ? 183.724 173.449 158.084 1.00 68.93  ? 56   PHE A CD2 1 
ATOM   428  C CE1 . PHE A 1 56   ? 183.599 176.194 157.956 1.00 73.25  ? 56   PHE A CE1 1 
ATOM   429  C CE2 . PHE A 1 56   ? 184.782 174.207 158.536 1.00 68.64  ? 56   PHE A CE2 1 
ATOM   430  C CZ  . PHE A 1 56   ? 184.719 175.581 158.472 1.00 72.39  ? 56   PHE A CZ  1 
ATOM   431  N N   . LYS A 1 57   ? 177.787 173.059 157.264 1.00 64.20  ? 57   LYS A N   1 
ATOM   432  C CA  . LYS A 1 57   ? 176.694 172.206 156.819 1.00 64.36  ? 57   LYS A CA  1 
ATOM   433  C C   . LYS A 1 57   ? 176.233 172.611 155.427 1.00 63.43  ? 57   LYS A C   1 
ATOM   434  O O   . LYS A 1 57   ? 176.100 173.801 155.126 1.00 66.42  ? 57   LYS A O   1 
ATOM   435  C CB  . LYS A 1 57   ? 175.531 172.286 157.805 1.00 63.39  ? 57   LYS A CB  1 
ATOM   436  C CG  . LYS A 1 57   ? 174.383 171.346 157.502 1.00 63.00  ? 57   LYS A CG  1 
ATOM   437  C CD  . LYS A 1 57   ? 173.293 171.480 158.548 1.00 60.20  ? 57   LYS A CD  1 
ATOM   438  C CE  . LYS A 1 57   ? 172.147 170.526 158.283 1.00 62.52  ? 57   LYS A CE  1 
ATOM   439  N NZ  . LYS A 1 57   ? 171.049 170.698 159.271 1.00 67.92  ? 57   LYS A NZ  1 
ATOM   440  N N   . GLU A 1 58   ? 175.993 171.619 154.574 1.00 74.44  ? 58   GLU A N   1 
ATOM   441  C CA  . GLU A 1 58   ? 175.501 171.843 153.224 1.00 73.91  ? 58   GLU A CA  1 
ATOM   442  C C   . GLU A 1 58   ? 174.345 170.898 152.940 1.00 73.50  ? 58   GLU A C   1 
ATOM   443  O O   . GLU A 1 58   ? 174.272 169.799 153.495 1.00 80.67  ? 58   GLU A O   1 
ATOM   444  C CB  . GLU A 1 58   ? 176.603 171.641 152.179 1.00 73.12  ? 58   GLU A CB  1 
ATOM   445  C CG  . GLU A 1 58   ? 177.734 172.646 152.267 1.00 76.36  ? 58   GLU A CG  1 
ATOM   446  C CD  . GLU A 1 58   ? 177.295 174.050 151.901 1.00 83.15  ? 58   GLU A CD  1 
ATOM   447  O OE1 . GLU A 1 58   ? 176.287 174.192 151.178 1.00 84.17  ? 58   GLU A OE1 1 
ATOM   448  O OE2 . GLU A 1 58   ? 177.959 175.013 152.337 1.00 84.73  ? 58   GLU A OE2 1 
ATOM   449  N N   . HIS A 1 59   ? 173.444 171.334 152.068 1.00 71.83  ? 59   HIS A N   1 
ATOM   450  C CA  . HIS A 1 59   ? 172.292 170.543 151.665 1.00 70.30  ? 59   HIS A CA  1 
ATOM   451  C C   . HIS A 1 59   ? 172.383 170.212 150.183 1.00 74.12  ? 59   HIS A C   1 
ATOM   452  O O   . HIS A 1 59   ? 172.718 171.074 149.365 1.00 83.48  ? 59   HIS A O   1 
ATOM   453  C CB  . HIS A 1 59   ? 170.986 171.286 151.942 1.00 71.44  ? 59   HIS A CB  1 
ATOM   454  C CG  . HIS A 1 59   ? 170.772 171.617 153.385 1.00 76.75  ? 59   HIS A CG  1 
ATOM   455  N ND1 . HIS A 1 59   ? 169.742 172.423 153.817 1.00 82.04  ? 59   HIS A ND1 1 
ATOM   456  C CD2 . HIS A 1 59   ? 171.454 171.250 154.495 1.00 76.59  ? 59   HIS A CD2 1 
ATOM   457  C CE1 . HIS A 1 59   ? 169.798 172.540 155.131 1.00 79.11  ? 59   HIS A CE1 1 
ATOM   458  N NE2 . HIS A 1 59   ? 170.828 171.838 155.567 1.00 79.47  ? 59   HIS A NE2 1 
ATOM   459  N N   . GLU A 1 60   ? 172.086 168.963 149.842 1.00 66.11  ? 60   GLU A N   1 
ATOM   460  C CA  . GLU A 1 60   ? 172.005 168.543 148.451 1.00 70.49  ? 60   GLU A CA  1 
ATOM   461  C C   . GLU A 1 60   ? 170.559 168.666 147.991 1.00 77.16  ? 60   GLU A C   1 
ATOM   462  O O   . GLU A 1 60   ? 169.670 168.015 148.547 1.00 79.30  ? 60   GLU A O   1 
ATOM   463  C CB  . GLU A 1 60   ? 172.505 167.111 148.282 1.00 71.08  ? 60   GLU A CB  1 
ATOM   464  C CG  . GLU A 1 60   ? 172.490 166.634 146.846 1.00 74.01  ? 60   GLU A CG  1 
ATOM   465  C CD  . GLU A 1 60   ? 173.391 167.458 145.952 1.00 79.90  ? 60   GLU A CD  1 
ATOM   466  O OE1 . GLU A 1 60   ? 174.490 167.841 146.403 1.00 82.80  ? 60   GLU A OE1 1 
ATOM   467  O OE2 . GLU A 1 60   ? 172.998 167.730 144.799 1.00 78.52  ? 60   GLU A OE2 1 
ATOM   468  N N   . LYS A 1 61   ? 170.326 169.499 146.980 1.00 78.14  ? 61   LYS A N   1 
ATOM   469  C CA  . LYS A 1 61   ? 168.977 169.832 146.549 1.00 79.73  ? 61   LYS A CA  1 
ATOM   470  C C   . LYS A 1 61   ? 168.650 169.339 145.148 1.00 81.54  ? 61   LYS A C   1 
ATOM   471  O O   . LYS A 1 61   ? 167.502 169.472 144.715 1.00 85.22  ? 61   LYS A O   1 
ATOM   472  C CB  . LYS A 1 61   ? 168.769 171.348 146.626 1.00 79.08  ? 61   LYS A CB  1 
ATOM   473  C CG  . LYS A 1 61   ? 169.105 171.935 147.983 1.00 78.02  ? 61   LYS A CG  1 
ATOM   474  C CD  . LYS A 1 61   ? 169.123 173.450 147.946 1.00 79.88  ? 61   LYS A CD  1 
ATOM   475  C CE  . LYS A 1 61   ? 169.653 174.019 149.250 1.00 79.66  ? 61   LYS A CE  1 
ATOM   476  N NZ  . LYS A 1 61   ? 169.737 175.504 149.215 1.00 81.98  ? 61   LYS A NZ  1 
ATOM   477  N N   . ASP A 1 62   ? 169.616 168.776 144.431 1.00 75.63  ? 62   ASP A N   1 
ATOM   478  C CA  . ASP A 1 62   ? 169.353 168.296 143.082 1.00 74.43  ? 62   ASP A CA  1 
ATOM   479  C C   . ASP A 1 62   ? 168.545 167.006 143.136 1.00 76.56  ? 62   ASP A C   1 
ATOM   480  O O   . ASP A 1 62   ? 168.954 166.032 143.773 1.00 83.76  ? 62   ASP A O   1 
ATOM   481  C CB  . ASP A 1 62   ? 170.666 168.072 142.336 1.00 79.09  ? 62   ASP A CB  1 
ATOM   482  C CG  . ASP A 1 62   ? 170.460 167.821 140.856 1.00 81.36  ? 62   ASP A CG  1 
ATOM   483  O OD1 . ASP A 1 62   ? 169.321 167.987 140.374 1.00 82.66  ? 62   ASP A OD1 1 
ATOM   484  O OD2 . ASP A 1 62   ? 171.440 167.458 140.173 1.00 79.37  ? 62   ASP A OD2 1 
ATOM   485  N N   . ILE A 1 63   ? 167.397 167.000 142.458 1.00 71.29  ? 63   ILE A N   1 
ATOM   486  C CA  . ILE A 1 63   ? 166.531 165.826 142.478 1.00 69.40  ? 63   ILE A CA  1 
ATOM   487  C C   . ILE A 1 63   ? 167.208 164.647 141.794 1.00 66.68  ? 63   ILE A C   1 
ATOM   488  O O   . ILE A 1 63   ? 167.117 163.506 142.262 1.00 74.20  ? 63   ILE A O   1 
ATOM   489  C CB  . ILE A 1 63   ? 165.173 166.157 141.835 1.00 72.83  ? 63   ILE A CB  1 
ATOM   490  C CG1 . ILE A 1 63   ? 164.432 167.189 142.683 1.00 68.99  ? 63   ILE A CG1 1 
ATOM   491  C CG2 . ILE A 1 63   ? 164.336 164.903 141.672 1.00 74.88  ? 63   ILE A CG2 1 
ATOM   492  C CD1 . ILE A 1 63   ? 163.054 167.514 142.177 1.00 71.04  ? 63   ILE A CD1 1 
ATOM   493  N N   . TYR A 1 64   ? 167.895 164.899 140.679 1.00 69.63  ? 64   TYR A N   1 
ATOM   494  C CA  . TYR A 1 64   ? 168.635 163.833 140.012 1.00 74.16  ? 64   TYR A CA  1 
ATOM   495  C C   . TYR A 1 64   ? 169.701 163.256 140.932 1.00 79.02  ? 64   TYR A C   1 
ATOM   496  O O   . TYR A 1 64   ? 169.894 162.037 140.993 1.00 85.32  ? 64   TYR A O   1 
ATOM   497  C CB  . TYR A 1 64   ? 169.270 164.358 138.725 1.00 80.02  ? 64   TYR A CB  1 
ATOM   498  C CG  . TYR A 1 64   ? 168.291 164.641 137.611 1.00 79.70  ? 64   TYR A CG  1 
ATOM   499  C CD1 . TYR A 1 64   ? 167.549 165.813 137.593 1.00 81.58  ? 64   TYR A CD1 1 
ATOM   500  C CD2 . TYR A 1 64   ? 168.122 163.743 136.567 1.00 76.05  ? 64   TYR A CD2 1 
ATOM   501  C CE1 . TYR A 1 64   ? 166.659 166.078 136.573 1.00 81.19  ? 64   TYR A CE1 1 
ATOM   502  C CE2 . TYR A 1 64   ? 167.236 163.999 135.542 1.00 79.88  ? 64   TYR A CE2 1 
ATOM   503  C CZ  . TYR A 1 64   ? 166.508 165.169 135.549 1.00 82.72  ? 64   TYR A CZ  1 
ATOM   504  O OH  . TYR A 1 64   ? 165.621 165.430 134.531 1.00 82.19  ? 64   TYR A OH  1 
ATOM   505  N N   . LYS A 1 65   ? 170.410 164.123 141.654 1.00 68.32  ? 65   LYS A N   1 
ATOM   506  C CA  . LYS A 1 65   ? 171.427 163.652 142.586 1.00 72.56  ? 65   LYS A CA  1 
ATOM   507  C C   . LYS A 1 65   ? 170.811 162.820 143.704 1.00 71.67  ? 65   LYS A C   1 
ATOM   508  O O   . LYS A 1 65   ? 171.345 161.768 144.069 1.00 74.97  ? 65   LYS A O   1 
ATOM   509  C CB  . LYS A 1 65   ? 172.193 164.842 143.160 1.00 70.90  ? 65   LYS A CB  1 
ATOM   510  C CG  . LYS A 1 65   ? 173.401 164.471 143.997 1.00 70.66  ? 65   LYS A CG  1 
ATOM   511  C CD  . LYS A 1 65   ? 174.536 163.954 143.135 1.00 68.44  ? 65   LYS A CD  1 
ATOM   512  C CE  . LYS A 1 65   ? 175.791 163.744 143.961 1.00 72.50  ? 65   LYS A CE  1 
ATOM   513  N NZ  . LYS A 1 65   ? 176.934 163.292 143.126 1.00 75.32  ? 65   LYS A NZ  1 
ATOM   514  N N   . LEU A 1 66   ? 169.679 163.269 144.251 1.00 62.88  ? 66   LEU A N   1 
ATOM   515  C CA  . LEU A 1 66   ? 169.102 162.597 145.411 1.00 62.83  ? 66   LEU A CA  1 
ATOM   516  C C   . LEU A 1 66   ? 168.472 161.261 145.040 1.00 63.17  ? 66   LEU A C   1 
ATOM   517  O O   . LEU A 1 66   ? 168.658 160.266 145.750 1.00 66.61  ? 66   LEU A O   1 
ATOM   518  C CB  . LEU A 1 66   ? 168.062 163.495 146.076 1.00 59.79  ? 66   LEU A CB  1 
ATOM   519  C CG  . LEU A 1 66   ? 168.552 164.799 146.696 1.00 59.08  ? 66   LEU A CG  1 
ATOM   520  C CD1 . LEU A 1 66   ? 167.411 165.503 147.396 1.00 62.45  ? 66   LEU A CD1 1 
ATOM   521  C CD2 . LEU A 1 66   ? 169.679 164.525 147.660 1.00 59.95  ? 66   LEU A CD2 1 
ATOM   522  N N   . TYR A 1 67   ? 167.723 161.213 143.947 1.00 66.24  ? 67   TYR A N   1 
ATOM   523  C CA  . TYR A 1 67   ? 166.836 160.085 143.697 1.00 65.32  ? 67   TYR A CA  1 
ATOM   524  C C   . TYR A 1 67   ? 167.221 159.250 142.488 1.00 65.71  ? 67   TYR A C   1 
ATOM   525  O O   . TYR A 1 67   ? 166.995 158.039 142.489 1.00 73.19  ? 67   TYR A O   1 
ATOM   526  C CB  . TYR A 1 67   ? 165.399 160.593 143.527 1.00 63.19  ? 67   TYR A CB  1 
ATOM   527  C CG  . TYR A 1 67   ? 164.333 159.571 143.839 1.00 64.19  ? 67   TYR A CG  1 
ATOM   528  C CD1 . TYR A 1 67   ? 163.945 159.324 145.146 1.00 62.89  ? 67   TYR A CD1 1 
ATOM   529  C CD2 . TYR A 1 67   ? 163.708 158.862 142.826 1.00 69.06  ? 67   TYR A CD2 1 
ATOM   530  C CE1 . TYR A 1 67   ? 162.967 158.395 145.436 1.00 66.50  ? 67   TYR A CE1 1 
ATOM   531  C CE2 . TYR A 1 67   ? 162.727 157.934 143.107 1.00 68.63  ? 67   TYR A CE2 1 
ATOM   532  C CZ  . TYR A 1 67   ? 162.362 157.702 144.413 1.00 69.05  ? 67   TYR A CZ  1 
ATOM   533  O OH  . TYR A 1 67   ? 161.386 156.775 144.693 1.00 68.85  ? 67   TYR A OH  1 
ATOM   534  N N   . SER A 1 68   ? 167.791 159.856 141.452 1.00 75.64  ? 68   SER A N   1 
ATOM   535  C CA  . SER A 1 68   ? 168.108 159.118 140.241 1.00 79.57  ? 68   SER A CA  1 
ATOM   536  C C   . SER A 1 68   ? 169.382 158.305 140.417 1.00 80.14  ? 68   SER A C   1 
ATOM   537  O O   . SER A 1 68   ? 170.193 158.561 141.310 1.00 78.84  ? 68   SER A O   1 
ATOM   538  C CB  . SER A 1 68   ? 168.271 160.066 139.055 1.00 83.36  ? 68   SER A CB  1 
ATOM   539  O OG  . SER A 1 68   ? 169.485 160.789 139.147 1.00 82.49  ? 68   SER A OG  1 
ATOM   540  N N   . ILE A 1 69   ? 169.553 157.313 139.542 1.00 84.20  ? 69   ILE A N   1 
ATOM   541  C CA  . ILE A 1 69   ? 170.785 156.540 139.532 1.00 86.27  ? 69   ILE A CA  1 
ATOM   542  C C   . ILE A 1 69   ? 171.925 157.392 138.982 1.00 89.79  ? 69   ILE A C   1 
ATOM   543  O O   . ILE A 1 69   ? 171.720 158.453 138.381 1.00 91.51  ? 69   ILE A O   1 
ATOM   544  C CB  . ILE A 1 69   ? 170.604 155.253 138.714 1.00 85.62  ? 69   ILE A CB  1 
ATOM   545  C CG1 . ILE A 1 69   ? 169.162 154.764 138.822 1.00 87.51  ? 69   ILE A CG1 1 
ATOM   546  C CG2 . ILE A 1 69   ? 171.543 154.169 139.203 1.00 86.20  ? 69   ILE A CG2 1 
ATOM   547  C CD1 . ILE A 1 69   ? 168.868 153.565 137.957 1.00 90.69  ? 69   ILE A CD1 1 
ATOM   548  N N   . SER A 1 70   ? 173.154 156.918 139.202 1.00 98.60  ? 70   SER A N   1 
ATOM   549  C CA  . SER A 1 70   ? 174.324 157.659 138.742 1.00 100.11 ? 70   SER A CA  1 
ATOM   550  C C   . SER A 1 70   ? 174.352 157.772 137.223 1.00 100.77 ? 70   SER A C   1 
ATOM   551  O O   . SER A 1 70   ? 174.650 158.840 136.677 1.00 102.38 ? 70   SER A O   1 
ATOM   552  C CB  . SER A 1 70   ? 175.599 156.990 139.253 1.00 100.40 ? 70   SER A CB  1 
ATOM   553  O OG  . SER A 1 70   ? 175.682 155.649 138.806 1.00 101.24 ? 70   SER A OG  1 
ATOM   554  N N   . ASN A 1 71   ? 174.040 156.685 136.523 1.00 101.34 ? 71   ASN A N   1 
ATOM   555  C CA  . ASN A 1 71   ? 174.063 156.642 135.065 1.00 101.09 ? 71   ASN A CA  1 
ATOM   556  C C   . ASN A 1 71   ? 172.655 156.521 134.490 1.00 100.95 ? 71   ASN A C   1 
ATOM   557  O O   . ASN A 1 71   ? 172.413 155.759 133.554 1.00 104.36 ? 71   ASN A O   1 
ATOM   558  C CB  . ASN A 1 71   ? 174.942 155.497 134.573 1.00 102.80 ? 71   ASN A CB  1 
ATOM   559  C CG  . ASN A 1 71   ? 174.517 154.155 135.132 1.00 103.95 ? 71   ASN A CG  1 
ATOM   560  O OD1 . ASN A 1 71   ? 173.740 153.429 134.513 1.00 103.65 ? 71   ASN A OD1 1 
ATOM   561  N ND2 . ASN A 1 71   ? 175.025 153.817 136.311 1.00 104.10 ? 71   ASN A ND2 1 
ATOM   562  N N   . SER A 1 72   ? 171.713 157.270 135.059 1.00 91.01  ? 72   SER A N   1 
ATOM   563  C CA  . SER A 1 72   ? 170.323 157.191 134.629 1.00 89.58  ? 72   SER A CA  1 
ATOM   564  C C   . SER A 1 72   ? 170.189 157.544 133.156 1.00 85.88  ? 72   SER A C   1 
ATOM   565  O O   . SER A 1 72   ? 170.748 158.540 132.689 1.00 91.13  ? 72   SER A O   1 
ATOM   566  C CB  . SER A 1 72   ? 169.462 158.129 135.473 1.00 89.44  ? 72   SER A CB  1 
ATOM   567  O OG  . SER A 1 72   ? 168.148 158.213 134.953 1.00 91.61  ? 72   SER A OG  1 
ATOM   568  N N   . TYR A 1 73   ? 169.445 156.718 132.419 1.00 81.57  ? 73   TYR A N   1 
ATOM   569  C CA  . TYR A 1 73   ? 169.197 157.010 131.014 1.00 84.20  ? 73   TYR A CA  1 
ATOM   570  C C   . TYR A 1 73   ? 168.180 158.128 130.841 1.00 85.70  ? 73   TYR A C   1 
ATOM   571  O O   . TYR A 1 73   ? 168.192 158.815 129.814 1.00 89.99  ? 73   TYR A O   1 
ATOM   572  C CB  . TYR A 1 73   ? 168.726 155.757 130.280 1.00 87.29  ? 73   TYR A CB  1 
ATOM   573  C CG  . TYR A 1 73   ? 168.554 155.973 128.795 1.00 89.31  ? 73   TYR A CG  1 
ATOM   574  C CD1 . TYR A 1 73   ? 169.653 156.015 127.951 1.00 88.67  ? 73   TYR A CD1 1 
ATOM   575  C CD2 . TYR A 1 73   ? 167.295 156.146 128.240 1.00 89.71  ? 73   TYR A CD2 1 
ATOM   576  C CE1 . TYR A 1 73   ? 169.503 156.218 126.595 1.00 88.45  ? 73   TYR A CE1 1 
ATOM   577  C CE2 . TYR A 1 73   ? 167.136 156.348 126.885 1.00 89.40  ? 73   TYR A CE2 1 
ATOM   578  C CZ  . TYR A 1 73   ? 168.244 156.384 126.067 1.00 89.08  ? 73   TYR A CZ  1 
ATOM   579  O OH  . TYR A 1 73   ? 168.093 156.588 124.716 1.00 88.22  ? 73   TYR A OH  1 
ATOM   580  N N   . ALA A 1 74   ? 167.295 158.319 131.819 1.00 77.30  ? 74   ALA A N   1 
ATOM   581  C CA  . ALA A 1 74   ? 166.378 159.451 131.766 1.00 71.29  ? 74   ALA A CA  1 
ATOM   582  C C   . ALA A 1 74   ? 167.142 160.765 131.771 1.00 73.17  ? 74   ALA A C   1 
ATOM   583  O O   . ALA A 1 74   ? 166.749 161.724 131.098 1.00 81.79  ? 74   ALA A O   1 
ATOM   584  C CB  . ALA A 1 74   ? 165.399 159.392 132.936 1.00 75.37  ? 74   ALA A CB  1 
ATOM   585  N N   . TYR A 1 75   ? 168.240 160.827 132.524 1.00 73.89  ? 75   TYR A N   1 
ATOM   586  C CA  . TYR A 1 75   ? 169.081 162.018 132.517 1.00 75.33  ? 75   TYR A CA  1 
ATOM   587  C C   . TYR A 1 75   ? 169.665 162.265 131.132 1.00 79.96  ? 75   TYR A C   1 
ATOM   588  O O   . TYR A 1 75   ? 169.687 163.401 130.647 1.00 85.97  ? 75   TYR A O   1 
ATOM   589  C CB  . TYR A 1 75   ? 170.191 161.873 133.556 1.00 75.50  ? 75   TYR A CB  1 
ATOM   590  C CG  . TYR A 1 75   ? 171.153 163.034 133.601 1.00 79.03  ? 75   TYR A CG  1 
ATOM   591  C CD1 . TYR A 1 75   ? 170.858 164.175 134.332 1.00 79.41  ? 75   TYR A CD1 1 
ATOM   592  C CD2 . TYR A 1 75   ? 172.360 162.987 132.920 1.00 78.02  ? 75   TYR A CD2 1 
ATOM   593  C CE1 . TYR A 1 75   ? 171.735 165.238 134.379 1.00 80.53  ? 75   TYR A CE1 1 
ATOM   594  C CE2 . TYR A 1 75   ? 173.242 164.045 132.960 1.00 77.91  ? 75   TYR A CE2 1 
ATOM   595  C CZ  . TYR A 1 75   ? 172.925 165.168 133.691 1.00 79.96  ? 75   TYR A CZ  1 
ATOM   596  O OH  . TYR A 1 75   ? 173.804 166.225 133.733 1.00 78.64  ? 75   TYR A OH  1 
ATOM   597  N N   . GLU A 1 76   ? 170.140 161.204 130.477 1.00 70.59  ? 76   GLU A N   1 
ATOM   598  C CA  . GLU A 1 76   ? 170.689 161.348 129.133 1.00 66.08  ? 76   GLU A CA  1 
ATOM   599  C C   . GLU A 1 76   ? 169.622 161.812 128.151 1.00 71.43  ? 76   GLU A C   1 
ATOM   600  O O   . GLU A 1 76   ? 169.880 162.667 127.295 1.00 79.55  ? 76   GLU A O   1 
ATOM   601  C CB  . GLU A 1 76   ? 171.297 160.024 128.675 1.00 74.24  ? 76   GLU A CB  1 
ATOM   602  C CG  . GLU A 1 76   ? 172.246 160.143 127.499 1.00 81.31  ? 76   GLU A CG  1 
ATOM   603  C CD  . GLU A 1 76   ? 173.616 160.644 127.910 1.00 84.80  ? 76   GLU A CD  1 
ATOM   604  O OE1 . GLU A 1 76   ? 173.919 160.617 129.121 1.00 82.04  ? 76   GLU A OE1 1 
ATOM   605  O OE2 . GLU A 1 76   ? 174.390 161.064 127.024 1.00 81.50  ? 76   GLU A OE2 1 
ATOM   606  N N   . THR A 1 77   ? 168.416 161.254 128.259 1.00 63.42  ? 77   THR A N   1 
ATOM   607  C CA  . THR A 1 77   ? 167.329 161.663 127.377 1.00 56.51  ? 77   THR A CA  1 
ATOM   608  C C   . THR A 1 77   ? 166.960 163.122 127.600 1.00 60.42  ? 77   THR A C   1 
ATOM   609  O O   . THR A 1 77   ? 166.730 163.865 126.639 1.00 71.91  ? 77   THR A O   1 
ATOM   610  C CB  . THR A 1 77   ? 166.114 160.765 127.592 1.00 59.48  ? 77   THR A CB  1 
ATOM   611  O OG1 . THR A 1 77   ? 166.474 159.404 127.330 1.00 65.28  ? 77   THR A OG1 1 
ATOM   612  C CG2 . THR A 1 77   ? 164.991 161.167 126.662 1.00 63.49  ? 77   THR A CG2 1 
ATOM   613  N N   . ASN A 1 78   ? 166.897 163.553 128.861 1.00 58.53  ? 78   ASN A N   1 
ATOM   614  C CA  . ASN A 1 78   ? 166.608 164.954 129.147 1.00 59.47  ? 78   ASN A CA  1 
ATOM   615  C C   . ASN A 1 78   ? 167.693 165.858 128.583 1.00 63.39  ? 78   ASN A C   1 
ATOM   616  O O   . ASN A 1 78   ? 167.399 166.928 128.035 1.00 72.78  ? 78   ASN A O   1 
ATOM   617  C CB  . ASN A 1 78   ? 166.464 165.163 130.653 1.00 60.63  ? 78   ASN A CB  1 
ATOM   618  C CG  . ASN A 1 78   ? 166.124 166.593 131.012 1.00 63.58  ? 78   ASN A CG  1 
ATOM   619  O OD1 . ASN A 1 78   ? 165.494 167.305 130.233 1.00 67.55  ? 78   ASN A OD1 1 
ATOM   620  N ND2 . ASN A 1 78   ? 166.542 167.022 132.195 1.00 69.27  ? 78   ASN A ND2 1 
ATOM   621  N N   . GLU A 1 79   ? 168.955 165.443 128.707 1.00 71.91  ? 79   GLU A N   1 
ATOM   622  C CA  . GLU A 1 79   ? 170.045 166.225 128.136 1.00 69.81  ? 79   GLU A CA  1 
ATOM   623  C C   . GLU A 1 79   ? 169.899 166.349 126.627 1.00 69.54  ? 79   GLU A C   1 
ATOM   624  O O   . GLU A 1 79   ? 170.067 167.437 126.070 1.00 79.79  ? 79   GLU A O   1 
ATOM   625  C CB  . GLU A 1 79   ? 171.387 165.591 128.493 1.00 70.58  ? 79   GLU A CB  1 
ATOM   626  C CG  . GLU A 1 79   ? 171.777 165.748 129.949 1.00 77.74  ? 79   GLU A CG  1 
ATOM   627  C CD  . GLU A 1 79   ? 172.908 166.735 130.143 1.00 86.56  ? 79   GLU A CD  1 
ATOM   628  O OE1 . GLU A 1 79   ? 173.610 167.037 129.155 1.00 86.34  ? 79   GLU A OE1 1 
ATOM   629  O OE2 . GLU A 1 79   ? 173.096 167.208 131.283 1.00 87.00  ? 79   GLU A OE2 1 
ATOM   630  N N   . THR A 1 80   ? 169.572 165.247 125.950 1.00 51.07  ? 80   THR A N   1 
ATOM   631  C CA  . THR A 1 80   ? 169.400 165.299 124.501 1.00 48.44  ? 80   THR A CA  1 
ATOM   632  C C   . THR A 1 80   ? 168.244 166.212 124.115 1.00 52.90  ? 80   THR A C   1 
ATOM   633  O O   . THR A 1 80   ? 168.362 167.024 123.186 1.00 65.37  ? 80   THR A O   1 
ATOM   634  C CB  . THR A 1 80   ? 169.176 163.894 123.948 1.00 47.44  ? 80   THR A CB  1 
ATOM   635  O OG1 . THR A 1 80   ? 170.281 163.057 124.307 1.00 55.32  ? 80   THR A OG1 1 
ATOM   636  C CG2 . THR A 1 80   ? 169.058 163.934 122.440 1.00 49.75  ? 80   THR A CG2 1 
ATOM   637  N N   . ILE A 1 81   ? 167.122 166.102 124.826 1.00 50.24  ? 81   ILE A N   1 
ATOM   638  C CA  . ILE A 1 81   ? 165.953 166.919 124.515 1.00 45.02  ? 81   ILE A CA  1 
ATOM   639  C C   . ILE A 1 81   ? 166.281 168.395 124.683 1.00 55.36  ? 81   ILE A C   1 
ATOM   640  O O   . ILE A 1 81   ? 165.944 169.225 123.832 1.00 65.78  ? 81   ILE A O   1 
ATOM   641  C CB  . ILE A 1 81   ? 164.762 166.506 125.394 1.00 42.22  ? 81   ILE A CB  1 
ATOM   642  C CG1 . ILE A 1 81   ? 164.336 165.076 125.081 1.00 48.57  ? 81   ILE A CG1 1 
ATOM   643  C CG2 . ILE A 1 81   ? 163.603 167.455 125.190 1.00 47.81  ? 81   ILE A CG2 1 
ATOM   644  C CD1 . ILE A 1 81   ? 163.424 164.483 126.121 1.00 57.21  ? 81   ILE A CD1 1 
ATOM   645  N N   . ASN A 1 82   ? 166.949 168.744 125.784 1.00 57.43  ? 82   ASN A N   1 
ATOM   646  C CA  . ASN A 1 82   ? 167.300 170.141 126.006 1.00 56.55  ? 82   ASN A CA  1 
ATOM   647  C C   . ASN A 1 82   ? 168.343 170.625 125.011 1.00 58.51  ? 82   ASN A C   1 
ATOM   648  O O   . ASN A 1 82   ? 168.359 171.810 124.662 1.00 65.84  ? 82   ASN A O   1 
ATOM   649  C CB  . ASN A 1 82   ? 167.799 170.338 127.434 1.00 55.71  ? 82   ASN A CB  1 
ATOM   650  C CG  . ASN A 1 82   ? 166.700 170.178 128.456 1.00 60.07  ? 82   ASN A CG  1 
ATOM   651  O OD1 . ASN A 1 82   ? 166.008 171.137 128.794 1.00 64.22  ? 82   ASN A OD1 1 
ATOM   652  N ND2 . ASN A 1 82   ? 166.528 168.961 128.954 1.00 65.48  ? 82   ASN A ND2 1 
ATOM   653  N N   . ASP A 1 83   ? 169.218 169.735 124.544 1.00 57.25  ? 83   ASP A N   1 
ATOM   654  C CA  . ASP A 1 83   ? 170.267 170.154 123.624 1.00 55.47  ? 83   ASP A CA  1 
ATOM   655  C C   . ASP A 1 83   ? 169.726 170.387 122.222 1.00 52.70  ? 83   ASP A C   1 
ATOM   656  O O   . ASP A 1 83   ? 170.233 171.248 121.497 1.00 63.33  ? 83   ASP A O   1 
ATOM   657  C CB  . ASP A 1 83   ? 171.386 169.117 123.593 1.00 56.04  ? 83   ASP A CB  1 
ATOM   658  C CG  . ASP A 1 83   ? 172.236 169.144 124.842 1.00 65.65  ? 83   ASP A CG  1 
ATOM   659  O OD1 . ASP A 1 83   ? 172.341 170.219 125.467 1.00 66.90  ? 83   ASP A OD1 1 
ATOM   660  O OD2 . ASP A 1 83   ? 172.802 168.090 125.199 1.00 65.54  ? 83   ASP A OD2 1 
ATOM   661  N N   . PHE A 1 84   ? 168.709 169.631 121.810 1.00 47.90  ? 84   PHE A N   1 
ATOM   662  C CA  . PHE A 1 84   ? 168.285 169.676 120.418 1.00 52.04  ? 84   PHE A CA  1 
ATOM   663  C C   . PHE A 1 84   ? 166.838 170.091 120.195 1.00 50.07  ? 84   PHE A C   1 
ATOM   664  O O   . PHE A 1 84   ? 166.403 170.131 119.040 1.00 54.21  ? 84   PHE A O   1 
ATOM   665  C CB  . PHE A 1 84   ? 168.531 168.317 119.757 1.00 47.64  ? 84   PHE A CB  1 
ATOM   666  C CG  . PHE A 1 84   ? 169.980 167.960 119.655 1.00 49.67  ? 84   PHE A CG  1 
ATOM   667  C CD1 . PHE A 1 84   ? 170.726 168.362 118.566 1.00 50.25  ? 84   PHE A CD1 1 
ATOM   668  C CD2 . PHE A 1 84   ? 170.599 167.235 120.653 1.00 50.85  ? 84   PHE A CD2 1 
ATOM   669  C CE1 . PHE A 1 84   ? 172.060 168.040 118.470 1.00 52.70  ? 84   PHE A CE1 1 
ATOM   670  C CE2 . PHE A 1 84   ? 171.934 166.910 120.562 1.00 49.63  ? 84   PHE A CE2 1 
ATOM   671  C CZ  . PHE A 1 84   ? 172.665 167.313 119.469 1.00 49.26  ? 84   PHE A CZ  1 
ATOM   672  N N   . PHE A 1 85   ? 166.081 170.409 121.240 1.00 40.12  ? 85   PHE A N   1 
ATOM   673  C CA  . PHE A 1 85   ? 164.707 170.858 121.072 1.00 42.85  ? 85   PHE A CA  1 
ATOM   674  C C   . PHE A 1 85   ? 164.443 172.087 121.927 1.00 49.41  ? 85   PHE A C   1 
ATOM   675  O O   . PHE A 1 85   ? 165.062 172.282 122.976 1.00 54.66  ? 85   PHE A O   1 
ATOM   676  C CB  . PHE A 1 85   ? 163.705 169.758 121.421 1.00 41.56  ? 85   PHE A CB  1 
ATOM   677  C CG  . PHE A 1 85   ? 163.325 168.902 120.253 1.00 44.40  ? 85   PHE A CG  1 
ATOM   678  C CD1 . PHE A 1 85   ? 162.573 169.425 119.219 1.00 39.67  ? 85   PHE A CD1 1 
ATOM   679  C CD2 . PHE A 1 85   ? 163.716 167.580 120.187 1.00 41.39  ? 85   PHE A CD2 1 
ATOM   680  C CE1 . PHE A 1 85   ? 162.222 168.647 118.142 1.00 39.82  ? 85   PHE A CE1 1 
ATOM   681  C CE2 . PHE A 1 85   ? 163.365 166.798 119.111 1.00 40.45  ? 85   PHE A CE2 1 
ATOM   682  C CZ  . PHE A 1 85   ? 162.619 167.332 118.088 1.00 43.96  ? 85   PHE A CZ  1 
ATOM   683  N N   . TYR A 1 86   ? 163.511 172.916 121.463 1.00 61.86  ? 86   TYR A N   1 
ATOM   684  C CA  . TYR A 1 86   ? 163.138 174.152 122.148 1.00 58.77  ? 86   TYR A CA  1 
ATOM   685  C C   . TYR A 1 86   ? 161.901 173.879 122.994 1.00 65.79  ? 86   TYR A C   1 
ATOM   686  O O   . TYR A 1 86   ? 160.769 174.073 122.551 1.00 68.73  ? 86   TYR A O   1 
ATOM   687  C CB  . TYR A 1 86   ? 162.882 175.277 121.154 1.00 57.62  ? 86   TYR A CB  1 
ATOM   688  C CG  . TYR A 1 86   ? 164.129 175.943 120.628 1.00 66.70  ? 86   TYR A CG  1 
ATOM   689  C CD1 . TYR A 1 86   ? 164.905 176.752 121.446 1.00 67.15  ? 86   TYR A CD1 1 
ATOM   690  C CD2 . TYR A 1 86   ? 164.519 175.779 119.309 1.00 63.08  ? 86   TYR A CD2 1 
ATOM   691  C CE1 . TYR A 1 86   ? 166.042 177.368 120.966 1.00 65.55  ? 86   TYR A CE1 1 
ATOM   692  C CE2 . TYR A 1 86   ? 165.651 176.391 118.821 1.00 65.58  ? 86   TYR A CE2 1 
ATOM   693  C CZ  . TYR A 1 86   ? 166.409 177.182 119.652 1.00 69.20  ? 86   TYR A CZ  1 
ATOM   694  O OH  . TYR A 1 86   ? 167.538 177.789 119.159 1.00 68.27  ? 86   TYR A OH  1 
ATOM   695  N N   . LYS A 1 87   ? 162.120 173.428 124.221 1.00 78.20  ? 87   LYS A N   1 
ATOM   696  C CA  . LYS A 1 87   ? 161.038 173.327 125.183 1.00 73.47  ? 87   LYS A CA  1 
ATOM   697  C C   . LYS A 1 87   ? 160.743 174.701 125.769 1.00 74.60  ? 87   LYS A C   1 
ATOM   698  O O   . LYS A 1 87   ? 161.560 175.621 125.701 1.00 76.92  ? 87   LYS A O   1 
ATOM   699  C CB  . LYS A 1 87   ? 161.384 172.344 126.299 1.00 71.11  ? 87   LYS A CB  1 
ATOM   700  C CG  . LYS A 1 87   ? 161.580 170.920 125.830 1.00 71.02  ? 87   LYS A CG  1 
ATOM   701  C CD  . LYS A 1 87   ? 161.662 169.972 127.009 1.00 75.44  ? 87   LYS A CD  1 
ATOM   702  C CE  . LYS A 1 87   ? 160.386 170.018 127.828 1.00 75.67  ? 87   LYS A CE  1 
ATOM   703  N NZ  . LYS A 1 87   ? 159.196 169.691 126.997 1.00 75.42  ? 87   LYS A NZ  1 
ATOM   704  N N   . SER A 1 88   ? 159.552 174.836 126.339 1.00 63.81  ? 88   SER A N   1 
ATOM   705  C CA  . SER A 1 88   ? 159.136 176.077 126.971 1.00 61.34  ? 88   SER A CA  1 
ATOM   706  C C   . SER A 1 88   ? 158.655 175.789 128.383 1.00 64.88  ? 88   SER A C   1 
ATOM   707  O O   . SER A 1 88   ? 157.892 174.845 128.605 1.00 69.49  ? 88   SER A O   1 
ATOM   708  C CB  . SER A 1 88   ? 158.027 176.762 126.172 1.00 66.20  ? 88   SER A CB  1 
ATOM   709  O OG  . SER A 1 88   ? 156.873 175.944 126.105 1.00 72.77  ? 88   SER A OG  1 
ATOM   710  N N   . ARG A 1 89   ? 159.114 176.598 129.334 1.00 64.30  ? 89   ARG A N   1 
ATOM   711  C CA  . ARG A 1 89   ? 158.618 176.489 130.697 1.00 60.20  ? 89   ARG A CA  1 
ATOM   712  C C   . ARG A 1 89   ? 157.124 176.767 130.720 1.00 65.43  ? 89   ARG A C   1 
ATOM   713  O O   . ARG A 1 89   ? 156.637 177.664 130.033 1.00 71.65  ? 89   ARG A O   1 
ATOM   714  C CB  . ARG A 1 89   ? 159.351 177.469 131.610 1.00 62.98  ? 89   ARG A CB  1 
ATOM   715  C CG  . ARG A 1 89   ? 160.813 177.142 131.829 1.00 63.75  ? 89   ARG A CG  1 
ATOM   716  C CD  . ARG A 1 89   ? 161.507 178.247 132.603 1.00 67.54  ? 89   ARG A CD  1 
ATOM   717  N NE  . ARG A 1 89   ? 162.780 177.804 133.157 1.00 70.33  ? 89   ARG A NE  1 
ATOM   718  C CZ  . ARG A 1 89   ? 162.934 177.341 134.389 1.00 69.92  ? 89   ARG A CZ  1 
ATOM   719  N NH1 . ARG A 1 89   ? 161.917 177.260 135.229 1.00 69.15  ? 89   ARG A NH1 1 
ATOM   720  N NH2 . ARG A 1 89   ? 164.140 176.948 134.787 1.00 68.80  ? 89   ARG A NH2 1 
ATOM   721  N N   . ARG A 1 90   ? 156.389 175.990 131.505 1.00 67.18  ? 90   ARG A N   1 
ATOM   722  C CA  . ARG A 1 90   ? 154.942 176.120 131.577 1.00 64.69  ? 90   ARG A CA  1 
ATOM   723  C C   . ARG A 1 90   ? 154.530 176.376 133.016 1.00 68.04  ? 90   ARG A C   1 
ATOM   724  O O   . ARG A 1 90   ? 154.756 175.533 133.889 1.00 74.90  ? 90   ARG A O   1 
ATOM   725  C CB  . ARG A 1 90   ? 154.254 174.866 131.033 1.00 67.54  ? 90   ARG A CB  1 
ATOM   726  C CG  . ARG A 1 90   ? 154.561 174.596 129.569 1.00 65.75  ? 90   ARG A CG  1 
ATOM   727  C CD  . ARG A 1 90   ? 154.276 173.155 129.186 1.00 68.74  ? 90   ARG A CD  1 
ATOM   728  N NE  . ARG A 1 90   ? 152.856 172.836 129.254 1.00 75.00  ? 90   ARG A NE  1 
ATOM   729  C CZ  . ARG A 1 90   ? 151.999 173.030 128.261 1.00 76.74  ? 90   ARG A CZ  1 
ATOM   730  N NH1 . ARG A 1 90   ? 152.384 173.554 127.110 1.00 75.34  ? 90   ARG A NH1 1 
ATOM   731  N NH2 . ARG A 1 90   ? 150.725 172.688 128.427 1.00 68.90  ? 90   ARG A NH2 1 
ATOM   732  N N   . CYS A 1 91   ? 153.926 177.534 133.259 1.00 57.92  ? 91   CYS A N   1 
ATOM   733  C CA  . CYS A 1 91   ? 153.413 177.888 134.574 1.00 53.01  ? 91   CYS A CA  1 
ATOM   734  C C   . CYS A 1 91   ? 151.912 177.644 134.588 1.00 59.96  ? 91   CYS A C   1 
ATOM   735  O O   . CYS A 1 91   ? 151.178 178.248 133.800 1.00 66.87  ? 91   CYS A O   1 
ATOM   736  C CB  . CYS A 1 91   ? 153.727 179.345 134.903 1.00 53.69  ? 91   CYS A CB  1 
ATOM   737  S SG  . CYS A 1 91   ? 155.465 179.779 134.731 1.00 77.62  ? 91   CYS A SG  1 
ATOM   738  N N   . PHE A 1 92   ? 151.461 176.758 135.468 1.00 47.16  ? 92   PHE A N   1 
ATOM   739  C CA  . PHE A 1 92   ? 150.053 176.412 135.581 1.00 42.53  ? 92   PHE A CA  1 
ATOM   740  C C   . PHE A 1 92   ? 149.437 177.175 136.742 1.00 47.67  ? 92   PHE A C   1 
ATOM   741  O O   . PHE A 1 92   ? 149.950 177.124 137.864 1.00 64.32  ? 92   PHE A O   1 
ATOM   742  C CB  . PHE A 1 92   ? 149.875 174.910 135.794 1.00 51.33  ? 92   PHE A CB  1 
ATOM   743  C CG  . PHE A 1 92   ? 150.400 174.070 134.671 1.00 55.34  ? 92   PHE A CG  1 
ATOM   744  C CD1 . PHE A 1 92   ? 149.583 173.718 133.615 1.00 54.55  ? 92   PHE A CD1 1 
ATOM   745  C CD2 . PHE A 1 92   ? 151.708 173.623 134.677 1.00 56.62  ? 92   PHE A CD2 1 
ATOM   746  C CE1 . PHE A 1 92   ? 150.060 172.944 132.583 1.00 53.64  ? 92   PHE A CE1 1 
ATOM   747  C CE2 . PHE A 1 92   ? 152.190 172.847 133.647 1.00 61.29  ? 92   PHE A CE2 1 
ATOM   748  C CZ  . PHE A 1 92   ? 151.365 172.507 132.599 1.00 59.88  ? 92   PHE A CZ  1 
ATOM   749  N N   . ILE A 1 93   ? 148.316 177.842 136.489 1.00 40.16  ? 93   ILE A N   1 
ATOM   750  C CA  . ILE A 1 93   ? 147.612 178.550 137.548 1.00 42.97  ? 93   ILE A CA  1 
ATOM   751  C C   . ILE A 1 93   ? 146.176 178.063 137.592 1.00 53.11  ? 93   ILE A C   1 
ATOM   752  O O   . ILE A 1 93   ? 145.390 178.389 136.705 1.00 60.50  ? 93   ILE A O   1 
ATOM   753  C CB  . ILE A 1 93   ? 147.619 180.063 137.317 1.00 45.59  ? 93   ILE A CB  1 
ATOM   754  C CG1 . ILE A 1 93   ? 149.050 180.568 137.126 1.00 50.11  ? 93   ILE A CG1 1 
ATOM   755  C CG2 . ILE A 1 93   ? 146.949 180.778 138.479 1.00 48.14  ? 93   ILE A CG2 1 
ATOM   756  C CD1 . ILE A 1 93   ? 149.139 182.060 136.900 1.00 53.67  ? 93   ILE A CD1 1 
ATOM   757  N N   . LEU A 1 94   ? 145.821 177.287 138.609 1.00 46.28  ? 94   LEU A N   1 
ATOM   758  C CA  . LEU A 1 94   ? 144.477 176.718 138.688 1.00 40.13  ? 94   LEU A CA  1 
ATOM   759  C C   . LEU A 1 94   ? 143.629 177.389 139.748 1.00 49.38  ? 94   LEU A C   1 
ATOM   760  O O   . LEU A 1 94   ? 144.133 177.749 140.806 1.00 64.28  ? 94   LEU A O   1 
ATOM   761  C CB  . LEU A 1 94   ? 144.562 175.221 138.982 1.00 45.45  ? 94   LEU A CB  1 
ATOM   762  C CG  . LEU A 1 94   ? 143.255 174.457 139.184 1.00 46.60  ? 94   LEU A CG  1 
ATOM   763  C CD1 . LEU A 1 94   ? 142.376 174.563 137.948 1.00 51.88  ? 94   LEU A CD1 1 
ATOM   764  C CD2 . LEU A 1 94   ? 143.547 173.002 139.507 1.00 44.87  ? 94   LEU A CD2 1 
ATOM   765  N N   . VAL A 1 95   ? 142.343 177.562 139.471 1.00 48.21  ? 95   VAL A N   1 
ATOM   766  C CA  . VAL A 1 95   ? 141.442 178.157 140.447 1.00 40.35  ? 95   VAL A CA  1 
ATOM   767  C C   . VAL A 1 95   ? 140.285 177.217 140.747 1.00 51.47  ? 95   VAL A C   1 
ATOM   768  O O   . VAL A 1 95   ? 139.551 176.835 139.842 1.00 69.11  ? 95   VAL A O   1 
ATOM   769  C CB  . VAL A 1 95   ? 140.879 179.489 139.943 1.00 36.85  ? 95   VAL A CB  1 
ATOM   770  C CG1 . VAL A 1 95   ? 139.967 180.104 140.989 1.00 49.55  ? 95   VAL A CG1 1 
ATOM   771  C CG2 . VAL A 1 95   ? 142.008 180.439 139.584 1.00 44.49  ? 95   VAL A CG2 1 
ATOM   772  N N   . GLU A 1 96   ? 140.116 176.841 142.008 1.00 52.29  ? 96   GLU A N   1 
ATOM   773  C CA  . GLU A 1 96   ? 139.051 175.919 142.381 1.00 52.61  ? 96   GLU A CA  1 
ATOM   774  C C   . GLU A 1 96   ? 137.919 176.647 143.074 1.00 62.00  ? 96   GLU A C   1 
ATOM   775  O O   . GLU A 1 96   ? 138.135 177.704 143.661 1.00 76.58  ? 96   GLU A O   1 
ATOM   776  C CB  . GLU A 1 96   ? 139.586 174.854 143.323 1.00 50.51  ? 96   GLU A CB  1 
ATOM   777  C CG  . GLU A 1 96   ? 141.027 174.454 143.077 1.00 57.30  ? 96   GLU A CG  1 
ATOM   778  C CD  . GLU A 1 96   ? 141.538 173.519 144.152 1.00 70.37  ? 96   GLU A CD  1 
ATOM   779  O OE1 . GLU A 1 96   ? 140.706 172.975 144.908 1.00 68.89  ? 96   GLU A OE1 1 
ATOM   780  O OE2 . GLU A 1 96   ? 142.766 173.328 144.242 1.00 76.82  ? 96   GLU A OE2 1 
ATOM   781  N N   . SER A 1 97   ? 136.713 176.090 143.021 1.00 50.99  ? 97   SER A N   1 
ATOM   782  C CA  . SER A 1 97   ? 135.585 176.700 143.712 1.00 48.13  ? 97   SER A CA  1 
ATOM   783  C C   . SER A 1 97   ? 134.361 175.809 143.784 1.00 55.49  ? 97   SER A C   1 
ATOM   784  O O   . SER A 1 97   ? 134.016 175.150 142.809 1.00 63.06  ? 97   SER A O   1 
ATOM   785  C CB  . SER A 1 97   ? 135.194 178.000 143.021 1.00 55.28  ? 97   SER A CB  1 
ATOM   786  O OG  . SER A 1 97   ? 134.031 178.551 143.610 1.00 60.69  ? 97   SER A OG  1 
ATOM   787  N N   . ASN A 1 98   ? 133.692 175.794 144.931 1.00 69.26  ? 98   ASN A N   1 
ATOM   788  C CA  . ASN A 1 98   ? 132.459 175.030 145.058 1.00 69.59  ? 98   ASN A CA  1 
ATOM   789  C C   . ASN A 1 98   ? 131.382 175.818 144.368 1.00 68.31  ? 98   ASN A C   1 
ATOM   790  O O   . ASN A 1 98   ? 130.248 175.365 144.251 1.00 78.53  ? 98   ASN A O   1 
ATOM   791  C CB  . ASN A 1 98   ? 132.104 174.807 146.522 1.00 68.25  ? 98   ASN A CB  1 
ATOM   792  C CG  . ASN A 1 98   ? 132.095 176.092 147.325 1.00 67.87  ? 98   ASN A CG  1 
ATOM   793  O OD1 . ASN A 1 98   ? 132.399 177.166 146.807 1.00 73.32  ? 98   ASN A OD1 1 
ATOM   794  N ND2 . ASN A 1 98   ? 131.753 175.986 148.603 1.00 73.89  ? 98   ASN A ND2 1 
ATOM   795  N N   . VAL A 1 99   ? 131.734 177.007 143.912 1.00 63.19  ? 99   VAL A N   1 
ATOM   796  C CA  . VAL A 1 99   ? 130.793 177.864 143.206 1.00 68.21  ? 99   VAL A CA  1 
ATOM   797  C C   . VAL A 1 99   ? 131.210 177.916 141.744 1.00 70.93  ? 99   VAL A C   1 
ATOM   798  O O   . VAL A 1 99   ? 132.401 178.037 141.438 1.00 77.56  ? 99   VAL A O   1 
ATOM   799  C CB  . VAL A 1 99   ? 130.765 179.280 143.809 1.00 66.82  ? 99   VAL A CB  1 
ATOM   800  C CG1 . VAL A 1 99   ? 129.912 180.189 142.960 1.00 71.96  ? 99   VAL A CG1 1 
ATOM   801  C CG2 . VAL A 1 99   ? 130.264 179.236 145.240 1.00 72.51  ? 99   VAL A CG2 1 
ATOM   802  N N   . ASN A 1 100  ? 130.234 177.814 140.843 1.00 64.00  ? 100  ASN A N   1 
ATOM   803  C CA  . ASN A 1 100  ? 130.534 177.892 139.420 1.00 60.38  ? 100  ASN A CA  1 
ATOM   804  C C   . ASN A 1 100  ? 131.195 179.225 139.091 1.00 65.65  ? 100  ASN A C   1 
ATOM   805  O O   . ASN A 1 100  ? 130.724 180.287 139.506 1.00 72.12  ? 100  ASN A O   1 
ATOM   806  C CB  . ASN A 1 100  ? 129.261 177.707 138.600 1.00 65.09  ? 100  ASN A CB  1 
ATOM   807  C CG  . ASN A 1 100  ? 128.274 178.834 138.791 1.00 72.88  ? 100  ASN A CG  1 
ATOM   808  O OD1 . ASN A 1 100  ? 128.276 179.806 138.039 1.00 76.64  ? 100  ASN A OD1 1 
ATOM   809  N ND2 . ASN A 1 100  ? 127.425 178.713 139.804 1.00 69.90  ? 100  ASN A ND2 1 
ATOM   810  N N   . LEU A 1 101  ? 132.293 179.163 138.347 1.00 56.94  ? 101  LEU A N   1 
ATOM   811  C CA  . LEU A 1 101  ? 133.118 180.330 138.073 1.00 48.68  ? 101  LEU A CA  1 
ATOM   812  C C   . LEU A 1 101  ? 132.722 181.062 136.800 1.00 59.87  ? 101  LEU A C   1 
ATOM   813  O O   . LEU A 1 101  ? 133.397 182.024 136.425 1.00 68.35  ? 101  LEU A O   1 
ATOM   814  C CB  . LEU A 1 101  ? 134.591 179.923 137.986 1.00 45.13  ? 101  LEU A CB  1 
ATOM   815  C CG  . LEU A 1 101  ? 135.215 179.365 139.264 1.00 45.06  ? 101  LEU A CG  1 
ATOM   816  C CD1 . LEU A 1 101  ? 136.644 178.933 139.018 1.00 50.04  ? 101  LEU A CD1 1 
ATOM   817  C CD2 . LEU A 1 101  ? 135.160 180.400 140.362 1.00 54.70  ? 101  LEU A CD2 1 
ATOM   818  N N   . LEU A 1 102  ? 131.656 180.640 136.129 1.00 70.91  ? 102  LEU A N   1 
ATOM   819  C CA  . LEU A 1 102  ? 131.291 181.232 134.851 1.00 74.16  ? 102  LEU A CA  1 
ATOM   820  C C   . LEU A 1 102  ? 130.343 182.415 134.981 1.00 76.94  ? 102  LEU A C   1 
ATOM   821  O O   . LEU A 1 102  ? 129.916 182.956 133.957 1.00 76.04  ? 102  LEU A O   1 
ATOM   822  C CB  . LEU A 1 102  ? 130.672 180.174 133.938 1.00 70.47  ? 102  LEU A CB  1 
ATOM   823  C CG  . LEU A 1 102  ? 131.654 179.091 133.497 1.00 67.01  ? 102  LEU A CG  1 
ATOM   824  C CD1 . LEU A 1 102  ? 131.026 178.205 132.443 1.00 73.85  ? 102  LEU A CD1 1 
ATOM   825  C CD2 . LEU A 1 102  ? 132.933 179.718 132.978 1.00 66.89  ? 102  LEU A CD2 1 
ATOM   826  N N   . LYS A 1 103  ? 129.998 182.822 136.196 1.00 81.59  ? 103  LYS A N   1 
ATOM   827  C CA  . LYS A 1 103  ? 129.202 184.025 136.369 1.00 84.00  ? 103  LYS A CA  1 
ATOM   828  C C   . LYS A 1 103  ? 130.009 185.242 135.919 1.00 86.29  ? 103  LYS A C   1 
ATOM   829  O O   . LYS A 1 103  ? 131.235 185.265 136.096 1.00 85.28  ? 103  LYS A O   1 
ATOM   830  C CB  . LYS A 1 103  ? 128.776 184.183 137.827 1.00 81.36  ? 103  LYS A CB  1 
ATOM   831  C CG  . LYS A 1 103  ? 127.953 183.030 138.356 1.00 81.20  ? 103  LYS A CG  1 
ATOM   832  C CD  . LYS A 1 103  ? 127.156 183.448 139.577 1.00 84.84  ? 103  LYS A CD  1 
ATOM   833  C CE  . LYS A 1 103  ? 126.186 184.566 139.232 1.00 86.02  ? 103  LYS A CE  1 
ATOM   834  N NZ  . LYS A 1 103  ? 125.332 184.950 140.390 1.00 82.01  ? 103  LYS A NZ  1 
ATOM   835  N N   . PRO A 1 104  ? 129.371 186.256 135.334 1.00 84.45  ? 104  PRO A N   1 
ATOM   836  C CA  . PRO A 1 104  ? 130.136 187.400 134.810 1.00 83.86  ? 104  PRO A CA  1 
ATOM   837  C C   . PRO A 1 104  ? 130.988 188.105 135.850 1.00 86.16  ? 104  PRO A C   1 
ATOM   838  O O   . PRO A 1 104  ? 132.089 188.563 135.527 1.00 92.98  ? 104  PRO A O   1 
ATOM   839  C CB  . PRO A 1 104  ? 129.039 188.320 134.259 1.00 86.20  ? 104  PRO A CB  1 
ATOM   840  C CG  . PRO A 1 104  ? 127.904 187.409 133.957 1.00 88.52  ? 104  PRO A CG  1 
ATOM   841  C CD  . PRO A 1 104  ? 127.936 186.364 135.027 1.00 86.39  ? 104  PRO A CD  1 
ATOM   842  N N   . LYS A 1 105  ? 130.511 188.209 137.090 1.00 85.91  ? 105  LYS A N   1 
ATOM   843  C CA  . LYS A 1 105  ? 131.264 188.904 138.129 1.00 88.49  ? 105  LYS A CA  1 
ATOM   844  C C   . LYS A 1 105  ? 132.591 188.206 138.411 1.00 92.87  ? 105  LYS A C   1 
ATOM   845  O O   . LYS A 1 105  ? 133.666 188.824 138.380 1.00 95.51  ? 105  LYS A O   1 
ATOM   846  C CB  . LYS A 1 105  ? 130.409 188.992 139.393 1.00 87.33  ? 105  LYS A CB  1 
ATOM   847  C CG  . LYS A 1 105  ? 131.129 189.507 140.617 1.00 88.90  ? 105  LYS A CG  1 
ATOM   848  C CD  . LYS A 1 105  ? 130.212 189.459 141.826 1.00 89.11  ? 105  LYS A CD  1 
ATOM   849  C CE  . LYS A 1 105  ? 129.669 188.055 142.040 1.00 91.99  ? 105  LYS A CE  1 
ATOM   850  N NZ  . LYS A 1 105  ? 128.765 187.975 143.217 1.00 92.88  ? 105  LYS A NZ  1 
ATOM   851  N N   . ILE A 1 106  ? 132.528 186.901 138.676 1.00 76.19  ? 106  ILE A N   1 
ATOM   852  C CA  . ILE A 1 106  ? 133.741 186.148 138.968 1.00 74.18  ? 106  ILE A CA  1 
ATOM   853  C C   . ILE A 1 106  ? 134.645 186.107 137.745 1.00 78.79  ? 106  ILE A C   1 
ATOM   854  O O   . ILE A 1 106  ? 135.874 186.120 137.863 1.00 80.95  ? 106  ILE A O   1 
ATOM   855  C CB  . ILE A 1 106  ? 133.386 184.737 139.462 1.00 69.26  ? 106  ILE A CB  1 
ATOM   856  C CG1 . ILE A 1 106  ? 132.331 184.818 140.561 1.00 72.08  ? 106  ILE A CG1 1 
ATOM   857  C CG2 . ILE A 1 106  ? 134.620 184.039 139.987 1.00 74.16  ? 106  ILE A CG2 1 
ATOM   858  C CD1 . ILE A 1 106  ? 131.957 183.478 141.138 1.00 73.67  ? 106  ILE A CD1 1 
ATOM   859  N N   . LEU A 1 107  ? 134.053 186.051 136.551 1.00 75.98  ? 107  LEU A N   1 
ATOM   860  C CA  . LEU A 1 107  ? 134.856 186.069 135.334 1.00 75.12  ? 107  LEU A CA  1 
ATOM   861  C C   . LEU A 1 107  ? 135.618 187.380 135.189 1.00 76.32  ? 107  LEU A C   1 
ATOM   862  O O   . LEU A 1 107  ? 136.790 187.384 134.801 1.00 79.65  ? 107  LEU A O   1 
ATOM   863  C CB  . LEU A 1 107  ? 133.971 185.816 134.118 1.00 73.85  ? 107  LEU A CB  1 
ATOM   864  C CG  . LEU A 1 107  ? 133.552 184.359 133.949 1.00 74.03  ? 107  LEU A CG  1 
ATOM   865  C CD1 . LEU A 1 107  ? 132.672 184.187 132.725 1.00 78.71  ? 107  LEU A CD1 1 
ATOM   866  C CD2 . LEU A 1 107  ? 134.783 183.477 133.855 1.00 73.23  ? 107  LEU A CD2 1 
ATOM   867  N N   . ARG A 1 108  ? 134.971 188.506 135.498 1.00 81.35  ? 108  ARG A N   1 
ATOM   868  C CA  . ARG A 1 108  ? 135.665 189.790 135.457 1.00 79.97  ? 108  ARG A CA  1 
ATOM   869  C C   . ARG A 1 108  ? 136.798 189.826 136.472 1.00 81.72  ? 108  ARG A C   1 
ATOM   870  O O   . ARG A 1 108  ? 137.896 190.320 136.183 1.00 87.60  ? 108  ARG A O   1 
ATOM   871  C CB  . ARG A 1 108  ? 134.681 190.930 135.716 1.00 81.21  ? 108  ARG A CB  1 
ATOM   872  C CG  . ARG A 1 108  ? 133.684 191.169 134.602 1.00 83.13  ? 108  ARG A CG  1 
ATOM   873  C CD  . ARG A 1 108  ? 132.721 192.283 134.969 1.00 82.10  ? 108  ARG A CD  1 
ATOM   874  N NE  . ARG A 1 108  ? 131.770 192.561 133.901 1.00 84.98  ? 108  ARG A NE  1 
ATOM   875  C CZ  . ARG A 1 108  ? 131.997 193.398 132.899 1.00 88.33  ? 108  ARG A CZ  1 
ATOM   876  N NH1 . ARG A 1 108  ? 133.142 194.052 132.791 1.00 85.09  ? 108  ARG A NH1 1 
ATOM   877  N NH2 . ARG A 1 108  ? 131.054 193.582 131.980 1.00 88.83  ? 108  ARG A NH2 1 
ATOM   878  N N   . GLU A 1 109  ? 136.545 189.312 137.676 1.00 71.58  ? 109  GLU A N   1 
ATOM   879  C CA  . GLU A 1 109  ? 137.595 189.305 138.689 1.00 75.46  ? 109  GLU A CA  1 
ATOM   880  C C   . GLU A 1 109  ? 138.775 188.438 138.258 1.00 78.32  ? 109  GLU A C   1 
ATOM   881  O O   . GLU A 1 109  ? 139.937 188.810 138.457 1.00 79.29  ? 109  GLU A O   1 
ATOM   882  C CB  . GLU A 1 109  ? 137.028 188.839 140.026 1.00 72.99  ? 109  GLU A CB  1 
ATOM   883  C CG  . GLU A 1 109  ? 135.883 189.709 140.510 1.00 75.94  ? 109  GLU A CG  1 
ATOM   884  C CD  . GLU A 1 109  ? 136.034 190.130 141.955 1.00 82.66  ? 109  GLU A CD  1 
ATOM   885  O OE1 . GLU A 1 109  ? 136.783 189.462 142.697 1.00 86.47  ? 109  GLU A OE1 1 
ATOM   886  O OE2 . GLU A 1 109  ? 135.406 191.135 142.348 1.00 84.24  ? 109  GLU A OE2 1 
ATOM   887  N N   . LEU A 1 110  ? 138.499 187.289 137.643 1.00 70.21  ? 110  LEU A N   1 
ATOM   888  C CA  . LEU A 1 110  ? 139.579 186.427 137.173 1.00 61.90  ? 110  LEU A CA  1 
ATOM   889  C C   . LEU A 1 110  ? 140.322 187.061 136.003 1.00 66.29  ? 110  LEU A C   1 
ATOM   890  O O   . LEU A 1 110  ? 141.528 186.856 135.834 1.00 75.83  ? 110  LEU A O   1 
ATOM   891  C CB  . LEU A 1 110  ? 139.028 185.055 136.792 1.00 65.44  ? 110  LEU A CB  1 
ATOM   892  C CG  . LEU A 1 110  ? 138.450 184.245 137.952 1.00 62.77  ? 110  LEU A CG  1 
ATOM   893  C CD1 . LEU A 1 110  ? 137.945 182.902 137.470 1.00 69.18  ? 110  LEU A CD1 1 
ATOM   894  C CD2 . LEU A 1 110  ? 139.486 184.065 139.041 1.00 64.08  ? 110  LEU A CD2 1 
ATOM   895  N N   . GLN A 1 111  ? 139.615 187.828 135.171 1.00 72.20  ? 111  GLN A N   1 
ATOM   896  C CA  . GLN A 1 111  ? 140.291 188.563 134.108 1.00 72.85  ? 111  GLN A CA  1 
ATOM   897  C C   . GLN A 1 111  ? 141.242 189.599 134.687 1.00 75.81  ? 111  GLN A C   1 
ATOM   898  O O   . GLN A 1 111  ? 142.363 189.776 134.194 1.00 76.97  ? 111  GLN A O   1 
ATOM   899  C CB  . GLN A 1 111  ? 139.270 189.230 133.189 1.00 73.27  ? 111  GLN A CB  1 
ATOM   900  C CG  . GLN A 1 111  ? 139.889 189.929 131.996 1.00 71.94  ? 111  GLN A CG  1 
ATOM   901  C CD  . GLN A 1 111  ? 138.854 190.400 130.999 1.00 76.26  ? 111  GLN A CD  1 
ATOM   902  O OE1 . GLN A 1 111  ? 138.202 191.423 131.201 1.00 79.74  ? 111  GLN A OE1 1 
ATOM   903  N NE2 . GLN A 1 111  ? 138.695 189.652 129.915 1.00 75.50  ? 111  GLN A NE2 1 
ATOM   904  N N   . LYS A 1 112  ? 140.807 190.294 135.739 1.00 73.79  ? 112  LYS A N   1 
ATOM   905  C CA  . LYS A 1 112  ? 141.711 191.200 136.439 1.00 69.82  ? 112  LYS A CA  1 
ATOM   906  C C   . LYS A 1 112  ? 142.901 190.442 137.011 1.00 71.94  ? 112  LYS A C   1 
ATOM   907  O O   . LYS A 1 112  ? 144.029 190.945 137.010 1.00 71.72  ? 112  LYS A O   1 
ATOM   908  C CB  . LYS A 1 112  ? 140.968 191.941 137.549 1.00 70.27  ? 112  LYS A CB  1 
ATOM   909  C CG  . LYS A 1 112  ? 139.843 192.835 137.065 1.00 73.50  ? 112  LYS A CG  1 
ATOM   910  C CD  . LYS A 1 112  ? 139.352 193.741 138.182 1.00 75.83  ? 112  LYS A CD  1 
ATOM   911  C CE  . LYS A 1 112  ? 138.963 192.942 139.415 1.00 75.15  ? 112  LYS A CE  1 
ATOM   912  N NZ  . LYS A 1 112  ? 138.516 193.819 140.531 1.00 74.74  ? 112  LYS A NZ  1 
ATOM   913  N N   . PHE A 1 113  ? 142.663 189.227 137.505 1.00 65.21  ? 113  PHE A N   1 
ATOM   914  C CA  . PHE A 1 113  ? 143.750 188.395 138.016 1.00 58.40  ? 113  PHE A CA  1 
ATOM   915  C C   . PHE A 1 113  ? 144.768 188.074 136.925 1.00 61.15  ? 113  PHE A C   1 
ATOM   916  O O   . PHE A 1 113  ? 145.982 188.157 137.149 1.00 70.30  ? 113  PHE A O   1 
ATOM   917  C CB  . PHE A 1 113  ? 143.161 187.116 138.613 1.00 59.32  ? 113  PHE A CB  1 
ATOM   918  C CG  . PHE A 1 113  ? 144.180 186.108 139.045 1.00 58.16  ? 113  PHE A CG  1 
ATOM   919  C CD1 . PHE A 1 113  ? 144.866 186.262 140.233 1.00 62.38  ? 113  PHE A CD1 1 
ATOM   920  C CD2 . PHE A 1 113  ? 144.426 184.985 138.278 1.00 59.90  ? 113  PHE A CD2 1 
ATOM   921  C CE1 . PHE A 1 113  ? 145.792 185.327 140.636 1.00 62.27  ? 113  PHE A CE1 1 
ATOM   922  C CE2 . PHE A 1 113  ? 145.351 184.048 138.678 1.00 61.62  ? 113  PHE A CE2 1 
ATOM   923  C CZ  . PHE A 1 113  ? 146.035 184.219 139.857 1.00 58.19  ? 113  PHE A CZ  1 
ATOM   924  N N   . GLU A 1 114  ? 144.290 187.710 135.734 1.00 67.52  ? 114  GLU A N   1 
ATOM   925  C CA  . GLU A 1 114  ? 145.194 187.410 134.625 1.00 64.12  ? 114  GLU A CA  1 
ATOM   926  C C   . GLU A 1 114  ? 145.972 188.650 134.197 1.00 76.82  ? 114  GLU A C   1 
ATOM   927  O O   . GLU A 1 114  ? 147.174 188.580 133.906 1.00 82.69  ? 114  GLU A O   1 
ATOM   928  C CB  . GLU A 1 114  ? 144.409 186.839 133.447 1.00 65.69  ? 114  GLU A CB  1 
ATOM   929  C CG  . GLU A 1 114  ? 143.637 185.576 133.768 1.00 77.46  ? 114  GLU A CG  1 
ATOM   930  C CD  . GLU A 1 114  ? 144.535 184.381 133.998 1.00 82.12  ? 114  GLU A CD  1 
ATOM   931  O OE1 . GLU A 1 114  ? 145.682 184.395 133.507 1.00 80.61  ? 114  GLU A OE1 1 
ATOM   932  O OE2 . GLU A 1 114  ? 144.093 183.424 134.670 1.00 82.72  ? 114  GLU A OE2 1 
ATOM   933  N N   . GLU A 1 115  ? 145.298 189.799 134.144 1.00 78.98  ? 115  GLU A N   1 
ATOM   934  C CA  . GLU A 1 115  ? 146.000 191.036 133.818 1.00 69.85  ? 115  GLU A CA  1 
ATOM   935  C C   . GLU A 1 115  ? 147.067 191.345 134.860 1.00 67.41  ? 115  GLU A C   1 
ATOM   936  O O   . GLU A 1 115  ? 148.163 191.805 134.521 1.00 69.64  ? 115  GLU A O   1 
ATOM   937  C CB  . GLU A 1 115  ? 145.006 192.189 133.695 1.00 73.87  ? 115  GLU A CB  1 
ATOM   938  C CG  . GLU A 1 115  ? 143.981 192.005 132.589 1.00 74.72  ? 115  GLU A CG  1 
ATOM   939  C CD  . GLU A 1 115  ? 144.611 191.917 131.214 1.00 79.09  ? 115  GLU A CD  1 
ATOM   940  O OE1 . GLU A 1 115  ? 145.675 192.536 131.006 1.00 82.49  ? 115  GLU A OE1 1 
ATOM   941  O OE2 . GLU A 1 115  ? 144.044 191.227 130.342 1.00 78.82  ? 115  GLU A OE2 1 
ATOM   942  N N   . GLY A 1 116  ? 146.765 191.092 136.133 1.00 59.46  ? 116  GLY A N   1 
ATOM   943  C CA  . GLY A 1 116  ? 147.771 191.259 137.167 1.00 62.22  ? 116  GLY A CA  1 
ATOM   944  C C   . GLY A 1 116  ? 148.958 190.338 136.973 1.00 60.04  ? 116  GLY A C   1 
ATOM   945  O O   . GLY A 1 116  ? 150.104 190.730 137.207 1.00 67.30  ? 116  GLY A O   1 
ATOM   946  N N   . THR A 1 117  ? 148.700 189.098 136.549 1.00 66.04  ? 117  THR A N   1 
ATOM   947  C CA  . THR A 1 117  ? 149.805 188.203 136.212 1.00 66.90  ? 117  THR A CA  1 
ATOM   948  C C   . THR A 1 117  ? 150.657 188.795 135.100 1.00 65.55  ? 117  THR A C   1 
ATOM   949  O O   . THR A 1 117  ? 151.890 188.709 135.135 1.00 66.48  ? 117  THR A O   1 
ATOM   950  C CB  . THR A 1 117  ? 149.289 186.826 135.792 1.00 64.79  ? 117  THR A CB  1 
ATOM   951  O OG1 . THR A 1 117  ? 148.469 186.955 134.625 1.00 71.40  ? 117  THR A OG1 1 
ATOM   952  C CG2 . THR A 1 117  ? 148.487 186.182 136.903 1.00 66.39  ? 117  THR A CG2 1 
ATOM   953  N N   . LYS A 1 118  ? 150.014 189.398 134.101 1.00 72.07  ? 118  LYS A N   1 
ATOM   954  C CA  . LYS A 1 118  ? 150.766 190.039 133.025 1.00 67.49  ? 118  LYS A CA  1 
ATOM   955  C C   . LYS A 1 118  ? 151.550 191.251 133.515 1.00 67.06  ? 118  LYS A C   1 
ATOM   956  O O   . LYS A 1 118  ? 152.593 191.581 132.942 1.00 72.84  ? 118  LYS A O   1 
ATOM   957  C CB  . LYS A 1 118  ? 149.831 190.459 131.892 1.00 71.23  ? 118  LYS A CB  1 
ATOM   958  C CG  . LYS A 1 118  ? 149.362 189.322 131.008 1.00 74.11  ? 118  LYS A CG  1 
ATOM   959  C CD  . LYS A 1 118  ? 148.538 189.847 129.846 1.00 72.29  ? 118  LYS A CD  1 
ATOM   960  C CE  . LYS A 1 118  ? 148.094 188.723 128.929 1.00 74.51  ? 118  LYS A CE  1 
ATOM   961  N NZ  . LYS A 1 118  ? 147.326 189.237 127.763 1.00 76.82  ? 118  LYS A NZ  1 
ATOM   962  N N   . ASP A 1 119  ? 151.072 191.923 134.559 1.00 74.76  ? 119  ASP A N   1 
ATOM   963  C CA  . ASP A 1 119  ? 151.632 193.207 134.969 1.00 73.74  ? 119  ASP A CA  1 
ATOM   964  C C   . ASP A 1 119  ? 152.798 193.094 135.944 1.00 73.80  ? 119  ASP A C   1 
ATOM   965  O O   . ASP A 1 119  ? 153.309 194.129 136.383 1.00 74.35  ? 119  ASP A O   1 
ATOM   966  C CB  . ASP A 1 119  ? 150.539 194.080 135.591 1.00 76.69  ? 119  ASP A CB  1 
ATOM   967  C CG  . ASP A 1 119  ? 149.547 194.588 134.567 1.00 81.29  ? 119  ASP A CG  1 
ATOM   968  O OD1 . ASP A 1 119  ? 149.775 194.371 133.359 1.00 81.38  ? 119  ASP A OD1 1 
ATOM   969  O OD2 . ASP A 1 119  ? 148.538 195.205 134.968 1.00 78.74  ? 119  ASP A OD2 1 
ATOM   970  N N   . ILE A 1 120  ? 153.229 191.883 136.303 1.00 73.93  ? 120  ILE A N   1 
ATOM   971  C CA  . ILE A 1 120  ? 154.324 191.741 137.258 1.00 72.95  ? 120  ILE A CA  1 
ATOM   972  C C   . ILE A 1 120  ? 155.606 192.295 136.656 1.00 75.67  ? 120  ILE A C   1 
ATOM   973  O O   . ILE A 1 120  ? 155.935 192.027 135.495 1.00 77.69  ? 120  ILE A O   1 
ATOM   974  C CB  . ILE A 1 120  ? 154.488 190.271 137.667 1.00 68.71  ? 120  ILE A CB  1 
ATOM   975  C CG1 . ILE A 1 120  ? 153.234 189.774 138.381 1.00 70.25  ? 120  ILE A CG1 1 
ATOM   976  C CG2 . ILE A 1 120  ? 155.700 190.097 138.561 1.00 71.97  ? 120  ILE A CG2 1 
ATOM   977  C CD1 . ILE A 1 120  ? 153.345 188.352 138.871 1.00 70.92  ? 120  ILE A CD1 1 
ATOM   978  N N   . GLU A 1 121  ? 156.338 193.075 137.448 1.00 81.40  ? 121  GLU A N   1 
ATOM   979  C CA  . GLU A 1 121  ? 157.606 193.658 137.035 1.00 79.31  ? 121  GLU A CA  1 
ATOM   980  C C   . GLU A 1 121  ? 158.725 193.132 137.921 1.00 81.13  ? 121  GLU A C   1 
ATOM   981  O O   . GLU A 1 121  ? 158.565 193.030 139.141 1.00 82.92  ? 121  GLU A O   1 
ATOM   982  C CB  . GLU A 1 121  ? 157.569 195.185 137.109 1.00 80.57  ? 121  GLU A CB  1 
ATOM   983  C CG  . GLU A 1 121  ? 156.558 195.833 136.187 1.00 84.04  ? 121  GLU A CG  1 
ATOM   984  C CD  . GLU A 1 121  ? 156.607 197.346 136.252 1.00 87.43  ? 121  GLU A CD  1 
ATOM   985  O OE1 . GLU A 1 121  ? 157.413 197.880 137.042 1.00 85.30  ? 121  GLU A OE1 1 
ATOM   986  O OE2 . GLU A 1 121  ? 155.842 198.001 135.514 1.00 87.16  ? 121  GLU A OE2 1 
ATOM   987  N N   . VAL A 1 122  ? 159.857 192.801 137.304 1.00 73.56  ? 122  VAL A N   1 
ATOM   988  C CA  . VAL A 1 122  ? 161.027 192.298 138.011 1.00 70.67  ? 122  VAL A CA  1 
ATOM   989  C C   . VAL A 1 122  ? 162.213 193.181 137.657 1.00 75.78  ? 122  VAL A C   1 
ATOM   990  O O   . VAL A 1 122  ? 162.492 193.406 136.475 1.00 79.42  ? 122  VAL A O   1 
ATOM   991  C CB  . VAL A 1 122  ? 161.328 190.832 137.652 1.00 66.40  ? 122  VAL A CB  1 
ATOM   992  C CG1 . VAL A 1 122  ? 162.515 190.330 138.446 1.00 69.38  ? 122  VAL A CG1 1 
ATOM   993  C CG2 . VAL A 1 122  ? 160.112 189.966 137.900 1.00 73.93  ? 122  VAL A CG2 1 
ATOM   994  N N   . ASP A 1 123  ? 162.908 193.676 138.673 1.00 89.74  ? 123  ASP A N   1 
ATOM   995  C CA  . ASP A 1 123  ? 164.108 194.467 138.461 1.00 88.40  ? 123  ASP A CA  1 
ATOM   996  C C   . ASP A 1 123  ? 165.329 193.561 138.346 1.00 87.93  ? 123  ASP A C   1 
ATOM   997  O O   . ASP A 1 123  ? 165.374 192.463 138.903 1.00 90.23  ? 123  ASP A O   1 
ATOM   998  C CB  . ASP A 1 123  ? 164.299 195.472 139.596 1.00 90.86  ? 123  ASP A CB  1 
ATOM   999  C CG  . ASP A 1 123  ? 164.026 194.868 140.957 1.00 93.89  ? 123  ASP A CG  1 
ATOM   1000 O OD1 . ASP A 1 123  ? 163.553 193.714 141.009 1.00 94.49  ? 123  ASP A OD1 1 
ATOM   1001 O OD2 . ASP A 1 123  ? 164.282 195.545 141.974 1.00 93.97  ? 123  ASP A OD2 1 
ATOM   1002 N N   . LEU A 1 124  ? 166.334 194.046 137.614 1.00 87.47  ? 124  LEU A N   1 
ATOM   1003 C CA  . LEU A 1 124  ? 167.513 193.237 137.331 1.00 88.31  ? 124  LEU A CA  1 
ATOM   1004 C C   . LEU A 1 124  ? 168.326 192.921 138.578 1.00 87.65  ? 124  LEU A C   1 
ATOM   1005 O O   . LEU A 1 124  ? 169.131 191.985 138.554 1.00 87.08  ? 124  LEU A O   1 
ATOM   1006 C CB  . LEU A 1 124  ? 168.402 193.936 136.302 1.00 88.61  ? 124  LEU A CB  1 
ATOM   1007 C CG  . LEU A 1 124  ? 168.053 193.736 134.826 1.00 85.29  ? 124  LEU A CG  1 
ATOM   1008 C CD1 . LEU A 1 124  ? 167.899 192.258 134.517 1.00 86.41  ? 124  LEU A CD1 1 
ATOM   1009 C CD2 . LEU A 1 124  ? 166.802 194.497 134.437 1.00 86.77  ? 124  LEU A CD2 1 
ATOM   1010 N N   . SER A 1 125  ? 168.137 193.672 139.664 1.00 89.80  ? 125  SER A N   1 
ATOM   1011 C CA  . SER A 1 125  ? 168.871 193.392 140.891 1.00 90.66  ? 125  SER A CA  1 
ATOM   1012 C C   . SER A 1 125  ? 168.484 192.054 141.504 1.00 94.00  ? 125  SER A C   1 
ATOM   1013 O O   . SER A 1 125  ? 169.249 191.512 142.308 1.00 94.55  ? 125  SER A O   1 
ATOM   1014 C CB  . SER A 1 125  ? 168.643 194.509 141.907 1.00 94.01  ? 125  SER A CB  1 
ATOM   1015 O OG  . SER A 1 125  ? 167.277 194.591 142.272 1.00 96.22  ? 125  SER A OG  1 
ATOM   1016 N N   . GLU A 1 126  ? 167.322 191.514 141.147 1.00 96.04  ? 126  GLU A N   1 
ATOM   1017 C CA  . GLU A 1 126  ? 166.860 190.237 141.672 1.00 93.88  ? 126  GLU A CA  1 
ATOM   1018 C C   . GLU A 1 126  ? 167.394 189.044 140.892 1.00 96.87  ? 126  GLU A C   1 
ATOM   1019 O O   . GLU A 1 126  ? 167.076 187.904 141.241 1.00 99.42  ? 126  GLU A O   1 
ATOM   1020 C CB  . GLU A 1 126  ? 165.330 190.194 141.687 1.00 93.54  ? 126  GLU A CB  1 
ATOM   1021 C CG  . GLU A 1 126  ? 164.693 191.214 142.610 1.00 93.72  ? 126  GLU A CG  1 
ATOM   1022 C CD  . GLU A 1 126  ? 163.184 191.084 142.663 1.00 95.64  ? 126  GLU A CD  1 
ATOM   1023 O OE1 . GLU A 1 126  ? 162.660 190.039 142.224 1.00 96.87  ? 126  GLU A OE1 1 
ATOM   1024 O OE2 . GLU A 1 126  ? 162.521 192.028 143.142 1.00 94.25  ? 126  GLU A OE2 1 
ATOM   1025 N N   . ILE A 1 127  ? 168.189 189.274 139.851 1.00 96.29  ? 127  ILE A N   1 
ATOM   1026 C CA  . ILE A 1 127  ? 168.768 188.180 139.081 1.00 94.75  ? 127  ILE A CA  1 
ATOM   1027 C C   . ILE A 1 127  ? 169.969 187.642 139.842 1.00 98.04  ? 127  ILE A C   1 
ATOM   1028 O O   . ILE A 1 127  ? 171.088 188.147 139.699 1.00 102.12 ? 127  ILE A O   1 
ATOM   1029 C CB  . ILE A 1 127  ? 169.166 188.636 137.667 1.00 93.18  ? 127  ILE A CB  1 
ATOM   1030 C CG1 . ILE A 1 127  ? 167.985 189.319 136.980 1.00 96.45  ? 127  ILE A CG1 1 
ATOM   1031 C CG2 . ILE A 1 127  ? 169.641 187.456 136.845 1.00 93.97  ? 127  ILE A CG2 1 
ATOM   1032 C CD1 . ILE A 1 127  ? 166.757 188.450 136.879 1.00 93.36  ? 127  ILE A CD1 1 
ATOM   1033 N N   . ASN A 1 128  ? 169.743 186.611 140.659 1.00 97.16  ? 128  ASN A N   1 
ATOM   1034 C CA  . ASN A 1 128  ? 170.796 186.091 141.522 1.00 97.57  ? 128  ASN A CA  1 
ATOM   1035 C C   . ASN A 1 128  ? 171.937 185.460 140.738 1.00 96.17  ? 128  ASN A C   1 
ATOM   1036 O O   . ASN A 1 128  ? 173.015 185.244 141.302 1.00 95.78  ? 128  ASN A O   1 
ATOM   1037 C CB  . ASN A 1 128  ? 170.211 185.070 142.497 1.00 98.65  ? 128  ASN A CB  1 
ATOM   1038 C CG  . ASN A 1 128  ? 169.041 185.622 143.281 1.00 100.40 ? 128  ASN A CG  1 
ATOM   1039 O OD1 . ASN A 1 128  ? 167.899 185.581 142.825 1.00 99.23  ? 128  ASN A OD1 1 
ATOM   1040 N ND2 . ASN A 1 128  ? 169.319 186.143 144.470 1.00 101.81 ? 128  ASN A ND2 1 
ATOM   1041 N N   . GLU A 1 129  ? 171.731 185.162 139.459 1.00 96.51  ? 129  GLU A N   1 
ATOM   1042 C CA  . GLU A 1 129  ? 172.765 184.538 138.647 1.00 98.39  ? 129  GLU A CA  1 
ATOM   1043 C C   . GLU A 1 129  ? 173.722 185.548 138.029 1.00 100.77 ? 129  GLU A C   1 
ATOM   1044 O O   . GLU A 1 129  ? 174.623 185.147 137.286 1.00 101.90 ? 129  GLU A O   1 
ATOM   1045 C CB  . GLU A 1 129  ? 172.120 183.681 137.556 1.00 98.60  ? 129  GLU A CB  1 
ATOM   1046 C CG  . GLU A 1 129  ? 171.164 182.632 138.106 1.00 99.97  ? 129  GLU A CG  1 
ATOM   1047 C CD  . GLU A 1 129  ? 170.708 181.636 137.058 1.00 102.32 ? 129  GLU A CD  1 
ATOM   1048 O OE1 . GLU A 1 129  ? 171.190 181.715 135.909 1.00 103.39 ? 129  GLU A OE1 1 
ATOM   1049 O OE2 . GLU A 1 129  ? 169.868 180.773 137.386 1.00 102.41 ? 129  GLU A OE2 1 
ATOM   1050 N N   . CYS A 1 130  ? 173.546 186.839 138.308 1.00 110.49 ? 130  CYS A N   1 
ATOM   1051 C CA  . CYS A 1 130  ? 174.464 187.893 137.874 1.00 110.74 ? 130  CYS A CA  1 
ATOM   1052 C C   . CYS A 1 130  ? 174.726 188.778 139.088 1.00 110.49 ? 130  CYS A C   1 
ATOM   1053 O O   . CYS A 1 130  ? 174.031 189.774 139.301 1.00 111.13 ? 130  CYS A O   1 
ATOM   1054 C CB  . CYS A 1 130  ? 173.886 188.685 136.707 1.00 109.10 ? 130  CYS A CB  1 
ATOM   1055 S SG  . CYS A 1 130  ? 173.358 187.677 135.306 1.00 113.08 ? 130  CYS A SG  1 
ATOM   1056 N N   . LYS A 1 131  ? 175.736 188.417 139.881 1.00 117.15 ? 131  LYS A N   1 
ATOM   1057 C CA  . LYS A 1 131  ? 176.026 189.106 141.133 1.00 118.49 ? 131  LYS A CA  1 
ATOM   1058 C C   . LYS A 1 131  ? 177.424 189.716 141.154 1.00 121.67 ? 131  LYS A C   1 
ATOM   1059 O O   . LYS A 1 131  ? 177.964 189.975 142.234 1.00 122.40 ? 131  LYS A O   1 
ATOM   1060 C CB  . LYS A 1 131  ? 175.849 188.154 142.317 1.00 117.25 ? 131  LYS A CB  1 
ATOM   1061 N N   . THR A 1 132  ? 178.024 189.940 139.983 1.00 124.25 ? 132  THR A N   1 
ATOM   1062 C CA  . THR A 1 132  ? 179.339 190.568 139.846 1.00 122.65 ? 132  THR A CA  1 
ATOM   1063 C C   . THR A 1 132  ? 180.431 189.812 140.594 1.00 120.69 ? 132  THR A C   1 
ATOM   1064 O O   . THR A 1 132  ? 181.490 190.375 140.886 1.00 117.90 ? 132  THR A O   1 
ATOM   1065 C CB  . THR A 1 132  ? 179.314 192.031 140.310 1.00 121.57 ? 132  THR A CB  1 
ATOM   1066 O OG1 . THR A 1 132  ? 179.215 192.081 141.738 1.00 121.77 ? 132  THR A OG1 1 
ATOM   1067 C CG2 . THR A 1 132  ? 178.130 192.767 139.703 1.00 119.72 ? 132  THR A CG2 1 
ATOM   1068 N N   . ASN A 1 133  ? 180.195 188.539 140.918 1.00 130.97 ? 133  ASN A N   1 
ATOM   1069 C CA  . ASN A 1 133  ? 181.143 187.753 141.698 1.00 130.09 ? 133  ASN A CA  1 
ATOM   1070 C C   . ASN A 1 133  ? 181.251 186.311 141.213 1.00 131.60 ? 133  ASN A C   1 
ATOM   1071 O O   . ASN A 1 133  ? 181.648 185.438 141.993 1.00 131.46 ? 133  ASN A O   1 
ATOM   1072 C CB  . ASN A 1 133  ? 180.756 187.779 143.182 1.00 127.90 ? 133  ASN A CB  1 
ATOM   1073 C CG  . ASN A 1 133  ? 181.913 187.420 144.095 1.00 129.88 ? 133  ASN A CG  1 
ATOM   1074 O OD1 . ASN A 1 133  ? 183.077 187.520 143.709 1.00 129.81 ? 133  ASN A OD1 1 
ATOM   1075 N ND2 . ASN A 1 133  ? 181.596 186.998 145.313 1.00 131.76 ? 133  ASN A ND2 1 
ATOM   1076 N N   . SER A 1 134  ? 180.906 186.033 139.960 1.00 136.24 ? 134  SER A N   1 
ATOM   1077 C CA  . SER A 1 134  ? 180.913 184.675 139.442 1.00 135.76 ? 134  SER A CA  1 
ATOM   1078 C C   . SER A 1 134  ? 181.714 184.592 138.149 1.00 136.57 ? 134  SER A C   1 
ATOM   1079 O O   . SER A 1 134  ? 182.001 185.601 137.498 1.00 134.49 ? 134  SER A O   1 
ATOM   1080 C CB  . SER A 1 134  ? 179.486 184.167 139.203 1.00 134.92 ? 134  SER A CB  1 
ATOM   1081 O OG  . SER A 1 134  ? 179.494 182.854 138.670 1.00 135.97 ? 134  SER A OG  1 
ATOM   1082 N N   . GLU A 1 135  ? 182.065 183.361 137.783 1.00 140.58 ? 135  GLU A N   1 
ATOM   1083 C CA  . GLU A 1 135  ? 182.699 183.045 136.504 1.00 139.75 ? 135  GLU A CA  1 
ATOM   1084 C C   . GLU A 1 135  ? 181.678 182.505 135.512 1.00 139.64 ? 135  GLU A C   1 
ATOM   1085 O O   . GLU A 1 135  ? 181.948 181.573 134.749 1.00 139.21 ? 135  GLU A O   1 
ATOM   1086 C CB  . GLU A 1 135  ? 183.841 182.054 136.704 1.00 139.04 ? 135  GLU A CB  1 
ATOM   1087 C CG  . GLU A 1 135  ? 183.456 180.804 137.477 1.00 138.42 ? 135  GLU A CG  1 
ATOM   1088 C CD  . GLU A 1 135  ? 184.616 179.841 137.638 1.00 139.66 ? 135  GLU A CD  1 
ATOM   1089 O OE1 . GLU A 1 135  ? 185.711 180.134 137.115 1.00 140.49 ? 135  GLU A OE1 1 
ATOM   1090 O OE2 . GLU A 1 135  ? 184.432 178.790 138.287 1.00 140.11 ? 135  GLU A OE2 1 
ATOM   1091 N N   . LEU A 1 136  ? 180.488 183.096 135.525 1.00 134.28 ? 136  LEU A N   1 
ATOM   1092 C CA  . LEU A 1 136  ? 179.306 182.689 134.773 1.00 133.41 ? 136  LEU A CA  1 
ATOM   1093 C C   . LEU A 1 136  ? 179.501 182.508 133.266 1.00 134.20 ? 136  LEU A C   1 
ATOM   1094 O O   . LEU A 1 136  ? 178.712 181.780 132.656 1.00 134.05 ? 136  LEU A O   1 
ATOM   1095 C CB  . LEU A 1 136  ? 178.181 183.700 135.012 1.00 134.05 ? 136  LEU A CB  1 
ATOM   1096 N N   . PRO A 1 137  ? 180.431 183.205 132.610 1.00 132.02 ? 137  PRO A N   1 
ATOM   1097 C CA  . PRO A 1 137  ? 180.722 182.906 131.191 1.00 131.03 ? 137  PRO A CA  1 
ATOM   1098 C C   . PRO A 1 137  ? 181.831 181.880 131.022 1.00 131.18 ? 137  PRO A C   1 
ATOM   1099 O O   . PRO A 1 137  ? 182.998 182.259 130.839 1.00 131.03 ? 137  PRO A O   1 
ATOM   1100 C CB  . PRO A 1 137  ? 181.141 184.271 130.627 1.00 130.35 ? 137  PRO A CB  1 
ATOM   1101 C CG  . PRO A 1 137  ? 181.744 184.962 131.779 1.00 130.43 ? 137  PRO A CG  1 
ATOM   1102 C CD  . PRO A 1 137  ? 180.938 184.543 132.977 1.00 130.30 ? 137  PRO A CD  1 
ATOM   1103 N N   . PRO A 1 138  ? 181.532 180.569 131.076 1.00 123.01 ? 138  PRO A N   1 
ATOM   1104 C CA  . PRO A 1 138  ? 182.582 179.590 130.773 1.00 121.30 ? 138  PRO A CA  1 
ATOM   1105 C C   . PRO A 1 138  ? 182.923 179.626 129.293 1.00 122.13 ? 138  PRO A C   1 
ATOM   1106 O O   . PRO A 1 138  ? 182.138 180.140 128.491 1.00 122.69 ? 138  PRO A O   1 
ATOM   1107 C CB  . PRO A 1 138  ? 181.943 178.261 131.180 1.00 118.48 ? 138  PRO A CB  1 
ATOM   1108 C CG  . PRO A 1 138  ? 180.517 178.459 130.842 1.00 120.34 ? 138  PRO A CG  1 
ATOM   1109 C CD  . PRO A 1 138  ? 180.207 179.925 131.081 1.00 121.48 ? 138  PRO A CD  1 
ATOM   1110 N N   . GLU A 1 139  ? 184.075 179.088 128.910 1.00 108.08 ? 139  GLU A N   1 
ATOM   1111 C CA  . GLU A 1 139  ? 184.558 179.210 127.541 1.00 107.74 ? 139  GLU A CA  1 
ATOM   1112 C C   . GLU A 1 139  ? 183.841 178.211 126.641 1.00 109.29 ? 139  GLU A C   1 
ATOM   1113 O O   . GLU A 1 139  ? 183.837 177.006 126.917 1.00 110.95 ? 139  GLU A O   1 
ATOM   1114 C CB  . GLU A 1 139  ? 186.069 178.996 127.474 1.00 107.71 ? 139  GLU A CB  1 
ATOM   1115 C CG  . GLU A 1 139  ? 186.623 178.944 126.056 1.00 106.74 ? 139  GLU A CG  1 
ATOM   1116 C CD  . GLU A 1 139  ? 186.486 180.263 125.315 1.00 107.50 ? 139  GLU A CD  1 
ATOM   1117 O OE1 . GLU A 1 139  ? 186.319 181.311 125.974 1.00 109.20 ? 139  GLU A OE1 1 
ATOM   1118 O OE2 . GLU A 1 139  ? 186.550 180.251 124.068 1.00 106.95 ? 139  GLU A OE2 1 
ATOM   1119 N N   . GLN A 1 140  ? 183.232 178.717 125.572 1.00 94.42  ? 140  GLN A N   1 
ATOM   1120 C CA  . GLN A 1 140  ? 182.672 177.877 124.526 1.00 90.58  ? 140  GLN A CA  1 
ATOM   1121 C C   . GLN A 1 140  ? 183.743 177.557 123.489 1.00 92.29  ? 140  GLN A C   1 
ATOM   1122 O O   . GLN A 1 140  ? 184.617 178.378 123.201 1.00 98.68  ? 140  GLN A O   1 
ATOM   1123 C CB  . GLN A 1 140  ? 181.486 178.579 123.864 1.00 92.47  ? 140  GLN A CB  1 
ATOM   1124 C CG  . GLN A 1 140  ? 180.797 177.780 122.775 1.00 94.23  ? 140  GLN A CG  1 
ATOM   1125 C CD  . GLN A 1 140  ? 179.693 178.562 122.094 1.00 92.50  ? 140  GLN A CD  1 
ATOM   1126 O OE1 . GLN A 1 140  ? 179.449 179.724 122.418 1.00 93.77  ? 140  GLN A OE1 1 
ATOM   1127 N NE2 . GLN A 1 140  ? 179.017 177.928 121.145 1.00 90.86  ? 140  GLN A NE2 1 
ATOM   1128 N N   . SER A 1 141  ? 183.672 176.351 122.931 1.00 81.18  ? 141  SER A N   1 
ATOM   1129 C CA  . SER A 1 141  ? 184.669 175.929 121.957 1.00 84.49  ? 141  SER A CA  1 
ATOM   1130 C C   . SER A 1 141  ? 184.633 176.828 120.726 1.00 86.70  ? 141  SER A C   1 
ATOM   1131 O O   . SER A 1 141  ? 183.578 177.310 120.309 1.00 93.89  ? 141  SER A O   1 
ATOM   1132 C CB  . SER A 1 141  ? 184.443 174.472 121.558 1.00 87.56  ? 141  SER A CB  1 
ATOM   1133 O OG  . SER A 1 141  ? 183.101 174.251 121.172 1.00 89.68  ? 141  SER A OG  1 
ATOM   1134 N N   . HIS A 1 142  ? 185.815 177.056 120.150 1.00 87.41  ? 142  HIS A N   1 
ATOM   1135 C CA  . HIS A 1 142  ? 185.953 178.023 119.064 1.00 91.35  ? 142  HIS A CA  1 
ATOM   1136 C C   . HIS A 1 142  ? 185.140 177.611 117.842 1.00 93.89  ? 142  HIS A C   1 
ATOM   1137 O O   . HIS A 1 142  ? 184.451 178.438 117.227 1.00 93.85  ? 142  HIS A O   1 
ATOM   1138 C CB  . HIS A 1 142  ? 187.430 178.178 118.704 1.00 92.32  ? 142  HIS A CB  1 
ATOM   1139 C CG  . HIS A 1 142  ? 187.685 179.154 117.600 1.00 95.43  ? 142  HIS A CG  1 
ATOM   1140 N ND1 . HIS A 1 142  ? 187.352 180.488 117.695 1.00 96.90  ? 142  HIS A ND1 1 
ATOM   1141 C CD2 . HIS A 1 142  ? 188.245 178.991 116.379 1.00 92.50  ? 142  HIS A CD2 1 
ATOM   1142 C CE1 . HIS A 1 142  ? 187.695 181.105 116.579 1.00 95.61  ? 142  HIS A CE1 1 
ATOM   1143 N NE2 . HIS A 1 142  ? 188.239 180.219 115.763 1.00 94.43  ? 142  HIS A NE2 1 
ATOM   1144 N N   . VAL A 1 143  ? 185.210 176.330 117.475 1.00 85.00  ? 143  VAL A N   1 
ATOM   1145 C CA  . VAL A 1 143  ? 184.461 175.850 116.319 1.00 84.81  ? 143  VAL A CA  1 
ATOM   1146 C C   . VAL A 1 143  ? 182.968 176.032 116.546 1.00 86.48  ? 143  VAL A C   1 
ATOM   1147 O O   . VAL A 1 143  ? 182.223 176.375 115.621 1.00 88.28  ? 143  VAL A O   1 
ATOM   1148 C CB  . VAL A 1 143  ? 184.823 174.383 116.017 1.00 84.47  ? 143  VAL A CB  1 
ATOM   1149 C CG1 . VAL A 1 143  ? 184.652 173.518 117.255 1.00 84.00  ? 143  VAL A CG1 1 
ATOM   1150 C CG2 . VAL A 1 143  ? 183.983 173.852 114.867 1.00 80.26  ? 143  VAL A CG2 1 
ATOM   1151 N N   . ALA A 1 144  ? 182.509 175.824 117.782 1.00 79.15  ? 144  ALA A N   1 
ATOM   1152 C CA  . ALA A 1 144  ? 181.097 176.023 118.083 1.00 73.17  ? 144  ALA A CA  1 
ATOM   1153 C C   . ALA A 1 144  ? 180.689 177.474 117.881 1.00 76.78  ? 144  ALA A C   1 
ATOM   1154 O O   . ALA A 1 144  ? 179.615 177.750 117.340 1.00 82.59  ? 144  ALA A O   1 
ATOM   1155 C CB  . ALA A 1 144  ? 180.793 175.574 119.510 1.00 78.07  ? 144  ALA A CB  1 
ATOM   1156 N N   . LYS A 1 145  ? 181.526 178.418 118.316 1.00 86.95  ? 145  LYS A N   1 
ATOM   1157 C CA  . LYS A 1 145  ? 181.192 179.829 118.138 1.00 87.20  ? 145  LYS A CA  1 
ATOM   1158 C C   . LYS A 1 145  ? 181.158 180.208 116.663 1.00 87.31  ? 145  LYS A C   1 
ATOM   1159 O O   . LYS A 1 145  ? 180.249 180.924 116.217 1.00 89.27  ? 145  LYS A O   1 
ATOM   1160 C CB  . LYS A 1 145  ? 182.187 180.706 118.896 1.00 84.25  ? 145  LYS A CB  1 
ATOM   1161 C CG  . LYS A 1 145  ? 182.172 180.496 120.398 1.00 86.02  ? 145  LYS A CG  1 
ATOM   1162 C CD  . LYS A 1 145  ? 182.979 181.565 121.112 1.00 87.00  ? 145  LYS A CD  1 
ATOM   1163 C CE  . LYS A 1 145  ? 184.416 181.595 120.621 1.00 88.51  ? 145  LYS A CE  1 
ATOM   1164 N NZ  . LYS A 1 145  ? 185.210 182.649 121.310 1.00 88.65  ? 145  LYS A NZ  1 
ATOM   1165 N N   . GLU A 1 146  ? 182.139 179.740 115.888 1.00 85.19  ? 146  GLU A N   1 
ATOM   1166 C CA  . GLU A 1 146  ? 182.133 180.038 114.459 1.00 86.21  ? 146  GLU A CA  1 
ATOM   1167 C C   . GLU A 1 146  ? 180.907 179.442 113.780 1.00 84.95  ? 146  GLU A C   1 
ATOM   1168 O O   . GLU A 1 146  ? 180.274 180.091 112.937 1.00 85.41  ? 146  GLU A O   1 
ATOM   1169 C CB  . GLU A 1 146  ? 183.412 179.525 113.802 1.00 84.96  ? 146  GLU A CB  1 
ATOM   1170 C CG  . GLU A 1 146  ? 184.677 180.212 114.276 1.00 85.42  ? 146  GLU A CG  1 
ATOM   1171 C CD  . GLU A 1 146  ? 185.853 179.947 113.359 1.00 91.22  ? 146  GLU A CD  1 
ATOM   1172 O OE1 . GLU A 1 146  ? 185.625 179.516 112.209 1.00 92.82  ? 146  GLU A OE1 1 
ATOM   1173 O OE2 . GLU A 1 146  ? 187.006 180.167 113.783 1.00 92.64  ? 146  GLU A OE2 1 
ATOM   1174 N N   . LEU A 1 147  ? 180.553 178.207 114.141 1.00 76.09  ? 147  LEU A N   1 
ATOM   1175 C CA  . LEU A 1 147  ? 179.373 177.582 113.561 1.00 76.50  ? 147  LEU A CA  1 
ATOM   1176 C C   . LEU A 1 147  ? 178.106 178.323 113.959 1.00 77.13  ? 147  LEU A C   1 
ATOM   1177 O O   . LEU A 1 147  ? 177.190 178.467 113.149 1.00 85.49  ? 147  LEU A O   1 
ATOM   1178 C CB  . LEU A 1 147  ? 179.287 176.116 113.978 1.00 72.46  ? 147  LEU A CB  1 
ATOM   1179 C CG  . LEU A 1 147  ? 178.081 175.387 113.390 1.00 69.47  ? 147  LEU A CG  1 
ATOM   1180 C CD1 . LEU A 1 147  ? 178.120 175.446 111.874 1.00 70.58  ? 147  LEU A CD1 1 
ATOM   1181 C CD2 . LEU A 1 147  ? 178.032 173.955 113.867 1.00 73.73  ? 147  LEU A CD2 1 
ATOM   1182 N N   . TYR A 1 148  ? 178.028 178.790 115.206 1.00 69.71  ? 148  TYR A N   1 
ATOM   1183 C CA  . TYR A 1 148  ? 176.858 179.550 115.630 1.00 63.69  ? 148  TYR A CA  1 
ATOM   1184 C C   . TYR A 1 148  ? 176.721 180.834 114.828 1.00 69.95  ? 148  TYR A C   1 
ATOM   1185 O O   . TYR A 1 148  ? 175.619 181.191 114.395 1.00 73.01  ? 148  TYR A O   1 
ATOM   1186 C CB  . TYR A 1 148  ? 176.944 179.859 117.123 1.00 66.95  ? 148  TYR A CB  1 
ATOM   1187 C CG  . TYR A 1 148  ? 175.847 180.768 117.623 1.00 72.02  ? 148  TYR A CG  1 
ATOM   1188 C CD1 . TYR A 1 148  ? 174.616 180.256 118.000 1.00 76.55  ? 148  TYR A CD1 1 
ATOM   1189 C CD2 . TYR A 1 148  ? 176.044 182.137 117.723 1.00 73.70  ? 148  TYR A CD2 1 
ATOM   1190 C CE1 . TYR A 1 148  ? 173.611 181.080 118.457 1.00 75.80  ? 148  TYR A CE1 1 
ATOM   1191 C CE2 . TYR A 1 148  ? 175.044 182.969 118.179 1.00 74.09  ? 148  TYR A CE2 1 
ATOM   1192 C CZ  . TYR A 1 148  ? 173.830 182.435 118.545 1.00 75.97  ? 148  TYR A CZ  1 
ATOM   1193 O OH  . TYR A 1 148  ? 172.829 183.261 119.001 1.00 71.06  ? 148  TYR A OH  1 
ATOM   1194 N N   . LYS A 1 149  ? 177.832 181.541 114.617 1.00 83.34  ? 149  LYS A N   1 
ATOM   1195 C CA  . LYS A 1 149  ? 177.785 182.761 113.818 1.00 84.84  ? 149  LYS A CA  1 
ATOM   1196 C C   . LYS A 1 149  ? 177.334 182.462 112.392 1.00 84.02  ? 149  LYS A C   1 
ATOM   1197 O O   . LYS A 1 149  ? 176.449 183.139 111.846 1.00 82.11  ? 149  LYS A O   1 
ATOM   1198 C CB  . LYS A 1 149  ? 179.157 183.436 113.824 1.00 81.43  ? 149  LYS A CB  1 
ATOM   1199 C CG  . LYS A 1 149  ? 179.201 184.775 113.113 1.00 83.91  ? 149  LYS A CG  1 
ATOM   1200 C CD  . LYS A 1 149  ? 180.595 185.380 113.175 1.00 86.60  ? 149  LYS A CD  1 
ATOM   1201 C CE  . LYS A 1 149  ? 180.632 186.751 112.522 1.00 85.25  ? 149  LYS A CE  1 
ATOM   1202 N NZ  . LYS A 1 149  ? 180.215 186.699 111.095 1.00 82.11  ? 149  LYS A NZ  1 
ATOM   1203 N N   . THR A 1 150  ? 177.919 181.429 111.781 1.00 72.39  ? 150  THR A N   1 
ATOM   1204 C CA  . THR A 1 150  ? 177.554 181.081 110.412 1.00 68.09  ? 150  THR A CA  1 
ATOM   1205 C C   . THR A 1 150  ? 176.090 180.671 110.321 1.00 71.01  ? 150  THR A C   1 
ATOM   1206 O O   . THR A 1 150  ? 175.385 181.058 109.383 1.00 74.42  ? 150  THR A O   1 
ATOM   1207 C CB  . THR A 1 150  ? 178.454 179.960 109.900 1.00 67.45  ? 150  THR A CB  1 
ATOM   1208 O OG1 . THR A 1 150  ? 179.825 180.356 110.027 1.00 80.13  ? 150  THR A OG1 1 
ATOM   1209 C CG2 . THR A 1 150  ? 178.155 179.666 108.443 1.00 68.84  ? 150  THR A CG2 1 
ATOM   1210 N N   . LEU A 1 151  ? 175.612 179.899 111.297 1.00 73.09  ? 151  LEU A N   1 
ATOM   1211 C CA  . LEU A 1 151  ? 174.238 179.419 111.266 1.00 71.21  ? 151  LEU A CA  1 
ATOM   1212 C C   . LEU A 1 151  ? 173.248 180.551 111.484 1.00 72.52  ? 151  LEU A C   1 
ATOM   1213 O O   . LEU A 1 151  ? 172.180 180.563 110.869 1.00 74.32  ? 151  LEU A O   1 
ATOM   1214 C CB  . LEU A 1 151  ? 174.038 178.322 112.309 1.00 64.89  ? 151  LEU A CB  1 
ATOM   1215 C CG  . LEU A 1 151  ? 174.667 176.972 111.973 1.00 63.38  ? 151  LEU A CG  1 
ATOM   1216 C CD1 . LEU A 1 151  ? 174.346 175.953 113.047 1.00 65.62  ? 151  LEU A CD1 1 
ATOM   1217 C CD2 . LEU A 1 151  ? 174.195 176.490 110.615 1.00 65.21  ? 151  LEU A CD2 1 
ATOM   1218 N N   . ILE A 1 152  ? 173.571 181.511 112.351 1.00 77.81  ? 152  ILE A N   1 
ATOM   1219 C CA  . ILE A 1 152  ? 172.653 182.628 112.548 1.00 80.07  ? 152  ILE A CA  1 
ATOM   1220 C C   . ILE A 1 152  ? 172.613 183.507 111.300 1.00 77.76  ? 152  ILE A C   1 
ATOM   1221 O O   . ILE A 1 152  ? 171.544 183.989 110.897 1.00 77.97  ? 152  ILE A O   1 
ATOM   1222 C CB  . ILE A 1 152  ? 173.017 183.418 113.821 1.00 82.55  ? 152  ILE A CB  1 
ATOM   1223 C CG1 . ILE A 1 152  ? 171.811 184.216 114.313 1.00 81.60  ? 152  ILE A CG1 1 
ATOM   1224 C CG2 . ILE A 1 152  ? 174.199 184.343 113.604 1.00 81.50  ? 152  ILE A CG2 1 
ATOM   1225 C CD1 . ILE A 1 152  ? 170.659 183.353 114.767 1.00 80.93  ? 152  ILE A CD1 1 
ATOM   1226 N N   . GLN A 1 153  ? 173.762 183.695 110.640 1.00 80.82  ? 153  GLN A N   1 
ATOM   1227 C CA  . GLN A 1 153  ? 173.763 184.428 109.377 1.00 83.69  ? 153  GLN A CA  1 
ATOM   1228 C C   . GLN A 1 153  ? 172.928 183.710 108.323 1.00 81.24  ? 153  GLN A C   1 
ATOM   1229 O O   . GLN A 1 153  ? 172.127 184.336 107.614 1.00 80.34  ? 153  GLN A O   1 
ATOM   1230 C CB  . GLN A 1 153  ? 175.198 184.621 108.888 1.00 84.27  ? 153  GLN A CB  1 
ATOM   1231 C CG  . GLN A 1 153  ? 175.310 185.135 107.463 1.00 83.56  ? 153  GLN A CG  1 
ATOM   1232 C CD  . GLN A 1 153  ? 174.839 186.566 107.316 1.00 85.76  ? 153  GLN A CD  1 
ATOM   1233 O OE1 . GLN A 1 153  ? 174.771 187.314 108.291 1.00 85.01  ? 153  GLN A OE1 1 
ATOM   1234 N NE2 . GLN A 1 153  ? 174.510 186.956 106.091 1.00 85.57  ? 153  GLN A NE2 1 
ATOM   1235 N N   . ARG A 1 154  ? 173.096 182.391 108.214 1.00 70.90  ? 154  ARG A N   1 
ATOM   1236 C CA  . ARG A 1 154  ? 172.340 181.624 107.232 1.00 71.14  ? 154  ARG A CA  1 
ATOM   1237 C C   . ARG A 1 154  ? 170.853 181.636 107.552 1.00 76.28  ? 154  ARG A C   1 
ATOM   1238 O O   . ARG A 1 154  ? 170.017 181.668 106.645 1.00 78.76  ? 154  ARG A O   1 
ATOM   1239 C CB  . ARG A 1 154  ? 172.869 180.194 107.174 1.00 75.19  ? 154  ARG A CB  1 
ATOM   1240 C CG  . ARG A 1 154  ? 172.304 179.360 106.044 1.00 74.70  ? 154  ARG A CG  1 
ATOM   1241 C CD  . ARG A 1 154  ? 173.123 178.101 105.871 1.00 71.18  ? 154  ARG A CD  1 
ATOM   1242 N NE  . ARG A 1 154  ? 174.531 178.413 105.667 1.00 73.79  ? 154  ARG A NE  1 
ATOM   1243 C CZ  . ARG A 1 154  ? 175.506 177.516 105.683 1.00 76.63  ? 154  ARG A CZ  1 
ATOM   1244 N NH1 . ARG A 1 154  ? 175.263 176.235 105.900 1.00 74.95  ? 154  ARG A NH1 1 
ATOM   1245 N NH2 . ARG A 1 154  ? 176.757 177.916 105.478 1.00 79.90  ? 154  ARG A NH2 1 
ATOM   1246 N N   . SER A 1 155  ? 170.505 181.598 108.838 1.00 78.82  ? 155  SER A N   1 
ATOM   1247 C CA  . SER A 1 155  ? 169.105 181.673 109.232 1.00 74.62  ? 155  SER A CA  1 
ATOM   1248 C C   . SER A 1 155  ? 168.495 183.004 108.825 1.00 75.95  ? 155  SER A C   1 
ATOM   1249 O O   . SER A 1 155  ? 167.378 183.046 108.295 1.00 74.69  ? 155  SER A O   1 
ATOM   1250 C CB  . SER A 1 155  ? 168.975 181.462 110.738 1.00 75.55  ? 155  SER A CB  1 
ATOM   1251 O OG  . SER A 1 155  ? 167.640 181.657 111.165 1.00 78.68  ? 155  SER A OG  1 
ATOM   1252 N N   . GLU A 1 156  ? 169.215 184.103 109.060 1.00 89.76  ? 156  GLU A N   1 
ATOM   1253 C CA  . GLU A 1 156  ? 168.721 185.406 108.626 1.00 87.27  ? 156  GLU A CA  1 
ATOM   1254 C C   . GLU A 1 156  ? 168.524 185.437 107.115 1.00 86.72  ? 156  GLU A C   1 
ATOM   1255 O O   . GLU A 1 156  ? 167.479 185.879 106.619 1.00 88.33  ? 156  GLU A O   1 
ATOM   1256 C CB  . GLU A 1 156  ? 169.684 186.507 109.067 1.00 85.97  ? 156  GLU A CB  1 
ATOM   1257 C CG  . GLU A 1 156  ? 169.768 186.697 110.571 1.00 88.82  ? 156  GLU A CG  1 
ATOM   1258 C CD  . GLU A 1 156  ? 170.788 187.747 110.969 1.00 90.78  ? 156  GLU A CD  1 
ATOM   1259 O OE1 . GLU A 1 156  ? 171.574 188.175 110.097 1.00 88.62  ? 156  GLU A OE1 1 
ATOM   1260 O OE2 . GLU A 1 156  ? 170.804 188.145 112.152 1.00 90.57  ? 156  GLU A OE2 1 
ATOM   1261 N N   . GLU A 1 157  ? 169.517 184.947 106.367 1.00 84.56  ? 157  GLU A N   1 
ATOM   1262 C CA  . GLU A 1 157  ? 169.423 184.973 104.911 1.00 85.86  ? 157  GLU A CA  1 
ATOM   1263 C C   . GLU A 1 157  ? 168.251 184.137 104.411 1.00 84.65  ? 157  GLU A C   1 
ATOM   1264 O O   . GLU A 1 157  ? 167.499 184.572 103.531 1.00 83.63  ? 157  GLU A O   1 
ATOM   1265 C CB  . GLU A 1 157  ? 170.730 184.481 104.291 1.00 85.84  ? 157  GLU A CB  1 
ATOM   1266 C CG  . GLU A 1 157  ? 171.923 185.375 104.568 1.00 89.54  ? 157  GLU A CG  1 
ATOM   1267 C CD  . GLU A 1 157  ? 173.218 184.795 104.038 1.00 89.35  ? 157  GLU A CD  1 
ATOM   1268 O OE1 . GLU A 1 157  ? 173.191 183.664 103.510 1.00 88.38  ? 157  GLU A OE1 1 
ATOM   1269 O OE2 . GLU A 1 157  ? 174.264 185.469 104.150 1.00 87.50  ? 157  GLU A OE2 1 
ATOM   1270 N N   . ASN A 1 158  ? 168.078 182.934 104.961 1.00 80.56  ? 158  ASN A N   1 
ATOM   1271 C CA  . ASN A 1 158  ? 167.002 182.060 104.511 1.00 77.38  ? 158  ASN A CA  1 
ATOM   1272 C C   . ASN A 1 158  ? 165.637 182.624 104.877 1.00 80.93  ? 158  ASN A C   1 
ATOM   1273 O O   . ASN A 1 158  ? 164.697 182.550 104.077 1.00 82.32  ? 158  ASN A O   1 
ATOM   1274 C CB  . ASN A 1 158  ? 167.183 180.663 105.099 1.00 76.11  ? 158  ASN A CB  1 
ATOM   1275 C CG  . ASN A 1 158  ? 168.422 179.971 104.579 1.00 77.71  ? 158  ASN A CG  1 
ATOM   1276 O OD1 . ASN A 1 158  ? 168.877 180.240 103.469 1.00 83.38  ? 158  ASN A OD1 1 
ATOM   1277 N ND2 . ASN A 1 158  ? 168.975 179.070 105.380 1.00 76.25  ? 158  ASN A ND2 1 
ATOM   1278 N N   . LEU A 1 159  ? 165.501 183.185 106.081 1.00 76.61  ? 159  LEU A N   1 
ATOM   1279 C CA  . LEU A 1 159  ? 164.227 183.780 106.467 1.00 73.79  ? 159  LEU A CA  1 
ATOM   1280 C C   . LEU A 1 159  ? 163.880 184.959 105.573 1.00 79.66  ? 159  LEU A C   1 
ATOM   1281 O O   . LEU A 1 159  ? 162.717 185.137 105.195 1.00 82.25  ? 159  LEU A O   1 
ATOM   1282 C CB  . LEU A 1 159  ? 164.265 184.205 107.933 1.00 73.81  ? 159  LEU A CB  1 
ATOM   1283 C CG  . LEU A 1 159  ? 163.980 183.094 108.942 1.00 73.26  ? 159  LEU A CG  1 
ATOM   1284 C CD1 . LEU A 1 159  ? 164.091 183.618 110.361 1.00 77.43  ? 159  LEU A CD1 1 
ATOM   1285 C CD2 . LEU A 1 159  ? 162.604 182.505 108.698 1.00 75.65  ? 159  LEU A CD2 1 
ATOM   1286 N N   . LYS A 1 160  ? 164.873 185.780 105.223 1.00 88.53  ? 160  LYS A N   1 
ATOM   1287 C CA  . LYS A 1 160  ? 164.608 186.875 104.296 1.00 88.40  ? 160  LYS A CA  1 
ATOM   1288 C C   . LYS A 1 160  ? 164.224 186.351 102.918 1.00 87.02  ? 160  LYS A C   1 
ATOM   1289 O O   . LYS A 1 160  ? 163.300 186.873 102.283 1.00 87.85  ? 160  LYS A O   1 
ATOM   1290 C CB  . LYS A 1 160  ? 165.821 187.799 104.209 1.00 86.99  ? 160  LYS A CB  1 
ATOM   1291 C CG  . LYS A 1 160  ? 166.109 188.533 105.505 1.00 88.71  ? 160  LYS A CG  1 
ATOM   1292 C CD  . LYS A 1 160  ? 164.867 189.248 106.010 1.00 86.99  ? 160  LYS A CD  1 
ATOM   1293 C CE  . LYS A 1 160  ? 165.010 189.636 107.472 1.00 89.02  ? 160  LYS A CE  1 
ATOM   1294 N NZ  . LYS A 1 160  ? 165.133 188.439 108.350 1.00 83.07  ? 160  LYS A NZ  1 
ATOM   1295 N N   . SER A 1 161  ? 164.917 185.318 102.438 1.00 87.47  ? 161  SER A N   1 
ATOM   1296 C CA  . SER A 1 161  ? 164.609 184.769 101.122 1.00 90.19  ? 161  SER A CA  1 
ATOM   1297 C C   . SER A 1 161  ? 163.273 184.037 101.128 1.00 90.25  ? 161  SER A C   1 
ATOM   1298 O O   . SER A 1 161  ? 162.440 184.236 100.237 1.00 87.75  ? 161  SER A O   1 
ATOM   1299 C CB  . SER A 1 161  ? 165.730 183.835 100.668 1.00 90.89  ? 161  SER A CB  1 
ATOM   1300 O OG  . SER A 1 161  ? 165.820 182.704 101.514 1.00 91.44  ? 161  SER A OG  1 
ATOM   1301 N N   . GLY A 1 162  ? 163.051 183.188 102.126 1.00 91.75  ? 162  GLY A N   1 
ATOM   1302 C CA  . GLY A 1 162  ? 161.807 182.437 102.208 1.00 89.56  ? 162  GLY A CA  1 
ATOM   1303 C C   . GLY A 1 162  ? 161.593 181.467 101.066 1.00 92.09  ? 162  GLY A C   1 
ATOM   1304 O O   . GLY A 1 162  ? 160.471 181.348 100.558 1.00 91.09  ? 162  GLY A O   1 
ATOM   1305 N N   . LYS A 1 163  ? 162.644 180.766 100.651 1.00 92.99  ? 163  LYS A N   1 
ATOM   1306 C CA  . LYS A 1 163  ? 162.571 179.793 99.570  1.00 90.25  ? 163  LYS A CA  1 
ATOM   1307 C C   . LYS A 1 163  ? 163.002 178.429 100.083 1.00 91.79  ? 163  LYS A C   1 
ATOM   1308 O O   . LYS A 1 163  ? 163.973 178.324 100.839 1.00 94.39  ? 163  LYS A O   1 
ATOM   1309 C CB  . LYS A 1 163  ? 163.447 180.212 98.386  1.00 90.34  ? 163  LYS A CB  1 
ATOM   1310 C CG  . LYS A 1 163  ? 162.775 181.180 97.431  1.00 92.96  ? 163  LYS A CG  1 
ATOM   1311 C CD  . LYS A 1 163  ? 163.682 181.520 96.262  1.00 92.17  ? 163  LYS A CD  1 
ATOM   1312 C CE  . LYS A 1 163  ? 162.915 182.235 95.161  1.00 91.76  ? 163  LYS A CE  1 
ATOM   1313 N NZ  . LYS A 1 163  ? 162.209 183.445 95.663  1.00 91.11  ? 163  LYS A NZ  1 
ATOM   1314 N N   . ILE A 1 164  ? 162.280 177.393 99.675  1.00 81.54  ? 164  ILE A N   1 
ATOM   1315 C CA  . ILE A 1 164  ? 162.590 176.015 100.036 1.00 80.74  ? 164  ILE A CA  1 
ATOM   1316 C C   . ILE A 1 164  ? 163.003 175.307 98.752  1.00 83.67  ? 164  ILE A C   1 
ATOM   1317 O O   . ILE A 1 164  ? 162.190 175.125 97.840  1.00 87.61  ? 164  ILE A O   1 
ATOM   1318 C CB  . ILE A 1 164  ? 161.407 175.312 100.709 1.00 78.43  ? 164  ILE A CB  1 
ATOM   1319 C CG1 . ILE A 1 164  ? 161.138 175.905 102.092 1.00 79.84  ? 164  ILE A CG1 1 
ATOM   1320 C CG2 . ILE A 1 164  ? 161.671 173.827 100.821 1.00 81.62  ? 164  ILE A CG2 1 
ATOM   1321 C CD1 . ILE A 1 164  ? 160.184 177.078 102.089 1.00 82.44  ? 164  ILE A CD1 1 
ATOM   1322 N N   . ASN A 1 165  ? 164.269 174.907 98.673  1.00 90.83  ? 165  ASN A N   1 
ATOM   1323 C CA  . ASN A 1 165  ? 164.803 174.217 97.503  1.00 90.82  ? 165  ASN A CA  1 
ATOM   1324 C C   . ASN A 1 165  ? 165.769 173.143 97.981  1.00 91.76  ? 165  ASN A C   1 
ATOM   1325 O O   . ASN A 1 165  ? 166.894 173.451 98.386  1.00 93.97  ? 165  ASN A O   1 
ATOM   1326 C CB  . ASN A 1 165  ? 165.494 175.196 96.556  1.00 91.71  ? 165  ASN A CB  1 
ATOM   1327 C CG  . ASN A 1 165  ? 165.815 174.578 95.212  1.00 94.98  ? 165  ASN A CG  1 
ATOM   1328 O OD1 . ASN A 1 165  ? 165.405 173.456 94.917  1.00 96.24  ? 165  ASN A OD1 1 
ATOM   1329 N ND2 . ASN A 1 165  ? 166.546 175.312 94.384  1.00 96.29  ? 165  ASN A ND2 1 
ATOM   1330 N N   . GLY A 1 166  ? 165.336 171.888 97.931  1.00 79.25  ? 166  GLY A N   1 
ATOM   1331 C CA  . GLY A 1 166  ? 166.159 170.789 98.392  1.00 77.74  ? 166  GLY A CA  1 
ATOM   1332 C C   . GLY A 1 166  ? 166.958 170.141 97.282  1.00 79.08  ? 166  GLY A C   1 
ATOM   1333 O O   . GLY A 1 166  ? 167.423 169.006 97.422  1.00 80.83  ? 166  GLY A O   1 
ATOM   1334 N N   . SER A 1 167  ? 167.125 170.856 96.168  1.00 81.73  ? 167  SER A N   1 
ATOM   1335 C CA  . SER A 1 167  ? 167.816 170.289 95.017  1.00 82.68  ? 167  SER A CA  1 
ATOM   1336 C C   . SER A 1 167  ? 169.316 170.152 95.239  1.00 85.15  ? 167  SER A C   1 
ATOM   1337 O O   . SER A 1 167  ? 169.944 169.292 94.613  1.00 83.23  ? 167  SER A O   1 
ATOM   1338 C CB  . SER A 1 167  ? 167.556 171.146 93.779  1.00 79.94  ? 167  SER A CB  1 
ATOM   1339 O OG  . SER A 1 167  ? 166.168 171.274 93.533  1.00 82.78  ? 167  SER A OG  1 
ATOM   1340 N N   . LEU A 1 168  ? 169.905 170.968 96.112  1.00 89.09  ? 168  LEU A N   1 
ATOM   1341 C CA  . LEU A 1 168  ? 171.346 170.947 96.319  1.00 86.72  ? 168  LEU A CA  1 
ATOM   1342 C C   . LEU A 1 168  ? 171.791 169.993 97.417  1.00 85.26  ? 168  LEU A C   1 
ATOM   1343 O O   . LEU A 1 168  ? 172.989 169.711 97.519  1.00 85.75  ? 168  LEU A O   1 
ATOM   1344 C CB  . LEU A 1 168  ? 171.860 172.355 96.648  1.00 86.23  ? 168  LEU A CB  1 
ATOM   1345 C CG  . LEU A 1 168  ? 172.150 173.294 95.473  1.00 86.64  ? 168  LEU A CG  1 
ATOM   1346 C CD1 . LEU A 1 168  ? 173.081 172.624 94.476  1.00 86.26  ? 168  LEU A CD1 1 
ATOM   1347 C CD2 . LEU A 1 168  ? 170.870 173.756 94.792  1.00 84.43  ? 168  LEU A CD2 1 
ATOM   1348 N N   . PHE A 1 169  ? 170.869 169.492 98.230  1.00 77.11  ? 169  PHE A N   1 
ATOM   1349 C CA  . PHE A 1 169  ? 171.232 168.619 99.334  1.00 76.72  ? 169  PHE A CA  1 
ATOM   1350 C C   . PHE A 1 169  ? 171.563 167.218 98.836  1.00 78.26  ? 169  PHE A C   1 
ATOM   1351 O O   . PHE A 1 169  ? 171.091 166.779 97.784  1.00 79.82  ? 169  PHE A O   1 
ATOM   1352 C CB  . PHE A 1 169  ? 170.099 168.553 100.354 1.00 70.86  ? 169  PHE A CB  1 
ATOM   1353 C CG  . PHE A 1 169  ? 169.726 169.884 100.929 1.00 69.36  ? 169  PHE A CG  1 
ATOM   1354 C CD1 . PHE A 1 169  ? 170.689 170.847 101.158 1.00 73.86  ? 169  PHE A CD1 1 
ATOM   1355 C CD2 . PHE A 1 169  ? 168.410 170.177 101.230 1.00 69.52  ? 169  PHE A CD2 1 
ATOM   1356 C CE1 . PHE A 1 169  ? 170.348 172.074 101.684 1.00 73.12  ? 169  PHE A CE1 1 
ATOM   1357 C CE2 . PHE A 1 169  ? 168.063 171.401 101.755 1.00 73.77  ? 169  PHE A CE2 1 
ATOM   1358 C CZ  . PHE A 1 169  ? 169.033 172.351 101.982 1.00 73.66  ? 169  PHE A CZ  1 
ATOM   1359 N N   . ASP A 1 170  ? 172.390 166.519 99.606  1.00 82.65  ? 170  ASP A N   1 
ATOM   1360 C CA  . ASP A 1 170  ? 172.759 165.141 99.308  1.00 83.25  ? 170  ASP A CA  1 
ATOM   1361 C C   . ASP A 1 170  ? 171.858 164.205 100.103 1.00 86.28  ? 170  ASP A C   1 
ATOM   1362 O O   . ASP A 1 170  ? 171.870 164.226 101.338 1.00 87.20  ? 170  ASP A O   1 
ATOM   1363 C CB  . ASP A 1 170  ? 174.229 164.896 99.646  1.00 83.95  ? 170  ASP A CB  1 
ATOM   1364 C CG  . ASP A 1 170  ? 174.691 163.504 99.266  1.00 86.12  ? 170  ASP A CG  1 
ATOM   1365 O OD1 . ASP A 1 170  ? 173.963 162.811 98.527  1.00 85.19  ? 170  ASP A OD1 1 
ATOM   1366 O OD2 . ASP A 1 170  ? 175.786 163.103 99.711  1.00 86.47  ? 170  ASP A OD2 1 
ATOM   1367 N N   . TYR A 1 171  ? 171.083 163.384 99.398  1.00 80.05  ? 171  TYR A N   1 
ATOM   1368 C CA  . TYR A 1 171  ? 170.124 162.489 100.028 1.00 77.79  ? 171  TYR A CA  1 
ATOM   1369 C C   . TYR A 1 171  ? 170.639 161.062 100.160 1.00 78.06  ? 171  TYR A C   1 
ATOM   1370 O O   . TYR A 1 171  ? 169.867 160.168 100.519 1.00 77.86  ? 171  TYR A O   1 
ATOM   1371 C CB  . TYR A 1 171  ? 168.808 162.499 99.252  1.00 77.50  ? 171  TYR A CB  1 
ATOM   1372 C CG  . TYR A 1 171  ? 168.129 163.848 99.228  1.00 74.64  ? 171  TYR A CG  1 
ATOM   1373 C CD1 . TYR A 1 171  ? 167.311 164.253 100.272 1.00 72.13  ? 171  TYR A CD1 1 
ATOM   1374 C CD2 . TYR A 1 171  ? 168.305 164.714 98.161  1.00 77.50  ? 171  TYR A CD2 1 
ATOM   1375 C CE1 . TYR A 1 171  ? 166.689 165.482 100.253 1.00 70.36  ? 171  TYR A CE1 1 
ATOM   1376 C CE2 . TYR A 1 171  ? 167.687 165.944 98.134  1.00 79.47  ? 171  TYR A CE2 1 
ATOM   1377 C CZ  . TYR A 1 171  ? 166.880 166.323 99.182  1.00 76.70  ? 171  TYR A CZ  1 
ATOM   1378 O OH  . TYR A 1 171  ? 166.264 167.550 99.156  1.00 81.17  ? 171  TYR A OH  1 
ATOM   1379 N N   . SER A 1 172  ? 171.915 160.828 99.877  1.00 86.42  ? 172  SER A N   1 
ATOM   1380 C CA  . SER A 1 172  ? 172.475 159.492 100.013 1.00 86.00  ? 172  SER A CA  1 
ATOM   1381 C C   . SER A 1 172  ? 172.598 159.109 101.483 1.00 85.33  ? 172  SER A C   1 
ATOM   1382 O O   . SER A 1 172  ? 172.693 159.965 102.366 1.00 86.02  ? 172  SER A O   1 
ATOM   1383 C CB  . SER A 1 172  ? 173.844 159.416 99.340  1.00 87.04  ? 172  SER A CB  1 
ATOM   1384 O OG  . SER A 1 172  ? 174.761 160.302 99.957  1.00 87.88  ? 172  SER A OG  1 
ATOM   1385 N N   . ASP A 1 173  ? 172.589 157.804 101.741 1.00 88.54  ? 173  ASP A N   1 
ATOM   1386 C CA  . ASP A 1 173  ? 172.735 157.316 103.104 1.00 89.65  ? 173  ASP A CA  1 
ATOM   1387 C C   . ASP A 1 173  ? 174.114 157.661 103.650 1.00 92.98  ? 173  ASP A C   1 
ATOM   1388 O O   . ASP A 1 173  ? 175.119 157.590 102.938 1.00 94.42  ? 173  ASP A O   1 
ATOM   1389 C CB  . ASP A 1 173  ? 172.511 155.805 103.156 1.00 90.11  ? 173  ASP A CB  1 
ATOM   1390 C CG  . ASP A 1 173  ? 171.056 155.426 102.978 1.00 94.77  ? 173  ASP A CG  1 
ATOM   1391 O OD1 . ASP A 1 173  ? 170.183 156.165 103.480 1.00 93.60  ? 173  ASP A OD1 1 
ATOM   1392 O OD2 . ASP A 1 173  ? 170.784 154.390 102.337 1.00 96.34  ? 173  ASP A OD2 1 
ATOM   1393 N N   . LEU A 1 174  ? 174.156 158.043 104.921 1.00 91.74  ? 174  LEU A N   1 
ATOM   1394 C CA  . LEU A 1 174  ? 175.407 158.421 105.556 1.00 89.57  ? 174  LEU A CA  1 
ATOM   1395 C C   . LEU A 1 174  ? 176.256 157.193 105.860 1.00 90.54  ? 174  LEU A C   1 
ATOM   1396 O O   . LEU A 1 174  ? 175.750 156.078 106.006 1.00 89.22  ? 174  LEU A O   1 
ATOM   1397 C CB  . LEU A 1 174  ? 175.144 159.197 106.845 1.00 87.66  ? 174  LEU A CB  1 
ATOM   1398 C CG  . LEU A 1 174  ? 174.381 160.513 106.707 1.00 89.10  ? 174  LEU A CG  1 
ATOM   1399 C CD1 . LEU A 1 174  ? 174.282 161.213 108.050 1.00 89.07  ? 174  LEU A CD1 1 
ATOM   1400 C CD2 . LEU A 1 174  ? 175.045 161.412 105.681 1.00 90.78  ? 174  LEU A CD2 1 
ATOM   1401 N N   . ASP A 1 175  ? 177.563 157.413 105.951 1.00 107.60 ? 175  ASP A N   1 
ATOM   1402 C CA  . ASP A 1 175  ? 178.482 156.362 106.351 1.00 107.41 ? 175  ASP A CA  1 
ATOM   1403 C C   . ASP A 1 175  ? 178.347 156.089 107.848 1.00 107.03 ? 175  ASP A C   1 
ATOM   1404 O O   . ASP A 1 175  ? 177.680 156.822 108.583 1.00 106.88 ? 175  ASP A O   1 
ATOM   1405 C CB  . ASP A 1 175  ? 179.920 156.755 106.003 1.00 105.12 ? 175  ASP A CB  1 
ATOM   1406 C CG  . ASP A 1 175  ? 180.876 155.577 106.024 1.00 106.73 ? 175  ASP A CG  1 
ATOM   1407 O OD1 . ASP A 1 175  ? 180.948 154.881 107.058 1.00 107.56 ? 175  ASP A OD1 1 
ATOM   1408 O OD2 . ASP A 1 175  ? 181.553 155.343 105.001 1.00 107.25 ? 175  ASP A OD2 1 
ATOM   1409 N N   . GLU A 1 176  ? 178.984 155.004 108.294 1.00 114.70 ? 176  GLU A N   1 
ATOM   1410 C CA  . GLU A 1 176  ? 178.971 154.668 109.714 1.00 114.73 ? 176  GLU A CA  1 
ATOM   1411 C C   . GLU A 1 176  ? 179.538 155.799 110.561 1.00 115.59 ? 176  GLU A C   1 
ATOM   1412 O O   . GLU A 1 176  ? 179.094 156.008 111.696 1.00 115.14 ? 176  GLU A O   1 
ATOM   1413 C CB  . GLU A 1 176  ? 179.756 153.378 109.954 1.00 114.80 ? 176  GLU A CB  1 
ATOM   1414 C CG  . GLU A 1 176  ? 179.781 152.921 111.402 1.00 115.34 ? 176  GLU A CG  1 
ATOM   1415 C CD  . GLU A 1 176  ? 180.542 151.625 111.587 1.00 118.37 ? 176  GLU A CD  1 
ATOM   1416 O OE1 . GLU A 1 176  ? 180.907 150.999 110.570 1.00 118.10 ? 176  GLU A OE1 1 
ATOM   1417 O OE2 . GLU A 1 176  ? 180.776 151.231 112.749 1.00 119.83 ? 176  GLU A OE2 1 
ATOM   1418 N N   . ASN A 1 177  ? 180.504 156.542 110.029 1.00 116.83 ? 177  ASN A N   1 
ATOM   1419 C CA  . ASN A 1 177  ? 181.057 157.698 110.720 1.00 117.04 ? 177  ASN A CA  1 
ATOM   1420 C C   . ASN A 1 177  ? 180.253 158.968 110.483 1.00 115.23 ? 177  ASN A C   1 
ATOM   1421 O O   . ASN A 1 177  ? 180.637 160.028 110.986 1.00 114.63 ? 177  ASN A O   1 
ATOM   1422 C CB  . ASN A 1 177  ? 182.509 157.923 110.293 1.00 116.70 ? 177  ASN A CB  1 
ATOM   1423 C CG  . ASN A 1 177  ? 183.411 156.769 110.673 1.00 118.18 ? 177  ASN A CG  1 
ATOM   1424 O OD1 . ASN A 1 177  ? 182.941 155.671 110.972 1.00 118.03 ? 177  ASN A OD1 1 
ATOM   1425 N ND2 . ASN A 1 177  ? 184.717 157.009 110.663 1.00 115.76 ? 177  ASN A ND2 1 
ATOM   1426 N N   . GLY A 1 178  ? 179.155 158.889 109.733 1.00 103.94 ? 178  GLY A N   1 
ATOM   1427 C CA  . GLY A 1 178  ? 178.347 160.047 109.429 1.00 102.78 ? 178  GLY A CA  1 
ATOM   1428 C C   . GLY A 1 178  ? 178.717 160.767 108.153 1.00 104.30 ? 178  GLY A C   1 
ATOM   1429 O O   . GLY A 1 178  ? 178.015 161.711 107.769 1.00 108.01 ? 178  GLY A O   1 
ATOM   1430 N N   . LYS A 1 179  ? 179.790 160.359 107.485 1.00 107.80 ? 179  LYS A N   1 
ATOM   1431 C CA  . LYS A 1 179  ? 180.180 160.989 106.234 1.00 108.76 ? 179  LYS A CA  1 
ATOM   1432 C C   . LYS A 1 179  ? 179.207 160.620 105.120 1.00 108.37 ? 179  LYS A C   1 
ATOM   1433 O O   . LYS A 1 179  ? 178.510 159.604 105.182 1.00 111.30 ? 179  LYS A O   1 
ATOM   1434 C CB  . LYS A 1 179  ? 181.601 160.576 105.853 1.00 107.19 ? 179  LYS A CB  1 
ATOM   1435 C CG  . LYS A 1 179  ? 182.659 161.059 106.828 1.00 107.59 ? 179  LYS A CG  1 
ATOM   1436 C CD  . LYS A 1 179  ? 183.987 160.363 106.596 1.00 109.66 ? 179  LYS A CD  1 
ATOM   1437 C CE  . LYS A 1 179  ? 183.882 158.874 106.885 1.00 111.08 ? 179  LYS A CE  1 
ATOM   1438 N NZ  . LYS A 1 179  ? 185.190 158.181 106.725 1.00 109.26 ? 179  LYS A NZ  1 
ATOM   1439 N N   . SER A 1 180  ? 179.162 161.464 104.095 1.00 103.81 ? 180  SER A N   1 
ATOM   1440 C CA  . SER A 1 180  ? 178.270 161.250 102.961 1.00 105.52 ? 180  SER A CA  1 
ATOM   1441 C C   . SER A 1 180  ? 178.632 159.981 102.196 1.00 105.99 ? 180  SER A C   1 
ATOM   1442 O O   . SER A 1 180  ? 179.802 159.729 101.911 1.00 107.57 ? 180  SER A O   1 
ATOM   1443 C CB  . SER A 1 180  ? 178.305 162.456 102.020 1.00 105.04 ? 180  SER A CB  1 
ATOM   1444 O OG  . SER A 1 180  ? 179.616 162.683 101.533 1.00 105.25 ? 180  SER A OG  1 
ATOM   1445 N N   . ASN A 1 292  ? 188.093 168.836 118.194 1.00 98.46  ? 292  ASN A N   1 
ATOM   1446 C CA  . ASN A 1 292  ? 188.763 168.024 117.186 1.00 99.96  ? 292  ASN A CA  1 
ATOM   1447 C C   . ASN A 1 292  ? 188.015 168.078 115.860 1.00 101.88 ? 292  ASN A C   1 
ATOM   1448 O O   . ASN A 1 292  ? 188.608 167.937 114.790 1.00 102.90 ? 292  ASN A O   1 
ATOM   1449 C CB  . ASN A 1 292  ? 188.886 166.576 117.661 1.00 100.21 ? 292  ASN A CB  1 
ATOM   1450 C CG  . ASN A 1 292  ? 189.660 165.710 116.691 1.00 101.78 ? 292  ASN A CG  1 
ATOM   1451 O OD1 . ASN A 1 292  ? 190.544 166.190 115.983 1.00 102.29 ? 292  ASN A OD1 1 
ATOM   1452 N ND2 . ASN A 1 292  ? 189.330 164.424 116.650 1.00 101.54 ? 292  ASN A ND2 1 
ATOM   1453 N N   . VAL A 1 293  ? 186.703 168.284 115.944 1.00 93.19  ? 293  VAL A N   1 
ATOM   1454 C CA  . VAL A 1 293  ? 185.839 168.346 114.771 1.00 91.04  ? 293  VAL A CA  1 
ATOM   1455 C C   . VAL A 1 293  ? 186.205 169.547 113.908 1.00 87.51  ? 293  VAL A C   1 
ATOM   1456 O O   . VAL A 1 293  ? 186.471 170.639 114.421 1.00 85.01  ? 293  VAL A O   1 
ATOM   1457 C CB  . VAL A 1 293  ? 184.359 168.391 115.187 1.00 89.21  ? 293  VAL A CB  1 
ATOM   1458 C CG1 . VAL A 1 293  ? 183.931 167.045 115.740 1.00 85.92  ? 293  VAL A CG1 1 
ATOM   1459 C CG2 . VAL A 1 293  ? 184.137 169.479 116.220 1.00 90.08  ? 293  VAL A CG2 1 
ATOM   1460 N N   . ASN A 1 294  ? 186.224 169.349 112.594 1.00 86.72  ? 294  ASN A N   1 
ATOM   1461 C CA  . ASN A 1 294  ? 186.585 170.391 111.642 1.00 88.50  ? 294  ASN A CA  1 
ATOM   1462 C C   . ASN A 1 294  ? 185.361 171.240 111.325 1.00 88.33  ? 294  ASN A C   1 
ATOM   1463 O O   . ASN A 1 294  ? 184.269 170.706 111.105 1.00 89.70  ? 294  ASN A O   1 
ATOM   1464 C CB  . ASN A 1 294  ? 187.156 169.786 110.361 1.00 90.14  ? 294  ASN A CB  1 
ATOM   1465 C CG  . ASN A 1 294  ? 188.480 169.089 110.586 1.00 89.63  ? 294  ASN A CG  1 
ATOM   1466 O OD1 . ASN A 1 294  ? 189.136 169.290 111.606 1.00 91.37  ? 294  ASN A OD1 1 
ATOM   1467 N ND2 . ASN A 1 294  ? 188.882 168.265 109.626 1.00 87.46  ? 294  ASN A ND2 1 
ATOM   1468 N N   . PHE A 1 295  ? 185.552 172.560 111.293 1.00 82.62  ? 295  PHE A N   1 
ATOM   1469 C CA  . PHE A 1 295  ? 184.461 173.471 110.968 1.00 83.27  ? 295  PHE A CA  1 
ATOM   1470 C C   . PHE A 1 295  ? 183.982 173.298 109.532 1.00 80.38  ? 295  PHE A C   1 
ATOM   1471 O O   . PHE A 1 295  ? 182.859 173.693 109.199 1.00 83.71  ? 295  PHE A O   1 
ATOM   1472 C CB  . PHE A 1 295  ? 184.912 174.912 111.219 1.00 83.70  ? 295  PHE A CB  1 
ATOM   1473 C CG  . PHE A 1 295  ? 183.934 175.947 110.755 1.00 82.58  ? 295  PHE A CG  1 
ATOM   1474 C CD1 . PHE A 1 295  ? 182.791 176.212 111.485 1.00 82.20  ? 295  PHE A CD1 1 
ATOM   1475 C CD2 . PHE A 1 295  ? 184.164 176.663 109.596 1.00 79.67  ? 295  PHE A CD2 1 
ATOM   1476 C CE1 . PHE A 1 295  ? 181.893 177.166 111.063 1.00 81.72  ? 295  PHE A CE1 1 
ATOM   1477 C CE2 . PHE A 1 295  ? 183.270 177.619 109.169 1.00 81.87  ? 295  PHE A CE2 1 
ATOM   1478 C CZ  . PHE A 1 295  ? 182.133 177.870 109.903 1.00 82.02  ? 295  PHE A CZ  1 
ATOM   1479 N N   . THR A 1 296  ? 184.817 172.715 108.670 1.00 86.30  ? 296  THR A N   1 
ATOM   1480 C CA  . THR A 1 296  ? 184.456 172.567 107.263 1.00 89.11  ? 296  THR A CA  1 
ATOM   1481 C C   . THR A 1 296  ? 183.233 171.676 107.093 1.00 91.64  ? 296  THR A C   1 
ATOM   1482 O O   . THR A 1 296  ? 182.352 171.956 106.272 1.00 91.89  ? 296  THR A O   1 
ATOM   1483 C CB  . THR A 1 296  ? 185.641 172.005 106.477 1.00 89.70  ? 296  THR A CB  1 
ATOM   1484 O OG1 . THR A 1 296  ? 186.766 172.882 106.615 1.00 91.71  ? 296  THR A OG1 1 
ATOM   1485 C CG2 . THR A 1 296  ? 185.288 171.870 105.002 1.00 87.21  ? 296  THR A CG2 1 
ATOM   1486 N N   . ASP A 1 297  ? 183.166 170.588 107.862 1.00 90.58  ? 297  ASP A N   1 
ATOM   1487 C CA  . ASP A 1 297  ? 182.024 169.685 107.767 1.00 89.66  ? 297  ASP A CA  1 
ATOM   1488 C C   . ASP A 1 297  ? 180.732 170.383 108.172 1.00 93.96  ? 297  ASP A C   1 
ATOM   1489 O O   . ASP A 1 297  ? 179.687 170.188 107.541 1.00 92.20  ? 297  ASP A O   1 
ATOM   1490 C CB  . ASP A 1 297  ? 182.263 168.449 108.635 1.00 90.33  ? 297  ASP A CB  1 
ATOM   1491 C CG  . ASP A 1 297  ? 181.213 167.374 108.424 1.00 96.13  ? 297  ASP A CG  1 
ATOM   1492 O OD1 . ASP A 1 297  ? 180.426 167.483 107.462 1.00 94.20  ? 297  ASP A OD1 1 
ATOM   1493 O OD2 . ASP A 1 297  ? 181.176 166.416 109.224 1.00 94.45  ? 297  ASP A OD2 1 
ATOM   1494 N N   . TYR A 1 298  ? 180.784 171.200 109.222 1.00 75.28  ? 298  TYR A N   1 
ATOM   1495 C CA  . TYR A 1 298  ? 179.593 171.857 109.742 1.00 64.61  ? 298  TYR A CA  1 
ATOM   1496 C C   . TYR A 1 298  ? 179.188 173.099 108.963 1.00 70.63  ? 298  TYR A C   1 
ATOM   1497 O O   . TYR A 1 298  ? 178.020 173.494 109.026 1.00 74.35  ? 298  TYR A O   1 
ATOM   1498 C CB  . TYR A 1 298  ? 179.803 172.255 111.203 1.00 62.41  ? 298  TYR A CB  1 
ATOM   1499 C CG  . TYR A 1 298  ? 180.040 171.100 112.141 1.00 59.65  ? 298  TYR A CG  1 
ATOM   1500 C CD1 . TYR A 1 298  ? 181.298 170.537 112.274 1.00 66.88  ? 298  TYR A CD1 1 
ATOM   1501 C CD2 . TYR A 1 298  ? 179.009 170.586 112.908 1.00 65.30  ? 298  TYR A CD2 1 
ATOM   1502 C CE1 . TYR A 1 298  ? 181.519 169.488 113.135 1.00 67.95  ? 298  TYR A CE1 1 
ATOM   1503 C CE2 . TYR A 1 298  ? 179.221 169.537 113.771 1.00 70.51  ? 298  TYR A CE2 1 
ATOM   1504 C CZ  . TYR A 1 298  ? 180.477 168.991 113.881 1.00 72.29  ? 298  TYR A CZ  1 
ATOM   1505 O OH  . TYR A 1 298  ? 180.691 167.942 114.743 1.00 76.94  ? 298  TYR A OH  1 
ATOM   1506 N N   . LYS A 1 299  ? 180.114 173.724 108.232 1.00 77.29  ? 299  LYS A N   1 
ATOM   1507 C CA  . LYS A 1 299  ? 179.849 175.049 107.684 1.00 79.65  ? 299  LYS A CA  1 
ATOM   1508 C C   . LYS A 1 299  ? 178.765 175.051 106.614 1.00 80.23  ? 299  LYS A C   1 
ATOM   1509 O O   . LYS A 1 299  ? 178.257 176.123 106.273 1.00 85.21  ? 299  LYS A O   1 
ATOM   1510 C CB  . LYS A 1 299  ? 181.132 175.653 107.114 1.00 80.50  ? 299  LYS A CB  1 
ATOM   1511 C CG  . LYS A 1 299  ? 181.570 175.063 105.790 1.00 80.16  ? 299  LYS A CG  1 
ATOM   1512 C CD  . LYS A 1 299  ? 182.781 175.801 105.248 1.00 82.44  ? 299  LYS A CD  1 
ATOM   1513 C CE  . LYS A 1 299  ? 183.176 175.288 103.877 1.00 82.23  ? 299  LYS A CE  1 
ATOM   1514 N NZ  . LYS A 1 299  ? 184.373 175.998 103.349 1.00 80.82  ? 299  LYS A NZ  1 
ATOM   1515 N N   . ASP A 1 300  ? 178.398 173.890 106.073 1.00 77.74  ? 300  ASP A N   1 
ATOM   1516 C CA  . ASP A 1 300  ? 177.397 173.812 105.017 1.00 80.17  ? 300  ASP A CA  1 
ATOM   1517 C C   . ASP A 1 300  ? 176.109 173.137 105.476 1.00 83.47  ? 300  ASP A C   1 
ATOM   1518 O O   . ASP A 1 300  ? 175.475 172.419 104.697 1.00 85.90  ? 300  ASP A O   1 
ATOM   1519 C CB  . ASP A 1 300  ? 177.970 173.089 103.799 1.00 82.72  ? 300  ASP A CB  1 
ATOM   1520 C CG  . ASP A 1 300  ? 178.989 173.925 103.056 1.00 85.65  ? 300  ASP A CG  1 
ATOM   1521 O OD1 . ASP A 1 300  ? 178.858 175.166 103.066 1.00 86.42  ? 300  ASP A OD1 1 
ATOM   1522 O OD2 . ASP A 1 300  ? 179.918 173.341 102.461 1.00 88.25  ? 300  ASP A OD2 1 
ATOM   1523 N N   . ASP A 1 301  ? 175.706 173.353 106.724 1.00 73.27  ? 301  ASP A N   1 
ATOM   1524 C CA  . ASP A 1 301  ? 174.468 172.789 107.241 1.00 65.56  ? 301  ASP A CA  1 
ATOM   1525 C C   . ASP A 1 301  ? 173.317 173.757 107.011 1.00 65.64  ? 301  ASP A C   1 
ATOM   1526 O O   . ASP A 1 301  ? 173.440 174.954 107.283 1.00 73.05  ? 301  ASP A O   1 
ATOM   1527 C CB  . ASP A 1 301  ? 174.597 172.473 108.730 1.00 61.14  ? 301  ASP A CB  1 
ATOM   1528 C CG  . ASP A 1 301  ? 175.554 171.338 108.999 1.00 65.92  ? 301  ASP A CG  1 
ATOM   1529 O OD1 . ASP A 1 301  ? 176.255 170.915 108.056 1.00 67.82  ? 301  ASP A OD1 1 
ATOM   1530 O OD2 . ASP A 1 301  ? 175.602 170.862 110.151 1.00 70.50  ? 301  ASP A OD2 1 
ATOM   1531 N N   . VAL A 1 302  ? 172.201 173.235 106.511 1.00 59.06  ? 302  VAL A N   1 
ATOM   1532 C CA  . VAL A 1 302  ? 170.983 174.010 106.313 1.00 62.10  ? 302  VAL A CA  1 
ATOM   1533 C C   . VAL A 1 302  ? 169.894 173.384 107.169 1.00 61.58  ? 302  VAL A C   1 
ATOM   1534 O O   . VAL A 1 302  ? 169.592 172.193 107.024 1.00 70.16  ? 302  VAL A O   1 
ATOM   1535 C CB  . VAL A 1 302  ? 170.562 174.051 104.838 1.00 59.56  ? 302  VAL A CB  1 
ATOM   1536 C CG1 . VAL A 1 302  ? 169.340 174.934 104.665 1.00 55.51  ? 302  VAL A CG1 1 
ATOM   1537 C CG2 . VAL A 1 302  ? 171.710 174.541 103.977 1.00 60.30  ? 302  VAL A CG2 1 
ATOM   1538 N N   . PHE A 1 303  ? 169.302 174.181 108.051 1.00 42.84  ? 303  PHE A N   1 
ATOM   1539 C CA  . PHE A 1 303  ? 168.284 173.712 108.978 1.00 35.19  ? 303  PHE A CA  1 
ATOM   1540 C C   . PHE A 1 303  ? 166.913 174.203 108.544 1.00 43.97  ? 303  PHE A C   1 
ATOM   1541 O O   . PHE A 1 303  ? 166.766 175.338 108.082 1.00 59.15  ? 303  PHE A O   1 
ATOM   1542 C CB  . PHE A 1 303  ? 168.565 174.194 110.401 1.00 41.20  ? 303  PHE A CB  1 
ATOM   1543 C CG  . PHE A 1 303  ? 169.541 173.342 111.151 1.00 35.33  ? 303  PHE A CG  1 
ATOM   1544 C CD1 . PHE A 1 303  ? 169.133 172.164 111.741 1.00 37.95  ? 303  PHE A CD1 1 
ATOM   1545 C CD2 . PHE A 1 303  ? 170.859 173.726 111.279 1.00 43.73  ? 303  PHE A CD2 1 
ATOM   1546 C CE1 . PHE A 1 303  ? 170.023 171.381 112.435 1.00 38.37  ? 303  PHE A CE1 1 
ATOM   1547 C CE2 . PHE A 1 303  ? 171.752 172.947 111.974 1.00 43.46  ? 303  PHE A CE2 1 
ATOM   1548 C CZ  . PHE A 1 303  ? 171.332 171.773 112.551 1.00 42.11  ? 303  PHE A CZ  1 
ATOM   1549 N N   . TYR A 1 304  ? 165.911 173.341 108.689 1.00 44.01  ? 304  TYR A N   1 
ATOM   1550 C CA  . TYR A 1 304  ? 164.533 173.757 108.511 1.00 44.75  ? 304  TYR A CA  1 
ATOM   1551 C C   . TYR A 1 304  ? 163.717 173.317 109.719 1.00 52.55  ? 304  TYR A C   1 
ATOM   1552 O O   . TYR A 1 304  ? 163.862 172.179 110.180 1.00 57.39  ? 304  TYR A O   1 
ATOM   1553 C CB  . TYR A 1 304  ? 163.923 173.178 107.232 1.00 43.35  ? 304  TYR A CB  1 
ATOM   1554 C CG  . TYR A 1 304  ? 162.595 173.801 106.893 1.00 52.24  ? 304  TYR A CG  1 
ATOM   1555 C CD1 . TYR A 1 304  ? 162.525 174.933 106.098 1.00 58.83  ? 304  TYR A CD1 1 
ATOM   1556 C CD2 . TYR A 1 304  ? 161.414 173.273 107.385 1.00 58.73  ? 304  TYR A CD2 1 
ATOM   1557 C CE1 . TYR A 1 304  ? 161.316 175.514 105.793 1.00 57.57  ? 304  TYR A CE1 1 
ATOM   1558 C CE2 . TYR A 1 304  ? 160.201 173.848 107.089 1.00 59.21  ? 304  TYR A CE2 1 
ATOM   1559 C CZ  . TYR A 1 304  ? 160.157 174.968 106.291 1.00 59.22  ? 304  TYR A CZ  1 
ATOM   1560 O OH  . TYR A 1 304  ? 158.947 175.543 105.989 1.00 64.81  ? 304  TYR A OH  1 
ATOM   1561 N N   . PRO A 1 305  ? 162.851 174.187 110.258 1.00 60.20  ? 305  PRO A N   1 
ATOM   1562 C CA  . PRO A 1 305  ? 162.524 175.550 109.812 1.00 62.69  ? 305  PRO A CA  1 
ATOM   1563 C C   . PRO A 1 305  ? 163.711 176.496 109.921 1.00 68.70  ? 305  PRO A C   1 
ATOM   1564 O O   . PRO A 1 305  ? 164.599 176.295 110.741 1.00 69.42  ? 305  PRO A O   1 
ATOM   1565 C CB  . PRO A 1 305  ? 161.376 175.952 110.748 1.00 63.38  ? 305  PRO A CB  1 
ATOM   1566 C CG  . PRO A 1 305  ? 161.604 175.144 111.984 1.00 62.42  ? 305  PRO A CG  1 
ATOM   1567 C CD  . PRO A 1 305  ? 162.120 173.829 111.484 1.00 57.62  ? 305  PRO A CD  1 
ATOM   1568 N N   . TYR A 1 306  ? 163.744 177.532 109.083 1.00 69.06  ? 306  TYR A N   1 
ATOM   1569 C CA  . TYR A 1 306  ? 164.944 178.347 108.945 1.00 60.79  ? 306  TYR A CA  1 
ATOM   1570 C C   . TYR A 1 306  ? 165.320 179.067 110.230 1.00 66.26  ? 306  TYR A C   1 
ATOM   1571 O O   . TYR A 1 306  ? 166.489 179.426 110.402 1.00 74.45  ? 306  TYR A O   1 
ATOM   1572 C CB  . TYR A 1 306  ? 164.753 179.350 107.812 1.00 61.93  ? 306  TYR A CB  1 
ATOM   1573 C CG  . TYR A 1 306  ? 164.756 178.712 106.445 1.00 63.92  ? 306  TYR A CG  1 
ATOM   1574 C CD1 . TYR A 1 306  ? 165.599 177.650 106.159 1.00 66.07  ? 306  TYR A CD1 1 
ATOM   1575 C CD2 . TYR A 1 306  ? 163.916 179.169 105.443 1.00 66.46  ? 306  TYR A CD2 1 
ATOM   1576 C CE1 . TYR A 1 306  ? 165.608 177.064 104.912 1.00 68.54  ? 306  TYR A CE1 1 
ATOM   1577 C CE2 . TYR A 1 306  ? 163.918 178.588 104.193 1.00 70.41  ? 306  TYR A CE2 1 
ATOM   1578 C CZ  . TYR A 1 306  ? 164.766 177.535 103.933 1.00 67.64  ? 306  TYR A CZ  1 
ATOM   1579 O OH  . TYR A 1 306  ? 164.771 176.952 102.689 1.00 69.98  ? 306  TYR A OH  1 
ATOM   1580 N N   . GLN A 1 307  ? 164.372 179.278 111.137 1.00 63.98  ? 307  GLN A N   1 
ATOM   1581 C CA  . GLN A 1 307  ? 164.684 179.932 112.399 1.00 63.62  ? 307  GLN A CA  1 
ATOM   1582 C C   . GLN A 1 307  ? 165.215 178.967 113.449 1.00 67.83  ? 307  GLN A C   1 
ATOM   1583 O O   . GLN A 1 307  ? 165.521 179.401 114.564 1.00 71.11  ? 307  GLN A O   1 
ATOM   1584 C CB  . GLN A 1 307  ? 163.450 180.655 112.944 1.00 62.35  ? 307  GLN A CB  1 
ATOM   1585 C CG  . GLN A 1 307  ? 162.311 179.742 113.356 1.00 66.75  ? 307  GLN A CG  1 
ATOM   1586 C CD  . GLN A 1 307  ? 161.467 179.290 112.183 1.00 74.60  ? 307  GLN A CD  1 
ATOM   1587 O OE1 . GLN A 1 307  ? 161.803 179.543 111.026 1.00 74.68  ? 307  GLN A OE1 1 
ATOM   1588 N NE2 . GLN A 1 307  ? 160.359 178.622 112.476 1.00 74.82  ? 307  GLN A NE2 1 
ATOM   1589 N N   . TYR A 1 308  ? 165.336 177.683 113.128 1.00 59.16  ? 308  TYR A N   1 
ATOM   1590 C CA  . TYR A 1 308  ? 165.827 176.699 114.082 1.00 55.07  ? 308  TYR A CA  1 
ATOM   1591 C C   . TYR A 1 308  ? 167.347 176.677 114.082 1.00 51.38  ? 308  TYR A C   1 
ATOM   1592 O O   . TYR A 1 308  ? 167.976 176.587 113.025 1.00 55.17  ? 308  TYR A O   1 
ATOM   1593 C CB  . TYR A 1 308  ? 165.296 175.302 113.765 1.00 51.75  ? 308  TYR A CB  1 
ATOM   1594 C CG  . TYR A 1 308  ? 165.863 174.239 114.679 1.00 45.52  ? 308  TYR A CG  1 
ATOM   1595 C CD1 . TYR A 1 308  ? 165.319 174.017 115.934 1.00 53.45  ? 308  TYR A CD1 1 
ATOM   1596 C CD2 . TYR A 1 308  ? 166.948 173.468 114.293 1.00 46.90  ? 308  TYR A CD2 1 
ATOM   1597 C CE1 . TYR A 1 308  ? 165.836 173.056 116.775 1.00 51.30  ? 308  TYR A CE1 1 
ATOM   1598 C CE2 . TYR A 1 308  ? 167.472 172.505 115.129 1.00 46.77  ? 308  TYR A CE2 1 
ATOM   1599 C CZ  . TYR A 1 308  ? 166.912 172.302 116.368 1.00 48.06  ? 308  TYR A CZ  1 
ATOM   1600 O OH  . TYR A 1 308  ? 167.427 171.342 117.206 1.00 55.25  ? 308  TYR A OH  1 
ATOM   1601 N N   . ILE A 1 309  ? 167.926 176.755 115.273 1.00 50.21  ? 309  ILE A N   1 
ATOM   1602 C CA  . ILE A 1 309  ? 169.355 176.543 115.474 1.00 54.83  ? 309  ILE A CA  1 
ATOM   1603 C C   . ILE A 1 309  ? 169.485 175.740 116.763 1.00 64.63  ? 309  ILE A C   1 
ATOM   1604 O O   . ILE A 1 309  ? 168.769 176.027 117.734 1.00 63.34  ? 309  ILE A O   1 
ATOM   1605 C CB  . ILE A 1 309  ? 170.117 177.878 115.518 1.00 60.73  ? 309  ILE A CB  1 
ATOM   1606 C CG1 . ILE A 1 309  ? 171.610 177.651 115.741 1.00 60.31  ? 309  ILE A CG1 1 
ATOM   1607 C CG2 . ILE A 1 309  ? 169.543 178.799 116.582 1.00 63.83  ? 309  ILE A CG2 1 
ATOM   1608 C CD1 . ILE A 1 309  ? 172.425 178.903 115.599 1.00 65.79  ? 309  ILE A CD1 1 
ATOM   1609 N N   . PRO A 1 310  ? 170.331 174.714 116.812 1.00 60.48  ? 310  PRO A N   1 
ATOM   1610 C CA  . PRO A 1 310  ? 170.370 173.833 117.984 1.00 53.45  ? 310  PRO A CA  1 
ATOM   1611 C C   . PRO A 1 310  ? 170.593 174.619 119.261 1.00 55.31  ? 310  PRO A C   1 
ATOM   1612 O O   . PRO A 1 310  ? 171.529 175.427 119.350 1.00 64.77  ? 310  PRO A O   1 
ATOM   1613 C CB  . PRO A 1 310  ? 171.555 172.908 117.684 1.00 50.13  ? 310  PRO A CB  1 
ATOM   1614 C CG  . PRO A 1 310  ? 171.603 172.855 116.210 1.00 49.42  ? 310  PRO A CG  1 
ATOM   1615 C CD  . PRO A 1 310  ? 171.197 174.218 115.729 1.00 51.15  ? 310  PRO A CD  1 
ATOM   1616 N N   . PRO A 1 311  ? 169.746 174.413 120.271 1.00 51.76  ? 311  PRO A N   1 
ATOM   1617 C CA  . PRO A 1 311  ? 169.897 175.170 121.523 1.00 53.36  ? 311  PRO A CA  1 
ATOM   1618 C C   . PRO A 1 311  ? 171.227 174.948 122.211 1.00 54.51  ? 311  PRO A C   1 
ATOM   1619 O O   . PRO A 1 311  ? 171.664 175.819 122.971 1.00 67.30  ? 311  PRO A O   1 
ATOM   1620 C CB  . PRO A 1 311  ? 168.732 174.660 122.379 1.00 61.02  ? 311  PRO A CB  1 
ATOM   1621 C CG  . PRO A 1 311  ? 167.726 174.192 121.391 1.00 61.49  ? 311  PRO A CG  1 
ATOM   1622 C CD  . PRO A 1 311  ? 168.513 173.613 120.256 1.00 57.14  ? 311  PRO A CD  1 
ATOM   1623 N N   . MET A 1 312  ? 171.882 173.812 121.977 1.00 51.13  ? 312  MET A N   1 
ATOM   1624 C CA  . MET A 1 312  ? 173.209 173.593 122.534 1.00 54.44  ? 312  MET A CA  1 
ATOM   1625 C C   . MET A 1 312  ? 174.226 174.596 122.012 1.00 57.91  ? 312  MET A C   1 
ATOM   1626 O O   . MET A 1 312  ? 175.190 174.905 122.718 1.00 58.05  ? 312  MET A O   1 
ATOM   1627 C CB  . MET A 1 312  ? 173.676 172.175 122.221 1.00 52.27  ? 312  MET A CB  1 
ATOM   1628 C CG  . MET A 1 312  ? 173.467 171.783 120.776 1.00 53.39  ? 312  MET A CG  1 
ATOM   1629 S SD  . MET A 1 312  ? 174.671 170.572 120.224 1.00 68.27  ? 312  MET A SD  1 
ATOM   1630 C CE  . MET A 1 312  ? 176.178 171.505 120.451 1.00 56.03  ? 312  MET A CE  1 
ATOM   1631 N N   . LEU A 1 313  ? 174.038 175.108 120.796 1.00 62.20  ? 313  LEU A N   1 
ATOM   1632 C CA  . LEU A 1 313  ? 174.956 176.089 120.235 1.00 59.88  ? 313  LEU A CA  1 
ATOM   1633 C C   . LEU A 1 313  ? 174.700 177.503 120.733 1.00 62.50  ? 313  LEU A C   1 
ATOM   1634 O O   . LEU A 1 313  ? 175.569 178.363 120.565 1.00 66.51  ? 313  LEU A O   1 
ATOM   1635 C CB  . LEU A 1 313  ? 174.878 176.077 118.710 1.00 56.90  ? 313  LEU A CB  1 
ATOM   1636 C CG  . LEU A 1 313  ? 175.479 174.856 118.023 1.00 57.57  ? 313  LEU A CG  1 
ATOM   1637 C CD1 . LEU A 1 313  ? 175.463 175.042 116.520 1.00 61.39  ? 313  LEU A CD1 1 
ATOM   1638 C CD2 . LEU A 1 313  ? 176.891 174.628 118.521 1.00 64.70  ? 313  LEU A CD2 1 
ATOM   1639 N N   . ILE A 1 314  ? 173.544 177.767 121.336 1.00 66.71  ? 314  ILE A N   1 
ATOM   1640 C CA  . ILE A 1 314  ? 173.214 179.109 121.813 1.00 67.05  ? 314  ILE A CA  1 
ATOM   1641 C C   . ILE A 1 314  ? 173.821 179.234 123.207 1.00 74.18  ? 314  ILE A C   1 
ATOM   1642 O O   . ILE A 1 314  ? 173.190 178.934 124.220 1.00 75.88  ? 314  ILE A O   1 
ATOM   1643 C CB  . ILE A 1 314  ? 171.713 179.371 121.799 1.00 62.44  ? 314  ILE A CB  1 
ATOM   1644 C CG1 . ILE A 1 314  ? 171.182 179.282 120.371 1.00 64.27  ? 314  ILE A CG1 1 
ATOM   1645 C CG2 . ILE A 1 314  ? 171.405 180.739 122.379 1.00 68.84  ? 314  ILE A CG2 1 
ATOM   1646 C CD1 . ILE A 1 314  ? 169.769 179.781 120.216 1.00 71.80  ? 314  ILE A CD1 1 
ATOM   1647 N N   . LYS A 1 315  ? 175.079 179.669 123.251 1.00 79.85  ? 315  LYS A N   1 
ATOM   1648 C CA  . LYS A 1 315  ? 175.785 179.959 124.498 1.00 79.15  ? 315  LYS A CA  1 
ATOM   1649 C C   . LYS A 1 315  ? 176.299 181.388 124.379 1.00 81.59  ? 315  LYS A C   1 
ATOM   1650 O O   . LYS A 1 315  ? 177.448 181.614 123.993 1.00 84.13  ? 315  LYS A O   1 
ATOM   1651 C CB  . LYS A 1 315  ? 176.917 178.967 124.743 1.00 79.06  ? 315  LYS A CB  1 
ATOM   1652 C CG  . LYS A 1 315  ? 176.479 177.515 124.809 1.00 77.92  ? 315  LYS A CG  1 
ATOM   1653 C CD  . LYS A 1 315  ? 175.540 177.270 125.976 1.00 77.11  ? 315  LYS A CD  1 
ATOM   1654 C CE  . LYS A 1 315  ? 175.152 175.805 126.068 1.00 77.99  ? 315  LYS A CE  1 
ATOM   1655 N NZ  . LYS A 1 315  ? 174.218 175.547 127.197 1.00 80.86  ? 315  LYS A NZ  1 
ATOM   1656 N N   . ALA A 1 316  ? 175.446 182.349 124.710 1.00 92.12  ? 316  ALA A N   1 
ATOM   1657 C CA  . ALA A 1 316  ? 175.800 183.758 124.668 1.00 92.90  ? 316  ALA A CA  1 
ATOM   1658 C C   . ALA A 1 316  ? 176.058 184.271 126.079 1.00 93.84  ? 316  ALA A C   1 
ATOM   1659 O O   . ALA A 1 316  ? 175.766 183.604 127.073 1.00 93.64  ? 316  ALA A O   1 
ATOM   1660 C CB  . ALA A 1 316  ? 174.694 184.571 123.991 1.00 88.50  ? 316  ALA A CB  1 
ATOM   1661 N N   . ASP A 1 317  ? 176.617 185.474 126.159 1.00 97.79  ? 317  ASP A N   1 
ATOM   1662 C CA  . ASP A 1 317  ? 176.888 186.084 127.456 1.00 97.08  ? 317  ASP A CA  1 
ATOM   1663 C C   . ASP A 1 317  ? 175.554 186.385 128.122 1.00 96.13  ? 317  ASP A C   1 
ATOM   1664 O O   . ASP A 1 317  ? 174.861 187.338 127.761 1.00 94.19  ? 317  ASP A O   1 
ATOM   1665 C CB  . ASP A 1 317  ? 177.732 187.344 127.303 1.00 98.57  ? 317  ASP A CB  1 
ATOM   1666 C CG  . ASP A 1 317  ? 178.337 187.799 128.618 1.00 100.23 ? 317  ASP A CG  1 
ATOM   1667 O OD1 . ASP A 1 317  ? 178.091 187.137 129.648 1.00 96.77  ? 317  ASP A OD1 1 
ATOM   1668 O OD2 . ASP A 1 317  ? 179.064 188.813 128.623 1.00 100.50 ? 317  ASP A OD2 1 
ATOM   1669 N N   . ARG A 1 318  ? 175.194 185.559 129.102 1.00 95.77  ? 318  ARG A N   1 
ATOM   1670 C CA  . ARG A 1 318  ? 173.893 185.663 129.747 1.00 96.47  ? 318  ARG A CA  1 
ATOM   1671 C C   . ARG A 1 318  ? 173.755 186.931 130.577 1.00 96.66  ? 318  ARG A C   1 
ATOM   1672 O O   . ARG A 1 318  ? 172.629 187.358 130.852 1.00 92.82  ? 318  ARG A O   1 
ATOM   1673 C CB  . ARG A 1 318  ? 173.667 184.430 130.619 1.00 95.43  ? 318  ARG A CB  1 
ATOM   1674 C CG  . ARG A 1 318  ? 172.243 184.217 131.067 1.00 94.00  ? 318  ARG A CG  1 
ATOM   1675 C CD  . ARG A 1 318  ? 172.079 182.823 131.631 1.00 93.51  ? 318  ARG A CD  1 
ATOM   1676 N NE  . ARG A 1 318  ? 172.941 182.591 132.782 1.00 95.67  ? 318  ARG A NE  1 
ATOM   1677 C CZ  . ARG A 1 318  ? 173.006 181.446 133.445 1.00 96.60  ? 318  ARG A CZ  1 
ATOM   1678 N NH1 . ARG A 1 318  ? 172.272 180.402 133.096 1.00 92.28  ? 318  ARG A NH1 1 
ATOM   1679 N NH2 . ARG A 1 318  ? 173.828 181.344 134.485 1.00 97.93  ? 318  ARG A NH2 1 
ATOM   1680 N N   . CYS A 1 319  ? 174.868 187.546 130.970 1.00 103.43 ? 319  CYS A N   1 
ATOM   1681 C CA  . CYS A 1 319  ? 174.829 188.712 131.841 1.00 97.53  ? 319  CYS A CA  1 
ATOM   1682 C C   . CYS A 1 319  ? 174.757 190.028 131.080 1.00 100.28 ? 319  CYS A C   1 
ATOM   1683 O O   . CYS A 1 319  ? 174.676 191.083 131.714 1.00 105.78 ? 319  CYS A O   1 
ATOM   1684 C CB  . CYS A 1 319  ? 176.053 188.711 132.756 1.00 99.79  ? 319  CYS A CB  1 
ATOM   1685 S SG  . CYS A 1 319  ? 176.360 187.120 133.555 1.00 107.16 ? 319  CYS A SG  1 
ATOM   1686 N N   . LYS A 1 320  ? 174.788 189.998 129.752 1.00 95.80  ? 320  LYS A N   1 
ATOM   1687 C CA  . LYS A 1 320  ? 174.679 191.202 128.941 1.00 94.62  ? 320  LYS A CA  1 
ATOM   1688 C C   . LYS A 1 320  ? 173.237 191.376 128.489 1.00 96.47  ? 320  LYS A C   1 
ATOM   1689 O O   . LYS A 1 320  ? 172.634 190.445 127.947 1.00 100.45 ? 320  LYS A O   1 
ATOM   1690 C CB  . LYS A 1 320  ? 175.610 191.136 127.731 1.00 95.73  ? 320  LYS A CB  1 
ATOM   1691 C CG  . LYS A 1 320  ? 177.079 191.288 128.075 1.00 96.06  ? 320  LYS A CG  1 
ATOM   1692 C CD  . LYS A 1 320  ? 177.933 191.313 126.821 1.00 97.85  ? 320  LYS A CD  1 
ATOM   1693 C CE  . LYS A 1 320  ? 179.381 191.627 127.146 1.00 95.37  ? 320  LYS A CE  1 
ATOM   1694 N NZ  . LYS A 1 320  ? 180.229 191.648 125.924 1.00 96.02  ? 320  LYS A NZ  1 
ATOM   1695 N N   . LEU A 1 321  ? 172.689 192.571 128.711 1.00 96.83  ? 321  LEU A N   1 
ATOM   1696 C CA  . LEU A 1 321  ? 171.279 192.800 128.418 1.00 97.37  ? 321  LEU A CA  1 
ATOM   1697 C C   . LEU A 1 321  ? 171.001 192.780 126.921 1.00 97.66  ? 321  LEU A C   1 
ATOM   1698 O O   . LEU A 1 321  ? 169.879 192.466 126.507 1.00 100.19 ? 321  LEU A O   1 
ATOM   1699 C CB  . LEU A 1 321  ? 170.828 194.127 129.024 1.00 97.72  ? 321  LEU A CB  1 
ATOM   1700 C CG  . LEU A 1 321  ? 169.342 194.230 129.361 1.00 97.43  ? 321  LEU A CG  1 
ATOM   1701 C CD1 . LEU A 1 321  ? 168.978 193.207 130.419 1.00 96.21  ? 321  LEU A CD1 1 
ATOM   1702 C CD2 . LEU A 1 321  ? 168.996 195.631 129.827 1.00 99.19  ? 321  LEU A CD2 1 
ATOM   1703 N N   . GLN A 1 322  ? 171.996 193.112 126.097 1.00 98.00  ? 322  GLN A N   1 
ATOM   1704 C CA  . GLN A 1 322  ? 171.788 193.105 124.654 1.00 97.96  ? 322  GLN A CA  1 
ATOM   1705 C C   . GLN A 1 322  ? 171.535 191.698 124.133 1.00 100.63 ? 322  GLN A C   1 
ATOM   1706 O O   . GLN A 1 322  ? 170.840 191.523 123.127 1.00 101.19 ? 322  GLN A O   1 
ATOM   1707 C CB  . GLN A 1 322  ? 172.991 193.720 123.940 1.00 97.66  ? 322  GLN A CB  1 
ATOM   1708 C CG  . GLN A 1 322  ? 173.709 194.791 124.737 1.00 100.69 ? 322  GLN A CG  1 
ATOM   1709 C CD  . GLN A 1 322  ? 174.825 194.226 125.590 1.00 100.91 ? 322  GLN A CD  1 
ATOM   1710 O OE1 . GLN A 1 322  ? 175.434 193.216 125.242 1.00 102.28 ? 322  GLN A OE1 1 
ATOM   1711 N NE2 . GLN A 1 322  ? 175.098 194.873 126.717 1.00 99.95  ? 322  GLN A NE2 1 
ATOM   1712 N N   . ASN A 1 323  ? 172.096 190.686 124.796 1.00 94.12  ? 323  ASN A N   1 
ATOM   1713 C CA  . ASN A 1 323  ? 171.908 189.314 124.343 1.00 92.98  ? 323  ASN A CA  1 
ATOM   1714 C C   . ASN A 1 323  ? 170.498 188.811 124.620 1.00 95.33  ? 323  ASN A C   1 
ATOM   1715 O O   . ASN A 1 323  ? 170.020 187.908 123.925 1.00 96.73  ? 323  ASN A O   1 
ATOM   1716 C CB  . ASN A 1 323  ? 172.936 188.400 125.008 1.00 93.70  ? 323  ASN A CB  1 
ATOM   1717 C CG  . ASN A 1 323  ? 174.358 188.779 124.660 1.00 94.66  ? 323  ASN A CG  1 
ATOM   1718 O OD1 . ASN A 1 323  ? 174.607 189.845 124.100 1.00 95.74  ? 323  ASN A OD1 1 
ATOM   1719 N ND2 . ASN A 1 323  ? 175.301 187.908 124.994 1.00 95.44  ? 323  ASN A ND2 1 
ATOM   1720 N N   . VAL A 1 324  ? 169.821 189.368 125.620 1.00 88.35  ? 324  VAL A N   1 
ATOM   1721 C CA  . VAL A 1 324  ? 168.510 188.895 126.031 1.00 85.42  ? 324  VAL A CA  1 
ATOM   1722 C C   . VAL A 1 324  ? 167.402 189.858 125.623 1.00 87.27  ? 324  VAL A C   1 
ATOM   1723 O O   . VAL A 1 324  ? 166.371 189.431 125.100 1.00 86.38  ? 324  VAL A O   1 
ATOM   1724 C CB  . VAL A 1 324  ? 168.474 188.622 127.550 1.00 82.81  ? 324  VAL A CB  1 
ATOM   1725 C CG1 . VAL A 1 324  ? 169.208 187.335 127.864 1.00 87.06  ? 324  VAL A CG1 1 
ATOM   1726 C CG2 . VAL A 1 324  ? 169.091 189.775 128.316 1.00 84.87  ? 324  VAL A CG2 1 
ATOM   1727 N N   . PHE A 1 325  ? 167.589 191.156 125.847 1.00 96.10  ? 325  PHE A N   1 
ATOM   1728 C CA  . PHE A 1 325  ? 166.567 192.159 125.560 1.00 91.08  ? 325  PHE A CA  1 
ATOM   1729 C C   . PHE A 1 325  ? 167.104 193.103 124.489 1.00 93.26  ? 325  PHE A C   1 
ATOM   1730 O O   . PHE A 1 325  ? 167.648 194.167 124.796 1.00 94.04  ? 325  PHE A O   1 
ATOM   1731 C CB  . PHE A 1 325  ? 166.175 192.913 126.827 1.00 90.80  ? 325  PHE A CB  1 
ATOM   1732 C CG  . PHE A 1 325  ? 165.582 192.040 127.893 1.00 92.71  ? 325  PHE A CG  1 
ATOM   1733 C CD1 . PHE A 1 325  ? 164.864 190.907 127.559 1.00 94.73  ? 325  PHE A CD1 1 
ATOM   1734 C CD2 . PHE A 1 325  ? 165.744 192.353 129.230 1.00 91.39  ? 325  PHE A CD2 1 
ATOM   1735 C CE1 . PHE A 1 325  ? 164.319 190.103 128.539 1.00 91.47  ? 325  PHE A CE1 1 
ATOM   1736 C CE2 . PHE A 1 325  ? 165.201 191.552 130.213 1.00 91.64  ? 325  PHE A CE2 1 
ATOM   1737 C CZ  . PHE A 1 325  ? 164.488 190.428 129.867 1.00 89.63  ? 325  PHE A CZ  1 
ATOM   1738 N N   . GLY A 1 326  ? 166.950 192.707 123.226 1.00 104.55 ? 326  GLY A N   1 
ATOM   1739 C CA  . GLY A 1 326  ? 167.352 193.580 122.136 1.00 107.41 ? 326  GLY A CA  1 
ATOM   1740 C C   . GLY A 1 326  ? 166.467 194.805 122.008 1.00 109.08 ? 326  GLY A C   1 
ATOM   1741 O O   . GLY A 1 326  ? 166.950 195.902 121.716 1.00 108.60 ? 326  GLY A O   1 
ATOM   1742 N N   . ASP A 1 327  ? 165.160 194.634 122.223 1.00 114.61 ? 327  ASP A N   1 
ATOM   1743 C CA  . ASP A 1 327  ? 164.217 195.728 122.016 1.00 113.64 ? 327  ASP A CA  1 
ATOM   1744 C C   . ASP A 1 327  ? 164.469 196.877 122.984 1.00 113.28 ? 327  ASP A C   1 
ATOM   1745 O O   . ASP A 1 327  ? 164.347 198.049 122.612 1.00 114.87 ? 327  ASP A O   1 
ATOM   1746 C CB  . ASP A 1 327  ? 162.784 195.218 122.157 1.00 114.41 ? 327  ASP A CB  1 
ATOM   1747 C CG  . ASP A 1 327  ? 162.462 194.106 121.180 1.00 116.07 ? 327  ASP A CG  1 
ATOM   1748 O OD1 . ASP A 1 327  ? 163.352 193.730 120.389 1.00 115.52 ? 327  ASP A OD1 1 
ATOM   1749 O OD2 . ASP A 1 327  ? 161.318 193.607 121.204 1.00 115.85 ? 327  ASP A OD2 1 
ATOM   1750 N N   . LYS A 1 328  ? 164.815 196.561 124.234 1.00 104.72 ? 328  LYS A N   1 
ATOM   1751 C CA  . LYS A 1 328  ? 164.997 197.601 125.239 1.00 105.45 ? 328  LYS A CA  1 
ATOM   1752 C C   . LYS A 1 328  ? 166.182 198.508 124.930 1.00 105.96 ? 328  LYS A C   1 
ATOM   1753 O O   . LYS A 1 328  ? 166.276 199.598 125.505 1.00 105.31 ? 328  LYS A O   1 
ATOM   1754 C CB  . LYS A 1 328  ? 165.154 196.968 126.622 1.00 107.46 ? 328  LYS A CB  1 
ATOM   1755 C CG  . LYS A 1 328  ? 163.965 196.110 127.032 1.00 106.07 ? 328  LYS A CG  1 
ATOM   1756 C CD  . LYS A 1 328  ? 164.111 195.581 128.447 1.00 104.19 ? 328  LYS A CD  1 
ATOM   1757 C CE  . LYS A 1 328  ? 164.113 196.710 129.460 1.00 103.92 ? 328  LYS A CE  1 
ATOM   1758 N NZ  . LYS A 1 328  ? 164.221 196.195 130.851 1.00 105.11 ? 328  LYS A NZ  1 
ATOM   1759 N N   . ASN A 1 329  ? 167.083 198.085 124.045 1.00 114.42 ? 329  ASN A N   1 
ATOM   1760 C CA  . ASN A 1 329  ? 168.189 198.889 123.528 1.00 115.21 ? 329  ASN A CA  1 
ATOM   1761 C C   . ASN A 1 329  ? 169.155 199.354 124.609 1.00 115.27 ? 329  ASN A C   1 
ATOM   1762 O O   . ASN A 1 329  ? 169.844 200.364 124.418 1.00 111.88 ? 329  ASN A O   1 
ATOM   1763 C CB  . ASN A 1 329  ? 167.685 200.108 122.749 1.00 113.75 ? 329  ASN A CB  1 
ATOM   1764 C CG  . ASN A 1 329  ? 166.793 199.728 121.587 1.00 114.79 ? 329  ASN A CG  1 
ATOM   1765 O OD1 . ASN A 1 329  ? 166.971 198.677 120.971 1.00 114.01 ? 329  ASN A OD1 1 
ATOM   1766 N ND2 . ASN A 1 329  ? 165.825 200.583 121.280 1.00 113.92 ? 329  ASN A ND2 1 
ATOM   1767 N N   . LEU A 1 330  ? 169.224 198.660 125.740 1.00 118.42 ? 330  LEU A N   1 
ATOM   1768 C CA  . LEU A 1 330  ? 170.171 199.018 126.786 1.00 116.67 ? 330  LEU A CA  1 
ATOM   1769 C C   . LEU A 1 330  ? 171.381 198.096 126.736 1.00 115.70 ? 330  LEU A C   1 
ATOM   1770 O O   . LEU A 1 330  ? 171.238 196.871 126.668 1.00 117.59 ? 330  LEU A O   1 
ATOM   1771 C CB  . LEU A 1 330  ? 169.504 198.950 128.158 1.00 116.41 ? 330  LEU A CB  1 
ATOM   1772 C CG  . LEU A 1 330  ? 169.023 200.284 128.731 1.00 116.72 ? 330  LEU A CG  1 
ATOM   1773 C CD1 . LEU A 1 330  ? 168.136 201.018 127.740 1.00 114.99 ? 330  LEU A CD1 1 
ATOM   1774 C CD2 . LEU A 1 330  ? 168.292 200.069 130.044 1.00 116.08 ? 330  LEU A CD2 1 
ATOM   1775 N N   . ASN A 1 331  ? 172.572 198.685 126.775 1.00 111.27 ? 331  ASN A N   1 
ATOM   1776 C CA  . ASN A 1 331  ? 173.831 197.945 126.724 1.00 111.49 ? 331  ASN A CA  1 
ATOM   1777 C C   . ASN A 1 331  ? 174.417 197.947 128.133 1.00 110.87 ? 331  ASN A C   1 
ATOM   1778 O O   . ASN A 1 331  ? 175.191 198.833 128.499 1.00 115.33 ? 331  ASN A O   1 
ATOM   1779 C CB  . ASN A 1 331  ? 174.794 198.563 125.715 1.00 112.31 ? 331  ASN A CB  1 
ATOM   1780 C CG  . ASN A 1 331  ? 174.181 198.702 124.337 1.00 113.40 ? 331  ASN A CG  1 
ATOM   1781 O OD1 . ASN A 1 331  ? 173.280 197.951 123.967 1.00 114.55 ? 331  ASN A OD1 1 
ATOM   1782 N ND2 . ASN A 1 331  ? 174.669 199.668 123.568 1.00 112.34 ? 331  ASN A ND2 1 
ATOM   1783 N N   . ILE A 1 332  ? 174.046 196.943 128.922 1.00 105.17 ? 332  ILE A N   1 
ATOM   1784 C CA  . ILE A 1 332  ? 174.428 196.858 130.325 1.00 107.15 ? 332  ILE A CA  1 
ATOM   1785 C C   . ILE A 1 332  ? 175.090 195.511 130.571 1.00 107.62 ? 332  ILE A C   1 
ATOM   1786 O O   . ILE A 1 332  ? 174.576 194.474 130.140 1.00 110.69 ? 332  ILE A O   1 
ATOM   1787 C CB  . ILE A 1 332  ? 173.213 197.034 131.256 1.00 107.48 ? 332  ILE A CB  1 
ATOM   1788 C CG1 . ILE A 1 332  ? 172.490 198.345 130.948 1.00 108.24 ? 332  ILE A CG1 1 
ATOM   1789 C CG2 . ILE A 1 332  ? 173.646 196.988 132.710 1.00 108.35 ? 332  ILE A CG2 1 
ATOM   1790 C CD1 . ILE A 1 332  ? 173.349 199.572 131.134 1.00 107.25 ? 332  ILE A CD1 1 
ATOM   1791 N N   . ASP A 1 333  ? 176.229 195.529 131.255 1.00 104.41 ? 333  ASP A N   1 
ATOM   1792 C CA  . ASP A 1 333  ? 176.899 194.312 131.708 1.00 102.59 ? 333  ASP A CA  1 
ATOM   1793 C C   . ASP A 1 333  ? 176.580 194.150 133.189 1.00 100.67 ? 333  ASP A C   1 
ATOM   1794 O O   . ASP A 1 333  ? 177.116 194.871 134.033 1.00 104.89 ? 333  ASP A O   1 
ATOM   1795 C CB  . ASP A 1 333  ? 178.401 194.390 131.456 1.00 103.78 ? 333  ASP A CB  1 
ATOM   1796 C CG  . ASP A 1 333  ? 179.126 193.115 131.843 1.00 105.21 ? 333  ASP A CG  1 
ATOM   1797 O OD1 . ASP A 1 333  ? 178.458 192.135 132.232 1.00 106.84 ? 333  ASP A OD1 1 
ATOM   1798 O OD2 . ASP A 1 333  ? 180.371 193.093 131.755 1.00 104.50 ? 333  ASP A OD2 1 
ATOM   1799 N N   . LEU A 1 334  ? 175.703 193.196 133.503 1.00 100.83 ? 334  LEU A N   1 
ATOM   1800 C CA  . LEU A 1 334  ? 175.249 193.030 134.878 1.00 104.96 ? 334  LEU A CA  1 
ATOM   1801 C C   . LEU A 1 334  ? 176.372 192.608 135.814 1.00 106.56 ? 334  LEU A C   1 
ATOM   1802 O O   . LEU A 1 334  ? 176.290 192.876 137.017 1.00 110.45 ? 334  LEU A O   1 
ATOM   1803 C CB  . LEU A 1 334  ? 174.107 192.016 134.936 1.00 103.60 ? 334  LEU A CB  1 
ATOM   1804 C CG  . LEU A 1 334  ? 172.866 192.381 134.119 1.00 100.89 ? 334  LEU A CG  1 
ATOM   1805 C CD1 . LEU A 1 334  ? 171.761 191.365 134.339 1.00 102.51 ? 334  LEU A CD1 1 
ATOM   1806 C CD2 . LEU A 1 334  ? 172.387 193.780 134.461 1.00 100.76 ? 334  LEU A CD2 1 
ATOM   1807 N N   . ARG A 1 335  ? 177.414 191.953 135.299 1.00 109.59 ? 335  ARG A N   1 
ATOM   1808 C CA  . ARG A 1 335  ? 178.549 191.609 136.145 1.00 110.28 ? 335  ARG A CA  1 
ATOM   1809 C C   . ARG A 1 335  ? 179.448 192.807 136.418 1.00 112.52 ? 335  ARG A C   1 
ATOM   1810 O O   . ARG A 1 335  ? 180.311 192.730 137.299 1.00 113.25 ? 335  ARG A O   1 
ATOM   1811 C CB  . ARG A 1 335  ? 179.365 190.482 135.515 1.00 109.33 ? 335  ARG A CB  1 
ATOM   1812 C CG  . ARG A 1 335  ? 178.607 189.179 135.358 1.00 111.26 ? 335  ARG A CG  1 
ATOM   1813 C CD  . ARG A 1 335  ? 179.553 188.028 135.070 1.00 112.35 ? 335  ARG A CD  1 
ATOM   1814 N NE  . ARG A 1 335  ? 180.618 188.420 134.155 1.00 112.73 ? 335  ARG A NE  1 
ATOM   1815 C CZ  . ARG A 1 335  ? 180.537 188.350 132.834 1.00 112.36 ? 335  ARG A CZ  1 
ATOM   1816 N NH1 . ARG A 1 335  ? 179.451 187.896 132.231 1.00 112.96 ? 335  ARG A NH1 1 
ATOM   1817 N NH2 . ARG A 1 335  ? 181.572 188.746 132.100 1.00 111.06 ? 335  ARG A NH2 1 
ATOM   1818 N N   . GLU A 1 336  ? 179.276 193.902 135.684 1.00 112.22 ? 336  GLU A N   1 
ATOM   1819 C CA  . GLU A 1 336  ? 180.065 195.113 135.864 1.00 109.22 ? 336  GLU A CA  1 
ATOM   1820 C C   . GLU A 1 336  ? 179.167 196.312 136.139 1.00 109.73 ? 336  GLU A C   1 
ATOM   1821 O O   . GLU A 1 336  ? 179.510 197.453 135.825 1.00 110.40 ? 336  GLU A O   1 
ATOM   1822 C CB  . GLU A 1 336  ? 180.947 195.375 134.646 1.00 111.54 ? 336  GLU A CB  1 
ATOM   1823 C CG  . GLU A 1 336  ? 181.977 194.290 134.369 1.00 113.44 ? 336  GLU A CG  1 
ATOM   1824 C CD  . GLU A 1 336  ? 183.118 194.290 135.370 1.00 113.16 ? 336  GLU A CD  1 
ATOM   1825 O OE1 . GLU A 1 336  ? 183.233 195.259 136.150 1.00 115.11 ? 336  GLU A OE1 1 
ATOM   1826 O OE2 . GLU A 1 336  ? 183.905 193.320 135.374 1.00 109.41 ? 336  GLU A OE2 1 
ATOM   1827 N N   . ALA A 1 337  ? 178.004 196.066 136.734 1.00 112.19 ? 337  ALA A N   1 
ATOM   1828 C CA  . ALA A 1 337  ? 177.033 197.109 137.026 1.00 111.87 ? 337  ALA A CA  1 
ATOM   1829 C C   . ALA A 1 337  ? 176.739 197.139 138.517 1.00 113.76 ? 337  ALA A C   1 
ATOM   1830 O O   . ALA A 1 337  ? 176.736 196.097 139.180 1.00 113.28 ? 337  ALA A O   1 
ATOM   1831 C CB  . ALA A 1 337  ? 175.735 196.896 136.242 1.00 106.44 ? 337  ALA A CB  1 
ATOM   1832 N N   . SER A 1 338  ? 176.497 198.338 139.040 1.00 111.47 ? 338  SER A N   1 
ATOM   1833 C CA  . SER A 1 338  ? 176.197 198.491 140.453 1.00 109.56 ? 338  SER A CA  1 
ATOM   1834 C C   . SER A 1 338  ? 174.794 197.976 140.763 1.00 109.05 ? 338  SER A C   1 
ATOM   1835 O O   . SER A 1 338  ? 173.948 197.818 139.879 1.00 110.78 ? 338  SER A O   1 
ATOM   1836 C CB  . SER A 1 338  ? 176.323 199.953 140.875 1.00 109.29 ? 338  SER A CB  1 
ATOM   1837 O OG  . SER A 1 338  ? 176.091 200.099 142.265 1.00 110.99 ? 338  SER A OG  1 
ATOM   1838 N N   . ASP A 1 339  ? 174.556 197.710 142.049 1.00 101.88 ? 339  ASP A N   1 
ATOM   1839 C CA  . ASP A 1 339  ? 173.270 197.163 142.466 1.00 102.39 ? 339  ASP A CA  1 
ATOM   1840 C C   . ASP A 1 339  ? 172.132 198.130 142.166 1.00 102.66 ? 339  ASP A C   1 
ATOM   1841 O O   . ASP A 1 339  ? 171.075 197.721 141.673 1.00 104.36 ? 339  ASP A O   1 
ATOM   1842 C CB  . ASP A 1 339  ? 173.307 196.821 143.955 1.00 100.73 ? 339  ASP A CB  1 
ATOM   1843 C CG  . ASP A 1 339  ? 172.108 196.008 144.397 1.00 100.49 ? 339  ASP A CG  1 
ATOM   1844 O OD1 . ASP A 1 339  ? 171.344 195.546 143.525 1.00 101.60 ? 339  ASP A OD1 1 
ATOM   1845 O OD2 . ASP A 1 339  ? 171.929 195.830 145.620 1.00 103.48 ? 339  ASP A OD2 1 
ATOM   1846 N N   . GLY A 1 340  ? 172.330 199.417 142.453 1.00 94.59  ? 340  GLY A N   1 
ATOM   1847 C CA  . GLY A 1 340  ? 171.291 200.392 142.167 1.00 91.72  ? 340  GLY A CA  1 
ATOM   1848 C C   . GLY A 1 340  ? 171.030 200.546 140.682 1.00 94.44  ? 340  GLY A C   1 
ATOM   1849 O O   . GLY A 1 340  ? 169.880 200.682 140.254 1.00 97.39  ? 340  GLY A O   1 
ATOM   1850 N N   . LEU A 1 341  ? 172.093 200.526 139.876 1.00 94.76  ? 341  LEU A N   1 
ATOM   1851 C CA  . LEU A 1 341  ? 171.931 200.652 138.432 1.00 97.33  ? 341  LEU A CA  1 
ATOM   1852 C C   . LEU A 1 341  ? 171.113 199.498 137.869 1.00 99.05  ? 341  LEU A C   1 
ATOM   1853 O O   . LEU A 1 341  ? 170.254 199.700 137.004 1.00 98.25  ? 341  LEU A O   1 
ATOM   1854 C CB  . LEU A 1 341  ? 173.301 200.724 137.758 1.00 99.75  ? 341  LEU A CB  1 
ATOM   1855 C CG  . LEU A 1 341  ? 173.318 200.943 136.245 1.00 99.46  ? 341  LEU A CG  1 
ATOM   1856 C CD1 . LEU A 1 341  ? 172.683 202.275 135.892 1.00 98.96  ? 341  LEU A CD1 1 
ATOM   1857 C CD2 . LEU A 1 341  ? 174.738 200.867 135.712 1.00 98.06  ? 341  LEU A CD2 1 
ATOM   1858 N N   . LYS A 1 342  ? 171.369 198.278 138.346 1.00 94.03  ? 342  LYS A N   1 
ATOM   1859 C CA  . LYS A 1 342  ? 170.563 197.139 137.923 1.00 91.81  ? 342  LYS A CA  1 
ATOM   1860 C C   . LYS A 1 342  ? 169.138 197.245 138.453 1.00 92.23  ? 342  LYS A C   1 
ATOM   1861 O O   . LYS A 1 342  ? 168.185 196.864 137.764 1.00 94.28  ? 342  LYS A O   1 
ATOM   1862 C CB  . LYS A 1 342  ? 171.213 195.834 138.382 1.00 90.63  ? 342  LYS A CB  1 
ATOM   1863 C CG  . LYS A 1 342  ? 172.583 195.581 137.775 1.00 92.83  ? 342  LYS A CG  1 
ATOM   1864 C CD  . LYS A 1 342  ? 173.113 194.201 138.133 1.00 91.90  ? 342  LYS A CD  1 
ATOM   1865 C CE  . LYS A 1 342  ? 173.342 194.062 139.627 1.00 89.87  ? 342  LYS A CE  1 
ATOM   1866 N NZ  . LYS A 1 342  ? 173.854 192.710 139.980 1.00 92.16  ? 342  LYS A NZ  1 
ATOM   1867 N N   . LYS A 1 343  ? 168.973 197.758 139.674 1.00 92.54  ? 343  LYS A N   1 
ATOM   1868 C CA  . LYS A 1 343  ? 167.639 197.874 140.253 1.00 89.81  ? 343  LYS A CA  1 
ATOM   1869 C C   . LYS A 1 343  ? 166.792 198.901 139.513 1.00 89.92  ? 343  LYS A C   1 
ATOM   1870 O O   . LYS A 1 343  ? 165.559 198.808 139.518 1.00 88.78  ? 343  LYS A O   1 
ATOM   1871 C CB  . LYS A 1 343  ? 167.743 198.229 141.736 1.00 90.28  ? 343  LYS A CB  1 
ATOM   1872 C CG  . LYS A 1 343  ? 166.424 198.169 142.488 1.00 89.65  ? 343  LYS A CG  1 
ATOM   1873 C CD  . LYS A 1 343  ? 166.641 198.214 143.989 1.00 91.13  ? 343  LYS A CD  1 
ATOM   1874 C CE  . LYS A 1 343  ? 167.447 197.016 144.460 1.00 90.01  ? 343  LYS A CE  1 
ATOM   1875 N NZ  . LYS A 1 343  ? 167.639 197.016 145.935 1.00 89.11  ? 343  LYS A NZ  1 
ATOM   1876 N N   . GLN A 1 344  ? 167.428 199.886 138.876 1.00 97.16  ? 344  GLN A N   1 
ATOM   1877 C CA  . GLN A 1 344  ? 166.673 200.856 138.088 1.00 98.53  ? 344  GLN A CA  1 
ATOM   1878 C C   . GLN A 1 344  ? 165.957 200.188 136.919 1.00 100.64 ? 344  GLN A C   1 
ATOM   1879 O O   . GLN A 1 344  ? 164.794 200.498 136.638 1.00 99.33  ? 344  GLN A O   1 
ATOM   1880 C CB  . GLN A 1 344  ? 167.603 201.959 137.583 1.00 98.85  ? 344  GLN A CB  1 
ATOM   1881 C CG  . GLN A 1 344  ? 168.208 202.815 138.679 1.00 99.28  ? 344  GLN A CG  1 
ATOM   1882 C CD  . GLN A 1 344  ? 169.326 203.703 138.170 1.00 100.54 ? 344  GLN A CD  1 
ATOM   1883 O OE1 . GLN A 1 344  ? 169.574 203.781 136.967 1.00 99.02  ? 344  GLN A OE1 1 
ATOM   1884 N NE2 . GLN A 1 344  ? 170.011 204.376 139.087 1.00 99.48  ? 344  GLN A NE2 1 
ATOM   1885 N N   . ILE A 1 345  ? 166.634 199.269 136.229 1.00 97.70  ? 345  ILE A N   1 
ATOM   1886 C CA  . ILE A 1 345  ? 166.061 198.640 135.046 1.00 95.92  ? 345  ILE A CA  1 
ATOM   1887 C C   . ILE A 1 345  ? 165.141 197.500 135.458 1.00 95.97  ? 345  ILE A C   1 
ATOM   1888 O O   . ILE A 1 345  ? 165.448 196.727 136.375 1.00 97.86  ? 345  ILE A O   1 
ATOM   1889 C CB  . ILE A 1 345  ? 167.179 198.140 134.117 1.00 96.28  ? 345  ILE A CB  1 
ATOM   1890 C CG1 . ILE A 1 345  ? 168.281 199.192 134.004 1.00 98.67  ? 345  ILE A CG1 1 
ATOM   1891 C CG2 . ILE A 1 345  ? 166.622 197.814 132.745 1.00 95.48  ? 345  ILE A CG2 1 
ATOM   1892 C CD1 . ILE A 1 345  ? 169.491 198.723 133.236 1.00 98.61  ? 345  ILE A CD1 1 
ATOM   1893 N N   . THR A 1 346  ? 164.002 197.387 134.777 1.00 89.04  ? 346  THR A N   1 
ATOM   1894 C CA  . THR A 1 346  ? 163.027 196.345 135.061 1.00 87.56  ? 346  THR A CA  1 
ATOM   1895 C C   . THR A 1 346  ? 162.546 195.728 133.757 1.00 87.91  ? 346  THR A C   1 
ATOM   1896 O O   . THR A 1 346  ? 162.694 196.306 132.679 1.00 90.93  ? 346  THR A O   1 
ATOM   1897 C CB  . THR A 1 346  ? 161.820 196.882 135.844 1.00 90.06  ? 346  THR A CB  1 
ATOM   1898 O OG1 . THR A 1 346  ? 161.185 197.923 135.092 1.00 92.44  ? 346  THR A OG1 1 
ATOM   1899 C CG2 . THR A 1 346  ? 162.249 197.425 137.198 1.00 90.10  ? 346  THR A CG2 1 
ATOM   1900 N N   . TYR A 1 347  ? 161.966 194.536 133.873 1.00 75.79  ? 347  TYR A N   1 
ATOM   1901 C CA  . TYR A 1 347  ? 161.335 193.864 132.748 1.00 75.60  ? 347  TYR A CA  1 
ATOM   1902 C C   . TYR A 1 347  ? 160.038 193.223 133.219 1.00 76.24  ? 347  TYR A C   1 
ATOM   1903 O O   . TYR A 1 347  ? 159.841 192.965 134.408 1.00 80.95  ? 347  TYR A O   1 
ATOM   1904 C CB  . TYR A 1 347  ? 162.257 192.813 132.114 1.00 77.49  ? 347  TYR A CB  1 
ATOM   1905 C CG  . TYR A 1 347  ? 162.551 191.617 132.989 1.00 75.52  ? 347  TYR A CG  1 
ATOM   1906 C CD1 . TYR A 1 347  ? 163.622 191.624 133.868 1.00 71.61  ? 347  TYR A CD1 1 
ATOM   1907 C CD2 . TYR A 1 347  ? 161.769 190.474 132.922 1.00 76.95  ? 347  TYR A CD2 1 
ATOM   1908 C CE1 . TYR A 1 347  ? 163.899 190.532 134.663 1.00 71.08  ? 347  TYR A CE1 1 
ATOM   1909 C CE2 . TYR A 1 347  ? 162.038 189.379 133.714 1.00 74.07  ? 347  TYR A CE2 1 
ATOM   1910 C CZ  . TYR A 1 347  ? 163.103 189.413 134.581 1.00 70.93  ? 347  TYR A CZ  1 
ATOM   1911 O OH  . TYR A 1 347  ? 163.374 188.323 135.371 1.00 74.42  ? 347  TYR A OH  1 
ATOM   1912 N N   . THR A 1 348  ? 159.150 192.963 132.270 1.00 75.98  ? 348  THR A N   1 
ATOM   1913 C CA  . THR A 1 348  ? 157.836 192.411 132.565 1.00 79.34  ? 348  THR A CA  1 
ATOM   1914 C C   . THR A 1 348  ? 157.699 191.030 131.927 1.00 80.28  ? 348  THR A C   1 
ATOM   1915 O O   . THR A 1 348  ? 158.655 190.473 131.384 1.00 80.55  ? 348  THR A O   1 
ATOM   1916 C CB  . THR A 1 348  ? 156.736 193.359 132.087 1.00 78.42  ? 348  THR A CB  1 
ATOM   1917 O OG1 . THR A 1 348  ? 155.475 192.678 132.117 1.00 83.91  ? 348  THR A OG1 1 
ATOM   1918 C CG2 . THR A 1 348  ? 157.018 193.829 130.673 1.00 77.74  ? 348  THR A CG2 1 
ATOM   1919 N N   . LEU A 1 349  ? 156.488 190.476 132.009 1.00 72.78  ? 349  LEU A N   1 
ATOM   1920 C CA  . LEU A 1 349  ? 156.234 189.153 131.450 1.00 71.94  ? 349  LEU A CA  1 
ATOM   1921 C C   . LEU A 1 349  ? 156.421 189.143 129.940 1.00 74.69  ? 349  LEU A C   1 
ATOM   1922 O O   . LEU A 1 349  ? 156.953 188.179 129.380 1.00 79.61  ? 349  LEU A O   1 
ATOM   1923 C CB  . LEU A 1 349  ? 154.824 188.694 131.817 1.00 72.89  ? 349  LEU A CB  1 
ATOM   1924 C CG  . LEU A 1 349  ? 154.289 187.459 131.092 1.00 68.55  ? 349  LEU A CG  1 
ATOM   1925 C CD1 . LEU A 1 349  ? 155.151 186.253 131.391 1.00 69.84  ? 349  LEU A CD1 1 
ATOM   1926 C CD2 . LEU A 1 349  ? 152.848 187.195 131.481 1.00 68.96  ? 349  LEU A CD2 1 
ATOM   1927 N N   . GLU A 1 350  ? 155.998 190.213 129.266 1.00 80.23  ? 350  GLU A N   1 
ATOM   1928 C CA  . GLU A 1 350  ? 156.023 190.247 127.809 1.00 78.02  ? 350  GLU A CA  1 
ATOM   1929 C C   . GLU A 1 350  ? 157.428 190.115 127.241 1.00 83.71  ? 350  GLU A C   1 
ATOM   1930 O O   . GLU A 1 350  ? 157.578 189.773 126.064 1.00 90.79  ? 350  GLU A O   1 
ATOM   1931 C CB  . GLU A 1 350  ? 155.388 191.544 127.311 1.00 83.88  ? 350  GLU A CB  1 
ATOM   1932 C CG  . GLU A 1 350  ? 154.078 191.892 127.993 1.00 87.86  ? 350  GLU A CG  1 
ATOM   1933 C CD  . GLU A 1 350  ? 153.610 193.297 127.669 1.00 90.84  ? 350  GLU A CD  1 
ATOM   1934 O OE1 . GLU A 1 350  ? 154.053 193.851 126.642 1.00 93.09  ? 350  GLU A OE1 1 
ATOM   1935 O OE2 . GLU A 1 350  ? 152.806 193.851 128.447 1.00 85.51  ? 350  GLU A OE2 1 
ATOM   1936 N N   . ASP A 1 351  ? 158.459 190.379 128.040 1.00 78.04  ? 351  ASP A N   1 
ATOM   1937 C CA  . ASP A 1 351  ? 159.826 190.336 127.546 1.00 76.46  ? 351  ASP A CA  1 
ATOM   1938 C C   . ASP A 1 351  ? 160.437 188.943 127.566 1.00 80.16  ? 351  ASP A C   1 
ATOM   1939 O O   . ASP A 1 351  ? 161.457 188.724 126.904 1.00 80.28  ? 351  ASP A O   1 
ATOM   1940 C CB  . ASP A 1 351  ? 160.708 191.280 128.366 1.00 77.50  ? 351  ASP A CB  1 
ATOM   1941 C CG  . ASP A 1 351  ? 160.160 192.689 128.412 1.00 83.48  ? 351  ASP A CG  1 
ATOM   1942 O OD1 . ASP A 1 351  ? 159.529 193.113 127.423 1.00 83.82  ? 351  ASP A OD1 1 
ATOM   1943 O OD2 . ASP A 1 351  ? 160.357 193.371 129.438 1.00 86.15  ? 351  ASP A OD2 1 
ATOM   1944 N N   . ILE A 1 352  ? 159.854 188.001 128.306 1.00 73.21  ? 352  ILE A N   1 
ATOM   1945 C CA  . ILE A 1 352  ? 160.412 186.656 128.397 1.00 66.88  ? 352  ILE A CA  1 
ATOM   1946 C C   . ILE A 1 352  ? 159.336 185.613 128.134 1.00 71.79  ? 352  ILE A C   1 
ATOM   1947 O O   . ILE A 1 352  ? 159.485 184.446 128.511 1.00 75.12  ? 352  ILE A O   1 
ATOM   1948 C CB  . ILE A 1 352  ? 161.065 186.415 129.768 1.00 65.82  ? 352  ILE A CB  1 
ATOM   1949 C CG1 . ILE A 1 352  ? 160.023 186.525 130.876 1.00 67.30  ? 352  ILE A CG1 1 
ATOM   1950 C CG2 . ILE A 1 352  ? 162.195 187.398 130.005 1.00 69.96  ? 352  ILE A CG2 1 
ATOM   1951 C CD1 . ILE A 1 352  ? 160.566 186.205 132.240 1.00 69.24  ? 352  ILE A CD1 1 
ATOM   1952 N N   . CYS A 1 353  ? 158.251 186.014 127.483 1.00 72.90  ? 353  CYS A N   1 
ATOM   1953 C CA  . CYS A 1 353  ? 157.124 185.130 127.233 1.00 69.47  ? 353  CYS A CA  1 
ATOM   1954 C C   . CYS A 1 353  ? 157.101 184.709 125.772 1.00 78.42  ? 353  CYS A C   1 
ATOM   1955 O O   . CYS A 1 353  ? 157.413 185.505 124.881 1.00 85.89  ? 353  CYS A O   1 
ATOM   1956 C CB  . CYS A 1 353  ? 155.801 185.805 127.595 1.00 75.31  ? 353  CYS A CB  1 
ATOM   1957 S SG  . CYS A 1 353  ? 154.350 184.768 127.323 1.00 84.05  ? 353  CYS A SG  1 
ATOM   1958 N N   . GLU A 1 354  ? 156.738 183.451 125.534 1.00 79.74  ? 354  GLU A N   1 
ATOM   1959 C CA  . GLU A 1 354  ? 156.598 182.960 124.171 1.00 80.65  ? 354  GLU A CA  1 
ATOM   1960 C C   . GLU A 1 354  ? 155.509 183.738 123.444 1.00 87.46  ? 354  GLU A C   1 
ATOM   1961 O O   . GLU A 1 354  ? 154.458 184.045 124.010 1.00 89.84  ? 354  GLU A O   1 
ATOM   1962 C CB  . GLU A 1 354  ? 156.276 181.466 124.178 1.00 79.93  ? 354  GLU A CB  1 
ATOM   1963 C CG  . GLU A 1 354  ? 156.218 180.839 122.799 1.00 87.03  ? 354  GLU A CG  1 
ATOM   1964 C CD  . GLU A 1 354  ? 156.003 179.341 122.849 1.00 89.91  ? 354  GLU A CD  1 
ATOM   1965 O OE1 . GLU A 1 354  ? 156.140 178.756 123.943 1.00 88.45  ? 354  GLU A OE1 1 
ATOM   1966 O OE2 . GLU A 1 354  ? 155.694 178.748 121.794 1.00 89.54  ? 354  GLU A OE2 1 
ATOM   1967 N N   . LYS A 1 355  ? 155.768 184.059 122.182 1.00 88.94  ? 355  LYS A N   1 
ATOM   1968 C CA  . LYS A 1 355  ? 154.912 184.939 121.402 1.00 89.19  ? 355  LYS A CA  1 
ATOM   1969 C C   . LYS A 1 355  ? 154.013 184.131 120.478 1.00 89.60  ? 355  LYS A C   1 
ATOM   1970 O O   . LYS A 1 355  ? 154.453 183.159 119.858 1.00 90.80  ? 355  LYS A O   1 
ATOM   1971 C CB  . LYS A 1 355  ? 155.746 185.921 120.577 1.00 87.61  ? 355  LYS A CB  1 
ATOM   1972 C CG  . LYS A 1 355  ? 156.738 186.731 121.391 1.00 89.38  ? 355  LYS A CG  1 
ATOM   1973 C CD  . LYS A 1 355  ? 156.033 187.614 122.401 1.00 90.06  ? 355  LYS A CD  1 
ATOM   1974 C CE  . LYS A 1 355  ? 157.023 188.497 123.137 1.00 87.58  ? 355  LYS A CE  1 
ATOM   1975 N NZ  . LYS A 1 355  ? 156.343 189.413 124.091 1.00 87.78  ? 355  LYS A NZ  1 
ATOM   1976 N N   . LYS A 1 356  ? 152.749 184.537 120.399 1.00 98.68  ? 356  LYS A N   1 
ATOM   1977 C CA  . LYS A 1 356  ? 151.788 183.988 119.452 1.00 98.78  ? 356  LYS A CA  1 
ATOM   1978 C C   . LYS A 1 356  ? 151.163 185.151 118.698 1.00 98.97  ? 356  LYS A C   1 
ATOM   1979 O O   . LYS A 1 356  ? 150.387 185.919 119.276 1.00 101.78 ? 356  LYS A O   1 
ATOM   1980 C CB  . LYS A 1 356  ? 150.717 183.163 120.166 1.00 97.73  ? 356  LYS A CB  1 
ATOM   1981 C CG  . LYS A 1 356  ? 149.701 182.518 119.244 1.00 98.34  ? 356  LYS A CG  1 
ATOM   1982 C CD  . LYS A 1 356  ? 150.345 181.476 118.350 1.00 97.36  ? 356  LYS A CD  1 
ATOM   1983 C CE  . LYS A 1 356  ? 149.295 180.672 117.601 1.00 99.57  ? 356  LYS A CE  1 
ATOM   1984 N NZ  . LYS A 1 356  ? 149.907 179.688 116.668 1.00 102.87 ? 356  LYS A NZ  1 
ATOM   1985 N N   . TYR A 1 357  ? 151.506 185.281 117.416 1.00 102.56 ? 357  TYR A N   1 
ATOM   1986 C CA  . TYR A 1 357  ? 151.116 186.435 116.604 1.00 102.85 ? 357  TYR A CA  1 
ATOM   1987 C C   . TYR A 1 357  ? 151.548 187.745 117.254 1.00 103.15 ? 357  TYR A C   1 
ATOM   1988 O O   . TYR A 1 357  ? 150.832 188.746 117.192 1.00 105.80 ? 357  TYR A O   1 
ATOM   1989 C CB  . TYR A 1 357  ? 149.609 186.456 116.333 1.00 104.10 ? 357  TYR A CB  1 
ATOM   1990 C CG  . TYR A 1 357  ? 149.058 185.183 115.740 1.00 105.00 ? 357  TYR A CG  1 
ATOM   1991 C CD1 . TYR A 1 357  ? 149.413 184.777 114.462 1.00 104.54 ? 357  TYR A CD1 1 
ATOM   1992 C CD2 . TYR A 1 357  ? 148.166 184.396 116.452 1.00 106.79 ? 357  TYR A CD2 1 
ATOM   1993 C CE1 . TYR A 1 357  ? 148.906 183.615 113.916 1.00 103.51 ? 357  TYR A CE1 1 
ATOM   1994 C CE2 . TYR A 1 357  ? 147.652 183.235 115.914 1.00 107.01 ? 357  TYR A CE2 1 
ATOM   1995 C CZ  . TYR A 1 357  ? 148.025 182.848 114.647 1.00 105.22 ? 357  TYR A CZ  1 
ATOM   1996 O OH  . TYR A 1 357  ? 147.515 181.690 114.108 1.00 106.20 ? 357  TYR A OH  1 
ATOM   1997 N N   . GLY A 1 358  ? 152.717 187.748 117.887 1.00 104.04 ? 358  GLY A N   1 
ATOM   1998 C CA  . GLY A 1 358  ? 153.194 188.931 118.575 1.00 105.93 ? 358  GLY A CA  1 
ATOM   1999 C C   . GLY A 1 358  ? 152.797 188.970 120.036 1.00 106.77 ? 358  GLY A C   1 
ATOM   2000 O O   . GLY A 1 358  ? 153.620 189.283 120.901 1.00 106.99 ? 358  GLY A O   1 
ATOM   2001 N N   . ASP A 1 359  ? 151.536 188.661 120.323 1.00 104.82 ? 359  ASP A N   1 
ATOM   2002 C CA  . ASP A 1 359  ? 151.055 188.666 121.695 1.00 103.43 ? 359  ASP A CA  1 
ATOM   2003 C C   . ASP A 1 359  ? 151.570 187.447 122.454 1.00 101.47 ? 359  ASP A C   1 
ATOM   2004 O O   . ASP A 1 359  ? 152.076 186.483 121.873 1.00 104.37 ? 359  ASP A O   1 
ATOM   2005 C CB  . ASP A 1 359  ? 149.528 188.689 121.727 1.00 102.62 ? 359  ASP A CB  1 
ATOM   2006 C CG  . ASP A 1 359  ? 148.952 189.868 120.978 1.00 104.85 ? 359  ASP A CG  1 
ATOM   2007 O OD1 . ASP A 1 359  ? 149.638 190.907 120.888 1.00 105.69 ? 359  ASP A OD1 1 
ATOM   2008 O OD2 . ASP A 1 359  ? 147.814 189.757 120.477 1.00 103.84 ? 359  ASP A OD2 1 
ATOM   2009 N N   . CYS A 1 360  ? 151.437 187.505 123.776 1.00 90.39  ? 360  CYS A N   1 
ATOM   2010 C CA  . CYS A 1 360  ? 151.823 186.381 124.617 1.00 90.61  ? 360  CYS A CA  1 
ATOM   2011 C C   . CYS A 1 360  ? 150.955 185.168 124.312 1.00 94.52  ? 360  CYS A C   1 
ATOM   2012 O O   . CYS A 1 360  ? 149.742 185.284 124.118 1.00 94.58  ? 360  CYS A O   1 
ATOM   2013 C CB  . CYS A 1 360  ? 151.701 186.760 126.092 1.00 89.22  ? 360  CYS A CB  1 
ATOM   2014 S SG  . CYS A 1 360  ? 152.764 188.128 126.601 1.00 99.61  ? 360  CYS A SG  1 
ATOM   2015 N N   . ASN A 1 361  ? 151.583 183.993 124.274 1.00 90.45  ? 361  ASN A N   1 
ATOM   2016 C CA  . ASN A 1 361  ? 150.896 182.757 123.903 1.00 89.13  ? 361  ASN A CA  1 
ATOM   2017 C C   . ASN A 1 361  ? 150.172 182.154 125.110 1.00 92.31  ? 361  ASN A C   1 
ATOM   2018 O O   . ASN A 1 361  ? 150.342 180.990 125.467 1.00 92.61  ? 361  ASN A O   1 
ATOM   2019 C CB  . ASN A 1 361  ? 151.885 181.769 123.299 1.00 84.73  ? 361  ASN A CB  1 
ATOM   2020 C CG  . ASN A 1 361  ? 151.199 180.591 122.638 1.00 88.19  ? 361  ASN A CG  1 
ATOM   2021 O OD1 . ASN A 1 361  ? 150.007 180.641 122.339 1.00 83.33  ? 361  ASN A OD1 1 
ATOM   2022 N ND2 . ASN A 1 361  ? 151.951 179.522 122.405 1.00 89.97  ? 361  ASN A ND2 1 
ATOM   2023 N N   . PHE A 1 362  ? 149.340 182.980 125.736 1.00 82.32  ? 362  PHE A N   1 
ATOM   2024 C CA  . PHE A 1 362  ? 148.566 182.536 126.883 1.00 71.71  ? 362  PHE A CA  1 
ATOM   2025 C C   . PHE A 1 362  ? 147.594 181.432 126.488 1.00 73.17  ? 362  PHE A C   1 
ATOM   2026 O O   . PHE A 1 362  ? 147.044 181.421 125.385 1.00 81.70  ? 362  PHE A O   1 
ATOM   2027 C CB  . PHE A 1 362  ? 147.794 183.704 127.490 1.00 76.23  ? 362  PHE A CB  1 
ATOM   2028 C CG  . PHE A 1 362  ? 148.453 184.309 128.689 1.00 75.46  ? 362  PHE A CG  1 
ATOM   2029 C CD1 . PHE A 1 362  ? 149.546 185.142 128.547 1.00 80.54  ? 362  PHE A CD1 1 
ATOM   2030 C CD2 . PHE A 1 362  ? 147.973 184.052 129.959 1.00 75.23  ? 362  PHE A CD2 1 
ATOM   2031 C CE1 . PHE A 1 362  ? 150.151 185.702 129.650 1.00 83.17  ? 362  PHE A CE1 1 
ATOM   2032 C CE2 . PHE A 1 362  ? 148.573 184.610 131.065 1.00 77.69  ? 362  PHE A CE2 1 
ATOM   2033 C CZ  . PHE A 1 362  ? 149.664 185.435 130.911 1.00 82.46  ? 362  PHE A CZ  1 
ATOM   2034 N N   . SER A 1 363  ? 147.394 180.490 127.403 1.00 64.97  ? 363  SER A N   1 
ATOM   2035 C CA  . SER A 1 363  ? 146.393 179.435 127.260 1.00 68.41  ? 363  SER A CA  1 
ATOM   2036 C C   . SER A 1 363  ? 145.397 179.612 128.398 1.00 70.25  ? 363  SER A C   1 
ATOM   2037 O O   . SER A 1 363  ? 145.514 178.981 129.450 1.00 68.17  ? 363  SER A O   1 
ATOM   2038 C CB  . SER A 1 363  ? 147.032 178.060 127.278 1.00 68.76  ? 363  SER A CB  1 
ATOM   2039 O OG  . SER A 1 363  ? 146.045 177.045 127.235 1.00 70.07  ? 363  SER A OG  1 
ATOM   2040 N N   . SER A 1 364  ? 144.409 180.476 128.180 1.00 72.07  ? 364  SER A N   1 
ATOM   2041 C CA  . SER A 1 364  ? 143.449 180.825 129.213 1.00 65.45  ? 364  SER A CA  1 
ATOM   2042 C C   . SER A 1 364  ? 142.059 180.916 128.607 1.00 65.30  ? 364  SER A C   1 
ATOM   2043 O O   . SER A 1 364  ? 141.892 181.017 127.390 1.00 70.82  ? 364  SER A O   1 
ATOM   2044 C CB  . SER A 1 364  ? 143.807 182.150 129.894 1.00 71.23  ? 364  SER A CB  1 
ATOM   2045 O OG  . SER A 1 364  ? 143.783 183.220 128.969 1.00 71.45  ? 364  SER A OG  1 
ATOM   2046 N N   . LEU A 1 365  ? 141.056 180.876 129.485 1.00 64.07  ? 365  LEU A N   1 
ATOM   2047 C CA  . LEU A 1 365  ? 139.672 180.994 129.044 1.00 69.70  ? 365  LEU A CA  1 
ATOM   2048 C C   . LEU A 1 365  ? 139.420 182.314 128.334 1.00 69.16  ? 365  LEU A C   1 
ATOM   2049 O O   . LEU A 1 365  ? 138.616 182.372 127.398 1.00 77.30  ? 365  LEU A O   1 
ATOM   2050 C CB  . LEU A 1 365  ? 138.735 180.848 130.242 1.00 66.34  ? 365  LEU A CB  1 
ATOM   2051 C CG  . LEU A 1 365  ? 137.275 181.260 130.064 1.00 63.41  ? 365  LEU A CG  1 
ATOM   2052 C CD1 . LEU A 1 365  ? 136.585 180.378 129.043 1.00 65.54  ? 365  LEU A CD1 1 
ATOM   2053 C CD2 . LEU A 1 365  ? 136.553 181.213 131.395 1.00 65.20  ? 365  LEU A CD2 1 
ATOM   2054 N N   . PHE A 1 366  ? 140.108 183.376 128.743 1.00 65.98  ? 366  PHE A N   1 
ATOM   2055 C CA  . PHE A 1 366  ? 139.807 184.711 128.245 1.00 69.14  ? 366  PHE A CA  1 
ATOM   2056 C C   . PHE A 1 366  ? 140.261 184.938 126.812 1.00 72.60  ? 366  PHE A C   1 
ATOM   2057 O O   . PHE A 1 366  ? 140.129 186.062 126.317 1.00 75.58  ? 366  PHE A O   1 
ATOM   2058 C CB  . PHE A 1 366  ? 140.425 185.749 129.178 1.00 69.93  ? 366  PHE A CB  1 
ATOM   2059 C CG  . PHE A 1 366  ? 139.981 185.603 130.600 1.00 69.39  ? 366  PHE A CG  1 
ATOM   2060 C CD1 . PHE A 1 366  ? 138.776 186.135 131.018 1.00 70.24  ? 366  PHE A CD1 1 
ATOM   2061 C CD2 . PHE A 1 366  ? 140.754 184.912 131.513 1.00 69.85  ? 366  PHE A CD2 1 
ATOM   2062 C CE1 . PHE A 1 366  ? 138.358 185.992 132.321 1.00 71.70  ? 366  PHE A CE1 1 
ATOM   2063 C CE2 . PHE A 1 366  ? 140.339 184.767 132.817 1.00 69.32  ? 366  PHE A CE2 1 
ATOM   2064 C CZ  . PHE A 1 366  ? 139.141 185.308 133.221 1.00 70.81  ? 366  PHE A CZ  1 
ATOM   2065 N N   . LEU A 1 367  ? 140.793 183.920 126.133 1.00 83.52  ? 367  LEU A N   1 
ATOM   2066 C CA  . LEU A 1 367  ? 141.008 184.034 124.697 1.00 84.49  ? 367  LEU A CA  1 
ATOM   2067 C C   . LEU A 1 367  ? 139.696 184.056 123.928 1.00 85.26  ? 367  LEU A C   1 
ATOM   2068 O O   . LEU A 1 367  ? 139.669 184.524 122.786 1.00 90.82  ? 367  LEU A O   1 
ATOM   2069 C CB  . LEU A 1 367  ? 141.883 182.886 124.195 1.00 83.17  ? 367  LEU A CB  1 
ATOM   2070 C CG  . LEU A 1 367  ? 143.317 182.846 124.717 1.00 82.34  ? 367  LEU A CG  1 
ATOM   2071 C CD1 . LEU A 1 367  ? 144.069 181.681 124.102 1.00 82.86  ? 367  LEU A CD1 1 
ATOM   2072 C CD2 . LEU A 1 367  ? 144.026 184.157 124.428 1.00 81.71  ? 367  LEU A CD2 1 
ATOM   2073 N N   . TYR A 1 368  ? 138.613 183.555 124.526 1.00 85.23  ? 368  TYR A N   1 
ATOM   2074 C CA  . TYR A 1 368  ? 137.315 183.592 123.863 1.00 85.42  ? 368  TYR A CA  1 
ATOM   2075 C C   . TYR A 1 368  ? 136.806 185.020 123.721 1.00 86.48  ? 368  TYR A C   1 
ATOM   2076 O O   . TYR A 1 368  ? 136.240 185.382 122.684 1.00 88.73  ? 368  TYR A O   1 
ATOM   2077 C CB  . TYR A 1 368  ? 136.311 182.737 124.633 1.00 85.57  ? 368  TYR A CB  1 
ATOM   2078 C CG  . TYR A 1 368  ? 134.908 182.795 124.079 1.00 87.55  ? 368  TYR A CG  1 
ATOM   2079 C CD1 . TYR A 1 368  ? 134.531 181.996 123.012 1.00 87.68  ? 368  TYR A CD1 1 
ATOM   2080 C CD2 . TYR A 1 368  ? 133.960 183.648 124.625 1.00 89.44  ? 368  TYR A CD2 1 
ATOM   2081 C CE1 . TYR A 1 368  ? 133.252 182.046 122.502 1.00 89.05  ? 368  TYR A CE1 1 
ATOM   2082 C CE2 . TYR A 1 368  ? 132.679 183.706 124.122 1.00 88.31  ? 368  TYR A CE2 1 
ATOM   2083 C CZ  . TYR A 1 368  ? 132.329 182.903 123.061 1.00 90.08  ? 368  TYR A CZ  1 
ATOM   2084 O OH  . TYR A 1 368  ? 131.051 182.956 122.558 1.00 93.26  ? 368  TYR A OH  1 
ATOM   2085 N N   . TYR A 1 369  ? 136.993 185.842 124.749 1.00 85.13  ? 369  TYR A N   1 
ATOM   2086 C CA  . TYR A 1 369  ? 136.537 187.224 124.730 1.00 87.61  ? 369  TYR A CA  1 
ATOM   2087 C C   . TYR A 1 369  ? 137.530 188.164 124.063 1.00 88.59  ? 369  TYR A C   1 
ATOM   2088 O O   . TYR A 1 369  ? 137.265 189.367 123.984 1.00 86.91  ? 369  TYR A O   1 
ATOM   2089 C CB  . TYR A 1 369  ? 136.261 187.711 126.154 1.00 86.02  ? 369  TYR A CB  1 
ATOM   2090 C CG  . TYR A 1 369  ? 135.486 186.733 127.000 1.00 85.05  ? 369  TYR A CG  1 
ATOM   2091 C CD1 . TYR A 1 369  ? 134.106 186.648 126.907 1.00 87.35  ? 369  TYR A CD1 1 
ATOM   2092 C CD2 . TYR A 1 369  ? 136.133 185.900 127.898 1.00 87.21  ? 369  TYR A CD2 1 
ATOM   2093 C CE1 . TYR A 1 369  ? 133.395 185.757 127.680 1.00 87.80  ? 369  TYR A CE1 1 
ATOM   2094 C CE2 . TYR A 1 369  ? 135.431 185.007 128.674 1.00 85.76  ? 369  TYR A CE2 1 
ATOM   2095 C CZ  . TYR A 1 369  ? 134.063 184.939 128.562 1.00 84.66  ? 369  TYR A CZ  1 
ATOM   2096 O OH  . TYR A 1 369  ? 133.359 184.049 129.336 1.00 85.24  ? 369  TYR A OH  1 
ATOM   2097 N N   . GLU A 1 370  ? 138.660 187.648 123.594 1.00 104.70 ? 370  GLU A N   1 
ATOM   2098 C CA  . GLU A 1 370  ? 139.709 188.501 123.057 1.00 103.71 ? 370  GLU A CA  1 
ATOM   2099 C C   . GLU A 1 370  ? 139.255 189.187 121.775 1.00 105.86 ? 370  GLU A C   1 
ATOM   2100 O O   . GLU A 1 370  ? 138.666 188.561 120.889 1.00 106.51 ? 370  GLU A O   1 
ATOM   2101 C CB  . GLU A 1 370  ? 140.969 187.680 122.798 1.00 103.33 ? 370  GLU A CB  1 
ATOM   2102 C CG  . GLU A 1 370  ? 142.215 188.507 122.557 1.00 105.75 ? 370  GLU A CG  1 
ATOM   2103 C CD  . GLU A 1 370  ? 143.444 187.649 122.340 1.00 108.58 ? 370  GLU A CD  1 
ATOM   2104 O OE1 . GLU A 1 370  ? 143.284 186.438 122.079 1.00 108.55 ? 370  GLU A OE1 1 
ATOM   2105 O OE2 . GLU A 1 370  ? 144.569 188.181 122.435 1.00 111.10 ? 370  GLU A OE2 1 
ATOM   2106 N N   . LYS A 1 371  ? 139.537 190.487 121.688 1.00 111.21 ? 371  LYS A N   1 
ATOM   2107 C CA  . LYS A 1 371  ? 139.257 191.295 120.499 1.00 110.41 ? 371  LYS A CA  1 
ATOM   2108 C C   . LYS A 1 371  ? 137.786 191.215 120.096 1.00 110.12 ? 371  LYS A C   1 
ATOM   2109 O O   . LYS A 1 371  ? 137.443 191.137 118.915 1.00 111.38 ? 371  LYS A O   1 
ATOM   2110 C CB  . LYS A 1 371  ? 140.170 190.895 119.338 1.00 110.31 ? 371  LYS A CB  1 
ATOM   2111 C CG  . LYS A 1 371  ? 140.425 192.016 118.343 1.00 111.72 ? 371  LYS A CG  1 
ATOM   2112 C CD  . LYS A 1 371  ? 141.676 191.755 117.521 1.00 113.05 ? 371  LYS A CD  1 
ATOM   2113 C CE  . LYS A 1 371  ? 141.524 190.526 116.644 1.00 112.52 ? 371  LYS A CE  1 
ATOM   2114 N NZ  . LYS A 1 371  ? 140.488 190.720 115.595 1.00 110.32 ? 371  LYS A NZ  1 
ATOM   2115 N N   . GLY A 1 372  ? 136.906 191.227 121.093 1.00 105.49 ? 372  GLY A N   1 
ATOM   2116 C CA  . GLY A 1 372  ? 135.486 191.354 120.842 1.00 107.69 ? 372  GLY A CA  1 
ATOM   2117 C C   . GLY A 1 372  ? 134.802 190.133 120.274 1.00 107.79 ? 372  GLY A C   1 
ATOM   2118 O O   . GLY A 1 372  ? 133.656 190.246 119.824 1.00 107.60 ? 372  GLY A O   1 
ATOM   2119 N N   . ASN A 1 373  ? 135.461 188.973 120.265 1.00 106.70 ? 373  ASN A N   1 
ATOM   2120 C CA  . ASN A 1 373  ? 134.799 187.763 119.789 1.00 106.68 ? 373  ASN A CA  1 
ATOM   2121 C C   . ASN A 1 373  ? 133.609 187.408 120.669 1.00 108.09 ? 373  ASN A C   1 
ATOM   2122 O O   . ASN A 1 373  ? 132.548 187.022 120.168 1.00 109.73 ? 373  ASN A O   1 
ATOM   2123 C CB  . ASN A 1 373  ? 135.791 186.604 119.738 1.00 103.77 ? 373  ASN A CB  1 
ATOM   2124 C CG  . ASN A 1 373  ? 135.175 185.337 119.184 1.00 105.77 ? 373  ASN A CG  1 
ATOM   2125 O OD1 . ASN A 1 373  ? 134.213 185.385 118.418 1.00 105.48 ? 373  ASN A OD1 1 
ATOM   2126 N ND2 . ASN A 1 373  ? 135.725 184.194 119.570 1.00 107.19 ? 373  ASN A ND2 1 
ATOM   2127 N N   . GLY A 1 374  ? 133.769 187.529 121.987 1.00 101.70 ? 374  GLY A N   1 
ATOM   2128 C CA  . GLY A 1 374  ? 132.683 187.287 122.909 1.00 101.12 ? 374  GLY A CA  1 
ATOM   2129 C C   . GLY A 1 374  ? 132.636 188.371 123.967 1.00 103.75 ? 374  GLY A C   1 
ATOM   2130 O O   . GLY A 1 374  ? 133.504 189.243 124.030 1.00 100.82 ? 374  GLY A O   1 
ATOM   2131 N N   . TYR A 1 375  ? 131.600 188.304 124.795 1.00 109.53 ? 375  TYR A N   1 
ATOM   2132 C CA  . TYR A 1 375  ? 131.404 189.256 125.876 1.00 107.95 ? 375  TYR A CA  1 
ATOM   2133 C C   . TYR A 1 375  ? 131.257 188.514 127.195 1.00 107.60 ? 375  TYR A C   1 
ATOM   2134 O O   . TYR A 1 375  ? 130.617 187.460 127.259 1.00 104.82 ? 375  TYR A O   1 
ATOM   2135 C CB  . TYR A 1 375  ? 130.183 190.135 125.619 1.00 107.60 ? 375  TYR A CB  1 
ATOM   2136 C CG  . TYR A 1 375  ? 130.326 191.002 124.391 1.00 107.83 ? 375  TYR A CG  1 
ATOM   2137 C CD1 . TYR A 1 375  ? 130.936 192.245 124.466 1.00 107.87 ? 375  TYR A CD1 1 
ATOM   2138 C CD2 . TYR A 1 375  ? 129.864 190.572 123.156 1.00 107.37 ? 375  TYR A CD2 1 
ATOM   2139 C CE1 . TYR A 1 375  ? 131.074 193.041 123.347 1.00 108.20 ? 375  TYR A CE1 1 
ATOM   2140 C CE2 . TYR A 1 375  ? 129.997 191.360 122.030 1.00 108.00 ? 375  TYR A CE2 1 
ATOM   2141 C CZ  . TYR A 1 375  ? 130.603 192.594 122.131 1.00 109.63 ? 375  TYR A CZ  1 
ATOM   2142 O OH  . TYR A 1 375  ? 130.739 193.383 121.013 1.00 109.31 ? 375  TYR A OH  1 
ATOM   2143 N N   . ILE A 1 376  ? 131.861 189.075 128.245 1.00 101.21 ? 376  ILE A N   1 
ATOM   2144 C CA  . ILE A 1 376  ? 131.875 188.415 129.545 1.00 99.88  ? 376  ILE A CA  1 
ATOM   2145 C C   . ILE A 1 376  ? 130.472 188.301 130.118 1.00 101.77 ? 376  ILE A C   1 
ATOM   2146 O O   . ILE A 1 376  ? 130.109 187.266 130.689 1.00 104.21 ? 376  ILE A O   1 
ATOM   2147 C CB  . ILE A 1 376  ? 132.812 189.167 130.506 1.00 96.11  ? 376  ILE A CB  1 
ATOM   2148 C CG1 . ILE A 1 376  ? 134.165 189.409 129.842 1.00 98.57  ? 376  ILE A CG1 1 
ATOM   2149 C CG2 . ILE A 1 376  ? 132.993 188.383 131.786 1.00 94.91  ? 376  ILE A CG2 1 
ATOM   2150 C CD1 . ILE A 1 376  ? 135.130 190.196 130.696 1.00 97.15  ? 376  ILE A CD1 1 
ATOM   2151 N N   . ASP A 1 377  ? 129.663 189.352 129.980 1.00 107.20 ? 377  ASP A N   1 
ATOM   2152 C CA  . ASP A 1 377  ? 128.334 189.349 130.582 1.00 107.56 ? 377  ASP A CA  1 
ATOM   2153 C C   . ASP A 1 377  ? 127.451 188.264 129.977 1.00 105.73 ? 377  ASP A C   1 
ATOM   2154 O O   . ASP A 1 377  ? 126.796 187.508 130.702 1.00 104.47 ? 377  ASP A O   1 
ATOM   2155 C CB  . ASP A 1 377  ? 127.688 190.724 130.417 1.00 107.50 ? 377  ASP A CB  1 
ATOM   2156 C CG  . ASP A 1 377  ? 128.598 191.849 130.858 1.00 108.53 ? 377  ASP A CG  1 
ATOM   2157 O OD1 . ASP A 1 377  ? 129.437 191.620 131.753 1.00 108.42 ? 377  ASP A OD1 1 
ATOM   2158 O OD2 . ASP A 1 377  ? 128.477 192.963 130.307 1.00 105.85 ? 377  ASP A OD2 1 
ATOM   2159 N N   . TYR A 1 378  ? 127.425 188.170 128.654 1.00 111.16 ? 378  TYR A N   1 
ATOM   2160 C CA  . TYR A 1 378  ? 126.586 187.200 127.970 1.00 111.92 ? 378  TYR A CA  1 
ATOM   2161 C C   . TYR A 1 378  ? 127.165 185.799 128.114 1.00 114.54 ? 378  TYR A C   1 
ATOM   2162 O O   . TYR A 1 378  ? 128.370 185.623 128.304 1.00 115.37 ? 378  TYR A O   1 
ATOM   2163 C CB  . TYR A 1 378  ? 126.445 187.592 126.502 1.00 112.66 ? 378  TYR A CB  1 
ATOM   2164 C CG  . TYR A 1 378  ? 125.886 188.980 126.304 1.00 113.93 ? 378  TYR A CG  1 
ATOM   2165 C CD1 . TYR A 1 378  ? 124.528 189.228 126.443 1.00 112.16 ? 378  TYR A CD1 1 
ATOM   2166 C CD2 . TYR A 1 378  ? 126.716 190.044 125.983 1.00 115.36 ? 378  TYR A CD2 1 
ATOM   2167 C CE1 . TYR A 1 378  ? 124.012 190.496 126.266 1.00 113.66 ? 378  TYR A CE1 1 
ATOM   2168 C CE2 . TYR A 1 378  ? 126.211 191.315 125.804 1.00 116.75 ? 378  TYR A CE2 1 
ATOM   2169 C CZ  . TYR A 1 378  ? 124.858 191.536 125.946 1.00 117.53 ? 378  TYR A CZ  1 
ATOM   2170 O OH  . TYR A 1 378  ? 124.350 192.802 125.768 1.00 116.75 ? 378  TYR A OH  1 
ATOM   2171 N N   . PRO A 1 379  ? 126.322 184.772 128.042 1.00 107.74 ? 379  PRO A N   1 
ATOM   2172 C CA  . PRO A 1 379  ? 126.829 183.399 128.120 1.00 105.36 ? 379  PRO A CA  1 
ATOM   2173 C C   . PRO A 1 379  ? 127.683 183.049 126.913 1.00 103.82 ? 379  PRO A C   1 
ATOM   2174 O O   . PRO A 1 379  ? 127.497 183.575 125.814 1.00 104.46 ? 379  PRO A O   1 
ATOM   2175 C CB  . PRO A 1 379  ? 125.555 182.550 128.165 1.00 105.71 ? 379  PRO A CB  1 
ATOM   2176 C CG  . PRO A 1 379  ? 124.510 183.407 127.542 1.00 105.71 ? 379  PRO A CG  1 
ATOM   2177 C CD  . PRO A 1 379  ? 124.854 184.811 127.935 1.00 106.52 ? 379  PRO A CD  1 
ATOM   2178 N N   . ILE A 1 380  ? 128.627 182.143 127.133 1.00 92.04  ? 380  ILE A N   1 
ATOM   2179 C CA  . ILE A 1 380  ? 129.590 181.767 126.106 1.00 91.78  ? 380  ILE A CA  1 
ATOM   2180 C C   . ILE A 1 380  ? 129.036 180.623 125.269 1.00 93.48  ? 380  ILE A C   1 
ATOM   2181 O O   . ILE A 1 380  ? 128.570 179.609 125.801 1.00 97.41  ? 380  ILE A O   1 
ATOM   2182 C CB  . ILE A 1 380  ? 130.935 181.392 126.752 1.00 91.69  ? 380  ILE A CB  1 
ATOM   2183 C CG1 . ILE A 1 380  ? 131.829 180.662 125.754 1.00 90.66  ? 380  ILE A CG1 1 
ATOM   2184 C CG2 . ILE A 1 380  ? 130.714 180.545 127.994 1.00 93.12  ? 380  ILE A CG2 1 
ATOM   2185 C CD1 . ILE A 1 380  ? 133.176 180.295 126.318 1.00 91.23  ? 380  ILE A CD1 1 
ATOM   2186 N N   . LYS A 1 381  ? 129.088 180.784 123.949 1.00 98.07  ? 381  LYS A N   1 
ATOM   2187 C CA  . LYS A 1 381  ? 128.664 179.756 123.005 1.00 100.41 ? 381  LYS A CA  1 
ATOM   2188 C C   . LYS A 1 381  ? 129.846 179.412 122.115 1.00 100.19 ? 381  LYS A C   1 
ATOM   2189 O O   . LYS A 1 381  ? 130.509 180.312 121.590 1.00 102.71 ? 381  LYS A O   1 
ATOM   2190 C CB  . LYS A 1 381  ? 127.479 180.225 122.157 1.00 102.51 ? 381  LYS A CB  1 
ATOM   2191 C CG  . LYS A 1 381  ? 126.256 180.642 122.953 1.00 102.20 ? 381  LYS A CG  1 
ATOM   2192 C CD  . LYS A 1 381  ? 125.107 181.015 122.028 1.00 101.68 ? 381  LYS A CD  1 
ATOM   2193 C CE  . LYS A 1 381  ? 125.516 182.109 121.054 1.00 101.37 ? 381  LYS A CE  1 
ATOM   2194 N NZ  . LYS A 1 381  ? 124.410 182.469 120.124 1.00 101.26 ? 381  LYS A NZ  1 
ATOM   2195 N N   . VAL A 1 382  ? 130.107 178.119 121.941 1.00 101.89 ? 382  VAL A N   1 
ATOM   2196 C CA  . VAL A 1 382  ? 131.250 177.657 121.165 1.00 102.87 ? 382  VAL A CA  1 
ATOM   2197 C C   . VAL A 1 382  ? 130.816 176.495 120.282 1.00 106.58 ? 382  VAL A C   1 
ATOM   2198 O O   . VAL A 1 382  ? 130.047 175.626 120.699 1.00 106.29 ? 382  VAL A O   1 
ATOM   2199 C CB  . VAL A 1 382  ? 132.425 177.255 122.083 1.00 99.87  ? 382  VAL A CB  1 
ATOM   2200 C CG1 . VAL A 1 382  ? 131.983 176.205 123.085 1.00 100.24 ? 382  VAL A CG1 1 
ATOM   2201 C CG2 . VAL A 1 382  ? 133.597 176.759 121.266 1.00 101.11 ? 382  VAL A CG2 1 
ATOM   2202 N N   . ASP A 1 383  ? 131.320 176.484 119.048 1.00 106.78 ? 383  ASP A N   1 
ATOM   2203 C CA  . ASP A 1 383  ? 130.938 175.481 118.064 1.00 104.92 ? 383  ASP A CA  1 
ATOM   2204 C C   . ASP A 1 383  ? 131.672 174.157 118.228 1.00 103.34 ? 383  ASP A C   1 
ATOM   2205 O O   . ASP A 1 383  ? 131.304 173.181 117.567 1.00 103.58 ? 383  ASP A O   1 
ATOM   2206 C CB  . ASP A 1 383  ? 131.171 176.018 116.646 1.00 103.87 ? 383  ASP A CB  1 
ATOM   2207 C CG  . ASP A 1 383  ? 132.593 176.494 116.429 1.00 104.79 ? 383  ASP A CG  1 
ATOM   2208 O OD1 . ASP A 1 383  ? 133.397 176.432 117.382 1.00 102.70 ? 383  ASP A OD1 1 
ATOM   2209 O OD2 . ASP A 1 383  ? 132.908 176.933 115.303 1.00 107.28 ? 383  ASP A OD2 1 
ATOM   2210 N N   . ASN A 1 384  ? 132.692 174.096 119.080 1.00 100.37 ? 384  ASN A N   1 
ATOM   2211 C CA  . ASN A 1 384  ? 133.432 172.861 119.316 1.00 99.41  ? 384  ASN A CA  1 
ATOM   2212 C C   . ASN A 1 384  ? 134.106 172.944 120.676 1.00 100.08 ? 384  ASN A C   1 
ATOM   2213 O O   . ASN A 1 384  ? 134.875 173.874 120.932 1.00 103.63 ? 384  ASN A O   1 
ATOM   2214 C CB  . ASN A 1 384  ? 134.471 172.615 118.220 1.00 101.21 ? 384  ASN A CB  1 
ATOM   2215 C CG  . ASN A 1 384  ? 135.348 171.417 118.513 1.00 100.74 ? 384  ASN A CG  1 
ATOM   2216 O OD1 . ASN A 1 384  ? 136.449 171.554 119.046 1.00 101.55 ? 384  ASN A OD1 1 
ATOM   2217 N ND2 . ASN A 1 384  ? 134.861 170.231 118.173 1.00 96.94  ? 384  ASN A ND2 1 
ATOM   2218 N N   . LEU A 1 385  ? 133.835 171.964 121.534 1.00 92.45  ? 385  LEU A N   1 
ATOM   2219 C CA  . LEU A 1 385  ? 134.361 171.960 122.893 1.00 94.07  ? 385  LEU A CA  1 
ATOM   2220 C C   . LEU A 1 385  ? 135.749 171.349 123.000 1.00 94.04  ? 385  LEU A C   1 
ATOM   2221 O O   . LEU A 1 385  ? 136.271 171.239 124.114 1.00 92.97  ? 385  LEU A O   1 
ATOM   2222 C CB  . LEU A 1 385  ? 133.405 171.215 123.824 1.00 93.34  ? 385  LEU A CB  1 
ATOM   2223 C CG  . LEU A 1 385  ? 132.144 171.977 124.223 1.00 94.03  ? 385  LEU A CG  1 
ATOM   2224 C CD1 . LEU A 1 385  ? 131.214 171.084 125.025 1.00 94.25  ? 385  LEU A CD1 1 
ATOM   2225 C CD2 . LEU A 1 385  ? 132.517 173.210 125.020 1.00 91.98  ? 385  LEU A CD2 1 
ATOM   2226 N N   . ASP A 1 386  ? 136.358 170.942 121.888 1.00 97.68  ? 386  ASP A N   1 
ATOM   2227 C CA  . ASP A 1 386  ? 137.685 170.343 121.911 1.00 97.81  ? 386  ASP A CA  1 
ATOM   2228 C C   . ASP A 1 386  ? 138.746 171.283 121.355 1.00 98.55  ? 386  ASP A C   1 
ATOM   2229 O O   . ASP A 1 386  ? 139.802 171.455 121.970 1.00 101.71 ? 386  ASP A O   1 
ATOM   2230 C CB  . ASP A 1 386  ? 137.681 169.021 121.134 1.00 99.33  ? 386  ASP A CB  1 
ATOM   2231 C CG  . ASP A 1 386  ? 138.930 168.197 121.379 1.00 101.13 ? 386  ASP A CG  1 
ATOM   2232 O OD1 . ASP A 1 386  ? 139.732 168.575 122.260 1.00 99.71  ? 386  ASP A OD1 1 
ATOM   2233 O OD2 . ASP A 1 386  ? 139.110 167.172 120.690 1.00 99.80  ? 386  ASP A OD2 1 
ATOM   2234 N N   . PHE A 1 387  ? 138.497 171.896 120.200 1.00 96.89  ? 387  PHE A N   1 
ATOM   2235 C CA  . PHE A 1 387  ? 139.464 172.772 119.536 1.00 94.69  ? 387  PHE A CA  1 
ATOM   2236 C C   . PHE A 1 387  ? 138.704 173.927 118.894 1.00 95.37  ? 387  PHE A C   1 
ATOM   2237 O O   . PHE A 1 387  ? 138.148 173.785 117.803 1.00 96.86  ? 387  PHE A O   1 
ATOM   2238 C CB  . PHE A 1 387  ? 140.279 171.992 118.513 1.00 95.07  ? 387  PHE A CB  1 
ATOM   2239 C CG  . PHE A 1 387  ? 141.196 172.844 117.689 1.00 95.79  ? 387  PHE A CG  1 
ATOM   2240 C CD1 . PHE A 1 387  ? 142.402 173.280 118.201 1.00 97.40  ? 387  PHE A CD1 1 
ATOM   2241 C CD2 . PHE A 1 387  ? 140.857 173.200 116.396 1.00 95.45  ? 387  PHE A CD2 1 
ATOM   2242 C CE1 . PHE A 1 387  ? 143.251 174.058 117.443 1.00 98.37  ? 387  PHE A CE1 1 
ATOM   2243 C CE2 . PHE A 1 387  ? 141.701 173.978 115.634 1.00 94.40  ? 387  PHE A CE2 1 
ATOM   2244 C CZ  . PHE A 1 387  ? 142.899 174.409 116.159 1.00 97.50  ? 387  PHE A CZ  1 
ATOM   2245 N N   . TYR A 1 388  ? 138.675 175.068 119.573 1.00 97.09  ? 388  TYR A N   1 
ATOM   2246 C CA  . TYR A 1 388  ? 138.003 176.254 119.064 1.00 96.94  ? 388  TYR A CA  1 
ATOM   2247 C C   . TYR A 1 388  ? 139.026 177.303 118.654 1.00 97.94  ? 388  TYR A C   1 
ATOM   2248 O O   . TYR A 1 388  ? 139.969 177.590 119.393 1.00 100.39 ? 388  TYR A O   1 
ATOM   2249 C CB  . TYR A 1 388  ? 137.053 176.840 120.108 1.00 93.80  ? 388  TYR A CB  1 
ATOM   2250 C CG  . TYR A 1 388  ? 136.487 178.187 119.720 1.00 96.05  ? 388  TYR A CG  1 
ATOM   2251 C CD1 . TYR A 1 388  ? 135.480 178.293 118.774 1.00 97.63  ? 388  TYR A CD1 1 
ATOM   2252 C CD2 . TYR A 1 388  ? 136.961 179.353 120.301 1.00 98.94  ? 388  TYR A CD2 1 
ATOM   2253 C CE1 . TYR A 1 388  ? 134.960 179.520 118.418 1.00 97.77  ? 388  TYR A CE1 1 
ATOM   2254 C CE2 . TYR A 1 388  ? 136.449 180.585 119.950 1.00 98.50  ? 388  TYR A CE2 1 
ATOM   2255 C CZ  . TYR A 1 388  ? 135.448 180.663 119.009 1.00 97.32  ? 388  TYR A CZ  1 
ATOM   2256 O OH  . TYR A 1 388  ? 134.934 181.888 118.657 1.00 97.92  ? 388  TYR A OH  1 
ATOM   2257 N N   . VAL A 1 389  ? 138.828 177.881 117.475 1.00 99.20  ? 389  VAL A N   1 
ATOM   2258 C CA  . VAL A 1 389  ? 139.686 178.941 116.965 1.00 97.47  ? 389  VAL A CA  1 
ATOM   2259 C C   . VAL A 1 389  ? 138.898 180.237 117.044 1.00 97.13  ? 389  VAL A C   1 
ATOM   2260 O O   . VAL A 1 389  ? 137.832 180.362 116.428 1.00 100.83 ? 389  VAL A O   1 
ATOM   2261 C CB  . VAL A 1 389  ? 140.151 178.670 115.530 1.00 100.23 ? 389  VAL A CB  1 
ATOM   2262 C CG1 . VAL A 1 389  ? 140.895 179.876 114.985 1.00 101.33 ? 389  VAL A CG1 1 
ATOM   2263 C CG2 . VAL A 1 389  ? 141.030 177.437 115.485 1.00 100.55 ? 389  VAL A CG2 1 
ATOM   2264 N N   . ASN A 1 390  ? 139.411 181.198 117.806 1.00 103.89 ? 390  ASN A N   1 
ATOM   2265 C CA  . ASN A 1 390  ? 138.798 182.517 117.856 1.00 106.99 ? 390  ASN A CA  1 
ATOM   2266 C C   . ASN A 1 390  ? 138.861 183.161 116.482 1.00 108.08 ? 390  ASN A C   1 
ATOM   2267 O O   . ASN A 1 390  ? 139.944 183.350 115.923 1.00 106.08 ? 390  ASN A O   1 
ATOM   2268 C CB  . ASN A 1 390  ? 139.510 183.386 118.894 1.00 106.75 ? 390  ASN A CB  1 
ATOM   2269 C CG  . ASN A 1 390  ? 138.780 184.686 119.173 1.00 107.25 ? 390  ASN A CG  1 
ATOM   2270 O OD1 . ASN A 1 390  ? 138.404 185.415 118.257 1.00 110.64 ? 390  ASN A OD1 1 
ATOM   2271 N ND2 . ASN A 1 390  ? 138.573 184.979 120.449 1.00 105.00 ? 390  ASN A ND2 1 
ATOM   2272 N N   . ARG A 1 391  ? 137.690 183.491 115.935 1.00 107.73 ? 391  ARG A N   1 
ATOM   2273 C CA  . ARG A 1 391  ? 137.634 184.024 114.579 1.00 106.44 ? 391  ARG A CA  1 
ATOM   2274 C C   . ARG A 1 391  ? 138.371 185.352 114.479 1.00 106.63 ? 391  ARG A C   1 
ATOM   2275 O O   . ARG A 1 391  ? 139.073 185.609 113.494 1.00 108.59 ? 391  ARG A O   1 
ATOM   2276 C CB  . ARG A 1 391  ? 136.180 184.180 114.139 1.00 106.49 ? 391  ARG A CB  1 
ATOM   2277 C CG  . ARG A 1 391  ? 135.321 182.961 114.430 1.00 109.10 ? 391  ARG A CG  1 
ATOM   2278 C CD  . ARG A 1 391  ? 135.928 181.702 113.834 1.00 109.57 ? 391  ARG A CD  1 
ATOM   2279 N NE  . ARG A 1 391  ? 135.298 180.496 114.358 1.00 106.93 ? 391  ARG A NE  1 
ATOM   2280 C CZ  . ARG A 1 391  ? 135.702 179.263 114.087 1.00 107.05 ? 391  ARG A CZ  1 
ATOM   2281 N NH1 . ARG A 1 391  ? 136.736 179.033 113.293 1.00 106.31 ? 391  ARG A NH1 1 
ATOM   2282 N NH2 . ARG A 1 391  ? 135.054 178.235 114.626 1.00 106.94 ? 391  ARG A NH2 1 
ATOM   2283 N N   . ARG A 1 392  ? 138.223 186.210 115.488 1.00 106.39 ? 392  ARG A N   1 
ATOM   2284 C CA  . ARG A 1 392  ? 138.866 187.518 115.447 1.00 108.88 ? 392  ARG A CA  1 
ATOM   2285 C C   . ARG A 1 392  ? 140.384 187.391 115.513 1.00 109.73 ? 392  ARG A C   1 
ATOM   2286 O O   . ARG A 1 392  ? 141.103 187.964 114.687 1.00 109.79 ? 392  ARG A O   1 
ATOM   2287 C CB  . ARG A 1 392  ? 138.350 188.386 116.593 1.00 107.93 ? 392  ARG A CB  1 
ATOM   2288 C CG  . ARG A 1 392  ? 136.840 188.393 116.738 1.00 108.48 ? 392  ARG A CG  1 
ATOM   2289 C CD  . ARG A 1 392  ? 136.163 189.088 115.572 1.00 109.06 ? 392  ARG A CD  1 
ATOM   2290 N NE  . ARG A 1 392  ? 134.712 189.085 115.714 1.00 110.01 ? 392  ARG A NE  1 
ATOM   2291 C CZ  . ARG A 1 392  ? 134.028 189.967 116.430 1.00 110.41 ? 392  ARG A CZ  1 
ATOM   2292 N NH1 . ARG A 1 392  ? 134.632 190.943 117.086 1.00 110.15 ? 392  ARG A NH1 1 
ATOM   2293 N NH2 . ARG A 1 392  ? 132.703 189.865 116.490 1.00 109.08 ? 392  ARG A NH2 1 
ATOM   2294 N N   . THR A 1 393  ? 140.891 186.636 116.487 1.00 109.62 ? 393  THR A N   1 
ATOM   2295 C CA  . THR A 1 393  ? 142.321 186.601 116.767 1.00 108.16 ? 393  THR A CA  1 
ATOM   2296 C C   . THR A 1 393  ? 143.049 185.439 116.105 1.00 108.99 ? 393  THR A C   1 
ATOM   2297 O O   . THR A 1 393  ? 144.283 185.397 116.165 1.00 109.67 ? 393  THR A O   1 
ATOM   2298 C CB  . THR A 1 393  ? 142.560 186.537 118.277 1.00 108.31 ? 393  THR A CB  1 
ATOM   2299 O OG1 . THR A 1 393  ? 142.080 185.287 118.783 1.00 107.73 ? 393  THR A OG1 1 
ATOM   2300 C CG2 . THR A 1 393  ? 141.831 187.668 118.975 1.00 109.09 ? 393  THR A CG2 1 
ATOM   2301 N N   . TYR A 1 394  ? 142.328 184.505 115.484 1.00 110.74 ? 394  TYR A N   1 
ATOM   2302 C CA  . TYR A 1 394  ? 142.923 183.321 114.859 1.00 110.17 ? 394  TYR A CA  1 
ATOM   2303 C C   . TYR A 1 394  ? 143.742 182.507 115.857 1.00 109.36 ? 394  TYR A C   1 
ATOM   2304 O O   . TYR A 1 394  ? 144.738 181.881 115.491 1.00 108.59 ? 394  TYR A O   1 
ATOM   2305 C CB  . TYR A 1 394  ? 143.790 183.693 113.651 1.00 108.42 ? 394  TYR A CB  1 
ATOM   2306 C CG  . TYR A 1 394  ? 143.232 184.807 112.797 1.00 111.06 ? 394  TYR A CG  1 
ATOM   2307 C CD1 . TYR A 1 394  ? 142.208 184.570 111.892 1.00 109.13 ? 394  TYR A CD1 1 
ATOM   2308 C CD2 . TYR A 1 394  ? 143.743 186.095 112.888 1.00 111.34 ? 394  TYR A CD2 1 
ATOM   2309 C CE1 . TYR A 1 394  ? 141.700 185.587 111.109 1.00 107.90 ? 394  TYR A CE1 1 
ATOM   2310 C CE2 . TYR A 1 394  ? 143.242 187.117 112.109 1.00 109.94 ? 394  TYR A CE2 1 
ATOM   2311 C CZ  . TYR A 1 394  ? 142.222 186.859 111.221 1.00 109.11 ? 394  TYR A CZ  1 
ATOM   2312 O OH  . TYR A 1 394  ? 141.722 187.878 110.444 1.00 110.45 ? 394  TYR A OH  1 
ATOM   2313 N N   . LYS A 1 395  ? 143.334 182.506 117.121 1.00 99.97  ? 395  LYS A N   1 
ATOM   2314 C CA  . LYS A 1 395  ? 144.065 181.829 118.184 1.00 97.30  ? 395  LYS A CA  1 
ATOM   2315 C C   . LYS A 1 395  ? 143.313 180.577 118.610 1.00 97.39  ? 395  LYS A C   1 
ATOM   2316 O O   . LYS A 1 395  ? 142.088 180.605 118.767 1.00 96.51  ? 395  LYS A O   1 
ATOM   2317 C CB  . LYS A 1 395  ? 144.276 182.757 119.381 1.00 97.49  ? 395  LYS A CB  1 
ATOM   2318 C CG  . LYS A 1 395  ? 145.257 183.886 119.119 1.00 97.56  ? 395  LYS A CG  1 
ATOM   2319 C CD  . LYS A 1 395  ? 145.524 184.682 120.383 1.00 96.85  ? 395  LYS A CD  1 
ATOM   2320 C CE  . LYS A 1 395  ? 146.580 185.746 120.154 1.00 96.60  ? 395  LYS A CE  1 
ATOM   2321 N NZ  . LYS A 1 395  ? 146.848 186.523 121.392 1.00 97.58  ? 395  LYS A NZ  1 
ATOM   2322 N N   . GLU A 1 396  ? 144.049 179.484 118.786 1.00 100.59 ? 396  GLU A N   1 
ATOM   2323 C CA  . GLU A 1 396  ? 143.451 178.222 119.189 1.00 96.63  ? 396  GLU A CA  1 
ATOM   2324 C C   . GLU A 1 396  ? 143.220 178.187 120.696 1.00 99.71  ? 396  GLU A C   1 
ATOM   2325 O O   . GLU A 1 396  ? 143.882 178.886 121.466 1.00 101.25 ? 396  GLU A O   1 
ATOM   2326 C CB  . GLU A 1 396  ? 144.344 177.055 118.771 1.00 97.93  ? 396  GLU A CB  1 
ATOM   2327 C CG  . GLU A 1 396  ? 145.719 177.038 119.429 1.00 102.32 ? 396  GLU A CG  1 
ATOM   2328 C CD  . GLU A 1 396  ? 146.700 178.007 118.789 1.00 107.19 ? 396  GLU A CD  1 
ATOM   2329 O OE1 . GLU A 1 396  ? 146.327 178.666 117.796 1.00 106.64 ? 396  GLU A OE1 1 
ATOM   2330 O OE2 . GLU A 1 396  ? 147.844 178.109 119.280 1.00 103.99 ? 396  GLU A OE2 1 
ATOM   2331 N N   . MET A 1 397  ? 142.269 177.353 121.113 1.00 92.29  ? 397  MET A N   1 
ATOM   2332 C CA  . MET A 1 397  ? 141.925 177.218 122.524 1.00 87.42  ? 397  MET A CA  1 
ATOM   2333 C C   . MET A 1 397  ? 141.198 175.899 122.725 1.00 86.99  ? 397  MET A C   1 
ATOM   2334 O O   . MET A 1 397  ? 140.302 175.561 121.946 1.00 93.54  ? 397  MET A O   1 
ATOM   2335 C CB  . MET A 1 397  ? 141.059 178.391 122.986 1.00 87.05  ? 397  MET A CB  1 
ATOM   2336 C CG  . MET A 1 397  ? 140.202 178.096 124.200 1.00 91.68  ? 397  MET A CG  1 
ATOM   2337 S SD  . MET A 1 397  ? 139.349 179.559 124.809 1.00 94.07  ? 397  MET A SD  1 
ATOM   2338 C CE  . MET A 1 397  ? 138.695 180.216 123.280 1.00 88.21  ? 397  MET A CE  1 
ATOM   2339 N N   . MET A 1 398  ? 141.587 175.157 123.761 1.00 84.18  ? 398  MET A N   1 
ATOM   2340 C CA  . MET A 1 398  ? 140.975 173.873 124.101 1.00 87.17  ? 398  MET A CA  1 
ATOM   2341 C C   . MET A 1 398  ? 140.212 174.038 125.411 1.00 88.57  ? 398  MET A C   1 
ATOM   2342 O O   . MET A 1 398  ? 140.813 174.206 126.474 1.00 93.44  ? 398  MET A O   1 
ATOM   2343 C CB  . MET A 1 398  ? 142.035 172.783 124.205 1.00 86.63  ? 398  MET A CB  1 
ATOM   2344 C CG  . MET A 1 398  ? 141.512 171.460 124.731 1.00 89.62  ? 398  MET A CG  1 
ATOM   2345 S SD  . MET A 1 398  ? 142.811 170.222 124.902 1.00 103.99 ? 398  MET A SD  1 
ATOM   2346 C CE  . MET A 1 398  ? 143.400 170.114 123.214 1.00 92.72  ? 398  MET A CE  1 
ATOM   2347 N N   . PHE A 1 399  ? 138.881 173.977 125.334 1.00 76.85  ? 399  PHE A N   1 
ATOM   2348 C CA  . PHE A 1 399  ? 138.065 174.231 126.517 1.00 74.92  ? 399  PHE A CA  1 
ATOM   2349 C C   . PHE A 1 399  ? 138.150 173.088 127.518 1.00 73.89  ? 399  PHE A C   1 
ATOM   2350 O O   . PHE A 1 399  ? 137.955 173.294 128.721 1.00 75.77  ? 399  PHE A O   1 
ATOM   2351 C CB  . PHE A 1 399  ? 136.615 174.481 126.113 1.00 73.26  ? 399  PHE A CB  1 
ATOM   2352 C CG  . PHE A 1 399  ? 136.364 175.865 125.608 1.00 69.65  ? 399  PHE A CG  1 
ATOM   2353 C CD1 . PHE A 1 399  ? 136.231 176.920 126.489 1.00 68.05  ? 399  PHE A CD1 1 
ATOM   2354 C CD2 . PHE A 1 399  ? 136.272 176.117 124.253 1.00 76.49  ? 399  PHE A CD2 1 
ATOM   2355 C CE1 . PHE A 1 399  ? 136.004 178.198 126.031 1.00 74.48  ? 399  PHE A CE1 1 
ATOM   2356 C CE2 . PHE A 1 399  ? 136.043 177.394 123.788 1.00 79.90  ? 399  PHE A CE2 1 
ATOM   2357 C CZ  . PHE A 1 399  ? 135.909 178.436 124.679 1.00 77.08  ? 399  PHE A CZ  1 
ATOM   2358 N N   . LYS A 1 400  ? 138.426 171.873 127.045 1.00 73.21  ? 400  LYS A N   1 
ATOM   2359 C CA  . LYS A 1 400  ? 138.558 170.744 127.958 1.00 73.88  ? 400  LYS A CA  1 
ATOM   2360 C C   . LYS A 1 400  ? 139.707 170.964 128.932 1.00 73.40  ? 400  LYS A C   1 
ATOM   2361 O O   . LYS A 1 400  ? 139.586 170.688 130.129 1.00 73.82  ? 400  LYS A O   1 
ATOM   2362 C CB  . LYS A 1 400  ? 138.762 169.450 127.170 1.00 78.17  ? 400  LYS A CB  1 
ATOM   2363 C CG  . LYS A 1 400  ? 137.597 169.076 126.276 1.00 79.32  ? 400  LYS A CG  1 
ATOM   2364 C CD  . LYS A 1 400  ? 136.351 168.786 127.087 1.00 75.57  ? 400  LYS A CD  1 
ATOM   2365 C CE  . LYS A 1 400  ? 135.184 168.425 126.184 1.00 76.84  ? 400  LYS A CE  1 
ATOM   2366 N NZ  . LYS A 1 400  ? 135.486 167.233 125.346 1.00 79.52  ? 400  LYS A NZ  1 
ATOM   2367 N N   . GLY A 1 401  ? 140.836 171.463 128.430 1.00 69.92  ? 401  GLY A N   1 
ATOM   2368 C CA  . GLY A 1 401  ? 141.977 171.697 129.298 1.00 68.66  ? 401  GLY A CA  1 
ATOM   2369 C C   . GLY A 1 401  ? 141.815 172.918 130.182 1.00 72.26  ? 401  GLY A C   1 
ATOM   2370 O O   . GLY A 1 401  ? 142.458 173.025 131.228 1.00 73.60  ? 401  GLY A O   1 
ATOM   2371 N N   . ILE A 1 402  ? 140.963 173.858 129.776 1.00 55.00  ? 402  ILE A N   1 
ATOM   2372 C CA  . ILE A 1 402  ? 140.823 175.107 130.518 1.00 50.13  ? 402  ILE A CA  1 
ATOM   2373 C C   . ILE A 1 402  ? 139.797 174.966 131.634 1.00 58.84  ? 402  ILE A C   1 
ATOM   2374 O O   . ILE A 1 402  ? 140.114 175.126 132.818 1.00 65.28  ? 402  ILE A O   1 
ATOM   2375 C CB  . ILE A 1 402  ? 140.458 176.258 129.566 1.00 53.00  ? 402  ILE A CB  1 
ATOM   2376 C CG1 . ILE A 1 402  ? 141.595 176.499 128.578 1.00 56.17  ? 402  ILE A CG1 1 
ATOM   2377 C CG2 . ILE A 1 402  ? 140.169 177.514 130.355 1.00 63.50  ? 402  ILE A CG2 1 
ATOM   2378 C CD1 . ILE A 1 402  ? 141.328 177.622 127.614 1.00 57.06  ? 402  ILE A CD1 1 
ATOM   2379 N N   . LEU A 1 403  ? 138.552 174.672 131.276 1.00 58.58  ? 403  LEU A N   1 
ATOM   2380 C CA  . LEU A 1 403  ? 137.487 174.573 132.261 1.00 54.86  ? 403  LEU A CA  1 
ATOM   2381 C C   . LEU A 1 403  ? 137.514 173.213 132.946 1.00 57.47  ? 403  LEU A C   1 
ATOM   2382 O O   . LEU A 1 403  ? 137.939 172.210 132.369 1.00 63.27  ? 403  LEU A O   1 
ATOM   2383 C CB  . LEU A 1 403  ? 136.124 174.802 131.610 1.00 55.90  ? 403  LEU A CB  1 
ATOM   2384 C CG  . LEU A 1 403  ? 135.684 176.248 131.372 1.00 52.24  ? 403  LEU A CG  1 
ATOM   2385 C CD1 . LEU A 1 403  ? 136.546 176.933 130.335 1.00 58.33  ? 403  LEU A CD1 1 
ATOM   2386 C CD2 . LEU A 1 403  ? 134.234 176.289 130.948 1.00 62.56  ? 403  LEU A CD2 1 
ATOM   2387 N N   . GLY A 1 404  ? 137.040 173.186 134.187 1.00 59.94  ? 404  GLY A N   1 
ATOM   2388 C CA  . GLY A 1 404  ? 137.090 171.979 134.985 1.00 59.18  ? 404  GLY A CA  1 
ATOM   2389 C C   . GLY A 1 404  ? 135.807 171.180 134.939 1.00 62.93  ? 404  GLY A C   1 
ATOM   2390 O O   . GLY A 1 404  ? 135.511 170.535 133.931 1.00 74.55  ? 404  GLY A O   1 
ATOM   2391 N N   . ASN A 1 405  ? 135.029 171.219 136.020 1.00 59.55  ? 405  ASN A N   1 
ATOM   2392 C CA  . ASN A 1 405  ? 133.768 170.481 136.100 1.00 62.72  ? 405  ASN A CA  1 
ATOM   2393 C C   . ASN A 1 405  ? 132.739 171.173 135.203 1.00 69.00  ? 405  ASN A C   1 
ATOM   2394 O O   . ASN A 1 405  ? 131.738 171.738 135.647 1.00 71.46  ? 405  ASN A O   1 
ATOM   2395 C CB  . ASN A 1 405  ? 133.299 170.391 137.545 1.00 63.46  ? 405  ASN A CB  1 
ATOM   2396 C CG  . ASN A 1 405  ? 132.199 169.372 137.743 1.00 70.51  ? 405  ASN A CG  1 
ATOM   2397 O OD1 . ASN A 1 405  ? 131.262 169.284 136.952 1.00 73.23  ? 405  ASN A OD1 1 
ATOM   2398 N ND2 . ASN A 1 405  ? 132.308 168.589 138.810 1.00 70.04  ? 405  ASN A ND2 1 
ATOM   2399 N N   . MET A 1 406  ? 133.009 171.109 133.904 1.00 76.25  ? 406  MET A N   1 
ATOM   2400 C CA  . MET A 1 406  ? 132.228 171.853 132.928 1.00 74.29  ? 406  MET A CA  1 
ATOM   2401 C C   . MET A 1 406  ? 130.868 171.207 132.704 1.00 73.81  ? 406  MET A C   1 
ATOM   2402 O O   . MET A 1 406  ? 130.759 169.992 132.522 1.00 81.77  ? 406  MET A O   1 
ATOM   2403 C CB  . MET A 1 406  ? 132.992 171.939 131.608 1.00 75.13  ? 406  MET A CB  1 
ATOM   2404 C CG  . MET A 1 406  ? 132.217 172.586 130.481 1.00 81.44  ? 406  MET A CG  1 
ATOM   2405 S SD  . MET A 1 406  ? 133.218 172.802 128.999 1.00 94.57  ? 406  MET A SD  1 
ATOM   2406 C CE  . MET A 1 406  ? 133.754 171.119 128.707 1.00 78.25  ? 406  MET A CE  1 
ATOM   2407 N N   . VAL A 1 407  ? 129.827 172.034 132.722 1.00 73.18  ? 407  VAL A N   1 
ATOM   2408 C CA  . VAL A 1 407  ? 128.468 171.611 132.409 1.00 75.35  ? 407  VAL A CA  1 
ATOM   2409 C C   . VAL A 1 407  ? 127.943 172.508 131.301 1.00 81.61  ? 407  VAL A C   1 
ATOM   2410 O O   . VAL A 1 407  ? 127.975 173.737 131.425 1.00 85.59  ? 407  VAL A O   1 
ATOM   2411 C CB  . VAL A 1 407  ? 127.546 171.675 133.640 1.00 77.61  ? 407  VAL A CB  1 
ATOM   2412 C CG1 . VAL A 1 407  ? 126.119 171.339 133.248 1.00 80.43  ? 407  VAL A CG1 1 
ATOM   2413 C CG2 . VAL A 1 407  ? 128.040 170.730 134.720 1.00 78.79  ? 407  VAL A CG2 1 
ATOM   2414 N N   . TYR A 1 408  ? 127.458 171.899 130.221 1.00 94.20  ? 408  TYR A N   1 
ATOM   2415 C CA  . TYR A 1 408  ? 126.978 172.658 129.075 1.00 94.22  ? 408  TYR A CA  1 
ATOM   2416 C C   . TYR A 1 408  ? 125.596 172.186 128.645 1.00 95.59  ? 408  TYR A C   1 
ATOM   2417 O O   . TYR A 1 408  ? 124.974 171.365 129.326 1.00 96.35  ? 408  TYR A O   1 
ATOM   2418 C CB  . TYR A 1 408  ? 127.964 172.549 127.912 1.00 93.69  ? 408  TYR A CB  1 
ATOM   2419 C CG  . TYR A 1 408  ? 128.475 171.148 127.679 1.00 92.24  ? 408  TYR A CG  1 
ATOM   2420 C CD1 . TYR A 1 408  ? 127.764 170.250 126.900 1.00 94.21  ? 408  TYR A CD1 1 
ATOM   2421 C CD2 . TYR A 1 408  ? 129.669 170.723 128.242 1.00 92.99  ? 408  TYR A CD2 1 
ATOM   2422 C CE1 . TYR A 1 408  ? 128.227 168.969 126.687 1.00 97.50  ? 408  TYR A CE1 1 
ATOM   2423 C CE2 . TYR A 1 408  ? 130.141 169.445 128.035 1.00 93.54  ? 408  TYR A CE2 1 
ATOM   2424 C CZ  . TYR A 1 408  ? 129.417 168.572 127.257 1.00 97.04  ? 408  TYR A CZ  1 
ATOM   2425 O OH  . TYR A 1 408  ? 129.884 167.296 127.048 1.00 97.61  ? 408  TYR A OH  1 
ATOM   2426 N N   . GLU A 1 409  ? 125.107 172.699 127.519 1.00 106.53 ? 409  GLU A N   1 
ATOM   2427 C CA  . GLU A 1 409  ? 123.777 172.370 127.029 1.00 106.50 ? 409  GLU A CA  1 
ATOM   2428 C C   . GLU A 1 409  ? 123.768 171.672 125.679 1.00 111.57 ? 409  GLU A C   1 
ATOM   2429 O O   . GLU A 1 409  ? 122.938 170.783 125.472 1.00 113.02 ? 409  GLU A O   1 
ATOM   2430 C CB  . GLU A 1 409  ? 122.916 173.640 126.936 1.00 107.87 ? 409  GLU A CB  1 
ATOM   2431 C CG  . GLU A 1 409  ? 121.484 173.394 126.494 1.00 110.40 ? 409  GLU A CG  1 
ATOM   2432 C CD  . GLU A 1 409  ? 120.651 174.660 126.486 1.00 112.31 ? 409  GLU A CD  1 
ATOM   2433 O OE1 . GLU A 1 409  ? 121.130 175.690 127.003 1.00 112.70 ? 409  GLU A OE1 1 
ATOM   2434 O OE2 . GLU A 1 409  ? 119.517 174.625 125.963 1.00 112.66 ? 409  GLU A OE2 1 
ATOM   2435 N N   . LYS A 1 410  ? 124.666 172.041 124.762 1.00 117.39 ? 410  LYS A N   1 
ATOM   2436 C CA  . LYS A 1 410  ? 124.710 171.468 123.415 1.00 116.72 ? 410  LYS A CA  1 
ATOM   2437 C C   . LYS A 1 410  ? 123.375 171.665 122.696 1.00 116.18 ? 410  LYS A C   1 
ATOM   2438 O O   . LYS A 1 410  ? 122.681 170.710 122.343 1.00 115.38 ? 410  LYS A O   1 
ATOM   2439 C CB  . LYS A 1 410  ? 125.106 169.989 123.453 1.00 117.02 ? 410  LYS A CB  1 
ATOM   2440 C CG  . LYS A 1 410  ? 125.458 169.395 122.096 1.00 114.86 ? 410  LYS A CG  1 
ATOM   2441 C CD  . LYS A 1 410  ? 125.613 167.886 122.180 1.00 117.29 ? 410  LYS A CD  1 
ATOM   2442 C CE  . LYS A 1 410  ? 126.660 167.494 123.209 1.00 117.93 ? 410  LYS A CE  1 
ATOM   2443 N NZ  . LYS A 1 410  ? 126.772 166.016 123.351 1.00 117.72 ? 410  LYS A NZ  1 
ATOM   2444 N N   . SER A 1 411  ? 123.009 172.927 122.494 1.00 118.63 ? 411  SER A N   1 
ATOM   2445 C CA  . SER A 1 411  ? 121.763 173.283 121.837 1.00 119.41 ? 411  SER A CA  1 
ATOM   2446 C C   . SER A 1 411  ? 122.030 174.259 120.700 1.00 118.94 ? 411  SER A C   1 
ATOM   2447 O O   . SER A 1 411  ? 122.975 175.052 120.748 1.00 117.87 ? 411  SER A O   1 
ATOM   2448 C CB  . SER A 1 411  ? 120.769 173.898 122.828 1.00 116.12 ? 411  SER A CB  1 
ATOM   2449 O OG  . SER A 1 411  ? 121.311 175.054 123.440 1.00 116.06 ? 411  SER A OG  1 
ATOM   2450 N N   . GLY A 1 412  ? 121.182 174.194 119.677 1.00 122.02 ? 412  GLY A N   1 
ATOM   2451 C CA  . GLY A 1 412  ? 121.315 175.082 118.540 1.00 121.07 ? 412  GLY A CA  1 
ATOM   2452 C C   . GLY A 1 412  ? 122.561 174.871 117.714 1.00 123.62 ? 412  GLY A C   1 
ATOM   2453 O O   . GLY A 1 412  ? 123.204 175.849 117.319 1.00 124.06 ? 412  GLY A O   1 
ATOM   2454 N N   . SER A 1 413  ? 122.928 173.617 117.449 1.00 126.64 ? 413  SER A N   1 
ATOM   2455 C CA  . SER A 1 413  ? 124.108 173.212 116.689 1.00 126.52 ? 413  SER A CA  1 
ATOM   2456 C C   . SER A 1 413  ? 125.410 173.671 117.334 1.00 126.52 ? 413  SER A C   1 
ATOM   2457 O O   . SER A 1 413  ? 126.472 173.536 116.714 1.00 124.28 ? 413  SER A O   1 
ATOM   2458 C CB  . SER A 1 413  ? 124.073 173.709 115.235 1.00 125.21 ? 413  SER A CB  1 
ATOM   2459 O OG  . SER A 1 413  ? 124.192 175.120 115.169 1.00 124.67 ? 413  SER A OG  1 
ATOM   2460 N N   . LYS A 1 414  ? 125.367 174.206 118.552 1.00 118.71 ? 414  LYS A N   1 
ATOM   2461 C CA  . LYS A 1 414  ? 126.558 174.647 119.259 1.00 115.54 ? 414  LYS A CA  1 
ATOM   2462 C C   . LYS A 1 414  ? 126.442 174.251 120.723 1.00 114.10 ? 414  LYS A C   1 
ATOM   2463 O O   . LYS A 1 414  ? 125.405 173.765 121.179 1.00 114.82 ? 414  LYS A O   1 
ATOM   2464 C CB  . LYS A 1 414  ? 126.771 176.161 119.139 1.00 115.23 ? 414  LYS A CB  1 
ATOM   2465 C CG  . LYS A 1 414  ? 127.064 176.639 117.729 1.00 114.90 ? 414  LYS A CG  1 
ATOM   2466 C CD  . LYS A 1 414  ? 127.366 178.125 117.711 1.00 114.27 ? 414  LYS A CD  1 
ATOM   2467 C CE  . LYS A 1 414  ? 126.239 178.923 118.343 1.00 115.47 ? 414  LYS A CE  1 
ATOM   2468 N NZ  . LYS A 1 414  ? 124.950 178.717 117.631 1.00 115.71 ? 414  LYS A NZ  1 
ATOM   2469 N N   . TYR A 1 415  ? 127.532 174.457 121.452 1.00 107.28 ? 415  TYR A N   1 
ATOM   2470 C CA  . TYR A 1 415  ? 127.593 174.146 122.872 1.00 108.41 ? 415  TYR A CA  1 
ATOM   2471 C C   . TYR A 1 415  ? 127.544 175.443 123.671 1.00 109.20 ? 415  TYR A C   1 
ATOM   2472 O O   . TYR A 1 415  ? 128.334 176.361 123.425 1.00 109.64 ? 415  TYR A O   1 
ATOM   2473 C CB  . TYR A 1 415  ? 128.863 173.360 123.191 1.00 109.42 ? 415  TYR A CB  1 
ATOM   2474 C CG  . TYR A 1 415  ? 129.121 172.205 122.250 1.00 110.80 ? 415  TYR A CG  1 
ATOM   2475 C CD1 . TYR A 1 415  ? 129.818 172.393 121.064 1.00 108.90 ? 415  TYR A CD1 1 
ATOM   2476 C CD2 . TYR A 1 415  ? 128.670 170.928 122.548 1.00 109.55 ? 415  TYR A CD2 1 
ATOM   2477 C CE1 . TYR A 1 415  ? 130.055 171.344 120.202 1.00 109.81 ? 415  TYR A CE1 1 
ATOM   2478 C CE2 . TYR A 1 415  ? 128.904 169.873 121.693 1.00 109.06 ? 415  TYR A CE2 1 
ATOM   2479 C CZ  . TYR A 1 415  ? 129.596 170.086 120.522 1.00 111.63 ? 415  TYR A CZ  1 
ATOM   2480 O OH  . TYR A 1 415  ? 129.831 169.036 119.666 1.00 112.16 ? 415  TYR A OH  1 
ATOM   2481 N N   . ILE A 1 416  ? 126.620 175.516 124.621 1.00 100.73 ? 416  ILE A N   1 
ATOM   2482 C CA  . ILE A 1 416  ? 126.488 176.664 125.508 1.00 98.38  ? 416  ILE A CA  1 
ATOM   2483 C C   . ILE A 1 416  ? 126.953 176.226 126.889 1.00 100.47 ? 416  ILE A C   1 
ATOM   2484 O O   . ILE A 1 416  ? 126.325 175.374 127.526 1.00 98.49  ? 416  ILE A O   1 
ATOM   2485 C CB  . ILE A 1 416  ? 125.048 177.189 125.539 1.00 96.67  ? 416  ILE A CB  1 
ATOM   2486 C CG1 . ILE A 1 416  ? 124.585 177.546 124.125 1.00 99.20  ? 416  ILE A CG1 1 
ATOM   2487 C CG2 . ILE A 1 416  ? 124.945 178.390 126.460 1.00 97.33  ? 416  ILE A CG2 1 
ATOM   2488 C CD1 . ILE A 1 416  ? 123.156 178.031 124.055 1.00 100.43 ? 416  ILE A CD1 1 
ATOM   2489 N N   . ILE A 1 417  ? 128.053 176.808 127.356 1.00 90.62  ? 417  ILE A N   1 
ATOM   2490 C CA  . ILE A 1 417  ? 128.664 176.406 128.619 1.00 87.36  ? 417  ILE A CA  1 
ATOM   2491 C C   . ILE A 1 417  ? 128.012 177.202 129.743 1.00 87.20  ? 417  ILE A C   1 
ATOM   2492 O O   . ILE A 1 417  ? 128.053 178.433 129.749 1.00 86.75  ? 417  ILE A O   1 
ATOM   2493 C CB  . ILE A 1 417  ? 130.181 176.614 128.598 1.00 85.03  ? 417  ILE A CB  1 
ATOM   2494 C CG1 . ILE A 1 417  ? 130.756 176.164 127.257 1.00 80.47  ? 417  ILE A CG1 1 
ATOM   2495 C CG2 . ILE A 1 417  ? 130.828 175.837 129.718 1.00 83.20  ? 417  ILE A CG2 1 
ATOM   2496 C CD1 . ILE A 1 417  ? 132.251 176.290 127.170 1.00 85.70  ? 417  ILE A CD1 1 
ATOM   2497 N N   . LYS A 1 418  ? 127.401 176.496 130.696 1.00 88.47  ? 418  LYS A N   1 
ATOM   2498 C CA  . LYS A 1 418  ? 126.691 177.175 131.774 1.00 88.84  ? 418  LYS A CA  1 
ATOM   2499 C C   . LYS A 1 418  ? 127.577 177.360 133.000 1.00 88.77  ? 418  LYS A C   1 
ATOM   2500 O O   . LYS A 1 418  ? 127.697 178.472 133.525 1.00 91.71  ? 418  LYS A O   1 
ATOM   2501 C CB  . LYS A 1 418  ? 125.423 176.401 132.135 1.00 84.80  ? 418  LYS A CB  1 
ATOM   2502 C CG  . LYS A 1 418  ? 124.427 176.294 130.994 1.00 86.21  ? 418  LYS A CG  1 
ATOM   2503 C CD  . LYS A 1 418  ? 123.171 175.558 131.418 1.00 87.38  ? 418  LYS A CD  1 
ATOM   2504 C CE  . LYS A 1 418  ? 122.185 175.463 130.268 1.00 90.01  ? 418  LYS A CE  1 
ATOM   2505 N NZ  . LYS A 1 418  ? 121.828 176.807 129.738 1.00 87.44  ? 418  LYS A NZ  1 
ATOM   2506 N N   . SER A 1 419  ? 128.213 176.289 133.468 1.00 74.52  ? 419  SER A N   1 
ATOM   2507 C CA  . SER A 1 419  ? 128.904 176.334 134.748 1.00 73.79  ? 419  SER A CA  1 
ATOM   2508 C C   . SER A 1 419  ? 130.231 175.597 134.646 1.00 74.08  ? 419  SER A C   1 
ATOM   2509 O O   . SER A 1 419  ? 130.426 174.734 133.788 1.00 80.02  ? 419  SER A O   1 
ATOM   2510 C CB  . SER A 1 419  ? 128.043 175.735 135.864 1.00 71.49  ? 419  SER A CB  1 
ATOM   2511 O OG  . SER A 1 419  ? 127.783 174.365 135.626 1.00 72.93  ? 419  SER A OG  1 
ATOM   2512 N N   . ALA A 1 420  ? 131.147 175.928 135.550 1.00 56.72  ? 420  ALA A N   1 
ATOM   2513 C CA  . ALA A 1 420  ? 132.450 175.283 135.574 1.00 49.23  ? 420  ALA A CA  1 
ATOM   2514 C C   . ALA A 1 420  ? 133.059 175.577 136.925 1.00 54.58  ? 420  ALA A C   1 
ATOM   2515 O O   . ALA A 1 420  ? 133.210 176.738 137.292 1.00 72.10  ? 420  ALA A O   1 
ATOM   2516 C CB  . ALA A 1 420  ? 133.328 175.817 134.471 1.00 56.44  ? 420  ALA A CB  1 
ATOM   2517 N N   . ASN A 1 421  ? 133.407 174.546 137.680 1.00 51.41  ? 421  ASN A N   1 
ATOM   2518 C CA  . ASN A 1 421  ? 133.910 174.772 139.028 1.00 46.41  ? 421  ASN A CA  1 
ATOM   2519 C C   . ASN A 1 421  ? 135.427 174.758 139.092 1.00 47.82  ? 421  ASN A C   1 
ATOM   2520 O O   . ASN A 1 421  ? 135.998 174.453 140.136 1.00 62.81  ? 421  ASN A O   1 
ATOM   2521 C CB  . ASN A 1 421  ? 133.329 173.741 139.995 1.00 53.87  ? 421  ASN A CB  1 
ATOM   2522 C CG  . ASN A 1 421  ? 131.853 173.956 140.251 1.00 58.86  ? 421  ASN A CG  1 
ATOM   2523 O OD1 . ASN A 1 421  ? 131.456 174.393 141.331 1.00 59.46  ? 421  ASN A OD1 1 
ATOM   2524 N ND2 . ASN A 1 421  ? 131.029 173.660 139.253 1.00 61.10  ? 421  ASN A ND2 1 
ATOM   2525 N N   . ALA A 1 422  ? 136.083 175.090 137.987 1.00 39.94  ? 422  ALA A N   1 
ATOM   2526 C CA  . ALA A 1 422  ? 137.540 175.161 137.981 1.00 38.41  ? 422  ALA A CA  1 
ATOM   2527 C C   . ALA A 1 422  ? 138.051 175.796 136.707 1.00 41.70  ? 422  ALA A C   1 
ATOM   2528 O O   . ALA A 1 422  ? 137.453 175.633 135.648 1.00 55.45  ? 422  ALA A O   1 
ATOM   2529 C CB  . ALA A 1 422  ? 138.144 173.783 138.154 1.00 43.13  ? 422  ALA A CB  1 
ATOM   2530 N N   . ILE A 1 423  ? 139.162 176.511 136.802 1.00 43.18  ? 423  ILE A N   1 
ATOM   2531 C CA  . ILE A 1 423  ? 139.722 177.194 135.641 1.00 46.06  ? 423  ILE A CA  1 
ATOM   2532 C C   . ILE A 1 423  ? 141.238 177.080 135.674 1.00 50.87  ? 423  ILE A C   1 
ATOM   2533 O O   . ILE A 1 423  ? 141.878 177.381 136.683 1.00 53.59  ? 423  ILE A O   1 
ATOM   2534 C CB  . ILE A 1 423  ? 139.292 178.675 135.583 1.00 41.39  ? 423  ILE A CB  1 
ATOM   2535 C CG1 . ILE A 1 423  ? 137.822 178.789 135.191 1.00 45.51  ? 423  ILE A CG1 1 
ATOM   2536 C CG2 . ILE A 1 423  ? 140.155 179.446 134.609 1.00 45.54  ? 423  ILE A CG2 1 
ATOM   2537 C CD1 . ILE A 1 423  ? 137.362 180.207 134.979 1.00 45.90  ? 423  ILE A CD1 1 
ATOM   2538 N N   . MET A 1 424  ? 141.820 176.660 134.554 1.00 52.24  ? 424  MET A N   1 
ATOM   2539 C CA  . MET A 1 424  ? 143.262 176.496 134.454 1.00 45.78  ? 424  MET A CA  1 
ATOM   2540 C C   . MET A 1 424  ? 143.819 177.414 133.378 1.00 51.17  ? 424  MET A C   1 
ATOM   2541 O O   . MET A 1 424  ? 143.225 177.566 132.308 1.00 56.99  ? 424  MET A O   1 
ATOM   2542 C CB  . MET A 1 424  ? 143.641 175.045 134.149 1.00 47.97  ? 424  MET A CB  1 
ATOM   2543 C CG  . MET A 1 424  ? 145.119 174.841 133.876 1.00 47.72  ? 424  MET A CG  1 
ATOM   2544 S SD  . MET A 1 424  ? 145.662 173.148 134.145 1.00 64.31  ? 424  MET A SD  1 
ATOM   2545 C CE  . MET A 1 424  ? 145.520 173.037 135.923 1.00 53.24  ? 424  MET A CE  1 
ATOM   2546 N N   . THR A 1 425  ? 144.963 178.027 133.675 1.00 60.32  ? 425  THR A N   1 
ATOM   2547 C CA  . THR A 1 425  ? 145.669 178.904 132.754 1.00 59.92  ? 425  THR A CA  1 
ATOM   2548 C C   . THR A 1 425  ? 147.117 178.450 132.650 1.00 56.45  ? 425  THR A C   1 
ATOM   2549 O O   . THR A 1 425  ? 147.757 178.162 133.663 1.00 65.02  ? 425  THR A O   1 
ATOM   2550 C CB  . THR A 1 425  ? 145.610 180.359 133.226 1.00 61.33  ? 425  THR A CB  1 
ATOM   2551 O OG1 . THR A 1 425  ? 144.248 180.801 133.244 1.00 67.83  ? 425  THR A OG1 1 
ATOM   2552 C CG2 . THR A 1 425  ? 146.422 181.256 132.311 1.00 60.11  ? 425  THR A CG2 1 
ATOM   2553 N N   . VAL A 1 426  ? 147.631 178.382 131.427 1.00 52.53  ? 426  VAL A N   1 
ATOM   2554 C CA  . VAL A 1 426  ? 149.000 177.949 131.175 1.00 56.80  ? 426  VAL A CA  1 
ATOM   2555 C C   . VAL A 1 426  ? 149.761 179.116 130.568 1.00 65.18  ? 426  VAL A C   1 
ATOM   2556 O O   . VAL A 1 426  ? 149.375 179.634 129.514 1.00 74.11  ? 426  VAL A O   1 
ATOM   2557 C CB  . VAL A 1 426  ? 149.054 176.725 130.250 1.00 56.76  ? 426  VAL A CB  1 
ATOM   2558 C CG1 . VAL A 1 426  ? 150.492 176.301 130.029 1.00 58.68  ? 426  VAL A CG1 1 
ATOM   2559 C CG2 . VAL A 1 426  ? 148.244 175.588 130.835 1.00 56.12  ? 426  VAL A CG2 1 
ATOM   2560 N N   . ILE A 1 427  ? 150.836 179.524 131.228 1.00 56.64  ? 427  ILE A N   1 
ATOM   2561 C CA  . ILE A 1 427  ? 151.679 180.625 130.771 1.00 58.30  ? 427  ILE A CA  1 
ATOM   2562 C C   . ILE A 1 427  ? 152.985 180.032 130.255 1.00 60.54  ? 427  ILE A C   1 
ATOM   2563 O O   . ILE A 1 427  ? 153.725 179.422 131.042 1.00 68.25  ? 427  ILE A O   1 
ATOM   2564 C CB  . ILE A 1 427  ? 151.942 181.635 131.895 1.00 56.59  ? 427  ILE A CB  1 
ATOM   2565 C CG1 . ILE A 1 427  ? 150.621 182.105 132.500 1.00 57.53  ? 427  ILE A CG1 1 
ATOM   2566 C CG2 . ILE A 1 427  ? 152.730 182.818 131.370 1.00 58.11  ? 427  ILE A CG2 1 
ATOM   2567 C CD1 . ILE A 1 427  ? 150.783 183.124 133.597 1.00 60.26  ? 427  ILE A CD1 1 
ATOM   2568 N N   . PRO A 1 428  ? 153.287 180.149 128.967 1.00 56.76  ? 428  PRO A N   1 
ATOM   2569 C CA  . PRO A 1 428  ? 154.577 179.665 128.467 1.00 51.77  ? 428  PRO A CA  1 
ATOM   2570 C C   . PRO A 1 428  ? 155.665 180.721 128.545 1.00 64.23  ? 428  PRO A C   1 
ATOM   2571 O O   . PRO A 1 428  ? 155.493 181.847 128.072 1.00 77.83  ? 428  PRO A O   1 
ATOM   2572 C CB  . PRO A 1 428  ? 154.262 179.293 127.017 1.00 65.30  ? 428  PRO A CB  1 
ATOM   2573 C CG  . PRO A 1 428  ? 153.197 180.251 126.631 1.00 63.61  ? 428  PRO A CG  1 
ATOM   2574 C CD  . PRO A 1 428  ? 152.384 180.535 127.872 1.00 63.11  ? 428  PRO A CD  1 
ATOM   2575 N N   . LEU A 1 429  ? 156.790 180.360 129.144 1.00 59.21  ? 429  LEU A N   1 
ATOM   2576 C CA  . LEU A 1 429  ? 157.963 181.212 129.232 1.00 58.84  ? 429  LEU A CA  1 
ATOM   2577 C C   . LEU A 1 429  ? 159.083 180.587 128.419 1.00 55.53  ? 429  LEU A C   1 
ATOM   2578 O O   . LEU A 1 429  ? 159.241 179.362 128.406 1.00 63.27  ? 429  LEU A O   1 
ATOM   2579 C CB  . LEU A 1 429  ? 158.411 181.397 130.680 1.00 54.58  ? 429  LEU A CB  1 
ATOM   2580 C CG  . LEU A 1 429  ? 157.319 181.726 131.693 1.00 47.94  ? 429  LEU A CG  1 
ATOM   2581 C CD1 . LEU A 1 429  ? 157.932 181.983 133.050 1.00 50.46  ? 429  LEU A CD1 1 
ATOM   2582 C CD2 . LEU A 1 429  ? 156.512 182.919 131.237 1.00 54.67  ? 429  LEU A CD2 1 
ATOM   2583 N N   . LEU A 1 430  ? 159.849 181.432 127.734 1.00 59.27  ? 430  LEU A N   1 
ATOM   2584 C CA  . LEU A 1 430  ? 160.965 180.949 126.938 1.00 64.10  ? 430  LEU A CA  1 
ATOM   2585 C C   . LEU A 1 430  ? 161.953 180.196 127.817 1.00 67.94  ? 430  LEU A C   1 
ATOM   2586 O O   . LEU A 1 430  ? 162.361 180.680 128.875 1.00 70.53  ? 430  LEU A O   1 
ATOM   2587 C CB  . LEU A 1 430  ? 161.656 182.123 126.245 1.00 64.49  ? 430  LEU A CB  1 
ATOM   2588 C CG  . LEU A 1 430  ? 160.745 182.987 125.373 1.00 66.58  ? 430  LEU A CG  1 
ATOM   2589 C CD1 . LEU A 1 430  ? 161.464 184.243 124.920 1.00 65.00  ? 430  LEU A CD1 1 
ATOM   2590 C CD2 . LEU A 1 430  ? 160.250 182.197 124.176 1.00 68.91  ? 430  LEU A CD2 1 
ATOM   2591 N N   . ASN A 1 431  ? 162.334 178.998 127.373 1.00 73.34  ? 431  ASN A N   1 
ATOM   2592 C CA  . ASN A 1 431  ? 163.242 178.131 128.119 1.00 72.66  ? 431  ASN A CA  1 
ATOM   2593 C C   . ASN A 1 431  ? 164.508 177.933 127.289 1.00 73.24  ? 431  ASN A C   1 
ATOM   2594 O O   . ASN A 1 431  ? 164.643 176.969 126.535 1.00 80.48  ? 431  ASN A O   1 
ATOM   2595 C CB  . ASN A 1 431  ? 162.584 176.795 128.463 1.00 75.76  ? 431  ASN A CB  1 
ATOM   2596 C CG  . ASN A 1 431  ? 163.531 175.845 129.170 1.00 74.33  ? 431  ASN A CG  1 
ATOM   2597 O OD1 . ASN A 1 431  ? 164.492 176.269 129.809 1.00 74.81  ? 431  ASN A OD1 1 
ATOM   2598 N ND2 . ASN A 1 431  ? 163.264 174.549 129.057 1.00 72.94  ? 431  ASN A ND2 1 
ATOM   2599 N N   . SER A 1 432  ? 165.438 178.866 127.435 1.00 70.37  ? 432  SER A N   1 
ATOM   2600 C CA  . SER A 1 432  ? 166.751 178.785 126.824 1.00 69.41  ? 432  SER A CA  1 
ATOM   2601 C C   . SER A 1 432  ? 167.797 179.084 127.886 1.00 76.39  ? 432  SER A C   1 
ATOM   2602 O O   . SER A 1 432  ? 167.470 179.441 129.021 1.00 82.27  ? 432  SER A O   1 
ATOM   2603 C CB  . SER A 1 432  ? 166.887 179.762 125.653 1.00 70.42  ? 432  SER A CB  1 
ATOM   2604 O OG  . SER A 1 432  ? 168.192 179.721 125.107 1.00 79.63  ? 432  SER A OG  1 
ATOM   2605 N N   . HIS A 1 433  ? 169.066 178.918 127.517 1.00 89.08  ? 433  HIS A N   1 
ATOM   2606 C CA  . HIS A 1 433  ? 170.137 179.249 128.446 1.00 88.14  ? 433  HIS A CA  1 
ATOM   2607 C C   . HIS A 1 433  ? 170.086 180.722 128.827 1.00 91.11  ? 433  HIS A C   1 
ATOM   2608 O O   . HIS A 1 433  ? 170.008 181.069 130.010 1.00 94.21  ? 433  HIS A O   1 
ATOM   2609 C CB  . HIS A 1 433  ? 171.491 178.899 127.829 1.00 88.99  ? 433  HIS A CB  1 
ATOM   2610 C CG  . HIS A 1 433  ? 172.657 179.275 128.688 1.00 90.90  ? 433  HIS A CG  1 
ATOM   2611 N ND1 . HIS A 1 433  ? 172.853 178.750 129.946 1.00 90.41  ? 433  HIS A ND1 1 
ATOM   2612 C CD2 . HIS A 1 433  ? 173.685 180.128 128.470 1.00 89.59  ? 433  HIS A CD2 1 
ATOM   2613 C CE1 . HIS A 1 433  ? 173.954 179.261 130.467 1.00 90.99  ? 433  HIS A CE1 1 
ATOM   2614 N NE2 . HIS A 1 433  ? 174.478 180.100 129.591 1.00 92.49  ? 433  HIS A NE2 1 
ATOM   2615 N N   . THR A 1 434  ? 170.068 181.602 127.822 1.00 79.44  ? 434  THR A N   1 
ATOM   2616 C CA  . THR A 1 434  ? 170.098 183.036 128.085 1.00 77.14  ? 434  THR A CA  1 
ATOM   2617 C C   . THR A 1 434  ? 168.876 183.493 128.868 1.00 78.39  ? 434  THR A C   1 
ATOM   2618 O O   . THR A 1 434  ? 168.961 184.446 129.649 1.00 83.56  ? 434  THR A O   1 
ATOM   2619 C CB  . THR A 1 434  ? 170.197 183.809 126.772 1.00 75.36  ? 434  THR A CB  1 
ATOM   2620 O OG1 . THR A 1 434  ? 169.003 183.607 126.008 1.00 80.00  ? 434  THR A OG1 1 
ATOM   2621 C CG2 . THR A 1 434  ? 171.387 183.327 125.965 1.00 78.57  ? 434  THR A CG2 1 
ATOM   2622 N N   . TYR A 1 435  ? 167.738 182.833 128.679 1.00 75.14  ? 435  TYR A N   1 
ATOM   2623 C CA  . TYR A 1 435  ? 166.518 183.172 129.395 1.00 72.78  ? 435  TYR A CA  1 
ATOM   2624 C C   . TYR A 1 435  ? 166.315 182.338 130.649 1.00 76.88  ? 435  TYR A C   1 
ATOM   2625 O O   . TYR A 1 435  ? 165.263 182.453 131.284 1.00 80.84  ? 435  TYR A O   1 
ATOM   2626 C CB  . TYR A 1 435  ? 165.307 183.019 128.472 1.00 71.09  ? 435  TYR A CB  1 
ATOM   2627 C CG  . TYR A 1 435  ? 165.259 184.051 127.376 1.00 71.65  ? 435  TYR A CG  1 
ATOM   2628 C CD1 . TYR A 1 435  ? 165.480 185.390 127.652 1.00 72.65  ? 435  TYR A CD1 1 
ATOM   2629 C CD2 . TYR A 1 435  ? 165.009 183.686 126.064 1.00 74.33  ? 435  TYR A CD2 1 
ATOM   2630 C CE1 . TYR A 1 435  ? 165.441 186.339 126.654 1.00 75.37  ? 435  TYR A CE1 1 
ATOM   2631 C CE2 . TYR A 1 435  ? 164.972 184.626 125.058 1.00 75.88  ? 435  TYR A CE2 1 
ATOM   2632 C CZ  . TYR A 1 435  ? 165.187 185.951 125.358 1.00 79.33  ? 435  TYR A CZ  1 
ATOM   2633 O OH  . TYR A 1 435  ? 165.148 186.891 124.356 1.00 82.58  ? 435  TYR A OH  1 
ATOM   2634 N N   . GLU A 1 436  ? 167.283 181.500 131.018 1.00 85.35  ? 436  GLU A N   1 
ATOM   2635 C CA  . GLU A 1 436  ? 167.119 180.676 132.214 1.00 83.35  ? 436  GLU A CA  1 
ATOM   2636 C C   . GLU A 1 436  ? 166.940 181.491 133.489 1.00 84.67  ? 436  GLU A C   1 
ATOM   2637 O O   . GLU A 1 436  ? 165.980 181.223 134.231 1.00 91.85  ? 436  GLU A O   1 
ATOM   2638 C CB  . GLU A 1 436  ? 168.301 179.710 132.346 1.00 85.54  ? 436  GLU A CB  1 
ATOM   2639 C CG  . GLU A 1 436  ? 168.255 178.866 133.610 1.00 87.14  ? 436  GLU A CG  1 
ATOM   2640 C CD  . GLU A 1 436  ? 169.536 178.088 133.844 1.00 91.64  ? 436  GLU A CD  1 
ATOM   2641 O OE1 . GLU A 1 436  ? 170.506 178.296 133.086 1.00 92.83  ? 436  GLU A OE1 1 
ATOM   2642 O OE2 . GLU A 1 436  ? 169.573 177.270 134.787 1.00 90.31  ? 436  GLU A OE2 1 
ATOM   2643 N N   . PRO A 1 437  ? 167.792 182.480 133.814 1.00 77.79  ? 437  PRO A N   1 
ATOM   2644 C CA  . PRO A 1 437  ? 167.646 183.155 135.110 1.00 77.72  ? 437  PRO A CA  1 
ATOM   2645 C C   . PRO A 1 437  ? 166.427 184.057 135.178 1.00 78.62  ? 437  PRO A C   1 
ATOM   2646 O O   . PRO A 1 437  ? 165.693 184.038 136.171 1.00 82.47  ? 437  PRO A O   1 
ATOM   2647 C CB  . PRO A 1 437  ? 168.943 183.961 135.232 1.00 78.15  ? 437  PRO A CB  1 
ATOM   2648 C CG  . PRO A 1 437  ? 169.332 184.236 133.839 1.00 78.84  ? 437  PRO A CG  1 
ATOM   2649 C CD  . PRO A 1 437  ? 168.925 183.029 133.049 1.00 77.96  ? 437  PRO A CD  1 
ATOM   2650 N N   . TYR A 1 438  ? 166.201 184.843 134.124 1.00 75.93  ? 438  TYR A N   1 
ATOM   2651 C CA  . TYR A 1 438  ? 165.122 185.824 134.144 1.00 75.66  ? 438  TYR A CA  1 
ATOM   2652 C C   . TYR A 1 438  ? 163.780 185.153 134.394 1.00 75.22  ? 438  TYR A C   1 
ATOM   2653 O O   . TYR A 1 438  ? 163.021 185.567 135.278 1.00 82.17  ? 438  TYR A O   1 
ATOM   2654 C CB  . TYR A 1 438  ? 165.107 186.605 132.833 1.00 74.26  ? 438  TYR A CB  1 
ATOM   2655 C CG  . TYR A 1 438  ? 166.438 187.237 132.502 1.00 77.07  ? 438  TYR A CG  1 
ATOM   2656 C CD1 . TYR A 1 438  ? 166.787 188.475 133.017 1.00 78.75  ? 438  TYR A CD1 1 
ATOM   2657 C CD2 . TYR A 1 438  ? 167.348 186.591 131.682 1.00 77.66  ? 438  TYR A CD2 1 
ATOM   2658 C CE1 . TYR A 1 438  ? 168.002 189.052 132.721 1.00 77.81  ? 438  TYR A CE1 1 
ATOM   2659 C CE2 . TYR A 1 438  ? 168.564 187.161 131.381 1.00 78.33  ? 438  TYR A CE2 1 
ATOM   2660 C CZ  . TYR A 1 438  ? 168.886 188.391 131.902 1.00 79.97  ? 438  TYR A CZ  1 
ATOM   2661 O OH  . TYR A 1 438  ? 170.099 188.962 131.602 1.00 86.20  ? 438  TYR A OH  1 
ATOM   2662 N N   . ALA A 1 439  ? 163.487 184.089 133.646 1.00 62.26  ? 439  ALA A N   1 
ATOM   2663 C CA  . ALA A 1 439  ? 162.287 183.310 133.921 1.00 60.13  ? 439  ALA A CA  1 
ATOM   2664 C C   . ALA A 1 439  ? 162.300 182.795 135.352 1.00 59.74  ? 439  ALA A C   1 
ATOM   2665 O O   . ALA A 1 439  ? 161.314 182.940 136.085 1.00 73.21  ? 439  ALA A O   1 
ATOM   2666 C CB  . ALA A 1 439  ? 162.170 182.156 132.928 1.00 59.65  ? 439  ALA A CB  1 
ATOM   2667 N N   . LEU A 1 440  ? 163.433 182.232 135.783 1.00 55.69  ? 440  LEU A N   1 
ATOM   2668 C CA  . LEU A 1 440  ? 163.550 181.757 137.157 1.00 58.45  ? 440  LEU A CA  1 
ATOM   2669 C C   . LEU A 1 440  ? 163.256 182.862 138.156 1.00 63.83  ? 440  LEU A C   1 
ATOM   2670 O O   . LEU A 1 440  ? 162.793 182.586 139.268 1.00 69.10  ? 440  LEU A O   1 
ATOM   2671 C CB  . LEU A 1 440  ? 164.941 181.181 137.408 1.00 60.78  ? 440  LEU A CB  1 
ATOM   2672 C CG  . LEU A 1 440  ? 165.150 179.726 136.997 1.00 61.27  ? 440  LEU A CG  1 
ATOM   2673 C CD1 . LEU A 1 440  ? 166.543 179.258 137.382 1.00 65.22  ? 440  LEU A CD1 1 
ATOM   2674 C CD2 . LEU A 1 440  ? 164.091 178.845 137.632 1.00 61.70  ? 440  LEU A CD2 1 
ATOM   2675 N N   . ALA A 1 441  ? 163.518 184.115 137.788 1.00 63.46  ? 441  ALA A N   1 
ATOM   2676 C CA  . ALA A 1 441  ? 163.102 185.221 138.639 1.00 56.02  ? 441  ALA A CA  1 
ATOM   2677 C C   . ALA A 1 441  ? 161.594 185.409 138.566 1.00 59.84  ? 441  ALA A C   1 
ATOM   2678 O O   . ALA A 1 441  ? 160.897 185.345 139.587 1.00 68.92  ? 441  ALA A O   1 
ATOM   2679 C CB  . ALA A 1 441  ? 163.830 186.502 138.234 1.00 58.99  ? 441  ALA A CB  1 
ATOM   2680 N N   . TYR A 1 442  ? 161.068 185.588 137.352 1.00 57.30  ? 442  TYR A N   1 
ATOM   2681 C CA  . TYR A 1 442  ? 159.662 185.946 137.198 1.00 50.11  ? 442  TYR A CA  1 
ATOM   2682 C C   . TYR A 1 442  ? 158.762 184.897 137.828 1.00 59.46  ? 442  TYR A C   1 
ATOM   2683 O O   . TYR A 1 442  ? 157.832 185.230 138.574 1.00 71.19  ? 442  TYR A O   1 
ATOM   2684 C CB  . TYR A 1 442  ? 159.324 186.125 135.720 1.00 50.41  ? 442  TYR A CB  1 
ATOM   2685 C CG  . TYR A 1 442  ? 157.854 186.340 135.457 1.00 52.16  ? 442  TYR A CG  1 
ATOM   2686 C CD1 . TYR A 1 442  ? 157.285 187.597 135.584 1.00 61.04  ? 442  TYR A CD1 1 
ATOM   2687 C CD2 . TYR A 1 442  ? 157.034 185.288 135.078 1.00 55.78  ? 442  TYR A CD2 1 
ATOM   2688 C CE1 . TYR A 1 442  ? 155.942 187.800 135.344 1.00 61.79  ? 442  TYR A CE1 1 
ATOM   2689 C CE2 . TYR A 1 442  ? 155.691 185.481 134.838 1.00 55.22  ? 442  TYR A CE2 1 
ATOM   2690 C CZ  . TYR A 1 442  ? 155.151 186.739 134.971 1.00 58.48  ? 442  TYR A CZ  1 
ATOM   2691 O OH  . TYR A 1 442  ? 153.812 186.937 134.731 1.00 61.83  ? 442  TYR A OH  1 
ATOM   2692 N N   . GLU A 1 443  ? 159.053 183.619 137.571 1.00 57.48  ? 443  GLU A N   1 
ATOM   2693 C CA  . GLU A 1 443  ? 158.259 182.543 138.150 1.00 55.43  ? 443  GLU A CA  1 
ATOM   2694 C C   . GLU A 1 443  ? 158.120 182.721 139.652 1.00 56.43  ? 443  GLU A C   1 
ATOM   2695 O O   . GLU A 1 443  ? 157.012 182.636 140.197 1.00 69.68  ? 443  GLU A O   1 
ATOM   2696 C CB  . GLU A 1 443  ? 158.890 181.188 137.827 1.00 52.54  ? 443  GLU A CB  1 
ATOM   2697 C CG  . GLU A 1 443  ? 158.813 180.797 136.365 1.00 55.93  ? 443  GLU A CG  1 
ATOM   2698 C CD  . GLU A 1 443  ? 159.420 179.435 136.098 1.00 63.95  ? 443  GLU A CD  1 
ATOM   2699 O OE1 . GLU A 1 443  ? 160.046 178.872 137.019 1.00 67.55  ? 443  GLU A OE1 1 
ATOM   2700 O OE2 . GLU A 1 443  ? 159.271 178.923 134.969 1.00 62.23  ? 443  GLU A OE2 1 
ATOM   2701 N N   . LYS A 1 444  ? 159.230 183.021 140.334 1.00 50.57  ? 444  LYS A N   1 
ATOM   2702 C CA  . LYS A 1 444  ? 159.167 183.222 141.776 1.00 57.99  ? 444  LYS A CA  1 
ATOM   2703 C C   . LYS A 1 444  ? 158.116 184.263 142.125 1.00 55.93  ? 444  LYS A C   1 
ATOM   2704 O O   . LYS A 1 444  ? 157.189 183.993 142.899 1.00 61.37  ? 444  LYS A O   1 
ATOM   2705 C CB  . LYS A 1 444  ? 160.532 183.642 142.316 1.00 56.19  ? 444  LYS A CB  1 
ATOM   2706 C CG  . LYS A 1 444  ? 160.483 184.140 143.750 1.00 54.86  ? 444  LYS A CG  1 
ATOM   2707 C CD  . LYS A 1 444  ? 161.834 184.651 144.216 1.00 60.59  ? 444  LYS A CD  1 
ATOM   2708 C CE  . LYS A 1 444  ? 162.842 183.526 144.331 1.00 59.85  ? 444  LYS A CE  1 
ATOM   2709 N NZ  . LYS A 1 444  ? 164.163 184.020 144.804 1.00 61.99  ? 444  LYS A NZ  1 
ATOM   2710 N N   . LYS A 1 445  ? 158.201 185.437 141.498 1.00 51.61  ? 445  LYS A N   1 
ATOM   2711 C CA  . LYS A 1 445  ? 157.215 186.473 141.772 1.00 51.90  ? 445  LYS A CA  1 
ATOM   2712 C C   . LYS A 1 445  ? 155.820 185.987 141.426 1.00 49.81  ? 445  LYS A C   1 
ATOM   2713 O O   . LYS A 1 445  ? 154.870 186.216 142.186 1.00 56.19  ? 445  LYS A O   1 
ATOM   2714 C CB  . LYS A 1 445  ? 157.552 187.750 141.005 1.00 50.58  ? 445  LYS A CB  1 
ATOM   2715 C CG  . LYS A 1 445  ? 158.669 188.558 141.634 1.00 49.54  ? 445  LYS A CG  1 
ATOM   2716 C CD  . LYS A 1 445  ? 158.586 190.016 141.228 1.00 51.91  ? 445  LYS A CD  1 
ATOM   2717 C CE  . LYS A 1 445  ? 159.534 190.868 142.048 1.00 50.17  ? 445  LYS A CE  1 
ATOM   2718 N NZ  . LYS A 1 445  ? 159.425 192.306 141.688 1.00 55.75  ? 445  LYS A NZ  1 
ATOM   2719 N N   . LEU A 1 446  ? 155.686 185.270 140.307 1.00 45.04  ? 446  LEU A N   1 
ATOM   2720 C CA  . LEU A 1 446  ? 154.384 184.735 139.934 1.00 47.67  ? 446  LEU A CA  1 
ATOM   2721 C C   . LEU A 1 446  ? 153.806 183.892 141.058 1.00 51.55  ? 446  LEU A C   1 
ATOM   2722 O O   . LEU A 1 446  ? 152.620 184.017 141.389 1.00 56.86  ? 446  LEU A O   1 
ATOM   2723 C CB  . LEU A 1 446  ? 154.499 183.917 138.650 1.00 43.53  ? 446  LEU A CB  1 
ATOM   2724 C CG  . LEU A 1 446  ? 153.196 183.291 138.158 1.00 47.62  ? 446  LEU A CG  1 
ATOM   2725 C CD1 . LEU A 1 446  ? 152.146 184.362 137.946 1.00 48.78  ? 446  LEU A CD1 1 
ATOM   2726 C CD2 . LEU A 1 446  ? 153.429 182.509 136.880 1.00 46.83  ? 446  LEU A CD2 1 
ATOM   2727 N N   . ILE A 1 447  ? 154.639 183.064 141.690 1.00 53.25  ? 447  ILE A N   1 
ATOM   2728 C CA  . ILE A 1 447  ? 154.157 182.246 142.798 1.00 44.88  ? 447  ILE A CA  1 
ATOM   2729 C C   . ILE A 1 447  ? 153.642 183.137 143.918 1.00 54.09  ? 447  ILE A C   1 
ATOM   2730 O O   . ILE A 1 447  ? 152.539 182.936 144.440 1.00 63.38  ? 447  ILE A O   1 
ATOM   2731 C CB  . ILE A 1 447  ? 155.267 181.301 143.286 1.00 51.74  ? 447  ILE A CB  1 
ATOM   2732 C CG1 . ILE A 1 447  ? 155.569 180.251 142.221 1.00 51.67  ? 447  ILE A CG1 1 
ATOM   2733 C CG2 . ILE A 1 447  ? 154.869 180.644 144.586 1.00 55.27  ? 447  ILE A CG2 1 
ATOM   2734 C CD1 . ILE A 1 447  ? 156.640 179.272 142.622 1.00 52.16  ? 447  ILE A CD1 1 
ATOM   2735 N N   . ASP A 1 448  ? 154.412 184.169 144.269 1.00 60.82  ? 448  ASP A N   1 
ATOM   2736 C CA  . ASP A 1 448  ? 153.969 185.081 145.314 1.00 58.12  ? 448  ASP A CA  1 
ATOM   2737 C C   . ASP A 1 448  ? 152.696 185.805 144.912 1.00 59.96  ? 448  ASP A C   1 
ATOM   2738 O O   . ASP A 1 448  ? 151.933 186.247 145.777 1.00 68.23  ? 448  ASP A O   1 
ATOM   2739 C CB  . ASP A 1 448  ? 155.074 186.084 145.640 1.00 62.44  ? 448  ASP A CB  1 
ATOM   2740 C CG  . ASP A 1 448  ? 156.251 185.440 146.339 1.00 69.42  ? 448  ASP A CG  1 
ATOM   2741 O OD1 . ASP A 1 448  ? 156.820 184.478 145.783 1.00 72.31  ? 448  ASP A OD1 1 
ATOM   2742 O OD2 . ASP A 1 448  ? 156.611 185.898 147.443 1.00 70.49  ? 448  ASP A OD2 1 
ATOM   2743 N N   . TYR A 1 449  ? 152.445 185.933 143.610 1.00 51.23  ? 449  TYR A N   1 
ATOM   2744 C CA  . TYR A 1 449  ? 151.213 186.567 143.171 1.00 49.92  ? 449  TYR A CA  1 
ATOM   2745 C C   . TYR A 1 449  ? 150.017 185.641 143.310 1.00 52.59  ? 449  TYR A C   1 
ATOM   2746 O O   . TYR A 1 449  ? 148.889 186.116 143.466 1.00 55.42  ? 449  TYR A O   1 
ATOM   2747 C CB  . TYR A 1 449  ? 151.343 187.036 141.723 1.00 52.30  ? 449  TYR A CB  1 
ATOM   2748 C CG  . TYR A 1 449  ? 150.125 187.769 141.222 1.00 50.98  ? 449  TYR A CG  1 
ATOM   2749 C CD1 . TYR A 1 449  ? 149.889 189.085 141.583 1.00 58.97  ? 449  TYR A CD1 1 
ATOM   2750 C CD2 . TYR A 1 449  ? 149.210 187.146 140.391 1.00 48.01  ? 449  TYR A CD2 1 
ATOM   2751 C CE1 . TYR A 1 449  ? 148.778 189.758 141.131 1.00 59.86  ? 449  TYR A CE1 1 
ATOM   2752 C CE2 . TYR A 1 449  ? 148.097 187.813 139.935 1.00 47.98  ? 449  TYR A CE2 1 
ATOM   2753 C CZ  . TYR A 1 449  ? 147.886 189.117 140.306 1.00 54.52  ? 449  TYR A CZ  1 
ATOM   2754 O OH  . TYR A 1 449  ? 146.774 189.784 139.851 1.00 60.74  ? 449  TYR A OH  1 
ATOM   2755 N N   . VAL A 1 450  ? 150.235 184.331 143.263 1.00 59.39  ? 450  VAL A N   1 
ATOM   2756 C CA  . VAL A 1 450  ? 149.127 183.382 143.243 1.00 54.68  ? 450  VAL A CA  1 
ATOM   2757 C C   . VAL A 1 450  ? 148.813 182.862 144.637 1.00 54.61  ? 450  VAL A C   1 
ATOM   2758 O O   . VAL A 1 450  ? 147.656 182.854 145.062 1.00 57.17  ? 450  VAL A O   1 
ATOM   2759 C CB  . VAL A 1 450  ? 149.440 182.228 142.270 1.00 43.88  ? 450  VAL A CB  1 
ATOM   2760 C CG1 . VAL A 1 450  ? 148.323 181.212 142.287 1.00 51.81  ? 450  VAL A CG1 1 
ATOM   2761 C CG2 . VAL A 1 450  ? 149.645 182.766 140.870 1.00 43.54  ? 450  VAL A CG2 1 
ATOM   2762 N N   . ARG A 1 451  ? 149.838 182.425 145.372 1.00 63.60  ? 451  ARG A N   1 
ATOM   2763 C CA  . ARG A 1 451  ? 149.607 181.817 146.677 1.00 64.10  ? 451  ARG A CA  1 
ATOM   2764 C C   . ARG A 1 451  ? 149.052 182.813 147.685 1.00 69.19  ? 451  ARG A C   1 
ATOM   2765 O O   . ARG A 1 451  ? 148.528 182.408 148.729 1.00 79.12  ? 451  ARG A O   1 
ATOM   2766 C CB  . ARG A 1 451  ? 150.902 181.198 147.199 1.00 65.81  ? 451  ARG A CB  1 
ATOM   2767 C CG  . ARG A 1 451  ? 151.155 179.787 146.702 1.00 62.83  ? 451  ARG A CG  1 
ATOM   2768 C CD  . ARG A 1 451  ? 152.575 179.343 147.003 1.00 65.38  ? 451  ARG A CD  1 
ATOM   2769 N NE  . ARG A 1 451  ? 152.987 179.687 148.358 1.00 67.45  ? 451  ARG A NE  1 
ATOM   2770 C CZ  . ARG A 1 451  ? 152.817 178.906 149.415 1.00 69.67  ? 451  ARG A CZ  1 
ATOM   2771 N NH1 . ARG A 1 451  ? 152.236 177.722 149.313 1.00 67.36  ? 451  ARG A NH1 1 
ATOM   2772 N NH2 . ARG A 1 451  ? 153.240 179.323 150.604 1.00 68.81  ? 451  ARG A NH2 1 
ATOM   2773 N N   . PHE A 1 452  ? 149.160 184.109 147.408 1.00 65.59  ? 452  PHE A N   1 
ATOM   2774 C CA  . PHE A 1 452  ? 148.664 185.134 148.314 1.00 63.54  ? 452  PHE A CA  1 
ATOM   2775 C C   . PHE A 1 452  ? 147.430 185.854 147.787 1.00 68.50  ? 452  PHE A C   1 
ATOM   2776 O O   . PHE A 1 452  ? 147.020 186.858 148.376 1.00 71.17  ? 452  PHE A O   1 
ATOM   2777 C CB  . PHE A 1 452  ? 149.766 186.154 148.608 1.00 66.74  ? 452  PHE A CB  1 
ATOM   2778 C CG  . PHE A 1 452  ? 150.971 185.566 149.284 1.00 75.06  ? 452  PHE A CG  1 
ATOM   2779 C CD1 . PHE A 1 452  ? 150.868 184.396 150.018 1.00 72.05  ? 452  PHE A CD1 1 
ATOM   2780 C CD2 . PHE A 1 452  ? 152.205 186.183 149.184 1.00 71.59  ? 452  PHE A CD2 1 
ATOM   2781 C CE1 . PHE A 1 452  ? 151.973 183.854 150.639 1.00 72.51  ? 452  PHE A CE1 1 
ATOM   2782 C CE2 . PHE A 1 452  ? 153.314 185.645 149.804 1.00 70.82  ? 452  PHE A CE2 1 
ATOM   2783 C CZ  . PHE A 1 452  ? 153.198 184.479 150.532 1.00 73.30  ? 452  PHE A CZ  1 
ATOM   2784 N N   . TYR A 1 453  ? 146.834 185.375 146.700 1.00 60.86  ? 453  TYR A N   1 
ATOM   2785 C CA  . TYR A 1 453  ? 145.685 186.045 146.109 1.00 49.44  ? 453  TYR A CA  1 
ATOM   2786 C C   . TYR A 1 453  ? 144.395 185.563 146.757 1.00 53.59  ? 453  TYR A C   1 
ATOM   2787 O O   . TYR A 1 453  ? 144.202 184.365 146.973 1.00 64.34  ? 453  TYR A O   1 
ATOM   2788 C CB  . TYR A 1 453  ? 145.644 185.790 144.604 1.00 49.63  ? 453  TYR A CB  1 
ATOM   2789 C CG  . TYR A 1 453  ? 145.109 186.947 143.796 1.00 52.01  ? 453  TYR A CG  1 
ATOM   2790 C CD1 . TYR A 1 453  ? 145.945 187.971 143.387 1.00 57.29  ? 453  TYR A CD1 1 
ATOM   2791 C CD2 . TYR A 1 453  ? 143.773 187.013 143.440 1.00 56.02  ? 453  TYR A CD2 1 
ATOM   2792 C CE1 . TYR A 1 453  ? 145.466 189.030 142.649 1.00 56.72  ? 453  TYR A CE1 1 
ATOM   2793 C CE2 . TYR A 1 453  ? 143.285 188.068 142.700 1.00 54.83  ? 453  TYR A CE2 1 
ATOM   2794 C CZ  . TYR A 1 453  ? 144.136 189.073 142.308 1.00 59.20  ? 453  TYR A CZ  1 
ATOM   2795 O OH  . TYR A 1 453  ? 143.658 190.130 141.571 1.00 66.72  ? 453  TYR A OH  1 
ATOM   2796 N N   . ASN A 1 454  ? 143.508 186.506 147.067 1.00 65.58  ? 454  ASN A N   1 
ATOM   2797 C CA  . ASN A 1 454  ? 142.226 186.205 147.692 1.00 64.27  ? 454  ASN A CA  1 
ATOM   2798 C C   . ASN A 1 454  ? 141.120 186.957 146.970 1.00 66.21  ? 454  ASN A C   1 
ATOM   2799 O O   . ASN A 1 454  ? 141.257 188.153 146.696 1.00 71.91  ? 454  ASN A O   1 
ATOM   2800 C CB  . ASN A 1 454  ? 142.228 186.581 149.177 1.00 70.51  ? 454  ASN A CB  1 
ATOM   2801 C CG  . ASN A 1 454  ? 143.160 185.716 149.995 1.00 76.11  ? 454  ASN A CG  1 
ATOM   2802 O OD1 . ASN A 1 454  ? 143.380 184.549 149.677 1.00 79.44  ? 454  ASN A OD1 1 
ATOM   2803 N ND2 . ASN A 1 454  ? 143.712 186.284 151.060 1.00 71.36  ? 454  ASN A ND2 1 
ATOM   2804 N N   . LEU A 1 455  ? 140.026 186.256 146.670 1.00 72.03  ? 455  LEU A N   1 
ATOM   2805 C CA  . LEU A 1 455  ? 138.854 186.855 146.042 1.00 73.68  ? 455  LEU A CA  1 
ATOM   2806 C C   . LEU A 1 455  ? 137.568 186.352 146.685 1.00 73.98  ? 455  LEU A C   1 
ATOM   2807 O O   . LEU A 1 455  ? 136.558 186.170 146.003 1.00 76.15  ? 455  LEU A O   1 
ATOM   2808 C CB  . LEU A 1 455  ? 138.836 186.581 144.539 1.00 70.46  ? 455  LEU A CB  1 
ATOM   2809 C CG  . LEU A 1 455  ? 139.936 187.237 143.707 1.00 71.04  ? 455  LEU A CG  1 
ATOM   2810 C CD1 . LEU A 1 455  ? 139.814 186.820 142.256 1.00 72.71  ? 455  LEU A CD1 1 
ATOM   2811 C CD2 . LEU A 1 455  ? 139.879 188.749 143.834 1.00 68.40  ? 455  LEU A CD2 1 
ATOM   2812 N N   . ASP A 1 456  ? 137.588 186.130 147.999 1.00 83.06  ? 456  ASP A N   1 
ATOM   2813 C CA  . ASP A 1 456  ? 136.460 185.512 148.686 1.00 79.03  ? 456  ASP A CA  1 
ATOM   2814 C C   . ASP A 1 456  ? 135.243 186.421 148.789 1.00 84.01  ? 456  ASP A C   1 
ATOM   2815 O O   . ASP A 1 456  ? 134.141 185.917 149.037 1.00 87.26  ? 456  ASP A O   1 
ATOM   2816 C CB  . ASP A 1 456  ? 136.887 185.073 150.084 1.00 82.06  ? 456  ASP A CB  1 
ATOM   2817 C CG  . ASP A 1 456  ? 138.164 184.264 150.071 1.00 90.08  ? 456  ASP A CG  1 
ATOM   2818 O OD1 . ASP A 1 456  ? 138.746 184.098 148.980 1.00 87.29  ? 456  ASP A OD1 1 
ATOM   2819 O OD2 . ASP A 1 456  ? 138.587 183.797 151.148 1.00 93.31  ? 456  ASP A OD2 1 
ATOM   2820 N N   . ASP A 1 457  ? 135.411 187.732 148.609 1.00 96.41  ? 457  ASP A N   1 
ATOM   2821 C CA  . ASP A 1 457  ? 134.310 188.667 148.824 1.00 98.72  ? 457  ASP A CA  1 
ATOM   2822 C C   . ASP A 1 457  ? 133.135 188.359 147.904 1.00 98.36  ? 457  ASP A C   1 
ATOM   2823 O O   . ASP A 1 457  ? 131.981 188.299 148.343 1.00 94.17  ? 457  ASP A O   1 
ATOM   2824 C CB  . ASP A 1 457  ? 134.802 190.099 148.616 1.00 92.94  ? 457  ASP A CB  1 
ATOM   2825 C CG  . ASP A 1 457  ? 136.103 190.376 149.336 1.00 94.51  ? 457  ASP A CG  1 
ATOM   2826 O OD1 . ASP A 1 457  ? 136.699 189.420 149.874 1.00 94.86  ? 457  ASP A OD1 1 
ATOM   2827 O OD2 . ASP A 1 457  ? 136.530 191.548 149.367 1.00 97.35  ? 457  ASP A OD2 1 
ATOM   2828 N N   . ILE A 1 458  ? 133.413 188.161 146.615 1.00 88.27  ? 458  ILE A N   1 
ATOM   2829 C CA  . ILE A 1 458  ? 132.350 187.830 145.672 1.00 87.12  ? 458  ILE A CA  1 
ATOM   2830 C C   . ILE A 1 458  ? 131.828 186.423 145.928 1.00 90.29  ? 458  ILE A C   1 
ATOM   2831 O O   . ILE A 1 458  ? 130.641 186.138 145.729 1.00 93.14  ? 458  ILE A O   1 
ATOM   2832 C CB  . ILE A 1 458  ? 132.850 187.997 144.227 1.00 84.21  ? 458  ILE A CB  1 
ATOM   2833 C CG1 . ILE A 1 458  ? 134.098 187.147 143.998 1.00 84.31  ? 458  ILE A CG1 1 
ATOM   2834 C CG2 . ILE A 1 458  ? 133.152 189.452 143.941 1.00 85.34  ? 458  ILE A CG2 1 
ATOM   2835 C CD1 . ILE A 1 458  ? 134.519 187.065 142.556 1.00 87.45  ? 458  ILE A CD1 1 
ATOM   2836 N N   . ILE A 1 459  ? 132.706 185.520 146.365 1.00 82.49  ? 459  ILE A N   1 
ATOM   2837 C CA  . ILE A 1 459  ? 132.326 184.124 146.550 1.00 81.90  ? 459  ILE A CA  1 
ATOM   2838 C C   . ILE A 1 459  ? 131.339 183.968 147.698 1.00 89.37  ? 459  ILE A C   1 
ATOM   2839 O O   . ILE A 1 459  ? 130.479 183.078 147.668 1.00 96.56  ? 459  ILE A O   1 
ATOM   2840 C CB  . ILE A 1 459  ? 133.590 183.269 146.757 1.00 81.33  ? 459  ILE A CB  1 
ATOM   2841 C CG1 . ILE A 1 459  ? 134.461 183.324 145.505 1.00 84.90  ? 459  ILE A CG1 1 
ATOM   2842 C CG2 . ILE A 1 459  ? 133.236 181.833 147.072 1.00 83.65  ? 459  ILE A CG2 1 
ATOM   2843 C CD1 . ILE A 1 459  ? 133.775 182.801 144.270 1.00 83.69  ? 459  ILE A CD1 1 
ATOM   2844 N N   . GLN A 1 460  ? 131.429 184.830 148.714 1.00 94.00  ? 460  GLN A N   1 
ATOM   2845 C CA  . GLN A 1 460  ? 130.609 184.670 149.914 1.00 93.64  ? 460  GLN A CA  1 
ATOM   2846 C C   . GLN A 1 460  ? 129.119 184.599 149.587 1.00 92.32  ? 460  GLN A C   1 
ATOM   2847 O O   . GLN A 1 460  ? 128.361 183.881 150.248 1.00 94.18  ? 460  GLN A O   1 
ATOM   2848 C CB  . GLN A 1 460  ? 130.882 185.814 150.892 1.00 90.16  ? 460  GLN A CB  1 
ATOM   2849 C CG  . GLN A 1 460  ? 132.266 185.790 151.509 1.00 92.90  ? 460  GLN A CG  1 
ATOM   2850 C CD  . GLN A 1 460  ? 132.532 184.526 152.296 1.00 94.77  ? 460  GLN A CD  1 
ATOM   2851 O OE1 . GLN A 1 460  ? 131.637 183.986 152.945 1.00 95.27  ? 460  GLN A OE1 1 
ATOM   2852 N NE2 . GLN A 1 460  ? 133.767 184.042 152.240 1.00 93.22  ? 460  GLN A NE2 1 
ATOM   2853 N N   . ASP A 1 461  ? 128.680 185.341 148.571 1.00 96.07  ? 461  ASP A N   1 
ATOM   2854 C CA  . ASP A 1 461  ? 127.249 185.431 148.297 1.00 99.69  ? 461  ASP A CA  1 
ATOM   2855 C C   . ASP A 1 461  ? 126.731 184.250 147.485 1.00 103.38 ? 461  ASP A C   1 
ATOM   2856 O O   . ASP A 1 461  ? 125.581 183.836 147.668 1.00 105.93 ? 461  ASP A O   1 
ATOM   2857 C CB  . ASP A 1 461  ? 126.940 186.737 147.569 1.00 102.42 ? 461  ASP A CB  1 
ATOM   2858 C CG  . ASP A 1 461  ? 127.480 187.947 148.296 1.00 106.02 ? 461  ASP A CG  1 
ATOM   2859 O OD1 . ASP A 1 461  ? 128.219 187.763 149.286 1.00 106.14 ? 461  ASP A OD1 1 
ATOM   2860 O OD2 . ASP A 1 461  ? 127.165 189.081 147.880 1.00 106.65 ? 461  ASP A OD2 1 
ATOM   2861 N N   . GLU A 1 462  ? 127.547 183.700 146.592 1.00 96.48  ? 462  GLU A N   1 
ATOM   2862 C CA  . GLU A 1 462  ? 127.039 182.797 145.570 1.00 92.16  ? 462  GLU A CA  1 
ATOM   2863 C C   . GLU A 1 462  ? 126.747 181.406 146.129 1.00 93.66  ? 462  GLU A C   1 
ATOM   2864 O O   . GLU A 1 462  ? 127.278 180.990 147.162 1.00 93.91  ? 462  GLU A O   1 
ATOM   2865 C CB  . GLU A 1 462  ? 128.032 182.692 144.416 1.00 91.35  ? 462  GLU A CB  1 
ATOM   2866 C CG  . GLU A 1 462  ? 128.350 184.012 143.742 1.00 95.07  ? 462  GLU A CG  1 
ATOM   2867 C CD  . GLU A 1 462  ? 127.200 184.539 142.908 1.00 95.57  ? 462  GLU A CD  1 
ATOM   2868 O OE1 . GLU A 1 462  ? 126.232 183.785 142.676 1.00 92.17  ? 462  GLU A OE1 1 
ATOM   2869 O OE2 . GLU A 1 462  ? 127.266 185.710 142.480 1.00 97.24  ? 462  GLU A OE2 1 
ATOM   2870 N N   . GLU A 1 463  ? 125.886 180.684 145.414 1.00 99.50  ? 463  GLU A N   1 
ATOM   2871 C CA  . GLU A 1 463  ? 125.496 179.334 145.796 1.00 100.69 ? 463  GLU A CA  1 
ATOM   2872 C C   . GLU A 1 463  ? 126.608 178.335 145.493 1.00 99.78  ? 463  GLU A C   1 
ATOM   2873 O O   . GLU A 1 463  ? 127.309 178.439 144.484 1.00 102.14 ? 463  GLU A O   1 
ATOM   2874 C CB  . GLU A 1 463  ? 124.214 178.930 145.065 1.00 98.67  ? 463  GLU A CB  1 
ATOM   2875 C CG  . GLU A 1 463  ? 123.743 177.519 145.356 1.00 99.67  ? 463  GLU A CG  1 
ATOM   2876 C CD  . GLU A 1 463  ? 123.508 177.279 146.833 1.00 103.82 ? 463  GLU A CD  1 
ATOM   2877 O OE1 . GLU A 1 463  ? 122.991 178.190 147.512 1.00 105.21 ? 463  GLU A OE1 1 
ATOM   2878 O OE2 . GLU A 1 463  ? 123.847 176.179 147.317 1.00 103.12 ? 463  GLU A OE2 1 
ATOM   2879 N N   . THR A 1 464  ? 126.749 177.345 146.371 1.00 92.79  ? 464  THR A N   1 
ATOM   2880 C CA  . THR A 1 464  ? 127.830 176.376 146.303 1.00 92.51  ? 464  THR A CA  1 
ATOM   2881 C C   . THR A 1 464  ? 127.349 175.067 145.682 1.00 92.43  ? 464  THR A C   1 
ATOM   2882 O O   . THR A 1 464  ? 126.209 174.936 145.232 1.00 91.79  ? 464  THR A O   1 
ATOM   2883 C CB  . THR A 1 464  ? 128.404 176.120 147.695 1.00 91.66  ? 464  THR A CB  1 
ATOM   2884 O OG1 . THR A 1 464  ? 127.529 175.242 148.414 1.00 93.53  ? 464  THR A OG1 1 
ATOM   2885 C CG2 . THR A 1 464  ? 128.527 177.422 148.458 1.00 91.36  ? 464  THR A CG2 1 
ATOM   2886 N N   . ASN A 1 465  ? 128.247 174.084 145.660 1.00 91.84  ? 465  ASN A N   1 
ATOM   2887 C CA  . ASN A 1 465  ? 127.951 172.735 145.193 1.00 89.84  ? 465  ASN A CA  1 
ATOM   2888 C C   . ASN A 1 465  ? 127.893 171.716 146.320 1.00 93.15  ? 465  ASN A C   1 
ATOM   2889 O O   . ASN A 1 465  ? 126.977 170.891 146.355 1.00 95.89  ? 465  ASN A O   1 
ATOM   2890 C CB  . ASN A 1 465  ? 128.997 172.285 144.168 1.00 86.84  ? 465  ASN A CB  1 
ATOM   2891 C CG  . ASN A 1 465  ? 128.734 172.841 142.787 1.00 89.12  ? 465  ASN A CG  1 
ATOM   2892 O OD1 . ASN A 1 465  ? 127.870 173.698 142.606 1.00 90.07  ? 465  ASN A OD1 1 
ATOM   2893 N ND2 . ASN A 1 465  ? 129.479 172.355 141.801 1.00 90.28  ? 465  ASN A ND2 1 
ATOM   2894 N N   . ASP A 1 466  ? 128.848 171.758 147.245 1.00 101.80 ? 466  ASP A N   1 
ATOM   2895 C CA  . ASP A 1 466  ? 128.941 170.786 148.324 1.00 101.76 ? 466  ASP A CA  1 
ATOM   2896 C C   . ASP A 1 466  ? 128.155 171.206 149.558 1.00 103.44 ? 466  ASP A C   1 
ATOM   2897 O O   . ASP A 1 466  ? 128.240 170.533 150.590 1.00 104.16 ? 466  ASP A O   1 
ATOM   2898 C CB  . ASP A 1 466  ? 130.405 170.554 148.698 1.00 101.61 ? 466  ASP A CB  1 
ATOM   2899 C CG  . ASP A 1 466  ? 131.295 170.384 147.487 1.00 103.13 ? 466  ASP A CG  1 
ATOM   2900 O OD1 . ASP A 1 466  ? 130.786 170.505 146.353 1.00 101.62 ? 466  ASP A OD1 1 
ATOM   2901 O OD2 . ASP A 1 466  ? 132.505 170.132 147.668 1.00 104.36 ? 466  ASP A OD2 1 
ATOM   2902 N N   . ASP A 1 467  ? 127.411 172.308 149.479 1.00 113.38 ? 467  ASP A N   1 
ATOM   2903 C CA  . ASP A 1 467  ? 126.612 172.885 150.556 1.00 114.27 ? 467  ASP A CA  1 
ATOM   2904 C C   . ASP A 1 467  ? 127.464 173.402 151.707 1.00 113.43 ? 467  ASP A C   1 
ATOM   2905 O O   . ASP A 1 467  ? 126.911 173.780 152.745 1.00 114.03 ? 467  ASP A O   1 
ATOM   2906 C CB  . ASP A 1 467  ? 125.570 171.900 151.108 1.00 115.55 ? 467  ASP A CB  1 
ATOM   2907 C CG  . ASP A 1 467  ? 124.714 171.287 150.018 1.00 117.16 ? 467  ASP A CG  1 
ATOM   2908 O OD1 . ASP A 1 467  ? 124.587 171.907 148.941 1.00 115.81 ? 467  ASP A OD1 1 
ATOM   2909 O OD2 . ASP A 1 467  ? 124.167 170.186 150.238 1.00 115.61 ? 467  ASP A OD2 1 
ATOM   2910 N N   . ASN A 1 468  ? 128.786 173.428 151.565 1.00 103.67 ? 468  ASN A N   1 
ATOM   2911 C CA  . ASN A 1 468  ? 129.656 174.001 152.576 1.00 101.42 ? 468  ASN A CA  1 
ATOM   2912 C C   . ASN A 1 468  ? 129.743 175.516 152.404 1.00 100.31 ? 468  ASN A C   1 
ATOM   2913 O O   . ASN A 1 468  ? 129.064 176.118 151.569 1.00 102.20 ? 468  ASN A O   1 
ATOM   2914 C CB  . ASN A 1 468  ? 131.049 173.381 152.498 1.00 102.47 ? 468  ASN A CB  1 
ATOM   2915 C CG  . ASN A 1 468  ? 131.030 171.884 152.706 1.00 104.30 ? 468  ASN A CG  1 
ATOM   2916 O OD1 . ASN A 1 468  ? 129.969 171.261 152.722 1.00 103.79 ? 468  ASN A OD1 1 
ATOM   2917 N ND2 . ASN A 1 468  ? 132.209 171.293 152.862 1.00 103.03 ? 468  ASN A ND2 1 
ATOM   2918 N N   . ASP A 1 469  ? 130.592 176.132 153.216 1.00 94.27  ? 469  ASP A N   1 
ATOM   2919 C CA  . ASP A 1 469  ? 130.851 177.556 153.069 1.00 96.35  ? 469  ASP A CA  1 
ATOM   2920 C C   . ASP A 1 469  ? 131.515 177.815 151.720 1.00 98.17  ? 469  ASP A C   1 
ATOM   2921 O O   . ASP A 1 469  ? 132.480 177.122 151.369 1.00 99.57  ? 469  ASP A O   1 
ATOM   2922 C CB  . ASP A 1 469  ? 131.742 178.057 154.204 1.00 96.62  ? 469  ASP A CB  1 
ATOM   2923 C CG  . ASP A 1 469  ? 132.076 179.530 154.076 1.00 97.33  ? 469  ASP A CG  1 
ATOM   2924 O OD1 . ASP A 1 469  ? 131.152 180.362 154.182 1.00 96.96  ? 469  ASP A OD1 1 
ATOM   2925 O OD2 . ASP A 1 469  ? 133.265 179.854 153.872 1.00 96.83  ? 469  ASP A OD2 1 
ATOM   2926 N N   . PRO A 1 470  ? 131.024 178.812 150.959 1.00 84.46  ? 470  PRO A N   1 
ATOM   2927 C CA  . PRO A 1 470  ? 131.598 179.012 149.625 1.00 83.56  ? 470  PRO A CA  1 
ATOM   2928 C C   . PRO A 1 470  ? 133.095 179.277 149.676 1.00 82.11  ? 470  PRO A C   1 
ATOM   2929 O O   . PRO A 1 470  ? 133.572 179.846 150.654 1.00 82.33  ? 470  PRO A O   1 
ATOM   2930 C CB  . PRO A 1 470  ? 130.868 180.257 149.115 1.00 82.64  ? 470  PRO A CB  1 
ATOM   2931 C CG  . PRO A 1 470  ? 130.370 180.946 150.338 1.00 82.35  ? 470  PRO A CG  1 
ATOM   2932 C CD  . PRO A 1 470  ? 130.003 179.830 151.264 1.00 81.94  ? 470  PRO A CD  1 
ATOM   2933 N N   . PHE A 1 471  ? 133.825 178.877 148.638 1.00 68.61  ? 471  PHE A N   1 
ATOM   2934 C CA  . PHE A 1 471  ? 135.274 179.055 148.630 1.00 70.43  ? 471  PHE A CA  1 
ATOM   2935 C C   . PHE A 1 471  ? 135.865 179.224 147.244 1.00 66.04  ? 471  PHE A C   1 
ATOM   2936 O O   . PHE A 1 471  ? 135.247 178.842 146.254 1.00 68.44  ? 471  PHE A O   1 
ATOM   2937 C CB  . PHE A 1 471  ? 135.955 177.856 149.290 1.00 72.95  ? 471  PHE A CB  1 
ATOM   2938 C CG  . PHE A 1 471  ? 136.012 176.634 148.419 1.00 69.32  ? 471  PHE A CG  1 
ATOM   2939 C CD1 . PHE A 1 471  ? 136.988 176.504 147.444 1.00 59.34  ? 471  PHE A CD1 1 
ATOM   2940 C CD2 . PHE A 1 471  ? 135.098 175.611 148.582 1.00 71.37  ? 471  PHE A CD2 1 
ATOM   2941 C CE1 . PHE A 1 471  ? 137.041 175.384 146.640 1.00 60.71  ? 471  PHE A CE1 1 
ATOM   2942 C CE2 . PHE A 1 471  ? 135.150 174.485 147.785 1.00 72.14  ? 471  PHE A CE2 1 
ATOM   2943 C CZ  . PHE A 1 471  ? 136.122 174.371 146.813 1.00 68.34  ? 471  PHE A CZ  1 
ATOM   2944 N N   . ILE A 1 472  ? 137.062 179.792 147.166 1.00 63.50  ? 472  ILE A N   1 
ATOM   2945 C CA  . ILE A 1 472  ? 137.751 179.911 145.886 1.00 59.31  ? 472  ILE A CA  1 
ATOM   2946 C C   . ILE A 1 472  ? 139.236 179.866 146.182 1.00 59.82  ? 472  ILE A C   1 
ATOM   2947 O O   . ILE A 1 472  ? 139.751 180.703 146.917 1.00 68.22  ? 472  ILE A O   1 
ATOM   2948 C CB  . ILE A 1 472  ? 137.387 181.198 145.132 1.00 52.45  ? 472  ILE A CB  1 
ATOM   2949 C CG1 . ILE A 1 472  ? 138.180 181.287 143.829 1.00 51.67  ? 472  ILE A CG1 1 
ATOM   2950 C CG2 . ILE A 1 472  ? 137.642 182.424 145.995 1.00 64.63  ? 472  ILE A CG2 1 
ATOM   2951 C CD1 . ILE A 1 472  ? 137.887 182.533 143.025 1.00 53.93  ? 472  ILE A CD1 1 
ATOM   2952 N N   . ARG A 1 473  ? 139.934 178.881 145.638 1.00 46.21  ? 473  ARG A N   1 
ATOM   2953 C CA  . ARG A 1 473  ? 141.345 178.737 145.957 1.00 44.40  ? 473  ARG A CA  1 
ATOM   2954 C C   . ARG A 1 473  ? 142.208 178.787 144.715 1.00 57.81  ? 473  ARG A C   1 
ATOM   2955 O O   . ARG A 1 473  ? 141.869 178.187 143.699 1.00 65.20  ? 473  ARG A O   1 
ATOM   2956 C CB  . ARG A 1 473  ? 141.578 177.432 146.710 1.00 49.22  ? 473  ARG A CB  1 
ATOM   2957 C CG  . ARG A 1 473  ? 140.913 177.385 148.074 1.00 55.46  ? 473  ARG A CG  1 
ATOM   2958 C CD  . ARG A 1 473  ? 141.267 176.108 148.816 1.00 63.61  ? 473  ARG A CD  1 
ATOM   2959 N NE  . ARG A 1 473  ? 140.747 174.924 148.141 1.00 62.48  ? 473  ARG A NE  1 
ATOM   2960 C CZ  . ARG A 1 473  ? 139.572 174.367 148.414 1.00 59.11  ? 473  ARG A CZ  1 
ATOM   2961 N NH1 . ARG A 1 473  ? 138.792 174.883 149.354 1.00 59.79  ? 473  ARG A NH1 1 
ATOM   2962 N NH2 . ARG A 1 473  ? 139.178 173.291 147.748 1.00 62.10  ? 473  ARG A NH2 1 
ATOM   2963 N N   . PHE A 1 474  ? 143.321 179.504 144.792 1.00 49.09  ? 474  PHE A N   1 
ATOM   2964 C CA  . PHE A 1 474  ? 144.217 179.615 143.655 1.00 38.06  ? 474  PHE A CA  1 
ATOM   2965 C C   . PHE A 1 474  ? 145.427 178.727 143.869 1.00 38.39  ? 474  PHE A C   1 
ATOM   2966 O O   . PHE A 1 474  ? 145.993 178.705 144.957 1.00 58.60  ? 474  PHE A O   1 
ATOM   2967 C CB  . PHE A 1 474  ? 144.659 181.062 143.469 1.00 37.62  ? 474  PHE A CB  1 
ATOM   2968 C CG  . PHE A 1 474  ? 143.526 182.043 143.401 1.00 39.13  ? 474  PHE A CG  1 
ATOM   2969 C CD1 . PHE A 1 474  ? 142.929 182.512 144.559 1.00 45.72  ? 474  PHE A CD1 1 
ATOM   2970 C CD2 . PHE A 1 474  ? 143.069 182.511 142.183 1.00 36.42  ? 474  PHE A CD2 1 
ATOM   2971 C CE1 . PHE A 1 474  ? 141.890 183.419 144.502 1.00 43.96  ? 474  PHE A CE1 1 
ATOM   2972 C CE2 . PHE A 1 474  ? 142.031 183.418 142.118 1.00 38.87  ? 474  PHE A CE2 1 
ATOM   2973 C CZ  . PHE A 1 474  ? 141.440 183.873 143.279 1.00 36.52  ? 474  PHE A CZ  1 
ATOM   2974 N N   . HIS A 1 475  ? 145.826 177.992 142.841 1.00 29.35  ? 475  HIS A N   1 
ATOM   2975 C CA  . HIS A 1 475  ? 146.976 177.108 142.951 1.00 41.94  ? 475  HIS A CA  1 
ATOM   2976 C C   . HIS A 1 475  ? 147.961 177.381 141.828 1.00 48.98  ? 475  HIS A C   1 
ATOM   2977 O O   . HIS A 1 475  ? 147.564 177.807 140.748 1.00 48.40  ? 475  HIS A O   1 
ATOM   2978 C CB  . HIS A 1 475  ? 146.524 175.654 142.914 1.00 41.83  ? 475  HIS A CB  1 
ATOM   2979 C CG  . HIS A 1 475  ? 145.664 175.261 144.073 1.00 43.88  ? 475  HIS A CG  1 
ATOM   2980 N ND1 . HIS A 1 475  ? 146.043 174.304 144.989 1.00 52.45  ? 475  HIS A ND1 1 
ATOM   2981 C CD2 . HIS A 1 475  ? 144.449 175.704 144.472 1.00 42.07  ? 475  HIS A CD2 1 
ATOM   2982 C CE1 . HIS A 1 475  ? 145.095 174.170 145.899 1.00 46.58  ? 475  HIS A CE1 1 
ATOM   2983 N NE2 . HIS A 1 475  ? 144.117 175.009 145.609 1.00 45.42  ? 475  HIS A NE2 1 
ATOM   2984 N N   . VAL A 1 476  ? 149.244 177.139 142.074 1.00 52.84  ? 476  VAL A N   1 
ATOM   2985 C CA  . VAL A 1 476  ? 150.260 177.415 141.063 1.00 40.18  ? 476  VAL A CA  1 
ATOM   2986 C C   . VAL A 1 476  ? 151.334 176.343 141.002 1.00 42.49  ? 476  VAL A C   1 
ATOM   2987 O O   . VAL A 1 476  ? 151.700 175.773 142.024 1.00 52.09  ? 476  VAL A O   1 
ATOM   2988 C CB  . VAL A 1 476  ? 150.928 178.777 141.309 1.00 43.23  ? 476  VAL A CB  1 
ATOM   2989 C CG1 . VAL A 1 476  ? 151.631 178.791 142.656 1.00 52.42  ? 476  VAL A CG1 1 
ATOM   2990 C CG2 . VAL A 1 476  ? 151.897 179.113 140.186 1.00 44.95  ? 476  VAL A CG2 1 
ATOM   2991 N N   . PHE A 1 477  ? 151.835 176.059 139.807 1.00 41.75  ? 477  PHE A N   1 
ATOM   2992 C CA  . PHE A 1 477  ? 152.890 175.072 139.637 1.00 41.79  ? 477  PHE A CA  1 
ATOM   2993 C C   . PHE A 1 477  ? 153.823 175.507 138.520 1.00 48.89  ? 477  PHE A C   1 
ATOM   2994 O O   . PHE A 1 477  ? 153.377 175.845 137.422 1.00 57.52  ? 477  PHE A O   1 
ATOM   2995 C CB  . PHE A 1 477  ? 152.323 173.695 139.323 1.00 43.87  ? 477  PHE A CB  1 
ATOM   2996 C CG  . PHE A 1 477  ? 153.362 172.619 139.249 1.00 47.17  ? 477  PHE A CG  1 
ATOM   2997 C CD1 . PHE A 1 477  ? 153.849 172.031 140.400 1.00 51.60  ? 477  PHE A CD1 1 
ATOM   2998 C CD2 . PHE A 1 477  ? 153.848 172.192 138.029 1.00 47.62  ? 477  PHE A CD2 1 
ATOM   2999 C CE1 . PHE A 1 477  ? 154.804 171.039 140.336 1.00 50.33  ? 477  PHE A CE1 1 
ATOM   3000 C CE2 . PHE A 1 477  ? 154.802 171.201 137.959 1.00 48.10  ? 477  PHE A CE2 1 
ATOM   3001 C CZ  . PHE A 1 477  ? 155.280 170.623 139.113 1.00 48.67  ? 477  PHE A CZ  1 
ATOM   3002 N N   . THR A 1 478  ? 155.121 175.486 138.803 1.00 54.33  ? 478  THR A N   1 
ATOM   3003 C CA  . THR A 1 478  ? 156.123 175.870 137.822 1.00 47.49  ? 478  THR A CA  1 
ATOM   3004 C C   . THR A 1 478  ? 157.259 174.863 137.868 1.00 55.99  ? 478  THR A C   1 
ATOM   3005 O O   . THR A 1 478  ? 157.324 174.013 138.758 1.00 67.81  ? 478  THR A O   1 
ATOM   3006 C CB  . THR A 1 478  ? 156.660 177.281 138.078 1.00 52.07  ? 478  THR A CB  1 
ATOM   3007 O OG1 . THR A 1 478  ? 157.277 177.327 139.369 1.00 61.37  ? 478  THR A OG1 1 
ATOM   3008 C CG2 . THR A 1 478  ? 155.539 178.302 138.029 1.00 53.60  ? 478  THR A CG2 1 
ATOM   3009 N N   . ASP A 1 479  ? 158.160 174.964 136.888 1.00 59.33  ? 479  ASP A N   1 
ATOM   3010 C CA  . ASP A 1 479  ? 159.361 174.138 136.918 1.00 65.89  ? 479  ASP A CA  1 
ATOM   3011 C C   . ASP A 1 479  ? 160.221 174.461 138.130 1.00 70.59  ? 479  ASP A C   1 
ATOM   3012 O O   . ASP A 1 479  ? 161.000 173.617 138.586 1.00 72.39  ? 479  ASP A O   1 
ATOM   3013 C CB  . ASP A 1 479  ? 160.161 174.326 135.630 1.00 65.35  ? 479  ASP A CB  1 
ATOM   3014 C CG  . ASP A 1 479  ? 159.399 173.874 134.402 1.00 70.50  ? 479  ASP A CG  1 
ATOM   3015 O OD1 . ASP A 1 479  ? 158.211 173.517 134.539 1.00 71.32  ? 479  ASP A OD1 1 
ATOM   3016 O OD2 . ASP A 1 479  ? 159.987 173.873 133.301 1.00 71.02  ? 479  ASP A OD2 1 
ATOM   3017 N N   . ARG A 1 480  ? 160.092 175.676 138.662 1.00 68.14  ? 480  ARG A N   1 
ATOM   3018 C CA  . ARG A 1 480  ? 160.804 176.068 139.869 1.00 59.34  ? 480  ARG A CA  1 
ATOM   3019 C C   . ARG A 1 480  ? 160.196 175.456 141.123 1.00 61.66  ? 480  ARG A C   1 
ATOM   3020 O O   . ARG A 1 480  ? 160.875 175.383 142.152 1.00 65.03  ? 480  ARG A O   1 
ATOM   3021 C CB  . ARG A 1 480  ? 160.802 177.592 139.982 1.00 59.35  ? 480  ARG A CB  1 
ATOM   3022 C CG  . ARG A 1 480  ? 161.802 178.171 140.958 1.00 65.33  ? 480  ARG A CG  1 
ATOM   3023 C CD  . ARG A 1 480  ? 161.602 179.669 141.098 1.00 60.93  ? 480  ARG A CD  1 
ATOM   3024 N NE  . ARG A 1 480  ? 162.851 180.356 141.396 1.00 59.67  ? 480  ARG A NE  1 
ATOM   3025 C CZ  . ARG A 1 480  ? 163.361 180.486 142.611 1.00 65.15  ? 480  ARG A CZ  1 
ATOM   3026 N NH1 . ARG A 1 480  ? 162.750 179.988 143.673 1.00 64.19  ? 480  ARG A NH1 1 
ATOM   3027 N NH2 . ARG A 1 480  ? 164.515 181.128 142.766 1.00 74.78  ? 480  ARG A NH2 1 
ATOM   3028 N N   . SER A 1 481  ? 158.936 175.019 141.054 1.00 61.77  ? 481  SER A N   1 
ATOM   3029 C CA  . SER A 1 481  ? 158.204 174.633 142.257 1.00 57.77  ? 481  SER A CA  1 
ATOM   3030 C C   . SER A 1 481  ? 158.799 173.397 142.914 1.00 60.93  ? 481  SER A C   1 
ATOM   3031 O O   . SER A 1 481  ? 158.909 173.338 144.143 1.00 68.81  ? 481  SER A O   1 
ATOM   3032 C CB  . SER A 1 481  ? 156.733 174.398 141.919 1.00 57.04  ? 481  SER A CB  1 
ATOM   3033 O OG  . SER A 1 481  ? 156.158 175.552 141.336 1.00 58.36  ? 481  SER A OG  1 
ATOM   3034 N N   . LEU A 1 482  ? 159.167 172.391 142.122 1.00 63.33  ? 482  LEU A N   1 
ATOM   3035 C CA  . LEU A 1 482  ? 159.706 171.168 142.705 1.00 66.10  ? 482  LEU A CA  1 
ATOM   3036 C C   . LEU A 1 482  ? 161.032 171.432 143.407 1.00 69.69  ? 482  LEU A C   1 
ATOM   3037 O O   . LEU A 1 482  ? 161.261 170.950 144.523 1.00 73.46  ? 482  LEU A O   1 
ATOM   3038 C CB  . LEU A 1 482  ? 159.866 170.101 141.624 1.00 70.79  ? 482  LEU A CB  1 
ATOM   3039 C CG  . LEU A 1 482  ? 159.496 168.681 142.046 1.00 69.76  ? 482  LEU A CG  1 
ATOM   3040 C CD1 . LEU A 1 482  ? 158.100 168.658 142.633 1.00 68.12  ? 482  LEU A CD1 1 
ATOM   3041 C CD2 . LEU A 1 482  ? 159.590 167.734 140.865 1.00 68.39  ? 482  LEU A CD2 1 
ATOM   3042 N N   . GLU A 1 483  ? 161.910 172.212 142.775 1.00 73.55  ? 483  GLU A N   1 
ATOM   3043 C CA  . GLU A 1 483  ? 163.177 172.569 143.404 1.00 71.01  ? 483  GLU A CA  1 
ATOM   3044 C C   . GLU A 1 483  ? 162.950 173.386 144.668 1.00 70.94  ? 483  GLU A C   1 
ATOM   3045 O O   . GLU A 1 483  ? 163.626 173.182 145.683 1.00 75.36  ? 483  GLU A O   1 
ATOM   3046 C CB  . GLU A 1 483  ? 164.053 173.338 142.416 1.00 73.99  ? 483  GLU A CB  1 
ATOM   3047 C CG  . GLU A 1 483  ? 164.907 172.460 141.521 1.00 77.09  ? 483  GLU A CG  1 
ATOM   3048 C CD  . GLU A 1 483  ? 166.186 172.008 142.198 1.00 79.64  ? 483  GLU A CD  1 
ATOM   3049 O OE1 . GLU A 1 483  ? 166.385 172.344 143.385 1.00 80.00  ? 483  GLU A OE1 1 
ATOM   3050 O OE2 . GLU A 1 483  ? 166.996 171.321 141.542 1.00 79.30  ? 483  GLU A OE2 1 
ATOM   3051 N N   . ASP A 1 484  ? 162.001 174.325 144.626 1.00 63.08  ? 484  ASP A N   1 
ATOM   3052 C CA  . ASP A 1 484  ? 161.723 175.136 145.805 1.00 65.17  ? 484  ASP A CA  1 
ATOM   3053 C C   . ASP A 1 484  ? 161.208 174.280 146.953 1.00 68.47  ? 484  ASP A C   1 
ATOM   3054 O O   . ASP A 1 484  ? 161.600 174.476 148.109 1.00 77.38  ? 484  ASP A O   1 
ATOM   3055 C CB  . ASP A 1 484  ? 160.720 176.235 145.461 1.00 67.64  ? 484  ASP A CB  1 
ATOM   3056 C CG  . ASP A 1 484  ? 161.283 177.251 144.491 1.00 72.89  ? 484  ASP A CG  1 
ATOM   3057 O OD1 . ASP A 1 484  ? 162.452 177.095 144.081 1.00 74.37  ? 484  ASP A OD1 1 
ATOM   3058 O OD2 . ASP A 1 484  ? 160.560 178.205 144.138 1.00 75.08  ? 484  ASP A OD2 1 
ATOM   3059 N N   . GLU A 1 485  ? 160.330 173.323 146.655 1.00 66.53  ? 485  GLU A N   1 
ATOM   3060 C CA  . GLU A 1 485  ? 159.808 172.456 147.704 1.00 66.75  ? 485  GLU A CA  1 
ATOM   3061 C C   . GLU A 1 485  ? 160.893 171.550 148.265 1.00 68.63  ? 485  GLU A C   1 
ATOM   3062 O O   . GLU A 1 485  ? 160.934 171.304 149.475 1.00 74.37  ? 485  GLU A O   1 
ATOM   3063 C CB  . GLU A 1 485  ? 158.633 171.639 147.176 1.00 65.83  ? 485  GLU A CB  1 
ATOM   3064 C CG  . GLU A 1 485  ? 157.350 172.439 147.065 1.00 72.33  ? 485  GLU A CG  1 
ATOM   3065 C CD  . GLU A 1 485  ? 156.900 173.002 148.399 1.00 74.37  ? 485  GLU A CD  1 
ATOM   3066 O OE1 . GLU A 1 485  ? 157.049 172.302 149.422 1.00 75.75  ? 485  GLU A OE1 1 
ATOM   3067 O OE2 . GLU A 1 485  ? 156.404 174.147 148.429 1.00 70.52  ? 485  GLU A OE2 1 
ATOM   3068 N N   . VAL A 1 486  ? 161.783 171.046 147.410 1.00 75.12  ? 486  VAL A N   1 
ATOM   3069 C CA  . VAL A 1 486  ? 162.898 170.245 147.907 1.00 71.54  ? 486  VAL A CA  1 
ATOM   3070 C C   . VAL A 1 486  ? 163.786 171.082 148.819 1.00 69.21  ? 486  VAL A C   1 
ATOM   3071 O O   . VAL A 1 486  ? 164.221 170.622 149.882 1.00 71.83  ? 486  VAL A O   1 
ATOM   3072 C CB  . VAL A 1 486  ? 163.693 169.642 146.735 1.00 67.44  ? 486  VAL A CB  1 
ATOM   3073 C CG1 . VAL A 1 486  ? 165.003 169.058 147.226 1.00 64.37  ? 486  VAL A CG1 1 
ATOM   3074 C CG2 . VAL A 1 486  ? 162.868 168.575 146.039 1.00 65.28  ? 486  VAL A CG2 1 
ATOM   3075 N N   . ASP A 1 487  ? 164.058 172.328 148.425 1.00 76.46  ? 487  ASP A N   1 
ATOM   3076 C CA  . ASP A 1 487  ? 164.871 173.207 149.258 1.00 78.83  ? 487  ASP A CA  1 
ATOM   3077 C C   . ASP A 1 487  ? 164.204 173.467 150.602 1.00 80.31  ? 487  ASP A C   1 
ATOM   3078 O O   . ASP A 1 487  ? 164.863 173.436 151.647 1.00 83.08  ? 487  ASP A O   1 
ATOM   3079 C CB  . ASP A 1 487  ? 165.130 174.522 148.524 1.00 80.58  ? 487  ASP A CB  1 
ATOM   3080 C CG  . ASP A 1 487  ? 166.074 175.440 149.277 1.00 85.55  ? 487  ASP A CG  1 
ATOM   3081 O OD1 . ASP A 1 487  ? 166.737 174.975 150.226 1.00 84.53  ? 487  ASP A OD1 1 
ATOM   3082 O OD2 . ASP A 1 487  ? 166.151 176.633 148.916 1.00 89.33  ? 487  ASP A OD2 1 
ATOM   3083 N N   . ARG A 1 488  ? 162.895 173.721 150.595 1.00 82.66  ? 488  ARG A N   1 
ATOM   3084 C CA  . ARG A 1 488  ? 162.185 173.966 151.846 1.00 83.69  ? 488  ARG A CA  1 
ATOM   3085 C C   . ARG A 1 488  ? 162.192 172.728 152.734 1.00 85.68  ? 488  ARG A C   1 
ATOM   3086 O O   . ARG A 1 488  ? 162.344 172.831 153.957 1.00 86.58  ? 488  ARG A O   1 
ATOM   3087 C CB  . ARG A 1 488  ? 160.754 174.415 151.557 1.00 79.96  ? 488  ARG A CB  1 
ATOM   3088 C CG  . ARG A 1 488  ? 159.989 174.870 152.784 1.00 82.90  ? 488  ARG A CG  1 
ATOM   3089 C CD  . ARG A 1 488  ? 158.613 175.386 152.409 1.00 85.68  ? 488  ARG A CD  1 
ATOM   3090 N NE  . ARG A 1 488  ? 157.781 174.343 151.823 1.00 89.62  ? 488  ARG A NE  1 
ATOM   3091 C CZ  . ARG A 1 488  ? 156.959 173.564 152.513 1.00 88.33  ? 488  ARG A CZ  1 
ATOM   3092 N NH1 . ARG A 1 488  ? 156.833 173.683 153.825 1.00 83.25  ? 488  ARG A NH1 1 
ATOM   3093 N NH2 . ARG A 1 488  ? 156.245 172.644 151.872 1.00 88.18  ? 488  ARG A NH2 1 
ATOM   3094 N N   . ILE A 1 489  ? 162.030 171.547 152.134 1.00 77.60  ? 489  ILE A N   1 
ATOM   3095 C CA  . ILE A 1 489  ? 162.031 170.304 152.892 1.00 70.18  ? 489  ILE A CA  1 
ATOM   3096 C C   . ILE A 1 489  ? 163.410 169.986 153.454 1.00 72.03  ? 489  ILE A C   1 
ATOM   3097 O O   . ILE A 1 489  ? 163.511 169.369 154.521 1.00 73.38  ? 489  ILE A O   1 
ATOM   3098 C CB  . ILE A 1 489  ? 161.494 169.164 152.001 1.00 69.85  ? 489  ILE A CB  1 
ATOM   3099 C CG1 . ILE A 1 489  ? 160.009 168.924 152.281 1.00 73.90  ? 489  ILE A CG1 1 
ATOM   3100 C CG2 . ILE A 1 489  ? 162.288 167.882 152.183 1.00 71.98  ? 489  ILE A CG2 1 
ATOM   3101 C CD1 . ILE A 1 489  ? 159.133 170.135 152.043 1.00 74.47  ? 489  ILE A CD1 1 
ATOM   3102 N N   . SER A 1 490  ? 164.479 170.414 152.775 1.00 82.49  ? 490  SER A N   1 
ATOM   3103 C CA  . SER A 1 490  ? 165.829 170.075 153.220 1.00 82.16  ? 490  SER A CA  1 
ATOM   3104 C C   . SER A 1 490  ? 166.093 170.573 154.635 1.00 83.90  ? 490  SER A C   1 
ATOM   3105 O O   . SER A 1 490  ? 166.644 169.839 155.464 1.00 82.49  ? 490  SER A O   1 
ATOM   3106 C CB  . SER A 1 490  ? 166.860 170.650 152.251 1.00 77.78  ? 490  SER A CB  1 
ATOM   3107 O OG  . SER A 1 490  ? 166.688 170.112 150.953 1.00 80.99  ? 490  SER A OG  1 
ATOM   3108 N N   . LYS A 1 491  ? 165.715 171.812 154.931 1.00 82.14  ? 491  LYS A N   1 
ATOM   3109 C CA  . LYS A 1 491  ? 165.800 172.291 156.299 1.00 79.13  ? 491  LYS A CA  1 
ATOM   3110 C C   . LYS A 1 491  ? 164.807 171.533 157.175 1.00 76.21  ? 491  LYS A C   1 
ATOM   3111 O O   . LYS A 1 491  ? 163.683 171.228 156.769 1.00 81.99  ? 491  LYS A O   1 
ATOM   3112 C CB  . LYS A 1 491  ? 165.531 173.793 156.360 1.00 78.39  ? 491  LYS A CB  1 
ATOM   3113 N N   . ILE A 1 492  ? 165.231 171.227 158.395 1.00 75.15  ? 492  ILE A N   1 
ATOM   3114 C CA  . ILE A 1 492  ? 164.421 170.435 159.313 1.00 76.23  ? 492  ILE A CA  1 
ATOM   3115 C C   . ILE A 1 492  ? 163.346 171.337 159.908 1.00 78.45  ? 492  ILE A C   1 
ATOM   3116 O O   . ILE A 1 492  ? 163.647 172.394 160.472 1.00 79.22  ? 492  ILE A O   1 
ATOM   3117 C CB  . ILE A 1 492  ? 165.283 169.788 160.407 1.00 75.13  ? 492  ILE A CB  1 
ATOM   3118 C CG1 . ILE A 1 492  ? 164.397 169.172 161.489 1.00 71.30  ? 492  ILE A CG1 1 
ATOM   3119 C CG2 . ILE A 1 492  ? 166.270 170.791 160.990 1.00 76.28  ? 492  ILE A CG2 1 
ATOM   3120 C CD1 . ILE A 1 492  ? 165.169 168.433 162.554 1.00 75.06  ? 492  ILE A CD1 1 
ATOM   3121 N N   . ASP A 1 493  ? 162.092 170.926 159.768 1.00 70.46  ? 493  ASP A N   1 
ATOM   3122 C CA  . ASP A 1 493  ? 160.959 171.746 160.158 1.00 68.02  ? 493  ASP A CA  1 
ATOM   3123 C C   . ASP A 1 493  ? 160.682 171.621 161.652 1.00 70.35  ? 493  ASP A C   1 
ATOM   3124 O O   . ASP A 1 493  ? 161.229 170.765 162.347 1.00 75.61  ? 493  ASP A O   1 
ATOM   3125 C CB  . ASP A 1 493  ? 159.724 171.358 159.348 1.00 65.62  ? 493  ASP A CB  1 
ATOM   3126 C CG  . ASP A 1 493  ? 159.541 169.862 159.254 1.00 71.36  ? 493  ASP A CG  1 
ATOM   3127 O OD1 . ASP A 1 493  ? 160.556 169.137 159.324 1.00 72.97  ? 493  ASP A OD1 1 
ATOM   3128 O OD2 . ASP A 1 493  ? 158.387 169.408 159.108 1.00 75.84  ? 493  ASP A OD2 1 
ATOM   3129 N N   . ASN A 1 494  ? 159.811 172.505 162.145 1.00 69.00  ? 494  ASN A N   1 
ATOM   3130 C CA  . ASN A 1 494  ? 159.471 172.507 163.563 1.00 62.43  ? 494  ASN A CA  1 
ATOM   3131 C C   . ASN A 1 494  ? 158.739 171.238 163.973 1.00 64.81  ? 494  ASN A C   1 
ATOM   3132 O O   . ASN A 1 494  ? 158.881 170.788 165.114 1.00 68.05  ? 494  ASN A O   1 
ATOM   3133 C CB  . ASN A 1 494  ? 158.623 173.732 163.898 1.00 66.51  ? 494  ASN A CB  1 
ATOM   3134 C CG  . ASN A 1 494  ? 159.349 175.032 163.636 1.00 72.93  ? 494  ASN A CG  1 
ATOM   3135 O OD1 . ASN A 1 494  ? 160.560 175.130 163.831 1.00 73.29  ? 494  ASN A OD1 1 
ATOM   3136 N ND2 . ASN A 1 494  ? 158.611 176.040 163.188 1.00 71.51  ? 494  ASN A ND2 1 
ATOM   3137 N N   . LEU A 1 495  ? 157.941 170.661 163.073 1.00 59.37  ? 495  LEU A N   1 
ATOM   3138 C CA  . LEU A 1 495  ? 157.222 169.439 163.414 1.00 57.82  ? 495  LEU A CA  1 
ATOM   3139 C C   . LEU A 1 495  ? 158.186 168.300 163.712 1.00 58.85  ? 495  LEU A C   1 
ATOM   3140 O O   . LEU A 1 495  ? 157.990 167.548 164.673 1.00 64.82  ? 495  LEU A O   1 
ATOM   3141 C CB  . LEU A 1 495  ? 156.270 169.053 162.284 1.00 57.17  ? 495  LEU A CB  1 
ATOM   3142 C CG  . LEU A 1 495  ? 155.462 167.780 162.531 1.00 54.22  ? 495  LEU A CG  1 
ATOM   3143 C CD1 . LEU A 1 495  ? 154.610 167.931 163.776 1.00 55.21  ? 495  LEU A CD1 1 
ATOM   3144 C CD2 . LEU A 1 495  ? 154.601 167.444 161.329 1.00 54.83  ? 495  LEU A CD2 1 
ATOM   3145 N N   . THR A 1 496  ? 159.236 168.158 162.902 1.00 55.64  ? 496  THR A N   1 
ATOM   3146 C CA  . THR A 1 496  ? 160.219 167.110 163.149 1.00 55.08  ? 496  THR A CA  1 
ATOM   3147 C C   . THR A 1 496  ? 160.946 167.338 164.467 1.00 53.12  ? 496  THR A C   1 
ATOM   3148 O O   . THR A 1 496  ? 161.211 166.387 165.210 1.00 64.15  ? 496  THR A O   1 
ATOM   3149 C CB  . THR A 1 496  ? 161.211 167.037 161.990 1.00 63.77  ? 496  THR A CB  1 
ATOM   3150 O OG1 . THR A 1 496  ? 160.514 166.687 160.788 1.00 64.71  ? 496  THR A OG1 1 
ATOM   3151 C CG2 . THR A 1 496  ? 162.281 165.996 162.264 1.00 60.56  ? 496  THR A CG2 1 
ATOM   3152 N N   . ARG A 1 497  ? 161.276 168.593 164.778 1.00 56.66  ? 497  ARG A N   1 
ATOM   3153 C CA  . ARG A 1 497  ? 161.928 168.888 166.050 1.00 55.56  ? 497  ARG A CA  1 
ATOM   3154 C C   . ARG A 1 497  ? 161.020 168.552 167.225 1.00 59.16  ? 497  ARG A C   1 
ATOM   3155 O O   . ARG A 1 497  ? 161.475 168.006 168.237 1.00 60.51  ? 497  ARG A O   1 
ATOM   3156 C CB  . ARG A 1 497  ? 162.348 170.355 166.089 1.00 55.00  ? 497  ARG A CB  1 
ATOM   3157 C CG  . ARG A 1 497  ? 163.157 170.778 164.879 1.00 61.79  ? 497  ARG A CG  1 
ATOM   3158 C CD  . ARG A 1 497  ? 164.561 171.202 165.258 1.00 64.77  ? 497  ARG A CD  1 
ATOM   3159 N NE  . ARG A 1 497  ? 164.598 172.568 165.766 1.00 67.14  ? 497  ARG A NE  1 
ATOM   3160 C CZ  . ARG A 1 497  ? 164.739 173.643 165.004 1.00 67.16  ? 497  ARG A CZ  1 
ATOM   3161 N NH1 . ARG A 1 497  ? 164.854 173.548 163.689 1.00 59.50  ? 497  ARG A NH1 1 
ATOM   3162 N NH2 . ARG A 1 497  ? 164.767 174.844 165.575 1.00 67.16  ? 497  ARG A NH2 1 
ATOM   3163 N N   . LEU A 1 498  ? 159.729 168.868 167.109 1.00 60.38  ? 498  LEU A N   1 
ATOM   3164 C CA  . LEU A 1 498  ? 158.787 168.526 168.169 1.00 57.77  ? 498  LEU A CA  1 
ATOM   3165 C C   . LEU A 1 498  ? 158.660 167.018 168.329 1.00 60.44  ? 498  LEU A C   1 
ATOM   3166 O O   . LEU A 1 498  ? 158.605 166.507 169.454 1.00 65.71  ? 498  LEU A O   1 
ATOM   3167 C CB  . LEU A 1 498  ? 157.423 169.148 167.878 1.00 55.55  ? 498  LEU A CB  1 
ATOM   3168 C CG  . LEU A 1 498  ? 156.319 168.800 168.874 1.00 57.03  ? 498  LEU A CG  1 
ATOM   3169 C CD1 . LEU A 1 498  ? 156.672 169.318 170.256 1.00 58.70  ? 498  LEU A CD1 1 
ATOM   3170 C CD2 . LEU A 1 498  ? 154.986 169.356 168.410 1.00 59.30  ? 498  LEU A CD2 1 
ATOM   3171 N N   . LEU A 1 499  ? 158.604 166.288 167.214 1.00 46.19  ? 499  LEU A N   1 
ATOM   3172 C CA  . LEU A 1 499  ? 158.533 164.833 167.293 1.00 41.77  ? 499  LEU A CA  1 
ATOM   3173 C C   . LEU A 1 499  ? 159.788 164.260 167.935 1.00 44.25  ? 499  LEU A C   1 
ATOM   3174 O O   . LEU A 1 499  ? 159.714 163.311 168.723 1.00 52.87  ? 499  LEU A O   1 
ATOM   3175 C CB  . LEU A 1 499  ? 158.318 164.239 165.903 1.00 48.14  ? 499  LEU A CB  1 
ATOM   3176 C CG  . LEU A 1 499  ? 156.993 164.592 165.229 1.00 44.95  ? 499  LEU A CG  1 
ATOM   3177 C CD1 . LEU A 1 499  ? 156.875 163.910 163.879 1.00 47.13  ? 499  LEU A CD1 1 
ATOM   3178 C CD2 . LEU A 1 499  ? 155.827 164.220 166.122 1.00 46.42  ? 499  LEU A CD2 1 
ATOM   3179 N N   . LEU A 1 500  ? 160.951 164.821 167.607 1.00 46.91  ? 500  LEU A N   1 
ATOM   3180 C CA  . LEU A 1 500  ? 162.190 164.374 168.231 1.00 45.85  ? 500  LEU A CA  1 
ATOM   3181 C C   . LEU A 1 500  ? 162.177 164.644 169.728 1.00 55.22  ? 500  LEU A C   1 
ATOM   3182 O O   . LEU A 1 500  ? 162.626 163.809 170.519 1.00 66.76  ? 500  LEU A O   1 
ATOM   3183 C CB  . LEU A 1 500  ? 163.387 165.055 167.572 1.00 47.98  ? 500  LEU A CB  1 
ATOM   3184 C CG  . LEU A 1 500  ? 164.754 164.691 168.149 1.00 48.44  ? 500  LEU A CG  1 
ATOM   3185 C CD1 . LEU A 1 500  ? 164.957 163.192 168.103 1.00 50.42  ? 500  LEU A CD1 1 
ATOM   3186 C CD2 . LEU A 1 500  ? 165.859 165.405 167.394 1.00 50.81  ? 500  LEU A CD2 1 
ATOM   3187 N N   . LEU A 1 501  ? 161.670 165.808 170.135 1.00 51.38  ? 501  LEU A N   1 
ATOM   3188 C CA  . LEU A 1 501  ? 161.582 166.109 171.559 1.00 53.38  ? 501  LEU A CA  1 
ATOM   3189 C C   . LEU A 1 501  ? 160.654 165.134 172.271 1.00 51.87  ? 501  LEU A C   1 
ATOM   3190 O O   . LEU A 1 501  ? 160.961 164.661 173.370 1.00 54.75  ? 501  LEU A O   1 
ATOM   3191 C CB  . LEU A 1 501  ? 161.108 167.546 171.765 1.00 58.13  ? 501  LEU A CB  1 
ATOM   3192 C CG  . LEU A 1 501  ? 161.037 168.007 173.220 1.00 58.11  ? 501  LEU A CG  1 
ATOM   3193 C CD1 . LEU A 1 501  ? 162.419 167.989 173.847 1.00 57.29  ? 501  LEU A CD1 1 
ATOM   3194 C CD2 . LEU A 1 501  ? 160.418 169.389 173.318 1.00 55.61  ? 501  LEU A CD2 1 
ATOM   3195 N N   . ILE A 1 502  ? 159.514 164.818 171.656 1.00 50.29  ? 502  ILE A N   1 
ATOM   3196 C CA  . ILE A 1 502  ? 158.581 163.874 172.266 1.00 49.28  ? 502  ILE A CA  1 
ATOM   3197 C C   . ILE A 1 502  ? 159.210 162.490 172.367 1.00 55.73  ? 502  ILE A C   1 
ATOM   3198 O O   . ILE A 1 502  ? 159.051 161.792 173.375 1.00 62.38  ? 502  ILE A O   1 
ATOM   3199 C CB  . ILE A 1 502  ? 157.258 163.841 171.481 1.00 52.54  ? 502  ILE A CB  1 
ATOM   3200 C CG1 . ILE A 1 502  ? 156.575 165.206 171.537 1.00 49.82  ? 502  ILE A CG1 1 
ATOM   3201 C CG2 . ILE A 1 502  ? 156.333 162.776 172.038 1.00 53.98  ? 502  ILE A CG2 1 
ATOM   3202 C CD1 . ILE A 1 502  ? 155.262 165.256 170.799 1.00 51.93  ? 502  ILE A CD1 1 
ATOM   3203 N N   . GLY A 1 503  ? 159.932 162.069 171.328 1.00 54.31  ? 503  GLY A N   1 
ATOM   3204 C CA  . GLY A 1 503  ? 160.601 160.778 171.380 1.00 50.64  ? 503  GLY A CA  1 
ATOM   3205 C C   . GLY A 1 503  ? 161.679 160.722 172.443 1.00 55.43  ? 503  GLY A C   1 
ATOM   3206 O O   . GLY A 1 503  ? 161.833 159.712 173.135 1.00 64.02  ? 503  GLY A O   1 
ATOM   3207 N N   . VAL A 1 504  ? 162.445 161.804 172.584 1.00 51.37  ? 504  VAL A N   1 
ATOM   3208 C CA  . VAL A 1 504  ? 163.458 161.863 173.632 1.00 49.95  ? 504  VAL A CA  1 
ATOM   3209 C C   . VAL A 1 504  ? 162.802 161.800 175.003 1.00 55.66  ? 504  VAL A C   1 
ATOM   3210 O O   . VAL A 1 504  ? 163.291 161.116 175.908 1.00 67.54  ? 504  VAL A O   1 
ATOM   3211 C CB  . VAL A 1 504  ? 164.326 163.124 173.472 1.00 55.54  ? 504  VAL A CB  1 
ATOM   3212 C CG1 . VAL A 1 504  ? 165.179 163.339 174.708 1.00 55.03  ? 504  VAL A CG1 1 
ATOM   3213 C CG2 . VAL A 1 504  ? 165.205 162.998 172.245 1.00 60.71  ? 504  VAL A CG2 1 
ATOM   3214 N N   . LEU A 1 505  ? 161.686 162.508 175.182 1.00 54.67  ? 505  LEU A N   1 
ATOM   3215 C CA  . LEU A 1 505  ? 160.974 162.431 176.453 1.00 56.86  ? 505  LEU A CA  1 
ATOM   3216 C C   . LEU A 1 505  ? 160.491 161.015 176.727 1.00 58.38  ? 505  LEU A C   1 
ATOM   3217 O O   . LEU A 1 505  ? 160.604 160.521 177.854 1.00 65.68  ? 505  LEU A O   1 
ATOM   3218 C CB  . LEU A 1 505  ? 159.801 163.409 176.466 1.00 56.80  ? 505  LEU A CB  1 
ATOM   3219 C CG  . LEU A 1 505  ? 160.167 164.890 176.550 1.00 60.42  ? 505  LEU A CG  1 
ATOM   3220 C CD1 . LEU A 1 505  ? 158.916 165.746 176.622 1.00 61.48  ? 505  LEU A CD1 1 
ATOM   3221 C CD2 . LEU A 1 505  ? 161.063 165.146 177.747 1.00 60.98  ? 505  LEU A CD2 1 
ATOM   3222 N N   . LEU A 1 506  ? 159.955 160.342 175.707 1.00 55.18  ? 506  LEU A N   1 
ATOM   3223 C CA  . LEU A 1 506  ? 159.468 158.980 175.897 1.00 55.91  ? 506  LEU A CA  1 
ATOM   3224 C C   . LEU A 1 506  ? 160.597 158.036 176.282 1.00 58.09  ? 506  LEU A C   1 
ATOM   3225 O O   . LEU A 1 506  ? 160.452 157.229 177.208 1.00 68.06  ? 506  LEU A O   1 
ATOM   3226 C CB  . LEU A 1 506  ? 158.773 158.483 174.631 1.00 55.95  ? 506  LEU A CB  1 
ATOM   3227 C CG  . LEU A 1 506  ? 157.384 159.045 174.344 1.00 58.33  ? 506  LEU A CG  1 
ATOM   3228 C CD1 . LEU A 1 506  ? 156.820 158.422 173.084 1.00 54.75  ? 506  LEU A CD1 1 
ATOM   3229 C CD2 . LEU A 1 506  ? 156.465 158.797 175.523 1.00 61.97  ? 506  LEU A CD2 1 
ATOM   3230 N N   . ILE A 1 507  ? 161.731 158.118 175.586 1.00 55.12  ? 507  ILE A N   1 
ATOM   3231 C CA  . ILE A 1 507  ? 162.825 157.203 175.888 1.00 54.74  ? 507  ILE A CA  1 
ATOM   3232 C C   . ILE A 1 507  ? 163.427 157.521 177.251 1.00 57.57  ? 507  ILE A C   1 
ATOM   3233 O O   . ILE A 1 507  ? 163.817 156.616 177.996 1.00 57.77  ? 507  ILE A O   1 
ATOM   3234 C CB  . ILE A 1 507  ? 163.881 157.215 174.767 1.00 58.34  ? 507  ILE A CB  1 
ATOM   3235 C CG1 . ILE A 1 507  ? 164.955 156.169 175.045 1.00 52.56  ? 507  ILE A CG1 1 
ATOM   3236 C CG2 . ILE A 1 507  ? 164.524 158.571 174.622 1.00 60.17  ? 507  ILE A CG2 1 
ATOM   3237 C CD1 . ILE A 1 507  ? 164.397 154.837 175.442 1.00 54.82  ? 507  ILE A CD1 1 
ATOM   3238 N N   . PHE A 1 508  ? 163.502 158.804 177.609 1.00 66.85  ? 508  PHE A N   1 
ATOM   3239 C CA  . PHE A 1 508  ? 163.986 159.171 178.933 1.00 63.45  ? 508  PHE A CA  1 
ATOM   3240 C C   . PHE A 1 508  ? 163.069 158.631 180.021 1.00 67.74  ? 508  PHE A C   1 
ATOM   3241 O O   . PHE A 1 508  ? 163.544 158.093 181.027 1.00 75.20  ? 508  PHE A O   1 
ATOM   3242 C CB  . PHE A 1 508  ? 164.117 160.689 179.030 1.00 58.11  ? 508  PHE A CB  1 
ATOM   3243 C CG  . PHE A 1 508  ? 164.066 161.218 180.429 1.00 68.75  ? 508  PHE A CG  1 
ATOM   3244 C CD1 . PHE A 1 508  ? 165.122 161.020 181.298 1.00 71.82  ? 508  PHE A CD1 1 
ATOM   3245 C CD2 . PHE A 1 508  ? 162.967 161.933 180.869 1.00 76.85  ? 508  PHE A CD2 1 
ATOM   3246 C CE1 . PHE A 1 508  ? 165.075 161.514 182.585 1.00 65.84  ? 508  PHE A CE1 1 
ATOM   3247 C CE2 . PHE A 1 508  ? 162.916 162.431 182.154 1.00 77.68  ? 508  PHE A CE2 1 
ATOM   3248 C CZ  . PHE A 1 508  ? 163.971 162.221 183.012 1.00 70.41  ? 508  PHE A CZ  1 
ATOM   3249 N N   . MET A 1 509  ? 161.754 158.745 179.827 1.00 65.14  ? 509  MET A N   1 
ATOM   3250 C CA  . MET A 1 509  ? 160.816 158.201 180.803 1.00 66.52  ? 509  MET A CA  1 
ATOM   3251 C C   . MET A 1 509  ? 160.947 156.689 180.912 1.00 66.74  ? 509  MET A C   1 
ATOM   3252 O O   . MET A 1 509  ? 160.936 156.140 182.017 1.00 75.08  ? 509  MET A O   1 
ATOM   3253 C CB  . MET A 1 509  ? 159.385 158.586 180.432 1.00 70.13  ? 509  MET A CB  1 
ATOM   3254 C CG  . MET A 1 509  ? 159.058 160.051 180.652 1.00 72.17  ? 509  MET A CG  1 
ATOM   3255 S SD  . MET A 1 509  ? 157.402 160.473 180.082 1.00 87.52  ? 509  MET A SD  1 
ATOM   3256 C CE  . MET A 1 509  ? 156.418 159.318 181.032 1.00 72.18  ? 509  MET A CE  1 
ATOM   3257 N N   . TYR A 1 510  ? 161.075 155.999 179.777 1.00 53.47  ? 510  TYR A N   1 
ATOM   3258 C CA  . TYR A 1 510  ? 161.194 154.544 179.805 1.00 54.77  ? 510  TYR A CA  1 
ATOM   3259 C C   . TYR A 1 510  ? 162.469 154.108 180.517 1.00 61.30  ? 510  TYR A C   1 
ATOM   3260 O O   . TYR A 1 510  ? 162.449 153.200 181.359 1.00 68.09  ? 510  TYR A O   1 
ATOM   3261 C CB  . TYR A 1 510  ? 161.155 153.997 178.379 1.00 55.66  ? 510  TYR A CB  1 
ATOM   3262 C CG  . TYR A 1 510  ? 161.370 152.508 178.276 1.00 54.51  ? 510  TYR A CG  1 
ATOM   3263 C CD1 . TYR A 1 510  ? 160.356 151.618 178.592 1.00 57.26  ? 510  TYR A CD1 1 
ATOM   3264 C CD2 . TYR A 1 510  ? 162.582 151.992 177.845 1.00 54.70  ? 510  TYR A CD2 1 
ATOM   3265 C CE1 . TYR A 1 510  ? 160.546 150.256 178.492 1.00 58.95  ? 510  TYR A CE1 1 
ATOM   3266 C CE2 . TYR A 1 510  ? 162.780 150.633 177.742 1.00 53.50  ? 510  TYR A CE2 1 
ATOM   3267 C CZ  . TYR A 1 510  ? 161.760 149.770 178.067 1.00 57.25  ? 510  TYR A CZ  1 
ATOM   3268 O OH  . TYR A 1 510  ? 161.954 148.413 177.967 1.00 62.52  ? 510  TYR A OH  1 
ATOM   3269 N N   . ALA A 1 511  ? 163.590 154.756 180.197 1.00 58.34  ? 511  ALA A N   1 
ATOM   3270 C CA  . ALA A 1 511  ? 164.854 154.402 180.829 1.00 53.55  ? 511  ALA A CA  1 
ATOM   3271 C C   . ALA A 1 511  ? 164.825 154.690 182.322 1.00 54.86  ? 511  ALA A C   1 
ATOM   3272 O O   . ALA A 1 511  ? 165.303 153.881 183.125 1.00 68.59  ? 511  ALA A O   1 
ATOM   3273 C CB  . ALA A 1 511  ? 166.002 155.152 180.157 1.00 57.57  ? 511  ALA A CB  1 
ATOM   3274 N N   . LEU A 1 512  ? 164.268 155.836 182.716 1.00 49.76  ? 512  LEU A N   1 
ATOM   3275 C CA  . LEU A 1 512  ? 164.169 156.146 184.136 1.00 54.16  ? 512  LEU A CA  1 
ATOM   3276 C C   . LEU A 1 512  ? 163.276 155.144 184.853 1.00 62.40  ? 512  LEU A C   1 
ATOM   3277 O O   . LEU A 1 512  ? 163.603 154.684 185.951 1.00 69.79  ? 512  LEU A O   1 
ATOM   3278 C CB  . LEU A 1 512  ? 163.643 157.566 184.325 1.00 59.16  ? 512  LEU A CB  1 
ATOM   3279 C CG  . LEU A 1 512  ? 164.409 158.427 185.327 1.00 64.62  ? 512  LEU A CG  1 
ATOM   3280 C CD1 . LEU A 1 512  ? 165.838 158.636 184.860 1.00 66.68  ? 512  LEU A CD1 1 
ATOM   3281 C CD2 . LEU A 1 512  ? 163.710 159.757 185.527 1.00 63.31  ? 512  LEU A CD2 1 
ATOM   3282 N N   . PHE A 1 513  ? 162.150 154.780 184.237 1.00 68.98  ? 513  PHE A N   1 
ATOM   3283 C CA  . PHE A 1 513  ? 161.236 153.827 184.853 1.00 65.55  ? 513  PHE A CA  1 
ATOM   3284 C C   . PHE A 1 513  ? 161.903 152.474 185.045 1.00 63.09  ? 513  PHE A C   1 
ATOM   3285 O O   . PHE A 1 513  ? 161.703 151.816 186.072 1.00 70.55  ? 513  PHE A O   1 
ATOM   3286 C CB  . PHE A 1 513  ? 159.976 153.696 183.997 1.00 64.09  ? 513  PHE A CB  1 
ATOM   3287 C CG  . PHE A 1 513  ? 159.098 152.542 184.374 1.00 68.48  ? 513  PHE A CG  1 
ATOM   3288 C CD1 . PHE A 1 513  ? 158.244 152.629 185.458 1.00 72.72  ? 513  PHE A CD1 1 
ATOM   3289 C CD2 . PHE A 1 513  ? 159.113 151.374 183.632 1.00 70.39  ? 513  PHE A CD2 1 
ATOM   3290 C CE1 . PHE A 1 513  ? 157.429 151.568 185.803 1.00 70.02  ? 513  PHE A CE1 1 
ATOM   3291 C CE2 . PHE A 1 513  ? 158.302 150.311 183.972 1.00 72.09  ? 513  PHE A CE2 1 
ATOM   3292 C CZ  . PHE A 1 513  ? 157.459 150.408 185.059 1.00 70.79  ? 513  PHE A CZ  1 
ATOM   3293 N N   . ASN A 1 514  ? 162.699 152.041 184.069 1.00 54.83  ? 514  ASN A N   1 
ATOM   3294 C CA  . ASN A 1 514  ? 163.373 150.754 184.210 1.00 58.98  ? 514  ASN A CA  1 
ATOM   3295 C C   . ASN A 1 514  ? 164.517 150.822 185.216 1.00 69.02  ? 514  ASN A C   1 
ATOM   3296 O O   . ASN A 1 514  ? 164.773 149.849 185.933 1.00 71.85  ? 514  ASN A O   1 
ATOM   3297 C CB  . ASN A 1 514  ? 163.877 150.273 182.853 1.00 59.53  ? 514  ASN A CB  1 
ATOM   3298 C CG  . ASN A 1 514  ? 162.769 149.715 181.994 1.00 65.86  ? 514  ASN A CG  1 
ATOM   3299 O OD1 . ASN A 1 514  ? 162.543 148.507 181.962 1.00 67.81  ? 514  ASN A OD1 1 
ATOM   3300 N ND2 . ASN A 1 514  ? 162.062 150.594 181.297 1.00 73.03  ? 514  ASN A ND2 1 
ATOM   3301 N N   . ASN A 1 515  ? 165.214 151.953 185.289 1.00 63.08  ? 515  ASN A N   1 
ATOM   3302 C CA  . ASN A 1 515  ? 166.424 152.052 186.094 1.00 55.75  ? 515  ASN A CA  1 
ATOM   3303 C C   . ASN A 1 515  ? 166.215 152.723 187.446 1.00 59.13  ? 515  ASN A C   1 
ATOM   3304 O O   . ASN A 1 515  ? 167.201 153.004 188.133 1.00 65.93  ? 515  ASN A O   1 
ATOM   3305 C CB  . ASN A 1 515  ? 167.511 152.799 185.319 1.00 55.07  ? 515  ASN A CB  1 
ATOM   3306 C CG  . ASN A 1 515  ? 167.918 152.078 184.057 1.00 59.07  ? 515  ASN A CG  1 
ATOM   3307 O OD1 . ASN A 1 515  ? 168.144 152.698 183.021 1.00 70.62  ? 515  ASN A OD1 1 
ATOM   3308 N ND2 . ASN A 1 515  ? 168.007 150.758 184.134 1.00 55.04  ? 515  ASN A ND2 1 
ATOM   3309 N N   . VAL A 1 516  ? 164.977 152.994 187.846 1.00 62.09  ? 516  VAL A N   1 
ATOM   3310 C CA  . VAL A 1 516  ? 164.676 153.535 189.168 1.00 64.15  ? 516  VAL A CA  1 
ATOM   3311 C C   . VAL A 1 516  ? 163.862 152.504 189.932 1.00 68.78  ? 516  VAL A C   1 
ATOM   3312 O O   . VAL A 1 516  ? 162.826 152.036 189.445 1.00 70.25  ? 516  VAL A O   1 
ATOM   3313 C CB  . VAL A 1 516  ? 163.929 154.876 189.083 1.00 64.17  ? 516  VAL A CB  1 
ATOM   3314 C CG1 . VAL A 1 516  ? 163.359 155.245 190.437 1.00 65.46  ? 516  VAL A CG1 1 
ATOM   3315 C CG2 . VAL A 1 516  ? 164.864 155.965 188.593 1.00 63.22  ? 516  VAL A CG2 1 
ATOM   3316 N N   . THR A 1 517  ? 164.330 152.150 191.128 1.00 64.89  ? 517  THR A N   1 
ATOM   3317 C CA  . THR A 1 517  ? 163.685 151.113 191.922 1.00 65.09  ? 517  THR A CA  1 
ATOM   3318 C C   . THR A 1 517  ? 163.351 151.614 193.320 1.00 62.39  ? 517  THR A C   1 
ATOM   3319 O O   . THR A 1 517  ? 163.438 152.815 193.593 1.00 60.39  ? 517  THR A O   1 
ATOM   3320 C CB  . THR A 1 517  ? 164.575 149.874 192.007 1.00 65.03  ? 517  THR A CB  1 
ATOM   3321 O OG1 . THR A 1 517  ? 165.840 150.232 192.575 1.00 60.62  ? 517  THR A OG1 1 
ATOM   3322 C CG2 . THR A 1 517  ? 164.796 149.290 190.625 1.00 65.54  ? 517  THR A CG2 1 
ATOM   3323 N N   . SER A 1 518  ? 162.958 150.698 194.208 1.00 63.46  ? 518  SER A N   1 
ATOM   3324 C CA  . SER A 1 518  ? 162.566 151.091 195.557 1.00 63.32  ? 518  SER A CA  1 
ATOM   3325 C C   . SER A 1 518  ? 163.729 151.715 196.316 1.00 60.95  ? 518  SER A C   1 
ATOM   3326 O O   . SER A 1 518  ? 163.558 152.723 197.009 1.00 67.81  ? 518  SER A O   1 
ATOM   3327 C CB  . SER A 1 518  ? 162.020 149.884 196.317 1.00 67.37  ? 518  SER A CB  1 
ATOM   3328 O OG  . SER A 1 518  ? 163.008 148.879 196.453 1.00 69.50  ? 518  SER A OG  1 
ATOM   3329 N N   . VAL A 1 519  ? 164.916 151.134 196.199 1.00 56.55  ? 519  VAL A N   1 
ATOM   3330 C CA  . VAL A 1 519  ? 166.100 151.643 196.880 1.00 56.12  ? 519  VAL A CA  1 
ATOM   3331 C C   . VAL A 1 519  ? 166.758 152.679 195.982 1.00 61.25  ? 519  VAL A C   1 
ATOM   3332 O O   . VAL A 1 519  ? 167.075 152.397 194.822 1.00 72.14  ? 519  VAL A O   1 
ATOM   3333 C CB  . VAL A 1 519  ? 167.074 150.509 197.223 1.00 54.23  ? 519  VAL A CB  1 
ATOM   3334 C CG1 . VAL A 1 519  ? 168.294 151.066 197.909 1.00 53.44  ? 519  VAL A CG1 1 
ATOM   3335 C CG2 . VAL A 1 519  ? 166.393 149.484 198.106 1.00 62.99  ? 519  VAL A CG2 1 
ATOM   3336 N N   . LEU A 1 520  ? 166.960 153.884 196.514 1.00 61.42  ? 520  LEU A N   1 
ATOM   3337 C CA  . LEU A 1 520  ? 167.457 154.977 195.689 1.00 65.75  ? 520  LEU A CA  1 
ATOM   3338 C C   . LEU A 1 520  ? 168.948 154.871 195.399 1.00 73.32  ? 520  LEU A C   1 
ATOM   3339 O O   . LEU A 1 520  ? 169.374 155.187 194.284 1.00 81.50  ? 520  LEU A O   1 
ATOM   3340 C CB  . LEU A 1 520  ? 167.147 156.318 196.353 1.00 70.08  ? 520  LEU A CB  1 
ATOM   3341 C CG  . LEU A 1 520  ? 165.727 156.832 196.118 1.00 69.24  ? 520  LEU A CG  1 
ATOM   3342 C CD1 . LEU A 1 520  ? 165.450 158.072 196.952 1.00 73.50  ? 520  LEU A CD1 1 
ATOM   3343 C CD2 . LEU A 1 520  ? 165.512 157.120 194.641 1.00 67.67  ? 520  LEU A CD2 1 
ATOM   3344 N N   . TYR A 1 521  ? 169.758 154.434 196.364 1.00 64.72  ? 521  TYR A N   1 
ATOM   3345 C CA  . TYR A 1 521  ? 171.196 154.422 196.134 1.00 64.09  ? 521  TYR A CA  1 
ATOM   3346 C C   . TYR A 1 521  ? 171.647 153.273 195.246 1.00 63.18  ? 521  TYR A C   1 
ATOM   3347 O O   . TYR A 1 521  ? 172.773 153.311 194.741 1.00 72.92  ? 521  TYR A O   1 
ATOM   3348 C CB  . TYR A 1 521  ? 171.962 154.390 197.462 1.00 61.60  ? 521  TYR A CB  1 
ATOM   3349 C CG  . TYR A 1 521  ? 171.809 153.132 198.288 1.00 61.26  ? 521  TYR A CG  1 
ATOM   3350 C CD1 . TYR A 1 521  ? 172.593 152.015 198.042 1.00 64.40  ? 521  TYR A CD1 1 
ATOM   3351 C CD2 . TYR A 1 521  ? 170.910 153.078 199.341 1.00 67.75  ? 521  TYR A CD2 1 
ATOM   3352 C CE1 . TYR A 1 521  ? 172.466 150.872 198.803 1.00 68.09  ? 521  TYR A CE1 1 
ATOM   3353 C CE2 . TYR A 1 521  ? 170.779 151.940 200.110 1.00 68.81  ? 521  TYR A CE2 1 
ATOM   3354 C CZ  . TYR A 1 521  ? 171.558 150.840 199.835 1.00 69.84  ? 521  TYR A CZ  1 
ATOM   3355 O OH  . TYR A 1 521  ? 171.429 149.702 200.596 1.00 70.92  ? 521  TYR A OH  1 
ATOM   3356 N N   . ARG A 1 522  ? 170.809 152.261 195.042 1.00 59.17  ? 522  ARG A N   1 
ATOM   3357 C CA  . ARG A 1 522  ? 171.111 151.206 194.087 1.00 55.36  ? 522  ARG A CA  1 
ATOM   3358 C C   . ARG A 1 522  ? 170.575 151.502 192.695 1.00 60.60  ? 522  ARG A C   1 
ATOM   3359 O O   . ARG A 1 522  ? 170.892 150.764 191.758 1.00 63.68  ? 522  ARG A O   1 
ATOM   3360 C CB  . ARG A 1 522  ? 170.547 149.868 194.573 1.00 49.76  ? 522  ARG A CB  1 
ATOM   3361 C CG  . ARG A 1 522  ? 171.203 149.353 195.836 1.00 55.77  ? 522  ARG A CG  1 
ATOM   3362 C CD  . ARG A 1 522  ? 170.687 147.981 196.214 1.00 55.21  ? 522  ARG A CD  1 
ATOM   3363 N NE  . ARG A 1 522  ? 171.347 147.471 197.408 1.00 55.42  ? 522  ARG A NE  1 
ATOM   3364 C CZ  . ARG A 1 522  ? 172.521 146.855 197.405 1.00 63.44  ? 522  ARG A CZ  1 
ATOM   3365 N NH1 . ARG A 1 522  ? 173.194 146.657 196.284 1.00 63.93  ? 522  ARG A NH1 1 
ATOM   3366 N NH2 . ARG A 1 522  ? 173.033 146.430 198.555 1.00 65.81  ? 522  ARG A NH2 1 
ATOM   3367 N N   . SER A 1 523  ? 169.784 152.557 192.537 1.00 59.12  ? 523  SER A N   1 
ATOM   3368 C CA  . SER A 1 523  ? 169.251 152.917 191.235 1.00 59.71  ? 523  SER A CA  1 
ATOM   3369 C C   . SER A 1 523  ? 170.300 153.652 190.409 1.00 63.87  ? 523  SER A C   1 
ATOM   3370 O O   . SER A 1 523  ? 171.295 154.161 190.929 1.00 66.29  ? 523  SER A O   1 
ATOM   3371 C CB  . SER A 1 523  ? 168.005 153.787 191.384 1.00 56.59  ? 523  SER A CB  1 
ATOM   3372 O OG  . SER A 1 523  ? 167.608 154.305 190.129 1.00 71.82  ? 523  SER A OG  1 
ATOM   3373 N N   . LYS A 1 524  ? 170.063 153.705 189.100 1.00 61.01  ? 524  LYS A N   1 
ATOM   3374 C CA  . LYS A 1 524  ? 170.953 154.380 188.157 1.00 55.27  ? 524  LYS A CA  1 
ATOM   3375 C C   . LYS A 1 524  ? 170.144 155.294 187.245 1.00 65.25  ? 524  LYS A C   1 
ATOM   3376 O O   . LYS A 1 524  ? 170.022 155.039 186.041 1.00 69.59  ? 524  LYS A O   1 
ATOM   3377 C CB  . LYS A 1 524  ? 171.746 153.365 187.333 1.00 54.21  ? 524  LYS A CB  1 
ATOM   3378 C CG  . LYS A 1 524  ? 172.520 152.353 188.156 1.00 61.24  ? 524  LYS A CG  1 
ATOM   3379 C CD  . LYS A 1 524  ? 173.587 153.023 188.994 1.00 59.42  ? 524  LYS A CD  1 
ATOM   3380 C CE  . LYS A 1 524  ? 174.328 152.013 189.844 1.00 62.48  ? 524  LYS A CE  1 
ATOM   3381 N NZ  . LYS A 1 524  ? 175.379 152.662 190.671 1.00 64.22  ? 524  LYS A NZ  1 
ATOM   3382 N N   . PRO A 1 525  ? 169.571 156.374 187.786 1.00 68.71  ? 525  PRO A N   1 
ATOM   3383 C CA  . PRO A 1 525  ? 168.897 157.338 186.904 1.00 68.00  ? 525  PRO A CA  1 
ATOM   3384 C C   . PRO A 1 525  ? 169.879 158.175 186.112 1.00 68.63  ? 525  PRO A C   1 
ATOM   3385 O O   . PRO A 1 525  ? 169.658 158.442 184.920 1.00 74.64  ? 525  PRO A O   1 
ATOM   3386 C CB  . PRO A 1 525  ? 168.076 158.198 187.878 1.00 67.27  ? 525  PRO A CB  1 
ATOM   3387 C CG  . PRO A 1 525  ? 168.205 157.531 189.226 1.00 68.06  ? 525  PRO A CG  1 
ATOM   3388 C CD  . PRO A 1 525  ? 169.490 156.787 189.193 1.00 63.38  ? 525  PRO A CD  1 
ATOM   3389 N N   . LEU A 1 526  ? 170.969 158.597 186.756 1.00 61.71  ? 526  LEU A N   1 
ATOM   3390 C CA  . LEU A 1 526  ? 171.979 159.392 186.074 1.00 66.78  ? 526  LEU A CA  1 
ATOM   3391 C C   . LEU A 1 526  ? 172.569 158.629 184.899 1.00 69.44  ? 526  LEU A C   1 
ATOM   3392 O O   . LEU A 1 526  ? 172.855 159.216 183.851 1.00 72.98  ? 526  LEU A O   1 
ATOM   3393 C CB  . LEU A 1 526  ? 173.073 159.794 187.061 1.00 62.64  ? 526  LEU A CB  1 
ATOM   3394 C CG  . LEU A 1 526  ? 174.031 160.898 186.627 1.00 63.09  ? 526  LEU A CG  1 
ATOM   3395 C CD1 . LEU A 1 526  ? 173.267 162.186 186.390 1.00 64.70  ? 526  LEU A CD1 1 
ATOM   3396 C CD2 . LEU A 1 526  ? 175.106 161.098 187.677 1.00 64.79  ? 526  LEU A CD2 1 
ATOM   3397 N N   . CYS A 1 527  ? 172.749 157.316 185.052 1.00 63.47  ? 527  CYS A N   1 
ATOM   3398 C CA  . CYS A 1 527  ? 173.267 156.514 183.950 1.00 59.76  ? 527  CYS A CA  1 
ATOM   3399 C C   . CYS A 1 527  ? 172.321 156.532 182.758 1.00 64.78  ? 527  CYS A C   1 
ATOM   3400 O O   . CYS A 1 527  ? 172.765 156.649 181.615 1.00 74.31  ? 527  CYS A O   1 
ATOM   3401 C CB  . CYS A 1 527  ? 173.520 155.082 184.410 1.00 67.23  ? 527  CYS A CB  1 
ATOM   3402 S SG  . CYS A 1 527  ? 175.152 154.821 185.122 1.00 82.58  ? 527  CYS A SG  1 
ATOM   3403 N N   . ALA A 1 528  ? 171.014 156.430 183.001 1.00 62.36  ? 528  ALA A N   1 
ATOM   3404 C CA  . ALA A 1 528  ? 170.060 156.468 181.895 1.00 62.74  ? 528  ALA A CA  1 
ATOM   3405 C C   . ALA A 1 528  ? 170.042 157.833 181.217 1.00 67.21  ? 528  ALA A C   1 
ATOM   3406 O O   . ALA A 1 528  ? 170.043 157.925 179.978 1.00 70.28  ? 528  ALA A O   1 
ATOM   3407 C CB  . ALA A 1 528  ? 168.666 156.102 182.398 1.00 58.95  ? 528  ALA A CB  1 
ATOM   3408 N N   . VAL A 1 529  ? 170.023 158.907 182.012 1.00 63.48  ? 529  VAL A N   1 
ATOM   3409 C CA  . VAL A 1 529  ? 170.014 160.248 181.433 1.00 59.21  ? 529  VAL A CA  1 
ATOM   3410 C C   . VAL A 1 529  ? 171.268 160.473 180.601 1.00 65.48  ? 529  VAL A C   1 
ATOM   3411 O O   . VAL A 1 529  ? 171.206 160.982 179.474 1.00 69.61  ? 529  VAL A O   1 
ATOM   3412 C CB  . VAL A 1 529  ? 169.871 161.309 182.538 1.00 61.14  ? 529  VAL A CB  1 
ATOM   3413 C CG1 . VAL A 1 529  ? 169.913 162.702 181.941 1.00 64.12  ? 529  VAL A CG1 1 
ATOM   3414 C CG2 . VAL A 1 529  ? 168.581 161.099 183.303 1.00 66.99  ? 529  VAL A CG2 1 
ATOM   3415 N N   . MET A 1 530  ? 172.425 160.078 181.129 1.00 63.25  ? 530  MET A N   1 
ATOM   3416 C CA  . MET A 1 530  ? 173.659 160.258 180.386 1.00 57.38  ? 530  MET A CA  1 
ATOM   3417 C C   . MET A 1 530  ? 173.779 159.292 179.219 1.00 57.07  ? 530  MET A C   1 
ATOM   3418 O O   . MET A 1 530  ? 174.517 159.580 178.283 1.00 72.95  ? 530  MET A O   1 
ATOM   3419 C CB  . MET A 1 530  ? 174.856 160.126 181.320 1.00 60.20  ? 530  MET A CB  1 
ATOM   3420 C CG  . MET A 1 530  ? 174.888 161.204 182.383 1.00 63.69  ? 530  MET A CG  1 
ATOM   3421 S SD  . MET A 1 530  ? 174.610 162.840 181.682 1.00 71.95  ? 530  MET A SD  1 
ATOM   3422 C CE  . MET A 1 530  ? 174.415 163.818 183.166 1.00 65.55  ? 530  MET A CE  1 
ATOM   3423 N N   . GLY A 1 531  ? 173.065 158.167 179.234 1.00 48.64  ? 531  GLY A N   1 
ATOM   3424 C CA  . GLY A 1 531  ? 172.998 157.337 178.042 1.00 47.31  ? 531  GLY A CA  1 
ATOM   3425 C C   . GLY A 1 531  ? 172.238 158.009 176.916 1.00 50.82  ? 531  GLY A C   1 
ATOM   3426 O O   . GLY A 1 531  ? 172.663 157.978 175.754 1.00 64.58  ? 531  GLY A O   1 
ATOM   3427 N N   . ILE A 1 532  ? 171.105 158.632 177.243 1.00 52.35  ? 532  ILE A N   1 
ATOM   3428 C CA  . ILE A 1 532  ? 170.390 159.417 176.237 1.00 57.99  ? 532  ILE A CA  1 
ATOM   3429 C C   . ILE A 1 532  ? 171.280 160.542 175.724 1.00 56.95  ? 532  ILE A C   1 
ATOM   3430 O O   . ILE A 1 532  ? 171.355 160.808 174.513 1.00 60.19  ? 532  ILE A O   1 
ATOM   3431 C CB  . ILE A 1 532  ? 169.072 159.965 176.814 1.00 57.94  ? 532  ILE A CB  1 
ATOM   3432 C CG1 . ILE A 1 532  ? 168.263 158.849 177.466 1.00 58.51  ? 532  ILE A CG1 1 
ATOM   3433 C CG2 . ILE A 1 532  ? 168.262 160.639 175.725 1.00 58.04  ? 532  ILE A CG2 1 
ATOM   3434 C CD1 . ILE A 1 532  ? 167.837 157.781 176.510 1.00 55.13  ? 532  ILE A CD1 1 
ATOM   3435 N N   . PHE A 1 533  ? 171.972 161.218 176.642 1.00 58.70  ? 533  PHE A N   1 
ATOM   3436 C CA  . PHE A 1 533  ? 172.883 162.282 176.248 1.00 51.54  ? 533  PHE A CA  1 
ATOM   3437 C C   . PHE A 1 533  ? 174.024 161.751 175.390 1.00 51.61  ? 533  PHE A C   1 
ATOM   3438 O O   . PHE A 1 533  ? 174.475 162.438 174.473 1.00 63.12  ? 533  PHE A O   1 
ATOM   3439 C CB  . PHE A 1 533  ? 173.421 162.987 177.491 1.00 53.98  ? 533  PHE A CB  1 
ATOM   3440 C CG  . PHE A 1 533  ? 173.707 164.443 177.285 1.00 56.37  ? 533  PHE A CG  1 
ATOM   3441 C CD1 . PHE A 1 533  ? 172.674 165.344 177.103 1.00 59.78  ? 533  PHE A CD1 1 
ATOM   3442 C CD2 . PHE A 1 533  ? 175.008 164.914 177.289 1.00 64.20  ? 533  PHE A CD2 1 
ATOM   3443 C CE1 . PHE A 1 533  ? 172.934 166.687 176.915 1.00 64.12  ? 533  PHE A CE1 1 
ATOM   3444 C CE2 . PHE A 1 533  ? 175.275 166.257 177.104 1.00 61.24  ? 533  PHE A CE2 1 
ATOM   3445 C CZ  . PHE A 1 533  ? 174.237 167.144 176.917 1.00 59.17  ? 533  PHE A CZ  1 
ATOM   3446 N N   . CYS A 1 534  ? 174.504 160.538 175.673 1.00 55.09  ? 534  CYS A N   1 
ATOM   3447 C CA  . CYS A 1 534  ? 175.542 159.927 174.851 1.00 57.20  ? 534  CYS A CA  1 
ATOM   3448 C C   . CYS A 1 534  ? 175.047 159.685 173.438 1.00 61.09  ? 534  CYS A C   1 
ATOM   3449 O O   . CYS A 1 534  ? 175.771 159.933 172.471 1.00 65.99  ? 534  CYS A O   1 
ATOM   3450 C CB  . CYS A 1 534  ? 176.008 158.611 175.472 1.00 51.13  ? 534  CYS A CB  1 
ATOM   3451 S SG  . CYS A 1 534  ? 177.210 158.774 176.798 1.00 71.88  ? 534  CYS A SG  1 
ATOM   3452 N N   . GLY A 1 535  ? 173.819 159.188 173.300 1.00 53.99  ? 535  GLY A N   1 
ATOM   3453 C CA  . GLY A 1 535  ? 173.263 159.015 171.967 1.00 49.86  ? 535  GLY A CA  1 
ATOM   3454 C C   . GLY A 1 535  ? 173.184 160.325 171.206 1.00 53.89  ? 535  GLY A C   1 
ATOM   3455 O O   . GLY A 1 535  ? 173.600 160.418 170.045 1.00 63.21  ? 535  GLY A O   1 
ATOM   3456 N N   . PHE A 1 536  ? 172.672 161.367 171.866 1.00 57.71  ? 536  PHE A N   1 
ATOM   3457 C CA  . PHE A 1 536  ? 172.546 162.662 171.200 1.00 47.14  ? 536  PHE A CA  1 
ATOM   3458 C C   . PHE A 1 536  ? 173.912 163.234 170.831 1.00 51.18  ? 536  PHE A C   1 
ATOM   3459 O O   . PHE A 1 536  ? 174.098 163.761 169.726 1.00 62.41  ? 536  PHE A O   1 
ATOM   3460 C CB  . PHE A 1 536  ? 171.779 163.634 172.092 1.00 47.16  ? 536  PHE A CB  1 
ATOM   3461 C CG  . PHE A 1 536  ? 171.309 164.864 171.380 1.00 54.22  ? 536  PHE A CG  1 
ATOM   3462 C CD1 . PHE A 1 536  ? 170.225 164.809 170.523 1.00 56.37  ? 536  PHE A CD1 1 
ATOM   3463 C CD2 . PHE A 1 536  ? 171.945 166.077 171.571 1.00 60.21  ? 536  PHE A CD2 1 
ATOM   3464 C CE1 . PHE A 1 536  ? 169.786 165.940 169.865 1.00 57.11  ? 536  PHE A CE1 1 
ATOM   3465 C CE2 . PHE A 1 536  ? 171.509 167.212 170.917 1.00 61.65  ? 536  PHE A CE2 1 
ATOM   3466 C CZ  . PHE A 1 536  ? 170.429 167.142 170.062 1.00 57.94  ? 536  PHE A CZ  1 
ATOM   3467 N N   . LEU A 1 537  ? 174.881 163.134 171.742 1.00 48.03  ? 537  LEU A N   1 
ATOM   3468 C CA  . LEU A 1 537  ? 176.213 163.664 171.480 1.00 40.56  ? 537  LEU A CA  1 
ATOM   3469 C C   . LEU A 1 537  ? 176.912 162.884 170.379 1.00 48.82  ? 537  LEU A C   1 
ATOM   3470 O O   . LEU A 1 537  ? 177.656 163.463 169.583 1.00 56.17  ? 537  LEU A O   1 
ATOM   3471 C CB  . LEU A 1 537  ? 177.046 163.645 172.758 1.00 39.15  ? 537  LEU A CB  1 
ATOM   3472 C CG  . LEU A 1 537  ? 176.671 164.673 173.821 1.00 43.61  ? 537  LEU A CG  1 
ATOM   3473 C CD1 . LEU A 1 537  ? 177.653 164.615 174.971 1.00 45.93  ? 537  LEU A CD1 1 
ATOM   3474 C CD2 . LEU A 1 537  ? 176.626 166.064 173.222 1.00 51.51  ? 537  LEU A CD2 1 
ATOM   3475 N N   . GLY A 1 538  ? 176.705 161.569 170.326 1.00 44.88  ? 538  GLY A N   1 
ATOM   3476 C CA  . GLY A 1 538  ? 177.253 160.795 169.230 1.00 43.63  ? 538  GLY A CA  1 
ATOM   3477 C C   . GLY A 1 538  ? 176.674 161.215 167.896 1.00 48.51  ? 538  GLY A C   1 
ATOM   3478 O O   . GLY A 1 538  ? 177.400 161.341 166.906 1.00 56.17  ? 538  GLY A O   1 
ATOM   3479 N N   . PHE A 1 539  ? 175.361 161.451 167.854 1.00 50.89  ? 539  PHE A N   1 
ATOM   3480 C CA  . PHE A 1 539  ? 174.753 161.958 166.628 1.00 37.12  ? 539  PHE A CA  1 
ATOM   3481 C C   . PHE A 1 539  ? 175.382 163.282 166.216 1.00 41.45  ? 539  PHE A C   1 
ATOM   3482 O O   . PHE A 1 539  ? 175.758 163.472 165.051 1.00 47.45  ? 539  PHE A O   1 
ATOM   3483 C CB  . PHE A 1 539  ? 173.246 162.119 166.809 1.00 35.01  ? 539  PHE A CB  1 
ATOM   3484 C CG  . PHE A 1 539  ? 172.629 163.107 165.864 1.00 41.17  ? 539  PHE A CG  1 
ATOM   3485 C CD1 . PHE A 1 539  ? 172.470 162.801 164.526 1.00 47.72  ? 539  PHE A CD1 1 
ATOM   3486 C CD2 . PHE A 1 539  ? 172.209 164.344 166.314 1.00 50.03  ? 539  PHE A CD2 1 
ATOM   3487 C CE1 . PHE A 1 539  ? 171.905 163.709 163.656 1.00 44.41  ? 539  PHE A CE1 1 
ATOM   3488 C CE2 . PHE A 1 539  ? 171.644 165.254 165.448 1.00 49.56  ? 539  PHE A CE2 1 
ATOM   3489 C CZ  . PHE A 1 539  ? 171.493 164.937 164.119 1.00 42.45  ? 539  PHE A CZ  1 
ATOM   3490 N N   . LEU A 1 540  ? 175.508 164.211 167.167 1.00 44.56  ? 540  LEU A N   1 
ATOM   3491 C CA  . LEU A 1 540  ? 176.068 165.520 166.846 1.00 40.81  ? 540  LEU A CA  1 
ATOM   3492 C C   . LEU A 1 540  ? 177.507 165.407 166.359 1.00 47.50  ? 540  LEU A C   1 
ATOM   3493 O O   . LEU A 1 540  ? 177.884 166.039 165.366 1.00 56.65  ? 540  LEU A O   1 
ATOM   3494 C CB  . LEU A 1 540  ? 175.990 166.441 168.061 1.00 49.34  ? 540  LEU A CB  1 
ATOM   3495 C CG  . LEU A 1 540  ? 174.599 166.927 168.462 1.00 50.38  ? 540  LEU A CG  1 
ATOM   3496 C CD1 . LEU A 1 540  ? 174.699 167.935 169.592 1.00 45.63  ? 540  LEU A CD1 1 
ATOM   3497 C CD2 . LEU A 1 540  ? 173.885 167.529 167.268 1.00 48.85  ? 540  LEU A CD2 1 
ATOM   3498 N N   . SER A 1 541  ? 178.323 164.603 167.042 1.00 45.62  ? 541  SER A N   1 
ATOM   3499 C CA  . SER A 1 541  ? 179.725 164.472 166.664 1.00 45.25  ? 541  SER A CA  1 
ATOM   3500 C C   . SER A 1 541  ? 179.872 163.832 165.292 1.00 51.97  ? 541  SER A C   1 
ATOM   3501 O O   . SER A 1 541  ? 180.694 164.274 164.481 1.00 60.26  ? 541  SER A O   1 
ATOM   3502 C CB  . SER A 1 541  ? 180.478 163.660 167.715 1.00 47.39  ? 541  SER A CB  1 
ATOM   3503 O OG  . SER A 1 541  ? 180.426 164.295 168.979 1.00 56.03  ? 541  SER A OG  1 
ATOM   3504 N N   . GLY A 1 542  ? 179.089 162.790 165.010 1.00 49.13  ? 542  GLY A N   1 
ATOM   3505 C CA  . GLY A 1 542  ? 179.166 162.163 163.701 1.00 44.19  ? 542  GLY A CA  1 
ATOM   3506 C C   . GLY A 1 542  ? 178.739 163.094 162.585 1.00 51.11  ? 542  GLY A C   1 
ATOM   3507 O O   . GLY A 1 542  ? 179.398 163.174 161.541 1.00 60.49  ? 542  GLY A O   1 
ATOM   3508 N N   . SER A 1 543  ? 177.635 163.817 162.788 1.00 45.93  ? 543  SER A N   1 
ATOM   3509 C CA  . SER A 1 543  ? 177.195 164.769 161.777 1.00 45.12  ? 543  SER A CA  1 
ATOM   3510 C C   . SER A 1 543  ? 178.239 165.854 161.556 1.00 44.03  ? 543  SER A C   1 
ATOM   3511 O O   . SER A 1 543  ? 178.519 166.229 160.413 1.00 55.20  ? 543  SER A O   1 
ATOM   3512 C CB  . SER A 1 543  ? 175.857 165.381 162.182 1.00 49.55  ? 543  SER A CB  1 
ATOM   3513 O OG  . SER A 1 543  ? 174.864 164.381 162.313 1.00 47.99  ? 543  SER A OG  1 
ATOM   3514 N N   . GLY A 1 544  ? 178.832 166.365 162.636 1.00 38.30  ? 544  GLY A N   1 
ATOM   3515 C CA  . GLY A 1 544  ? 179.858 167.381 162.487 1.00 45.22  ? 544  GLY A CA  1 
ATOM   3516 C C   . GLY A 1 544  ? 181.085 166.871 161.758 1.00 47.17  ? 544  GLY A C   1 
ATOM   3517 O O   . GLY A 1 544  ? 181.661 167.574 160.926 1.00 52.77  ? 544  GLY A O   1 
ATOM   3518 N N   . PHE A 1 545  ? 181.503 165.642 162.061 1.00 46.97  ? 545  PHE A N   1 
ATOM   3519 C CA  . PHE A 1 545  ? 182.653 165.068 161.374 1.00 47.63  ? 545  PHE A CA  1 
ATOM   3520 C C   . PHE A 1 545  ? 182.382 164.917 159.885 1.00 49.87  ? 545  PHE A C   1 
ATOM   3521 O O   . PHE A 1 545  ? 183.232 165.256 159.051 1.00 55.46  ? 545  PHE A O   1 
ATOM   3522 C CB  . PHE A 1 545  ? 183.009 163.720 161.996 1.00 51.86  ? 545  PHE A CB  1 
ATOM   3523 C CG  . PHE A 1 545  ? 184.170 163.038 161.342 1.00 54.82  ? 545  PHE A CG  1 
ATOM   3524 C CD1 . PHE A 1 545  ? 185.462 163.472 161.569 1.00 54.57  ? 545  PHE A CD1 1 
ATOM   3525 C CD2 . PHE A 1 545  ? 183.972 161.951 160.512 1.00 51.79  ? 545  PHE A CD2 1 
ATOM   3526 C CE1 . PHE A 1 545  ? 186.533 162.843 160.972 1.00 55.93  ? 545  PHE A CE1 1 
ATOM   3527 C CE2 . PHE A 1 545  ? 185.038 161.317 159.914 1.00 50.63  ? 545  PHE A CE2 1 
ATOM   3528 C CZ  . PHE A 1 545  ? 186.320 161.764 160.144 1.00 55.01  ? 545  PHE A CZ  1 
ATOM   3529 N N   . LEU A 1 546  ? 181.196 164.426 159.526 1.00 50.65  ? 546  LEU A N   1 
ATOM   3530 C CA  . LEU A 1 546  ? 180.898 164.254 158.109 1.00 47.74  ? 546  LEU A CA  1 
ATOM   3531 C C   . LEU A 1 546  ? 180.754 165.597 157.403 1.00 47.25  ? 546  LEU A C   1 
ATOM   3532 O O   . LEU A 1 546  ? 181.127 165.728 156.232 1.00 55.66  ? 546  LEU A O   1 
ATOM   3533 C CB  . LEU A 1 546  ? 179.648 163.401 157.929 1.00 43.34  ? 546  LEU A CB  1 
ATOM   3534 C CG  . LEU A 1 546  ? 179.920 161.912 158.123 1.00 36.07  ? 546  LEU A CG  1 
ATOM   3535 C CD1 . LEU A 1 546  ? 178.745 161.097 157.657 1.00 46.87  ? 546  LEU A CD1 1 
ATOM   3536 C CD2 . LEU A 1 546  ? 181.172 161.504 157.374 1.00 44.11  ? 546  LEU A CD2 1 
ATOM   3537 N N   . TYR A 1 547  ? 180.219 166.607 158.091 1.00 54.48  ? 547  TYR A N   1 
ATOM   3538 C CA  . TYR A 1 547  ? 180.181 167.946 157.513 1.00 47.76  ? 547  TYR A CA  1 
ATOM   3539 C C   . TYR A 1 547  ? 181.587 168.479 157.284 1.00 42.89  ? 547  TYR A C   1 
ATOM   3540 O O   . TYR A 1 547  ? 181.858 169.121 156.263 1.00 42.34  ? 547  TYR A O   1 
ATOM   3541 C CB  . TYR A 1 547  ? 179.387 168.888 158.414 1.00 45.80  ? 547  TYR A CB  1 
ATOM   3542 C CG  . TYR A 1 547  ? 177.908 168.601 158.425 1.00 47.45  ? 547  TYR A CG  1 
ATOM   3543 C CD1 . TYR A 1 547  ? 177.282 168.063 157.314 1.00 48.17  ? 547  TYR A CD1 1 
ATOM   3544 C CD2 . TYR A 1 547  ? 177.140 168.863 159.545 1.00 47.13  ? 547  TYR A CD2 1 
ATOM   3545 C CE1 . TYR A 1 547  ? 175.933 167.801 157.317 1.00 53.55  ? 547  TYR A CE1 1 
ATOM   3546 C CE2 . TYR A 1 547  ? 175.789 168.599 159.559 1.00 44.27  ? 547  TYR A CE2 1 
ATOM   3547 C CZ  . TYR A 1 547  ? 175.191 168.068 158.442 1.00 50.52  ? 547  TYR A CZ  1 
ATOM   3548 O OH  . TYR A 1 547  ? 173.843 167.804 158.449 1.00 59.21  ? 547  TYR A OH  1 
ATOM   3549 N N   . PHE A 1 548  ? 182.494 168.229 158.230 1.00 56.25  ? 548  PHE A N   1 
ATOM   3550 C CA  . PHE A 1 548  ? 183.900 168.540 158.004 1.00 56.34  ? 548  PHE A CA  1 
ATOM   3551 C C   . PHE A 1 548  ? 184.429 167.829 156.770 1.00 61.28  ? 548  PHE A C   1 
ATOM   3552 O O   . PHE A 1 548  ? 185.221 168.402 156.015 1.00 67.30  ? 548  PHE A O   1 
ATOM   3553 C CB  . PHE A 1 548  ? 184.730 168.152 159.227 1.00 58.12  ? 548  PHE A CB  1 
ATOM   3554 C CG  . PHE A 1 548  ? 184.864 169.245 160.245 1.00 58.02  ? 548  PHE A CG  1 
ATOM   3555 C CD1 . PHE A 1 548  ? 184.852 170.571 159.862 1.00 57.81  ? 548  PHE A CD1 1 
ATOM   3556 C CD2 . PHE A 1 548  ? 185.009 168.942 161.587 1.00 58.97  ? 548  PHE A CD2 1 
ATOM   3557 C CE1 . PHE A 1 548  ? 184.980 171.576 160.799 1.00 63.08  ? 548  PHE A CE1 1 
ATOM   3558 C CE2 . PHE A 1 548  ? 185.135 169.942 162.527 1.00 54.45  ? 548  PHE A CE2 1 
ATOM   3559 C CZ  . PHE A 1 548  ? 185.122 171.260 162.133 1.00 57.75  ? 548  PHE A CZ  1 
ATOM   3560 N N   . LEU A 1 549  ? 184.002 166.587 156.543 1.00 53.12  ? 549  LEU A N   1 
ATOM   3561 C CA  . LEU A 1 549  ? 184.422 165.863 155.351 1.00 52.17  ? 549  LEU A CA  1 
ATOM   3562 C C   . LEU A 1 549  ? 183.715 166.331 154.085 1.00 53.37  ? 549  LEU A C   1 
ATOM   3563 O O   . LEU A 1 549  ? 184.138 165.955 152.988 1.00 58.52  ? 549  LEU A O   1 
ATOM   3564 C CB  . LEU A 1 549  ? 184.199 164.363 155.536 1.00 49.03  ? 549  LEU A CB  1 
ATOM   3565 C CG  . LEU A 1 549  ? 185.109 163.696 156.565 1.00 53.15  ? 549  LEU A CG  1 
ATOM   3566 C CD1 . LEU A 1 549  ? 185.026 162.186 156.444 1.00 54.06  ? 549  LEU A CD1 1 
ATOM   3567 C CD2 . LEU A 1 549  ? 186.541 164.173 156.400 1.00 55.26  ? 549  LEU A CD2 1 
ATOM   3568 N N   . GLY A 1 550  ? 182.658 167.131 154.203 1.00 52.88  ? 550  GLY A N   1 
ATOM   3569 C CA  . GLY A 1 550  ? 182.016 167.725 153.051 1.00 51.72  ? 550  GLY A CA  1 
ATOM   3570 C C   . GLY A 1 550  ? 180.761 167.037 152.561 1.00 52.36  ? 550  GLY A C   1 
ATOM   3571 O O   . GLY A 1 550  ? 180.210 167.458 151.538 1.00 60.92  ? 550  GLY A O   1 
ATOM   3572 N N   . VAL A 1 551  ? 180.291 165.996 153.246 1.00 49.45  ? 551  VAL A N   1 
ATOM   3573 C CA  . VAL A 1 551  ? 179.073 165.318 152.822 1.00 49.26  ? 551  VAL A CA  1 
ATOM   3574 C C   . VAL A 1 551  ? 177.878 166.230 153.061 1.00 58.65  ? 551  VAL A C   1 
ATOM   3575 O O   . VAL A 1 551  ? 177.725 166.810 154.142 1.00 62.66  ? 551  VAL A O   1 
ATOM   3576 C CB  . VAL A 1 551  ? 178.913 163.984 153.564 1.00 50.00  ? 551  VAL A CB  1 
ATOM   3577 C CG1 . VAL A 1 551  ? 177.692 163.245 153.059 1.00 51.89  ? 551  VAL A CG1 1 
ATOM   3578 C CG2 . VAL A 1 551  ? 180.158 163.137 153.393 1.00 48.22  ? 551  VAL A CG2 1 
ATOM   3579 N N   . LYS A 1 552  ? 177.027 166.364 152.050 1.00 63.62  ? 552  LYS A N   1 
ATOM   3580 C CA  . LYS A 1 552  ? 175.860 167.227 152.140 1.00 60.22  ? 552  LYS A CA  1 
ATOM   3581 C C   . LYS A 1 552  ? 174.681 166.476 152.744 1.00 61.27  ? 552  LYS A C   1 
ATOM   3582 O O   . LYS A 1 552  ? 174.538 165.263 152.574 1.00 68.37  ? 552  LYS A O   1 
ATOM   3583 C CB  . LYS A 1 552  ? 175.485 167.773 150.763 1.00 65.68  ? 552  LYS A CB  1 
ATOM   3584 C CG  . LYS A 1 552  ? 176.592 168.580 150.106 1.00 63.42  ? 552  LYS A CG  1 
ATOM   3585 C CD  . LYS A 1 552  ? 176.117 169.233 148.823 1.00 69.22  ? 552  LYS A CD  1 
ATOM   3586 C CE  . LYS A 1 552  ? 177.209 170.084 148.201 1.00 70.84  ? 552  LYS A CE  1 
ATOM   3587 N NZ  . LYS A 1 552  ? 176.733 170.777 146.973 1.00 69.37  ? 552  LYS A NZ  1 
ATOM   3588 N N   . SER A 1 553  ? 173.831 167.214 153.452 1.00 60.45  ? 553  SER A N   1 
ATOM   3589 C CA  . SER A 1 553  ? 172.721 166.625 154.193 1.00 58.91  ? 553  SER A CA  1 
ATOM   3590 C C   . SER A 1 553  ? 171.516 166.462 153.275 1.00 61.08  ? 553  SER A C   1 
ATOM   3591 O O   . SER A 1 553  ? 170.981 167.445 152.756 1.00 66.35  ? 553  SER A O   1 
ATOM   3592 C CB  . SER A 1 553  ? 172.370 167.491 155.398 1.00 61.58  ? 553  SER A CB  1 
ATOM   3593 O OG  . SER A 1 553  ? 171.241 166.976 156.077 1.00 67.85  ? 553  SER A OG  1 
ATOM   3594 N N   . VAL A 1 554  ? 171.086 165.220 153.080 1.00 55.85  ? 554  VAL A N   1 
ATOM   3595 C CA  . VAL A 1 554  ? 169.899 164.911 152.290 1.00 56.37  ? 554  VAL A CA  1 
ATOM   3596 C C   . VAL A 1 554  ? 168.676 165.003 153.194 1.00 62.39  ? 554  VAL A C   1 
ATOM   3597 O O   . VAL A 1 554  ? 168.814 164.913 154.421 1.00 62.99  ? 554  VAL A O   1 
ATOM   3598 C CB  . VAL A 1 554  ? 170.018 163.525 151.644 1.00 58.86  ? 554  VAL A CB  1 
ATOM   3599 C CG1 . VAL A 1 554  ? 171.227 163.486 150.741 1.00 57.36  ? 554  VAL A CG1 1 
ATOM   3600 C CG2 . VAL A 1 554  ? 170.121 162.459 152.713 1.00 56.30  ? 554  VAL A CG2 1 
ATOM   3601 N N   . PRO A 1 555  ? 167.478 165.205 152.652 1.00 66.88  ? 555  PRO A N   1 
ATOM   3602 C CA  . PRO A 1 555  ? 166.281 165.307 153.500 1.00 62.63  ? 555  PRO A CA  1 
ATOM   3603 C C   . PRO A 1 555  ? 166.051 164.063 154.347 1.00 64.96  ? 555  PRO A C   1 
ATOM   3604 O O   . PRO A 1 555  ? 165.622 164.190 155.505 1.00 68.24  ? 555  PRO A O   1 
ATOM   3605 C CB  . PRO A 1 555  ? 165.149 165.527 152.486 1.00 56.89  ? 555  PRO A CB  1 
ATOM   3606 C CG  . PRO A 1 555  ? 165.819 166.191 151.340 1.00 57.27  ? 555  PRO A CG  1 
ATOM   3607 C CD  . PRO A 1 555  ? 167.202 165.608 151.262 1.00 63.18  ? 555  PRO A CD  1 
ATOM   3608 N N   . PRO A 1 556  ? 166.320 162.849 153.841 1.00 51.71  ? 556  PRO A N   1 
ATOM   3609 C CA  . PRO A 1 556  ? 166.211 161.667 154.716 1.00 45.58  ? 556  PRO A CA  1 
ATOM   3610 C C   . PRO A 1 556  ? 166.987 161.784 156.016 1.00 48.01  ? 556  PRO A C   1 
ATOM   3611 O O   . PRO A 1 556  ? 166.599 161.147 157.005 1.00 59.29  ? 556  PRO A O   1 
ATOM   3612 C CB  . PRO A 1 556  ? 166.772 160.530 153.855 1.00 50.49  ? 556  PRO A CB  1 
ATOM   3613 C CG  . PRO A 1 556  ? 166.672 160.990 152.461 1.00 50.20  ? 556  PRO A CG  1 
ATOM   3614 C CD  . PRO A 1 556  ? 166.315 162.440 152.424 1.00 51.35  ? 556  PRO A CD  1 
ATOM   3615 N N   . ALA A 1 557  ? 168.044 162.595 156.061 1.00 55.50  ? 557  ALA A N   1 
ATOM   3616 C CA  . ALA A 1 557  ? 168.827 162.741 157.279 1.00 52.26  ? 557  ALA A CA  1 
ATOM   3617 C C   . ALA A 1 557  ? 168.015 163.311 158.431 1.00 58.66  ? 557  ALA A C   1 
ATOM   3618 O O   . ALA A 1 557  ? 168.477 163.253 159.574 1.00 61.28  ? 557  ALA A O   1 
ATOM   3619 C CB  . ALA A 1 557  ? 170.047 163.623 157.024 1.00 54.16  ? 557  ALA A CB  1 
ATOM   3620 N N   . GLU A 1 558  ? 166.827 163.860 158.164 1.00 67.62  ? 558  GLU A N   1 
ATOM   3621 C CA  . GLU A 1 558  ? 165.968 164.305 159.255 1.00 61.84  ? 558  GLU A CA  1 
ATOM   3622 C C   . GLU A 1 558  ? 165.615 163.149 160.180 1.00 61.63  ? 558  GLU A C   1 
ATOM   3623 O O   . GLU A 1 558  ? 165.346 163.356 161.368 1.00 65.25  ? 558  GLU A O   1 
ATOM   3624 C CB  . GLU A 1 558  ? 164.699 164.952 158.703 1.00 59.86  ? 558  GLU A CB  1 
ATOM   3625 C CG  . GLU A 1 558  ? 163.703 163.966 158.122 1.00 61.61  ? 558  GLU A CG  1 
ATOM   3626 C CD  . GLU A 1 558  ? 162.360 164.601 157.835 1.00 70.56  ? 558  GLU A CD  1 
ATOM   3627 O OE1 . GLU A 1 558  ? 162.319 165.825 157.594 1.00 74.90  ? 558  GLU A OE1 1 
ATOM   3628 O OE2 . GLU A 1 558  ? 161.345 163.875 157.859 1.00 68.04  ? 558  GLU A OE2 1 
ATOM   3629 N N   . THR A 1 559  ? 165.607 161.922 159.657 1.00 56.37  ? 559  THR A N   1 
ATOM   3630 C CA  . THR A 1 559  ? 165.326 160.762 160.492 1.00 51.31  ? 559  THR A CA  1 
ATOM   3631 C C   . THR A 1 559  ? 166.576 160.176 161.128 1.00 55.66  ? 559  THR A C   1 
ATOM   3632 O O   . THR A 1 559  ? 166.465 159.209 161.887 1.00 64.83  ? 559  THR A O   1 
ATOM   3633 C CB  . THR A 1 559  ? 164.619 159.678 159.680 1.00 46.21  ? 559  THR A CB  1 
ATOM   3634 O OG1 . THR A 1 559  ? 165.443 159.298 158.572 1.00 49.46  ? 559  THR A OG1 1 
ATOM   3635 C CG2 . THR A 1 559  ? 163.291 160.189 159.165 1.00 55.35  ? 559  THR A CG2 1 
ATOM   3636 N N   . VAL A 1 560  ? 167.753 160.725 160.830 1.00 40.32  ? 560  VAL A N   1 
ATOM   3637 C CA  . VAL A 1 560  ? 168.979 160.228 161.453 1.00 36.08  ? 560  VAL A CA  1 
ATOM   3638 C C   . VAL A 1 560  ? 168.947 160.332 162.972 1.00 43.80  ? 560  VAL A C   1 
ATOM   3639 O O   . VAL A 1 560  ? 169.310 159.350 163.640 1.00 47.36  ? 560  VAL A O   1 
ATOM   3640 C CB  . VAL A 1 560  ? 170.205 160.929 160.839 1.00 45.27  ? 560  VAL A CB  1 
ATOM   3641 C CG1 . VAL A 1 560  ? 171.420 160.731 161.721 1.00 41.78  ? 560  VAL A CG1 1 
ATOM   3642 C CG2 . VAL A 1 560  ? 170.472 160.385 159.454 1.00 47.28  ? 560  VAL A CG2 1 
ATOM   3643 N N   . PRO A 1 561  ? 168.541 161.456 163.584 1.00 46.72  ? 561  PRO A N   1 
ATOM   3644 C CA  . PRO A 1 561  ? 168.597 161.523 165.054 1.00 35.72  ? 561  PRO A CA  1 
ATOM   3645 C C   . PRO A 1 561  ? 167.823 160.415 165.739 1.00 47.98  ? 561  PRO A C   1 
ATOM   3646 O O   . PRO A 1 561  ? 168.419 159.633 166.493 1.00 50.94  ? 561  PRO A O   1 
ATOM   3647 C CB  . PRO A 1 561  ? 167.997 162.900 165.364 1.00 41.26  ? 561  PRO A CB  1 
ATOM   3648 C CG  . PRO A 1 561  ? 168.223 163.688 164.148 1.00 45.93  ? 561  PRO A CG  1 
ATOM   3649 C CD  . PRO A 1 561  ? 168.084 162.734 163.010 1.00 49.70  ? 561  PRO A CD  1 
ATOM   3650 N N   . PHE A 1 562  ? 166.518 160.311 165.462 1.00 57.07  ? 562  PHE A N   1 
ATOM   3651 C CA  . PHE A 1 562  ? 165.675 159.308 166.108 1.00 48.81  ? 562  PHE A CA  1 
ATOM   3652 C C   . PHE A 1 562  ? 166.366 157.955 166.144 1.00 50.11  ? 562  PHE A C   1 
ATOM   3653 O O   . PHE A 1 562  ? 166.727 157.453 167.217 1.00 53.29  ? 562  PHE A O   1 
ATOM   3654 C CB  . PHE A 1 562  ? 164.344 159.176 165.365 1.00 45.17  ? 562  PHE A CB  1 
ATOM   3655 C CG  . PHE A 1 562  ? 163.582 160.460 165.218 1.00 47.06  ? 562  PHE A CG  1 
ATOM   3656 C CD1 . PHE A 1 562  ? 163.916 161.373 164.236 1.00 49.42  ? 562  PHE A CD1 1 
ATOM   3657 C CD2 . PHE A 1 562  ? 162.506 160.735 166.038 1.00 47.73  ? 562  PHE A CD2 1 
ATOM   3658 C CE1 . PHE A 1 562  ? 163.208 162.546 164.092 1.00 53.41  ? 562  PHE A CE1 1 
ATOM   3659 C CE2 . PHE A 1 562  ? 161.792 161.901 165.894 1.00 49.99  ? 562  PHE A CE2 1 
ATOM   3660 C CZ  . PHE A 1 562  ? 162.146 162.810 164.923 1.00 48.66  ? 562  PHE A CZ  1 
ATOM   3661 N N   . LEU A 1 563  ? 166.619 157.389 164.964 1.00 46.49  ? 563  LEU A N   1 
ATOM   3662 C CA  . LEU A 1 563  ? 167.218 156.066 164.873 1.00 47.39  ? 563  LEU A CA  1 
ATOM   3663 C C   . LEU A 1 563  ? 168.485 155.976 165.709 1.00 47.72  ? 563  LEU A C   1 
ATOM   3664 O O   . LEU A 1 563  ? 168.646 155.038 166.499 1.00 56.95  ? 563  LEU A O   1 
ATOM   3665 C CB  . LEU A 1 563  ? 167.508 155.734 163.412 1.00 46.86  ? 563  LEU A CB  1 
ATOM   3666 C CG  . LEU A 1 563  ? 168.014 154.327 163.131 1.00 57.55  ? 563  LEU A CG  1 
ATOM   3667 C CD1 . LEU A 1 563  ? 167.041 153.315 163.696 1.00 56.39  ? 563  LEU A CD1 1 
ATOM   3668 C CD2 . LEU A 1 563  ? 168.191 154.131 161.639 1.00 56.43  ? 563  LEU A CD2 1 
ATOM   3669 N N   . VAL A 1 564  ? 169.368 156.971 165.592 1.00 42.88  ? 564  VAL A N   1 
ATOM   3670 C CA  . VAL A 1 564  ? 170.631 156.919 166.321 1.00 40.93  ? 564  VAL A CA  1 
ATOM   3671 C C   . VAL A 1 564  ? 170.369 156.825 167.815 1.00 51.62  ? 564  VAL A C   1 
ATOM   3672 O O   . VAL A 1 564  ? 170.914 155.955 168.506 1.00 54.75  ? 564  VAL A O   1 
ATOM   3673 C CB  . VAL A 1 564  ? 171.505 158.135 165.973 1.00 40.41  ? 564  VAL A CB  1 
ATOM   3674 C CG1 . VAL A 1 564  ? 172.649 158.255 166.958 1.00 37.72  ? 564  VAL A CG1 1 
ATOM   3675 C CG2 . VAL A 1 564  ? 172.036 158.001 164.564 1.00 41.72  ? 564  VAL A CG2 1 
ATOM   3676 N N   . ILE A 1 565  ? 169.479 157.678 168.324 1.00 53.75  ? 565  ILE A N   1 
ATOM   3677 C CA  . ILE A 1 565  ? 169.146 157.603 169.740 1.00 48.46  ? 565  ILE A CA  1 
ATOM   3678 C C   . ILE A 1 565  ? 168.559 156.240 170.061 1.00 48.76  ? 565  ILE A C   1 
ATOM   3679 O O   . ILE A 1 565  ? 168.950 155.597 171.042 1.00 58.20  ? 565  ILE A O   1 
ATOM   3680 C CB  . ILE A 1 565  ? 168.194 158.745 170.132 1.00 52.24  ? 565  ILE A CB  1 
ATOM   3681 C CG1 . ILE A 1 565  ? 168.867 160.095 169.898 1.00 53.26  ? 565  ILE A CG1 1 
ATOM   3682 C CG2 . ILE A 1 565  ? 167.788 158.617 171.584 1.00 54.83  ? 565  ILE A CG2 1 
ATOM   3683 C CD1 . ILE A 1 565  ? 168.018 161.272 170.303 1.00 45.84  ? 565  ILE A CD1 1 
ATOM   3684 N N   . GLY A 1 566  ? 167.666 155.748 169.199 1.00 52.18  ? 566  GLY A N   1 
ATOM   3685 C CA  . GLY A 1 566  ? 167.064 154.449 169.434 1.00 50.24  ? 566  GLY A CA  1 
ATOM   3686 C C   . GLY A 1 566  ? 168.095 153.345 169.549 1.00 52.16  ? 566  GLY A C   1 
ATOM   3687 O O   . GLY A 1 566  ? 167.864 152.332 170.211 1.00 54.40  ? 566  GLY A O   1 
ATOM   3688 N N   . VAL A 1 567  ? 169.251 153.528 168.910 1.00 49.27  ? 567  VAL A N   1 
ATOM   3689 C CA  . VAL A 1 567  ? 170.319 152.552 169.065 1.00 51.89  ? 567  VAL A CA  1 
ATOM   3690 C C   . VAL A 1 567  ? 171.291 152.960 170.161 1.00 57.99  ? 567  VAL A C   1 
ATOM   3691 O O   . VAL A 1 567  ? 171.820 152.090 170.866 1.00 55.88  ? 567  VAL A O   1 
ATOM   3692 C CB  . VAL A 1 567  ? 171.053 152.349 167.731 1.00 43.68  ? 567  VAL A CB  1 
ATOM   3693 C CG1 . VAL A 1 567  ? 172.036 151.200 167.836 1.00 53.05  ? 567  VAL A CG1 1 
ATOM   3694 C CG2 . VAL A 1 567  ? 170.055 152.092 166.622 1.00 46.21  ? 567  VAL A CG2 1 
ATOM   3695 N N   . GLY A 1 568  ? 171.500 154.263 170.359 1.00 58.16  ? 568  GLY A N   1 
ATOM   3696 C CA  . GLY A 1 568  ? 172.522 154.717 171.284 1.00 60.84  ? 568  GLY A CA  1 
ATOM   3697 C C   . GLY A 1 568  ? 172.271 154.321 172.721 1.00 71.39  ? 568  GLY A C   1 
ATOM   3698 O O   . GLY A 1 568  ? 173.205 154.331 173.529 1.00 77.78  ? 568  GLY A O   1 
ATOM   3699 N N   . VAL A 1 569  ? 171.029 153.972 173.058 1.00 61.34  ? 569  VAL A N   1 
ATOM   3700 C CA  . VAL A 1 569  ? 170.712 153.529 174.411 1.00 57.13  ? 569  VAL A CA  1 
ATOM   3701 C C   . VAL A 1 569  ? 170.917 152.038 174.600 1.00 61.12  ? 569  VAL A C   1 
ATOM   3702 O O   . VAL A 1 569  ? 171.150 151.598 175.733 1.00 66.71  ? 569  VAL A O   1 
ATOM   3703 C CB  . VAL A 1 569  ? 169.262 153.902 174.766 1.00 56.50  ? 569  VAL A CB  1 
ATOM   3704 C CG1 . VAL A 1 569  ? 169.056 153.876 176.266 1.00 60.36  ? 569  VAL A CG1 1 
ATOM   3705 C CG2 . VAL A 1 569  ? 168.923 155.266 174.210 1.00 56.24  ? 569  VAL A CG2 1 
ATOM   3706 N N   . ASP A 1 570  ? 170.870 151.251 173.519 1.00 55.46  ? 570  ASP A N   1 
ATOM   3707 C CA  . ASP A 1 570  ? 170.889 149.798 173.663 1.00 60.83  ? 570  ASP A CA  1 
ATOM   3708 C C   . ASP A 1 570  ? 172.105 149.335 174.449 1.00 67.13  ? 570  ASP A C   1 
ATOM   3709 O O   . ASP A 1 570  ? 171.968 148.651 175.472 1.00 74.61  ? 570  ASP A O   1 
ATOM   3710 C CB  . ASP A 1 570  ? 170.865 149.133 172.287 1.00 65.39  ? 570  ASP A CB  1 
ATOM   3711 C CG  . ASP A 1 570  ? 169.623 149.479 171.494 1.00 74.24  ? 570  ASP A CG  1 
ATOM   3712 O OD1 . ASP A 1 570  ? 168.786 150.251 172.004 1.00 72.86  ? 570  ASP A OD1 1 
ATOM   3713 O OD2 . ASP A 1 570  ? 169.480 148.973 170.361 1.00 69.49  ? 570  ASP A OD2 1 
ATOM   3714 N N   . ASP A 1 571  ? 173.298 149.750 174.020 1.00 58.29  ? 571  ASP A N   1 
ATOM   3715 C CA  . ASP A 1 571  ? 174.516 149.360 174.718 1.00 50.69  ? 571  ASP A CA  1 
ATOM   3716 C C   . ASP A 1 571  ? 174.434 149.720 176.192 1.00 57.47  ? 571  ASP A C   1 
ATOM   3717 O O   . ASP A 1 571  ? 174.815 148.918 177.055 1.00 68.13  ? 571  ASP A O   1 
ATOM   3718 C CB  . ASP A 1 571  ? 175.724 150.027 174.067 1.00 62.08  ? 571  ASP A CB  1 
ATOM   3719 C CG  . ASP A 1 571  ? 175.745 149.849 172.562 1.00 73.13  ? 571  ASP A CG  1 
ATOM   3720 O OD1 . ASP A 1 571  ? 175.361 148.761 172.086 1.00 72.35  ? 571  ASP A OD1 1 
ATOM   3721 O OD2 . ASP A 1 571  ? 176.140 150.799 171.854 1.00 67.58  ? 571  ASP A OD2 1 
ATOM   3722 N N   . VAL A 1 572  ? 173.897 150.905 176.495 1.00 52.66  ? 572  VAL A N   1 
ATOM   3723 C CA  . VAL A 1 572  ? 173.713 151.317 177.882 1.00 54.06  ? 572  VAL A CA  1 
ATOM   3724 C C   . VAL A 1 572  ? 173.063 150.201 178.681 1.00 50.21  ? 572  VAL A C   1 
ATOM   3725 O O   . VAL A 1 572  ? 173.637 149.702 179.659 1.00 58.10  ? 572  VAL A O   1 
ATOM   3726 C CB  . VAL A 1 572  ? 172.878 152.608 177.951 1.00 49.85  ? 572  VAL A CB  1 
ATOM   3727 C CG1 . VAL A 1 572  ? 172.826 153.125 179.375 1.00 46.92  ? 572  VAL A CG1 1 
ATOM   3728 C CG2 . VAL A 1 572  ? 173.434 153.657 177.005 1.00 52.96  ? 572  VAL A CG2 1 
ATOM   3729 N N   . PHE A 1 573  ? 171.888 149.745 178.235 1.00 48.03  ? 573  PHE A N   1 
ATOM   3730 C CA  . PHE A 1 573  ? 171.172 148.720 178.982 1.00 44.59  ? 573  PHE A CA  1 
ATOM   3731 C C   . PHE A 1 573  ? 172.055 147.509 179.216 1.00 47.41  ? 573  PHE A C   1 
ATOM   3732 O O   . PHE A 1 573  ? 172.152 147.014 180.346 1.00 54.46  ? 573  PHE A O   1 
ATOM   3733 C CB  . PHE A 1 573  ? 169.896 148.319 178.248 1.00 48.84  ? 573  PHE A CB  1 
ATOM   3734 C CG  . PHE A 1 573  ? 168.776 149.302 178.401 1.00 54.66  ? 573  PHE A CG  1 
ATOM   3735 C CD1 . PHE A 1 573  ? 168.065 149.378 179.583 1.00 56.67  ? 573  PHE A CD1 1 
ATOM   3736 C CD2 . PHE A 1 573  ? 168.430 150.145 177.364 1.00 57.30  ? 573  PHE A CD2 1 
ATOM   3737 C CE1 . PHE A 1 573  ? 167.033 150.279 179.729 1.00 59.18  ? 573  PHE A CE1 1 
ATOM   3738 C CE2 . PHE A 1 573  ? 167.399 151.047 177.505 1.00 56.71  ? 573  PHE A CE2 1 
ATOM   3739 C CZ  . PHE A 1 573  ? 166.701 151.114 178.689 1.00 59.58  ? 573  PHE A CZ  1 
ATOM   3740 N N   . VAL A 1 574  ? 172.767 147.066 178.176 1.00 50.45  ? 574  VAL A N   1 
ATOM   3741 C CA  . VAL A 1 574  ? 173.602 145.881 178.317 1.00 48.29  ? 574  VAL A CA  1 
ATOM   3742 C C   . VAL A 1 574  ? 174.576 146.067 179.466 1.00 51.22  ? 574  VAL A C   1 
ATOM   3743 O O   . VAL A 1 574  ? 174.651 145.229 180.374 1.00 56.49  ? 574  VAL A O   1 
ATOM   3744 C CB  . VAL A 1 574  ? 174.333 145.578 176.998 1.00 42.53  ? 574  VAL A CB  1 
ATOM   3745 C CG1 . VAL A 1 574  ? 175.108 144.283 177.116 1.00 47.68  ? 574  VAL A CG1 1 
ATOM   3746 C CG2 . VAL A 1 574  ? 173.342 145.508 175.854 1.00 42.27  ? 574  VAL A CG2 1 
ATOM   3747 N N   . ILE A 1 575  ? 175.273 147.206 179.494 1.00 47.61  ? 575  ILE A N   1 
ATOM   3748 C CA  . ILE A 1 575  ? 176.218 147.447 180.576 1.00 47.00  ? 575  ILE A CA  1 
ATOM   3749 C C   . ILE A 1 575  ? 175.504 147.370 181.912 1.00 49.42  ? 575  ILE A C   1 
ATOM   3750 O O   . ILE A 1 575  ? 175.918 146.626 182.812 1.00 55.62  ? 575  ILE A O   1 
ATOM   3751 C CB  . ILE A 1 575  ? 176.928 148.798 180.387 1.00 45.19  ? 575  ILE A CB  1 
ATOM   3752 C CG1 . ILE A 1 575  ? 178.112 148.643 179.441 1.00 44.73  ? 575  ILE A CG1 1 
ATOM   3753 C CG2 . ILE A 1 575  ? 177.403 149.335 181.716 1.00 49.25  ? 575  ILE A CG2 1 
ATOM   3754 C CD1 . ILE A 1 575  ? 178.878 149.919 179.212 1.00 48.07  ? 575  ILE A CD1 1 
ATOM   3755 N N   . LEU A 1 576  ? 174.372 148.069 182.033 1.00 43.39  ? 576  LEU A N   1 
ATOM   3756 C CA  . LEU A 1 576  ? 173.638 148.044 183.288 1.00 41.91  ? 576  LEU A CA  1 
ATOM   3757 C C   . LEU A 1 576  ? 173.292 146.618 183.670 1.00 49.81  ? 576  LEU A C   1 
ATOM   3758 O O   . LEU A 1 576  ? 173.469 146.218 184.828 1.00 60.96  ? 576  LEU A O   1 
ATOM   3759 C CB  . LEU A 1 576  ? 172.380 148.902 183.182 1.00 46.11  ? 576  LEU A CB  1 
ATOM   3760 C CG  . LEU A 1 576  ? 172.639 150.401 183.052 1.00 42.45  ? 576  LEU A CG  1 
ATOM   3761 C CD1 . LEU A 1 576  ? 171.334 151.166 182.973 1.00 51.13  ? 576  LEU A CD1 1 
ATOM   3762 C CD2 . LEU A 1 576  ? 173.469 150.883 184.221 1.00 41.31  ? 576  LEU A CD2 1 
ATOM   3763 N N   . ASN A 1 577  ? 172.868 145.816 182.690 1.00 46.46  ? 577  ASN A N   1 
ATOM   3764 C CA  . ASN A 1 577  ? 172.539 144.426 182.972 1.00 39.64  ? 577  ASN A CA  1 
ATOM   3765 C C   . ASN A 1 577  ? 173.698 143.740 183.673 1.00 43.16  ? 577  ASN A C   1 
ATOM   3766 O O   . ASN A 1 577  ? 173.535 143.181 184.764 1.00 51.20  ? 577  ASN A O   1 
ATOM   3767 C CB  . ASN A 1 577  ? 172.184 143.697 181.681 1.00 44.81  ? 577  ASN A CB  1 
ATOM   3768 C CG  . ASN A 1 577  ? 171.672 142.299 181.927 1.00 48.36  ? 577  ASN A CG  1 
ATOM   3769 O OD1 . ASN A 1 577  ? 170.960 142.052 182.898 1.00 56.08  ? 577  ASN A OD1 1 
ATOM   3770 N ND2 . ASN A 1 577  ? 172.039 141.372 181.054 1.00 43.90  ? 577  ASN A ND2 1 
ATOM   3771 N N   . SER A 1 578  ? 174.898 143.841 183.098 1.00 42.62  ? 578  SER A N   1 
ATOM   3772 C CA  . SER A 1 578  ? 176.051 143.213 183.727 1.00 38.64  ? 578  SER A CA  1 
ATOM   3773 C C   . SER A 1 578  ? 176.283 143.788 185.113 1.00 45.99  ? 578  SER A C   1 
ATOM   3774 O O   . SER A 1 578  ? 176.480 143.040 186.078 1.00 50.56  ? 578  SER A O   1 
ATOM   3775 C CB  . SER A 1 578  ? 177.289 143.390 182.853 1.00 46.65  ? 578  SER A CB  1 
ATOM   3776 O OG  . SER A 1 578  ? 177.079 142.839 181.566 1.00 60.93  ? 578  SER A OG  1 
ATOM   3777 N N   . TYR A 1 579  ? 176.203 145.113 185.244 1.00 51.59  ? 579  TYR A N   1 
ATOM   3778 C CA  . TYR A 1 579  ? 176.430 145.720 186.547 1.00 47.44  ? 579  TYR A CA  1 
ATOM   3779 C C   . TYR A 1 579  ? 175.339 145.320 187.527 1.00 49.46  ? 579  TYR A C   1 
ATOM   3780 O O   . TYR A 1 579  ? 175.566 145.291 188.742 1.00 54.20  ? 579  TYR A O   1 
ATOM   3781 C CB  . TYR A 1 579  ? 176.511 147.238 186.420 1.00 46.52  ? 579  TYR A CB  1 
ATOM   3782 C CG  . TYR A 1 579  ? 176.872 147.919 187.716 1.00 49.45  ? 579  TYR A CG  1 
ATOM   3783 C CD1 . TYR A 1 579  ? 178.191 148.009 188.128 1.00 50.94  ? 579  TYR A CD1 1 
ATOM   3784 C CD2 . TYR A 1 579  ? 175.894 148.462 188.533 1.00 52.81  ? 579  TYR A CD2 1 
ATOM   3785 C CE1 . TYR A 1 579  ? 178.526 148.625 189.313 1.00 53.55  ? 579  TYR A CE1 1 
ATOM   3786 C CE2 . TYR A 1 579  ? 176.219 149.078 189.719 1.00 50.18  ? 579  TYR A CE2 1 
ATOM   3787 C CZ  . TYR A 1 579  ? 177.536 149.157 190.104 1.00 52.92  ? 579  TYR A CZ  1 
ATOM   3788 O OH  . TYR A 1 579  ? 177.860 149.773 191.288 1.00 62.81  ? 579  TYR A OH  1 
ATOM   3789 N N   . SER A 1 580  ? 174.147 145.004 187.021 1.00 41.56  ? 580  SER A N   1 
ATOM   3790 C CA  . SER A 1 580  ? 173.087 144.551 187.911 1.00 35.93  ? 580  SER A CA  1 
ATOM   3791 C C   . SER A 1 580  ? 173.334 143.121 188.360 1.00 43.77  ? 580  SER A C   1 
ATOM   3792 O O   . SER A 1 580  ? 172.920 142.725 189.455 1.00 51.31  ? 580  SER A O   1 
ATOM   3793 C CB  . SER A 1 580  ? 171.730 144.678 187.223 1.00 42.09  ? 580  SER A CB  1 
ATOM   3794 O OG  . SER A 1 580  ? 171.677 143.883 186.054 1.00 49.40  ? 580  SER A OG  1 
ATOM   3795 N N   . LEU A 1 581  ? 174.013 142.329 187.530 1.00 43.51  ? 581  LEU A N   1 
ATOM   3796 C CA  . LEU A 1 581  ? 174.203 140.922 187.853 1.00 40.18  ? 581  LEU A CA  1 
ATOM   3797 C C   . LEU A 1 581  ? 175.413 140.685 188.743 1.00 48.97  ? 581  LEU A C   1 
ATOM   3798 O O   . LEU A 1 581  ? 175.582 139.572 189.250 1.00 54.19  ? 581  LEU A O   1 
ATOM   3799 C CB  . LEU A 1 581  ? 174.330 140.104 186.572 1.00 40.80  ? 581  LEU A CB  1 
ATOM   3800 C CG  . LEU A 1 581  ? 173.081 140.080 185.694 1.00 42.86  ? 581  LEU A CG  1 
ATOM   3801 C CD1 . LEU A 1 581  ? 173.324 139.257 184.446 1.00 48.18  ? 581  LEU A CD1 1 
ATOM   3802 C CD2 . LEU A 1 581  ? 171.905 139.534 186.476 1.00 46.42  ? 581  LEU A CD2 1 
ATOM   3803 N N   . LEU A 1 582  ? 176.259 141.694 188.943 1.00 50.74  ? 582  LEU A N   1 
ATOM   3804 C CA  . LEU A 1 582  ? 177.474 141.550 189.734 1.00 48.77  ? 582  LEU A CA  1 
ATOM   3805 C C   . LEU A 1 582  ? 177.360 142.215 191.100 1.00 52.70  ? 582  LEU A C   1 
ATOM   3806 O O   . LEU A 1 582  ? 178.335 142.791 191.593 1.00 55.34  ? 582  LEU A O   1 
ATOM   3807 C CB  . LEU A 1 582  ? 178.670 142.106 188.966 1.00 52.91  ? 582  LEU A CB  1 
ATOM   3808 C CG  . LEU A 1 582  ? 179.015 141.338 187.692 1.00 48.49  ? 582  LEU A CG  1 
ATOM   3809 C CD1 . LEU A 1 582  ? 180.208 141.960 187.007 1.00 51.55  ? 582  LEU A CD1 1 
ATOM   3810 C CD2 . LEU A 1 582  ? 179.285 139.884 188.015 1.00 47.07  ? 582  LEU A CD2 1 
ATOM   3811 N N   . PHE A 1 583  ? 176.182 142.146 191.723 1.00 58.35  ? 583  PHE A N   1 
ATOM   3812 C CA  . PHE A 1 583  ? 176.010 142.714 193.056 1.00 57.78  ? 583  PHE A CA  1 
ATOM   3813 C C   . PHE A 1 583  ? 176.891 142.018 194.082 1.00 57.06  ? 583  PHE A C   1 
ATOM   3814 O O   . PHE A 1 583  ? 177.229 142.609 195.113 1.00 57.83  ? 583  PHE A O   1 
ATOM   3815 C CB  . PHE A 1 583  ? 174.546 142.619 193.478 1.00 59.78  ? 583  PHE A CB  1 
ATOM   3816 C CG  . PHE A 1 583  ? 174.015 141.215 193.500 1.00 60.44  ? 583  PHE A CG  1 
ATOM   3817 C CD1 . PHE A 1 583  ? 173.453 140.657 192.368 1.00 57.90  ? 583  PHE A CD1 1 
ATOM   3818 C CD2 . PHE A 1 583  ? 174.079 140.453 194.652 1.00 59.16  ? 583  PHE A CD2 1 
ATOM   3819 C CE1 . PHE A 1 583  ? 172.967 139.370 192.383 1.00 54.65  ? 583  PHE A CE1 1 
ATOM   3820 C CE2 . PHE A 1 583  ? 173.594 139.165 194.672 1.00 60.51  ? 583  PHE A CE2 1 
ATOM   3821 C CZ  . PHE A 1 583  ? 173.038 138.624 193.536 1.00 59.84  ? 583  PHE A CZ  1 
ATOM   3822 N N   . MET A 1 584  ? 177.261 140.763 193.824 1.00 67.98  ? 584  MET A N   1 
ATOM   3823 C CA  . MET A 1 584  ? 178.027 139.994 194.798 1.00 65.64  ? 584  MET A CA  1 
ATOM   3824 C C   . MET A 1 584  ? 179.433 140.549 194.982 1.00 69.35  ? 584  MET A C   1 
ATOM   3825 O O   . MET A 1 584  ? 180.037 140.363 196.044 1.00 71.87  ? 584  MET A O   1 
ATOM   3826 C CB  . MET A 1 584  ? 178.086 138.531 194.369 1.00 65.74  ? 584  MET A CB  1 
ATOM   3827 C CG  . MET A 1 584  ? 178.745 138.323 193.019 1.00 70.46  ? 584  MET A CG  1 
ATOM   3828 S SD  . MET A 1 584  ? 177.932 137.058 192.032 1.00 80.83  ? 584  MET A SD  1 
ATOM   3829 C CE  . MET A 1 584  ? 176.311 137.787 191.844 1.00 73.73  ? 584  MET A CE  1 
ATOM   3830 N N   . VAL A 1 585  ? 179.969 141.226 193.971 1.00 62.41  ? 585  VAL A N   1 
ATOM   3831 C CA  . VAL A 1 585  ? 181.337 141.731 194.037 1.00 61.37  ? 585  VAL A CA  1 
ATOM   3832 C C   . VAL A 1 585  ? 181.355 142.954 194.946 1.00 66.50  ? 585  VAL A C   1 
ATOM   3833 O O   . VAL A 1 585  ? 180.758 143.986 194.628 1.00 70.24  ? 585  VAL A O   1 
ATOM   3834 C CB  . VAL A 1 585  ? 181.879 142.064 192.645 1.00 58.96  ? 585  VAL A CB  1 
ATOM   3835 C CG1 . VAL A 1 585  ? 183.334 142.475 192.733 1.00 62.70  ? 585  VAL A CG1 1 
ATOM   3836 C CG2 . VAL A 1 585  ? 181.713 140.873 191.725 1.00 64.41  ? 585  VAL A CG2 1 
ATOM   3837 N N   . LYS A 1 586  ? 182.045 142.844 196.081 1.00 77.34  ? 586  LYS A N   1 
ATOM   3838 C CA  . LYS A 1 586  ? 182.102 143.951 197.027 1.00 78.42  ? 586  LYS A CA  1 
ATOM   3839 C C   . LYS A 1 586  ? 183.021 145.067 196.549 1.00 78.48  ? 586  LYS A C   1 
ATOM   3840 O O   . LYS A 1 586  ? 182.737 146.244 196.796 1.00 80.49  ? 586  LYS A O   1 
ATOM   3841 C CB  . LYS A 1 586  ? 182.555 143.446 198.397 1.00 80.43  ? 586  LYS A CB  1 
ATOM   3842 C CG  . LYS A 1 586  ? 181.803 142.213 198.879 1.00 80.12  ? 586  LYS A CG  1 
ATOM   3843 C CD  . LYS A 1 586  ? 180.300 142.449 198.914 1.00 79.62  ? 586  LYS A CD  1 
ATOM   3844 C CE  . LYS A 1 586  ? 179.921 143.484 199.960 1.00 81.99  ? 586  LYS A CE  1 
ATOM   3845 N NZ  . LYS A 1 586  ? 180.297 143.048 201.333 1.00 79.24  ? 586  LYS A NZ  1 
ATOM   3846 N N   . ASP A 1 587  ? 184.115 144.726 195.873 1.00 75.10  ? 587  ASP A N   1 
ATOM   3847 C CA  . ASP A 1 587  ? 185.042 145.730 195.361 1.00 74.50  ? 587  ASP A CA  1 
ATOM   3848 C C   . ASP A 1 587  ? 184.429 146.397 194.137 1.00 73.39  ? 587  ASP A C   1 
ATOM   3849 O O   . ASP A 1 587  ? 184.310 145.775 193.077 1.00 70.41  ? 587  ASP A O   1 
ATOM   3850 C CB  . ASP A 1 587  ? 186.381 145.083 195.023 1.00 70.81  ? 587  ASP A CB  1 
ATOM   3851 C CG  . ASP A 1 587  ? 187.450 146.099 194.681 1.00 75.50  ? 587  ASP A CG  1 
ATOM   3852 O OD1 . ASP A 1 587  ? 187.184 147.313 194.801 1.00 78.91  ? 587  ASP A OD1 1 
ATOM   3853 O OD2 . ASP A 1 587  ? 188.561 145.683 194.293 1.00 75.93  ? 587  ASP A OD2 1 
ATOM   3854 N N   . ASN A 1 588  ? 184.044 147.667 194.278 1.00 68.87  ? 588  ASN A N   1 
ATOM   3855 C CA  . ASN A 1 588  ? 183.324 148.344 193.205 1.00 68.26  ? 588  ASN A CA  1 
ATOM   3856 C C   . ASN A 1 588  ? 184.182 148.497 191.958 1.00 71.10  ? 588  ASN A C   1 
ATOM   3857 O O   . ASN A 1 588  ? 183.681 148.366 190.837 1.00 79.19  ? 588  ASN A O   1 
ATOM   3858 C CB  . ASN A 1 588  ? 182.821 149.704 193.677 1.00 67.50  ? 588  ASN A CB  1 
ATOM   3859 C CG  . ASN A 1 588  ? 181.417 149.637 194.229 1.00 75.76  ? 588  ASN A CG  1 
ATOM   3860 O OD1 . ASN A 1 588  ? 181.069 148.713 194.961 1.00 73.39  ? 588  ASN A OD1 1 
ATOM   3861 N ND2 . ASN A 1 588  ? 180.594 150.608 193.863 1.00 78.63  ? 588  ASN A ND2 1 
ATOM   3862 N N   . LYS A 1 589  ? 185.470 148.797 192.126 1.00 66.29  ? 589  LYS A N   1 
ATOM   3863 C CA  . LYS A 1 589  ? 186.344 148.920 190.964 1.00 67.24  ? 589  LYS A CA  1 
ATOM   3864 C C   . LYS A 1 589  ? 186.418 147.605 190.200 1.00 68.05  ? 589  LYS A C   1 
ATOM   3865 O O   . LYS A 1 589  ? 186.249 147.571 188.975 1.00 70.67  ? 589  LYS A O   1 
ATOM   3866 C CB  . LYS A 1 589  ? 187.737 149.373 191.399 1.00 63.57  ? 589  LYS A CB  1 
ATOM   3867 C CG  . LYS A 1 589  ? 188.721 149.506 190.253 1.00 64.10  ? 589  LYS A CG  1 
ATOM   3868 C CD  . LYS A 1 589  ? 190.048 150.071 190.721 1.00 64.60  ? 589  LYS A CD  1 
ATOM   3869 C CE  . LYS A 1 589  ? 190.997 150.271 189.553 1.00 66.64  ? 589  LYS A CE  1 
ATOM   3870 N NZ  . LYS A 1 589  ? 192.290 150.865 189.984 1.00 69.87  ? 589  LYS A NZ  1 
ATOM   3871 N N   . LYS A 1 590  ? 186.648 146.505 190.916 1.00 64.43  ? 590  LYS A N   1 
ATOM   3872 C CA  . LYS A 1 590  ? 186.680 145.203 190.265 1.00 62.29  ? 590  LYS A CA  1 
ATOM   3873 C C   . LYS A 1 590  ? 185.308 144.818 189.730 1.00 67.16  ? 590  LYS A C   1 
ATOM   3874 O O   . LYS A 1 590  ? 185.214 144.137 188.704 1.00 75.52  ? 590  LYS A O   1 
ATOM   3875 C CB  . LYS A 1 590  ? 187.199 144.143 191.234 1.00 66.08  ? 590  LYS A CB  1 
ATOM   3876 C CG  . LYS A 1 590  ? 187.577 142.834 190.571 1.00 63.86  ? 590  LYS A CG  1 
ATOM   3877 C CD  . LYS A 1 590  ? 188.380 141.954 191.513 1.00 67.63  ? 590  LYS A CD  1 
ATOM   3878 C CE  . LYS A 1 590  ? 187.599 141.636 192.775 1.00 71.34  ? 590  LYS A CE  1 
ATOM   3879 N NZ  . LYS A 1 590  ? 186.364 140.859 192.485 1.00 72.32  ? 590  LYS A NZ  1 
ATOM   3880 N N   . ARG A 1 591  ? 184.239 145.252 190.400 1.00 52.12  ? 591  ARG A N   1 
ATOM   3881 C CA  . ARG A 1 591  ? 182.896 144.993 189.893 1.00 52.36  ? 591  ARG A CA  1 
ATOM   3882 C C   . ARG A 1 591  ? 182.688 145.657 188.539 1.00 52.99  ? 591  ARG A C   1 
ATOM   3883 O O   . ARG A 1 591  ? 182.168 145.039 187.605 1.00 62.24  ? 591  ARG A O   1 
ATOM   3884 C CB  . ARG A 1 591  ? 181.855 145.484 190.894 1.00 56.58  ? 591  ARG A CB  1 
ATOM   3885 C CG  . ARG A 1 591  ? 180.428 145.342 190.412 1.00 54.04  ? 591  ARG A CG  1 
ATOM   3886 C CD  . ARG A 1 591  ? 179.452 145.902 191.423 1.00 50.42  ? 591  ARG A CD  1 
ATOM   3887 N NE  . ARG A 1 591  ? 178.071 145.719 190.997 1.00 54.48  ? 591  ARG A NE  1 
ATOM   3888 C CZ  . ARG A 1 591  ? 177.020 146.183 191.657 1.00 57.45  ? 591  ARG A CZ  1 
ATOM   3889 N NH1 . ARG A 1 591  ? 177.157 146.871 192.777 1.00 62.72  ? 591  ARG A NH1 1 
ATOM   3890 N NH2 . ARG A 1 591  ? 175.801 145.949 191.181 1.00 52.05  ? 591  ARG A NH2 1 
ATOM   3891 N N   . ILE A 1 592  ? 183.098 146.919 188.416 1.00 52.70  ? 592  ILE A N   1 
ATOM   3892 C CA  . ILE A 1 592  ? 182.975 147.625 187.144 1.00 57.75  ? 592  ILE A CA  1 
ATOM   3893 C C   . ILE A 1 592  ? 183.860 146.981 186.091 1.00 57.50  ? 592  ILE A C   1 
ATOM   3894 O O   . ILE A 1 592  ? 183.471 146.855 184.923 1.00 62.12  ? 592  ILE A O   1 
ATOM   3895 C CB  . ILE A 1 592  ? 183.311 149.115 187.324 1.00 54.53  ? 592  ILE A CB  1 
ATOM   3896 C CG1 . ILE A 1 592  ? 182.287 149.784 188.231 1.00 54.54  ? 592  ILE A CG1 1 
ATOM   3897 C CG2 . ILE A 1 592  ? 183.356 149.818 185.982 1.00 51.79  ? 592  ILE A CG2 1 
ATOM   3898 C CD1 . ILE A 1 592  ? 182.550 151.240 188.423 1.00 55.86  ? 592  ILE A CD1 1 
ATOM   3899 N N   . GLN A 1 593  ? 185.070 146.577 186.478 1.00 56.36  ? 593  GLN A N   1 
ATOM   3900 C CA  . GLN A 1 593  ? 185.963 145.929 185.525 1.00 50.43  ? 593  GLN A CA  1 
ATOM   3901 C C   . GLN A 1 593  ? 185.343 144.648 184.983 1.00 52.85  ? 593  GLN A C   1 
ATOM   3902 O O   . GLN A 1 593  ? 185.367 144.399 183.774 1.00 63.14  ? 593  GLN A O   1 
ATOM   3903 C CB  . GLN A 1 593  ? 187.313 145.647 186.180 1.00 49.02  ? 593  GLN A CB  1 
ATOM   3904 C CG  . GLN A 1 593  ? 188.107 146.893 186.497 1.00 56.27  ? 593  GLN A CG  1 
ATOM   3905 C CD  . GLN A 1 593  ? 189.475 146.587 187.060 1.00 59.04  ? 593  GLN A CD  1 
ATOM   3906 O OE1 . GLN A 1 593  ? 189.650 146.480 188.272 1.00 61.68  ? 593  GLN A OE1 1 
ATOM   3907 N NE2 . GLN A 1 593  ? 190.459 146.451 186.182 1.00 55.69  ? 593  GLN A NE2 1 
ATOM   3908 N N   . MET A 1 594  ? 184.757 143.834 185.861 1.00 56.19  ? 594  MET A N   1 
ATOM   3909 C CA  . MET A 1 594  ? 184.141 142.591 185.407 1.00 58.63  ? 594  MET A CA  1 
ATOM   3910 C C   . MET A 1 594  ? 182.884 142.854 184.587 1.00 63.64  ? 594  MET A C   1 
ATOM   3911 O O   . MET A 1 594  ? 182.614 142.142 183.613 1.00 69.86  ? 594  MET A O   1 
ATOM   3912 C CB  . MET A 1 594  ? 183.835 141.689 186.599 1.00 55.73  ? 594  MET A CB  1 
ATOM   3913 C CG  . MET A 1 594  ? 184.932 140.687 186.892 1.00 59.52  ? 594  MET A CG  1 
ATOM   3914 S SD  . MET A 1 594  ? 184.585 139.684 188.342 1.00 79.63  ? 594  MET A SD  1 
ATOM   3915 C CE  . MET A 1 594  ? 184.613 140.943 189.609 1.00 67.31  ? 594  MET A CE  1 
ATOM   3916 N N   . CYS A 1 595  ? 182.106 143.872 184.958 1.00 47.99  ? 595  CYS A N   1 
ATOM   3917 C CA  . CYS A 1 595  ? 180.929 144.230 184.172 1.00 41.85  ? 595  CYS A CA  1 
ATOM   3918 C C   . CYS A 1 595  ? 181.320 144.630 182.758 1.00 50.38  ? 595  CYS A C   1 
ATOM   3919 O O   . CYS A 1 595  ? 180.718 144.175 181.776 1.00 55.20  ? 595  CYS A O   1 
ATOM   3920 C CB  . CYS A 1 595  ? 180.174 145.366 184.859 1.00 51.05  ? 595  CYS A CB  1 
ATOM   3921 S SG  . CYS A 1 595  ? 179.188 146.375 183.740 1.00 68.48  ? 595  CYS A SG  1 
ATOM   3922 N N   . LEU A 1 596  ? 182.337 145.482 182.636 1.00 56.02  ? 596  LEU A N   1 
ATOM   3923 C CA  . LEU A 1 596  ? 182.801 145.899 181.321 1.00 49.47  ? 596  LEU A CA  1 
ATOM   3924 C C   . LEU A 1 596  ? 183.381 144.722 180.552 1.00 56.95  ? 596  LEU A C   1 
ATOM   3925 O O   . LEU A 1 596  ? 183.180 144.603 179.341 1.00 66.28  ? 596  LEU A O   1 
ATOM   3926 C CB  . LEU A 1 596  ? 183.829 147.018 181.456 1.00 47.01  ? 596  LEU A CB  1 
ATOM   3927 C CG  . LEU A 1 596  ? 184.226 147.656 180.129 1.00 55.77  ? 596  LEU A CG  1 
ATOM   3928 C CD1 . LEU A 1 596  ? 182.991 148.127 179.389 1.00 54.54  ? 596  LEU A CD1 1 
ATOM   3929 C CD2 . LEU A 1 596  ? 185.177 148.807 180.363 1.00 61.25  ? 596  LEU A CD2 1 
ATOM   3930 N N   . LYS A 1 597  ? 184.100 143.835 181.242 1.00 54.04  ? 597  LYS A N   1 
ATOM   3931 C CA  . LYS A 1 597  ? 184.636 142.647 180.590 1.00 48.64  ? 597  LYS A CA  1 
ATOM   3932 C C   . LYS A 1 597  ? 183.522 141.790 180.009 1.00 49.98  ? 597  LYS A C   1 
ATOM   3933 O O   . LYS A 1 597  ? 183.639 141.274 178.893 1.00 61.80  ? 597  LYS A O   1 
ATOM   3934 C CB  . LYS A 1 597  ? 185.469 141.843 181.587 1.00 43.93  ? 597  LYS A CB  1 
ATOM   3935 C CG  . LYS A 1 597  ? 185.931 140.494 181.077 1.00 52.94  ? 597  LYS A CG  1 
ATOM   3936 C CD  . LYS A 1 597  ? 186.660 139.726 182.164 1.00 56.20  ? 597  LYS A CD  1 
ATOM   3937 C CE  . LYS A 1 597  ? 187.072 138.347 181.686 1.00 56.72  ? 597  LYS A CE  1 
ATOM   3938 N NZ  . LYS A 1 597  ? 187.726 137.563 182.769 1.00 56.37  ? 597  LYS A NZ  1 
ATOM   3939 N N   . ASP A 1 598  ? 182.431 141.626 180.756 1.00 52.84  ? 598  ASP A N   1 
ATOM   3940 C CA  . ASP A 1 598  ? 181.326 140.809 180.269 1.00 54.29  ? 598  ASP A CA  1 
ATOM   3941 C C   . ASP A 1 598  ? 180.602 141.477 179.106 1.00 59.06  ? 598  ASP A C   1 
ATOM   3942 O O   . ASP A 1 598  ? 180.239 140.809 178.132 1.00 63.75  ? 598  ASP A O   1 
ATOM   3943 C CB  . ASP A 1 598  ? 180.353 140.513 181.407 1.00 55.40  ? 598  ASP A CB  1 
ATOM   3944 C CG  . ASP A 1 598  ? 180.995 139.725 182.527 1.00 65.58  ? 598  ASP A CG  1 
ATOM   3945 O OD1 . ASP A 1 598  ? 182.206 139.441 182.433 1.00 69.08  ? 598  ASP A OD1 1 
ATOM   3946 O OD2 . ASP A 1 598  ? 180.290 139.389 183.502 1.00 64.87  ? 598  ASP A OD2 1 
ATOM   3947 N N   . SER A 1 599  ? 180.381 142.789 179.183 1.00 57.25  ? 599  SER A N   1 
ATOM   3948 C CA  . SER A 1 599  ? 179.560 143.465 178.185 1.00 54.45  ? 599  SER A CA  1 
ATOM   3949 C C   . SER A 1 599  ? 180.340 143.968 176.976 1.00 61.34  ? 599  SER A C   1 
ATOM   3950 O O   . SER A 1 599  ? 179.718 144.411 176.000 1.00 66.85  ? 599  SER A O   1 
ATOM   3951 C CB  . SER A 1 599  ? 178.821 144.641 178.825 1.00 53.66  ? 599  SER A CB  1 
ATOM   3952 O OG  . SER A 1 599  ? 177.927 144.190 179.825 1.00 61.99  ? 599  SER A OG  1 
ATOM   3953 N N   . ALA A 1 600  ? 181.672 143.910 177.011 1.00 59.65  ? 600  ALA A N   1 
ATOM   3954 C CA  . ALA A 1 600  ? 182.470 144.517 175.953 1.00 56.38  ? 600  ALA A CA  1 
ATOM   3955 C C   . ALA A 1 600  ? 182.241 143.833 174.617 1.00 58.95  ? 600  ALA A C   1 
ATOM   3956 O O   . ALA A 1 600  ? 182.024 144.497 173.598 1.00 66.08  ? 600  ALA A O   1 
ATOM   3957 C CB  . ALA A 1 600  ? 183.948 144.468 176.329 1.00 52.25  ? 600  ALA A CB  1 
ATOM   3958 N N   . LEU A 1 601  ? 182.306 142.502 174.597 1.00 55.69  ? 601  LEU A N   1 
ATOM   3959 C CA  . LEU A 1 601  ? 182.149 141.787 173.338 1.00 61.41  ? 601  LEU A CA  1 
ATOM   3960 C C   . LEU A 1 601  ? 180.772 142.034 172.741 1.00 65.76  ? 601  LEU A C   1 
ATOM   3961 O O   . LEU A 1 601  ? 180.647 142.305 171.542 1.00 67.08  ? 601  LEU A O   1 
ATOM   3962 C CB  . LEU A 1 601  ? 182.385 140.294 173.550 1.00 64.81  ? 601  LEU A CB  1 
ATOM   3963 C CG  . LEU A 1 601  ? 182.532 139.469 172.275 1.00 64.96  ? 601  LEU A CG  1 
ATOM   3964 C CD1 . LEU A 1 601  ? 183.706 139.978 171.460 1.00 57.32  ? 601  LEU A CD1 1 
ATOM   3965 C CD2 . LEU A 1 601  ? 182.704 137.999 172.610 1.00 64.22  ? 601  LEU A CD2 1 
ATOM   3966 N N   . ALA A 1 602  ? 179.730 141.973 173.570 1.00 62.75  ? 602  ALA A N   1 
ATOM   3967 C CA  . ALA A 1 602  ? 178.376 142.189 173.076 1.00 55.42  ? 602  ALA A CA  1 
ATOM   3968 C C   . ALA A 1 602  ? 178.218 143.587 172.496 1.00 58.29  ? 602  ALA A C   1 
ATOM   3969 O O   . ALA A 1 602  ? 177.708 143.754 171.381 1.00 68.54  ? 602  ALA A O   1 
ATOM   3970 C CB  . ALA A 1 602  ? 177.367 141.955 174.199 1.00 55.27  ? 602  ALA A CB  1 
ATOM   3971 N N   . ILE A 1 603  ? 178.664 144.607 173.233 1.00 44.15  ? 603  ILE A N   1 
ATOM   3972 C CA  . ILE A 1 603  ? 178.487 145.981 172.771 1.00 49.82  ? 603  ILE A CA  1 
ATOM   3973 C C   . ILE A 1 603  ? 179.274 146.221 171.489 1.00 49.10  ? 603  ILE A C   1 
ATOM   3974 O O   . ILE A 1 603  ? 178.768 146.819 170.528 1.00 52.39  ? 603  ILE A O   1 
ATOM   3975 C CB  . ILE A 1 603  ? 178.893 146.971 173.874 1.00 47.86  ? 603  ILE A CB  1 
ATOM   3976 C CG1 . ILE A 1 603  ? 177.879 146.932 175.011 1.00 50.55  ? 603  ILE A CG1 1 
ATOM   3977 C CG2 . ILE A 1 603  ? 179.015 148.373 173.314 1.00 53.26  ? 603  ILE A CG2 1 
ATOM   3978 C CD1 . ILE A 1 603  ? 178.089 148.011 176.023 1.00 53.27  ? 603  ILE A CD1 1 
ATOM   3979 N N   . THR A 1 604  ? 180.528 145.768 171.459 1.00 38.87  ? 604  THR A N   1 
ATOM   3980 C CA  . THR A 1 604  ? 181.370 145.991 170.294 1.00 38.67  ? 604  THR A CA  1 
ATOM   3981 C C   . THR A 1 604  ? 180.797 145.294 169.069 1.00 48.63  ? 604  THR A C   1 
ATOM   3982 O O   . THR A 1 604  ? 180.748 145.872 167.981 1.00 55.98  ? 604  THR A O   1 
ATOM   3983 C CB  . THR A 1 604  ? 182.792 145.511 170.578 1.00 44.55  ? 604  THR A CB  1 
ATOM   3984 O OG1 . THR A 1 604  ? 183.326 146.235 171.691 1.00 54.57  ? 604  THR A OG1 1 
ATOM   3985 C CG2 . THR A 1 604  ? 183.677 145.741 169.371 1.00 48.41  ? 604  THR A CG2 1 
ATOM   3986 N N   . VAL A 1 605  ? 180.338 144.051 169.230 1.00 48.67  ? 605  VAL A N   1 
ATOM   3987 C CA  . VAL A 1 605  ? 179.767 143.326 168.101 1.00 39.17  ? 605  VAL A CA  1 
ATOM   3988 C C   . VAL A 1 605  ? 178.499 144.012 167.611 1.00 46.31  ? 605  VAL A C   1 
ATOM   3989 O O   . VAL A 1 605  ? 178.282 144.147 166.402 1.00 56.60  ? 605  VAL A O   1 
ATOM   3990 C CB  . VAL A 1 605  ? 179.512 141.857 168.480 1.00 39.55  ? 605  VAL A CB  1 
ATOM   3991 C CG1 . VAL A 1 605  ? 178.613 141.192 167.456 1.00 45.87  ? 605  VAL A CG1 1 
ATOM   3992 C CG2 . VAL A 1 605  ? 180.827 141.112 168.581 1.00 48.19  ? 605  VAL A CG2 1 
ATOM   3993 N N   . THR A 1 606  ? 177.648 144.465 168.534 1.00 49.75  ? 606  THR A N   1 
ATOM   3994 C CA  . THR A 1 606  ? 176.417 145.139 168.131 1.00 49.37  ? 606  THR A CA  1 
ATOM   3995 C C   . THR A 1 606  ? 176.714 146.393 167.318 1.00 56.19  ? 606  THR A C   1 
ATOM   3996 O O   . THR A 1 606  ? 176.180 146.577 166.214 1.00 58.43  ? 606  THR A O   1 
ATOM   3997 C CB  . THR A 1 606  ? 175.588 145.486 169.367 1.00 49.08  ? 606  THR A CB  1 
ATOM   3998 O OG1 . THR A 1 606  ? 175.103 144.283 169.972 1.00 50.41  ? 606  THR A OG1 1 
ATOM   3999 C CG2 . THR A 1 606  ? 174.415 146.370 168.994 1.00 54.85  ? 606  THR A CG2 1 
ATOM   4000 N N   . THR A 1 607  ? 177.573 147.267 167.846 1.00 47.58  ? 607  THR A N   1 
ATOM   4001 C CA  . THR A 1 607  ? 177.873 148.508 167.138 1.00 40.89  ? 607  THR A CA  1 
ATOM   4002 C C   . THR A 1 607  ? 178.587 148.234 165.823 1.00 45.28  ? 607  THR A C   1 
ATOM   4003 O O   . THR A 1 607  ? 178.315 148.894 164.814 1.00 53.37  ? 607  THR A O   1 
ATOM   4004 C CB  . THR A 1 607  ? 178.708 149.436 168.013 1.00 48.36  ? 607  THR A CB  1 
ATOM   4005 O OG1 . THR A 1 607  ? 179.928 148.780 168.377 1.00 53.02  ? 607  THR A OG1 1 
ATOM   4006 C CG2 . THR A 1 607  ? 177.938 149.807 169.266 1.00 43.33  ? 607  THR A CG2 1 
ATOM   4007 N N   . LEU A 1 608  ? 179.504 147.266 165.811 1.00 41.95  ? 608  LEU A N   1 
ATOM   4008 C CA  . LEU A 1 608  ? 180.225 146.938 164.590 1.00 41.02  ? 608  LEU A CA  1 
ATOM   4009 C C   . LEU A 1 608  ? 179.278 146.421 163.520 1.00 41.33  ? 608  LEU A C   1 
ATOM   4010 O O   . LEU A 1 608  ? 179.406 146.768 162.343 1.00 46.39  ? 608  LEU A O   1 
ATOM   4011 C CB  . LEU A 1 608  ? 181.311 145.908 164.892 1.00 32.59  ? 608  LEU A CB  1 
ATOM   4012 C CG  . LEU A 1 608  ? 182.148 145.451 163.704 1.00 36.21  ? 608  LEU A CG  1 
ATOM   4013 C CD1 . LEU A 1 608  ? 182.886 146.630 163.104 1.00 43.42  ? 608  LEU A CD1 1 
ATOM   4014 C CD2 . LEU A 1 608  ? 183.119 144.371 164.133 1.00 44.16  ? 608  LEU A CD2 1 
ATOM   4015 N N   . THR A 1 609  ? 178.318 145.584 163.910 1.00 41.47  ? 609  THR A N   1 
ATOM   4016 C CA  . THR A 1 609  ? 177.363 145.056 162.945 1.00 36.37  ? 609  THR A CA  1 
ATOM   4017 C C   . THR A 1 609  ? 176.471 146.161 162.400 1.00 45.02  ? 609  THR A C   1 
ATOM   4018 O O   . THR A 1 609  ? 176.178 146.202 161.199 1.00 51.37  ? 609  THR A O   1 
ATOM   4019 C CB  . THR A 1 609  ? 176.526 143.956 163.587 1.00 42.59  ? 609  THR A CB  1 
ATOM   4020 O OG1 . THR A 1 609  ? 177.376 143.093 164.347 1.00 47.36  ? 609  THR A OG1 1 
ATOM   4021 C CG2 . THR A 1 609  ? 175.849 143.148 162.516 1.00 49.90  ? 609  THR A CG2 1 
ATOM   4022 N N   . ASN A 1 610  ? 176.024 147.070 163.270 1.00 45.86  ? 610  ASN A N   1 
ATOM   4023 C CA  . ASN A 1 610  ? 175.227 148.197 162.792 1.00 38.12  ? 610  ASN A CA  1 
ATOM   4024 C C   . ASN A 1 610  ? 176.022 149.046 161.808 1.00 45.32  ? 610  ASN A C   1 
ATOM   4025 O O   . ASN A 1 610  ? 175.515 149.435 160.747 1.00 48.59  ? 610  ASN A O   1 
ATOM   4026 C CB  . ASN A 1 610  ? 174.751 149.043 163.971 1.00 43.76  ? 610  ASN A CB  1 
ATOM   4027 C CG  . ASN A 1 610  ? 173.881 148.266 164.931 1.00 52.29  ? 610  ASN A CG  1 
ATOM   4028 O OD1 . ASN A 1 610  ? 173.283 147.257 164.565 1.00 60.43  ? 610  ASN A OD1 1 
ATOM   4029 N ND2 . ASN A 1 610  ? 173.804 148.734 166.169 1.00 50.59  ? 610  ASN A ND2 1 
ATOM   4030 N N   . ILE A 1 611  ? 177.283 149.327 162.139 1.00 46.04  ? 611  ILE A N   1 
ATOM   4031 C CA  . ILE A 1 611  ? 178.128 150.135 161.265 1.00 40.61  ? 611  ILE A CA  1 
ATOM   4032 C C   . ILE A 1 611  ? 178.331 149.435 159.930 1.00 46.64  ? 611  ILE A C   1 
ATOM   4033 O O   . ILE A 1 611  ? 178.289 150.064 158.869 1.00 49.57  ? 611  ILE A O   1 
ATOM   4034 C CB  . ILE A 1 611  ? 179.469 150.442 161.952 1.00 35.62  ? 611  ILE A CB  1 
ATOM   4035 C CG1 . ILE A 1 611  ? 179.262 151.414 163.110 1.00 37.82  ? 611  ILE A CG1 1 
ATOM   4036 C CG2 . ILE A 1 611  ? 180.463 151.010 160.961 1.00 41.09  ? 611  ILE A CG2 1 
ATOM   4037 C CD1 . ILE A 1 611  ? 180.520 151.691 163.891 1.00 41.91  ? 611  ILE A CD1 1 
ATOM   4038 N N   . ILE A 1 612  ? 178.562 148.121 159.962 1.00 46.71  ? 612  ILE A N   1 
ATOM   4039 C CA  . ILE A 1 612  ? 178.776 147.363 158.730 1.00 40.40  ? 612  ILE A CA  1 
ATOM   4040 C C   . ILE A 1 612  ? 177.533 147.416 157.854 1.00 47.04  ? 612  ILE A C   1 
ATOM   4041 O O   . ILE A 1 612  ? 177.610 147.645 156.642 1.00 54.29  ? 612  ILE A O   1 
ATOM   4042 C CB  . ILE A 1 612  ? 179.172 145.913 159.051 1.00 40.16  ? 612  ILE A CB  1 
ATOM   4043 C CG1 . ILE A 1 612  ? 180.648 145.840 159.433 1.00 45.99  ? 612  ILE A CG1 1 
ATOM   4044 C CG2 . ILE A 1 612  ? 178.879 145.006 157.874 1.00 43.19  ? 612  ILE A CG2 1 
ATOM   4045 C CD1 . ILE A 1 612  ? 181.138 144.440 159.690 1.00 45.47  ? 612  ILE A CD1 1 
ATOM   4046 N N   . ALA A 1 613  ? 176.364 147.203 158.461 1.00 41.50  ? 613  ALA A N   1 
ATOM   4047 C CA  . ALA A 1 613  ? 175.126 147.233 157.691 1.00 36.40  ? 613  ALA A CA  1 
ATOM   4048 C C   . ALA A 1 613  ? 174.909 148.596 157.052 1.00 42.41  ? 613  ALA A C   1 
ATOM   4049 O O   . ALA A 1 613  ? 174.574 148.690 155.865 1.00 52.64  ? 613  ALA A O   1 
ATOM   4050 C CB  . ALA A 1 613  ? 173.943 146.866 158.584 1.00 43.51  ? 613  ALA A CB  1 
ATOM   4051 N N   . PHE A 1 614  ? 175.121 149.669 157.815 1.00 43.92  ? 614  PHE A N   1 
ATOM   4052 C CA  . PHE A 1 614  ? 174.908 151.000 157.255 1.00 46.54  ? 614  PHE A CA  1 
ATOM   4053 C C   . PHE A 1 614  ? 175.939 151.330 156.181 1.00 51.42  ? 614  PHE A C   1 
ATOM   4054 O O   . PHE A 1 614  ? 175.604 151.946 155.164 1.00 58.57  ? 614  PHE A O   1 
ATOM   4055 C CB  . PHE A 1 614  ? 174.914 152.046 158.366 1.00 47.04  ? 614  PHE A CB  1 
ATOM   4056 C CG  . PHE A 1 614  ? 173.604 152.157 159.086 1.00 51.14  ? 614  PHE A CG  1 
ATOM   4057 C CD1 . PHE A 1 614  ? 172.543 152.830 158.512 1.00 49.11  ? 614  PHE A CD1 1 
ATOM   4058 C CD2 . PHE A 1 614  ? 173.428 151.582 160.329 1.00 51.99  ? 614  PHE A CD2 1 
ATOM   4059 C CE1 . PHE A 1 614  ? 171.338 152.930 159.165 1.00 49.36  ? 614  PHE A CE1 1 
ATOM   4060 C CE2 . PHE A 1 614  ? 172.224 151.680 160.987 1.00 50.34  ? 614  PHE A CE2 1 
ATOM   4061 C CZ  . PHE A 1 614  ? 171.177 152.354 160.404 1.00 51.32  ? 614  PHE A CZ  1 
ATOM   4062 N N   . LEU A 1 615  ? 177.195 150.926 156.375 1.00 44.87  ? 615  LEU A N   1 
ATOM   4063 C CA  . LEU A 1 615  ? 178.212 151.192 155.364 1.00 39.47  ? 615  LEU A CA  1 
ATOM   4064 C C   . LEU A 1 615  ? 177.918 150.441 154.074 1.00 43.24  ? 615  LEU A C   1 
ATOM   4065 O O   . LEU A 1 615  ? 178.113 150.981 152.979 1.00 46.29  ? 615  LEU A O   1 
ATOM   4066 C CB  . LEU A 1 615  ? 179.596 150.827 155.896 1.00 32.06  ? 615  LEU A CB  1 
ATOM   4067 C CG  . LEU A 1 615  ? 180.181 151.795 156.922 1.00 29.34  ? 615  LEU A CG  1 
ATOM   4068 C CD1 . LEU A 1 615  ? 181.590 151.387 157.296 1.00 40.06  ? 615  LEU A CD1 1 
ATOM   4069 C CD2 . LEU A 1 615  ? 180.160 153.207 156.379 1.00 35.17  ? 615  LEU A CD2 1 
ATOM   4070 N N   . ILE A 1 616  ? 177.453 149.195 154.176 1.00 41.71  ? 616  ILE A N   1 
ATOM   4071 C CA  . ILE A 1 616  ? 177.088 148.451 152.975 1.00 45.09  ? 616  ILE A CA  1 
ATOM   4072 C C   . ILE A 1 616  ? 175.884 149.092 152.302 1.00 49.84  ? 616  ILE A C   1 
ATOM   4073 O O   . ILE A 1 616  ? 175.800 149.151 151.070 1.00 54.61  ? 616  ILE A O   1 
ATOM   4074 C CB  . ILE A 1 616  ? 176.834 146.972 153.314 1.00 47.30  ? 616  ILE A CB  1 
ATOM   4075 C CG1 . ILE A 1 616  ? 178.126 146.315 153.793 1.00 43.86  ? 616  ILE A CG1 1 
ATOM   4076 C CG2 . ILE A 1 616  ? 176.290 146.235 152.106 1.00 39.16  ? 616  ILE A CG2 1 
ATOM   4077 C CD1 . ILE A 1 616  ? 177.982 144.847 154.100 1.00 45.21  ? 616  ILE A CD1 1 
ATOM   4078 N N   . SER A 1 617  ? 174.935 149.592 153.096 1.00 52.85  ? 617  SER A N   1 
ATOM   4079 C CA  . SER A 1 617  ? 173.804 150.305 152.513 1.00 49.82  ? 617  SER A CA  1 
ATOM   4080 C C   . SER A 1 617  ? 174.250 151.574 151.803 1.00 52.29  ? 617  SER A C   1 
ATOM   4081 O O   . SER A 1 617  ? 173.636 151.979 150.811 1.00 63.28  ? 617  SER A O   1 
ATOM   4082 C CB  . SER A 1 617  ? 172.779 150.638 153.594 1.00 52.10  ? 617  SER A CB  1 
ATOM   4083 O OG  . SER A 1 617  ? 171.706 151.384 153.053 1.00 67.34  ? 617  SER A OG  1 
ATOM   4084 N N   . ALA A 1 618  ? 175.314 152.212 152.292 1.00 49.17  ? 618  ALA A N   1 
ATOM   4085 C CA  . ALA A 1 618  ? 175.789 153.452 151.688 1.00 51.87  ? 618  ALA A CA  1 
ATOM   4086 C C   . ALA A 1 618  ? 176.313 153.254 150.274 1.00 54.73  ? 618  ALA A C   1 
ATOM   4087 O O   . ALA A 1 618  ? 176.483 154.237 149.547 1.00 60.21  ? 618  ALA A O   1 
ATOM   4088 C CB  . ALA A 1 618  ? 176.880 154.076 152.557 1.00 44.51  ? 618  ALA A CB  1 
ATOM   4089 N N   . ILE A 1 619  ? 176.580 152.011 149.866 1.00 52.04  ? 619  ILE A N   1 
ATOM   4090 C CA  . ILE A 1 619  ? 177.094 151.741 148.529 1.00 47.22  ? 619  ILE A CA  1 
ATOM   4091 C C   . ILE A 1 619  ? 176.058 151.980 147.441 1.00 49.10  ? 619  ILE A C   1 
ATOM   4092 O O   . ILE A 1 619  ? 176.418 152.064 146.262 1.00 55.82  ? 619  ILE A O   1 
ATOM   4093 C CB  . ILE A 1 619  ? 177.631 150.296 148.470 1.00 49.39  ? 619  ILE A CB  1 
ATOM   4094 C CG1 . ILE A 1 619  ? 178.548 150.026 149.660 1.00 53.97  ? 619  ILE A CG1 1 
ATOM   4095 C CG2 . ILE A 1 619  ? 178.417 150.050 147.198 1.00 54.69  ? 619  ILE A CG2 1 
ATOM   4096 C CD1 . ILE A 1 619  ? 179.799 150.874 149.666 1.00 55.14  ? 619  ILE A CD1 1 
ATOM   4097 N N   . SER A 1 620  ? 174.788 152.119 147.807 1.00 57.36  ? 620  SER A N   1 
ATOM   4098 C CA  . SER A 1 620  ? 173.732 152.233 146.812 1.00 56.10  ? 620  SER A CA  1 
ATOM   4099 C C   . SER A 1 620  ? 173.954 153.470 145.944 1.00 54.15  ? 620  SER A C   1 
ATOM   4100 O O   . SER A 1 620  ? 174.448 154.491 146.434 1.00 60.81  ? 620  SER A O   1 
ATOM   4101 C CB  . SER A 1 620  ? 172.366 152.305 147.491 1.00 48.19  ? 620  SER A CB  1 
ATOM   4102 O OG  . SER A 1 620  ? 172.262 153.471 148.282 1.00 59.25  ? 620  SER A OG  1 
ATOM   4103 N N   . PRO A 1 621  ? 173.617 153.407 144.652 1.00 59.86  ? 621  PRO A N   1 
ATOM   4104 C CA  . PRO A 1 621  ? 173.925 154.538 143.761 1.00 59.22  ? 621  PRO A CA  1 
ATOM   4105 C C   . PRO A 1 621  ? 173.242 155.836 144.151 1.00 66.18  ? 621  PRO A C   1 
ATOM   4106 O O   . PRO A 1 621  ? 173.807 156.914 143.933 1.00 67.33  ? 621  PRO A O   1 
ATOM   4107 C CB  . PRO A 1 621  ? 173.448 154.035 142.393 1.00 59.04  ? 621  PRO A CB  1 
ATOM   4108 C CG  . PRO A 1 621  ? 172.418 153.009 142.709 1.00 59.54  ? 621  PRO A CG  1 
ATOM   4109 C CD  . PRO A 1 621  ? 172.902 152.330 143.950 1.00 64.47  ? 621  PRO A CD  1 
ATOM   4110 N N   . PHE A 1 622  ? 172.039 155.768 144.713 1.00 65.65  ? 622  PHE A N   1 
ATOM   4111 C CA  . PHE A 1 622  ? 171.316 156.981 145.065 1.00 58.91  ? 622  PHE A CA  1 
ATOM   4112 C C   . PHE A 1 622  ? 172.046 157.729 146.170 1.00 60.95  ? 622  PHE A C   1 
ATOM   4113 O O   . PHE A 1 622  ? 172.398 157.149 147.200 1.00 67.32  ? 622  PHE A O   1 
ATOM   4114 C CB  . PHE A 1 622  ? 169.899 156.629 145.504 1.00 60.15  ? 622  PHE A CB  1 
ATOM   4115 C CG  . PHE A 1 622  ? 169.298 155.498 144.730 1.00 62.05  ? 622  PHE A CG  1 
ATOM   4116 C CD1 . PHE A 1 622  ? 168.903 155.674 143.418 1.00 64.55  ? 622  PHE A CD1 1 
ATOM   4117 C CD2 . PHE A 1 622  ? 169.134 154.256 145.312 1.00 67.00  ? 622  PHE A CD2 1 
ATOM   4118 C CE1 . PHE A 1 622  ? 168.353 154.634 142.702 1.00 66.08  ? 622  PHE A CE1 1 
ATOM   4119 C CE2 . PHE A 1 622  ? 168.583 153.213 144.600 1.00 68.55  ? 622  PHE A CE2 1 
ATOM   4120 C CZ  . PHE A 1 622  ? 168.192 153.403 143.295 1.00 65.45  ? 622  PHE A CZ  1 
ATOM   4121 N N   . TYR A 1 623  ? 172.274 159.024 145.956 1.00 58.61  ? 623  TYR A N   1 
ATOM   4122 C CA  . TYR A 1 623  ? 173.053 159.791 146.919 1.00 53.65  ? 623  TYR A CA  1 
ATOM   4123 C C   . TYR A 1 623  ? 172.281 160.063 148.200 1.00 56.25  ? 623  TYR A C   1 
ATOM   4124 O O   . TYR A 1 623  ? 172.895 160.239 149.255 1.00 67.49  ? 623  TYR A O   1 
ATOM   4125 C CB  . TYR A 1 623  ? 173.520 161.112 146.312 1.00 52.08  ? 623  TYR A CB  1 
ATOM   4126 C CG  . TYR A 1 623  ? 174.311 161.956 147.281 1.00 54.15  ? 623  TYR A CG  1 
ATOM   4127 C CD1 . TYR A 1 623  ? 175.634 161.659 147.568 1.00 60.19  ? 623  TYR A CD1 1 
ATOM   4128 C CD2 . TYR A 1 623  ? 173.732 163.040 147.920 1.00 54.57  ? 623  TYR A CD2 1 
ATOM   4129 C CE1 . TYR A 1 623  ? 176.359 162.422 148.458 1.00 60.04  ? 623  TYR A CE1 1 
ATOM   4130 C CE2 . TYR A 1 623  ? 174.448 163.808 148.811 1.00 57.92  ? 623  TYR A CE2 1 
ATOM   4131 C CZ  . TYR A 1 623  ? 175.762 163.495 149.076 1.00 59.27  ? 623  TYR A CZ  1 
ATOM   4132 O OH  . TYR A 1 623  ? 176.482 164.258 149.963 1.00 58.12  ? 623  TYR A OH  1 
ATOM   4133 N N   . SER A 1 624  ? 170.950 160.112 148.138 1.00 45.93  ? 624  SER A N   1 
ATOM   4134 C CA  . SER A 1 624  ? 170.171 160.305 149.357 1.00 41.54  ? 624  SER A CA  1 
ATOM   4135 C C   . SER A 1 624  ? 170.404 159.159 150.332 1.00 49.68  ? 624  SER A C   1 
ATOM   4136 O O   . SER A 1 624  ? 170.687 159.381 151.516 1.00 51.76  ? 624  SER A O   1 
ATOM   4137 C CB  . SER A 1 624  ? 168.688 160.435 149.017 1.00 51.07  ? 624  SER A CB  1 
ATOM   4138 O OG  . SER A 1 624  ? 168.213 159.268 148.375 1.00 58.31  ? 624  SER A OG  1 
ATOM   4139 N N   . ILE A 1 625  ? 170.324 157.923 149.840 1.00 53.55  ? 625  ILE A N   1 
ATOM   4140 C CA  . ILE A 1 625  ? 170.562 156.766 150.694 1.00 51.93  ? 625  ILE A CA  1 
ATOM   4141 C C   . ILE A 1 625  ? 172.017 156.714 151.135 1.00 58.00  ? 625  ILE A C   1 
ATOM   4142 O O   . ILE A 1 625  ? 172.318 156.360 152.280 1.00 66.55  ? 625  ILE A O   1 
ATOM   4143 C CB  . ILE A 1 625  ? 170.141 155.476 149.973 1.00 53.44  ? 625  ILE A CB  1 
ATOM   4144 C CG1 . ILE A 1 625  ? 168.640 155.502 149.722 1.00 52.34  ? 625  ILE A CG1 1 
ATOM   4145 C CG2 . ILE A 1 625  ? 170.493 154.266 150.806 1.00 62.02  ? 625  ILE A CG2 1 
ATOM   4146 C CD1 . ILE A 1 625  ? 167.850 155.788 150.969 1.00 59.85  ? 625  ILE A CD1 1 
ATOM   4147 N N   . CYS A 1 626  ? 172.942 157.064 150.241 1.00 47.96  ? 626  CYS A N   1 
ATOM   4148 C CA  . CYS A 1 626  ? 174.355 157.053 150.603 1.00 46.08  ? 626  CYS A CA  1 
ATOM   4149 C C   . CYS A 1 626  ? 174.629 158.008 151.756 1.00 50.23  ? 626  CYS A C   1 
ATOM   4150 O O   . CYS A 1 626  ? 175.280 157.642 152.740 1.00 63.60  ? 626  CYS A O   1 
ATOM   4151 C CB  . CYS A 1 626  ? 175.207 157.412 149.388 1.00 43.29  ? 626  CYS A CB  1 
ATOM   4152 S SG  . CYS A 1 626  ? 176.977 157.490 149.718 1.00 57.62  ? 626  CYS A SG  1 
ATOM   4153 N N   . ALA A 1 627  ? 174.119 159.236 151.661 1.00 37.99  ? 627  ALA A N   1 
ATOM   4154 C CA  . ALA A 1 627  ? 174.337 160.207 152.726 1.00 45.88  ? 627  ALA A CA  1 
ATOM   4155 C C   . ALA A 1 627  ? 173.628 159.794 154.008 1.00 50.48  ? 627  ALA A C   1 
ATOM   4156 O O   . ALA A 1 627  ? 174.188 159.935 155.100 1.00 54.24  ? 627  ALA A O   1 
ATOM   4157 C CB  . ALA A 1 627  ? 173.876 161.591 152.280 1.00 50.51  ? 627  ALA A CB  1 
ATOM   4158 N N   . PHE A 1 628  ? 172.397 159.289 153.901 1.00 50.53  ? 628  PHE A N   1 
ATOM   4159 C CA  . PHE A 1 628  ? 171.676 158.841 155.087 1.00 50.29  ? 628  PHE A CA  1 
ATOM   4160 C C   . PHE A 1 628  ? 172.454 157.755 155.818 1.00 50.65  ? 628  PHE A C   1 
ATOM   4161 O O   . PHE A 1 628  ? 172.661 157.830 157.037 1.00 51.87  ? 628  PHE A O   1 
ATOM   4162 C CB  . PHE A 1 628  ? 170.288 158.346 154.676 1.00 43.34  ? 628  PHE A CB  1 
ATOM   4163 C CG  . PHE A 1 628  ? 169.560 157.591 155.747 1.00 46.18  ? 628  PHE A CG  1 
ATOM   4164 C CD1 . PHE A 1 628  ? 168.901 158.262 156.760 1.00 49.84  ? 628  PHE A CD1 1 
ATOM   4165 C CD2 . PHE A 1 628  ? 169.508 156.210 155.723 1.00 54.47  ? 628  PHE A CD2 1 
ATOM   4166 C CE1 . PHE A 1 628  ? 168.222 157.568 157.739 1.00 48.26  ? 628  PHE A CE1 1 
ATOM   4167 C CE2 . PHE A 1 628  ? 168.831 155.512 156.699 1.00 49.42  ? 628  PHE A CE2 1 
ATOM   4168 C CZ  . PHE A 1 628  ? 168.187 156.192 157.707 1.00 48.70  ? 628  PHE A CZ  1 
ATOM   4169 N N   . SER A 1 629  ? 172.920 156.750 155.078 1.00 43.36  ? 629  SER A N   1 
ATOM   4170 C CA  . SER A 1 629  ? 173.670 155.660 155.685 1.00 39.36  ? 629  SER A CA  1 
ATOM   4171 C C   . SER A 1 629  ? 174.992 156.145 156.262 1.00 49.47  ? 629  SER A C   1 
ATOM   4172 O O   . SER A 1 629  ? 175.391 155.711 157.346 1.00 60.77  ? 629  SER A O   1 
ATOM   4173 C CB  . SER A 1 629  ? 173.905 154.558 154.657 1.00 50.33  ? 629  SER A CB  1 
ATOM   4174 O OG  . SER A 1 629  ? 172.678 154.079 154.140 1.00 52.76  ? 629  SER A OG  1 
ATOM   4175 N N   . LEU A 1 630  ? 175.692 157.036 155.554 1.00 44.24  ? 630  LEU A N   1 
ATOM   4176 C CA  . LEU A 1 630  ? 176.964 157.537 156.062 1.00 37.74  ? 630  LEU A CA  1 
ATOM   4177 C C   . LEU A 1 630  ? 176.773 158.301 157.364 1.00 40.11  ? 630  LEU A C   1 
ATOM   4178 O O   . LEU A 1 630  ? 177.521 158.104 158.330 1.00 53.60  ? 630  LEU A O   1 
ATOM   4179 C CB  . LEU A 1 630  ? 177.636 158.424 155.017 1.00 39.58  ? 630  LEU A CB  1 
ATOM   4180 C CG  . LEU A 1 630  ? 178.333 157.715 153.861 1.00 43.44  ? 630  LEU A CG  1 
ATOM   4181 C CD1 . LEU A 1 630  ? 178.885 158.730 152.882 1.00 43.12  ? 630  LEU A CD1 1 
ATOM   4182 C CD2 . LEU A 1 630  ? 179.437 156.823 154.387 1.00 43.70  ? 630  LEU A CD2 1 
ATOM   4183 N N   . PHE A 1 631  ? 175.773 159.185 157.407 1.00 39.60  ? 631  PHE A N   1 
ATOM   4184 C CA  . PHE A 1 631  ? 175.522 159.943 158.625 1.00 42.20  ? 631  PHE A CA  1 
ATOM   4185 C C   . PHE A 1 631  ? 175.143 159.022 159.771 1.00 52.90  ? 631  PHE A C   1 
ATOM   4186 O O   . PHE A 1 631  ? 175.637 159.183 160.893 1.00 56.09  ? 631  PHE A O   1 
ATOM   4187 C CB  . PHE A 1 631  ? 174.432 160.987 158.389 1.00 41.94  ? 631  PHE A CB  1 
ATOM   4188 C CG  . PHE A 1 631  ? 174.926 162.235 157.722 1.00 49.19  ? 631  PHE A CG  1 
ATOM   4189 C CD1 . PHE A 1 631  ? 175.795 163.084 158.376 1.00 50.06  ? 631  PHE A CD1 1 
ATOM   4190 C CD2 . PHE A 1 631  ? 174.515 162.564 156.446 1.00 49.33  ? 631  PHE A CD2 1 
ATOM   4191 C CE1 . PHE A 1 631  ? 176.250 164.230 157.767 1.00 43.16  ? 631  PHE A CE1 1 
ATOM   4192 C CE2 . PHE A 1 631  ? 174.968 163.708 155.833 1.00 49.98  ? 631  PHE A CE2 1 
ATOM   4193 C CZ  . PHE A 1 631  ? 175.836 164.540 156.495 1.00 46.12  ? 631  PHE A CZ  1 
ATOM   4194 N N   . THR A 1 632  ? 174.283 158.036 159.508 1.00 48.25  ? 632  THR A N   1 
ATOM   4195 C CA  . THR A 1 632  ? 173.880 157.130 160.575 1.00 33.27  ? 632  THR A CA  1 
ATOM   4196 C C   . THR A 1 632  ? 175.059 156.308 161.077 1.00 38.98  ? 632  THR A C   1 
ATOM   4197 O O   . THR A 1 632  ? 175.209 156.107 162.285 1.00 54.35  ? 632  THR A O   1 
ATOM   4198 C CB  . THR A 1 632  ? 172.754 156.221 160.100 1.00 41.19  ? 632  THR A CB  1 
ATOM   4199 O OG1 . THR A 1 632  ? 171.828 156.985 159.320 1.00 53.61  ? 632  THR A OG1 1 
ATOM   4200 C CG2 . THR A 1 632  ? 172.024 155.643 161.292 1.00 42.81  ? 632  THR A CG2 1 
ATOM   4201 N N   . ALA A 1 633  ? 175.914 155.833 160.170 1.00 37.91  ? 633  ALA A N   1 
ATOM   4202 C CA  . ALA A 1 633  ? 177.063 155.036 160.583 1.00 31.45  ? 633  ALA A CA  1 
ATOM   4203 C C   . ALA A 1 633  ? 178.048 155.858 161.403 1.00 37.21  ? 633  ALA A C   1 
ATOM   4204 O O   . ALA A 1 633  ? 178.548 155.389 162.433 1.00 49.68  ? 633  ALA A O   1 
ATOM   4205 C CB  . ALA A 1 633  ? 177.753 154.440 159.359 1.00 34.88  ? 633  ALA A CB  1 
ATOM   4206 N N   . SER A 1 634  ? 178.344 157.082 160.962 1.00 39.96  ? 634  SER A N   1 
ATOM   4207 C CA  . SER A 1 634  ? 179.252 157.931 161.725 1.00 45.65  ? 634  SER A CA  1 
ATOM   4208 C C   . SER A 1 634  ? 178.678 158.253 163.097 1.00 49.84  ? 634  SER A C   1 
ATOM   4209 O O   . SER A 1 634  ? 179.395 158.221 164.108 1.00 54.45  ? 634  SER A O   1 
ATOM   4210 C CB  . SER A 1 634  ? 179.544 159.213 160.950 1.00 45.13  ? 634  SER A CB  1 
ATOM   4211 O OG  . SER A 1 634  ? 180.438 160.044 161.666 1.00 43.69  ? 634  SER A OG  1 
ATOM   4212 N N   . SER A 1 635  ? 177.380 158.560 163.154 1.00 38.98  ? 635  SER A N   1 
ATOM   4213 C CA  . SER A 1 635  ? 176.748 158.849 164.432 1.00 17.93  ? 635  SER A CA  1 
ATOM   4214 C C   . SER A 1 635  ? 176.790 157.638 165.350 1.00 26.51  ? 635  SER A C   1 
ATOM   4215 O O   . SER A 1 635  ? 177.040 157.774 166.549 1.00 45.94  ? 635  SER A O   1 
ATOM   4216 C CB  . SER A 1 635  ? 175.311 159.309 164.211 1.00 29.50  ? 635  SER A CB  1 
ATOM   4217 O OG  . SER A 1 635  ? 175.272 160.500 163.448 1.00 41.54  ? 635  SER A OG  1 
ATOM   4218 N N   . LEU A 1 636  ? 176.554 156.443 164.806 1.00 33.64  ? 636  LEU A N   1 
ATOM   4219 C CA  . LEU A 1 636  ? 176.606 155.238 165.626 1.00 34.00  ? 636  LEU A CA  1 
ATOM   4220 C C   . LEU A 1 636  ? 178.010 154.987 166.157 1.00 41.94  ? 636  LEU A C   1 
ATOM   4221 O O   . LEU A 1 636  ? 178.180 154.606 167.319 1.00 44.15  ? 636  LEU A O   1 
ATOM   4222 C CB  . LEU A 1 636  ? 176.114 154.035 164.826 1.00 22.28  ? 636  LEU A CB  1 
ATOM   4223 C CG  . LEU A 1 636  ? 174.610 153.984 164.573 1.00 31.39  ? 636  LEU A CG  1 
ATOM   4224 C CD1 . LEU A 1 636  ? 174.254 152.757 163.764 1.00 36.27  ? 636  LEU A CD1 1 
ATOM   4225 C CD2 . LEU A 1 636  ? 173.859 153.995 165.886 1.00 44.73  ? 636  LEU A CD2 1 
ATOM   4226 N N   . PHE A 1 637  ? 179.031 155.189 165.323 1.00 38.68  ? 637  PHE A N   1 
ATOM   4227 C CA  . PHE A 1 637  ? 180.401 154.977 165.780 1.00 28.24  ? 637  PHE A CA  1 
ATOM   4228 C C   . PHE A 1 637  ? 180.763 155.942 166.902 1.00 42.07  ? 637  PHE A C   1 
ATOM   4229 O O   . PHE A 1 637  ? 181.301 155.539 167.945 1.00 54.05  ? 637  PHE A O   1 
ATOM   4230 C CB  . PHE A 1 637  ? 181.372 155.127 164.612 1.00 25.98  ? 637  PHE A CB  1 
ATOM   4231 C CG  . PHE A 1 637  ? 182.811 155.096 165.020 1.00 40.12  ? 637  PHE A CG  1 
ATOM   4232 C CD1 . PHE A 1 637  ? 183.402 153.917 165.426 1.00 42.04  ? 637  PHE A CD1 1 
ATOM   4233 C CD2 . PHE A 1 637  ? 183.575 156.246 164.996 1.00 45.20  ? 637  PHE A CD2 1 
ATOM   4234 C CE1 . PHE A 1 637  ? 184.725 153.885 165.803 1.00 40.26  ? 637  PHE A CE1 1 
ATOM   4235 C CE2 . PHE A 1 637  ? 184.899 156.220 165.371 1.00 42.60  ? 637  PHE A CE2 1 
ATOM   4236 C CZ  . PHE A 1 637  ? 185.474 155.038 165.775 1.00 40.05  ? 637  PHE A CZ  1 
ATOM   4237 N N   . PHE A 1 638  ? 180.469 157.228 166.711 1.00 47.33  ? 638  PHE A N   1 
ATOM   4238 C CA  . PHE A 1 638  ? 180.805 158.188 167.754 1.00 40.13  ? 638  PHE A CA  1 
ATOM   4239 C C   . PHE A 1 638  ? 179.950 157.985 168.998 1.00 44.84  ? 638  PHE A C   1 
ATOM   4240 O O   . PHE A 1 638  ? 180.423 158.225 170.112 1.00 53.54  ? 638  PHE A O   1 
ATOM   4241 C CB  . PHE A 1 638  ? 180.683 159.613 167.221 1.00 39.57  ? 638  PHE A CB  1 
ATOM   4242 C CG  . PHE A 1 638  ? 181.849 160.035 166.375 1.00 46.17  ? 638  PHE A CG  1 
ATOM   4243 C CD1 . PHE A 1 638  ? 183.029 160.450 166.963 1.00 44.53  ? 638  PHE A CD1 1 
ATOM   4244 C CD2 . PHE A 1 638  ? 181.771 160.005 164.997 1.00 47.87  ? 638  PHE A CD2 1 
ATOM   4245 C CE1 . PHE A 1 638  ? 184.105 160.833 166.192 1.00 44.21  ? 638  PHE A CE1 1 
ATOM   4246 C CE2 . PHE A 1 638  ? 182.844 160.387 164.221 1.00 45.67  ? 638  PHE A CE2 1 
ATOM   4247 C CZ  . PHE A 1 638  ? 184.011 160.801 164.820 1.00 44.55  ? 638  PHE A CZ  1 
ATOM   4248 N N   . GLY A 1 639  ? 178.712 157.518 168.840 1.00 45.95  ? 639  GLY A N   1 
ATOM   4249 C CA  . GLY A 1 639  ? 177.907 157.179 170.000 1.00 43.45  ? 639  GLY A CA  1 
ATOM   4250 C C   . GLY A 1 639  ? 178.461 155.991 170.758 1.00 46.74  ? 639  GLY A C   1 
ATOM   4251 O O   . GLY A 1 639  ? 178.376 155.934 171.984 1.00 58.30  ? 639  GLY A O   1 
ATOM   4252 N N   . TYR A 1 640  ? 179.026 155.020 170.040 1.00 42.67  ? 640  TYR A N   1 
ATOM   4253 C CA  . TYR A 1 640  ? 179.697 153.909 170.705 1.00 41.78  ? 640  TYR A CA  1 
ATOM   4254 C C   . TYR A 1 640  ? 180.897 154.396 171.503 1.00 43.70  ? 640  TYR A C   1 
ATOM   4255 O O   . TYR A 1 640  ? 181.114 153.966 172.644 1.00 52.51  ? 640  TYR A O   1 
ATOM   4256 C CB  . TYR A 1 640  ? 180.120 152.865 169.675 1.00 42.11  ? 640  TYR A CB  1 
ATOM   4257 C CG  . TYR A 1 640  ? 181.120 151.859 170.187 1.00 41.65  ? 640  TYR A CG  1 
ATOM   4258 C CD1 . TYR A 1 640  ? 180.744 150.872 171.082 1.00 46.85  ? 640  TYR A CD1 1 
ATOM   4259 C CD2 . TYR A 1 640  ? 182.439 151.889 169.763 1.00 44.00  ? 640  TYR A CD2 1 
ATOM   4260 C CE1 . TYR A 1 640  ? 181.653 149.948 171.547 1.00 49.44  ? 640  TYR A CE1 1 
ATOM   4261 C CE2 . TYR A 1 640  ? 183.355 150.968 170.222 1.00 51.53  ? 640  TYR A CE2 1 
ATOM   4262 C CZ  . TYR A 1 640  ? 182.956 150.001 171.114 1.00 53.79  ? 640  TYR A CZ  1 
ATOM   4263 O OH  . TYR A 1 640  ? 183.865 149.079 171.577 1.00 52.60  ? 640  TYR A OH  1 
ATOM   4264 N N   . LEU A 1 641  ? 181.685 155.303 170.922 1.00 48.65  ? 641  LEU A N   1 
ATOM   4265 C CA  . LEU A 1 641  ? 182.805 155.874 171.669 1.00 47.38  ? 641  LEU A CA  1 
ATOM   4266 C C   . LEU A 1 641  ? 182.318 156.630 172.902 1.00 41.45  ? 641  LEU A C   1 
ATOM   4267 O O   . LEU A 1 641  ? 182.913 156.529 173.986 1.00 51.34  ? 641  LEU A O   1 
ATOM   4268 C CB  . LEU A 1 641  ? 183.625 156.793 170.768 1.00 42.88  ? 641  LEU A CB  1 
ATOM   4269 C CG  . LEU A 1 641  ? 184.355 156.110 169.615 1.00 39.95  ? 641  LEU A CG  1 
ATOM   4270 C CD1 . LEU A 1 641  ? 185.192 157.115 168.852 1.00 45.40  ? 641  LEU A CD1 1 
ATOM   4271 C CD2 . LEU A 1 641  ? 185.217 154.980 170.139 1.00 43.56  ? 641  LEU A CD2 1 
ATOM   4272 N N   . MET A 1 642  ? 181.235 157.395 172.754 1.00 38.26  ? 642  MET A N   1 
ATOM   4273 C CA  . MET A 1 642  ? 180.674 158.112 173.892 1.00 47.33  ? 642  MET A CA  1 
ATOM   4274 C C   . MET A 1 642  ? 180.193 157.147 174.964 1.00 47.88  ? 642  MET A C   1 
ATOM   4275 O O   . MET A 1 642  ? 180.402 157.384 176.153 1.00 53.02  ? 642  MET A O   1 
ATOM   4276 C CB  . MET A 1 642  ? 179.536 159.024 173.437 1.00 48.85  ? 642  MET A CB  1 
ATOM   4277 C CG  . MET A 1 642  ? 179.973 160.159 172.529 1.00 53.62  ? 642  MET A CG  1 
ATOM   4278 S SD  . MET A 1 642  ? 181.179 161.254 173.294 1.00 63.05  ? 642  MET A SD  1 
ATOM   4279 C CE  . MET A 1 642  ? 180.191 161.968 174.601 1.00 50.98  ? 642  MET A CE  1 
ATOM   4280 N N   . VAL A 1 643  ? 179.561 156.045 174.566 1.00 47.91  ? 643  VAL A N   1 
ATOM   4281 C CA  . VAL A 1 643  ? 179.143 155.041 175.539 1.00 44.50  ? 643  VAL A CA  1 
ATOM   4282 C C   . VAL A 1 643  ? 180.352 154.490 176.278 1.00 42.95  ? 643  VAL A C   1 
ATOM   4283 O O   . VAL A 1 643  ? 180.322 154.306 177.500 1.00 55.27  ? 643  VAL A O   1 
ATOM   4284 C CB  . VAL A 1 643  ? 178.344 153.923 174.846 1.00 41.03  ? 643  VAL A CB  1 
ATOM   4285 C CG1 . VAL A 1 643  ? 178.219 152.718 175.756 1.00 44.97  ? 643  VAL A CG1 1 
ATOM   4286 C CG2 . VAL A 1 643  ? 176.970 154.427 174.450 1.00 51.32  ? 643  VAL A CG2 1 
ATOM   4287 N N   . LEU A 1 644  ? 181.439 154.234 175.552 1.00 45.41  ? 644  LEU A N   1 
ATOM   4288 C CA  . LEU A 1 644  ? 182.620 153.663 176.188 1.00 47.55  ? 644  LEU A CA  1 
ATOM   4289 C C   . LEU A 1 644  ? 183.272 154.624 177.173 1.00 46.83  ? 644  LEU A C   1 
ATOM   4290 O O   . LEU A 1 644  ? 183.837 154.180 178.177 1.00 45.77  ? 644  LEU A O   1 
ATOM   4291 C CB  . LEU A 1 644  ? 183.635 153.229 175.136 1.00 47.11  ? 644  LEU A CB  1 
ATOM   4292 C CG  . LEU A 1 644  ? 183.459 151.806 174.617 1.00 45.18  ? 644  LEU A CG  1 
ATOM   4293 C CD1 . LEU A 1 644  ? 184.670 151.397 173.804 1.00 51.06  ? 644  LEU A CD1 1 
ATOM   4294 C CD2 . LEU A 1 644  ? 183.236 150.848 175.772 1.00 47.13  ? 644  LEU A CD2 1 
ATOM   4295 N N   . THR A 1 645  ? 183.241 155.930 176.904 1.00 49.22  ? 645  THR A N   1 
ATOM   4296 C CA  . THR A 1 645  ? 183.941 156.874 177.774 1.00 46.61  ? 645  THR A CA  1 
ATOM   4297 C C   . THR A 1 645  ? 183.009 157.697 178.659 1.00 54.48  ? 645  THR A C   1 
ATOM   4298 O O   . THR A 1 645  ? 183.060 157.593 179.892 1.00 52.56  ? 645  THR A O   1 
ATOM   4299 C CB  . THR A 1 645  ? 184.806 157.808 176.922 1.00 47.63  ? 645  THR A CB  1 
ATOM   4300 O OG1 . THR A 1 645  ? 183.960 158.631 176.111 1.00 53.61  ? 645  THR A OG1 1 
ATOM   4301 C CG2 . THR A 1 645  ? 185.719 157.005 176.021 1.00 48.32  ? 645  THR A CG2 1 
ATOM   4302 N N   . PHE A 1 646  ? 182.126 158.488 178.053 1.00 53.68  ? 646  PHE A N   1 
ATOM   4303 C CA  . PHE A 1 646  ? 181.289 159.421 178.797 1.00 38.98  ? 646  PHE A CA  1 
ATOM   4304 C C   . PHE A 1 646  ? 180.323 158.682 179.711 1.00 43.51  ? 646  PHE A C   1 
ATOM   4305 O O   . PHE A 1 646  ? 180.208 159.000 180.899 1.00 58.05  ? 646  PHE A O   1 
ATOM   4306 C CB  . PHE A 1 646  ? 180.535 160.308 177.804 1.00 51.49  ? 646  PHE A CB  1 
ATOM   4307 C CG  . PHE A 1 646  ? 179.748 161.422 178.432 1.00 52.85  ? 646  PHE A CG  1 
ATOM   4308 C CD1 . PHE A 1 646  ? 180.346 162.635 178.711 1.00 53.48  ? 646  PHE A CD1 1 
ATOM   4309 C CD2 . PHE A 1 646  ? 178.401 161.271 178.701 1.00 49.80  ? 646  PHE A CD2 1 
ATOM   4310 C CE1 . PHE A 1 646  ? 179.623 163.665 179.270 1.00 52.73  ? 646  PHE A CE1 1 
ATOM   4311 C CE2 . PHE A 1 646  ? 177.673 162.297 179.257 1.00 50.21  ? 646  PHE A CE2 1 
ATOM   4312 C CZ  . PHE A 1 646  ? 178.285 163.496 179.542 1.00 52.49  ? 646  PHE A CZ  1 
ATOM   4313 N N   . LEU A 1 647  ? 179.625 157.683 179.173 1.00 45.28  ? 647  LEU A N   1 
ATOM   4314 C CA  . LEU A 1 647  ? 178.681 156.916 179.975 1.00 47.26  ? 647  LEU A CA  1 
ATOM   4315 C C   . LEU A 1 647  ? 179.381 156.053 181.012 1.00 52.55  ? 647  LEU A C   1 
ATOM   4316 O O   . LEU A 1 647  ? 178.885 155.915 182.135 1.00 62.18  ? 647  LEU A O   1 
ATOM   4317 C CB  . LEU A 1 647  ? 177.819 156.034 179.076 1.00 48.90  ? 647  LEU A CB  1 
ATOM   4318 C CG  . LEU A 1 647  ? 176.835 155.147 179.831 1.00 52.14  ? 647  LEU A CG  1 
ATOM   4319 C CD1 . LEU A 1 647  ? 175.655 155.964 180.318 1.00 53.70  ? 647  LEU A CD1 1 
ATOM   4320 C CD2 . LEU A 1 647  ? 176.383 153.994 178.964 1.00 54.05  ? 647  LEU A CD2 1 
ATOM   4321 N N   . LEU A 1 648  ? 180.521 155.460 180.659 1.00 52.27  ? 648  LEU A N   1 
ATOM   4322 C CA  . LEU A 1 648  ? 181.231 154.612 181.607 1.00 48.15  ? 648  LEU A CA  1 
ATOM   4323 C C   . LEU A 1 648  ? 181.738 155.418 182.794 1.00 56.04  ? 648  LEU A C   1 
ATOM   4324 O O   . LEU A 1 648  ? 181.767 154.918 183.923 1.00 59.27  ? 648  LEU A O   1 
ATOM   4325 C CB  . LEU A 1 648  ? 182.384 153.897 180.912 1.00 55.42  ? 648  LEU A CB  1 
ATOM   4326 C CG  . LEU A 1 648  ? 183.110 152.849 181.748 1.00 55.03  ? 648  LEU A CG  1 
ATOM   4327 C CD1 . LEU A 1 648  ? 182.145 151.760 182.163 1.00 47.06  ? 648  LEU A CD1 1 
ATOM   4328 C CD2 . LEU A 1 648  ? 184.269 152.269 180.966 1.00 54.00  ? 648  LEU A CD2 1 
ATOM   4329 N N   . SER A 1 649  ? 182.145 156.668 182.563 1.00 52.00  ? 649  SER A N   1 
ATOM   4330 C CA  . SER A 1 649  ? 182.571 157.502 183.682 1.00 54.34  ? 649  SER A CA  1 
ATOM   4331 C C   . SER A 1 649  ? 181.417 157.779 184.641 1.00 60.47  ? 649  SER A C   1 
ATOM   4332 O O   . SER A 1 649  ? 181.594 157.740 185.866 1.00 61.66  ? 649  SER A O   1 
ATOM   4333 C CB  . SER A 1 649  ? 183.166 158.804 183.161 1.00 57.34  ? 649  SER A CB  1 
ATOM   4334 O OG  . SER A 1 649  ? 184.185 158.540 182.218 1.00 61.48  ? 649  SER A OG  1 
ATOM   4335 N N   . PHE A 1 650  ? 180.227 158.061 184.107 1.00 52.24  ? 650  PHE A N   1 
ATOM   4336 C CA  . PHE A 1 650  ? 179.066 158.252 184.971 1.00 49.44  ? 650  PHE A CA  1 
ATOM   4337 C C   . PHE A 1 650  ? 178.713 156.967 185.702 1.00 59.83  ? 650  PHE A C   1 
ATOM   4338 O O   . PHE A 1 650  ? 178.286 157.000 186.863 1.00 67.40  ? 650  PHE A O   1 
ATOM   4339 C CB  . PHE A 1 650  ? 177.875 158.750 184.157 1.00 46.61  ? 650  PHE A CB  1 
ATOM   4340 C CG  . PHE A 1 650  ? 177.869 160.229 183.953 1.00 54.47  ? 650  PHE A CG  1 
ATOM   4341 C CD1 . PHE A 1 650  ? 177.345 161.068 184.917 1.00 57.48  ? 650  PHE A CD1 1 
ATOM   4342 C CD2 . PHE A 1 650  ? 178.396 160.784 182.805 1.00 57.25  ? 650  PHE A CD2 1 
ATOM   4343 C CE1 . PHE A 1 650  ? 177.341 162.431 184.736 1.00 58.84  ? 650  PHE A CE1 1 
ATOM   4344 C CE2 . PHE A 1 650  ? 178.395 162.147 182.620 1.00 56.89  ? 650  PHE A CE2 1 
ATOM   4345 C CZ  . PHE A 1 650  ? 177.867 162.972 183.586 1.00 60.01  ? 650  PHE A CZ  1 
ATOM   4346 N N   . LEU A 1 651  ? 178.874 155.825 185.035 1.00 51.92  ? 651  LEU A N   1 
ATOM   4347 C CA  . LEU A 1 651  ? 178.660 154.548 185.704 1.00 42.91  ? 651  LEU A CA  1 
ATOM   4348 C C   . LEU A 1 651  ? 179.621 154.383 186.871 1.00 53.72  ? 651  LEU A C   1 
ATOM   4349 O O   . LEU A 1 651  ? 179.227 153.929 187.948 1.00 62.06  ? 651  LEU A O   1 
ATOM   4350 C CB  . LEU A 1 651  ? 178.823 153.399 184.714 1.00 52.43  ? 651  LEU A CB  1 
ATOM   4351 C CG  . LEU A 1 651  ? 178.573 152.008 185.295 1.00 54.34  ? 651  LEU A CG  1 
ATOM   4352 C CD1 . LEU A 1 651  ? 177.087 151.774 185.486 1.00 51.78  ? 651  LEU A CD1 1 
ATOM   4353 C CD2 . LEU A 1 651  ? 179.181 150.934 184.415 1.00 54.57  ? 651  LEU A CD2 1 
ATOM   4354 N N   . CYS A 1 652  ? 180.886 154.755 186.674 1.00 54.74  ? 652  CYS A N   1 
ATOM   4355 C CA  . CYS A 1 652  ? 181.860 154.680 187.758 1.00 52.90  ? 652  CYS A CA  1 
ATOM   4356 C C   . CYS A 1 652  ? 181.481 155.603 188.907 1.00 59.93  ? 652  CYS A C   1 
ATOM   4357 O O   . CYS A 1 652  ? 181.592 155.227 190.081 1.00 65.64  ? 652  CYS A O   1 
ATOM   4358 C CB  . CYS A 1 652  ? 183.253 155.022 187.235 1.00 49.36  ? 652  CYS A CB  1 
ATOM   4359 S SG  . CYS A 1 652  ? 183.905 153.838 186.044 1.00 69.03  ? 652  CYS A SG  1 
ATOM   4360 N N   . ILE A 1 653  ? 181.034 156.818 188.591 1.00 60.66  ? 653  ILE A N   1 
ATOM   4361 C CA  . ILE A 1 653  ? 180.658 157.765 189.638 1.00 62.50  ? 653  ILE A CA  1 
ATOM   4362 C C   . ILE A 1 653  ? 179.483 157.227 190.446 1.00 59.86  ? 653  ILE A C   1 
ATOM   4363 O O   . ILE A 1 653  ? 179.490 157.248 191.685 1.00 68.02  ? 653  ILE A O   1 
ATOM   4364 C CB  . ILE A 1 653  ? 180.341 159.140 189.028 1.00 62.22  ? 653  ILE A CB  1 
ATOM   4365 C CG1 . ILE A 1 653  ? 181.601 159.747 188.412 1.00 61.72  ? 653  ILE A CG1 1 
ATOM   4366 C CG2 . ILE A 1 653  ? 179.763 160.065 190.079 1.00 62.68  ? 653  ILE A CG2 1 
ATOM   4367 C CD1 . ILE A 1 653  ? 181.382 161.106 187.798 1.00 62.93  ? 653  ILE A CD1 1 
ATOM   4368 N N   . GLU A 1 654  ? 178.457 156.726 189.756 1.00 60.08  ? 654  GLU A N   1 
ATOM   4369 C CA  . GLU A 1 654  ? 177.301 156.197 190.468 1.00 67.06  ? 654  GLU A CA  1 
ATOM   4370 C C   . GLU A 1 654  ? 177.643 154.926 191.232 1.00 71.18  ? 654  GLU A C   1 
ATOM   4371 O O   . GLU A 1 654  ? 177.054 154.665 192.284 1.00 74.65  ? 654  GLU A O   1 
ATOM   4372 C CB  . GLU A 1 654  ? 176.143 155.952 189.503 1.00 66.70  ? 654  GLU A CB  1 
ATOM   4373 C CG  . GLU A 1 654  ? 175.195 157.134 189.392 1.00 69.24  ? 654  GLU A CG  1 
ATOM   4374 C CD  . GLU A 1 654  ? 173.888 156.776 188.718 1.00 72.86  ? 654  GLU A CD  1 
ATOM   4375 O OE1 . GLU A 1 654  ? 173.908 155.963 187.774 1.00 75.11  ? 654  GLU A OE1 1 
ATOM   4376 O OE2 . GLU A 1 654  ? 172.837 157.302 189.137 1.00 75.63  ? 654  GLU A OE2 1 
ATOM   4377 N N   . ALA A 1 655  ? 178.592 154.131 190.736 1.00 59.16  ? 655  ALA A N   1 
ATOM   4378 C CA  . ALA A 1 655  ? 179.035 152.965 191.490 1.00 51.81  ? 655  ALA A CA  1 
ATOM   4379 C C   . ALA A 1 655  ? 179.746 153.377 192.769 1.00 60.66  ? 655  ALA A C   1 
ATOM   4380 O O   . ALA A 1 655  ? 179.564 152.751 193.818 1.00 72.05  ? 655  ALA A O   1 
ATOM   4381 C CB  . ALA A 1 655  ? 179.943 152.094 190.628 1.00 54.96  ? 655  ALA A CB  1 
ATOM   4382 N N   . LYS A 1 656  ? 180.572 154.423 192.699 1.00 59.71  ? 656  LYS A N   1 
ATOM   4383 C CA  . LYS A 1 656  ? 181.195 154.939 193.913 1.00 59.62  ? 656  LYS A CA  1 
ATOM   4384 C C   . LYS A 1 656  ? 180.142 155.426 194.899 1.00 57.98  ? 656  LYS A C   1 
ATOM   4385 O O   . LYS A 1 656  ? 180.241 155.170 196.107 1.00 61.17  ? 656  LYS A O   1 
ATOM   4386 C CB  . LYS A 1 656  ? 182.168 156.066 193.572 1.00 63.96  ? 656  LYS A CB  1 
ATOM   4387 C CG  . LYS A 1 656  ? 183.359 155.638 192.738 1.00 57.16  ? 656  LYS A CG  1 
ATOM   4388 C CD  . LYS A 1 656  ? 184.274 156.817 192.464 1.00 65.29  ? 656  LYS A CD  1 
ATOM   4389 C CE  . LYS A 1 656  ? 185.452 156.417 191.595 1.00 64.98  ? 656  LYS A CE  1 
ATOM   4390 N NZ  . LYS A 1 656  ? 186.361 157.565 191.333 1.00 61.94  ? 656  LYS A NZ  1 
ATOM   4391 N N   . LEU A 1 657  ? 179.123 156.127 194.401 1.00 59.34  ? 657  LEU A N   1 
ATOM   4392 C CA  . LEU A 1 657  ? 178.054 156.593 195.280 1.00 62.51  ? 657  LEU A CA  1 
ATOM   4393 C C   . LEU A 1 657  ? 177.306 155.425 195.914 1.00 65.77  ? 657  LEU A C   1 
ATOM   4394 O O   . LEU A 1 657  ? 176.963 155.468 197.102 1.00 68.27  ? 657  LEU A O   1 
ATOM   4395 C CB  . LEU A 1 657  ? 177.090 157.493 194.509 1.00 60.27  ? 657  LEU A CB  1 
ATOM   4396 C CG  . LEU A 1 657  ? 177.666 158.815 194.000 1.00 62.66  ? 657  LEU A CG  1 
ATOM   4397 C CD1 . LEU A 1 657  ? 176.565 159.692 193.431 1.00 62.07  ? 657  LEU A CD1 1 
ATOM   4398 C CD2 . LEU A 1 657  ? 178.417 159.538 195.104 1.00 64.10  ? 657  LEU A CD2 1 
ATOM   4399 N N   . GLU A 1 658  ? 177.038 154.375 195.136 1.00 62.00  ? 658  GLU A N   1 
ATOM   4400 C CA  . GLU A 1 658  ? 176.371 153.194 195.676 1.00 55.49  ? 658  GLU A CA  1 
ATOM   4401 C C   . GLU A 1 658  ? 177.222 152.518 196.743 1.00 60.19  ? 658  GLU A C   1 
ATOM   4402 O O   . GLU A 1 658  ? 176.703 152.077 197.775 1.00 65.80  ? 658  GLU A O   1 
ATOM   4403 C CB  . GLU A 1 658  ? 176.052 152.216 194.548 1.00 59.30  ? 658  GLU A CB  1 
ATOM   4404 C CG  . GLU A 1 658  ? 175.590 150.850 195.017 1.00 62.36  ? 658  GLU A CG  1 
ATOM   4405 C CD  . GLU A 1 658  ? 175.450 149.863 193.877 1.00 63.72  ? 658  GLU A CD  1 
ATOM   4406 O OE1 . GLU A 1 658  ? 175.481 150.297 192.707 1.00 64.23  ? 658  GLU A OE1 1 
ATOM   4407 O OE2 . GLU A 1 658  ? 175.313 148.652 194.150 1.00 60.69  ? 658  GLU A OE2 1 
ATOM   4408 N N   . LYS A 1 659  ? 178.531 152.421 196.507 1.00 71.37  ? 659  LYS A N   1 
ATOM   4409 C CA  . LYS A 1 659  ? 179.421 151.838 197.505 1.00 68.35  ? 659  LYS A CA  1 
ATOM   4410 C C   . LYS A 1 659  ? 179.413 152.658 198.785 1.00 71.42  ? 659  LYS A C   1 
ATOM   4411 O O   . LYS A 1 659  ? 179.416 152.104 199.890 1.00 71.66  ? 659  LYS A O   1 
ATOM   4412 C CB  . LYS A 1 659  ? 180.839 151.730 196.950 1.00 67.55  ? 659  LYS A CB  1 
ATOM   4413 C CG  . LYS A 1 659  ? 181.826 151.080 197.900 1.00 69.63  ? 659  LYS A CG  1 
ATOM   4414 C CD  . LYS A 1 659  ? 181.402 149.664 198.243 1.00 72.47  ? 659  LYS A CD  1 
ATOM   4415 C CE  . LYS A 1 659  ? 182.399 149.000 199.176 1.00 74.44  ? 659  LYS A CE  1 
ATOM   4416 N NZ  . LYS A 1 659  ? 181.994 147.610 199.518 1.00 71.79  ? 659  LYS A NZ  1 
ATOM   4417 N N   . LYS A 1 660  ? 179.402 153.984 198.657 1.00 79.55  ? 660  LYS A N   1 
ATOM   4418 C CA  . LYS A 1 660  ? 179.278 154.846 199.825 1.00 77.01  ? 660  LYS A CA  1 
ATOM   4419 C C   . LYS A 1 660  ? 177.853 154.904 200.358 1.00 75.02  ? 660  LYS A C   1 
ATOM   4420 O O   . LYS A 1 660  ? 177.616 155.576 201.367 1.00 74.63  ? 660  LYS A O   1 
ATOM   4421 C CB  . LYS A 1 660  ? 179.775 156.251 199.490 1.00 77.29  ? 660  LYS A CB  1 
ATOM   4422 C CG  . LYS A 1 660  ? 181.223 156.295 199.033 1.00 76.91  ? 660  LYS A CG  1 
ATOM   4423 C CD  . LYS A 1 660  ? 181.595 157.667 198.498 1.00 78.85  ? 660  LYS A CD  1 
ATOM   4424 C CE  . LYS A 1 660  ? 181.445 158.741 199.562 1.00 80.77  ? 660  LYS A CE  1 
ATOM   4425 N NZ  . LYS A 1 660  ? 182.366 158.521 200.710 1.00 79.80  ? 660  LYS A NZ  1 
ATOM   4426 N N   . LYS A 1 661  ? 176.908 154.228 199.699 1.00 70.22  ? 661  LYS A N   1 
ATOM   4427 C CA  . LYS A 1 661  ? 175.518 154.139 200.147 1.00 70.79  ? 661  LYS A CA  1 
ATOM   4428 C C   . LYS A 1 661  ? 174.856 155.512 200.229 1.00 72.63  ? 661  LYS A C   1 
ATOM   4429 O O   . LYS A 1 661  ? 174.089 155.791 201.149 1.00 79.35  ? 661  LYS A O   1 
ATOM   4430 C CB  . LYS A 1 661  ? 175.407 153.407 201.486 1.00 69.19  ? 661  LYS A CB  1 
ATOM   4431 C CG  . LYS A 1 661  ? 175.853 151.959 201.435 1.00 72.91  ? 661  LYS A CG  1 
ATOM   4432 C CD  . LYS A 1 661  ? 175.599 151.257 202.757 1.00 75.09  ? 661  LYS A CD  1 
ATOM   4433 C CE  . LYS A 1 661  ? 176.089 149.819 202.719 1.00 73.83  ? 661  LYS A CE  1 
ATOM   4434 N NZ  . LYS A 1 661  ? 175.438 149.042 201.630 1.00 69.75  ? 661  LYS A NZ  1 
ATOM   4435 N N   . ARG A 1 662  ? 175.156 156.375 199.263 1.00 72.66  ? 662  ARG A N   1 
ATOM   4436 C CA  . ARG A 1 662  ? 174.495 157.666 199.134 1.00 71.26  ? 662  ARG A CA  1 
ATOM   4437 C C   . ARG A 1 662  ? 174.013 157.826 197.702 1.00 72.78  ? 662  ARG A C   1 
ATOM   4438 O O   . ARG A 1 662  ? 174.775 157.595 196.760 1.00 78.66  ? 662  ARG A O   1 
ATOM   4439 C CB  . ARG A 1 662  ? 175.431 158.814 199.519 1.00 71.07  ? 662  ARG A CB  1 
ATOM   4440 C CG  . ARG A 1 662  ? 176.897 158.439 199.533 1.00 76.07  ? 662  ARG A CG  1 
ATOM   4441 C CD  . ARG A 1 662  ? 177.744 159.578 200.070 1.00 75.86  ? 662  ARG A CD  1 
ATOM   4442 N NE  . ARG A 1 662  ? 177.269 160.034 201.370 1.00 78.69  ? 662  ARG A NE  1 
ATOM   4443 C CZ  . ARG A 1 662  ? 177.714 159.580 202.533 1.00 78.66  ? 662  ARG A CZ  1 
ATOM   4444 N NH1 . ARG A 1 662  ? 178.661 158.659 202.599 1.00 75.15  ? 662  ARG A NH1 1 
ATOM   4445 N NH2 . ARG A 1 662  ? 177.197 160.062 203.659 1.00 79.39  ? 662  ARG A NH2 1 
ATOM   4446 N N   . ASN A 1 663  ? 172.753 158.217 197.543 1.00 75.05  ? 663  ASN A N   1 
ATOM   4447 C CA  . ASN A 1 663  ? 172.163 158.344 196.222 1.00 73.30  ? 663  ASN A CA  1 
ATOM   4448 C C   . ASN A 1 663  ? 172.581 159.662 195.576 1.00 78.78  ? 663  ASN A C   1 
ATOM   4449 O O   . ASN A 1 663  ? 173.472 160.368 196.053 1.00 83.28  ? 663  ASN A O   1 
ATOM   4450 C CB  . ASN A 1 663  ? 170.644 158.227 196.307 1.00 73.01  ? 663  ASN A CB  1 
ATOM   4451 C CG  . ASN A 1 663  ? 170.055 159.114 197.378 1.00 79.02  ? 663  ASN A CG  1 
ATOM   4452 O OD1 . ASN A 1 663  ? 170.721 159.447 198.356 1.00 82.53  ? 663  ASN A OD1 1 
ATOM   4453 N ND2 . ASN A 1 663  ? 168.797 159.498 197.202 1.00 75.25  ? 663  ASN A ND2 1 
ATOM   4454 N N   . ILE A 1 664  ? 171.924 159.992 194.463 1.00 75.61  ? 664  ILE A N   1 
ATOM   4455 C CA  . ILE A 1 664  ? 172.303 161.172 193.689 1.00 74.29  ? 664  ILE A CA  1 
ATOM   4456 C C   . ILE A 1 664  ? 172.069 162.441 194.499 1.00 77.95  ? 664  ILE A C   1 
ATOM   4457 O O   . ILE A 1 664  ? 172.908 163.346 194.520 1.00 78.11  ? 664  ILE A O   1 
ATOM   4458 C CB  . ILE A 1 664  ? 171.540 161.210 192.353 1.00 72.38  ? 664  ILE A CB  1 
ATOM   4459 C CG1 . ILE A 1 664  ? 172.008 160.085 191.428 1.00 76.01  ? 664  ILE A CG1 1 
ATOM   4460 C CG2 . ILE A 1 664  ? 171.724 162.551 191.670 1.00 73.43  ? 664  ILE A CG2 1 
ATOM   4461 C CD1 . ILE A 1 664  ? 171.286 158.771 191.630 1.00 75.96  ? 664  ILE A CD1 1 
ATOM   4462 N N   . PHE A 1 665  ? 170.925 162.525 195.180 1.00 85.00  ? 665  PHE A N   1 
ATOM   4463 C CA  . PHE A 1 665  ? 170.599 163.738 195.925 1.00 82.33  ? 665  PHE A CA  1 
ATOM   4464 C C   . PHE A 1 665  ? 171.525 163.917 197.123 1.00 85.05  ? 665  PHE A C   1 
ATOM   4465 O O   . PHE A 1 665  ? 172.072 165.005 197.345 1.00 89.90  ? 665  PHE A O   1 
ATOM   4466 C CB  . PHE A 1 665  ? 169.138 163.698 196.369 1.00 82.13  ? 665  PHE A CB  1 
ATOM   4467 C CG  . PHE A 1 665  ? 168.160 163.674 195.232 1.00 85.34  ? 665  PHE A CG  1 
ATOM   4468 C CD1 . PHE A 1 665  ? 168.500 164.196 193.997 1.00 85.79  ? 665  PHE A CD1 1 
ATOM   4469 C CD2 . PHE A 1 665  ? 166.898 163.129 195.397 1.00 87.90  ? 665  PHE A CD2 1 
ATOM   4470 C CE1 . PHE A 1 665  ? 167.603 164.177 192.950 1.00 88.87  ? 665  PHE A CE1 1 
ATOM   4471 C CE2 . PHE A 1 665  ? 165.995 163.106 194.353 1.00 87.08  ? 665  PHE A CE2 1 
ATOM   4472 C CZ  . PHE A 1 665  ? 166.349 163.630 193.128 1.00 88.25  ? 665  PHE A CZ  1 
ATOM   4473 N N   . THR A 1 666  ? 171.709 162.858 197.911 1.00 79.92  ? 666  THR A N   1 
ATOM   4474 C CA  . THR A 1 666  ? 172.612 162.941 199.054 1.00 79.70  ? 666  THR A CA  1 
ATOM   4475 C C   . THR A 1 666  ? 174.047 163.176 198.601 1.00 85.30  ? 666  THR A C   1 
ATOM   4476 O O   . THR A 1 666  ? 174.790 163.936 199.236 1.00 85.27  ? 666  THR A O   1 
ATOM   4477 C CB  . THR A 1 666  ? 172.514 161.667 199.890 1.00 82.17  ? 666  THR A CB  1 
ATOM   4478 O OG1 . THR A 1 666  ? 171.137 161.367 200.140 1.00 79.56  ? 666  THR A OG1 1 
ATOM   4479 C CG2 . THR A 1 666  ? 173.230 161.845 201.215 1.00 85.01  ? 666  THR A CG2 1 
ATOM   4480 N N   . GLY A 1 667  ? 174.454 162.529 197.508 1.00 95.10  ? 667  GLY A N   1 
ATOM   4481 C CA  . GLY A 1 667  ? 175.775 162.776 196.961 1.00 90.95  ? 667  GLY A CA  1 
ATOM   4482 C C   . GLY A 1 667  ? 175.968 164.212 196.519 1.00 93.78  ? 667  GLY A C   1 
ATOM   4483 O O   . GLY A 1 667  ? 177.035 164.790 196.729 1.00 94.68  ? 667  GLY A O   1 
ATOM   4484 N N   . THR A 1 668  ? 174.941 164.806 195.907 1.00 94.78  ? 668  THR A N   1 
ATOM   4485 C CA  . THR A 1 668  ? 175.010 166.215 195.533 1.00 96.53  ? 668  THR A CA  1 
ATOM   4486 C C   . THR A 1 668  ? 175.113 167.103 196.765 1.00 95.50  ? 668  THR A C   1 
ATOM   4487 O O   . THR A 1 668  ? 175.883 168.072 196.781 1.00 95.14  ? 668  THR A O   1 
ATOM   4488 C CB  . THR A 1 668  ? 173.786 166.595 194.698 1.00 94.59  ? 668  THR A CB  1 
ATOM   4489 O OG1 . THR A 1 668  ? 173.784 165.842 193.479 1.00 94.34  ? 668  THR A OG1 1 
ATOM   4490 C CG2 . THR A 1 668  ? 173.796 168.080 194.369 1.00 92.55  ? 668  THR A CG2 1 
ATOM   4491 N N   . PHE A 1 669  ? 174.347 166.785 197.812 1.00 102.72 ? 669  PHE A N   1 
ATOM   4492 C CA  . PHE A 1 669  ? 174.425 167.566 199.043 1.00 104.81 ? 669  PHE A CA  1 
ATOM   4493 C C   . PHE A 1 669  ? 175.824 167.508 199.641 1.00 104.53 ? 669  PHE A C   1 
ATOM   4494 O O   . PHE A 1 669  ? 176.371 168.532 200.066 1.00 104.10 ? 669  PHE A O   1 
ATOM   4495 C CB  . PHE A 1 669  ? 173.393 167.069 200.057 1.00 104.34 ? 669  PHE A CB  1 
ATOM   4496 C CG  . PHE A 1 669  ? 171.970 167.370 199.679 1.00 103.63 ? 669  PHE A CG  1 
ATOM   4497 C CD1 . PHE A 1 669  ? 171.680 168.256 198.655 1.00 105.05 ? 669  PHE A CD1 1 
ATOM   4498 C CD2 . PHE A 1 669  ? 170.922 166.770 200.356 1.00 102.66 ? 669  PHE A CD2 1 
ATOM   4499 C CE1 . PHE A 1 669  ? 170.372 168.531 198.309 1.00 105.98 ? 669  PHE A CE1 1 
ATOM   4500 C CE2 . PHE A 1 669  ? 169.613 167.043 200.014 1.00 105.87 ? 669  PHE A CE2 1 
ATOM   4501 C CZ  . PHE A 1 669  ? 169.338 167.924 198.990 1.00 104.70 ? 669  PHE A CZ  1 
ATOM   4502 N N   . HIS A 1 670  ? 176.424 166.317 199.672 1.00 30.00  ? 670  HIS A N   1 
ATOM   4503 C CA  . HIS A 1 670  ? 177.765 166.188 200.234 1.00 30.00  ? 670  HIS A CA  1 
ATOM   4504 C C   . HIS A 1 670  ? 178.818 166.842 199.347 1.00 30.00  ? 670  HIS A C   1 
ATOM   4505 O O   . HIS A 1 670  ? 179.793 167.403 199.860 1.00 30.00  ? 670  HIS A O   1 
ATOM   4506 C CB  . HIS A 1 670  ? 178.098 164.718 200.472 1.00 30.00  ? 670  HIS A CB  1 
ATOM   4507 C CG  . HIS A 1 670  ? 177.304 164.097 201.578 1.00 30.00  ? 670  HIS A CG  1 
ATOM   4508 N ND1 . HIS A 1 670  ? 177.311 164.590 202.864 1.00 30.00  ? 670  HIS A ND1 1 
ATOM   4509 C CD2 . HIS A 1 670  ? 176.476 163.027 201.590 1.00 30.00  ? 670  HIS A CD2 1 
ATOM   4510 C CE1 . HIS A 1 670  ? 176.521 163.850 203.622 1.00 30.00  ? 670  HIS A CE1 1 
ATOM   4511 N NE2 . HIS A 1 670  ? 176.003 162.894 202.872 1.00 30.00  ? 670  HIS A NE2 1 
ATOM   4512 N N   . LEU A 1 671  ? 178.645 166.779 198.025 1.00 30.00  ? 671  LEU A N   1 
ATOM   4513 C CA  . LEU A 1 671  ? 179.565 167.462 197.121 1.00 30.00  ? 671  LEU A CA  1 
ATOM   4514 C C   . LEU A 1 671  ? 179.507 168.969 197.329 1.00 30.00  ? 671  LEU A C   1 
ATOM   4515 O O   . LEU A 1 671  ? 180.539 169.650 197.323 1.00 30.00  ? 671  LEU A O   1 
ATOM   4516 C CB  . LEU A 1 671  ? 179.241 167.101 195.671 1.00 30.00  ? 671  LEU A CB  1 
ATOM   4517 N N   . PHE A 1 672  ? 178.300 169.508 197.512 1.00 30.00  ? 672  PHE A N   1 
ATOM   4518 C CA  . PHE A 1 672  ? 178.168 170.922 197.842 1.00 30.00  ? 672  PHE A CA  1 
ATOM   4519 C C   . PHE A 1 672  ? 178.822 171.230 199.182 1.00 30.00  ? 672  PHE A C   1 
ATOM   4520 O O   . PHE A 1 672  ? 179.487 172.262 199.335 1.00 30.00  ? 672  PHE A O   1 
ATOM   4521 C CB  . PHE A 1 672  ? 176.693 171.322 197.857 1.00 30.00  ? 672  PHE A CB  1 
ATOM   4522 N N   . ARG A 1 673  ? 178.642 170.346 200.166 1.00 30.00  ? 673  ARG A N   1 
ATOM   4523 C CA  . ARG A 1 673  ? 179.292 170.525 201.459 1.00 30.00  ? 673  ARG A CA  1 
ATOM   4524 C C   . ARG A 1 673  ? 180.809 170.463 201.324 1.00 30.00  ? 673  ARG A C   1 
ATOM   4525 O O   . ARG A 1 673  ? 181.533 171.260 201.930 1.00 30.00  ? 673  ARG A O   1 
ATOM   4526 C CB  . ARG A 1 673  ? 178.796 169.465 202.444 1.00 30.00  ? 673  ARG A CB  1 
ATOM   4527 N N   . SER A 1 674  ? 181.306 169.521 200.531 1.00 30.00  ? 674  SER A N   1 
ATOM   4528 C CA  . SER A 1 674  ? 182.743 169.371 200.335 1.00 30.00  ? 674  SER A CA  1 
ATOM   4529 C C   . SER A 1 674  ? 183.290 170.480 199.442 1.00 30.00  ? 674  SER A C   1 
ATOM   4530 O O   . SER A 1 674  ? 184.252 171.161 199.800 1.00 30.00  ? 674  SER A O   1 
ATOM   4531 C CB  . SER A 1 674  ? 183.063 168.003 199.731 1.00 30.00  ? 674  SER A CB  1 
ATOM   4532 O OG  . SER A 1 674  ? 182.487 167.868 198.445 1.00 30.00  ? 674  SER A OG  1 
ATOM   4533 N N   . ILE A 1 721  ? 185.225 134.612 189.043 1.00 124.91 ? 721  ILE A N   1 
ATOM   4534 C CA  . ILE A 1 721  ? 183.850 134.128 189.034 1.00 127.24 ? 721  ILE A CA  1 
ATOM   4535 C C   . ILE A 1 721  ? 183.144 134.560 187.753 1.00 126.75 ? 721  ILE A C   1 
ATOM   4536 O O   . ILE A 1 721  ? 183.180 135.731 187.375 1.00 127.31 ? 721  ILE A O   1 
ATOM   4537 C CB  . ILE A 1 721  ? 183.082 134.614 190.280 1.00 127.93 ? 721  ILE A CB  1 
ATOM   4538 C CG1 . ILE A 1 721  ? 181.580 134.366 190.118 1.00 127.71 ? 721  ILE A CG1 1 
ATOM   4539 C CG2 . ILE A 1 721  ? 183.368 136.084 190.552 1.00 125.14 ? 721  ILE A CG2 1 
ATOM   4540 C CD1 . ILE A 1 721  ? 180.752 134.835 191.296 1.00 125.93 ? 721  ILE A CD1 1 
ATOM   4541 N N   . SER A 1 722  ? 182.504 133.605 187.086 1.00 120.33 ? 722  SER A N   1 
ATOM   4542 C CA  . SER A 1 722  ? 181.763 133.855 185.860 1.00 122.12 ? 722  SER A CA  1 
ATOM   4543 C C   . SER A 1 722  ? 180.278 133.957 186.175 1.00 121.45 ? 722  SER A C   1 
ATOM   4544 O O   . SER A 1 722  ? 179.764 133.229 187.030 1.00 122.18 ? 722  SER A O   1 
ATOM   4545 C CB  . SER A 1 722  ? 182.006 132.747 184.832 1.00 120.93 ? 722  SER A CB  1 
ATOM   4546 O OG  . SER A 1 722  ? 183.371 132.689 184.457 1.00 120.97 ? 722  SER A OG  1 
ATOM   4547 N N   . ILE A 1 723  ? 179.594 134.871 185.483 1.00 103.73 ? 723  ILE A N   1 
ATOM   4548 C CA  . ILE A 1 723  ? 178.171 135.078 185.718 1.00 104.68 ? 723  ILE A CA  1 
ATOM   4549 C C   . ILE A 1 723  ? 177.361 133.840 185.360 1.00 103.60 ? 723  ILE A C   1 
ATOM   4550 O O   . ILE A 1 723  ? 176.367 133.534 186.028 1.00 100.83 ? 723  ILE A O   1 
ATOM   4551 C CB  . ILE A 1 723  ? 177.681 136.321 184.943 1.00 103.44 ? 723  ILE A CB  1 
ATOM   4552 C CG1 . ILE A 1 723  ? 176.220 136.614 185.274 1.00 100.85 ? 723  ILE A CG1 1 
ATOM   4553 C CG2 . ILE A 1 723  ? 177.887 136.150 183.443 1.00 101.16 ? 723  ILE A CG2 1 
ATOM   4554 C CD1 . ILE A 1 723  ? 175.976 136.845 186.745 1.00 99.02  ? 723  ILE A CD1 1 
ATOM   4555 N N   . TYR A 1 724  ? 177.767 133.110 184.319 1.00 99.54  ? 724  TYR A N   1 
ATOM   4556 C CA  . TYR A 1 724  ? 177.096 131.862 183.978 1.00 98.36  ? 724  TYR A CA  1 
ATOM   4557 C C   . TYR A 1 724  ? 177.262 130.830 185.084 1.00 101.50 ? 724  TYR A C   1 
ATOM   4558 O O   . TYR A 1 724  ? 176.319 130.098 185.404 1.00 103.34 ? 724  TYR A O   1 
ATOM   4559 C CB  . TYR A 1 724  ? 177.634 131.329 182.652 1.00 96.56  ? 724  TYR A CB  1 
ATOM   4560 C CG  . TYR A 1 724  ? 177.654 132.370 181.558 1.00 96.46  ? 724  TYR A CG  1 
ATOM   4561 C CD1 . TYR A 1 724  ? 176.501 132.685 180.854 1.00 97.08  ? 724  TYR A CD1 1 
ATOM   4562 C CD2 . TYR A 1 724  ? 178.823 133.041 181.233 1.00 98.00  ? 724  TYR A CD2 1 
ATOM   4563 C CE1 . TYR A 1 724  ? 176.511 133.639 179.857 1.00 98.74  ? 724  TYR A CE1 1 
ATOM   4564 C CE2 . TYR A 1 724  ? 178.845 133.996 180.237 1.00 100.86 ? 724  TYR A CE2 1 
ATOM   4565 C CZ  . TYR A 1 724  ? 177.686 134.291 179.551 1.00 101.90 ? 724  TYR A CZ  1 
ATOM   4566 O OH  . TYR A 1 724  ? 177.706 135.241 178.557 1.00 99.22  ? 724  TYR A OH  1 
ATOM   4567 N N   . GLU A 1 725  ? 178.451 130.766 185.685 1.00 114.64 ? 725  GLU A N   1 
ATOM   4568 C CA  . GLU A 1 725  ? 178.639 129.906 186.847 1.00 115.49 ? 725  GLU A CA  1 
ATOM   4569 C C   . GLU A 1 725  ? 177.713 130.318 187.980 1.00 114.48 ? 725  GLU A C   1 
ATOM   4570 O O   . GLU A 1 725  ? 177.140 129.464 188.665 1.00 112.47 ? 725  GLU A O   1 
ATOM   4571 C CB  . GLU A 1 725  ? 180.095 129.948 187.307 1.00 116.29 ? 725  GLU A CB  1 
ATOM   4572 C CG  . GLU A 1 725  ? 181.083 129.353 186.322 1.00 116.91 ? 725  GLU A CG  1 
ATOM   4573 C CD  . GLU A 1 725  ? 182.503 129.357 186.854 1.00 118.11 ? 725  GLU A CD  1 
ATOM   4574 O OE1 . GLU A 1 725  ? 182.738 129.967 187.919 1.00 116.11 ? 725  GLU A OE1 1 
ATOM   4575 O OE2 . GLU A 1 725  ? 183.383 128.749 186.210 1.00 118.50 ? 725  GLU A OE2 1 
ATOM   4576 N N   . TRP A 1 726  ? 177.549 131.627 188.190 1.00 104.76 ? 726  TRP A N   1 
ATOM   4577 C CA  . TRP A 1 726  ? 176.682 132.097 189.264 1.00 104.15 ? 726  TRP A CA  1 
ATOM   4578 C C   . TRP A 1 726  ? 175.230 131.706 189.024 1.00 105.50 ? 726  TRP A C   1 
ATOM   4579 O O   . TRP A 1 726  ? 174.542 131.260 189.948 1.00 107.26 ? 726  TRP A O   1 
ATOM   4580 C CB  . TRP A 1 726  ? 176.802 133.611 189.419 1.00 102.94 ? 726  TRP A CB  1 
ATOM   4581 C CG  . TRP A 1 726  ? 175.836 134.168 190.415 1.00 103.99 ? 726  TRP A CG  1 
ATOM   4582 C CD1 . TRP A 1 726  ? 175.979 134.189 191.770 1.00 103.26 ? 726  TRP A CD1 1 
ATOM   4583 C CD2 . TRP A 1 726  ? 174.570 134.777 190.136 1.00 105.00 ? 726  TRP A CD2 1 
ATOM   4584 N NE1 . TRP A 1 726  ? 174.884 134.776 192.353 1.00 105.75 ? 726  TRP A NE1 1 
ATOM   4585 C CE2 . TRP A 1 726  ? 174.004 135.146 191.371 1.00 106.01 ? 726  TRP A CE2 1 
ATOM   4586 C CE3 . TRP A 1 726  ? 173.862 135.047 188.962 1.00 103.37 ? 726  TRP A CE3 1 
ATOM   4587 C CZ2 . TRP A 1 726  ? 172.764 135.771 191.466 1.00 103.34 ? 726  TRP A CZ2 1 
ATOM   4588 C CZ3 . TRP A 1 726  ? 172.631 135.668 189.059 1.00 104.09 ? 726  TRP A CZ3 1 
ATOM   4589 C CH2 . TRP A 1 726  ? 172.094 136.023 190.301 1.00 104.08 ? 726  TRP A CH2 1 
ATOM   4590 N N   . ILE A 1 727  ? 174.741 131.869 187.793 1.00 101.10 ? 727  ILE A N   1 
ATOM   4591 C CA  . ILE A 1 727  ? 173.346 131.530 187.525 1.00 98.41  ? 727  ILE A CA  1 
ATOM   4592 C C   . ILE A 1 727  ? 173.139 130.020 187.593 1.00 98.30  ? 727  ILE A C   1 
ATOM   4593 O O   . ILE A 1 727  ? 172.097 129.543 188.062 1.00 101.03 ? 727  ILE A O   1 
ATOM   4594 C CB  . ILE A 1 727  ? 172.882 132.125 186.181 1.00 97.33  ? 727  ILE A CB  1 
ATOM   4595 C CG1 . ILE A 1 727  ? 171.371 131.969 186.027 1.00 97.51  ? 727  ILE A CG1 1 
ATOM   4596 C CG2 . ILE A 1 727  ? 173.590 131.481 185.009 1.00 98.74  ? 727  ILE A CG2 1 
ATOM   4597 C CD1 . ILE A 1 727  ? 170.577 132.697 187.082 1.00 98.21  ? 727  ILE A CD1 1 
ATOM   4598 N N   . HIS A 1 728  ? 174.130 129.240 187.148 1.00 100.87 ? 728  HIS A N   1 
ATOM   4599 C CA  . HIS A 1 728  ? 174.027 127.791 187.275 1.00 101.83 ? 728  HIS A CA  1 
ATOM   4600 C C   . HIS A 1 728  ? 173.997 127.370 188.738 1.00 106.58 ? 728  HIS A C   1 
ATOM   4601 O O   . HIS A 1 728  ? 173.228 126.482 189.120 1.00 106.48 ? 728  HIS A O   1 
ATOM   4602 C CB  . HIS A 1 728  ? 175.185 127.114 186.546 1.00 102.87 ? 728  HIS A CB  1 
ATOM   4603 C CG  . HIS A 1 728  ? 175.141 125.620 186.606 1.00 104.83 ? 728  HIS A CG  1 
ATOM   4604 N ND1 . HIS A 1 728  ? 174.041 124.893 186.209 1.00 103.40 ? 728  HIS A ND1 1 
ATOM   4605 C CD2 . HIS A 1 728  ? 176.061 124.717 187.020 1.00 105.39 ? 728  HIS A CD2 1 
ATOM   4606 C CE1 . HIS A 1 728  ? 174.285 123.605 186.374 1.00 104.66 ? 728  HIS A CE1 1 
ATOM   4607 N NE2 . HIS A 1 728  ? 175.504 123.471 186.865 1.00 106.25 ? 728  HIS A NE2 1 
ATOM   4608 N N   . ASN A 1 729  ? 174.828 128.000 189.573 1.00 113.48 ? 729  ASN A N   1 
ATOM   4609 C CA  . ASN A 1 729  ? 174.810 127.703 191.000 1.00 112.58 ? 729  ASN A CA  1 
ATOM   4610 C C   . ASN A 1 729  ? 173.482 128.100 191.627 1.00 111.51 ? 729  ASN A C   1 
ATOM   4611 O O   . ASN A 1 729  ? 172.967 127.395 192.500 1.00 113.99 ? 729  ASN A O   1 
ATOM   4612 C CB  . ASN A 1 729  ? 175.967 128.412 191.702 1.00 111.17 ? 729  ASN A CB  1 
ATOM   4613 C CG  . ASN A 1 729  ? 177.318 127.880 191.277 1.00 113.05 ? 729  ASN A CG  1 
ATOM   4614 O OD1 . ASN A 1 729  ? 177.464 126.697 190.974 1.00 111.73 ? 729  ASN A OD1 1 
ATOM   4615 N ND2 . ASN A 1 729  ? 178.317 128.755 191.249 1.00 113.24 ? 729  ASN A ND2 1 
ATOM   4616 N N   . LEU A 1 730  ? 172.918 129.231 191.202 1.00 109.19 ? 730  LEU A N   1 
ATOM   4617 C CA  . LEU A 1 730  ? 171.613 129.644 191.708 1.00 109.11 ? 730  LEU A CA  1 
ATOM   4618 C C   . LEU A 1 730  ? 170.544 128.617 191.361 1.00 110.85 ? 730  LEU A C   1 
ATOM   4619 O O   . LEU A 1 730  ? 169.719 128.249 192.206 1.00 112.56 ? 730  LEU A O   1 
ATOM   4620 C CB  . LEU A 1 730  ? 171.243 131.017 191.147 1.00 108.53 ? 730  LEU A CB  1 
ATOM   4621 C CG  . LEU A 1 730  ? 169.780 131.441 191.301 1.00 110.32 ? 730  LEU A CG  1 
ATOM   4622 C CD1 . LEU A 1 730  ? 169.385 131.537 192.765 1.00 111.30 ? 730  LEU A CD1 1 
ATOM   4623 C CD2 . LEU A 1 730  ? 169.525 132.759 190.592 1.00 109.81 ? 730  LEU A CD2 1 
ATOM   4624 N N   . TYR A 1 731  ? 170.551 128.130 190.121 1.00 106.96 ? 731  TYR A N   1 
ATOM   4625 C CA  . TYR A 1 731  ? 169.543 127.152 189.727 1.00 107.44 ? 731  TYR A CA  1 
ATOM   4626 C C   . TYR A 1 731  ? 169.761 125.805 190.406 1.00 107.74 ? 731  TYR A C   1 
ATOM   4627 O O   . TYR A 1 731  ? 168.789 125.102 190.704 1.00 108.77 ? 731  TYR A O   1 
ATOM   4628 C CB  . TYR A 1 731  ? 169.519 127.006 188.208 1.00 107.63 ? 731  TYR A CB  1 
ATOM   4629 C CG  . TYR A 1 731  ? 168.598 128.004 187.544 1.00 107.92 ? 731  TYR A CG  1 
ATOM   4630 C CD1 . TYR A 1 731  ? 167.299 128.181 187.998 1.00 107.81 ? 731  TYR A CD1 1 
ATOM   4631 C CD2 . TYR A 1 731  ? 169.032 128.785 186.483 1.00 108.28 ? 731  TYR A CD2 1 
ATOM   4632 C CE1 . TYR A 1 731  ? 166.453 129.094 187.406 1.00 106.24 ? 731  TYR A CE1 1 
ATOM   4633 C CE2 . TYR A 1 731  ? 168.191 129.703 185.884 1.00 108.66 ? 731  TYR A CE2 1 
ATOM   4634 C CZ  . TYR A 1 731  ? 166.903 129.852 186.350 1.00 107.67 ? 731  TYR A CZ  1 
ATOM   4635 O OH  . TYR A 1 731  ? 166.059 130.763 185.760 1.00 109.05 ? 731  TYR A OH  1 
ATOM   4636 N N   . LEU A 1 732  ? 171.016 125.426 190.657 1.00 116.16 ? 732  LEU A N   1 
ATOM   4637 C CA  . LEU A 1 732  ? 171.276 124.214 191.428 1.00 118.61 ? 732  LEU A CA  1 
ATOM   4638 C C   . LEU A 1 732  ? 170.792 124.361 192.866 1.00 120.80 ? 732  LEU A C   1 
ATOM   4639 O O   . LEU A 1 732  ? 170.210 123.428 193.431 1.00 121.88 ? 732  LEU A O   1 
ATOM   4640 C CB  . LEU A 1 732  ? 172.766 123.876 191.396 1.00 116.64 ? 732  LEU A CB  1 
ATOM   4641 C CG  . LEU A 1 732  ? 173.331 123.406 190.055 1.00 115.78 ? 732  LEU A CG  1 
ATOM   4642 C CD1 . LEU A 1 732  ? 174.802 123.053 190.190 1.00 115.30 ? 732  LEU A CD1 1 
ATOM   4643 C CD2 . LEU A 1 732  ? 172.538 122.224 189.523 1.00 116.40 ? 732  LEU A CD2 1 
ATOM   4644 N N   . PHE A 1 733  ? 171.028 125.526 193.474 1.00 125.63 ? 733  PHE A N   1 
ATOM   4645 C CA  . PHE A 1 733  ? 170.557 125.778 194.830 1.00 124.45 ? 733  PHE A CA  1 
ATOM   4646 C C   . PHE A 1 733  ? 169.037 125.811 194.894 1.00 126.75 ? 733  PHE A C   1 
ATOM   4647 O O   . PHE A 1 733  ? 168.450 125.476 195.929 1.00 128.76 ? 733  PHE A O   1 
ATOM   4648 C CB  . PHE A 1 733  ? 171.148 127.091 195.343 1.00 123.95 ? 733  PHE A CB  1 
ATOM   4649 C CG  . PHE A 1 733  ? 170.653 127.494 196.701 1.00 127.05 ? 733  PHE A CG  1 
ATOM   4650 C CD1 . PHE A 1 733  ? 171.183 126.920 197.844 1.00 127.30 ? 733  PHE A CD1 1 
ATOM   4651 C CD2 . PHE A 1 733  ? 169.668 128.457 196.836 1.00 126.00 ? 733  PHE A CD2 1 
ATOM   4652 C CE1 . PHE A 1 733  ? 170.732 127.291 199.095 1.00 127.10 ? 733  PHE A CE1 1 
ATOM   4653 C CE2 . PHE A 1 733  ? 169.213 128.833 198.084 1.00 126.69 ? 733  PHE A CE2 1 
ATOM   4654 C CZ  . PHE A 1 733  ? 169.746 128.250 199.215 1.00 127.28 ? 733  PHE A CZ  1 
ATOM   4655 N N   . GLU A 1 734  ? 168.386 126.218 193.802 1.00 126.65 ? 734  GLU A N   1 
ATOM   4656 C CA  . GLU A 1 734  ? 166.929 126.207 193.753 1.00 128.15 ? 734  GLU A CA  1 
ATOM   4657 C C   . GLU A 1 734  ? 166.359 124.799 193.876 1.00 127.79 ? 734  GLU A C   1 
ATOM   4658 O O   . GLU A 1 734  ? 165.203 124.643 194.285 1.00 126.62 ? 734  GLU A O   1 
ATOM   4659 C CB  . GLU A 1 734  ? 166.449 126.862 192.455 1.00 128.00 ? 734  GLU A CB  1 
ATOM   4660 C CG  . GLU A 1 734  ? 164.942 127.038 192.350 1.00 127.68 ? 734  GLU A CG  1 
ATOM   4661 C CD  . GLU A 1 734  ? 164.529 127.773 191.092 1.00 128.23 ? 734  GLU A CD  1 
ATOM   4662 O OE1 . GLU A 1 734  ? 165.385 128.457 190.493 1.00 129.14 ? 734  GLU A OE1 1 
ATOM   4663 O OE2 . GLU A 1 734  ? 163.348 127.665 190.699 1.00 128.08 ? 734  GLU A OE2 1 
ATOM   4664 N N   . GLU A 1 735  ? 167.144 123.770 193.547 1.00 132.21 ? 735  GLU A N   1 
ATOM   4665 C CA  . GLU A 1 735  ? 166.668 122.397 193.673 1.00 132.50 ? 735  GLU A CA  1 
ATOM   4666 C C   . GLU A 1 735  ? 166.408 122.000 195.120 1.00 133.56 ? 735  GLU A C   1 
ATOM   4667 O O   . GLU A 1 735  ? 165.735 120.992 195.360 1.00 134.25 ? 735  GLU A O   1 
ATOM   4668 C CB  . GLU A 1 735  ? 167.671 121.428 193.046 1.00 133.18 ? 735  GLU A CB  1 
ATOM   4669 C CG  . GLU A 1 735  ? 167.851 121.594 191.547 1.00 133.54 ? 735  GLU A CG  1 
ATOM   4670 C CD  . GLU A 1 735  ? 168.788 120.559 190.957 1.00 133.63 ? 735  GLU A CD  1 
ATOM   4671 O OE1 . GLU A 1 735  ? 169.396 119.794 191.734 1.00 133.75 ? 735  GLU A OE1 1 
ATOM   4672 O OE2 . GLU A 1 735  ? 168.914 120.508 189.715 1.00 132.65 ? 735  GLU A OE2 1 
ATOM   4673 N N   . SER A 1 736  ? 166.925 122.758 196.082 1.00 134.97 ? 736  SER A N   1 
ATOM   4674 C CA  . SER A 1 736  ? 166.708 122.462 197.493 1.00 135.30 ? 736  SER A CA  1 
ATOM   4675 C C   . SER A 1 736  ? 165.244 122.652 197.875 1.00 134.11 ? 736  SER A C   1 
ATOM   4676 O O   . SER A 1 736  ? 164.682 121.858 198.628 1.00 134.19 ? 736  SER A O   1 
ATOM   4677 C CB  . SER A 1 736  ? 167.597 123.347 198.368 1.00 134.82 ? 736  SER A CB  1 
ATOM   4678 O OG  . SER A 1 736  ? 167.309 124.718 198.162 1.00 134.30 ? 736  SER A OG  1 
ATOM   4679 N N   . TYR A 1 1047 ? 173.088 134.317 200.050 1.00 118.60 ? 1047 TYR A N   1 
ATOM   4680 C CA  . TYR A 1 1047 ? 173.945 135.490 200.169 1.00 120.38 ? 1047 TYR A CA  1 
ATOM   4681 C C   . TYR A 1 1047 ? 174.412 135.967 198.799 1.00 120.21 ? 1047 TYR A C   1 
ATOM   4682 O O   . TYR A 1 1047 ? 174.410 137.164 198.512 1.00 118.58 ? 1047 TYR A O   1 
ATOM   4683 C CB  . TYR A 1 1047 ? 175.152 135.186 201.059 1.00 119.17 ? 1047 TYR A CB  1 
ATOM   4684 N N   . ILE A 1 1048 ? 174.817 135.020 197.955 1.00 112.21 ? 1048 ILE A N   1 
ATOM   4685 C CA  . ILE A 1 1048 ? 175.286 135.330 196.610 1.00 112.35 ? 1048 ILE A CA  1 
ATOM   4686 C C   . ILE A 1 1048 ? 174.162 135.064 195.620 1.00 112.19 ? 1048 ILE A C   1 
ATOM   4687 O O   . ILE A 1 1048 ? 174.063 135.721 194.578 1.00 113.24 ? 1048 ILE A O   1 
ATOM   4688 C CB  . ILE A 1 1048 ? 176.541 134.510 196.256 1.00 113.32 ? 1048 ILE A CB  1 
ATOM   4689 C CG1 . ILE A 1 1048 ? 177.580 134.618 197.371 1.00 114.19 ? 1048 ILE A CG1 1 
ATOM   4690 C CG2 . ILE A 1 1048 ? 177.138 134.982 194.944 1.00 109.14 ? 1048 ILE A CG2 1 
ATOM   4691 C CD1 . ILE A 1 1048 ? 178.843 133.828 197.104 1.00 110.38 ? 1048 ILE A CD1 1 
ATOM   4692 N N   . TYR A 1 1049 ? 173.303 134.098 195.944 1.00 112.09 ? 1049 TYR A N   1 
ATOM   4693 C CA  . TYR A 1 1049 ? 172.260 133.681 195.015 1.00 111.76 ? 1049 TYR A CA  1 
ATOM   4694 C C   . TYR A 1 1049 ? 171.105 134.675 194.970 1.00 110.02 ? 1049 TYR A C   1 
ATOM   4695 O O   . TYR A 1 1049 ? 170.477 134.850 193.921 1.00 109.00 ? 1049 TYR A O   1 
ATOM   4696 C CB  . TYR A 1 1049 ? 171.756 132.289 195.396 1.00 110.23 ? 1049 TYR A CB  1 
ATOM   4697 C CG  . TYR A 1 1049 ? 172.859 131.262 195.512 1.00 111.83 ? 1049 TYR A CG  1 
ATOM   4698 C CD1 . TYR A 1 1049 ? 173.930 131.262 194.629 1.00 112.23 ? 1049 TYR A CD1 1 
ATOM   4699 C CD2 . TYR A 1 1049 ? 172.836 130.301 196.514 1.00 112.08 ? 1049 TYR A CD2 1 
ATOM   4700 C CE1 . TYR A 1 1049 ? 174.943 130.329 194.734 1.00 112.09 ? 1049 TYR A CE1 1 
ATOM   4701 C CE2 . TYR A 1 1049 ? 173.845 129.364 196.627 1.00 112.88 ? 1049 TYR A CE2 1 
ATOM   4702 C CZ  . TYR A 1 1049 ? 174.896 129.383 195.734 1.00 113.04 ? 1049 TYR A CZ  1 
ATOM   4703 O OH  . TYR A 1 1049 ? 175.902 128.452 195.843 1.00 112.00 ? 1049 TYR A OH  1 
ATOM   4704 N N   . GLU A 1 1050 ? 170.809 135.331 196.088 1.00 87.47  ? 1050 GLU A N   1 
ATOM   4705 C CA  . GLU A 1 1050 ? 169.656 136.216 196.179 1.00 87.26  ? 1050 GLU A CA  1 
ATOM   4706 C C   . GLU A 1 1050 ? 170.069 137.663 195.937 1.00 86.42  ? 1050 GLU A C   1 
ATOM   4707 O O   . GLU A 1 1050 ? 171.012 138.159 196.562 1.00 82.35  ? 1050 GLU A O   1 
ATOM   4708 C CB  . GLU A 1 1050 ? 168.985 136.081 197.545 1.00 90.12  ? 1050 GLU A CB  1 
ATOM   4709 C CG  . GLU A 1 1050 ? 167.805 137.013 197.753 1.00 90.68  ? 1050 GLU A CG  1 
ATOM   4710 C CD  . GLU A 1 1050 ? 166.633 136.691 196.846 1.00 93.41  ? 1050 GLU A CD  1 
ATOM   4711 O OE1 . GLU A 1 1050 ? 166.554 135.548 196.351 1.00 94.25  ? 1050 GLU A OE1 1 
ATOM   4712 O OE2 . GLU A 1 1050 ? 165.788 137.584 196.629 1.00 92.28  ? 1050 GLU A OE2 1 
ATOM   4713 N N   . GLU A 1 1051 ? 169.358 138.333 195.034 1.00 73.06  ? 1051 GLU A N   1 
ATOM   4714 C CA  . GLU A 1 1051 ? 169.637 139.729 194.746 1.00 67.84  ? 1051 GLU A CA  1 
ATOM   4715 C C   . GLU A 1 1051 ? 169.203 140.615 195.913 1.00 72.64  ? 1051 GLU A C   1 
ATOM   4716 O O   . GLU A 1 1051 ? 168.246 140.297 196.621 1.00 75.20  ? 1051 GLU A O   1 
ATOM   4717 C CB  . GLU A 1 1051 ? 168.920 140.170 193.475 1.00 65.10  ? 1051 GLU A CB  1 
ATOM   4718 C CG  . GLU A 1 1051 ? 169.394 139.476 192.216 1.00 70.03  ? 1051 GLU A CG  1 
ATOM   4719 C CD  . GLU A 1 1051 ? 168.875 140.142 190.960 1.00 73.62  ? 1051 GLU A CD  1 
ATOM   4720 O OE1 . GLU A 1 1051 ? 168.278 141.232 191.070 1.00 73.97  ? 1051 GLU A OE1 1 
ATOM   4721 O OE2 . GLU A 1 1051 ? 169.062 139.577 189.862 1.00 75.61  ? 1051 GLU A OE2 1 
ATOM   4722 N N   . PRO A 1 1052 ? 169.890 141.732 196.131 1.00 67.01  ? 1052 PRO A N   1 
ATOM   4723 C CA  . PRO A 1 1052 ? 169.482 142.650 197.196 1.00 60.47  ? 1052 PRO A CA  1 
ATOM   4724 C C   . PRO A 1 1052 ? 168.216 143.403 196.823 1.00 67.89  ? 1052 PRO A C   1 
ATOM   4725 O O   . PRO A 1 1052 ? 167.807 143.458 195.663 1.00 72.13  ? 1052 PRO A O   1 
ATOM   4726 C CB  . PRO A 1 1052 ? 170.675 143.599 197.320 1.00 63.64  ? 1052 PRO A CB  1 
ATOM   4727 C CG  . PRO A 1 1052 ? 171.277 143.596 195.965 1.00 60.81  ? 1052 PRO A CG  1 
ATOM   4728 C CD  . PRO A 1 1052 ? 171.100 142.201 195.438 1.00 65.89  ? 1052 PRO A CD  1 
ATOM   4729 N N   . LYS A 1 1053 ? 167.590 143.985 197.842 1.00 69.19  ? 1053 LYS A N   1 
ATOM   4730 C CA  . LYS A 1 1053 ? 166.379 144.766 197.628 1.00 66.28  ? 1053 LYS A CA  1 
ATOM   4731 C C   . LYS A 1 1053 ? 166.675 145.986 196.767 1.00 60.57  ? 1053 LYS A C   1 
ATOM   4732 O O   . LYS A 1 1053 ? 167.677 146.676 196.968 1.00 59.67  ? 1053 LYS A O   1 
ATOM   4733 C CB  . LYS A 1 1053 ? 165.786 145.199 198.968 1.00 66.98  ? 1053 LYS A CB  1 
ATOM   4734 C CG  . LYS A 1 1053 ? 164.648 146.200 198.851 1.00 63.70  ? 1053 LYS A CG  1 
ATOM   4735 C CD  . LYS A 1 1053 ? 164.110 146.589 200.217 1.00 65.75  ? 1053 LYS A CD  1 
ATOM   4736 C CE  . LYS A 1 1053 ? 163.110 147.726 200.110 1.00 64.48  ? 1053 LYS A CE  1 
ATOM   4737 N NZ  . LYS A 1 1053 ? 161.988 147.394 199.194 1.00 61.89  ? 1053 LYS A NZ  1 
ATOM   4738 N N   . GLY A 1 1054 ? 165.799 146.248 195.803 1.00 52.99  ? 1054 GLY A N   1 
ATOM   4739 C CA  . GLY A 1 1054 ? 165.930 147.428 194.976 1.00 57.03  ? 1054 GLY A CA  1 
ATOM   4740 C C   . GLY A 1 1054 ? 166.991 147.355 193.906 1.00 60.48  ? 1054 GLY A C   1 
ATOM   4741 O O   . GLY A 1 1054 ? 167.445 148.400 193.434 1.00 65.20  ? 1054 GLY A O   1 
ATOM   4742 N N   . ASN A 1 1055 ? 167.402 146.157 193.505 1.00 50.65  ? 1055 ASN A N   1 
ATOM   4743 C CA  . ASN A 1 1055 ? 168.397 146.027 192.455 1.00 43.52  ? 1055 ASN A CA  1 
ATOM   4744 C C   . ASN A 1 1055 ? 167.824 146.520 191.127 1.00 50.99  ? 1055 ASN A C   1 
ATOM   4745 O O   . ASN A 1 1055 ? 166.618 146.718 190.974 1.00 58.63  ? 1055 ASN A O   1 
ATOM   4746 C CB  . ASN A 1 1055 ? 168.863 144.579 192.339 1.00 47.58  ? 1055 ASN A CB  1 
ATOM   4747 C CG  . ASN A 1 1055 ? 170.248 144.464 191.755 1.00 52.40  ? 1055 ASN A CG  1 
ATOM   4748 O OD1 . ASN A 1 1055 ? 171.027 145.413 191.791 1.00 57.81  ? 1055 ASN A OD1 1 
ATOM   4749 N ND2 . ASN A 1 1055 ? 170.566 143.296 191.214 1.00 54.70  ? 1055 ASN A ND2 1 
ATOM   4750 N N   . ILE A 1 1056 ? 168.716 146.716 190.154 1.00 48.66  ? 1056 ILE A N   1 
ATOM   4751 C CA  . ILE A 1 1056 ? 168.332 147.380 188.909 1.00 50.27  ? 1056 ILE A CA  1 
ATOM   4752 C C   . ILE A 1 1056 ? 167.287 146.565 188.157 1.00 56.95  ? 1056 ILE A C   1 
ATOM   4753 O O   . ILE A 1 1056 ? 166.268 147.098 187.705 1.00 64.03  ? 1056 ILE A O   1 
ATOM   4754 C CB  . ILE A 1 1056 ? 169.573 147.642 188.039 1.00 54.75  ? 1056 ILE A CB  1 
ATOM   4755 C CG1 . ILE A 1 1056 ? 170.417 148.756 188.650 1.00 51.75  ? 1056 ILE A CG1 1 
ATOM   4756 C CG2 . ILE A 1 1056 ? 169.163 148.014 186.630 1.00 53.95  ? 1056 ILE A CG2 1 
ATOM   4757 C CD1 . ILE A 1 1056 ? 169.686 150.067 188.745 1.00 53.92  ? 1056 ILE A CD1 1 
ATOM   4758 N N   . GLY A 1 1057 ? 167.518 145.266 188.014 1.00 50.88  ? 1057 GLY A N   1 
ATOM   4759 C CA  . GLY A 1 1057 ? 166.602 144.442 187.250 1.00 55.17  ? 1057 GLY A CA  1 
ATOM   4760 C C   . GLY A 1 1057 ? 166.009 143.300 188.044 1.00 54.09  ? 1057 GLY A C   1 
ATOM   4761 O O   . GLY A 1 1057 ? 165.742 142.228 187.495 1.00 58.44  ? 1057 GLY A O   1 
ATOM   4762 N N   . LYS A 1 1058 ? 165.796 143.518 189.342 1.00 52.78  ? 1058 LYS A N   1 
ATOM   4763 C CA  . LYS A 1 1058 ? 165.310 142.445 190.201 1.00 48.27  ? 1058 LYS A CA  1 
ATOM   4764 C C   . LYS A 1 1058 ? 163.881 142.054 189.846 1.00 60.40  ? 1058 LYS A C   1 
ATOM   4765 O O   . LYS A 1 1058 ? 163.573 140.869 189.677 1.00 66.57  ? 1058 LYS A O   1 
ATOM   4766 C CB  . LYS A 1 1058 ? 165.402 142.867 191.666 1.00 50.77  ? 1058 LYS A CB  1 
ATOM   4767 C CG  . LYS A 1 1058 ? 165.003 141.785 192.649 1.00 52.53  ? 1058 LYS A CG  1 
ATOM   4768 C CD  . LYS A 1 1058 ? 165.019 142.304 194.073 1.00 54.43  ? 1058 LYS A CD  1 
ATOM   4769 C CE  . LYS A 1 1058 ? 164.777 141.182 195.063 1.00 60.84  ? 1058 LYS A CE  1 
ATOM   4770 N NZ  . LYS A 1 1058 ? 163.522 140.445 194.757 1.00 63.12  ? 1058 LYS A NZ  1 
ATOM   4771 N N   . TYR A 1 1059 ? 162.991 143.041 189.724 1.00 55.06  ? 1059 TYR A N   1 
ATOM   4772 C CA  . TYR A 1 1059 ? 161.577 142.733 189.534 1.00 44.62  ? 1059 TYR A CA  1 
ATOM   4773 C C   . TYR A 1 1059 ? 161.312 142.129 188.162 1.00 51.71  ? 1059 TYR A C   1 
ATOM   4774 O O   . TYR A 1 1059 ? 160.525 141.185 188.037 1.00 60.52  ? 1059 TYR A O   1 
ATOM   4775 C CB  . TYR A 1 1059 ? 160.734 143.988 189.736 1.00 46.97  ? 1059 TYR A CB  1 
ATOM   4776 C CG  . TYR A 1 1059 ? 159.251 143.737 189.616 1.00 57.60  ? 1059 TYR A CG  1 
ATOM   4777 C CD1 . TYR A 1 1059 ? 158.561 143.062 190.611 1.00 54.50  ? 1059 TYR A CD1 1 
ATOM   4778 C CD2 . TYR A 1 1059 ? 158.541 144.177 188.511 1.00 56.40  ? 1059 TYR A CD2 1 
ATOM   4779 C CE1 . TYR A 1 1059 ? 157.207 142.828 190.506 1.00 51.87  ? 1059 TYR A CE1 1 
ATOM   4780 C CE2 . TYR A 1 1059 ? 157.186 143.951 188.398 1.00 51.00  ? 1059 TYR A CE2 1 
ATOM   4781 C CZ  . TYR A 1 1059 ? 156.524 143.275 189.398 1.00 54.58  ? 1059 TYR A CZ  1 
ATOM   4782 O OH  . TYR A 1 1059 ? 155.173 143.046 189.290 1.00 61.72  ? 1059 TYR A OH  1 
ATOM   4783 N N   . PHE A 1 1060 ? 161.945 142.666 187.120 1.00 51.36  ? 1060 PHE A N   1 
ATOM   4784 C CA  . PHE A 1 1060 ? 161.728 142.128 185.782 1.00 46.03  ? 1060 PHE A CA  1 
ATOM   4785 C C   . PHE A 1 1060 ? 162.247 140.701 185.670 1.00 47.04  ? 1060 PHE A C   1 
ATOM   4786 O O   . PHE A 1 1060 ? 161.584 139.835 185.087 1.00 58.91  ? 1060 PHE A O   1 
ATOM   4787 C CB  . PHE A 1 1060 ? 162.391 143.024 184.741 1.00 50.97  ? 1060 PHE A CB  1 
ATOM   4788 C CG  . PHE A 1 1060 ? 162.087 142.630 183.330 1.00 51.15  ? 1060 PHE A CG  1 
ATOM   4789 C CD1 . PHE A 1 1060 ? 160.904 143.019 182.731 1.00 52.09  ? 1060 PHE A CD1 1 
ATOM   4790 C CD2 . PHE A 1 1060 ? 162.982 141.869 182.602 1.00 54.75  ? 1060 PHE A CD2 1 
ATOM   4791 C CE1 . PHE A 1 1060 ? 160.621 142.657 181.436 1.00 52.47  ? 1060 PHE A CE1 1 
ATOM   4792 C CE2 . PHE A 1 1060 ? 162.703 141.504 181.306 1.00 56.94  ? 1060 PHE A CE2 1 
ATOM   4793 C CZ  . PHE A 1 1060 ? 161.521 141.899 180.723 1.00 56.51  ? 1060 PHE A CZ  1 
ATOM   4794 N N   . ARG A 1 1061 ? 163.431 140.436 186.222 1.00 49.77  ? 1061 ARG A N   1 
ATOM   4795 C CA  . ARG A 1 1061 ? 163.952 139.075 186.211 1.00 43.08  ? 1061 ARG A CA  1 
ATOM   4796 C C   . ARG A 1 1061 ? 163.075 138.149 187.039 1.00 50.42  ? 1061 ARG A C   1 
ATOM   4797 O O   . ARG A 1 1061 ? 162.899 136.976 186.692 1.00 65.88  ? 1061 ARG A O   1 
ATOM   4798 C CB  . ARG A 1 1061 ? 165.393 139.054 186.717 1.00 46.75  ? 1061 ARG A CB  1 
ATOM   4799 C CG  . ARG A 1 1061 ? 166.403 139.572 185.710 1.00 53.19  ? 1061 ARG A CG  1 
ATOM   4800 C CD  . ARG A 1 1061 ? 167.827 139.342 186.180 1.00 50.76  ? 1061 ARG A CD  1 
ATOM   4801 N NE  . ARG A 1 1061 ? 168.162 140.162 187.336 1.00 58.00  ? 1061 ARG A NE  1 
ATOM   4802 C CZ  . ARG A 1 1061 ? 168.712 141.366 187.263 1.00 58.40  ? 1061 ARG A CZ  1 
ATOM   4803 N NH1 . ARG A 1 1061 ? 169.001 141.924 186.100 1.00 52.72  ? 1061 ARG A NH1 1 
ATOM   4804 N NH2 . ARG A 1 1061 ? 168.976 142.027 188.386 1.00 53.53  ? 1061 ARG A NH2 1 
ATOM   4805 N N   . SER A 1 1062 ? 162.511 138.657 188.137 1.00 53.59  ? 1062 SER A N   1 
ATOM   4806 C CA  . SER A 1 1062 ? 161.584 137.854 188.925 1.00 56.57  ? 1062 SER A CA  1 
ATOM   4807 C C   . SER A 1 1062 ? 160.348 137.490 188.116 1.00 61.24  ? 1062 SER A C   1 
ATOM   4808 O O   . SER A 1 1062 ? 159.880 136.347 188.163 1.00 65.78  ? 1062 SER A O   1 
ATOM   4809 C CB  . SER A 1 1062 ? 161.189 138.603 190.195 1.00 59.76  ? 1062 SER A CB  1 
ATOM   4810 O OG  . SER A 1 1062 ? 160.209 137.886 190.921 1.00 57.14  ? 1062 SER A OG  1 
ATOM   4811 N N   . LEU A 1 1063 ? 159.803 138.451 187.368 1.00 57.42  ? 1063 LEU A N   1 
ATOM   4812 C CA  . LEU A 1 1063 ? 158.656 138.159 186.513 1.00 49.30  ? 1063 LEU A CA  1 
ATOM   4813 C C   . LEU A 1 1063 ? 159.012 137.137 185.445 1.00 52.63  ? 1063 LEU A C   1 
ATOM   4814 O O   . LEU A 1 1063 ? 158.233 136.218 185.170 1.00 64.20  ? 1063 LEU A O   1 
ATOM   4815 C CB  . LEU A 1 1063 ? 158.139 139.438 185.860 1.00 45.66  ? 1063 LEU A CB  1 
ATOM   4816 C CG  . LEU A 1 1063 ? 157.404 140.432 186.751 1.00 55.74  ? 1063 LEU A CG  1 
ATOM   4817 C CD1 . LEU A 1 1063 ? 156.815 141.541 185.903 1.00 53.46  ? 1063 LEU A CD1 1 
ATOM   4818 C CD2 . LEU A 1 1063 ? 156.325 139.729 187.549 1.00 56.15  ? 1063 LEU A CD2 1 
ATOM   4819 N N   . VAL A 1 1064 ? 160.183 137.285 184.827 1.00 50.71  ? 1064 VAL A N   1 
ATOM   4820 C CA  . VAL A 1 1064 ? 160.581 136.367 183.764 1.00 44.77  ? 1064 VAL A CA  1 
ATOM   4821 C C   . VAL A 1 1064 ? 160.756 134.957 184.310 1.00 44.35  ? 1064 VAL A C   1 
ATOM   4822 O O   . VAL A 1 1064 ? 160.311 133.979 183.699 1.00 55.34  ? 1064 VAL A O   1 
ATOM   4823 C CB  . VAL A 1 1064 ? 161.860 136.871 183.073 1.00 41.84  ? 1064 VAL A CB  1 
ATOM   4824 C CG1 . VAL A 1 1064 ? 162.410 135.813 182.143 1.00 47.88  ? 1064 VAL A CG1 1 
ATOM   4825 C CG2 . VAL A 1 1064 ? 161.570 138.143 182.304 1.00 44.80  ? 1064 VAL A CG2 1 
ATOM   4826 N N   . LYS A 1 1065 ? 161.399 134.826 185.471 1.00 49.79  ? 1065 LYS A N   1 
ATOM   4827 C CA  . LYS A 1 1065 ? 161.676 133.502 186.015 1.00 55.23  ? 1065 LYS A CA  1 
ATOM   4828 C C   . LYS A 1 1065 ? 160.413 132.849 186.561 1.00 62.56  ? 1065 LYS A C   1 
ATOM   4829 O O   . LYS A 1 1065 ? 160.204 131.644 186.390 1.00 69.68  ? 1065 LYS A O   1 
ATOM   4830 C CB  . LYS A 1 1065 ? 162.742 133.596 187.105 1.00 58.42  ? 1065 LYS A CB  1 
ATOM   4831 C CG  . LYS A 1 1065 ? 163.228 132.246 187.601 1.00 64.13  ? 1065 LYS A CG  1 
ATOM   4832 C CD  . LYS A 1 1065 ? 163.999 132.375 188.900 1.00 64.28  ? 1065 LYS A CD  1 
ATOM   4833 C CE  . LYS A 1 1065 ? 163.096 132.856 190.022 1.00 66.79  ? 1065 LYS A CE  1 
ATOM   4834 N NZ  . LYS A 1 1065 ? 163.811 132.920 191.326 1.00 63.72  ? 1065 LYS A NZ  1 
ATOM   4835 N N   . ASN A 1 1066 ? 159.565 133.626 187.234 1.00 58.27  ? 1066 ASN A N   1 
ATOM   4836 C CA  . ASN A 1 1066 ? 158.407 133.039 187.899 1.00 63.61  ? 1066 ASN A CA  1 
ATOM   4837 C C   . ASN A 1 1066 ? 157.309 132.672 186.910 1.00 65.39  ? 1066 ASN A C   1 
ATOM   4838 O O   . ASN A 1 1066 ? 156.666 131.627 187.054 1.00 69.05  ? 1066 ASN A O   1 
ATOM   4839 C CB  . ASN A 1 1066 ? 157.871 133.999 188.959 1.00 64.05  ? 1066 ASN A CB  1 
ATOM   4840 C CG  . ASN A 1 1066 ? 158.827 134.173 190.118 1.00 67.78  ? 1066 ASN A CG  1 
ATOM   4841 O OD1 . ASN A 1 1066 ? 159.559 133.252 190.477 1.00 71.36  ? 1066 ASN A OD1 1 
ATOM   4842 N ND2 . ASN A 1 1066 ? 158.827 135.360 190.711 1.00 62.59  ? 1066 ASN A ND2 1 
ATOM   4843 N N   . TYR A 1 1067 ? 157.069 133.514 185.907 1.00 58.03  ? 1067 TYR A N   1 
ATOM   4844 C CA  . TYR A 1 1067 ? 155.917 133.352 185.029 1.00 56.66  ? 1067 TYR A CA  1 
ATOM   4845 C C   . TYR A 1 1067 ? 156.307 132.975 183.605 1.00 57.69  ? 1067 TYR A C   1 
ATOM   4846 O O   . TYR A 1 1067 ? 155.851 131.951 183.091 1.00 69.05  ? 1067 TYR A O   1 
ATOM   4847 C CB  . TYR A 1 1067 ? 155.082 134.638 185.022 1.00 61.95  ? 1067 TYR A CB  1 
ATOM   4848 C CG  . TYR A 1 1067 ? 154.541 135.033 186.377 1.00 64.06  ? 1067 TYR A CG  1 
ATOM   4849 C CD1 . TYR A 1 1067 ? 154.357 134.089 187.376 1.00 65.63  ? 1067 TYR A CD1 1 
ATOM   4850 C CD2 . TYR A 1 1067 ? 154.212 136.351 186.654 1.00 62.57  ? 1067 TYR A CD2 1 
ATOM   4851 C CE1 . TYR A 1 1067 ? 153.866 134.447 188.614 1.00 65.60  ? 1067 TYR A CE1 1 
ATOM   4852 C CE2 . TYR A 1 1067 ? 153.719 136.719 187.888 1.00 66.20  ? 1067 TYR A CE2 1 
ATOM   4853 C CZ  . TYR A 1 1067 ? 153.548 135.764 188.864 1.00 68.93  ? 1067 TYR A CZ  1 
ATOM   4854 O OH  . TYR A 1 1067 ? 153.056 136.126 190.096 1.00 69.27  ? 1067 TYR A OH  1 
ATOM   4855 N N   . TYR A 1 1068 ? 157.144 133.782 182.952 1.00 47.35  ? 1068 TYR A N   1 
ATOM   4856 C CA  . TYR A 1 1068 ? 157.383 133.608 181.522 1.00 49.77  ? 1068 TYR A CA  1 
ATOM   4857 C C   . TYR A 1 1068 ? 158.157 132.326 181.236 1.00 54.10  ? 1068 TYR A C   1 
ATOM   4858 O O   . TYR A 1 1068 ? 157.809 131.568 180.322 1.00 57.75  ? 1068 TYR A O   1 
ATOM   4859 C CB  . TYR A 1 1068 ? 158.125 134.827 180.978 1.00 49.27  ? 1068 TYR A CB  1 
ATOM   4860 C CG  . TYR A 1 1068 ? 158.344 134.816 179.485 1.00 54.99  ? 1068 TYR A CG  1 
ATOM   4861 C CD1 . TYR A 1 1068 ? 157.273 134.823 178.607 1.00 57.49  ? 1068 TYR A CD1 1 
ATOM   4862 C CD2 . TYR A 1 1068 ? 159.624 134.821 178.955 1.00 50.32  ? 1068 TYR A CD2 1 
ATOM   4863 C CE1 . TYR A 1 1068 ? 157.470 134.819 177.243 1.00 56.67  ? 1068 TYR A CE1 1 
ATOM   4864 C CE2 . TYR A 1 1068 ? 159.830 134.820 177.595 1.00 49.77  ? 1068 TYR A CE2 1 
ATOM   4865 C CZ  . TYR A 1 1068 ? 158.751 134.817 176.743 1.00 56.68  ? 1068 TYR A CZ  1 
ATOM   4866 O OH  . TYR A 1 1068 ? 158.956 134.815 175.383 1.00 63.50  ? 1068 TYR A OH  1 
ATOM   4867 N N   . VAL A 1 1069 ? 159.217 132.074 182.003 1.00 58.64  ? 1069 VAL A N   1 
ATOM   4868 C CA  . VAL A 1 1069 ? 160.020 130.870 181.784 1.00 55.66  ? 1069 VAL A CA  1 
ATOM   4869 C C   . VAL A 1 1069 ? 159.215 129.591 181.984 1.00 56.83  ? 1069 VAL A C   1 
ATOM   4870 O O   . VAL A 1 1069 ? 159.319 128.687 181.141 1.00 63.76  ? 1069 VAL A O   1 
ATOM   4871 C CB  . VAL A 1 1069 ? 161.289 130.919 182.653 1.00 57.73  ? 1069 VAL A CB  1 
ATOM   4872 C CG1 . VAL A 1 1069 ? 161.774 129.519 182.954 1.00 61.48  ? 1069 VAL A CG1 1 
ATOM   4873 C CG2 . VAL A 1 1069 ? 162.371 131.718 181.952 1.00 54.57  ? 1069 VAL A CG2 1 
ATOM   4874 N N   . PRO A 1 1070 ? 158.430 129.428 183.058 1.00 57.31  ? 1070 PRO A N   1 
ATOM   4875 C CA  . PRO A 1 1070 ? 157.600 128.215 183.147 1.00 59.52  ? 1070 PRO A CA  1 
ATOM   4876 C C   . PRO A 1 1070 ? 156.609 128.090 182.007 1.00 60.37  ? 1070 PRO A C   1 
ATOM   4877 O O   . PRO A 1 1070 ? 156.306 126.971 181.573 1.00 59.82  ? 1070 PRO A O   1 
ATOM   4878 C CB  . PRO A 1 1070 ? 156.898 128.373 184.501 1.00 55.69  ? 1070 PRO A CB  1 
ATOM   4879 C CG  . PRO A 1 1070 ? 157.793 129.248 185.280 1.00 58.11  ? 1070 PRO A CG  1 
ATOM   4880 C CD  . PRO A 1 1070 ? 158.333 130.226 184.291 1.00 56.96  ? 1070 PRO A CD  1 
ATOM   4881 N N   . PHE A 1 1071 ? 156.088 129.212 181.511 1.00 55.38  ? 1071 PHE A N   1 
ATOM   4882 C CA  . PHE A 1 1071 ? 155.188 129.164 180.365 1.00 48.52  ? 1071 PHE A CA  1 
ATOM   4883 C C   . PHE A 1 1071 ? 155.901 128.629 179.133 1.00 57.23  ? 1071 PHE A C   1 
ATOM   4884 O O   . PHE A 1 1071 ? 155.364 127.784 178.408 1.00 60.17  ? 1071 PHE A O   1 
ATOM   4885 C CB  . PHE A 1 1071 ? 154.612 130.551 180.092 1.00 48.50  ? 1071 PHE A CB  1 
ATOM   4886 C CG  . PHE A 1 1071 ? 153.948 130.675 178.754 1.00 57.79  ? 1071 PHE A CG  1 
ATOM   4887 C CD1 . PHE A 1 1071 ? 152.754 130.028 178.497 1.00 59.64  ? 1071 PHE A CD1 1 
ATOM   4888 C CD2 . PHE A 1 1071 ? 154.513 131.446 177.756 1.00 59.45  ? 1071 PHE A CD2 1 
ATOM   4889 C CE1 . PHE A 1 1071 ? 152.139 130.144 177.269 1.00 55.22  ? 1071 PHE A CE1 1 
ATOM   4890 C CE2 . PHE A 1 1071 ? 153.902 131.565 176.526 1.00 55.79  ? 1071 PHE A CE2 1 
ATOM   4891 C CZ  . PHE A 1 1071 ? 152.715 130.913 176.284 1.00 54.95  ? 1071 PHE A CZ  1 
ATOM   4892 N N   . LEU A 1 1072 ? 157.120 129.109 178.879 1.00 59.92  ? 1072 LEU A N   1 
ATOM   4893 C CA  . LEU A 1 1072 ? 157.857 128.644 177.707 1.00 49.05  ? 1072 LEU A CA  1 
ATOM   4894 C C   . LEU A 1 1072 ? 158.283 127.190 177.855 1.00 46.11  ? 1072 LEU A C   1 
ATOM   4895 O O   . LEU A 1 1072 ? 158.248 126.428 176.883 1.00 57.30  ? 1072 LEU A O   1 
ATOM   4896 C CB  . LEU A 1 1072 ? 159.071 129.532 177.458 1.00 46.10  ? 1072 LEU A CB  1 
ATOM   4897 C CG  . LEU A 1 1072 ? 158.770 130.904 176.862 1.00 44.27  ? 1072 LEU A CG  1 
ATOM   4898 C CD1 . LEU A 1 1072 ? 160.057 131.580 176.451 1.00 47.65  ? 1072 LEU A CD1 1 
ATOM   4899 C CD2 . LEU A 1 1072 ? 157.835 130.772 175.678 1.00 47.48  ? 1072 LEU A CD2 1 
ATOM   4900 N N   . SER A 1 1073 ? 158.694 126.786 179.055 1.00 53.59  ? 1073 SER A N   1 
ATOM   4901 C CA  . SER A 1 1073 ? 159.130 125.410 179.259 1.00 59.21  ? 1073 SER A CA  1 
ATOM   4902 C C   . SER A 1 1073 ? 157.970 124.429 179.234 1.00 63.88  ? 1073 SER A C   1 
ATOM   4903 O O   . SER A 1 1073 ? 158.181 123.247 178.947 1.00 68.64  ? 1073 SER A O   1 
ATOM   4904 C CB  . SER A 1 1073 ? 159.881 125.283 180.584 1.00 64.37  ? 1073 SER A CB  1 
ATOM   4905 O OG  . SER A 1 1073 ? 161.044 126.088 180.591 1.00 74.79  ? 1073 SER A OG  1 
ATOM   4906 N N   . SER A 1 1074 ? 156.757 124.888 179.525 1.00 67.60  ? 1074 SER A N   1 
ATOM   4907 C CA  . SER A 1 1074 ? 155.604 124.004 179.524 1.00 66.79  ? 1074 SER A CA  1 
ATOM   4908 C C   . SER A 1 1074 ? 155.271 123.555 178.108 1.00 68.97  ? 1074 SER A C   1 
ATOM   4909 O O   . SER A 1 1074 ? 155.529 124.260 177.130 1.00 75.35  ? 1074 SER A O   1 
ATOM   4910 C CB  . SER A 1 1074 ? 154.399 124.702 180.148 1.00 66.28  ? 1074 SER A CB  1 
ATOM   4911 O OG  . SER A 1 1074 ? 154.127 125.925 179.489 1.00 71.21  ? 1074 SER A OG  1 
ATOM   4912 N N   . ARG A 1 1075 ? 154.694 122.357 178.007 1.00 80.18  ? 1075 ARG A N   1 
ATOM   4913 C CA  . ARG A 1 1075 ? 154.276 121.840 176.708 1.00 78.05  ? 1075 ARG A CA  1 
ATOM   4914 C C   . ARG A 1 1075 ? 153.223 122.738 176.073 1.00 76.09  ? 1075 ARG A C   1 
ATOM   4915 O O   . ARG A 1 1075 ? 153.256 122.990 174.861 1.00 80.51  ? 1075 ARG A O   1 
ATOM   4916 C CB  . ARG A 1 1075 ? 153.751 120.414 176.869 1.00 80.72  ? 1075 ARG A CB  1 
ATOM   4917 C CG  . ARG A 1 1075 ? 152.701 119.998 175.856 1.00 86.10  ? 1075 ARG A CG  1 
ATOM   4918 C CD  . ARG A 1 1075 ? 152.113 118.645 176.224 1.00 82.97  ? 1075 ARG A CD  1 
ATOM   4919 N NE  . ARG A 1 1075 ? 150.965 118.296 175.397 1.00 85.01  ? 1075 ARG A NE  1 
ATOM   4920 C CZ  . ARG A 1 1075 ? 150.220 117.213 175.573 1.00 88.12  ? 1075 ARG A CZ  1 
ATOM   4921 N NH1 . ARG A 1 1075 ? 150.475 116.349 176.541 1.00 86.51  ? 1075 ARG A NH1 1 
ATOM   4922 N NH2 . ARG A 1 1075 ? 149.193 116.992 174.758 1.00 87.95  ? 1075 ARG A NH2 1 
ATOM   4923 N N   . PHE A 1 1076 ? 152.283 123.232 176.880 1.00 64.61  ? 1076 PHE A N   1 
ATOM   4924 C CA  . PHE A 1 1076 ? 151.237 124.103 176.358 1.00 68.40  ? 1076 PHE A CA  1 
ATOM   4925 C C   . PHE A 1 1076 ? 151.825 125.375 175.766 1.00 70.63  ? 1076 PHE A C   1 
ATOM   4926 O O   . PHE A 1 1076 ? 151.412 125.819 174.687 1.00 73.11  ? 1076 PHE A O   1 
ATOM   4927 C CB  . PHE A 1 1076 ? 150.241 124.432 177.466 1.00 69.17  ? 1076 PHE A CB  1 
ATOM   4928 C CG  . PHE A 1 1076 ? 148.892 124.843 176.966 1.00 71.81  ? 1076 PHE A CG  1 
ATOM   4929 C CD1 . PHE A 1 1076 ? 148.018 123.903 176.451 1.00 69.28  ? 1076 PHE A CD1 1 
ATOM   4930 C CD2 . PHE A 1 1076 ? 148.490 126.165 177.022 1.00 74.20  ? 1076 PHE A CD2 1 
ATOM   4931 C CE1 . PHE A 1 1076 ? 146.773 124.273 175.992 1.00 73.78  ? 1076 PHE A CE1 1 
ATOM   4932 C CE2 . PHE A 1 1076 ? 147.244 126.542 176.566 1.00 75.45  ? 1076 PHE A CE2 1 
ATOM   4933 C CZ  . PHE A 1 1076 ? 146.384 125.595 176.049 1.00 76.51  ? 1076 PHE A CZ  1 
ATOM   4934 N N   . GLY A 1 1077 ? 152.798 125.974 176.451 1.00 60.91  ? 1077 GLY A N   1 
ATOM   4935 C CA  . GLY A 1 1077 ? 153.445 127.154 175.907 1.00 57.26  ? 1077 GLY A CA  1 
ATOM   4936 C C   . GLY A 1 1077 ? 154.178 126.869 174.611 1.00 59.67  ? 1077 GLY A C   1 
ATOM   4937 O O   . GLY A 1 1077 ? 154.125 127.664 173.670 1.00 64.13  ? 1077 GLY A O   1 
ATOM   4938 N N   . LYS A 1 1078 ? 154.867 125.728 174.543 1.00 49.14  ? 1078 LYS A N   1 
ATOM   4939 C CA  . LYS A 1 1078 ? 155.595 125.384 173.328 1.00 45.52  ? 1078 LYS A CA  1 
ATOM   4940 C C   . LYS A 1 1078 ? 154.651 125.204 172.147 1.00 54.67  ? 1078 LYS A C   1 
ATOM   4941 O O   . LYS A 1 1078 ? 154.912 125.719 171.053 1.00 60.82  ? 1078 LYS A O   1 
ATOM   4942 C CB  . LYS A 1 1078 ? 156.425 124.121 173.548 1.00 49.15  ? 1078 LYS A CB  1 
ATOM   4943 C CG  . LYS A 1 1078 ? 157.664 124.341 174.394 1.00 54.26  ? 1078 LYS A CG  1 
ATOM   4944 C CD  . LYS A 1 1078 ? 158.555 123.113 174.405 1.00 53.61  ? 1078 LYS A CD  1 
ATOM   4945 C CE  . LYS A 1 1078 ? 159.827 123.370 175.192 1.00 52.98  ? 1078 LYS A CE  1 
ATOM   4946 N NZ  . LYS A 1 1078 ? 160.701 122.169 175.238 1.00 59.21  ? 1078 LYS A NZ  1 
ATOM   4947 N N   . THR A 1 1079 ? 153.541 124.488 172.345 1.00 61.06  ? 1079 THR A N   1 
ATOM   4948 C CA  . THR A 1 1079 ? 152.619 124.288 171.231 1.00 56.70  ? 1079 THR A CA  1 
ATOM   4949 C C   . THR A 1 1079 ? 151.926 125.591 170.851 1.00 51.55  ? 1079 THR A C   1 
ATOM   4950 O O   . THR A 1 1079 ? 151.685 125.846 169.665 1.00 56.60  ? 1079 THR A O   1 
ATOM   4951 C CB  . THR A 1 1079 ? 151.599 123.192 171.550 1.00 53.73  ? 1079 THR A CB  1 
ATOM   4952 O OG1 . THR A 1 1079 ? 150.716 123.026 170.434 1.00 55.25  ? 1079 THR A OG1 1 
ATOM   4953 C CG2 . THR A 1 1079 ? 150.780 123.531 172.771 1.00 58.66  ? 1079 THR A CG2 1 
ATOM   4954 N N   . ILE A 1 1080 ? 151.625 126.446 171.833 1.00 52.75  ? 1080 ILE A N   1 
ATOM   4955 C CA  . ILE A 1 1080 ? 151.037 127.744 171.514 1.00 59.21  ? 1080 ILE A CA  1 
ATOM   4956 C C   . ILE A 1 1080 ? 151.995 128.567 170.667 1.00 65.42  ? 1080 ILE A C   1 
ATOM   4957 O O   . ILE A 1 1080 ? 151.599 129.168 169.662 1.00 75.80  ? 1080 ILE A O   1 
ATOM   4958 C CB  . ILE A 1 1080 ? 150.641 128.489 172.801 1.00 61.90  ? 1080 ILE A CB  1 
ATOM   4959 C CG1 . ILE A 1 1080 ? 149.300 127.978 173.323 1.00 66.83  ? 1080 ILE A CG1 1 
ATOM   4960 C CG2 . ILE A 1 1080 ? 150.585 129.989 172.558 1.00 61.67  ? 1080 ILE A CG2 1 
ATOM   4961 C CD1 . ILE A 1 1080 ? 148.713 128.838 174.420 1.00 65.64  ? 1080 ILE A CD1 1 
ATOM   4962 N N   . VAL A 1 1081 ? 153.270 128.606 171.057 1.00 49.44  ? 1081 VAL A N   1 
ATOM   4963 C CA  . VAL A 1 1081 ? 154.251 129.384 170.308 1.00 46.48  ? 1081 VAL A CA  1 
ATOM   4964 C C   . VAL A 1 1081 ? 154.411 128.827 168.901 1.00 54.79  ? 1081 VAL A C   1 
ATOM   4965 O O   . VAL A 1 1081 ? 154.472 129.581 167.921 1.00 63.68  ? 1081 VAL A O   1 
ATOM   4966 C CB  . VAL A 1 1081 ? 155.591 129.420 171.064 1.00 55.13  ? 1081 VAL A CB  1 
ATOM   4967 C CG1 . VAL A 1 1081 ? 156.691 129.955 170.172 1.00 54.50  ? 1081 VAL A CG1 1 
ATOM   4968 C CG2 . VAL A 1 1081 ? 155.463 130.269 172.314 1.00 53.19  ? 1081 VAL A CG2 1 
ATOM   4969 N N   . TYR A 1 1082 ? 154.474 127.500 168.776 1.00 54.42  ? 1082 TYR A N   1 
ATOM   4970 C CA  . TYR A 1 1082 ? 154.635 126.893 167.459 1.00 47.93  ? 1082 TYR A CA  1 
ATOM   4971 C C   . TYR A 1 1082 ? 153.456 127.221 166.554 1.00 56.89  ? 1082 TYR A C   1 
ATOM   4972 O O   . TYR A 1 1082 ? 153.641 127.593 165.391 1.00 55.79  ? 1082 TYR A O   1 
ATOM   4973 C CB  . TYR A 1 1082 ? 154.809 125.383 167.597 1.00 45.68  ? 1082 TYR A CB  1 
ATOM   4974 C CG  . TYR A 1 1082 ? 156.228 124.963 167.883 1.00 51.21  ? 1082 TYR A CG  1 
ATOM   4975 C CD1 . TYR A 1 1082 ? 157.293 125.580 167.248 1.00 53.60  ? 1082 TYR A CD1 1 
ATOM   4976 C CD2 . TYR A 1 1082 ? 156.503 123.951 168.789 1.00 54.67  ? 1082 TYR A CD2 1 
ATOM   4977 C CE1 . TYR A 1 1082 ? 158.591 125.200 167.503 1.00 53.68  ? 1082 TYR A CE1 1 
ATOM   4978 C CE2 . TYR A 1 1082 ? 157.798 123.565 169.052 1.00 54.11  ? 1082 TYR A CE2 1 
ATOM   4979 C CZ  . TYR A 1 1082 ? 158.837 124.193 168.407 1.00 57.07  ? 1082 TYR A CZ  1 
ATOM   4980 O OH  . TYR A 1 1082 ? 160.131 123.811 168.667 1.00 62.63  ? 1082 TYR A OH  1 
ATOM   4981 N N   . ILE A 1 1083 ? 152.232 127.106 167.075 1.00 59.85  ? 1083 ILE A N   1 
ATOM   4982 C CA  . ILE A 1 1083 ? 151.052 127.404 166.267 1.00 51.82  ? 1083 ILE A CA  1 
ATOM   4983 C C   . ILE A 1 1083 ? 151.024 128.875 165.879 1.00 49.38  ? 1083 ILE A C   1 
ATOM   4984 O O   . ILE A 1 1083 ? 150.748 129.225 164.723 1.00 62.48  ? 1083 ILE A O   1 
ATOM   4985 C CB  . ILE A 1 1083 ? 149.773 126.994 167.018 1.00 49.50  ? 1083 ILE A CB  1 
ATOM   4986 C CG1 . ILE A 1 1083 ? 149.706 125.475 167.163 1.00 55.53  ? 1083 ILE A CG1 1 
ATOM   4987 C CG2 . ILE A 1 1083 ? 148.545 127.510 166.297 1.00 55.70  ? 1083 ILE A CG2 1 
ATOM   4988 C CD1 . ILE A 1 1083 ? 148.486 124.991 167.909 1.00 53.16  ? 1083 ILE A CD1 1 
ATOM   4989 N N   . MET A 1 1084 ? 151.310 129.761 166.836 1.00 48.89  ? 1084 MET A N   1 
ATOM   4990 C CA  . MET A 1 1084 ? 151.284 131.191 166.559 1.00 58.73  ? 1084 MET A CA  1 
ATOM   4991 C C   . MET A 1 1084 ? 152.290 131.562 165.479 1.00 59.05  ? 1084 MET A C   1 
ATOM   4992 O O   . MET A 1 1084 ? 151.966 132.306 164.544 1.00 60.09  ? 1084 MET A O   1 
ATOM   4993 C CB  . MET A 1 1084 ? 151.565 131.968 167.844 1.00 58.44  ? 1084 MET A CB  1 
ATOM   4994 C CG  . MET A 1 1084 ? 151.613 133.470 167.674 1.00 62.78  ? 1084 MET A CG  1 
ATOM   4995 S SD  . MET A 1 1084 ? 152.313 134.283 169.122 1.00 77.97  ? 1084 MET A SD  1 
ATOM   4996 C CE  . MET A 1 1084 ? 151.352 133.529 170.430 1.00 54.22  ? 1084 MET A CE  1 
ATOM   4997 N N   . PHE A 1 1085 ? 153.510 131.038 165.571 1.00 49.74  ? 1085 PHE A N   1 
ATOM   4998 C CA  . PHE A 1 1085 ? 154.514 131.402 164.582 1.00 48.57  ? 1085 PHE A CA  1 
ATOM   4999 C C   . PHE A 1 1085 ? 154.290 130.704 163.248 1.00 49.17  ? 1085 PHE A C   1 
ATOM   5000 O O   . PHE A 1 1085 ? 154.659 131.253 162.207 1.00 56.45  ? 1085 PHE A O   1 
ATOM   5001 C CB  . PHE A 1 1085 ? 155.911 131.128 165.127 1.00 47.24  ? 1085 PHE A CB  1 
ATOM   5002 C CG  . PHE A 1 1085 ? 156.406 132.205 166.044 1.00 46.71  ? 1085 PHE A CG  1 
ATOM   5003 C CD1 . PHE A 1 1085 ? 157.028 133.329 165.535 1.00 49.90  ? 1085 PHE A CD1 1 
ATOM   5004 C CD2 . PHE A 1 1085 ? 156.220 132.113 167.407 1.00 52.33  ? 1085 PHE A CD2 1 
ATOM   5005 C CE1 . PHE A 1 1085 ? 157.472 134.328 166.370 1.00 50.73  ? 1085 PHE A CE1 1 
ATOM   5006 C CE2 . PHE A 1 1085 ? 156.664 133.109 168.248 1.00 52.16  ? 1085 PHE A CE2 1 
ATOM   5007 C CZ  . PHE A 1 1085 ? 157.289 134.219 167.728 1.00 53.47  ? 1085 PHE A CZ  1 
ATOM   5008 N N   . THR A 1 1086 ? 153.668 129.524 163.241 1.00 54.38  ? 1086 THR A N   1 
ATOM   5009 C CA  . THR A 1 1086 ? 153.250 128.931 161.975 1.00 60.13  ? 1086 THR A CA  1 
ATOM   5010 C C   . THR A 1 1086 ? 152.222 129.810 161.279 1.00 61.29  ? 1086 THR A C   1 
ATOM   5011 O O   . THR A 1 1086 ? 152.305 130.038 160.065 1.00 60.96  ? 1086 THR A O   1 
ATOM   5012 C CB  . THR A 1 1086 ? 152.688 127.531 162.213 1.00 61.09  ? 1086 THR A CB  1 
ATOM   5013 O OG1 . THR A 1 1086 ? 153.766 126.623 162.472 1.00 64.37  ? 1086 THR A OG1 1 
ATOM   5014 C CG2 . THR A 1 1086 ? 151.901 127.052 161.006 1.00 53.55  ? 1086 THR A CG2 1 
ATOM   5015 N N   . ILE A 1 1087 ? 151.256 130.330 162.037 1.00 60.48  ? 1087 ILE A N   1 
ATOM   5016 C CA  . ILE A 1 1087 ? 150.275 131.249 161.466 1.00 50.88  ? 1087 ILE A CA  1 
ATOM   5017 C C   . ILE A 1 1087 ? 150.962 132.502 160.940 1.00 51.25  ? 1087 ILE A C   1 
ATOM   5018 O O   . ILE A 1 1087 ? 150.644 132.992 159.848 1.00 58.81  ? 1087 ILE A O   1 
ATOM   5019 C CB  . ILE A 1 1087 ? 149.194 131.590 162.506 1.00 52.63  ? 1087 ILE A CB  1 
ATOM   5020 C CG1 . ILE A 1 1087 ? 148.345 130.357 162.810 1.00 52.56  ? 1087 ILE A CG1 1 
ATOM   5021 C CG2 . ILE A 1 1087 ? 148.323 132.729 162.015 1.00 56.44  ? 1087 ILE A CG2 1 
ATOM   5022 C CD1 . ILE A 1 1087 ? 147.246 130.609 163.811 1.00 52.67  ? 1087 ILE A CD1 1 
ATOM   5023 N N   . ILE A 1 1088 ? 151.914 133.040 161.705 1.00 57.92  ? 1088 ILE A N   1 
ATOM   5024 C CA  . ILE A 1 1088 ? 152.610 134.253 161.279 1.00 58.44  ? 1088 ILE A CA  1 
ATOM   5025 C C   . ILE A 1 1088 ? 153.389 134.007 159.993 1.00 59.78  ? 1088 ILE A C   1 
ATOM   5026 O O   . ILE A 1 1088 ? 153.373 134.834 159.076 1.00 63.82  ? 1088 ILE A O   1 
ATOM   5027 C CB  . ILE A 1 1088 ? 153.523 134.774 162.403 1.00 50.79  ? 1088 ILE A CB  1 
ATOM   5028 C CG1 . ILE A 1 1088 ? 152.685 135.276 163.575 1.00 53.06  ? 1088 ILE A CG1 1 
ATOM   5029 C CG2 . ILE A 1 1088 ? 154.408 135.888 161.892 1.00 48.91  ? 1088 ILE A CG2 1 
ATOM   5030 C CD1 . ILE A 1 1088 ? 153.501 135.894 164.679 1.00 56.74  ? 1088 ILE A CD1 1 
ATOM   5031 N N   . ILE A 1 1089 ? 154.080 132.870 159.899 1.00 54.78  ? 1089 ILE A N   1 
ATOM   5032 C CA  . ILE A 1 1089 ? 154.863 132.576 158.703 1.00 58.32  ? 1089 ILE A CA  1 
ATOM   5033 C C   . ILE A 1 1089 ? 153.951 132.353 157.501 1.00 61.58  ? 1089 ILE A C   1 
ATOM   5034 O O   . ILE A 1 1089 ? 154.269 132.769 156.379 1.00 68.03  ? 1089 ILE A O   1 
ATOM   5035 C CB  . ILE A 1 1089 ? 155.786 131.371 158.955 1.00 61.11  ? 1089 ILE A CB  1 
ATOM   5036 C CG1 . ILE A 1 1089 ? 156.858 131.736 159.982 1.00 62.52  ? 1089 ILE A CG1 1 
ATOM   5037 C CG2 . ILE A 1 1089 ? 156.438 130.914 157.666 1.00 59.20  ? 1089 ILE A CG2 1 
ATOM   5038 C CD1 . ILE A 1 1089 ? 157.785 130.596 160.324 1.00 60.21  ? 1089 ILE A CD1 1 
ATOM   5039 N N   . ALA A 1 1090 ? 152.809 131.693 157.705 1.00 55.51  ? 1090 ALA A N   1 
ATOM   5040 C CA  . ALA A 1 1090 ? 151.866 131.521 156.605 1.00 55.14  ? 1090 ALA A CA  1 
ATOM   5041 C C   . ALA A 1 1090 ? 151.340 132.866 156.119 1.00 55.20  ? 1090 ALA A C   1 
ATOM   5042 O O   . ALA A 1 1090 ? 151.230 133.101 154.908 1.00 60.85  ? 1090 ALA A O   1 
ATOM   5043 C CB  . ALA A 1 1090 ? 150.715 130.615 157.038 1.00 54.92  ? 1090 ALA A CB  1 
ATOM   5044 N N   . MET A 1 1091 ? 151.015 133.764 157.051 1.00 59.46  ? 1091 MET A N   1 
ATOM   5045 C CA  . MET A 1 1091 ? 150.587 135.103 156.664 1.00 61.40  ? 1091 MET A CA  1 
ATOM   5046 C C   . MET A 1 1091 ? 151.697 135.836 155.925 1.00 65.74  ? 1091 MET A C   1 
ATOM   5047 O O   . MET A 1 1091 ? 151.434 136.588 154.982 1.00 73.10  ? 1091 MET A O   1 
ATOM   5048 C CB  . MET A 1 1091 ? 150.148 135.894 157.895 1.00 65.49  ? 1091 MET A CB  1 
ATOM   5049 C CG  . MET A 1 1091 ? 148.895 135.362 158.561 1.00 66.47  ? 1091 MET A CG  1 
ATOM   5050 S SD  . MET A 1 1091 ? 148.522 136.219 160.100 1.00 87.02  ? 1091 MET A SD  1 
ATOM   5051 C CE  . MET A 1 1091 ? 148.385 137.905 159.517 1.00 66.16  ? 1091 MET A CE  1 
ATOM   5052 N N   . SER A 1 1092 ? 152.947 135.632 156.345 1.00 64.47  ? 1092 SER A N   1 
ATOM   5053 C CA  . SER A 1 1092 ? 154.073 136.250 155.654 1.00 63.99  ? 1092 SER A CA  1 
ATOM   5054 C C   . SER A 1 1092 ? 154.179 135.750 154.221 1.00 64.93  ? 1092 SER A C   1 
ATOM   5055 O O   . SER A 1 1092 ? 154.428 136.533 153.299 1.00 71.69  ? 1092 SER A O   1 
ATOM   5056 C CB  . SER A 1 1092 ? 155.369 135.972 156.411 1.00 62.26  ? 1092 SER A CB  1 
ATOM   5057 O OG  . SER A 1 1092 ? 155.283 136.421 157.751 1.00 67.44  ? 1092 SER A OG  1 
ATOM   5058 N N   . ILE A 1 1093 ? 154.001 134.447 154.016 1.00 62.39  ? 1093 ILE A N   1 
ATOM   5059 C CA  . ILE A 1 1093 ? 154.046 133.894 152.664 1.00 64.06  ? 1093 ILE A CA  1 
ATOM   5060 C C   . ILE A 1 1093 ? 152.931 134.490 151.813 1.00 68.43  ? 1093 ILE A C   1 
ATOM   5061 O O   . ILE A 1 1093 ? 153.150 134.919 150.671 1.00 71.50  ? 1093 ILE A O   1 
ATOM   5062 C CB  . ILE A 1 1093 ? 153.959 132.358 152.710 1.00 61.51  ? 1093 ILE A CB  1 
ATOM   5063 C CG1 . ILE A 1 1093 ? 155.212 131.770 153.358 1.00 66.84  ? 1093 ILE A CG1 1 
ATOM   5064 C CG2 . ILE A 1 1093 ? 153.762 131.794 151.317 1.00 62.24  ? 1093 ILE A CG2 1 
ATOM   5065 C CD1 . ILE A 1 1093 ? 156.481 132.046 152.591 1.00 68.49  ? 1093 ILE A CD1 1 
ATOM   5066 N N   . TYR A 1 1094 ? 151.718 134.544 152.367 1.00 70.72  ? 1094 TYR A N   1 
ATOM   5067 C CA  . TYR A 1 1094 ? 150.598 135.099 151.614 1.00 67.75  ? 1094 TYR A CA  1 
ATOM   5068 C C   . TYR A 1 1094 ? 150.834 136.564 151.273 1.00 72.73  ? 1094 TYR A C   1 
ATOM   5069 O O   . TYR A 1 1094 ? 150.475 137.021 150.182 1.00 77.76  ? 1094 TYR A O   1 
ATOM   5070 C CB  . TYR A 1 1094 ? 149.297 134.935 152.393 1.00 70.80  ? 1094 TYR A CB  1 
ATOM   5071 C CG  . TYR A 1 1094 ? 148.133 135.648 151.752 1.00 72.53  ? 1094 TYR A CG  1 
ATOM   5072 C CD1 . TYR A 1 1094 ? 147.575 135.179 150.573 1.00 72.95  ? 1094 TYR A CD1 1 
ATOM   5073 C CD2 . TYR A 1 1094 ? 147.594 136.791 152.323 1.00 74.24  ? 1094 TYR A CD2 1 
ATOM   5074 C CE1 . TYR A 1 1094 ? 146.513 135.828 149.980 1.00 77.42  ? 1094 TYR A CE1 1 
ATOM   5075 C CE2 . TYR A 1 1094 ? 146.531 137.446 151.738 1.00 76.41  ? 1094 TYR A CE2 1 
ATOM   5076 C CZ  . TYR A 1 1094 ? 145.994 136.961 150.566 1.00 79.04  ? 1094 TYR A CZ  1 
ATOM   5077 O OH  . TYR A 1 1094 ? 144.934 137.610 149.978 1.00 78.09  ? 1094 TYR A OH  1 
ATOM   5078 N N   . GLY A 1 1095 ? 151.422 137.322 152.199 1.00 74.07  ? 1095 GLY A N   1 
ATOM   5079 C CA  . GLY A 1 1095 ? 151.781 138.697 151.894 1.00 72.11  ? 1095 GLY A CA  1 
ATOM   5080 C C   . GLY A 1 1095 ? 152.826 138.791 150.800 1.00 70.90  ? 1095 GLY A C   1 
ATOM   5081 O O   . GLY A 1 1095 ? 152.743 139.650 149.920 1.00 78.29  ? 1095 GLY A O   1 
ATOM   5082 N N   . CYS A 1 1096 ? 153.824 137.904 150.839 1.00 58.38  ? 1096 CYS A N   1 
ATOM   5083 C CA  . CYS A 1 1096 ? 154.819 137.862 149.774 1.00 65.37  ? 1096 CYS A CA  1 
ATOM   5084 C C   . CYS A 1 1096 ? 154.161 137.613 148.427 1.00 73.33  ? 1096 CYS A C   1 
ATOM   5085 O O   . CYS A 1 1096 ? 154.637 138.098 147.394 1.00 70.15  ? 1096 CYS A O   1 
ATOM   5086 C CB  . CYS A 1 1096 ? 155.862 136.784 150.064 1.00 72.10  ? 1096 CYS A CB  1 
ATOM   5087 S SG  . CYS A 1 1096 ? 156.959 137.142 151.448 1.00 82.05  ? 1096 CYS A SG  1 
ATOM   5088 N N   . THR A 1 1097 ? 153.066 136.851 148.416 1.00 79.58  ? 1097 THR A N   1 
ATOM   5089 C CA  . THR A 1 1097 ? 152.305 136.696 147.180 1.00 76.55  ? 1097 THR A CA  1 
ATOM   5090 C C   . THR A 1 1097 ? 151.762 138.032 146.688 1.00 77.65  ? 1097 THR A C   1 
ATOM   5091 O O   . THR A 1 1097 ? 151.827 138.325 145.490 1.00 80.09  ? 1097 THR A O   1 
ATOM   5092 C CB  . THR A 1 1097 ? 151.163 135.702 147.385 1.00 77.78  ? 1097 THR A CB  1 
ATOM   5093 O OG1 . THR A 1 1097 ? 151.701 134.424 147.743 1.00 79.69  ? 1097 THR A OG1 1 
ATOM   5094 C CG2 . THR A 1 1097 ? 150.345 135.561 146.115 1.00 77.76  ? 1097 THR A CG2 1 
ATOM   5095 N N   . LEU A 1 1098 ? 151.236 138.858 147.593 1.00 78.36  ? 1098 LEU A N   1 
ATOM   5096 C CA  . LEU A 1 1098 ? 150.680 140.163 147.237 1.00 76.40  ? 1098 LEU A CA  1 
ATOM   5097 C C   . LEU A 1 1098 ? 151.802 141.195 147.286 1.00 79.06  ? 1098 LEU A C   1 
ATOM   5098 O O   . LEU A 1 1098 ? 151.922 141.984 148.221 1.00 85.45  ? 1098 LEU A O   1 
ATOM   5099 C CB  . LEU A 1 1098 ? 149.538 140.534 148.174 1.00 77.67  ? 1098 LEU A CB  1 
ATOM   5100 C CG  . LEU A 1 1098 ? 148.454 139.481 148.393 1.00 80.85  ? 1098 LEU A CG  1 
ATOM   5101 C CD1 . LEU A 1 1098 ? 147.378 140.017 149.322 1.00 81.01  ? 1098 LEU A CD1 1 
ATOM   5102 C CD2 . LEU A 1 1098 ? 147.856 139.044 147.068 1.00 81.25  ? 1098 LEU A CD2 1 
ATOM   5103 N N   . MET A 1 1099 ? 152.631 141.189 146.248 1.00 92.28  ? 1099 MET A N   1 
ATOM   5104 C CA  . MET A 1 1099 ? 153.808 142.043 146.176 1.00 94.50  ? 1099 MET A CA  1 
ATOM   5105 C C   . MET A 1 1099 ? 153.568 143.173 145.186 1.00 95.64  ? 1099 MET A C   1 
ATOM   5106 O O   . MET A 1 1099 ? 153.166 142.930 144.044 1.00 96.91  ? 1099 MET A O   1 
ATOM   5107 C CB  . MET A 1 1099 ? 155.038 141.232 145.766 1.00 93.78  ? 1099 MET A CB  1 
ATOM   5108 C CG  . MET A 1 1099 ? 156.302 142.050 145.608 1.00 91.91  ? 1099 MET A CG  1 
ATOM   5109 S SD  . MET A 1 1099 ? 157.719 141.011 145.202 1.00 109.28 ? 1099 MET A SD  1 
ATOM   5110 C CE  . MET A 1 1099 ? 157.133 140.201 143.717 1.00 97.07  ? 1099 MET A CE  1 
ATOM   5111 N N   . LYS A 1 1100 ? 153.817 144.404 145.626 1.00 84.85  ? 1100 LYS A N   1 
ATOM   5112 C CA  . LYS A 1 1100 ? 153.687 145.582 144.784 1.00 82.78  ? 1100 LYS A CA  1 
ATOM   5113 C C   . LYS A 1 1100 ? 154.953 146.418 144.887 1.00 84.77  ? 1100 LYS A C   1 
ATOM   5114 O O   . LYS A 1 1100 ? 155.645 146.403 145.907 1.00 88.34  ? 1100 LYS A O   1 
ATOM   5115 C CB  . LYS A 1 1100 ? 152.467 146.425 145.169 1.00 84.14  ? 1100 LYS A CB  1 
ATOM   5116 C CG  . LYS A 1 1100 ? 151.142 145.716 144.958 1.00 83.52  ? 1100 LYS A CG  1 
ATOM   5117 C CD  . LYS A 1 1100 ? 149.974 146.674 145.100 1.00 88.17  ? 1100 LYS A CD  1 
ATOM   5118 C CE  . LYS A 1 1100 ? 149.970 147.341 146.463 1.00 87.08  ? 1100 LYS A CE  1 
ATOM   5119 N NZ  . LYS A 1 1100 ? 148.837 148.296 146.605 1.00 85.94  ? 1100 LYS A NZ  1 
ATOM   5120 N N   . LYS A 1 1101 ? 155.250 147.147 143.816 1.00 79.12  ? 1101 LYS A N   1 
ATOM   5121 C CA  . LYS A 1 1101 ? 156.499 147.881 143.690 1.00 79.95  ? 1101 LYS A CA  1 
ATOM   5122 C C   . LYS A 1 1101 ? 156.225 149.309 143.244 1.00 81.64  ? 1101 LYS A C   1 
ATOM   5123 O O   . LYS A 1 1101 ? 155.378 149.545 142.380 1.00 86.24  ? 1101 LYS A O   1 
ATOM   5124 C CB  . LYS A 1 1101 ? 157.429 147.184 142.691 1.00 80.00  ? 1101 LYS A CB  1 
ATOM   5125 C CG  . LYS A 1 1101 ? 158.668 147.968 142.312 1.00 80.29  ? 1101 LYS A CG  1 
ATOM   5126 C CD  . LYS A 1 1101 ? 159.550 147.157 141.378 1.00 83.19  ? 1101 LYS A CD  1 
ATOM   5127 C CE  . LYS A 1 1101 ? 158.770 146.672 140.167 1.00 81.78  ? 1101 LYS A CE  1 
ATOM   5128 N NZ  . LYS A 1 1101 ? 159.595 145.799 139.289 1.00 79.78  ? 1101 LYS A NZ  1 
ATOM   5129 N N   . GLY A 1 1102 ? 156.942 150.259 143.841 1.00 68.27  ? 1102 GLY A N   1 
ATOM   5130 C CA  . GLY A 1 1102 ? 156.881 151.636 143.395 1.00 64.28  ? 1102 GLY A CA  1 
ATOM   5131 C C   . GLY A 1 1102 ? 156.189 152.589 144.347 1.00 67.69  ? 1102 GLY A C   1 
ATOM   5132 O O   . GLY A 1 1102 ? 155.207 152.226 144.999 1.00 69.61  ? 1102 GLY A O   1 
ATOM   5133 N N   . ILE A 1 1103 ? 156.697 153.816 144.432 1.00 71.70  ? 1103 ILE A N   1 
ATOM   5134 C CA  . ILE A 1 1103 ? 156.087 154.880 145.218 1.00 70.30  ? 1103 ILE A CA  1 
ATOM   5135 C C   . ILE A 1 1103 ? 156.062 156.143 144.369 1.00 72.26  ? 1103 ILE A C   1 
ATOM   5136 O O   . ILE A 1 1103 ? 156.998 156.408 143.606 1.00 77.05  ? 1103 ILE A O   1 
ATOM   5137 C CB  . ILE A 1 1103 ? 156.840 155.123 146.544 1.00 67.71  ? 1103 ILE A CB  1 
ATOM   5138 C CG1 . ILE A 1 1103 ? 156.088 156.131 147.413 1.00 66.08  ? 1103 ILE A CG1 1 
ATOM   5139 C CG2 . ILE A 1 1103 ? 158.252 155.613 146.283 1.00 69.62  ? 1103 ILE A CG2 1 
ATOM   5140 C CD1 . ILE A 1 1103 ? 154.697 155.688 147.790 1.00 72.79  ? 1103 ILE A CD1 1 
ATOM   5141 N N   . LYS A 1 1104 ? 154.979 156.907 144.476 1.00 76.47  ? 1104 LYS A N   1 
ATOM   5142 C CA  . LYS A 1 1104 ? 154.897 158.170 143.758 1.00 76.48  ? 1104 LYS A CA  1 
ATOM   5143 C C   . LYS A 1 1104 ? 155.801 159.205 144.416 1.00 74.08  ? 1104 LYS A C   1 
ATOM   5144 O O   . LYS A 1 1104 ? 155.943 159.241 145.640 1.00 76.57  ? 1104 LYS A O   1 
ATOM   5145 C CB  . LYS A 1 1104 ? 153.455 158.668 143.716 1.00 73.90  ? 1104 LYS A CB  1 
ATOM   5146 C CG  . LYS A 1 1104 ? 153.200 159.707 142.640 1.00 75.03  ? 1104 LYS A CG  1 
ATOM   5147 C CD  . LYS A 1 1104 ? 151.735 160.096 142.582 1.00 75.55  ? 1104 LYS A CD  1 
ATOM   5148 C CE  . LYS A 1 1104 ? 151.488 161.133 141.500 1.00 77.04  ? 1104 LYS A CE  1 
ATOM   5149 N NZ  . LYS A 1 1104 ? 150.053 161.515 141.417 1.00 79.46  ? 1104 LYS A NZ  1 
ATOM   5150 N N   . TYR A 1 1105 ? 156.418 160.051 143.589 1.00 72.28  ? 1105 TYR A N   1 
ATOM   5151 C CA  . TYR A 1 1105 ? 157.413 160.991 144.095 1.00 72.57  ? 1105 TYR A CA  1 
ATOM   5152 C C   . TYR A 1 1105 ? 156.793 162.014 145.038 1.00 73.39  ? 1105 TYR A C   1 
ATOM   5153 O O   . TYR A 1 1105 ? 157.409 162.398 146.039 1.00 77.24  ? 1105 TYR A O   1 
ATOM   5154 C CB  . TYR A 1 1105 ? 158.113 161.692 142.931 1.00 72.67  ? 1105 TYR A CB  1 
ATOM   5155 C CG  . TYR A 1 1105 ? 157.233 162.660 142.177 1.00 75.96  ? 1105 TYR A CG  1 
ATOM   5156 C CD1 . TYR A 1 1105 ? 156.350 162.213 141.206 1.00 77.92  ? 1105 TYR A CD1 1 
ATOM   5157 C CD2 . TYR A 1 1105 ? 157.285 164.021 142.436 1.00 75.32  ? 1105 TYR A CD2 1 
ATOM   5158 C CE1 . TYR A 1 1105 ? 155.544 163.093 140.516 1.00 77.89  ? 1105 TYR A CE1 1 
ATOM   5159 C CE2 . TYR A 1 1105 ? 156.483 164.908 141.753 1.00 77.28  ? 1105 TYR A CE2 1 
ATOM   5160 C CZ  . TYR A 1 1105 ? 155.615 164.439 140.794 1.00 79.83  ? 1105 TYR A CZ  1 
ATOM   5161 O OH  . TYR A 1 1105 ? 154.813 165.321 140.108 1.00 80.28  ? 1105 TYR A OH  1 
ATOM   5162 N N   . ASP A 1 1106 ? 155.574 162.469 144.739 1.00 74.01  ? 1106 ASP A N   1 
ATOM   5163 C CA  . ASP A 1 1106 ? 154.970 163.539 145.526 1.00 75.22  ? 1106 ASP A CA  1 
ATOM   5164 C C   . ASP A 1 1106 ? 154.735 163.134 146.974 1.00 79.08  ? 1106 ASP A C   1 
ATOM   5165 O O   . ASP A 1 1106 ? 154.530 164.008 147.822 1.00 82.60  ? 1106 ASP A O   1 
ATOM   5166 C CB  . ASP A 1 1106 ? 153.654 163.989 144.889 1.00 76.48  ? 1106 ASP A CB  1 
ATOM   5167 C CG  . ASP A 1 1106 ? 152.641 162.868 144.782 1.00 82.37  ? 1106 ASP A CG  1 
ATOM   5168 O OD1 . ASP A 1 1106 ? 152.990 161.713 145.102 1.00 87.33  ? 1106 ASP A OD1 1 
ATOM   5169 O OD2 . ASP A 1 1106 ? 151.492 163.142 144.379 1.00 79.87  ? 1106 ASP A OD2 1 
ATOM   5170 N N   . LYS A 1 1107 ? 154.760 161.835 147.278 1.00 70.68  ? 1107 LYS A N   1 
ATOM   5171 C CA  . LYS A 1 1107 ? 154.648 161.395 148.662 1.00 68.79  ? 1107 LYS A CA  1 
ATOM   5172 C C   . LYS A 1 1107 ? 155.791 161.915 149.521 1.00 71.04  ? 1107 LYS A C   1 
ATOM   5173 O O   . LYS A 1 1107 ? 155.654 161.975 150.746 1.00 73.45  ? 1107 LYS A O   1 
ATOM   5174 C CB  . LYS A 1 1107 ? 154.601 159.869 148.730 1.00 63.66  ? 1107 LYS A CB  1 
ATOM   5175 C CG  . LYS A 1 1107 ? 153.202 159.287 148.794 1.00 65.30  ? 1107 LYS A CG  1 
ATOM   5176 C CD  . LYS A 1 1107 ? 152.385 159.652 147.573 1.00 76.27  ? 1107 LYS A CD  1 
ATOM   5177 C CE  . LYS A 1 1107 ? 150.985 159.075 147.659 1.00 76.31  ? 1107 LYS A CE  1 
ATOM   5178 N NZ  . LYS A 1 1107 ? 150.158 159.454 146.481 1.00 71.97  ? 1107 LYS A NZ  1 
ATOM   5179 N N   . ALA A 1 1108 ? 156.914 162.292 148.907 1.00 63.33  ? 1108 ALA A N   1 
ATOM   5180 C CA  . ALA A 1 1108 ? 158.024 162.853 149.664 1.00 57.49  ? 1108 ALA A CA  1 
ATOM   5181 C C   . ALA A 1 1108 ? 157.715 164.240 150.207 1.00 63.36  ? 1108 ALA A C   1 
ATOM   5182 O O   . ALA A 1 1108 ? 158.472 164.746 151.041 1.00 70.63  ? 1108 ALA A O   1 
ATOM   5183 C CB  . ALA A 1 1108 ? 159.279 162.909 148.796 1.00 61.36  ? 1108 ALA A CB  1 
ATOM   5184 N N   . PHE A 1 1109 ? 156.639 164.866 149.755 1.00 66.30  ? 1109 PHE A N   1 
ATOM   5185 C CA  . PHE A 1 1109 ? 156.335 166.207 150.219 1.00 67.63  ? 1109 PHE A CA  1 
ATOM   5186 C C   . PHE A 1 1109 ? 155.172 166.192 151.203 1.00 66.80  ? 1109 PHE A C   1 
ATOM   5187 O O   . PHE A 1 1109 ? 154.322 165.299 151.159 1.00 63.26  ? 1109 PHE A O   1 
ATOM   5188 C CB  . PHE A 1 1109 ? 155.985 167.122 149.043 1.00 63.97  ? 1109 PHE A CB  1 
ATOM   5189 C CG  . PHE A 1 1109 ? 157.092 167.275 148.045 1.00 65.27  ? 1109 PHE A CG  1 
ATOM   5190 C CD1 . PHE A 1 1109 ? 158.223 168.005 148.355 1.00 65.41  ? 1109 PHE A CD1 1 
ATOM   5191 C CD2 . PHE A 1 1109 ? 156.997 166.698 146.793 1.00 65.08  ? 1109 PHE A CD2 1 
ATOM   5192 C CE1 . PHE A 1 1109 ? 159.242 168.150 147.439 1.00 66.61  ? 1109 PHE A CE1 1 
ATOM   5193 C CE2 . PHE A 1 1109 ? 158.012 166.841 145.873 1.00 65.71  ? 1109 PHE A CE2 1 
ATOM   5194 C CZ  . PHE A 1 1109 ? 159.135 167.568 146.197 1.00 65.92  ? 1109 PHE A CZ  1 
ATOM   5195 N N   . PRO A 1 1110 ? 155.122 167.165 152.110 1.00 61.92  ? 1110 PRO A N   1 
ATOM   5196 C CA  . PRO A 1 1110 ? 153.972 167.270 153.011 1.00 60.71  ? 1110 PRO A CA  1 
ATOM   5197 C C   . PRO A 1 1110 ? 152.701 167.587 152.242 1.00 66.88  ? 1110 PRO A C   1 
ATOM   5198 O O   . PRO A 1 1110 ? 152.729 168.225 151.188 1.00 70.36  ? 1110 PRO A O   1 
ATOM   5199 C CB  . PRO A 1 1110 ? 154.358 168.418 153.949 1.00 61.00  ? 1110 PRO A CB  1 
ATOM   5200 C CG  . PRO A 1 1110 ? 155.838 168.522 153.841 1.00 61.62  ? 1110 PRO A CG  1 
ATOM   5201 C CD  . PRO A 1 1110 ? 156.168 168.145 152.437 1.00 60.26  ? 1110 PRO A CD  1 
ATOM   5202 N N   . VAL A 1 1111 ? 151.572 167.131 152.788 1.00 68.93  ? 1111 VAL A N   1 
ATOM   5203 C CA  . VAL A 1 1111 ? 150.291 167.292 152.111 1.00 68.44  ? 1111 VAL A CA  1 
ATOM   5204 C C   . VAL A 1 1111 ? 149.915 168.757 151.944 1.00 70.69  ? 1111 VAL A C   1 
ATOM   5205 O O   . VAL A 1 1111 ? 149.207 169.109 150.996 1.00 69.21  ? 1111 VAL A O   1 
ATOM   5206 C CB  . VAL A 1 1111 ? 149.193 166.527 152.877 1.00 68.12  ? 1111 VAL A CB  1 
ATOM   5207 C CG1 . VAL A 1 1111 ? 147.930 166.424 152.038 1.00 67.92  ? 1111 VAL A CG1 1 
ATOM   5208 C CG2 . VAL A 1 1111 ? 149.690 165.149 153.272 1.00 68.54  ? 1111 VAL A CG2 1 
ATOM   5209 N N   . ASP A 1 1112 ? 150.378 169.628 152.837 1.00 75.08  ? 1112 ASP A N   1 
ATOM   5210 C CA  . ASP A 1 1112 ? 150.019 171.038 152.779 1.00 70.97  ? 1112 ASP A CA  1 
ATOM   5211 C C   . ASP A 1 1112 ? 150.867 171.838 151.799 1.00 73.77  ? 1112 ASP A C   1 
ATOM   5212 O O   . ASP A 1 1112 ? 150.556 173.009 151.555 1.00 75.34  ? 1112 ASP A O   1 
ATOM   5213 C CB  . ASP A 1 1112 ? 150.121 171.667 154.172 1.00 72.23  ? 1112 ASP A CB  1 
ATOM   5214 C CG  . ASP A 1 1112 ? 151.479 171.457 154.809 1.00 76.76  ? 1112 ASP A CG  1 
ATOM   5215 O OD1 . ASP A 1 1112 ? 152.350 170.838 154.166 1.00 76.58  ? 1112 ASP A OD1 1 
ATOM   5216 O OD2 . ASP A 1 1112 ? 151.675 171.911 155.955 1.00 80.51  ? 1112 ASP A OD2 1 
ATOM   5217 N N   . SER A 1 1113 ? 151.921 171.249 151.240 1.00 65.89  ? 1113 SER A N   1 
ATOM   5218 C CA  . SER A 1 1113 ? 152.726 171.951 150.249 1.00 59.33  ? 1113 SER A CA  1 
ATOM   5219 C C   . SER A 1 1113 ? 151.881 172.271 149.024 1.00 65.79  ? 1113 SER A C   1 
ATOM   5220 O O   . SER A 1 1113 ? 151.046 171.468 148.602 1.00 66.93  ? 1113 SER A O   1 
ATOM   5221 C CB  . SER A 1 1113 ? 153.932 171.107 149.847 1.00 62.04  ? 1113 SER A CB  1 
ATOM   5222 O OG  . SER A 1 1113 ? 153.517 169.926 149.187 1.00 66.91  ? 1113 SER A OG  1 
ATOM   5223 N N   . TYR A 1 1114 ? 152.102 173.456 148.452 1.00 62.43  ? 1114 TYR A N   1 
ATOM   5224 C CA  . TYR A 1 1114 ? 151.237 173.909 147.368 1.00 57.23  ? 1114 TYR A CA  1 
ATOM   5225 C C   . TYR A 1 1114 ? 151.377 173.036 146.129 1.00 62.48  ? 1114 TYR A C   1 
ATOM   5226 O O   . TYR A 1 1114 ? 150.447 172.960 145.320 1.00 71.59  ? 1114 TYR A O   1 
ATOM   5227 C CB  . TYR A 1 1114 ? 151.517 175.375 147.037 1.00 54.45  ? 1114 TYR A CB  1 
ATOM   5228 C CG  . TYR A 1 1114 ? 152.840 175.648 146.360 1.00 64.50  ? 1114 TYR A CG  1 
ATOM   5229 C CD1 . TYR A 1 1114 ? 152.948 175.638 144.978 1.00 67.47  ? 1114 TYR A CD1 1 
ATOM   5230 C CD2 . TYR A 1 1114 ? 153.972 175.948 147.100 1.00 70.01  ? 1114 TYR A CD2 1 
ATOM   5231 C CE1 . TYR A 1 1114 ? 154.149 175.898 144.353 1.00 64.43  ? 1114 TYR A CE1 1 
ATOM   5232 C CE2 . TYR A 1 1114 ? 155.178 176.212 146.482 1.00 62.69  ? 1114 TYR A CE2 1 
ATOM   5233 C CZ  . TYR A 1 1114 ? 155.260 176.184 145.109 1.00 60.49  ? 1114 TYR A CZ  1 
ATOM   5234 O OH  . TYR A 1 1114 ? 156.457 176.444 144.488 1.00 66.21  ? 1114 TYR A OH  1 
ATOM   5235 N N   . VAL A 1 1115 ? 152.517 172.363 145.965 1.00 57.70  ? 1115 VAL A N   1 
ATOM   5236 C CA  . VAL A 1 1115 ? 152.683 171.456 144.832 1.00 52.14  ? 1115 VAL A CA  1 
ATOM   5237 C C   . VAL A 1 1115 ? 151.709 170.290 144.938 1.00 60.64  ? 1115 VAL A C   1 
ATOM   5238 O O   . VAL A 1 1115 ? 151.010 169.950 143.975 1.00 65.07  ? 1115 VAL A O   1 
ATOM   5239 C CB  . VAL A 1 1115 ? 154.139 170.969 144.744 1.00 51.88  ? 1115 VAL A CB  1 
ATOM   5240 C CG1 . VAL A 1 1115 ? 154.254 169.834 143.749 1.00 57.66  ? 1115 VAL A CG1 1 
ATOM   5241 C CG2 . VAL A 1 1115 ? 155.045 172.111 144.348 1.00 62.62  ? 1115 VAL A CG2 1 
ATOM   5242 N N   . ARG A 1 1116 ? 151.646 169.661 146.112 1.00 67.21  ? 1116 ARG A N   1 
ATOM   5243 C CA  . ARG A 1 1116 ? 150.738 168.534 146.292 1.00 57.57  ? 1116 ARG A CA  1 
ATOM   5244 C C   . ARG A 1 1116 ? 149.285 168.973 146.192 1.00 58.00  ? 1116 ARG A C   1 
ATOM   5245 O O   . ARG A 1 1116 ? 148.451 168.255 145.631 1.00 63.45  ? 1116 ARG A O   1 
ATOM   5246 C CB  . ARG A 1 1116 ? 150.999 167.849 147.631 1.00 53.85  ? 1116 ARG A CB  1 
ATOM   5247 C CG  . ARG A 1 1116 ? 152.306 167.091 147.685 1.00 58.40  ? 1116 ARG A CG  1 
ATOM   5248 C CD  . ARG A 1 1116 ? 152.292 166.064 148.798 1.00 63.90  ? 1116 ARG A CD  1 
ATOM   5249 N NE  . ARG A 1 1116 ? 151.269 165.048 148.586 1.00 67.21  ? 1116 ARG A NE  1 
ATOM   5250 C CZ  . ARG A 1 1116 ? 151.098 163.986 149.361 1.00 66.29  ? 1116 ARG A CZ  1 
ATOM   5251 N NH1 . ARG A 1 1116 ? 151.869 163.766 150.412 1.00 63.00  ? 1116 ARG A NH1 1 
ATOM   5252 N NH2 . ARG A 1 1116 ? 150.129 163.123 149.072 1.00 65.62  ? 1116 ARG A NH2 1 
ATOM   5253 N N   . ARG A 1 1117 ? 148.958 170.143 146.743 1.00 52.62  ? 1117 ARG A N   1 
ATOM   5254 C CA  . ARG A 1 1117 ? 147.590 170.637 146.642 1.00 51.55  ? 1117 ARG A CA  1 
ATOM   5255 C C   . ARG A 1 1117 ? 147.209 170.899 145.192 1.00 54.39  ? 1117 ARG A C   1 
ATOM   5256 O O   . ARG A 1 1117 ? 146.101 170.556 144.762 1.00 61.54  ? 1117 ARG A O   1 
ATOM   5257 C CB  . ARG A 1 1117 ? 147.420 171.900 147.482 1.00 53.63  ? 1117 ARG A CB  1 
ATOM   5258 C CG  . ARG A 1 1117 ? 147.766 171.716 148.946 1.00 55.34  ? 1117 ARG A CG  1 
ATOM   5259 C CD  . ARG A 1 1117 ? 146.999 172.691 149.817 1.00 60.05  ? 1117 ARG A CD  1 
ATOM   5260 N NE  . ARG A 1 1117 ? 147.036 174.044 149.278 1.00 66.04  ? 1117 ARG A NE  1 
ATOM   5261 C CZ  . ARG A 1 1117 ? 147.987 174.929 149.539 1.00 62.98  ? 1117 ARG A CZ  1 
ATOM   5262 N NH1 . ARG A 1 1117 ? 149.000 174.637 150.338 1.00 55.25  ? 1117 ARG A NH1 1 
ATOM   5263 N NH2 . ARG A 1 1117 ? 147.920 176.135 148.985 1.00 57.16  ? 1117 ARG A NH2 1 
ATOM   5264 N N   . PHE A 1 1118 ? 148.119 171.496 144.419 1.00 49.36  ? 1118 PHE A N   1 
ATOM   5265 C CA  . PHE A 1 1118 ? 147.848 171.713 143.004 1.00 41.20  ? 1118 PHE A CA  1 
ATOM   5266 C C   . PHE A 1 1118 ? 147.667 170.394 142.271 1.00 49.68  ? 1118 PHE A C   1 
ATOM   5267 O O   . PHE A 1 1118 ? 146.779 170.268 141.422 1.00 59.22  ? 1118 PHE A O   1 
ATOM   5268 C CB  . PHE A 1 1118 ? 148.975 172.516 142.360 1.00 41.25  ? 1118 PHE A CB  1 
ATOM   5269 C CG  . PHE A 1 1118 ? 148.946 172.491 140.860 1.00 47.91  ? 1118 PHE A CG  1 
ATOM   5270 C CD1 . PHE A 1 1118 ? 148.146 173.370 140.159 1.00 47.61  ? 1118 PHE A CD1 1 
ATOM   5271 C CD2 . PHE A 1 1118 ? 149.712 171.583 140.153 1.00 49.17  ? 1118 PHE A CD2 1 
ATOM   5272 C CE1 . PHE A 1 1118 ? 148.111 173.346 138.784 1.00 40.64  ? 1118 PHE A CE1 1 
ATOM   5273 C CE2 . PHE A 1 1118 ? 149.678 171.554 138.779 1.00 52.25  ? 1118 PHE A CE2 1 
ATOM   5274 C CZ  . PHE A 1 1118 ? 148.878 172.437 138.095 1.00 46.45  ? 1118 PHE A CZ  1 
ATOM   5275 N N   . THR A 1 1119 ? 148.517 169.409 142.563 1.00 50.92  ? 1119 THR A N   1 
ATOM   5276 C CA  . THR A 1 1119 ? 148.394 168.115 141.901 1.00 46.35  ? 1119 THR A CA  1 
ATOM   5277 C C   . THR A 1 1119 ? 147.060 167.461 142.224 1.00 51.64  ? 1119 THR A C   1 
ATOM   5278 O O   . THR A 1 1119 ? 146.391 166.921 141.335 1.00 64.59  ? 1119 THR A O   1 
ATOM   5279 C CB  . THR A 1 1119 ? 149.548 167.203 142.310 1.00 53.64  ? 1119 THR A CB  1 
ATOM   5280 O OG1 . THR A 1 1119 ? 150.793 167.826 141.974 1.00 64.77  ? 1119 THR A OG1 1 
ATOM   5281 C CG2 . THR A 1 1119 ? 149.450 165.870 141.592 1.00 54.23  ? 1119 THR A CG2 1 
ATOM   5282 N N   . THR A 1 1120 ? 146.676 167.509 143.492 1.00 52.25  ? 1120 THR A N   1 
ATOM   5283 C CA  . THR A 1 1120 ? 145.414 166.919 143.902 1.00 49.47  ? 1120 THR A CA  1 
ATOM   5284 C C   . THR A 1 1120 ? 144.284 167.563 143.142 1.00 51.38  ? 1120 THR A C   1 
ATOM   5285 O O   . THR A 1 1120 ? 143.415 166.878 142.606 1.00 62.19  ? 1120 THR A O   1 
ATOM   5286 C CB  . THR A 1 1120 ? 145.167 167.121 145.399 1.00 48.63  ? 1120 THR A CB  1 
ATOM   5287 O OG1 . THR A 1 1120 ? 146.266 166.582 146.142 1.00 59.81  ? 1120 THR A OG1 1 
ATOM   5288 C CG2 . THR A 1 1120 ? 143.884 166.424 145.820 1.00 52.97  ? 1120 THR A CG2 1 
ATOM   5289 N N   . ALA A 1 1121 ? 144.293 168.886 143.086 1.00 48.79  ? 1121 ALA A N   1 
ATOM   5290 C CA  . ALA A 1 1121 ? 143.230 169.595 142.401 1.00 50.34  ? 1121 ALA A CA  1 
ATOM   5291 C C   . ALA A 1 1121 ? 143.189 169.210 140.942 1.00 52.99  ? 1121 ALA A C   1 
ATOM   5292 O O   . ALA A 1 1121 ? 142.133 168.874 140.410 1.00 55.98  ? 1121 ALA A O   1 
ATOM   5293 C CB  . ALA A 1 1121 ? 143.435 171.085 142.528 1.00 54.46  ? 1121 ALA A CB  1 
ATOM   5294 N N   . LYS A 1 1122 ? 144.340 169.255 140.288 1.00 50.58  ? 1122 LYS A N   1 
ATOM   5295 C CA  . LYS A 1 1122 ? 144.373 168.943 138.875 1.00 51.11  ? 1122 LYS A CA  1 
ATOM   5296 C C   . LYS A 1 1122 ? 143.744 167.582 138.662 1.00 56.51  ? 1122 LYS A C   1 
ATOM   5297 O O   . LYS A 1 1122 ? 142.906 167.410 137.781 1.00 61.89  ? 1122 LYS A O   1 
ATOM   5298 C CB  . LYS A 1 1122 ? 145.799 168.959 138.343 1.00 52.43  ? 1122 LYS A CB  1 
ATOM   5299 C CG  . LYS A 1 1122 ? 145.888 168.878 136.830 1.00 54.01  ? 1122 LYS A CG  1 
ATOM   5300 C CD  . LYS A 1 1122 ? 147.320 169.047 136.357 1.00 57.27  ? 1122 LYS A CD  1 
ATOM   5301 C CE  . LYS A 1 1122 ? 147.396 169.076 134.840 1.00 59.89  ? 1122 LYS A CE  1 
ATOM   5302 N NZ  . LYS A 1 1122 ? 148.795 169.252 134.363 1.00 60.97  ? 1122 LYS A NZ  1 
ATOM   5303 N N   . ILE A 1 1123 ? 144.138 166.612 139.480 1.00 56.74  ? 1123 ILE A N   1 
ATOM   5304 C CA  . ILE A 1 1123 ? 143.575 165.272 139.347 1.00 54.00  ? 1123 ILE A CA  1 
ATOM   5305 C C   . ILE A 1 1123 ? 142.066 165.307 139.543 1.00 55.44  ? 1123 ILE A C   1 
ATOM   5306 O O   . ILE A 1 1123 ? 141.313 164.667 138.801 1.00 57.77  ? 1123 ILE A O   1 
ATOM   5307 C CB  . ILE A 1 1123 ? 144.252 164.308 140.337 1.00 49.42  ? 1123 ILE A CB  1 
ATOM   5308 C CG1 . ILE A 1 1123 ? 145.719 164.106 139.964 1.00 49.55  ? 1123 ILE A CG1 1 
ATOM   5309 C CG2 . ILE A 1 1123 ? 143.528 162.977 140.366 1.00 57.53  ? 1123 ILE A CG2 1 
ATOM   5310 C CD1 . ILE A 1 1123 ? 146.460 163.185 140.904 1.00 55.19  ? 1123 ILE A CD1 1 
ATOM   5311 N N   . LYS A 1 1124 ? 141.609 166.102 140.497 1.00 52.00  ? 1124 LYS A N   1 
ATOM   5312 C CA  . LYS A 1 1124 ? 140.180 166.190 140.758 1.00 55.47  ? 1124 LYS A CA  1 
ATOM   5313 C C   . LYS A 1 1124 ? 139.396 166.812 139.611 1.00 57.43  ? 1124 LYS A C   1 
ATOM   5314 O O   . LYS A 1 1124 ? 138.461 166.201 139.103 1.00 61.70  ? 1124 LYS A O   1 
ATOM   5315 C CB  . LYS A 1 1124 ? 139.926 166.997 142.027 1.00 57.62  ? 1124 LYS A CB  1 
ATOM   5316 C CG  . LYS A 1 1124 ? 138.455 167.198 142.337 1.00 58.30  ? 1124 LYS A CG  1 
ATOM   5317 C CD  . LYS A 1 1124 ? 138.262 168.126 143.523 1.00 57.36  ? 1124 LYS A CD  1 
ATOM   5318 C CE  . LYS A 1 1124 ? 136.790 168.249 143.879 1.00 61.97  ? 1124 LYS A CE  1 
ATOM   5319 N NZ  . LYS A 1 1124 ? 135.975 168.654 142.702 1.00 63.42  ? 1124 LYS A NZ  1 
ATOM   5320 N N   . TYR A 1 1125 ? 139.764 168.016 139.195 1.00 57.12  ? 1125 TYR A N   1 
ATOM   5321 C CA  . TYR A 1 1125 ? 138.984 168.710 138.167 1.00 55.24  ? 1125 TYR A CA  1 
ATOM   5322 C C   . TYR A 1 1125 ? 139.381 168.412 136.720 1.00 55.11  ? 1125 TYR A C   1 
ATOM   5323 O O   . TYR A 1 1125 ? 138.677 168.808 135.796 1.00 59.07  ? 1125 TYR A O   1 
ATOM   5324 C CB  . TYR A 1 1125 ? 139.051 170.219 138.404 1.00 59.06  ? 1125 TYR A CB  1 
ATOM   5325 C CG  . TYR A 1 1125 ? 138.430 170.662 139.705 1.00 58.92  ? 1125 TYR A CG  1 
ATOM   5326 C CD1 . TYR A 1 1125 ? 137.068 170.911 139.794 1.00 60.37  ? 1125 TYR A CD1 1 
ATOM   5327 C CD2 . TYR A 1 1125 ? 139.203 170.837 140.842 1.00 60.28  ? 1125 TYR A CD2 1 
ATOM   5328 C CE1 . TYR A 1 1125 ? 136.494 171.320 140.980 1.00 58.51  ? 1125 TYR A CE1 1 
ATOM   5329 C CE2 . TYR A 1 1125 ? 138.637 171.245 142.033 1.00 61.54  ? 1125 TYR A CE2 1 
ATOM   5330 C CZ  . TYR A 1 1125 ? 137.282 171.484 142.096 1.00 59.61  ? 1125 TYR A CZ  1 
ATOM   5331 O OH  . TYR A 1 1125 ? 136.711 171.890 143.279 1.00 58.81  ? 1125 TYR A OH  1 
ATOM   5332 N N   . PHE A 1 1126 ? 140.500 167.728 136.518 1.00 55.68  ? 1126 PHE A N   1 
ATOM   5333 C CA  . PHE A 1 1126 ? 140.955 167.422 135.165 1.00 54.58  ? 1126 PHE A CA  1 
ATOM   5334 C C   . PHE A 1 1126 ? 141.480 165.997 135.073 1.00 61.89  ? 1126 PHE A C   1 
ATOM   5335 O O   . PHE A 1 1126 ? 142.687 165.786 134.988 1.00 67.62  ? 1126 PHE A O   1 
ATOM   5336 C CB  . PHE A 1 1126 ? 142.037 168.408 134.734 1.00 54.34  ? 1126 PHE A CB  1 
ATOM   5337 C CG  . PHE A 1 1126 ? 141.580 169.838 134.711 1.00 60.45  ? 1126 PHE A CG  1 
ATOM   5338 C CD1 . PHE A 1 1126 ? 141.675 170.627 135.844 1.00 60.62  ? 1126 PHE A CD1 1 
ATOM   5339 C CD2 . PHE A 1 1126 ? 141.062 170.394 133.555 1.00 59.04  ? 1126 PHE A CD2 1 
ATOM   5340 C CE1 . PHE A 1 1126 ? 141.256 171.943 135.826 1.00 57.21  ? 1126 PHE A CE1 1 
ATOM   5341 C CE2 . PHE A 1 1126 ? 140.644 171.710 133.530 1.00 54.36  ? 1126 PHE A CE2 1 
ATOM   5342 C CZ  . PHE A 1 1126 ? 140.740 172.486 134.667 1.00 51.27  ? 1126 PHE A CZ  1 
ATOM   5343 N N   . PRO A 1 1127 ? 140.578 165.009 135.082 1.00 72.67  ? 1127 PRO A N   1 
ATOM   5344 C CA  . PRO A 1 1127 ? 141.002 163.600 135.066 1.00 72.63  ? 1127 PRO A CA  1 
ATOM   5345 C C   . PRO A 1 1127 ? 141.742 163.201 133.804 1.00 76.97  ? 1127 PRO A C   1 
ATOM   5346 O O   . PRO A 1 1127 ? 142.669 162.386 133.873 1.00 77.49  ? 1127 PRO A O   1 
ATOM   5347 C CB  . PRO A 1 1127 ? 139.677 162.834 135.200 1.00 72.03  ? 1127 PRO A CB  1 
ATOM   5348 C CG  . PRO A 1 1127 ? 138.697 163.831 135.722 1.00 74.44  ? 1127 PRO A CG  1 
ATOM   5349 C CD  . PRO A 1 1127 ? 139.115 165.142 135.147 1.00 73.91  ? 1127 PRO A CD  1 
ATOM   5350 N N   . ASP A 1 1128 ? 141.361 163.752 132.651 1.00 85.31  ? 1128 ASP A N   1 
ATOM   5351 C CA  . ASP A 1 1128 ? 141.968 163.332 131.393 1.00 86.69  ? 1128 ASP A CA  1 
ATOM   5352 C C   . ASP A 1 1128 ? 143.401 163.832 131.271 1.00 86.56  ? 1128 ASP A C   1 
ATOM   5353 O O   . ASP A 1 1128 ? 144.305 163.074 130.902 1.00 87.48  ? 1128 ASP A O   1 
ATOM   5354 C CB  . ASP A 1 1128 ? 141.125 163.828 130.220 1.00 85.27  ? 1128 ASP A CB  1 
ATOM   5355 C CG  . ASP A 1 1128 ? 139.689 163.366 130.304 1.00 90.43  ? 1128 ASP A CG  1 
ATOM   5356 O OD1 . ASP A 1 1128 ? 139.354 162.648 131.269 1.00 89.92  ? 1128 ASP A OD1 1 
ATOM   5357 O OD2 . ASP A 1 1128 ? 138.896 163.719 129.407 1.00 92.56  ? 1128 ASP A OD2 1 
ATOM   5358 N N   . PHE A 1 1129 ? 143.629 165.106 131.582 1.00 81.64  ? 1129 PHE A N   1 
ATOM   5359 C CA  . PHE A 1 1129 ? 144.932 165.737 131.385 1.00 78.28  ? 1129 PHE A CA  1 
ATOM   5360 C C   . PHE A 1 1129 ? 145.816 165.466 132.602 1.00 83.41  ? 1129 PHE A C   1 
ATOM   5361 O O   . PHE A 1 1129 ? 146.169 166.356 133.377 1.00 89.22  ? 1129 PHE A O   1 
ATOM   5362 C CB  . PHE A 1 1129 ? 144.761 167.226 131.128 1.00 76.52  ? 1129 PHE A CB  1 
ATOM   5363 C CG  . PHE A 1 1129 ? 143.820 167.538 130.001 1.00 82.15  ? 1129 PHE A CG  1 
ATOM   5364 C CD1 . PHE A 1 1129 ? 142.455 167.615 130.219 1.00 82.81  ? 1129 PHE A CD1 1 
ATOM   5365 C CD2 . PHE A 1 1129 ? 144.298 167.752 128.721 1.00 85.49  ? 1129 PHE A CD2 1 
ATOM   5366 C CE1 . PHE A 1 1129 ? 141.588 167.898 129.185 1.00 84.91  ? 1129 PHE A CE1 1 
ATOM   5367 C CE2 . PHE A 1 1129 ? 143.435 168.037 127.682 1.00 86.28  ? 1129 PHE A CE2 1 
ATOM   5368 C CZ  . PHE A 1 1129 ? 142.078 168.110 127.916 1.00 86.47  ? 1129 PHE A CZ  1 
ATOM   5369 N N   . GLY A 1 1130 ? 146.176 164.198 132.761 1.00 68.87  ? 1130 GLY A N   1 
ATOM   5370 C CA  . GLY A 1 1130 ? 146.970 163.790 133.902 1.00 69.92  ? 1130 GLY A CA  1 
ATOM   5371 C C   . GLY A 1 1130 ? 148.463 163.951 133.707 1.00 75.28  ? 1130 GLY A C   1 
ATOM   5372 O O   . GLY A 1 1130 ? 149.119 164.665 134.470 1.00 80.82  ? 1130 GLY A O   1 
ATOM   5373 N N   . ASP A 1 1131 ? 149.010 163.302 132.683 1.00 72.60  ? 1131 ASP A N   1 
ATOM   5374 C CA  . ASP A 1 1131 ? 150.437 163.332 132.396 1.00 68.38  ? 1131 ASP A CA  1 
ATOM   5375 C C   . ASP A 1 1131 ? 150.642 163.711 130.939 1.00 71.17  ? 1131 ASP A C   1 
ATOM   5376 O O   . ASP A 1 1131 ? 149.887 163.271 130.069 1.00 79.24  ? 1131 ASP A O   1 
ATOM   5377 C CB  . ASP A 1 1131 ? 151.087 161.978 132.689 1.00 71.90  ? 1131 ASP A CB  1 
ATOM   5378 C CG  . ASP A 1 1131 ? 151.135 161.664 134.169 1.00 78.52  ? 1131 ASP A CG  1 
ATOM   5379 O OD1 . ASP A 1 1131 ? 150.930 162.588 134.981 1.00 77.94  ? 1131 ASP A OD1 1 
ATOM   5380 O OD2 . ASP A 1 1131 ? 151.375 160.491 134.521 1.00 78.28  ? 1131 ASP A OD2 1 
ATOM   5381 N N   . PHE A 1 1132 ? 151.656 164.530 130.678 1.00 63.64  ? 1132 PHE A N   1 
ATOM   5382 C CA  . PHE A 1 1132 ? 151.930 165.025 129.331 1.00 59.69  ? 1132 PHE A CA  1 
ATOM   5383 C C   . PHE A 1 1132 ? 153.161 164.308 128.797 1.00 63.46  ? 1132 PHE A C   1 
ATOM   5384 O O   . PHE A 1 1132 ? 154.283 164.805 128.892 1.00 69.69  ? 1132 PHE A O   1 
ATOM   5385 C CB  . PHE A 1 1132 ? 152.117 166.535 129.361 1.00 63.25  ? 1132 PHE A CB  1 
ATOM   5386 C CG  . PHE A 1 1132 ? 152.271 167.158 128.011 1.00 60.18  ? 1132 PHE A CG  1 
ATOM   5387 C CD1 . PHE A 1 1132 ? 151.195 167.248 127.151 1.00 67.23  ? 1132 PHE A CD1 1 
ATOM   5388 C CD2 . PHE A 1 1132 ? 153.485 167.681 127.614 1.00 61.98  ? 1132 PHE A CD2 1 
ATOM   5389 C CE1 . PHE A 1 1132 ? 151.333 167.832 125.914 1.00 68.94  ? 1132 PHE A CE1 1 
ATOM   5390 C CE2 . PHE A 1 1132 ? 153.628 168.266 126.379 1.00 65.81  ? 1132 PHE A CE2 1 
ATOM   5391 C CZ  . PHE A 1 1132 ? 152.550 168.345 125.530 1.00 65.68  ? 1132 PHE A CZ  1 
ATOM   5392 N N   . ILE A 1 1133 ? 152.954 163.123 128.229 1.00 51.32  ? 1133 ILE A N   1 
ATOM   5393 C CA  . ILE A 1 1133 ? 154.064 162.301 127.762 1.00 47.53  ? 1133 ILE A CA  1 
ATOM   5394 C C   . ILE A 1 1133 ? 154.537 162.826 126.414 1.00 49.16  ? 1133 ILE A C   1 
ATOM   5395 O O   . ILE A 1 1133 ? 153.725 163.090 125.518 1.00 56.66  ? 1133 ILE A O   1 
ATOM   5396 C CB  . ILE A 1 1133 ? 153.645 160.829 127.664 1.00 41.78  ? 1133 ILE A CB  1 
ATOM   5397 C CG1 . ILE A 1 1133 ? 152.888 160.404 128.920 1.00 46.15  ? 1133 ILE A CG1 1 
ATOM   5398 C CG2 . ILE A 1 1133 ? 154.859 159.950 127.455 1.00 53.69  ? 1133 ILE A CG2 1 
ATOM   5399 C CD1 . ILE A 1 1133 ? 153.706 160.477 130.179 1.00 54.12  ? 1133 ILE A CD1 1 
ATOM   5400 N N   . GLU A 1 1134 ? 155.851 162.979 126.264 1.00 50.42  ? 1134 GLU A N   1 
ATOM   5401 C CA  . GLU A 1 1134 ? 156.439 163.518 125.047 1.00 47.35  ? 1134 GLU A CA  1 
ATOM   5402 C C   . GLU A 1 1134 ? 157.290 162.446 124.385 1.00 56.54  ? 1134 GLU A C   1 
ATOM   5403 O O   . GLU A 1 1134 ? 158.180 161.878 125.020 1.00 67.86  ? 1134 GLU A O   1 
ATOM   5404 C CB  . GLU A 1 1134 ? 157.289 164.746 125.362 1.00 48.91  ? 1134 GLU A CB  1 
ATOM   5405 C CG  . GLU A 1 1134 ? 156.822 165.518 126.577 1.00 61.95  ? 1134 GLU A CG  1 
ATOM   5406 C CD  . GLU A 1 1134 ? 157.912 166.389 127.165 1.00 63.75  ? 1134 GLU A CD  1 
ATOM   5407 O OE1 . GLU A 1 1134 ? 159.006 166.455 126.568 1.00 58.90  ? 1134 GLU A OE1 1 
ATOM   5408 O OE2 . GLU A 1 1134 ? 157.676 167.003 128.226 1.00 59.10  ? 1134 GLU A OE2 1 
ATOM   5409 N N   . VAL A 1 1135 ? 157.029 162.176 123.111 1.00 39.86  ? 1135 VAL A N   1 
ATOM   5410 C CA  . VAL A 1 1135 ? 157.717 161.127 122.372 1.00 33.13  ? 1135 VAL A CA  1 
ATOM   5411 C C   . VAL A 1 1135 ? 158.614 161.793 121.341 1.00 47.48  ? 1135 VAL A C   1 
ATOM   5412 O O   . VAL A 1 1135 ? 158.154 162.632 120.558 1.00 56.16  ? 1135 VAL A O   1 
ATOM   5413 C CB  . VAL A 1 1135 ? 156.721 160.166 121.710 1.00 41.90  ? 1135 VAL A CB  1 
ATOM   5414 C CG1 . VAL A 1 1135 ? 157.448 159.009 121.085 1.00 42.38  ? 1135 VAL A CG1 1 
ATOM   5415 C CG2 . VAL A 1 1135 ? 155.713 159.674 122.730 1.00 41.16  ? 1135 VAL A CG2 1 
ATOM   5416 N N   . TYR A 1 1136 ? 159.893 161.423 121.341 1.00 48.35  ? 1136 TYR A N   1 
ATOM   5417 C CA  . TYR A 1 1136 ? 160.907 162.046 120.503 1.00 36.12  ? 1136 TYR A CA  1 
ATOM   5418 C C   . TYR A 1 1136 ? 161.576 161.008 119.616 1.00 38.12  ? 1136 TYR A C   1 
ATOM   5419 O O   . TYR A 1 1136 ? 161.703 159.843 119.997 1.00 54.44  ? 1136 TYR A O   1 
ATOM   5420 C CB  . TYR A 1 1136 ? 161.982 162.730 121.346 1.00 28.75  ? 1136 TYR A CB  1 
ATOM   5421 C CG  . TYR A 1 1136 ? 161.487 163.844 122.226 1.00 36.53  ? 1136 TYR A CG  1 
ATOM   5422 C CD1 . TYR A 1 1136 ? 160.946 163.580 123.470 1.00 38.43  ? 1136 TYR A CD1 1 
ATOM   5423 C CD2 . TYR A 1 1136 ? 161.573 165.163 121.818 1.00 35.95  ? 1136 TYR A CD2 1 
ATOM   5424 C CE1 . TYR A 1 1136 ? 160.499 164.595 124.278 1.00 44.48  ? 1136 TYR A CE1 1 
ATOM   5425 C CE2 . TYR A 1 1136 ? 161.128 166.185 122.620 1.00 36.67  ? 1136 TYR A CE2 1 
ATOM   5426 C CZ  . TYR A 1 1136 ? 160.590 165.896 123.849 1.00 48.75  ? 1136 TYR A CZ  1 
ATOM   5427 O OH  . TYR A 1 1136 ? 160.142 166.915 124.654 1.00 54.15  ? 1136 TYR A OH  1 
ATOM   5428 N N   . TYR A 1 1137 ? 162.005 161.439 118.437 1.00 35.60  ? 1137 TYR A N   1 
ATOM   5429 C CA  . TYR A 1 1137 ? 162.888 160.664 117.579 1.00 33.05  ? 1137 TYR A CA  1 
ATOM   5430 C C   . TYR A 1 1137 ? 164.098 161.513 117.227 1.00 52.47  ? 1137 TYR A C   1 
ATOM   5431 O O   . TYR A 1 1137 ? 163.946 162.650 116.764 1.00 65.93  ? 1137 TYR A O   1 
ATOM   5432 C CB  . TYR A 1 1137 ? 162.182 160.218 116.301 1.00 39.33  ? 1137 TYR A CB  1 
ATOM   5433 C CG  . TYR A 1 1137 ? 163.145 159.808 115.213 1.00 44.54  ? 1137 TYR A CG  1 
ATOM   5434 C CD1 . TYR A 1 1137 ? 163.707 158.544 115.200 1.00 52.44  ? 1137 TYR A CD1 1 
ATOM   5435 C CD2 . TYR A 1 1137 ? 163.496 160.689 114.204 1.00 43.53  ? 1137 TYR A CD2 1 
ATOM   5436 C CE1 . TYR A 1 1137 ? 164.589 158.168 114.211 1.00 53.97  ? 1137 TYR A CE1 1 
ATOM   5437 C CE2 . TYR A 1 1137 ? 164.377 160.325 113.215 1.00 46.22  ? 1137 TYR A CE2 1 
ATOM   5438 C CZ  . TYR A 1 1137 ? 164.919 159.063 113.221 1.00 53.12  ? 1137 TYR A CZ  1 
ATOM   5439 O OH  . TYR A 1 1137 ? 165.798 158.697 112.230 1.00 62.21  ? 1137 TYR A OH  1 
ATOM   5440 N N   . PHE A 1 1138 ? 165.289 160.951 117.431 1.00 52.34  ? 1138 PHE A N   1 
ATOM   5441 C CA  . PHE A 1 1138 ? 166.554 161.603 117.122 1.00 39.92  ? 1138 PHE A CA  1 
ATOM   5442 C C   . PHE A 1 1138 ? 167.370 160.713 116.198 1.00 43.49  ? 1138 PHE A C   1 
ATOM   5443 O O   . PHE A 1 1138 ? 167.500 159.511 116.446 1.00 54.05  ? 1138 PHE A O   1 
ATOM   5444 C CB  . PHE A 1 1138 ? 167.363 161.885 118.389 1.00 39.78  ? 1138 PHE A CB  1 
ATOM   5445 C CG  . PHE A 1 1138 ? 166.635 162.695 119.413 1.00 37.43  ? 1138 PHE A CG  1 
ATOM   5446 C CD1 . PHE A 1 1138 ? 166.504 164.059 119.265 1.00 43.94  ? 1138 PHE A CD1 1 
ATOM   5447 C CD2 . PHE A 1 1138 ? 166.108 162.095 120.538 1.00 41.33  ? 1138 PHE A CD2 1 
ATOM   5448 C CE1 . PHE A 1 1138 ? 165.846 164.806 120.210 1.00 44.18  ? 1138 PHE A CE1 1 
ATOM   5449 C CE2 . PHE A 1 1138 ? 165.451 162.838 121.486 1.00 44.72  ? 1138 PHE A CE2 1 
ATOM   5450 C CZ  . PHE A 1 1138 ? 165.318 164.195 121.320 1.00 49.63  ? 1138 PHE A CZ  1 
ATOM   5451 N N   . ASP A 1 1139 ? 167.928 161.302 115.145 1.00 57.53  ? 1139 ASP A N   1 
ATOM   5452 C CA  . ASP A 1 1139 ? 168.842 160.574 114.277 1.00 52.59  ? 1139 ASP A CA  1 
ATOM   5453 C C   . ASP A 1 1139 ? 170.196 160.446 114.960 1.00 62.61  ? 1139 ASP A C   1 
ATOM   5454 O O   . ASP A 1 1139 ? 170.775 161.443 115.400 1.00 75.96  ? 1139 ASP A O   1 
ATOM   5455 C CB  . ASP A 1 1139 ? 168.980 161.294 112.937 1.00 60.37  ? 1139 ASP A CB  1 
ATOM   5456 C CG  . ASP A 1 1139 ? 169.883 160.564 111.963 1.00 67.41  ? 1139 ASP A CG  1 
ATOM   5457 O OD1 . ASP A 1 1139 ? 171.097 160.450 112.231 1.00 69.89  ? 1139 ASP A OD1 1 
ATOM   5458 O OD2 . ASP A 1 1139 ? 169.376 160.108 110.918 1.00 70.09  ? 1139 ASP A OD2 1 
ATOM   5459 N N   . LYS A 1 1140 ? 170.707 159.217 115.043 1.00 62.88  ? 1140 LYS A N   1 
ATOM   5460 C CA  . LYS A 1 1140 ? 171.957 158.987 115.762 1.00 66.89  ? 1140 LYS A CA  1 
ATOM   5461 C C   . LYS A 1 1140 ? 173.119 159.724 115.114 1.00 64.50  ? 1140 LYS A C   1 
ATOM   5462 O O   . LYS A 1 1140 ? 173.969 160.287 115.811 1.00 65.34  ? 1140 LYS A O   1 
ATOM   5463 C CB  . LYS A 1 1140 ? 172.258 157.494 115.841 1.00 66.17  ? 1140 LYS A CB  1 
ATOM   5464 C CG  . LYS A 1 1140 ? 171.504 156.769 116.931 1.00 66.11  ? 1140 LYS A CG  1 
ATOM   5465 C CD  . LYS A 1 1140 ? 172.068 155.377 117.138 1.00 71.59  ? 1140 LYS A CD  1 
ATOM   5466 C CE  . LYS A 1 1140 ? 171.336 154.651 118.247 1.00 73.35  ? 1140 LYS A CE  1 
ATOM   5467 N NZ  . LYS A 1 1140 ? 171.353 155.424 119.519 1.00 72.66  ? 1140 LYS A NZ  1 
ATOM   5468 N N   . HIS A 1 1141 ? 173.186 159.718 113.783 1.00 63.62  ? 1141 HIS A N   1 
ATOM   5469 C CA  . HIS A 1 1141 ? 174.288 160.389 113.102 1.00 64.16  ? 1141 HIS A CA  1 
ATOM   5470 C C   . HIS A 1 1141 ? 174.265 161.887 113.367 1.00 69.78  ? 1141 HIS A C   1 
ATOM   5471 O O   . HIS A 1 1141 ? 175.302 162.491 113.657 1.00 75.41  ? 1141 HIS A O   1 
ATOM   5472 C CB  . HIS A 1 1141 ? 174.230 160.101 111.605 1.00 64.85  ? 1141 HIS A CB  1 
ATOM   5473 C CG  . HIS A 1 1141 ? 174.603 158.698 111.251 1.00 70.68  ? 1141 HIS A CG  1 
ATOM   5474 N ND1 . HIS A 1 1141 ? 175.158 157.826 112.161 1.00 66.86  ? 1141 HIS A ND1 1 
ATOM   5475 C CD2 . HIS A 1 1141 ? 174.502 158.013 110.087 1.00 77.50  ? 1141 HIS A CD2 1 
ATOM   5476 C CE1 . HIS A 1 1141 ? 175.383 156.665 111.574 1.00 71.73  ? 1141 HIS A CE1 1 
ATOM   5477 N NE2 . HIS A 1 1141 ? 174.993 156.752 110.316 1.00 75.84  ? 1141 HIS A NE2 1 
ATOM   5478 N N   . PHE A 1 1142 ? 173.085 162.502 113.283 1.00 58.02  ? 1142 PHE A N   1 
ATOM   5479 C CA  . PHE A 1 1142 ? 172.970 163.934 113.545 1.00 49.36  ? 1142 PHE A CA  1 
ATOM   5480 C C   . PHE A 1 1142 ? 173.333 164.265 114.986 1.00 47.15  ? 1142 PHE A C   1 
ATOM   5481 O O   . PHE A 1 1142 ? 174.072 165.225 115.245 1.00 60.23  ? 1142 PHE A O   1 
ATOM   5482 C CB  . PHE A 1 1142 ? 171.551 164.398 113.219 1.00 53.90  ? 1142 PHE A CB  1 
ATOM   5483 C CG  . PHE A 1 1142 ? 171.155 165.682 113.884 1.00 49.56  ? 1142 PHE A CG  1 
ATOM   5484 C CD1 . PHE A 1 1142 ? 171.622 166.893 113.418 1.00 43.09  ? 1142 PHE A CD1 1 
ATOM   5485 C CD2 . PHE A 1 1142 ? 170.286 165.677 114.958 1.00 52.85  ? 1142 PHE A CD2 1 
ATOM   5486 C CE1 . PHE A 1 1142 ? 171.245 168.070 114.021 1.00 40.05  ? 1142 PHE A CE1 1 
ATOM   5487 C CE2 . PHE A 1 1142 ? 169.908 166.852 115.563 1.00 48.62  ? 1142 PHE A CE2 1 
ATOM   5488 C CZ  . PHE A 1 1142 ? 170.388 168.048 115.094 1.00 40.59  ? 1142 PHE A CZ  1 
ATOM   5489 N N   . ILE A 1 1143 ? 172.831 163.475 115.936 1.00 46.51  ? 1143 ILE A N   1 
ATOM   5490 C CA  . ILE A 1 1143 ? 173.121 163.724 117.344 1.00 44.98  ? 1143 ILE A CA  1 
ATOM   5491 C C   . ILE A 1 1143 ? 174.615 163.604 117.606 1.00 54.78  ? 1143 ILE A C   1 
ATOM   5492 O O   . ILE A 1 1143 ? 175.217 164.461 118.256 1.00 61.35  ? 1143 ILE A O   1 
ATOM   5493 C CB  . ILE A 1 1143 ? 172.314 162.766 118.237 1.00 49.24  ? 1143 ILE A CB  1 
ATOM   5494 C CG1 . ILE A 1 1143 ? 170.821 163.057 118.117 1.00 48.89  ? 1143 ILE A CG1 1 
ATOM   5495 C CG2 . ILE A 1 1143 ? 172.760 162.881 119.680 1.00 47.86  ? 1143 ILE A CG2 1 
ATOM   5496 C CD1 . ILE A 1 1143 ? 170.451 164.473 118.449 1.00 48.46  ? 1143 ILE A CD1 1 
ATOM   5497 N N   . ASN A 1 1144 ? 175.239 162.542 117.093 1.00 65.28  ? 1144 ASN A N   1 
ATOM   5498 C CA  . ASN A 1 1144 ? 176.669 162.355 117.310 1.00 61.45  ? 1144 ASN A CA  1 
ATOM   5499 C C   . ASN A 1 1144 ? 177.479 163.456 116.640 1.00 58.53  ? 1144 ASN A C   1 
ATOM   5500 O O   . ASN A 1 1144 ? 178.483 163.920 117.191 1.00 62.17  ? 1144 ASN A O   1 
ATOM   5501 C CB  . ASN A 1 1144 ? 177.103 160.982 116.803 1.00 57.56  ? 1144 ASN A CB  1 
ATOM   5502 C CG  . ASN A 1 1144 ? 176.557 159.854 117.650 1.00 62.70  ? 1144 ASN A CG  1 
ATOM   5503 O OD1 . ASN A 1 1144 ? 176.327 160.018 118.847 1.00 64.05  ? 1144 ASN A OD1 1 
ATOM   5504 N ND2 . ASN A 1 1144 ? 176.347 158.699 117.033 1.00 64.42  ? 1144 ASN A ND2 1 
ATOM   5505 N N   . LYS A 1 1145 ? 177.063 163.883 115.447 1.00 56.79  ? 1145 LYS A N   1 
ATOM   5506 C CA  . LYS A 1 1145 ? 177.780 164.943 114.751 1.00 58.67  ? 1145 LYS A CA  1 
ATOM   5507 C C   . LYS A 1 1145 ? 177.730 166.246 115.531 1.00 65.09  ? 1145 LYS A C   1 
ATOM   5508 O O   . LYS A 1 1145 ? 178.741 166.949 115.642 1.00 70.13  ? 1145 LYS A O   1 
ATOM   5509 C CB  . LYS A 1 1145 ? 177.200 165.134 113.351 1.00 58.06  ? 1145 LYS A CB  1 
ATOM   5510 C CG  . LYS A 1 1145 ? 177.807 166.289 112.575 1.00 58.04  ? 1145 LYS A CG  1 
ATOM   5511 C CD  . LYS A 1 1145 ? 177.157 166.435 111.210 1.00 62.37  ? 1145 LYS A CD  1 
ATOM   5512 C CE  . LYS A 1 1145 ? 177.760 167.589 110.433 1.00 61.76  ? 1145 LYS A CE  1 
ATOM   5513 N NZ  . LYS A 1 1145 ? 177.112 167.765 109.107 1.00 58.28  ? 1145 LYS A NZ  1 
ATOM   5514 N N   . TYR A 1 1146 ? 176.567 166.588 116.084 1.00 58.73  ? 1146 TYR A N   1 
ATOM   5515 C CA  . TYR A 1 1146 ? 176.459 167.868 116.772 1.00 49.53  ? 1146 TYR A CA  1 
ATOM   5516 C C   . TYR A 1 1146 ? 176.850 167.805 118.243 1.00 52.27  ? 1146 TYR A C   1 
ATOM   5517 O O   . TYR A 1 1146 ? 177.011 168.860 118.863 1.00 64.63  ? 1146 TYR A O   1 
ATOM   5518 C CB  . TYR A 1 1146 ? 175.046 168.427 116.621 1.00 37.07  ? 1146 TYR A CB  1 
ATOM   5519 C CG  . TYR A 1 1146 ? 174.927 169.343 115.430 1.00 49.16  ? 1146 TYR A CG  1 
ATOM   5520 C CD1 . TYR A 1 1146 ? 175.170 168.876 114.150 1.00 50.76  ? 1146 TYR A CD1 1 
ATOM   5521 C CD2 . TYR A 1 1146 ? 174.592 170.678 115.585 1.00 52.84  ? 1146 TYR A CD2 1 
ATOM   5522 C CE1 . TYR A 1 1146 ? 175.074 169.707 113.058 1.00 45.95  ? 1146 TYR A CE1 1 
ATOM   5523 C CE2 . TYR A 1 1146 ? 174.492 171.517 114.497 1.00 50.88  ? 1146 TYR A CE2 1 
ATOM   5524 C CZ  . TYR A 1 1146 ? 174.735 171.025 113.237 1.00 48.42  ? 1146 TYR A CZ  1 
ATOM   5525 O OH  . TYR A 1 1146 ? 174.638 171.855 112.147 1.00 52.15  ? 1146 TYR A OH  1 
ATOM   5526 N N   . ARG A 1 1147 ? 177.020 166.614 118.816 1.00 59.03  ? 1147 ARG A N   1 
ATOM   5527 C CA  . ARG A 1 1147 ? 177.534 166.513 120.175 1.00 60.65  ? 1147 ARG A CA  1 
ATOM   5528 C C   . ARG A 1 1147 ? 179.032 166.761 120.248 1.00 68.91  ? 1147 ARG A C   1 
ATOM   5529 O O   . ARG A 1 1147 ? 179.526 167.178 121.300 1.00 69.91  ? 1147 ARG A O   1 
ATOM   5530 C CB  . ARG A 1 1147 ? 177.228 165.136 120.766 1.00 59.49  ? 1147 ARG A CB  1 
ATOM   5531 C CG  . ARG A 1 1147 ? 175.789 164.920 121.194 1.00 63.70  ? 1147 ARG A CG  1 
ATOM   5532 C CD  . ARG A 1 1147 ? 175.483 165.562 122.529 1.00 65.13  ? 1147 ARG A CD  1 
ATOM   5533 N NE  . ARG A 1 1147 ? 174.281 164.986 123.120 1.00 64.68  ? 1147 ARG A NE  1 
ATOM   5534 C CZ  . ARG A 1 1147 ? 173.790 165.322 124.304 1.00 68.84  ? 1147 ARG A CZ  1 
ATOM   5535 N NH1 . ARG A 1 1147 ? 174.366 166.245 125.055 1.00 71.88  ? 1147 ARG A NH1 1 
ATOM   5536 N NH2 . ARG A 1 1147 ? 172.693 164.715 124.747 1.00 68.96  ? 1147 ARG A NH2 1 
ATOM   5537 N N   . GLY A 1 1148 ? 179.760 166.516 119.157 1.00 74.83  ? 1148 GLY A N   1 
ATOM   5538 C CA  . GLY A 1 1148 ? 181.202 166.682 119.183 1.00 72.45  ? 1148 GLY A CA  1 
ATOM   5539 C C   . GLY A 1 1148 ? 181.635 168.114 119.404 1.00 74.69  ? 1148 GLY A C   1 
ATOM   5540 O O   . GLY A 1 1148 ? 182.741 168.362 119.890 1.00 78.84  ? 1148 GLY A O   1 
ATOM   5541 N N   . LEU A 1 1149 ? 180.779 169.074 119.053 1.00 71.63  ? 1149 LEU A N   1 
ATOM   5542 C CA  . LEU A 1 1149 ? 181.112 170.476 119.265 1.00 69.68  ? 1149 LEU A CA  1 
ATOM   5543 C C   . LEU A 1 1149 ? 181.266 170.801 120.744 1.00 72.82  ? 1149 LEU A C   1 
ATOM   5544 O O   . LEU A 1 1149 ? 182.102 171.634 121.111 1.00 73.13  ? 1149 LEU A O   1 
ATOM   5545 C CB  . LEU A 1 1149 ? 180.038 171.361 118.637 1.00 67.57  ? 1149 LEU A CB  1 
ATOM   5546 C CG  . LEU A 1 1149 ? 179.751 171.081 117.165 1.00 67.54  ? 1149 LEU A CG  1 
ATOM   5547 C CD1 . LEU A 1 1149 ? 178.529 171.847 116.717 1.00 65.77  ? 1149 LEU A CD1 1 
ATOM   5548 C CD2 . LEU A 1 1149 ? 180.952 171.449 116.319 1.00 74.15  ? 1149 LEU A CD2 1 
ATOM   5549 N N   . GLU A 1 1150 ? 180.473 170.159 121.603 1.00 80.57  ? 1150 GLU A N   1 
ATOM   5550 C CA  . GLU A 1 1150 ? 180.532 170.455 123.031 1.00 80.71  ? 1150 GLU A CA  1 
ATOM   5551 C C   . GLU A 1 1150 ? 181.878 170.064 123.627 1.00 82.77  ? 1150 GLU A C   1 
ATOM   5552 O O   . GLU A 1 1150 ? 182.403 170.766 124.499 1.00 82.98  ? 1150 GLU A O   1 
ATOM   5553 C CB  . GLU A 1 1150 ? 179.396 169.739 123.760 1.00 81.55  ? 1150 GLU A CB  1 
ATOM   5554 C CG  . GLU A 1 1150 ? 178.011 170.140 123.285 1.00 81.61  ? 1150 GLU A CG  1 
ATOM   5555 C CD  . GLU A 1 1150 ? 176.910 169.359 123.973 1.00 83.77  ? 1150 GLU A CD  1 
ATOM   5556 O OE1 . GLU A 1 1150 ? 177.231 168.443 124.760 1.00 83.18  ? 1150 GLU A OE1 1 
ATOM   5557 O OE2 . GLU A 1 1150 ? 175.723 169.660 123.727 1.00 83.13  ? 1150 GLU A OE2 1 
ATOM   5558 N N   . LYS A 1 1151 ? 182.441 168.945 123.179 1.00 84.67  ? 1151 LYS A N   1 
ATOM   5559 C CA  . LYS A 1 1151 ? 183.720 168.439 123.677 1.00 84.40  ? 1151 LYS A CA  1 
ATOM   5560 C C   . LYS A 1 1151 ? 183.676 168.197 125.183 1.00 81.67  ? 1151 LYS A C   1 
ATOM   5561 O O   . LYS A 1 1151 ? 184.659 168.425 125.887 1.00 83.72  ? 1151 LYS A O   1 
ATOM   5562 C CB  . LYS A 1 1151 ? 184.858 169.406 123.333 1.00 83.61  ? 1151 LYS A CB  1 
ATOM   5563 C CG  . LYS A 1 1151 ? 184.969 169.735 121.854 1.00 81.27  ? 1151 LYS A CG  1 
ATOM   5564 C CD  . LYS A 1 1151 ? 186.044 170.779 121.599 1.00 80.28  ? 1151 LYS A CD  1 
ATOM   5565 C CE  . LYS A 1 1151 ? 186.111 171.152 120.128 1.00 81.53  ? 1151 LYS A CE  1 
ATOM   5566 N NZ  . LYS A 1 1151 ? 187.104 172.230 119.875 1.00 81.72  ? 1151 LYS A NZ  1 
ATOM   5567 N N   . LEU A 1 1161 ? 179.427 147.930 140.234 1.00 80.80  ? 1161 LEU A N   1 
ATOM   5568 C CA  . LEU A 1 1161 ? 178.837 146.875 141.051 1.00 82.25  ? 1161 LEU A CA  1 
ATOM   5569 C C   . LEU A 1 1161 ? 177.424 146.544 140.589 1.00 85.40  ? 1161 LEU A C   1 
ATOM   5570 O O   . LEU A 1 1161 ? 177.043 145.376 140.521 1.00 82.51  ? 1161 LEU A O   1 
ATOM   5571 C CB  . LEU A 1 1161 ? 178.823 147.282 142.524 1.00 78.82  ? 1161 LEU A CB  1 
ATOM   5572 C CG  . LEU A 1 1161 ? 178.156 146.295 143.482 1.00 77.38  ? 1161 LEU A CG  1 
ATOM   5573 C CD1 . LEU A 1 1161 ? 178.808 144.928 143.377 1.00 78.35  ? 1161 LEU A CD1 1 
ATOM   5574 C CD2 . LEU A 1 1161 ? 178.217 146.809 144.908 1.00 76.06  ? 1161 LEU A CD2 1 
ATOM   5575 N N   . TYR A 1 1162 ? 176.649 147.576 140.273 1.00 88.02  ? 1162 TYR A N   1 
ATOM   5576 C CA  . TYR A 1 1162 ? 175.269 147.418 139.834 1.00 83.51  ? 1162 TYR A CA  1 
ATOM   5577 C C   . TYR A 1 1162 ? 175.222 147.486 138.313 1.00 86.46  ? 1162 TYR A C   1 
ATOM   5578 O O   . TYR A 1 1162 ? 175.631 148.490 137.720 1.00 86.66  ? 1162 TYR A O   1 
ATOM   5579 C CB  . TYR A 1 1162 ? 174.374 148.492 140.450 1.00 80.87  ? 1162 TYR A CB  1 
ATOM   5580 C CG  . TYR A 1 1162 ? 174.409 148.522 141.960 1.00 82.83  ? 1162 TYR A CG  1 
ATOM   5581 C CD1 . TYR A 1 1162 ? 173.628 147.655 142.708 1.00 83.98  ? 1162 TYR A CD1 1 
ATOM   5582 C CD2 . TYR A 1 1162 ? 175.220 149.420 142.636 1.00 79.83  ? 1162 TYR A CD2 1 
ATOM   5583 C CE1 . TYR A 1 1162 ? 173.655 147.679 144.086 1.00 80.60  ? 1162 TYR A CE1 1 
ATOM   5584 C CE2 . TYR A 1 1162 ? 175.253 149.451 144.013 1.00 80.43  ? 1162 TYR A CE2 1 
ATOM   5585 C CZ  . TYR A 1 1162 ? 174.469 148.580 144.733 1.00 80.63  ? 1162 TYR A CZ  1 
ATOM   5586 O OH  . TYR A 1 1162 ? 174.502 148.609 146.107 1.00 80.84  ? 1162 TYR A OH  1 
ATOM   5587 N N   . SER A 1 1163 ? 174.723 146.422 137.688 1.00 109.75 ? 1163 SER A N   1 
ATOM   5588 C CA  . SER A 1 1163 ? 174.676 146.314 136.238 1.00 110.71 ? 1163 SER A CA  1 
ATOM   5589 C C   . SER A 1 1163 ? 173.296 146.615 135.668 1.00 113.79 ? 1163 SER A C   1 
ATOM   5590 O O   . SER A 1 1163 ? 173.044 146.325 134.495 1.00 113.79 ? 1163 SER A O   1 
ATOM   5591 C CB  . SER A 1 1163 ? 175.128 144.920 135.800 1.00 111.20 ? 1163 SER A CB  1 
ATOM   5592 O OG  . SER A 1 1163 ? 174.332 143.915 136.403 1.00 114.15 ? 1163 SER A OG  1 
ATOM   5593 N N   . ASP A 1 1164 ? 172.398 147.193 136.467 1.00 114.19 ? 1164 ASP A N   1 
ATOM   5594 C CA  . ASP A 1 1164 ? 171.034 147.484 136.025 1.00 112.30 ? 1164 ASP A CA  1 
ATOM   5595 C C   . ASP A 1 1164 ? 171.022 148.759 135.179 1.00 111.18 ? 1164 ASP A C   1 
ATOM   5596 O O   . ASP A 1 1164 ? 170.363 149.754 135.484 1.00 110.78 ? 1164 ASP A O   1 
ATOM   5597 C CB  . ASP A 1 1164 ? 170.101 147.595 137.223 1.00 112.08 ? 1164 ASP A CB  1 
ATOM   5598 C CG  . ASP A 1 1164 ? 170.681 148.444 138.338 1.00 111.06 ? 1164 ASP A CG  1 
ATOM   5599 O OD1 . ASP A 1 1164 ? 170.650 149.687 138.226 1.00 111.05 ? 1164 ASP A OD1 1 
ATOM   5600 O OD2 . ASP A 1 1164 ? 171.170 147.865 139.330 1.00 109.31 ? 1164 ASP A OD2 1 
ATOM   5601 N N   . LEU A 1 1165 ? 171.769 148.707 134.078 1.00 121.94 ? 1165 LEU A N   1 
ATOM   5602 C CA  . LEU A 1 1165 ? 171.818 149.814 133.122 1.00 123.56 ? 1165 LEU A CA  1 
ATOM   5603 C C   . LEU A 1 1165 ? 170.654 149.704 132.136 1.00 125.82 ? 1165 LEU A C   1 
ATOM   5604 O O   . LEU A 1 1165 ? 170.823 149.508 130.933 1.00 124.14 ? 1165 LEU A O   1 
ATOM   5605 C CB  . LEU A 1 1165 ? 173.162 149.837 132.402 1.00 121.85 ? 1165 LEU A CB  1 
ATOM   5606 C CG  . LEU A 1 1165 ? 174.371 150.416 133.145 1.00 123.91 ? 1165 LEU A CG  1 
ATOM   5607 C CD1 . LEU A 1 1165 ? 174.869 149.484 134.243 1.00 120.30 ? 1165 LEU A CD1 1 
ATOM   5608 C CD2 . LEU A 1 1165 ? 175.492 150.746 132.169 1.00 123.20 ? 1165 LEU A CD2 1 
ATOM   5609 N N   . THR A 1 1166 ? 169.450 149.838 132.682 1.00 124.64 ? 1166 THR A N   1 
ATOM   5610 C CA  . THR A 1 1166 ? 168.233 149.633 131.913 1.00 124.28 ? 1166 THR A CA  1 
ATOM   5611 C C   . THR A 1 1166 ? 167.971 150.802 130.972 1.00 123.62 ? 1166 THR A C   1 
ATOM   5612 O O   . THR A 1 1166 ? 168.422 151.928 131.201 1.00 120.03 ? 1166 THR A O   1 
ATOM   5613 C CB  . THR A 1 1166 ? 167.038 149.443 132.846 1.00 124.51 ? 1166 THR A CB  1 
ATOM   5614 O OG1 . THR A 1 1166 ? 166.870 150.616 133.652 1.00 124.32 ? 1166 THR A OG1 1 
ATOM   5615 C CG2 . THR A 1 1166 ? 167.260 148.242 133.753 1.00 120.70 ? 1166 THR A CG2 1 
ATOM   5616 N N   . ASP A 1 1167 ? 167.239 150.514 129.895 1.00 118.46 ? 1167 ASP A N   1 
ATOM   5617 C CA  . ASP A 1 1167 ? 166.796 151.476 128.888 1.00 118.02 ? 1167 ASP A CA  1 
ATOM   5618 C C   . ASP A 1 1167 ? 167.948 152.144 128.151 1.00 116.43 ? 1167 ASP A C   1 
ATOM   5619 O O   . ASP A 1 1167 ? 167.730 153.147 127.460 1.00 115.40 ? 1167 ASP A O   1 
ATOM   5620 C CB  . ASP A 1 1167 ? 165.889 152.553 129.491 1.00 117.94 ? 1167 ASP A CB  1 
ATOM   5621 C CG  . ASP A 1 1167 ? 164.598 151.984 130.043 1.00 118.06 ? 1167 ASP A CG  1 
ATOM   5622 O OD1 . ASP A 1 1167 ? 164.451 150.744 130.051 1.00 115.97 ? 1167 ASP A OD1 1 
ATOM   5623 O OD2 . ASP A 1 1167 ? 163.730 152.775 130.465 1.00 118.95 ? 1167 ASP A OD2 1 
ATOM   5624 N N   . ARG A 1 1168 ? 169.165 151.622 128.270 1.00 106.85 ? 1168 ARG A N   1 
ATOM   5625 C CA  . ARG A 1 1168 ? 170.323 152.171 127.579 1.00 106.52 ? 1168 ARG A CA  1 
ATOM   5626 C C   . ARG A 1 1168 ? 170.857 151.237 126.506 1.00 106.88 ? 1168 ARG A C   1 
ATOM   5627 O O   . ARG A 1 1168 ? 171.170 151.682 125.398 1.00 108.60 ? 1168 ARG A O   1 
ATOM   5628 C CB  . ARG A 1 1168 ? 171.433 152.492 128.589 1.00 105.25 ? 1168 ARG A CB  1 
ATOM   5629 C CG  . ARG A 1 1168 ? 172.676 153.102 127.968 1.00 106.03 ? 1168 ARG A CG  1 
ATOM   5630 C CD  . ARG A 1 1168 ? 173.714 153.425 129.025 1.00 105.09 ? 1168 ARG A CD  1 
ATOM   5631 N NE  . ARG A 1 1168 ? 173.167 154.272 130.077 1.00 105.03 ? 1168 ARG A NE  1 
ATOM   5632 C CZ  . ARG A 1 1168 ? 173.065 155.592 129.998 1.00 107.86 ? 1168 ARG A CZ  1 
ATOM   5633 N NH1 . ARG A 1 1168 ? 173.459 156.252 128.921 1.00 109.07 ? 1168 ARG A NH1 1 
ATOM   5634 N NH2 . ARG A 1 1168 ? 172.555 156.266 131.025 1.00 107.54 ? 1168 ARG A NH2 1 
ATOM   5635 N N   . GLN A 1 1169 ? 170.969 149.943 126.812 1.00 112.77 ? 1169 GLN A N   1 
ATOM   5636 C CA  . GLN A 1 1169 ? 171.492 148.991 125.838 1.00 112.54 ? 1169 GLN A CA  1 
ATOM   5637 C C   . GLN A 1 1169 ? 170.575 148.860 124.630 1.00 112.21 ? 1169 GLN A C   1 
ATOM   5638 O O   . GLN A 1 1169 ? 171.056 148.703 123.502 1.00 110.57 ? 1169 GLN A O   1 
ATOM   5639 C CB  . GLN A 1 1169 ? 171.699 147.629 126.500 1.00 114.14 ? 1169 GLN A CB  1 
ATOM   5640 C CG  . GLN A 1 1169 ? 172.599 147.669 127.725 1.00 112.90 ? 1169 GLN A CG  1 
ATOM   5641 C CD  . GLN A 1 1169 ? 172.710 146.323 128.415 1.00 113.13 ? 1169 GLN A CD  1 
ATOM   5642 O OE1 . GLN A 1 1169 ? 172.126 145.334 127.971 1.00 112.69 ? 1169 GLN A OE1 1 
ATOM   5643 N NE2 . GLN A 1 1169 ? 173.463 146.279 129.507 1.00 113.72 ? 1169 GLN A NE2 1 
ATOM   5644 N N   . ILE A 1 1170 ? 169.259 148.917 124.844 1.00 107.42 ? 1170 ILE A N   1 
ATOM   5645 C CA  . ILE A 1 1170 ? 168.318 148.802 123.733 1.00 107.86 ? 1170 ILE A CA  1 
ATOM   5646 C C   . ILE A 1 1170 ? 168.493 149.962 122.762 1.00 108.78 ? 1170 ILE A C   1 
ATOM   5647 O O   . ILE A 1 1170 ? 168.531 149.770 121.541 1.00 108.30 ? 1170 ILE A O   1 
ATOM   5648 C CB  . ILE A 1 1170 ? 166.875 148.721 124.262 1.00 106.77 ? 1170 ILE A CB  1 
ATOM   5649 C CG1 . ILE A 1 1170 ? 166.701 147.482 125.142 1.00 107.75 ? 1170 ILE A CG1 1 
ATOM   5650 C CG2 . ILE A 1 1170 ? 165.884 148.703 123.109 1.00 104.69 ? 1170 ILE A CG2 1 
ATOM   5651 C CD1 . ILE A 1 1170 ? 165.304 147.319 125.698 1.00 106.29 ? 1170 ILE A CD1 1 
ATOM   5652 N N   . MET A 1 1171 ? 168.613 151.180 123.287 1.00 108.30 ? 1171 MET A N   1 
ATOM   5653 C CA  . MET A 1 1171 ? 168.745 152.365 122.451 1.00 104.86 ? 1171 MET A CA  1 
ATOM   5654 C C   . MET A 1 1171 ? 170.107 152.480 121.782 1.00 103.93 ? 1171 MET A C   1 
ATOM   5655 O O   . MET A 1 1171 ? 170.282 153.351 120.924 1.00 102.53 ? 1171 MET A O   1 
ATOM   5656 C CB  . MET A 1 1171 ? 168.478 153.624 123.278 1.00 102.34 ? 1171 MET A CB  1 
ATOM   5657 C CG  . MET A 1 1171 ? 167.059 153.728 123.800 1.00 104.85 ? 1171 MET A CG  1 
ATOM   5658 S SD  . MET A 1 1171 ? 165.843 153.890 122.481 1.00 107.55 ? 1171 MET A SD  1 
ATOM   5659 C CE  . MET A 1 1171 ? 164.335 154.009 123.438 1.00 104.79 ? 1171 MET A CE  1 
ATOM   5660 N N   . ASN A 1 1172 ? 171.072 151.639 122.151 1.00 107.78 ? 1172 ASN A N   1 
ATOM   5661 C CA  . ASN A 1 1172 ? 172.416 151.699 121.595 1.00 108.54 ? 1172 ASN A CA  1 
ATOM   5662 C C   . ASN A 1 1172 ? 172.671 150.613 120.555 1.00 108.02 ? 1172 ASN A C   1 
ATOM   5663 O O   . ASN A 1 1172 ? 173.823 150.212 120.358 1.00 107.64 ? 1172 ASN A O   1 
ATOM   5664 C CB  . ASN A 1 1172 ? 173.454 151.613 122.714 1.00 108.81 ? 1172 ASN A CB  1 
ATOM   5665 C CG  . ASN A 1 1172 ? 173.489 152.861 123.572 1.00 107.70 ? 1172 ASN A CG  1 
ATOM   5666 O OD1 . ASN A 1 1172 ? 173.140 153.950 123.117 1.00 107.78 ? 1172 ASN A OD1 1 
ATOM   5667 N ND2 . ASN A 1 1172 ? 173.916 152.710 124.819 1.00 107.48 ? 1172 ASN A ND2 1 
ATOM   5668 N N   . SER A 1 1173 ? 171.627 150.126 119.896 1.00 99.29  ? 1173 SER A N   1 
ATOM   5669 C CA  . SER A 1 1173 ? 171.817 149.154 118.830 1.00 98.89  ? 1173 SER A CA  1 
ATOM   5670 C C   . SER A 1 1173 ? 172.543 149.813 117.660 1.00 99.57  ? 1173 SER A C   1 
ATOM   5671 O O   . SER A 1 1173 ? 172.253 150.970 117.330 1.00 101.10 ? 1173 SER A O   1 
ATOM   5672 C CB  . SER A 1 1173 ? 170.476 148.588 118.370 1.00 100.11 ? 1173 SER A CB  1 
ATOM   5673 O OG  . SER A 1 1173 ? 170.654 147.642 117.331 1.00 99.47  ? 1173 SER A OG  1 
ATOM   5674 N N   . PRO A 1 1174 ? 173.494 149.128 117.024 1.00 98.61  ? 1174 PRO A N   1 
ATOM   5675 C CA  . PRO A 1 1174 ? 174.241 149.760 115.925 1.00 98.23  ? 1174 PRO A CA  1 
ATOM   5676 C C   . PRO A 1 1174 ? 173.395 150.077 114.705 1.00 98.42  ? 1174 PRO A C   1 
ATOM   5677 O O   . PRO A 1 1174 ? 173.811 150.900 113.880 1.00 98.25  ? 1174 PRO A O   1 
ATOM   5678 C CB  . PRO A 1 1174 ? 175.325 148.722 115.594 1.00 98.10  ? 1174 PRO A CB  1 
ATOM   5679 C CG  . PRO A 1 1174 ? 175.408 147.845 116.807 1.00 98.06  ? 1174 PRO A CG  1 
ATOM   5680 C CD  . PRO A 1 1174 ? 174.020 147.796 117.358 1.00 99.35  ? 1174 PRO A CD  1 
ATOM   5681 N N   . LYS A 1 1175 ? 172.225 149.458 114.558 1.00 90.61  ? 1175 LYS A N   1 
ATOM   5682 C CA  . LYS A 1 1175 ? 171.419 149.577 113.350 1.00 89.93  ? 1175 LYS A CA  1 
ATOM   5683 C C   . LYS A 1 1175 ? 170.042 150.174 113.627 1.00 90.59  ? 1175 LYS A C   1 
ATOM   5684 O O   . LYS A 1 1175 ? 169.045 149.738 113.048 1.00 92.39  ? 1175 LYS A O   1 
ATOM   5685 C CB  . LYS A 1 1175 ? 171.281 148.212 112.680 1.00 92.79  ? 1175 LYS A CB  1 
ATOM   5686 C CG  . LYS A 1 1175 ? 170.866 147.107 113.638 1.00 92.23  ? 1175 LYS A CG  1 
ATOM   5687 C CD  . LYS A 1 1175 ? 171.005 145.735 113.002 1.00 92.72  ? 1175 LYS A CD  1 
ATOM   5688 C CE  . LYS A 1 1175 ? 170.721 144.634 114.011 1.00 93.69  ? 1175 LYS A CE  1 
ATOM   5689 N NZ  . LYS A 1 1175 ? 170.926 143.279 113.431 1.00 93.82  ? 1175 LYS A NZ  1 
ATOM   5690 N N   . ILE A 1 1176 ? 169.969 151.171 114.504 1.00 79.17  ? 1176 ILE A N   1 
ATOM   5691 C CA  . ILE A 1 1176 ? 168.705 151.783 114.888 1.00 78.88  ? 1176 ILE A CA  1 
ATOM   5692 C C   . ILE A 1 1176 ? 168.841 153.297 114.802 1.00 79.35  ? 1176 ILE A C   1 
ATOM   5693 O O   . ILE A 1 1176 ? 169.898 153.853 115.121 1.00 80.38  ? 1176 ILE A O   1 
ATOM   5694 C CB  . ILE A 1 1176 ? 168.273 151.338 116.303 1.00 79.15  ? 1176 ILE A CB  1 
ATOM   5695 C CG1 . ILE A 1 1176 ? 166.855 151.803 116.614 1.00 79.45  ? 1176 ILE A CG1 1 
ATOM   5696 C CG2 . ILE A 1 1176 ? 169.227 151.859 117.356 1.00 76.69  ? 1176 ILE A CG2 1 
ATOM   5697 C CD1 . ILE A 1 1176 ? 166.403 151.413 117.997 1.00 79.08  ? 1176 ILE A CD1 1 
ATOM   5698 N N   . ASN A 1 1177 ? 167.778 153.957 114.339 1.00 60.78  ? 1177 ASN A N   1 
ATOM   5699 C CA  . ASN A 1 1177 ? 167.725 155.417 114.244 1.00 51.89  ? 1177 ASN A CA  1 
ATOM   5700 C C   . ASN A 1 1177 ? 168.876 155.974 113.410 1.00 61.04  ? 1177 ASN A C   1 
ATOM   5701 O O   . ASN A 1 1177 ? 169.491 156.980 113.766 1.00 63.56  ? 1177 ASN A O   1 
ATOM   5702 C CB  . ASN A 1 1177 ? 167.707 156.058 115.632 1.00 53.87  ? 1177 ASN A CB  1 
ATOM   5703 C CG  . ASN A 1 1177 ? 166.479 155.690 116.426 1.00 48.21  ? 1177 ASN A CG  1 
ATOM   5704 O OD1 . ASN A 1 1177 ? 165.720 154.807 116.037 1.00 64.89  ? 1177 ASN A OD1 1 
ATOM   5705 N ND2 . ASN A 1 1177 ? 166.277 156.363 117.550 1.00 50.43  ? 1177 ASN A ND2 1 
ATOM   5706 N N   . LYS A 1 1178 ? 169.177 155.318 112.294 1.00 65.93  ? 1178 LYS A N   1 
ATOM   5707 C CA  . LYS A 1 1178 ? 170.239 155.759 111.402 1.00 61.62  ? 1178 LYS A CA  1 
ATOM   5708 C C   . LYS A 1 1178 ? 169.733 155.778 109.970 1.00 65.49  ? 1178 LYS A C   1 
ATOM   5709 O O   . LYS A 1 1178 ? 169.212 154.771 109.482 1.00 69.20  ? 1178 LYS A O   1 
ATOM   5710 C CB  . LYS A 1 1178 ? 171.468 154.856 111.515 1.00 64.26  ? 1178 LYS A CB  1 
ATOM   5711 C CG  . LYS A 1 1178 ? 172.179 154.950 112.850 1.00 67.02  ? 1178 LYS A CG  1 
ATOM   5712 C CD  . LYS A 1 1178 ? 173.436 154.102 112.862 1.00 70.54  ? 1178 LYS A CD  1 
ATOM   5713 C CE  . LYS A 1 1178 ? 174.201 154.275 114.162 1.00 68.17  ? 1178 LYS A CE  1 
ATOM   5714 N NZ  . LYS A 1 1178 ? 175.453 153.471 114.176 1.00 70.70  ? 1178 LYS A NZ  1 
ATOM   5715 N N   . ASN A 1 1179 ? 169.912 156.919 109.304 1.00 73.29  ? 1179 ASN A N   1 
ATOM   5716 C CA  . ASN A 1 1179 ? 169.515 157.143 107.910 1.00 79.43  ? 1179 ASN A CA  1 
ATOM   5717 C C   . ASN A 1 1179 ? 168.172 156.492 107.588 1.00 77.09  ? 1179 ASN A C   1 
ATOM   5718 O O   . ASN A 1 1179 ? 168.027 155.731 106.630 1.00 74.53  ? 1179 ASN A O   1 
ATOM   5719 C CB  . ASN A 1 1179 ? 170.604 156.678 106.940 1.00 78.01  ? 1179 ASN A CB  1 
ATOM   5720 C CG  . ASN A 1 1179 ? 171.018 155.239 107.160 1.00 82.85  ? 1179 ASN A CG  1 
ATOM   5721 O OD1 . ASN A 1 1179 ? 170.427 154.317 106.599 1.00 81.90  ? 1179 ASN A OD1 1 
ATOM   5722 N ND2 . ASN A 1 1179 ? 172.043 155.038 107.978 1.00 81.99  ? 1179 ASN A ND2 1 
ATOM   5723 N N   . VAL A 1 1180 ? 167.173 156.812 108.408 1.00 68.76  ? 1180 VAL A N   1 
ATOM   5724 C CA  . VAL A 1 1180 ? 165.828 156.302 108.183 1.00 65.39  ? 1180 VAL A CA  1 
ATOM   5725 C C   . VAL A 1 1180 ? 165.178 157.070 107.042 1.00 66.50  ? 1180 VAL A C   1 
ATOM   5726 O O   . VAL A 1 1180 ? 165.147 158.307 107.043 1.00 72.21  ? 1180 VAL A O   1 
ATOM   5727 C CB  . VAL A 1 1180 ? 164.994 156.405 109.466 1.00 63.64  ? 1180 VAL A CB  1 
ATOM   5728 C CG1 . VAL A 1 1180 ? 163.557 156.034 109.185 1.00 61.63  ? 1180 VAL A CG1 1 
ATOM   5729 C CG2 . VAL A 1 1180 ? 165.575 155.511 110.542 1.00 62.52  ? 1180 VAL A CG2 1 
ATOM   5730 N N   . HIS A 1 1181 ? 164.650 156.341 106.065 1.00 75.38  ? 1181 HIS A N   1 
ATOM   5731 C CA  . HIS A 1 1181 ? 163.978 156.946 104.921 1.00 77.99  ? 1181 HIS A CA  1 
ATOM   5732 C C   . HIS A 1 1181 ? 162.531 157.235 105.300 1.00 79.99  ? 1181 HIS A C   1 
ATOM   5733 O O   . HIS A 1 1181 ? 161.690 156.331 105.300 1.00 84.47  ? 1181 HIS A O   1 
ATOM   5734 C CB  . HIS A 1 1181 ? 164.049 156.026 103.706 1.00 76.78  ? 1181 HIS A CB  1 
ATOM   5735 C CG  . HIS A 1 1181 ? 165.443 155.750 103.238 1.00 80.89  ? 1181 HIS A CG  1 
ATOM   5736 N ND1 . HIS A 1 1181 ? 166.082 156.534 102.302 1.00 83.28  ? 1181 HIS A ND1 1 
ATOM   5737 C CD2 . HIS A 1 1181 ? 166.320 154.776 103.575 1.00 81.02  ? 1181 HIS A CD2 1 
ATOM   5738 C CE1 . HIS A 1 1181 ? 167.293 156.055 102.083 1.00 84.72  ? 1181 HIS A CE1 1 
ATOM   5739 N NE2 . HIS A 1 1181 ? 167.463 154.989 102.844 1.00 84.66  ? 1181 HIS A NE2 1 
ATOM   5740 N N   . TRP A 1 1182 ? 162.238 158.495 105.617 1.00 59.31  ? 1182 TRP A N   1 
ATOM   5741 C CA  . TRP A 1 1182 ? 160.880 158.881 105.969 1.00 56.30  ? 1182 TRP A CA  1 
ATOM   5742 C C   . TRP A 1 1182 ? 159.980 159.047 104.755 1.00 64.04  ? 1182 TRP A C   1 
ATOM   5743 O O   . TRP A 1 1182 ? 158.764 159.183 104.921 1.00 69.95  ? 1182 TRP A O   1 
ATOM   5744 C CB  . TRP A 1 1182 ? 160.892 160.176 106.782 1.00 55.16  ? 1182 TRP A CB  1 
ATOM   5745 C CG  . TRP A 1 1182 ? 161.545 160.021 108.111 1.00 58.88  ? 1182 TRP A CG  1 
ATOM   5746 C CD1 . TRP A 1 1182 ? 162.806 160.402 108.454 1.00 58.57  ? 1182 TRP A CD1 1 
ATOM   5747 C CD2 . TRP A 1 1182 ? 160.975 159.426 109.280 1.00 59.17  ? 1182 TRP A CD2 1 
ATOM   5748 N NE1 . TRP A 1 1182 ? 163.056 160.088 109.765 1.00 60.45  ? 1182 TRP A NE1 1 
ATOM   5749 C CE2 . TRP A 1 1182 ? 161.946 159.485 110.294 1.00 54.66  ? 1182 TRP A CE2 1 
ATOM   5750 C CE3 . TRP A 1 1182 ? 159.737 158.848 109.566 1.00 56.14  ? 1182 TRP A CE3 1 
ATOM   5751 C CZ2 . TRP A 1 1182 ? 161.719 158.993 111.572 1.00 49.78  ? 1182 TRP A CZ2 1 
ATOM   5752 C CZ3 . TRP A 1 1182 ? 159.514 158.360 110.835 1.00 57.94  ? 1182 TRP A CZ3 1 
ATOM   5753 C CH2 . TRP A 1 1182 ? 160.499 158.435 111.822 1.00 56.97  ? 1182 TRP A CH2 1 
ATOM   5754 N N   . GLU A 1 1183 ? 160.540 159.039 103.548 1.00 76.48  ? 1183 GLU A N   1 
ATOM   5755 C CA  . GLU A 1 1183 ? 159.737 159.123 102.338 1.00 75.50  ? 1183 GLU A CA  1 
ATOM   5756 C C   . GLU A 1 1183 ? 159.069 157.803 101.982 1.00 78.11  ? 1183 GLU A C   1 
ATOM   5757 O O   . GLU A 1 1183 ? 158.239 157.776 101.069 1.00 82.67  ? 1183 GLU A O   1 
ATOM   5758 C CB  . GLU A 1 1183 ? 160.602 159.595 101.166 1.00 76.85  ? 1183 GLU A CB  1 
ATOM   5759 C CG  . GLU A 1 1183 ? 161.704 158.627 100.755 1.00 81.15  ? 1183 GLU A CG  1 
ATOM   5760 C CD  . GLU A 1 1183 ? 162.927 158.693 101.654 1.00 83.67  ? 1183 GLU A CD  1 
ATOM   5761 O OE1 . GLU A 1 1183 ? 162.846 159.310 102.737 1.00 83.51  ? 1183 GLU A OE1 1 
ATOM   5762 O OE2 . GLU A 1 1183 ? 163.974 158.129 101.275 1.00 80.34  ? 1183 GLU A OE2 1 
ATOM   5763 N N   . ASN A 1 1184 ? 159.412 156.719 102.673 1.00 82.78  ? 1184 ASN A N   1 
ATOM   5764 C CA  . ASN A 1 1184 ? 158.825 155.420 102.378 1.00 83.07  ? 1184 ASN A CA  1 
ATOM   5765 C C   . ASN A 1 1184 ? 157.342 155.417 102.723 1.00 84.99  ? 1184 ASN A C   1 
ATOM   5766 O O   . ASN A 1 1184 ? 156.945 155.830 103.815 1.00 91.01  ? 1184 ASN A O   1 
ATOM   5767 C CB  . ASN A 1 1184 ? 159.557 154.332 103.164 1.00 79.86  ? 1184 ASN A CB  1 
ATOM   5768 C CG  . ASN A 1 1184 ? 159.240 152.937 102.669 1.00 85.42  ? 1184 ASN A CG  1 
ATOM   5769 O OD1 . ASN A 1 1184 ? 158.143 152.667 102.183 1.00 89.32  ? 1184 ASN A OD1 1 
ATOM   5770 N ND2 . ASN A 1 1184 ? 160.208 152.038 102.792 1.00 82.95  ? 1184 ASN A ND2 1 
ATOM   5771 N N   . THR A 1 1185 ? 156.521 154.946 101.782 1.00 80.83  ? 1185 THR A N   1 
ATOM   5772 C CA  . THR A 1 1185 ? 155.083 154.871 102.026 1.00 83.75  ? 1185 THR A CA  1 
ATOM   5773 C C   . THR A 1 1185 ? 154.763 153.879 103.136 1.00 85.00  ? 1185 THR A C   1 
ATOM   5774 O O   . THR A 1 1185 ? 153.875 154.124 103.961 1.00 85.62  ? 1185 THR A O   1 
ATOM   5775 C CB  . THR A 1 1185 ? 154.352 154.490 100.740 1.00 84.38  ? 1185 THR A CB  1 
ATOM   5776 O OG1 . THR A 1 1185 ? 154.626 155.466 99.728  1.00 87.25  ? 1185 THR A OG1 1 
ATOM   5777 C CG2 . THR A 1 1185 ? 152.853 154.426 100.975 1.00 80.77  ? 1185 THR A CG2 1 
ATOM   5778 N N   . ASN A 1 1186 ? 155.478 152.753 103.170 1.00 85.30  ? 1186 ASN A N   1 
ATOM   5779 C CA  . ASN A 1 1186 ? 155.239 151.755 104.206 1.00 84.84  ? 1186 ASN A CA  1 
ATOM   5780 C C   . ASN A 1 1186 ? 155.505 152.330 105.591 1.00 82.14  ? 1186 ASN A C   1 
ATOM   5781 O O   . ASN A 1 1186 ? 154.745 152.079 106.533 1.00 82.85  ? 1186 ASN A O   1 
ATOM   5782 C CB  . ASN A 1 1186 ? 156.112 150.526 103.952 1.00 82.02  ? 1186 ASN A CB  1 
ATOM   5783 C CG  . ASN A 1 1186 ? 155.608 149.291 104.672 1.00 88.24  ? 1186 ASN A CG  1 
ATOM   5784 O OD1 . ASN A 1 1186 ? 155.082 149.371 105.781 1.00 89.39  ? 1186 ASN A OD1 1 
ATOM   5785 N ND2 . ASN A 1 1186 ? 155.767 148.135 104.038 1.00 86.98  ? 1186 ASN A ND2 1 
ATOM   5786 N N   . LEU A 1 1187 ? 156.576 153.111 105.733 1.00 74.79  ? 1187 LEU A N   1 
ATOM   5787 C CA  . LEU A 1 1187 ? 156.880 153.715 107.025 1.00 71.89  ? 1187 LEU A CA  1 
ATOM   5788 C C   . LEU A 1 1187 ? 155.811 154.719 107.435 1.00 72.55  ? 1187 LEU A C   1 
ATOM   5789 O O   . LEU A 1 1187 ? 155.447 154.798 108.611 1.00 82.39  ? 1187 LEU A O   1 
ATOM   5790 C CB  . LEU A 1 1187 ? 158.252 154.379 106.987 1.00 73.83  ? 1187 LEU A CB  1 
ATOM   5791 C CG  . LEU A 1 1187 ? 158.695 155.047 108.286 1.00 72.23  ? 1187 LEU A CG  1 
ATOM   5792 C CD1 . LEU A 1 1187 ? 158.606 154.074 109.445 1.00 67.45  ? 1187 LEU A CD1 1 
ATOM   5793 C CD2 . LEU A 1 1187 ? 160.106 155.562 108.137 1.00 78.21  ? 1187 LEU A CD2 1 
ATOM   5794 N N   . GLN A 1 1188 ? 155.301 155.502 106.483 1.00 71.82  ? 1188 GLN A N   1 
ATOM   5795 C CA  . GLN A 1 1188 ? 154.239 156.450 106.803 1.00 73.31  ? 1188 GLN A CA  1 
ATOM   5796 C C   . GLN A 1 1188 ? 152.968 155.729 107.234 1.00 75.99  ? 1188 GLN A C   1 
ATOM   5797 O O   . GLN A 1 1188 ? 152.289 156.153 108.179 1.00 80.05  ? 1188 GLN A O   1 
ATOM   5798 C CB  . GLN A 1 1188 ? 153.973 157.353 105.601 1.00 74.65  ? 1188 GLN A CB  1 
ATOM   5799 C CG  . GLN A 1 1188 ? 155.183 158.164 105.176 1.00 71.29  ? 1188 GLN A CG  1 
ATOM   5800 C CD  . GLN A 1 1188 ? 155.033 158.755 103.793 1.00 74.20  ? 1188 GLN A CD  1 
ATOM   5801 O OE1 . GLN A 1 1188 ? 153.997 158.600 103.150 1.00 80.27  ? 1188 GLN A OE1 1 
ATOM   5802 N NE2 . GLN A 1 1188 ? 156.072 159.432 103.324 1.00 73.98  ? 1188 GLN A NE2 1 
ATOM   5803 N N   . GLU A 1 1189 ? 152.631 154.632 106.555 1.00 77.74  ? 1189 GLU A N   1 
ATOM   5804 C CA  . GLU A 1 1189 ? 151.468 153.851 106.957 1.00 78.17  ? 1189 GLU A CA  1 
ATOM   5805 C C   . GLU A 1 1189 ? 151.669 153.247 108.341 1.00 78.79  ? 1189 GLU A C   1 
ATOM   5806 O O   . GLU A 1 1189 ? 150.730 153.185 109.143 1.00 83.77  ? 1189 GLU A O   1 
ATOM   5807 C CB  . GLU A 1 1189 ? 151.187 152.763 105.922 1.00 82.63  ? 1189 GLU A CB  1 
ATOM   5808 C CG  . GLU A 1 1189 ? 149.750 152.279 105.900 1.00 81.25  ? 1189 GLU A CG  1 
ATOM   5809 C CD  . GLU A 1 1189 ? 149.454 151.400 104.701 1.00 87.76  ? 1189 GLU A CD  1 
ATOM   5810 O OE1 . GLU A 1 1189 ? 150.414 150.907 104.072 1.00 89.32  ? 1189 GLU A OE1 1 
ATOM   5811 O OE2 . GLU A 1 1189 ? 148.262 151.208 104.382 1.00 87.86  ? 1189 GLU A OE2 1 
ATOM   5812 N N   . GLU A 1 1190 ? 152.890 152.796 108.639 1.00 72.15  ? 1190 GLU A N   1 
ATOM   5813 C CA  . GLU A 1 1190 ? 153.182 152.292 109.976 1.00 72.38  ? 1190 GLU A CA  1 
ATOM   5814 C C   . GLU A 1 1190 ? 153.047 153.391 111.020 1.00 73.00  ? 1190 GLU A C   1 
ATOM   5815 O O   . GLU A 1 1190 ? 152.579 153.141 112.133 1.00 78.49  ? 1190 GLU A O   1 
ATOM   5816 C CB  . GLU A 1 1190 ? 154.579 151.679 110.022 1.00 73.45  ? 1190 GLU A CB  1 
ATOM   5817 C CG  . GLU A 1 1190 ? 154.694 150.347 109.304 1.00 77.87  ? 1190 GLU A CG  1 
ATOM   5818 C CD  . GLU A 1 1190 ? 155.910 149.556 109.741 1.00 79.65  ? 1190 GLU A CD  1 
ATOM   5819 O OE1 . GLU A 1 1190 ? 156.559 149.961 110.728 1.00 79.97  ? 1190 GLU A OE1 1 
ATOM   5820 O OE2 . GLU A 1 1190 ? 156.217 148.529 109.101 1.00 78.76  ? 1190 GLU A OE2 1 
ATOM   5821 N N   . LEU A 1 1191 ? 153.464 154.612 110.684 1.00 64.90  ? 1191 LEU A N   1 
ATOM   5822 C CA  . LEU A 1 1191 ? 153.286 155.732 111.603 1.00 63.88  ? 1191 LEU A CA  1 
ATOM   5823 C C   . LEU A 1 1191 ? 151.811 156.000 111.866 1.00 70.95  ? 1191 LEU A C   1 
ATOM   5824 O O   . LEU A 1 1191 ? 151.410 156.259 113.008 1.00 78.79  ? 1191 LEU A O   1 
ATOM   5825 C CB  . LEU A 1 1191 ? 153.958 156.985 111.046 1.00 63.39  ? 1191 LEU A CB  1 
ATOM   5826 C CG  . LEU A 1 1191 ? 155.481 157.044 111.089 1.00 62.65  ? 1191 LEU A CG  1 
ATOM   5827 C CD1 . LEU A 1 1191 ? 155.968 158.325 110.449 1.00 61.47  ? 1191 LEU A CD1 1 
ATOM   5828 C CD2 . LEU A 1 1191 ? 155.971 156.945 112.517 1.00 67.86  ? 1191 LEU A CD2 1 
ATOM   5829 N N   . ILE A 1 1192 ? 150.988 155.956 110.818 1.00 61.40  ? 1192 ILE A N   1 
ATOM   5830 C CA  . ILE A 1 1192 ? 149.555 156.178 110.997 1.00 58.49  ? 1192 ILE A CA  1 
ATOM   5831 C C   . ILE A 1 1192 ? 148.949 155.086 111.870 1.00 63.45  ? 1192 ILE A C   1 
ATOM   5832 O O   . ILE A 1 1192 ? 148.144 155.361 112.771 1.00 70.24  ? 1192 ILE A O   1 
ATOM   5833 C CB  . ILE A 1 1192 ? 148.853 156.268 109.631 1.00 63.28  ? 1192 ILE A CB  1 
ATOM   5834 C CG1 . ILE A 1 1192 ? 149.323 157.510 108.879 1.00 65.37  ? 1192 ILE A CG1 1 
ATOM   5835 C CG2 . ILE A 1 1192 ? 147.349 156.295 109.808 1.00 66.09  ? 1192 ILE A CG2 1 
ATOM   5836 C CD1 . ILE A 1 1192 ? 148.637 157.710 107.551 1.00 69.05  ? 1192 ILE A CD1 1 
ATOM   5837 N N   . ASN A 1 1193 ? 149.323 153.830 111.618 1.00 65.62  ? 1193 ASN A N   1 
ATOM   5838 C CA  . ASN A 1 1193 ? 148.818 152.734 112.439 1.00 62.12  ? 1193 ASN A CA  1 
ATOM   5839 C C   . ASN A 1 1193 ? 149.281 152.869 113.882 1.00 66.00  ? 1193 ASN A C   1 
ATOM   5840 O O   . ASN A 1 1193 ? 148.532 152.559 114.812 1.00 69.49  ? 1193 ASN A O   1 
ATOM   5841 C CB  . ASN A 1 1193 ? 149.256 151.392 111.858 1.00 67.26  ? 1193 ASN A CB  1 
ATOM   5842 C CG  . ASN A 1 1193 ? 148.576 151.080 110.544 1.00 75.66  ? 1193 ASN A CG  1 
ATOM   5843 O OD1 . ASN A 1 1193 ? 147.484 151.571 110.266 1.00 76.37  ? 1193 ASN A OD1 1 
ATOM   5844 N ND2 . ASN A 1 1193 ? 149.219 150.256 109.726 1.00 76.83  ? 1193 ASN A ND2 1 
ATOM   5845 N N   . MET A 1 1194 ? 150.519 153.322 114.088 1.00 70.42  ? 1194 MET A N   1 
ATOM   5846 C CA  . MET A 1 1194 ? 151.022 153.542 115.439 1.00 66.95  ? 1194 MET A CA  1 
ATOM   5847 C C   . MET A 1 1194 ? 150.229 154.626 116.152 1.00 63.00  ? 1194 MET A C   1 
ATOM   5848 O O   . MET A 1 1194 ? 149.899 154.488 117.335 1.00 71.40  ? 1194 MET A O   1 
ATOM   5849 C CB  . MET A 1 1194 ? 152.504 153.905 115.384 1.00 60.73  ? 1194 MET A CB  1 
ATOM   5850 C CG  . MET A 1 1194 ? 152.985 154.767 116.533 1.00 65.22  ? 1194 MET A CG  1 
ATOM   5851 S SD  . MET A 1 1194 ? 154.670 155.348 116.271 1.00 81.18  ? 1194 MET A SD  1 
ATOM   5852 C CE  . MET A 1 1194 ? 154.818 156.547 117.586 1.00 67.55  ? 1194 MET A CE  1 
ATOM   5853 N N   . HIS A 1 1195 ? 149.916 155.716 115.452 1.00 54.35  ? 1195 HIS A N   1 
ATOM   5854 C CA  . HIS A 1 1195 ? 149.104 156.766 116.055 1.00 48.45  ? 1195 HIS A CA  1 
ATOM   5855 C C   . HIS A 1 1195 ? 147.720 156.248 116.420 1.00 54.93  ? 1195 HIS A C   1 
ATOM   5856 O O   . HIS A 1 1195 ? 147.205 156.537 117.507 1.00 64.19  ? 1195 HIS A O   1 
ATOM   5857 C CB  . HIS A 1 1195 ? 148.993 157.956 115.106 1.00 51.43  ? 1195 HIS A CB  1 
ATOM   5858 C CG  . HIS A 1 1195 ? 147.933 158.937 115.491 1.00 53.70  ? 1195 HIS A CG  1 
ATOM   5859 N ND1 . HIS A 1 1195 ? 148.088 159.835 116.525 1.00 56.33  ? 1195 HIS A ND1 1 
ATOM   5860 C CD2 . HIS A 1 1195 ? 146.699 159.160 114.982 1.00 57.57  ? 1195 HIS A CD2 1 
ATOM   5861 C CE1 . HIS A 1 1195 ? 146.997 160.571 116.633 1.00 55.96  ? 1195 HIS A CE1 1 
ATOM   5862 N NE2 . HIS A 1 1195 ? 146.138 160.182 115.709 1.00 53.47  ? 1195 HIS A NE2 1 
ATOM   5863 N N   . ASN A 1 1196 ? 147.103 155.477 115.523 1.00 67.05  ? 1196 ASN A N   1 
ATOM   5864 C CA  . ASN A 1 1196 ? 145.785 154.924 115.818 1.00 67.13  ? 1196 ASN A CA  1 
ATOM   5865 C C   . ASN A 1 1196 ? 145.839 153.971 117.005 1.00 63.21  ? 1196 ASN A C   1 
ATOM   5866 O O   . ASN A 1 1196 ? 144.948 153.982 117.861 1.00 64.99  ? 1196 ASN A O   1 
ATOM   5867 C CB  . ASN A 1 1196 ? 145.221 154.220 114.586 1.00 65.12  ? 1196 ASN A CB  1 
ATOM   5868 C CG  . ASN A 1 1196 ? 144.881 155.186 113.472 1.00 66.16  ? 1196 ASN A CG  1 
ATOM   5869 O OD1 . ASN A 1 1196 ? 144.520 156.334 113.722 1.00 64.73  ? 1196 ASN A OD1 1 
ATOM   5870 N ND2 . ASN A 1 1196 ? 144.995 154.725 112.233 1.00 67.97  ? 1196 ASN A ND2 1 
ATOM   5871 N N   . THR A 1 1197 ? 146.879 153.139 117.073 1.00 56.19  ? 1197 THR A N   1 
ATOM   5872 C CA  . THR A 1 1197 ? 147.030 152.226 118.199 1.00 55.54  ? 1197 THR A CA  1 
ATOM   5873 C C   . THR A 1 1197 ? 147.211 152.988 119.503 1.00 62.62  ? 1197 THR A C   1 
ATOM   5874 O O   . THR A 1 1197 ? 146.623 152.628 120.529 1.00 73.65  ? 1197 THR A O   1 
ATOM   5875 C CB  . THR A 1 1197 ? 148.215 151.293 117.958 1.00 57.10  ? 1197 THR A CB  1 
ATOM   5876 O OG1 . THR A 1 1197 ? 147.957 150.481 116.807 1.00 63.46  ? 1197 THR A OG1 1 
ATOM   5877 C CG2 . THR A 1 1197 ? 148.443 150.400 119.161 1.00 63.30  ? 1197 THR A CG2 1 
ATOM   5878 N N   . LEU A 1 1198 ? 148.018 154.049 119.481 1.00 67.15  ? 1198 LEU A N   1 
ATOM   5879 C CA  . LEU A 1 1198 ? 148.219 154.848 120.683 1.00 63.78  ? 1198 LEU A CA  1 
ATOM   5880 C C   . LEU A 1 1198 ? 146.919 155.501 121.126 1.00 62.48  ? 1198 LEU A C   1 
ATOM   5881 O O   . LEU A 1 1198 ? 146.636 155.588 122.326 1.00 68.37  ? 1198 LEU A O   1 
ATOM   5882 C CB  . LEU A 1 1198 ? 149.298 155.899 120.436 1.00 54.50  ? 1198 LEU A CB  1 
ATOM   5883 C CG  . LEU A 1 1198 ? 150.027 156.398 121.680 1.00 54.83  ? 1198 LEU A CG  1 
ATOM   5884 C CD1 . LEU A 1 1198 ? 150.705 155.239 122.380 1.00 57.43  ? 1198 LEU A CD1 1 
ATOM   5885 C CD2 . LEU A 1 1198 ? 151.040 157.458 121.304 1.00 63.41  ? 1198 LEU A CD2 1 
ATOM   5886 N N   . GLU A 1 1199 ? 146.114 155.972 120.171 1.00 63.06  ? 1199 GLU A N   1 
ATOM   5887 C CA  . GLU A 1 1199 ? 144.797 156.493 120.522 1.00 65.47  ? 1199 GLU A CA  1 
ATOM   5888 C C   . GLU A 1 1199 ? 143.886 155.401 121.066 1.00 72.57  ? 1199 GLU A C   1 
ATOM   5889 O O   . GLU A 1 1199 ? 143.012 155.680 121.894 1.00 74.48  ? 1199 GLU A O   1 
ATOM   5890 C CB  . GLU A 1 1199 ? 144.146 157.157 119.312 1.00 67.90  ? 1199 GLU A CB  1 
ATOM   5891 C CG  . GLU A 1 1199 ? 144.642 158.559 119.024 1.00 72.79  ? 1199 GLU A CG  1 
ATOM   5892 C CD  . GLU A 1 1199 ? 143.854 159.230 117.919 1.00 77.06  ? 1199 GLU A CD  1 
ATOM   5893 O OE1 . GLU A 1 1199 ? 143.035 158.544 117.272 1.00 75.59  ? 1199 GLU A OE1 1 
ATOM   5894 O OE2 . GLU A 1 1199 ? 144.048 160.444 117.698 1.00 75.49  ? 1199 GLU A OE2 1 
ATOM   5895 N N   . SER A 1 1200 ? 144.068 154.159 120.614 1.00 71.44  ? 1200 SER A N   1 
ATOM   5896 C CA  . SER A 1 1200 ? 143.168 153.085 121.016 1.00 70.11  ? 1200 SER A CA  1 
ATOM   5897 C C   . SER A 1 1200 ? 143.323 152.725 122.488 1.00 70.35  ? 1200 SER A C   1 
ATOM   5898 O O   . SER A 1 1200 ? 142.411 152.135 123.075 1.00 77.27  ? 1200 SER A O   1 
ATOM   5899 C CB  . SER A 1 1200 ? 143.402 151.850 120.147 1.00 68.35  ? 1200 SER A CB  1 
ATOM   5900 O OG  . SER A 1 1200 ? 143.168 152.139 118.781 1.00 75.21  ? 1200 SER A OG  1 
ATOM   5901 N N   . GLN A 1 1201 ? 144.458 153.058 123.096 1.00 68.70  ? 1201 GLN A N   1 
ATOM   5902 C CA  . GLN A 1 1201 ? 144.684 152.702 124.489 1.00 67.89  ? 1201 GLN A CA  1 
ATOM   5903 C C   . GLN A 1 1201 ? 143.714 153.443 125.400 1.00 76.56  ? 1201 GLN A C   1 
ATOM   5904 O O   . GLN A 1 1201 ? 143.385 154.610 125.172 1.00 76.78  ? 1201 GLN A O   1 
ATOM   5905 C CB  . GLN A 1 1201 ? 146.123 153.013 124.890 1.00 65.47  ? 1201 GLN A CB  1 
ATOM   5906 C CG  . GLN A 1 1201 ? 147.161 152.268 124.079 1.00 69.95  ? 1201 GLN A CG  1 
ATOM   5907 C CD  . GLN A 1 1201 ? 147.059 150.768 124.245 1.00 77.06  ? 1201 GLN A CD  1 
ATOM   5908 O OE1 . GLN A 1 1201 ? 146.591 150.276 125.270 1.00 78.97  ? 1201 GLN A OE1 1 
ATOM   5909 N NE2 . GLN A 1 1201 ? 147.496 150.031 123.232 1.00 74.47  ? 1201 GLN A NE2 1 
ATOM   5910 N N   . GLU A 1 1202 ? 143.251 152.747 126.441 1.00 82.89  ? 1202 GLU A N   1 
ATOM   5911 C CA  . GLU A 1 1202 ? 142.304 153.347 127.374 1.00 81.35  ? 1202 GLU A CA  1 
ATOM   5912 C C   . GLU A 1 1202 ? 142.939 154.467 128.182 1.00 80.30  ? 1202 GLU A C   1 
ATOM   5913 O O   . GLU A 1 1202 ? 142.271 155.458 128.497 1.00 80.65  ? 1202 GLU A O   1 
ATOM   5914 C CB  . GLU A 1 1202 ? 141.739 152.279 128.309 1.00 78.76  ? 1202 GLU A CB  1 
ATOM   5915 C CG  . GLU A 1 1202 ? 141.044 151.137 127.593 1.00 83.68  ? 1202 GLU A CG  1 
ATOM   5916 C CD  . GLU A 1 1202 ? 139.785 151.579 126.875 1.00 88.12  ? 1202 GLU A CD  1 
ATOM   5917 O OE1 . GLU A 1 1202 ? 139.179 152.586 127.296 1.00 85.39  ? 1202 GLU A OE1 1 
ATOM   5918 O OE2 . GLU A 1 1202 ? 139.399 150.920 125.887 1.00 89.18  ? 1202 GLU A OE2 1 
ATOM   5919 N N   . PHE A 1 1203 ? 144.217 154.332 128.527 1.00 71.56  ? 1203 PHE A N   1 
ATOM   5920 C CA  . PHE A 1 1203 ? 144.891 155.323 129.353 1.00 71.37  ? 1203 PHE A CA  1 
ATOM   5921 C C   . PHE A 1 1203 ? 145.318 156.561 128.578 1.00 71.51  ? 1203 PHE A C   1 
ATOM   5922 O O   . PHE A 1 1203 ? 145.749 157.537 129.198 1.00 76.41  ? 1203 PHE A O   1 
ATOM   5923 C CB  . PHE A 1 1203 ? 146.109 154.696 130.033 1.00 69.36  ? 1203 PHE A CB  1 
ATOM   5924 C CG  . PHE A 1 1203 ? 147.026 153.977 129.091 1.00 70.96  ? 1203 PHE A CG  1 
ATOM   5925 C CD1 . PHE A 1 1203 ? 146.849 152.632 128.824 1.00 69.15  ? 1203 PHE A CD1 1 
ATOM   5926 C CD2 . PHE A 1 1203 ? 148.070 154.643 128.477 1.00 76.07  ? 1203 PHE A CD2 1 
ATOM   5927 C CE1 . PHE A 1 1203 ? 147.690 151.969 127.960 1.00 72.32  ? 1203 PHE A CE1 1 
ATOM   5928 C CE2 . PHE A 1 1203 ? 148.916 153.984 127.612 1.00 75.69  ? 1203 PHE A CE2 1 
ATOM   5929 C CZ  . PHE A 1 1203 ? 148.725 152.645 127.353 1.00 75.36  ? 1203 PHE A CZ  1 
ATOM   5930 N N   . VAL A 1 1204 ? 145.211 156.551 127.253 1.00 62.69  ? 1204 VAL A N   1 
ATOM   5931 C CA  . VAL A 1 1204 ? 145.562 157.698 126.426 1.00 62.20  ? 1204 VAL A CA  1 
ATOM   5932 C C   . VAL A 1 1204 ? 144.278 158.414 126.041 1.00 66.67  ? 1204 VAL A C   1 
ATOM   5933 O O   . VAL A 1 1204 ? 143.374 157.809 125.452 1.00 69.39  ? 1204 VAL A O   1 
ATOM   5934 C CB  . VAL A 1 1204 ? 146.351 157.273 125.180 1.00 57.46  ? 1204 VAL A CB  1 
ATOM   5935 C CG1 . VAL A 1 1204 ? 146.524 158.449 124.247 1.00 59.35  ? 1204 VAL A CG1 1 
ATOM   5936 C CG2 . VAL A 1 1204 ? 147.699 156.712 125.577 1.00 62.65  ? 1204 VAL A CG2 1 
ATOM   5937 N N   . THR A 1 1205 ? 144.193 159.700 126.372 1.00 66.57  ? 1205 THR A N   1 
ATOM   5938 C CA  . THR A 1 1205 ? 142.996 160.478 126.083 1.00 65.88  ? 1205 THR A CA  1 
ATOM   5939 C C   . THR A 1 1205 ? 143.112 161.256 124.780 1.00 70.78  ? 1205 THR A C   1 
ATOM   5940 O O   . THR A 1 1205 ? 142.207 161.197 123.942 1.00 74.37  ? 1205 THR A O   1 
ATOM   5941 C CB  . THR A 1 1205 ? 142.704 161.446 127.230 1.00 70.50  ? 1205 THR A CB  1 
ATOM   5942 O OG1 . THR A 1 1205 ? 143.750 162.420 127.307 1.00 70.20  ? 1205 THR A OG1 1 
ATOM   5943 C CG2 . THR A 1 1205 ? 142.623 160.697 128.544 1.00 68.23  ? 1205 THR A CG2 1 
ATOM   5944 N N   . SER A 1 1206 ? 144.211 161.981 124.591 1.00 64.21  ? 1206 SER A N   1 
ATOM   5945 C CA  . SER A 1 1206 ? 144.407 162.793 123.401 1.00 64.97  ? 1206 SER A CA  1 
ATOM   5946 C C   . SER A 1 1206 ? 145.833 162.630 122.902 1.00 59.80  ? 1206 SER A C   1 
ATOM   5947 O O   . SER A 1 1206 ? 146.761 162.437 123.689 1.00 66.34  ? 1206 SER A O   1 
ATOM   5948 C CB  . SER A 1 1206 ? 144.119 164.273 123.676 1.00 64.68  ? 1206 SER A CB  1 
ATOM   5949 O OG  . SER A 1 1206 ? 144.439 165.071 122.551 1.00 65.34  ? 1206 SER A OG  1 
ATOM   5950 N N   . VAL A 1 1207 ? 145.997 162.711 121.585 1.00 50.52  ? 1207 VAL A N   1 
ATOM   5951 C CA  . VAL A 1 1207 ? 147.301 162.632 120.942 1.00 49.15  ? 1207 VAL A CA  1 
ATOM   5952 C C   . VAL A 1 1207 ? 147.446 163.818 120.003 1.00 55.46  ? 1207 VAL A C   1 
ATOM   5953 O O   . VAL A 1 1207 ? 146.543 164.109 119.213 1.00 66.07  ? 1207 VAL A O   1 
ATOM   5954 C CB  . VAL A 1 1207 ? 147.484 161.312 120.166 1.00 47.96  ? 1207 VAL A CB  1 
ATOM   5955 C CG1 . VAL A 1 1207 ? 148.852 161.270 119.517 1.00 49.12  ? 1207 VAL A CG1 1 
ATOM   5956 C CG2 . VAL A 1 1207 ? 147.298 160.125 121.084 1.00 55.47  ? 1207 VAL A CG2 1 
ATOM   5957 N N   . ALA A 1 1208 ? 148.588 164.500 120.085 1.00 57.26  ? 1208 ALA A N   1 
ATOM   5958 C CA  . ALA A 1 1208 ? 148.884 165.660 119.243 1.00 55.62  ? 1208 ALA A CA  1 
ATOM   5959 C C   . ALA A 1 1208 ? 150.112 165.318 118.407 1.00 57.94  ? 1208 ALA A C   1 
ATOM   5960 O O   . ALA A 1 1208 ? 151.244 165.618 118.788 1.00 66.62  ? 1208 ALA A O   1 
ATOM   5961 C CB  . ALA A 1 1208 ? 149.095 166.906 120.088 1.00 30.00  ? 1208 ALA A CB  1 
ATOM   5962 N N   . ASN A 1 1209 ? 149.879 164.694 117.257 1.00 52.42  ? 1209 ASN A N   1 
ATOM   5963 C CA  . ASN A 1 1209 ? 150.946 164.216 116.386 1.00 47.83  ? 1209 ASN A CA  1 
ATOM   5964 C C   . ASN A 1 1209 ? 150.869 164.961 115.060 1.00 55.59  ? 1209 ASN A C   1 
ATOM   5965 O O   . ASN A 1 1209 ? 150.010 164.665 114.224 1.00 64.87  ? 1209 ASN A O   1 
ATOM   5966 C CB  . ASN A 1 1209 ? 150.827 162.709 116.181 1.00 45.70  ? 1209 ASN A CB  1 
ATOM   5967 C CG  . ASN A 1 1209 ? 151.958 162.144 115.359 1.00 50.12  ? 1209 ASN A CG  1 
ATOM   5968 O OD1 . ASN A 1 1209 ? 152.992 162.782 115.186 1.00 61.23  ? 1209 ASN A OD1 1 
ATOM   5969 N ND2 . ASN A 1 1209 ? 151.769 160.934 114.849 1.00 52.11  ? 1209 ASN A ND2 1 
ATOM   5970 N N   . GLY A 1 1210 ? 151.771 165.923 114.865 1.00 52.61  ? 1210 GLY A N   1 
ATOM   5971 C CA  . GLY A 1 1210 ? 151.768 166.685 113.627 1.00 49.87  ? 1210 GLY A CA  1 
ATOM   5972 C C   . GLY A 1 1210 ? 152.060 165.828 112.411 1.00 47.69  ? 1210 GLY A C   1 
ATOM   5973 O O   . GLY A 1 1210 ? 151.547 166.085 111.320 1.00 58.55  ? 1210 GLY A O   1 
ATOM   5974 N N   . PHE A 1 1211 ? 152.894 164.801 112.583 1.00 42.43  ? 1211 PHE A N   1 
ATOM   5975 C CA  . PHE A 1 1211 ? 153.222 163.912 111.474 1.00 46.43  ? 1211 PHE A CA  1 
ATOM   5976 C C   . PHE A 1 1211 ? 151.979 163.204 110.954 1.00 58.15  ? 1211 PHE A C   1 
ATOM   5977 O O   . PHE A 1 1211 ? 151.806 163.041 109.741 1.00 60.97  ? 1211 PHE A O   1 
ATOM   5978 C CB  . PHE A 1 1211 ? 154.274 162.897 111.921 1.00 48.55  ? 1211 PHE A CB  1 
ATOM   5979 C CG  . PHE A 1 1211 ? 155.246 162.513 110.846 1.00 49.58  ? 1211 PHE A CG  1 
ATOM   5980 C CD1 . PHE A 1 1211 ? 154.932 162.682 109.512 1.00 50.39  ? 1211 PHE A CD1 1 
ATOM   5981 C CD2 . PHE A 1 1211 ? 156.478 161.982 111.173 1.00 56.51  ? 1211 PHE A CD2 1 
ATOM   5982 C CE1 . PHE A 1 1211 ? 155.828 162.327 108.528 1.00 54.36  ? 1211 PHE A CE1 1 
ATOM   5983 C CE2 . PHE A 1 1211 ? 157.374 161.628 110.193 1.00 45.30  ? 1211 PHE A CE2 1 
ATOM   5984 C CZ  . PHE A 1 1211 ? 157.049 161.801 108.870 1.00 48.99  ? 1211 PHE A CZ  1 
ATOM   5985 N N   . THR A 1 1212 ? 151.102 162.774 111.861 1.00 65.55  ? 1212 THR A N   1 
ATOM   5986 C CA  . THR A 1 1212 ? 149.862 162.126 111.450 1.00 60.20  ? 1212 THR A CA  1 
ATOM   5987 C C   . THR A 1 1212 ? 148.987 163.080 110.647 1.00 60.77  ? 1212 THR A C   1 
ATOM   5988 O O   . THR A 1 1212 ? 148.404 162.698 109.628 1.00 71.10  ? 1212 THR A O   1 
ATOM   5989 C CB  . THR A 1 1212 ? 149.112 161.608 112.676 1.00 63.62  ? 1212 THR A CB  1 
ATOM   5990 O OG1 . THR A 1 1212 ? 149.905 160.615 113.335 1.00 68.64  ? 1212 THR A OG1 1 
ATOM   5991 C CG2 . THR A 1 1212 ? 147.789 160.994 112.263 1.00 70.04  ? 1212 THR A CG2 1 
ATOM   5992 N N   . PHE A 1 1213 ? 148.883 164.332 111.097 1.00 64.32  ? 1213 PHE A N   1 
ATOM   5993 C CA  . PHE A 1 1213 ? 148.104 165.321 110.358 1.00 67.15  ? 1213 PHE A CA  1 
ATOM   5994 C C   . PHE A 1 1213 ? 148.683 165.548 108.970 1.00 67.99  ? 1213 PHE A C   1 
ATOM   5995 O O   . PHE A 1 1213 ? 147.945 165.634 107.982 1.00 72.16  ? 1213 PHE A O   1 
ATOM   5996 C CB  . PHE A 1 1213 ? 148.051 166.638 111.131 1.00 64.29  ? 1213 PHE A CB  1 
ATOM   5997 C CG  . PHE A 1 1213 ? 147.062 166.640 112.253 1.00 70.24  ? 1213 PHE A CG  1 
ATOM   5998 C CD1 . PHE A 1 1213 ? 145.723 166.882 112.010 1.00 69.97  ? 1213 PHE A CD1 1 
ATOM   5999 C CD2 . PHE A 1 1213 ? 147.469 166.401 113.552 1.00 72.31  ? 1213 PHE A CD2 1 
ATOM   6000 C CE1 . PHE A 1 1213 ? 144.809 166.885 113.041 1.00 72.02  ? 1213 PHE A CE1 1 
ATOM   6001 C CE2 . PHE A 1 1213 ? 146.559 166.403 114.589 1.00 70.02  ? 1213 PHE A CE2 1 
ATOM   6002 C CZ  . PHE A 1 1213 ? 145.228 166.645 114.332 1.00 71.88  ? 1213 PHE A CZ  1 
ATOM   6003 N N   . PHE A 1 1214 ? 150.009 165.652 108.879 1.00 67.79  ? 1214 PHE A N   1 
ATOM   6004 C CA  . PHE A 1 1214 ? 150.651 165.853 107.586 1.00 65.37  ? 1214 PHE A CA  1 
ATOM   6005 C C   . PHE A 1 1214 ? 150.371 164.685 106.650 1.00 70.99  ? 1214 PHE A C   1 
ATOM   6006 O O   . PHE A 1 1214 ? 150.025 164.875 105.480 1.00 76.35  ? 1214 PHE A O   1 
ATOM   6007 C CB  . PHE A 1 1214 ? 152.155 166.046 107.772 1.00 63.58  ? 1214 PHE A CB  1 
ATOM   6008 C CG  . PHE A 1 1214 ? 152.935 165.977 106.492 1.00 69.71  ? 1214 PHE A CG  1 
ATOM   6009 C CD1 . PHE A 1 1214 ? 152.958 167.051 105.623 1.00 70.63  ? 1214 PHE A CD1 1 
ATOM   6010 C CD2 . PHE A 1 1214 ? 153.647 164.840 106.160 1.00 70.58  ? 1214 PHE A CD2 1 
ATOM   6011 C CE1 . PHE A 1 1214 ? 153.673 166.990 104.447 1.00 68.29  ? 1214 PHE A CE1 1 
ATOM   6012 C CE2 . PHE A 1 1214 ? 154.363 164.775 104.985 1.00 69.58  ? 1214 PHE A CE2 1 
ATOM   6013 C CZ  . PHE A 1 1214 ? 154.376 165.851 104.129 1.00 67.34  ? 1214 PHE A CZ  1 
ATOM   6014 N N   . LEU A 1 1215 ? 150.515 163.460 107.158 1.00 70.22  ? 1215 LEU A N   1 
ATOM   6015 C CA  . LEU A 1 1215 ? 150.292 162.284 106.324 1.00 66.02  ? 1215 LEU A CA  1 
ATOM   6016 C C   . LEU A 1 1215 ? 148.838 162.187 105.882 1.00 72.48  ? 1215 LEU A C   1 
ATOM   6017 O O   . LEU A 1 1215 ? 148.548 161.850 104.729 1.00 76.89  ? 1215 LEU A O   1 
ATOM   6018 C CB  . LEU A 1 1215 ? 150.720 161.024 107.075 1.00 67.03  ? 1215 LEU A CB  1 
ATOM   6019 C CG  . LEU A 1 1215 ? 152.222 160.922 107.330 1.00 66.77  ? 1215 LEU A CG  1 
ATOM   6020 C CD1 . LEU A 1 1215 ? 152.558 159.656 108.092 1.00 65.06  ? 1215 LEU A CD1 1 
ATOM   6021 C CD2 . LEU A 1 1215 ? 152.977 160.974 106.018 1.00 67.99  ? 1215 LEU A CD2 1 
ATOM   6022 N N   . ASN A 1 1216 ? 147.904 162.476 106.789 1.00 73.59  ? 1216 ASN A N   1 
ATOM   6023 C CA  . ASN A 1 1216 ? 146.490 162.430 106.435 1.00 69.55  ? 1216 ASN A CA  1 
ATOM   6024 C C   . ASN A 1 1216 ? 146.154 163.475 105.380 1.00 75.00  ? 1216 ASN A C   1 
ATOM   6025 O O   . ASN A 1 1216 ? 145.415 163.199 104.429 1.00 80.29  ? 1216 ASN A O   1 
ATOM   6026 C CB  . ASN A 1 1216 ? 145.631 162.628 107.683 1.00 71.79  ? 1216 ASN A CB  1 
ATOM   6027 C CG  . ASN A 1 1216 ? 145.730 161.466 108.647 1.00 72.17  ? 1216 ASN A CG  1 
ATOM   6028 O OD1 . ASN A 1 1216 ? 146.554 160.570 108.474 1.00 70.98  ? 1216 ASN A OD1 1 
ATOM   6029 N ND2 . ASN A 1 1216 ? 144.891 161.478 109.675 1.00 72.99  ? 1216 ASN A ND2 1 
ATOM   6030 N N   . LYS A 1 1217 ? 146.685 164.688 105.537 1.00 80.31  ? 1217 LYS A N   1 
ATOM   6031 C CA  . LYS A 1 1217 ? 146.379 165.756 104.592 1.00 81.36  ? 1217 LYS A CA  1 
ATOM   6032 C C   . LYS A 1 1217 ? 146.930 165.442 103.206 1.00 80.83  ? 1217 LYS A C   1 
ATOM   6033 O O   . LYS A 1 1217 ? 146.261 165.672 102.193 1.00 83.36  ? 1217 LYS A O   1 
ATOM   6034 C CB  . LYS A 1 1217 ? 146.932 167.084 105.106 1.00 79.64  ? 1217 LYS A CB  1 
ATOM   6035 C CG  . LYS A 1 1217 ? 146.699 168.253 104.168 1.00 83.11  ? 1217 LYS A CG  1 
ATOM   6036 C CD  . LYS A 1 1217 ? 145.219 168.451 103.893 1.00 85.86  ? 1217 LYS A CD  1 
ATOM   6037 C CE  . LYS A 1 1217 ? 144.993 169.554 102.875 1.00 86.37  ? 1217 LYS A CE  1 
ATOM   6038 N NZ  . LYS A 1 1217 ? 145.649 169.245 101.575 1.00 85.25  ? 1217 LYS A NZ  1 
ATOM   6039 N N   . ASN A 1 1218 ? 148.149 164.915 103.140 1.00 80.82  ? 1218 ASN A N   1 
ATOM   6040 C CA  . ASN A 1 1218 ? 148.837 164.669 101.875 1.00 82.12  ? 1218 ASN A CA  1 
ATOM   6041 C C   . ASN A 1 1218 ? 149.141 163.181 101.754 1.00 83.48  ? 1218 ASN A C   1 
ATOM   6042 O O   . ASN A 1 1218 ? 150.004 162.655 102.461 1.00 88.48  ? 1218 ASN A O   1 
ATOM   6043 C CB  . ASN A 1 1218 ? 150.117 165.494 101.789 1.00 80.80  ? 1218 ASN A CB  1 
ATOM   6044 C CG  . ASN A 1 1218 ? 149.885 166.957 102.086 1.00 84.88  ? 1218 ASN A CG  1 
ATOM   6045 O OD1 . ASN A 1 1218 ? 148.829 167.504 101.777 1.00 86.07  ? 1218 ASN A OD1 1 
ATOM   6046 N ND2 . ASN A 1 1218 ? 150.873 167.599 102.693 1.00 86.55  ? 1218 ASN A ND2 1 
ATOM   6047 N N   . LYS A 1 1219 ? 148.437 162.505 100.851 1.00 93.29  ? 1219 LYS A N   1 
ATOM   6048 C CA  . LYS A 1 1219 ? 148.724 161.114 100.524 1.00 94.82  ? 1219 LYS A CA  1 
ATOM   6049 C C   . LYS A 1 1219 ? 149.107 160.925 99.065  1.00 96.60  ? 1219 LYS A C   1 
ATOM   6050 O O   . LYS A 1 1219 ? 150.068 160.210 98.766  1.00 93.75  ? 1219 LYS A O   1 
ATOM   6051 C CB  . LYS A 1 1219 ? 147.520 160.226 100.866 1.00 94.98  ? 1219 LYS A CB  1 
ATOM   6052 C CG  . LYS A 1 1219 ? 147.230 160.126 102.353 1.00 94.22  ? 1219 LYS A CG  1 
ATOM   6053 C CD  . LYS A 1 1219 ? 146.159 159.089 102.637 1.00 92.52  ? 1219 LYS A CD  1 
ATOM   6054 C CE  . LYS A 1 1219 ? 146.578 157.718 102.135 1.00 92.91  ? 1219 LYS A CE  1 
ATOM   6055 N NZ  . LYS A 1 1219 ? 145.539 156.687 102.403 1.00 93.13  ? 1219 LYS A NZ  1 
ATOM   6056 N N   . SER A 1 1220 ? 148.372 161.549 98.143  1.00 107.44 ? 1220 SER A N   1 
ATOM   6057 C CA  . SER A 1 1220 ? 148.704 161.434 96.727  1.00 107.51 ? 1220 SER A CA  1 
ATOM   6058 C C   . SER A 1 1220 ? 150.048 162.082 96.420  1.00 109.39 ? 1220 SER A C   1 
ATOM   6059 O O   . SER A 1 1220 ? 150.827 161.562 95.613  1.00 111.31 ? 1220 SER A O   1 
ATOM   6060 C CB  . SER A 1 1220 ? 147.601 162.063 95.879  1.00 107.19 ? 1220 SER A CB  1 
ATOM   6061 O OG  . SER A 1 1220 ? 147.430 163.431 96.208  1.00 107.65 ? 1220 SER A OG  1 
ATOM   6062 N N   . SER A 1 1221 ? 150.333 163.222 97.053  1.00 102.28 ? 1221 SER A N   1 
ATOM   6063 C CA  . SER A 1 1221 ? 151.573 163.940 96.774  1.00 101.92 ? 1221 SER A CA  1 
ATOM   6064 C C   . SER A 1 1221 ? 152.794 163.122 97.176  1.00 100.19 ? 1221 SER A C   1 
ATOM   6065 O O   . SER A 1 1221 ? 153.865 163.252 96.573  1.00 97.91  ? 1221 SER A O   1 
ATOM   6066 C CB  . SER A 1 1221 ? 151.569 165.286 97.497  1.00 100.53 ? 1221 SER A CB  1 
ATOM   6067 O OG  . SER A 1 1221 ? 150.407 166.029 97.177  1.00 99.91  ? 1221 SER A OG  1 
ATOM   6068 N N   . LEU A 1 1222 ? 152.653 162.273 98.190  1.00 94.92  ? 1222 LEU A N   1 
ATOM   6069 C CA  . LEU A 1 1222 ? 153.769 161.487 98.694  1.00 95.40  ? 1222 LEU A CA  1 
ATOM   6070 C C   . LEU A 1 1222 ? 153.907 160.135 98.006  1.00 98.02  ? 1222 LEU A C   1 
ATOM   6071 O O   . LEU A 1 1222 ? 154.743 159.329 98.428  1.00 98.02  ? 1222 LEU A O   1 
ATOM   6072 C CB  . LEU A 1 1222 ? 153.623 161.288 100.204 1.00 93.03  ? 1222 LEU A CB  1 
ATOM   6073 C CG  . LEU A 1 1222 ? 153.375 162.567 101.005 1.00 91.65  ? 1222 LEU A CG  1 
ATOM   6074 C CD1 . LEU A 1 1222 ? 153.319 162.269 102.491 1.00 95.31  ? 1222 LEU A CD1 1 
ATOM   6075 C CD2 . LEU A 1 1222 ? 154.444 163.600 100.708 1.00 90.57  ? 1222 LEU A CD2 1 
ATOM   6076 N N   . ARG A 1 1223 ? 153.112 159.867 96.968  1.00 107.09 ? 1223 ARG A N   1 
ATOM   6077 C CA  . ARG A 1 1223 ? 153.196 158.582 96.280  1.00 106.95 ? 1223 ARG A CA  1 
ATOM   6078 C C   . ARG A 1 1223 ? 154.551 158.395 95.610  1.00 105.74 ? 1223 ARG A C   1 
ATOM   6079 O O   . ARG A 1 1223 ? 155.030 157.264 95.468  1.00 104.41 ? 1223 ARG A O   1 
ATOM   6080 C CB  . ARG A 1 1223 ? 152.073 158.468 95.250  1.00 106.85 ? 1223 ARG A CB  1 
ATOM   6081 C CG  . ARG A 1 1223 ? 150.695 158.276 95.855  1.00 105.30 ? 1223 ARG A CG  1 
ATOM   6082 C CD  . ARG A 1 1223 ? 150.538 156.875 96.418  1.00 108.25 ? 1223 ARG A CD  1 
ATOM   6083 N NE  . ARG A 1 1223 ? 150.720 155.857 95.390  1.00 109.30 ? 1223 ARG A NE  1 
ATOM   6084 C CZ  . ARG A 1 1223 ? 150.580 154.554 95.591  1.00 107.81 ? 1223 ARG A CZ  1 
ATOM   6085 N NH1 . ARG A 1 1223 ? 150.254 154.068 96.778  1.00 106.05 ? 1223 ARG A NH1 1 
ATOM   6086 N NH2 . ARG A 1 1223 ? 150.769 153.717 94.575  1.00 107.38 ? 1223 ARG A NH2 1 
ATOM   6087 N N   . LYS A 1 1224 ? 155.183 159.491 95.187  1.00 97.86  ? 1224 LYS A N   1 
ATOM   6088 C CA  . LYS A 1 1224 ? 156.460 159.395 94.490  1.00 98.50  ? 1224 LYS A CA  1 
ATOM   6089 C C   . LYS A 1 1224 ? 157.567 158.843 95.377  1.00 99.84  ? 1224 LYS A C   1 
ATOM   6090 O O   . LYS A 1 1224 ? 158.500 158.216 94.862  1.00 97.06  ? 1224 LYS A O   1 
ATOM   6091 C CB  . LYS A 1 1224 ? 156.867 160.767 93.951  1.00 97.46  ? 1224 LYS A CB  1 
ATOM   6092 C CG  . LYS A 1 1224 ? 155.849 161.389 93.013  1.00 99.34  ? 1224 LYS A CG  1 
ATOM   6093 C CD  . LYS A 1 1224 ? 155.600 160.503 91.806  1.00 99.05  ? 1224 LYS A CD  1 
ATOM   6094 C CE  . LYS A 1 1224 ? 154.580 161.125 90.868  1.00 98.47  ? 1224 LYS A CE  1 
ATOM   6095 N NZ  . LYS A 1 1224 ? 154.303 160.254 89.692  1.00 98.57  ? 1224 LYS A NZ  1 
ATOM   6096 N N   . GLU A 1 1225 ? 157.486 159.065 96.690  1.00 93.82  ? 1225 GLU A N   1 
ATOM   6097 C CA  . GLU A 1 1225 ? 158.502 158.610 97.641  1.00 89.79  ? 1225 GLU A CA  1 
ATOM   6098 C C   . GLU A 1 1225 ? 159.875 159.187 97.313  1.00 90.17  ? 1225 GLU A C   1 
ATOM   6099 O O   . GLU A 1 1225 ? 160.906 158.559 97.563  1.00 90.15  ? 1225 GLU A O   1 
ATOM   6100 C CB  . GLU A 1 1225 ? 158.562 157.083 97.707  1.00 88.03  ? 1225 GLU A CB  1 
ATOM   6101 C CG  . GLU A 1 1225 ? 157.215 156.421 97.918  1.00 89.14  ? 1225 GLU A CG  1 
ATOM   6102 C CD  . GLU A 1 1225 ? 157.338 154.947 98.240  1.00 92.60  ? 1225 GLU A CD  1 
ATOM   6103 O OE1 . GLU A 1 1225 ? 158.205 154.588 99.064  1.00 92.96  ? 1225 GLU A OE1 1 
ATOM   6104 O OE2 . GLU A 1 1225 ? 156.573 154.146 97.665  1.00 93.05  ? 1225 GLU A OE2 1 
ATOM   6105 N N   . ASN A 1 1226 ? 159.896 160.384 96.748  1.00 90.43  ? 1226 ASN A N   1 
ATOM   6106 C CA  . ASN A 1 1226 ? 161.155 161.056 96.456  1.00 89.36  ? 1226 ASN A CA  1 
ATOM   6107 C C   . ASN A 1 1226 ? 161.603 161.851 97.677  1.00 91.00  ? 1226 ASN A C   1 
ATOM   6108 O O   . ASN A 1 1226 ? 160.840 162.685 98.175  1.00 93.50  ? 1226 ASN A O   1 
ATOM   6109 C CB  . ASN A 1 1226 ? 161.002 161.980 95.254  1.00 88.27  ? 1226 ASN A CB  1 
ATOM   6110 C CG  . ASN A 1 1226 ? 162.331 162.455 94.711  1.00 91.99  ? 1226 ASN A CG  1 
ATOM   6111 O OD1 . ASN A 1 1226 ? 163.332 161.743 94.778  1.00 93.17  ? 1226 ASN A OD1 1 
ATOM   6112 N ND2 . ASN A 1 1226 ? 162.350 163.666 94.167  1.00 91.36  ? 1226 ASN A ND2 1 
ATOM   6113 N N   . PRO A 1 1227 ? 162.815 161.616 98.193  1.00 86.81  ? 1227 PRO A N   1 
ATOM   6114 C CA  . PRO A 1 1227 ? 163.238 162.333 99.408  1.00 85.08  ? 1227 PRO A CA  1 
ATOM   6115 C C   . PRO A 1 1227 ? 163.184 163.843 99.267  1.00 86.63  ? 1227 PRO A C   1 
ATOM   6116 O O   . PRO A 1 1227 ? 162.744 164.533 100.196 1.00 86.23  ? 1227 PRO A O   1 
ATOM   6117 C CB  . PRO A 1 1227 ? 164.674 161.837 99.621  1.00 83.10  ? 1227 PRO A CB  1 
ATOM   6118 C CG  . PRO A 1 1227 ? 164.739 160.534 98.910  1.00 83.85  ? 1227 PRO A CG  1 
ATOM   6119 C CD  . PRO A 1 1227 ? 163.837 160.667 97.724  1.00 84.56  ? 1227 PRO A CD  1 
ATOM   6120 N N   . GLN A 1 1228 ? 163.603 164.377 98.119  1.00 87.14  ? 1228 GLN A N   1 
ATOM   6121 C CA  . GLN A 1 1228 ? 163.510 165.816 97.905  1.00 83.05  ? 1228 GLN A CA  1 
ATOM   6122 C C   . GLN A 1 1228 ? 162.059 166.271 97.880  1.00 84.14  ? 1228 GLN A C   1 
ATOM   6123 O O   . GLN A 1 1228 ? 161.713 167.304 98.465  1.00 86.65  ? 1228 GLN A O   1 
ATOM   6124 C CB  . GLN A 1 1228 ? 164.216 166.201 96.607  1.00 82.68  ? 1228 GLN A CB  1 
ATOM   6125 C CG  . GLN A 1 1228 ? 164.129 167.679 96.279  1.00 83.12  ? 1228 GLN A CG  1 
ATOM   6126 C CD  . GLN A 1 1228 ? 164.820 168.027 94.979  1.00 87.96  ? 1228 GLN A CD  1 
ATOM   6127 O OE1 . GLN A 1 1228 ? 165.517 167.199 94.393  1.00 86.69  ? 1228 GLN A OE1 1 
ATOM   6128 N NE2 . GLN A 1 1228 ? 164.629 169.257 94.518  1.00 87.87  ? 1228 GLN A NE2 1 
ATOM   6129 N N   . GLU A 1 1229 ? 161.193 165.510 97.206  1.00 84.37  ? 1229 GLU A N   1 
ATOM   6130 C CA  . GLU A 1 1229 ? 159.777 165.854 97.176  1.00 82.54  ? 1229 GLU A CA  1 
ATOM   6131 C C   . GLU A 1 1229 ? 159.171 165.803 98.570  1.00 83.20  ? 1229 GLU A C   1 
ATOM   6132 O O   . GLU A 1 1229 ? 158.392 166.684 98.947  1.00 85.12  ? 1229 GLU A O   1 
ATOM   6133 C CB  . GLU A 1 1229 ? 159.026 164.916 96.233  1.00 83.38  ? 1229 GLU A CB  1 
ATOM   6134 C CG  . GLU A 1 1229 ? 159.242 165.212 94.761  1.00 88.50  ? 1229 GLU A CG  1 
ATOM   6135 C CD  . GLU A 1 1229 ? 158.551 166.486 94.315  1.00 88.29  ? 1229 GLU A CD  1 
ATOM   6136 O OE1 . GLU A 1 1229 ? 157.674 166.981 95.053  1.00 84.75  ? 1229 GLU A OE1 1 
ATOM   6137 O OE2 . GLU A 1 1229 ? 158.884 166.992 93.223  1.00 87.29  ? 1229 GLU A OE2 1 
ATOM   6138 N N   . PHE A 1 1230 ? 159.518 164.777 99.349  1.00 74.37  ? 1230 PHE A N   1 
ATOM   6139 C CA  . PHE A 1 1230 ? 159.013 164.678 100.714 1.00 70.93  ? 1230 PHE A CA  1 
ATOM   6140 C C   . PHE A 1 1230 ? 159.458 165.872 101.544 1.00 72.44  ? 1230 PHE A C   1 
ATOM   6141 O O   . PHE A 1 1230 ? 158.656 166.478 102.264 1.00 75.06  ? 1230 PHE A O   1 
ATOM   6142 C CB  . PHE A 1 1230 ? 159.486 163.369 101.348 1.00 71.46  ? 1230 PHE A CB  1 
ATOM   6143 C CG  . PHE A 1 1230 ? 159.154 163.239 102.806 1.00 68.35  ? 1230 PHE A CG  1 
ATOM   6144 C CD1 . PHE A 1 1230 ? 157.922 162.761 103.207 1.00 70.74  ? 1230 PHE A CD1 1 
ATOM   6145 C CD2 . PHE A 1 1230 ? 160.080 163.580 103.773 1.00 64.11  ? 1230 PHE A CD2 1 
ATOM   6146 C CE1 . PHE A 1 1230 ? 157.618 162.637 104.545 1.00 69.92  ? 1230 PHE A CE1 1 
ATOM   6147 C CE2 . PHE A 1 1230 ? 159.778 163.458 105.110 1.00 64.87  ? 1230 PHE A CE2 1 
ATOM   6148 C CZ  . PHE A 1 1230 ? 158.547 162.985 105.496 1.00 66.52  ? 1230 PHE A CZ  1 
ATOM   6149 N N   . TYR A 1 1231 ? 160.738 166.235 101.442 1.00 68.81  ? 1231 TYR A N   1 
ATOM   6150 C CA  . TYR A 1 1231 ? 161.250 167.368 102.203 1.00 65.87  ? 1231 TYR A CA  1 
ATOM   6151 C C   . TYR A 1 1231 ? 160.541 168.656 101.815 1.00 64.59  ? 1231 TYR A C   1 
ATOM   6152 O O   . TYR A 1 1231 ? 160.120 169.431 102.681 1.00 67.35  ? 1231 TYR A O   1 
ATOM   6153 C CB  . TYR A 1 1231 ? 162.757 167.499 101.993 1.00 65.66  ? 1231 TYR A CB  1 
ATOM   6154 C CG  . TYR A 1 1231 ? 163.330 168.819 102.452 1.00 66.79  ? 1231 TYR A CG  1 
ATOM   6155 C CD1 . TYR A 1 1231 ? 163.516 169.086 103.798 1.00 69.10  ? 1231 TYR A CD1 1 
ATOM   6156 C CD2 . TYR A 1 1231 ? 163.693 169.794 101.536 1.00 66.90  ? 1231 TYR A CD2 1 
ATOM   6157 C CE1 . TYR A 1 1231 ? 164.041 170.288 104.220 1.00 67.05  ? 1231 TYR A CE1 1 
ATOM   6158 C CE2 . TYR A 1 1231 ? 164.219 170.999 101.948 1.00 66.16  ? 1231 TYR A CE2 1 
ATOM   6159 C CZ  . TYR A 1 1231 ? 164.391 171.241 103.291 1.00 66.75  ? 1231 TYR A CZ  1 
ATOM   6160 O OH  . TYR A 1 1231 ? 164.915 172.441 103.706 1.00 65.81  ? 1231 TYR A OH  1 
ATOM   6161 N N   . GLU A 1 1232 ? 160.393 168.900 100.512 1.00 75.56  ? 1232 GLU A N   1 
ATOM   6162 C CA  . GLU A 1 1232 ? 159.766 170.139 100.067 1.00 78.45  ? 1232 GLU A CA  1 
ATOM   6163 C C   . GLU A 1 1232 ? 158.301 170.200 100.479 1.00 82.24  ? 1232 GLU A C   1 
ATOM   6164 O O   . GLU A 1 1232 ? 157.820 171.249 100.924 1.00 86.68  ? 1232 GLU A O   1 
ATOM   6165 C CB  . GLU A 1 1232 ? 159.910 170.287 98.554  1.00 79.52  ? 1232 GLU A CB  1 
ATOM   6166 C CG  . GLU A 1 1232 ? 161.346 170.443 98.091  1.00 80.10  ? 1232 GLU A CG  1 
ATOM   6167 C CD  . GLU A 1 1232 ? 161.454 170.713 96.606  1.00 85.76  ? 1232 GLU A CD  1 
ATOM   6168 O OE1 . GLU A 1 1232 ? 160.425 171.053 95.986  1.00 87.26  ? 1232 GLU A OE1 1 
ATOM   6169 O OE2 . GLU A 1 1232 ? 162.568 170.585 96.057  1.00 88.13  ? 1232 GLU A OE2 1 
ATOM   6170 N N   . ILE A 1 1233 ? 157.574 169.090 100.340 1.00 74.06  ? 1233 ILE A N   1 
ATOM   6171 C CA  . ILE A 1 1233 ? 156.164 169.082 100.711 1.00 71.01  ? 1233 ILE A CA  1 
ATOM   6172 C C   . ILE A 1 1233 ? 156.003 169.293 102.210 1.00 74.10  ? 1233 ILE A C   1 
ATOM   6173 O O   . ILE A 1 1233 ? 155.135 170.055 102.650 1.00 74.61  ? 1233 ILE A O   1 
ATOM   6174 C CB  . ILE A 1 1233 ? 155.492 167.780 100.243 1.00 73.05  ? 1233 ILE A CB  1 
ATOM   6175 C CG1 . ILE A 1 1233 ? 155.440 167.731 98.716  1.00 76.36  ? 1233 ILE A CG1 1 
ATOM   6176 C CG2 . ILE A 1 1233 ? 154.094 167.663 100.820 1.00 71.49  ? 1233 ILE A CG2 1 
ATOM   6177 C CD1 . ILE A 1 1233 ? 154.757 168.924 98.089  1.00 73.23  ? 1233 ILE A CD1 1 
ATOM   6178 N N   . PHE A 1 1234 ? 156.833 168.629 103.019 1.00 70.52  ? 1234 PHE A N   1 
ATOM   6179 C CA  . PHE A 1 1234 ? 156.753 168.815 104.464 1.00 65.78  ? 1234 PHE A CA  1 
ATOM   6180 C C   . PHE A 1 1234 ? 157.075 170.253 104.848 1.00 67.69  ? 1234 PHE A C   1 
ATOM   6181 O O   . PHE A 1 1234 ? 156.401 170.842 105.703 1.00 67.94  ? 1234 PHE A O   1 
ATOM   6182 C CB  . PHE A 1 1234 ? 157.700 167.847 105.170 1.00 60.93  ? 1234 PHE A CB  1 
ATOM   6183 C CG  . PHE A 1 1234 ? 157.225 167.414 106.525 1.00 64.59  ? 1234 PHE A CG  1 
ATOM   6184 C CD1 . PHE A 1 1234 ? 157.006 168.340 107.526 1.00 66.41  ? 1234 PHE A CD1 1 
ATOM   6185 C CD2 . PHE A 1 1234 ? 157.008 166.080 106.799 1.00 67.45  ? 1234 PHE A CD2 1 
ATOM   6186 C CE1 . PHE A 1 1234 ? 156.570 167.943 108.770 1.00 62.12  ? 1234 PHE A CE1 1 
ATOM   6187 C CE2 . PHE A 1 1234 ? 156.574 165.679 108.042 1.00 68.07  ? 1234 PHE A CE2 1 
ATOM   6188 C CZ  . PHE A 1 1234 ? 156.355 166.613 109.028 1.00 58.80  ? 1234 PHE A CZ  1 
ATOM   6189 N N   . ALA A 1 1235 ? 158.101 170.836 104.225 1.00 72.24  ? 1235 ALA A N   1 
ATOM   6190 C CA  . ALA A 1 1235 ? 158.459 172.215 104.529 1.00 66.38  ? 1235 ALA A CA  1 
ATOM   6191 C C   . ALA A 1 1235 ? 157.334 173.170 104.159 1.00 73.67  ? 1235 ALA A C   1 
ATOM   6192 O O   . ALA A 1 1235 ? 157.008 174.082 104.927 1.00 76.79  ? 1235 ALA A O   1 
ATOM   6193 C CB  . ALA A 1 1235 ? 159.747 172.593 103.801 1.00 61.63  ? 1235 ALA A CB  1 
ATOM   6194 N N   . ASN A 1 1236 ? 156.725 172.975 102.988 1.00 70.28  ? 1236 ASN A N   1 
ATOM   6195 C CA  . ASN A 1 1236 ? 155.626 173.840 102.578 1.00 67.87  ? 1236 ASN A CA  1 
ATOM   6196 C C   . ASN A 1 1236 ? 154.430 173.688 103.506 1.00 76.30  ? 1236 ASN A C   1 
ATOM   6197 O O   . ASN A 1 1236 ? 153.774 174.677 103.851 1.00 80.76  ? 1236 ASN A O   1 
ATOM   6198 C CB  . ASN A 1 1236 ? 155.229 173.538 101.136 1.00 70.12  ? 1236 ASN A CB  1 
ATOM   6199 C CG  . ASN A 1 1236 ? 156.295 173.944 100.147 1.00 76.39  ? 1236 ASN A CG  1 
ATOM   6200 O OD1 . ASN A 1 1236 ? 157.108 174.825 100.422 1.00 79.81  ? 1236 ASN A OD1 1 
ATOM   6201 N ND2 . ASN A 1 1236 ? 156.299 173.304 98.984  1.00 78.01  ? 1236 ASN A ND2 1 
ATOM   6202 N N   . TRP A 1 1237 ? 154.125 172.456 103.915 1.00 72.49  ? 1237 TRP A N   1 
ATOM   6203 C CA  . TRP A 1 1237 ? 153.009 172.242 104.829 1.00 71.37  ? 1237 TRP A CA  1 
ATOM   6204 C C   . TRP A 1 1237 ? 153.262 172.915 106.171 1.00 69.92  ? 1237 TRP A C   1 
ATOM   6205 O O   . TRP A 1 1237 ? 152.355 173.524 106.748 1.00 72.31  ? 1237 TRP A O   1 
ATOM   6206 C CB  . TRP A 1 1237 ? 152.760 170.747 105.012 1.00 68.74  ? 1237 TRP A CB  1 
ATOM   6207 C CG  . TRP A 1 1237 ? 151.631 170.448 105.936 1.00 72.24  ? 1237 TRP A CG  1 
ATOM   6208 C CD1 . TRP A 1 1237 ? 150.303 170.455 105.635 1.00 73.03  ? 1237 TRP A CD1 1 
ATOM   6209 C CD2 . TRP A 1 1237 ? 151.727 170.095 107.318 1.00 69.64  ? 1237 TRP A CD2 1 
ATOM   6210 N NE1 . TRP A 1 1237 ? 149.565 170.131 106.745 1.00 74.49  ? 1237 TRP A NE1 1 
ATOM   6211 C CE2 . TRP A 1 1237 ? 150.417 169.904 107.791 1.00 71.19  ? 1237 TRP A CE2 1 
ATOM   6212 C CE3 . TRP A 1 1237 ? 152.795 169.922 108.201 1.00 69.00  ? 1237 TRP A CE3 1 
ATOM   6213 C CZ2 . TRP A 1 1237 ? 150.146 169.549 109.107 1.00 70.97  ? 1237 TRP A CZ2 1 
ATOM   6214 C CZ3 . TRP A 1 1237 ? 152.523 169.569 109.505 1.00 69.29  ? 1237 TRP A CZ3 1 
ATOM   6215 C CH2 . TRP A 1 1237 ? 151.210 169.387 109.947 1.00 72.70  ? 1237 TRP A CH2 1 
ATOM   6216 N N   . LEU A 1 1238 ? 154.489 172.819 106.684 1.00 64.96  ? 1238 LEU A N   1 
ATOM   6217 C CA  . LEU A 1 1238 ? 154.817 173.497 107.933 1.00 63.64  ? 1238 LEU A CA  1 
ATOM   6218 C C   . LEU A 1 1238 ? 154.752 175.011 107.789 1.00 70.62  ? 1238 LEU A C   1 
ATOM   6219 O O   . LEU A 1 1238 ? 154.293 175.700 108.705 1.00 74.92  ? 1238 LEU A O   1 
ATOM   6220 C CB  . LEU A 1 1238 ? 156.203 173.076 108.415 1.00 64.91  ? 1238 LEU A CB  1 
ATOM   6221 C CG  . LEU A 1 1238 ? 156.336 171.667 108.985 1.00 65.05  ? 1238 LEU A CG  1 
ATOM   6222 C CD1 . LEU A 1 1238 ? 157.783 171.377 109.323 1.00 62.89  ? 1238 LEU A CD1 1 
ATOM   6223 C CD2 . LEU A 1 1238 ? 155.464 171.511 110.213 1.00 63.57  ? 1238 LEU A CD2 1 
ATOM   6224 N N   . LYS A 1 1239 ? 155.208 175.542 106.657 1.00 77.42  ? 1239 LYS A N   1 
ATOM   6225 C CA  . LYS A 1 1239 ? 155.300 176.981 106.461 1.00 77.12  ? 1239 LYS A CA  1 
ATOM   6226 C C   . LYS A 1 1239 ? 153.962 177.644 106.164 1.00 79.14  ? 1239 LYS A C   1 
ATOM   6227 O O   . LYS A 1 1239 ? 153.758 178.795 106.563 1.00 78.18  ? 1239 LYS A O   1 
ATOM   6228 C CB  . LYS A 1 1239 ? 156.279 177.282 105.322 1.00 74.31  ? 1239 LYS A CB  1 
ATOM   6229 C CG  . LYS A 1 1239 ? 156.530 178.754 105.067 1.00 78.78  ? 1239 LYS A CG  1 
ATOM   6230 C CD  . LYS A 1 1239 ? 157.472 178.941 103.892 1.00 78.74  ? 1239 LYS A CD  1 
ATOM   6231 C CE  . LYS A 1 1239 ? 157.733 180.410 103.618 1.00 79.79  ? 1239 LYS A CE  1 
ATOM   6232 N NZ  . LYS A 1 1239 ? 158.659 180.596 102.468 1.00 79.53  ? 1239 LYS A NZ  1 
ATOM   6233 N N   . LYS A 1 1240 ? 153.046 176.952 105.489 1.00 77.79  ? 1240 LYS A N   1 
ATOM   6234 C CA  . LYS A 1 1240 ? 151.831 177.572 104.976 1.00 80.07  ? 1240 LYS A CA  1 
ATOM   6235 C C   . LYS A 1 1240 ? 150.579 177.121 105.717 1.00 80.26  ? 1240 LYS A C   1 
ATOM   6236 O O   . LYS A 1 1240 ? 149.754 177.956 106.096 1.00 85.04  ? 1240 LYS A O   1 
ATOM   6237 C CB  . LYS A 1 1240 ? 151.699 177.277 103.477 1.00 79.61  ? 1240 LYS A CB  1 
ATOM   6238 C CG  . LYS A 1 1240 ? 152.916 177.678 102.665 1.00 78.40  ? 1240 LYS A CG  1 
ATOM   6239 C CD  . LYS A 1 1240 ? 152.743 177.322 101.200 1.00 80.97  ? 1240 LYS A CD  1 
ATOM   6240 C CE  . LYS A 1 1240 ? 153.979 177.687 100.399 1.00 81.82  ? 1240 LYS A CE  1 
ATOM   6241 N NZ  . LYS A 1 1240 ? 153.830 177.340 98.960  1.00 78.17  ? 1240 LYS A NZ  1 
ATOM   6242 N N   . ASP A 1 1241 ? 150.407 175.817 105.924 1.00 76.85  ? 1241 ASP A N   1 
ATOM   6243 C CA  . ASP A 1 1241 ? 149.180 175.310 106.524 1.00 80.76  ? 1241 ASP A CA  1 
ATOM   6244 C C   . ASP A 1 1241 ? 149.042 175.774 107.968 1.00 83.63  ? 1241 ASP A C   1 
ATOM   6245 O O   . ASP A 1 1241 ? 150.033 175.944 108.682 1.00 83.63  ? 1241 ASP A O   1 
ATOM   6246 C CB  . ASP A 1 1241 ? 149.151 173.783 106.462 1.00 78.24  ? 1241 ASP A CB  1 
ATOM   6247 C CG  . ASP A 1 1241 ? 147.865 173.209 107.010 1.00 82.74  ? 1241 ASP A CG  1 
ATOM   6248 O OD1 . ASP A 1 1241 ? 146.830 173.307 106.322 1.00 84.38  ? 1241 ASP A OD1 1 
ATOM   6249 O OD2 . ASP A 1 1241 ? 147.887 172.668 108.134 1.00 87.35  ? 1241 ASP A OD2 1 
ATOM   6250 N N   . PHE A 1 1242 ? 147.793 175.983 108.389 1.00 86.93  ? 1242 PHE A N   1 
ATOM   6251 C CA  . PHE A 1 1242 ? 147.520 176.427 109.753 1.00 86.52  ? 1242 PHE A CA  1 
ATOM   6252 C C   . PHE A 1 1242 ? 147.985 175.394 110.773 1.00 90.34  ? 1242 PHE A C   1 
ATOM   6253 O O   . PHE A 1 1242 ? 148.692 175.723 111.734 1.00 89.74  ? 1242 PHE A O   1 
ATOM   6254 C CB  . PHE A 1 1242 ? 146.025 176.711 109.903 1.00 86.78  ? 1242 PHE A CB  1 
ATOM   6255 C CG  . PHE A 1 1242 ? 145.622 177.161 111.275 1.00 91.18  ? 1242 PHE A CG  1 
ATOM   6256 C CD1 . PHE A 1 1242 ? 145.887 178.449 111.701 1.00 89.94  ? 1242 PHE A CD1 1 
ATOM   6257 C CD2 . PHE A 1 1242 ? 144.957 176.302 112.133 1.00 90.23  ? 1242 PHE A CD2 1 
ATOM   6258 C CE1 . PHE A 1 1242 ? 145.511 178.868 112.961 1.00 89.01  ? 1242 PHE A CE1 1 
ATOM   6259 C CE2 . PHE A 1 1242 ? 144.578 176.715 113.393 1.00 90.15  ? 1242 PHE A CE2 1 
ATOM   6260 C CZ  . PHE A 1 1242 ? 144.855 177.999 113.808 1.00 87.56  ? 1242 PHE A CZ  1 
ATOM   6261 N N   . VAL A 1 1243 ? 147.603 174.131 110.575 1.00 85.64  ? 1243 VAL A N   1 
ATOM   6262 C CA  . VAL A 1 1243 ? 148.049 173.071 111.475 1.00 85.26  ? 1243 VAL A CA  1 
ATOM   6263 C C   . VAL A 1 1243 ? 149.557 172.889 111.367 1.00 83.66  ? 1243 VAL A C   1 
ATOM   6264 O O   . VAL A 1 1243 ? 150.245 172.645 112.367 1.00 83.61  ? 1243 VAL A O   1 
ATOM   6265 C CB  . VAL A 1 1243 ? 147.291 171.766 111.173 1.00 85.49  ? 1243 VAL A CB  1 
ATOM   6266 C CG1 . VAL A 1 1243 ? 147.632 170.701 112.196 1.00 86.15  ? 1243 VAL A CG1 1 
ATOM   6267 C CG2 . VAL A 1 1243 ? 145.794 172.023 111.144 1.00 84.29  ? 1243 VAL A CG2 1 
ATOM   6268 N N   . GLY A 1 1244 ? 150.094 173.001 110.153 1.00 72.49  ? 1244 GLY A N   1 
ATOM   6269 C CA  . GLY A 1 1244 ? 151.537 172.984 109.996 1.00 70.64  ? 1244 GLY A CA  1 
ATOM   6270 C C   . GLY A 1 1244 ? 152.207 174.135 110.717 1.00 70.25  ? 1244 GLY A C   1 
ATOM   6271 O O   . GLY A 1 1244 ? 153.282 173.976 111.300 1.00 77.18  ? 1244 GLY A O   1 
ATOM   6272 N N   . ASN A 1 1245 ? 151.586 175.314 110.682 1.00 71.97  ? 1245 ASN A N   1 
ATOM   6273 C CA  . ASN A 1 1245 ? 152.121 176.438 111.438 1.00 75.25  ? 1245 ASN A CA  1 
ATOM   6274 C C   . ASN A 1 1245 ? 152.094 176.158 112.933 1.00 73.05  ? 1245 ASN A C   1 
ATOM   6275 O O   . ASN A 1 1245 ? 152.981 176.608 113.665 1.00 75.33  ? 1245 ASN A O   1 
ATOM   6276 C CB  . ASN A 1 1245 ? 151.337 177.708 111.120 1.00 74.37  ? 1245 ASN A CB  1 
ATOM   6277 C CG  . ASN A 1 1245 ? 151.938 178.936 111.761 1.00 75.30  ? 1245 ASN A CG  1 
ATOM   6278 O OD1 . ASN A 1 1245 ? 153.135 178.978 112.045 1.00 79.69  ? 1245 ASN A OD1 1 
ATOM   6279 N ND2 . ASN A 1 1245 ? 151.111 179.946 111.998 1.00 75.09  ? 1245 ASN A ND2 1 
ATOM   6280 N N   . LEU A 1 1246 ? 151.084 175.426 113.404 1.00 73.87  ? 1246 LEU A N   1 
ATOM   6281 C CA  . LEU A 1 1246 ? 151.054 175.044 114.813 1.00 78.93  ? 1246 LEU A CA  1 
ATOM   6282 C C   . LEU A 1 1246 ? 152.172 174.063 115.146 1.00 77.72  ? 1246 LEU A C   1 
ATOM   6283 O O   . LEU A 1 1246 ? 152.800 174.162 116.206 1.00 76.69  ? 1246 LEU A O   1 
ATOM   6284 C CB  . LEU A 1 1246 ? 149.695 174.443 115.166 1.00 82.05  ? 1246 LEU A CB  1 
ATOM   6285 C CG  . LEU A 1 1246 ? 148.496 175.389 115.096 1.00 82.18  ? 1246 LEU A CG  1 
ATOM   6286 C CD1 . LEU A 1 1246 ? 147.220 174.659 115.471 1.00 78.08  ? 1246 LEU A CD1 1 
ATOM   6287 C CD2 . LEU A 1 1246 ? 148.711 176.589 115.999 1.00 78.97  ? 1246 LEU A CD2 1 
ATOM   6288 N N   . PHE A 1 1247 ? 152.436 173.111 114.256 1.00 70.73  ? 1247 PHE A N   1 
ATOM   6289 C CA  . PHE A 1 1247 ? 153.387 172.039 114.526 1.00 65.08  ? 1247 PHE A CA  1 
ATOM   6290 C C   . PHE A 1 1247 ? 154.803 172.346 114.049 1.00 66.65  ? 1247 PHE A C   1 
ATOM   6291 O O   . PHE A 1 1247 ? 155.664 171.465 114.112 1.00 72.76  ? 1247 PHE A O   1 
ATOM   6292 C CB  . PHE A 1 1247 ? 152.907 170.734 113.890 1.00 59.11  ? 1247 PHE A CB  1 
ATOM   6293 C CG  . PHE A 1 1247 ? 151.818 170.052 114.659 1.00 62.52  ? 1247 PHE A CG  1 
ATOM   6294 C CD1 . PHE A 1 1247 ? 152.098 169.403 115.846 1.00 65.78  ? 1247 PHE A CD1 1 
ATOM   6295 C CD2 . PHE A 1 1247 ? 150.518 170.052 114.194 1.00 66.36  ? 1247 PHE A CD2 1 
ATOM   6296 C CE1 . PHE A 1 1247 ? 151.102 168.772 116.556 1.00 68.74  ? 1247 PHE A CE1 1 
ATOM   6297 C CE2 . PHE A 1 1247 ? 149.518 169.421 114.900 1.00 66.73  ? 1247 PHE A CE2 1 
ATOM   6298 C CZ  . PHE A 1 1247 ? 149.810 168.782 116.082 1.00 65.93  ? 1247 PHE A CZ  1 
ATOM   6299 N N   . LYS A 1 1248 ? 155.055 173.562 113.563 1.00 58.67  ? 1248 LYS A N   1 
ATOM   6300 C CA  . LYS A 1 1248 ? 156.379 173.906 113.047 1.00 55.21  ? 1248 LYS A CA  1 
ATOM   6301 C C   . LYS A 1 1248 ? 157.490 173.657 114.061 1.00 55.50  ? 1248 LYS A C   1 
ATOM   6302 O O   . LYS A 1 1248 ? 158.627 173.359 113.682 1.00 63.75  ? 1248 LYS A O   1 
ATOM   6303 C CB  . LYS A 1 1248 ? 156.397 175.369 112.603 1.00 59.14  ? 1248 LYS A CB  1 
ATOM   6304 C CG  . LYS A 1 1248 ? 156.153 176.357 113.731 1.00 59.93  ? 1248 LYS A CG  1 
ATOM   6305 C CD  . LYS A 1 1248 ? 156.202 177.792 113.239 1.00 57.87  ? 1248 LYS A CD  1 
ATOM   6306 C CE  . LYS A 1 1248 ? 155.900 178.767 114.365 1.00 61.36  ? 1248 LYS A CE  1 
ATOM   6307 N NZ  . LYS A 1 1248 ? 156.839 178.607 115.509 1.00 58.30  ? 1248 LYS A NZ  1 
ATOM   6308 N N   . ASN A 1 1249 ? 157.191 173.772 115.351 1.00 55.89  ? 1249 ASN A N   1 
ATOM   6309 C CA  . ASN A 1 1249 ? 158.213 173.685 116.384 1.00 56.66  ? 1249 ASN A CA  1 
ATOM   6310 C C   . ASN A 1 1249 ? 158.531 172.256 116.800 1.00 60.12  ? 1249 ASN A C   1 
ATOM   6311 O O   . ASN A 1 1249 ? 159.271 172.061 117.769 1.00 60.28  ? 1249 ASN A O   1 
ATOM   6312 C CB  . ASN A 1 1249 ? 157.790 174.490 117.614 1.00 54.54  ? 1249 ASN A CB  1 
ATOM   6313 C CG  . ASN A 1 1249 ? 157.858 175.980 117.381 1.00 62.19  ? 1249 ASN A CG  1 
ATOM   6314 O OD1 . ASN A 1 1249 ? 158.706 176.462 116.633 1.00 64.17  ? 1249 ASN A OD1 1 
ATOM   6315 N ND2 . ASN A 1 1249 ? 156.962 176.720 118.020 1.00 63.96  ? 1249 ASN A ND2 1 
ATOM   6316 N N   . ASP A 1 1250 ? 157.998 171.256 116.101 1.00 50.17  ? 1250 ASP A N   1 
ATOM   6317 C CA  . ASP A 1 1250 ? 158.184 169.863 116.483 1.00 43.58  ? 1250 ASP A CA  1 
ATOM   6318 C C   . ASP A 1 1250 ? 158.954 169.063 115.441 1.00 45.10  ? 1250 ASP A C   1 
ATOM   6319 O O   . ASP A 1 1250 ? 158.949 167.831 115.488 1.00 56.94  ? 1250 ASP A O   1 
ATOM   6320 C CB  . ASP A 1 1250 ? 156.832 169.204 116.751 1.00 47.22  ? 1250 ASP A CB  1 
ATOM   6321 C CG  . ASP A 1 1250 ? 156.130 169.787 117.955 1.00 53.99  ? 1250 ASP A CG  1 
ATOM   6322 O OD1 . ASP A 1 1250 ? 156.744 170.616 118.656 1.00 58.00  ? 1250 ASP A OD1 1 
ATOM   6323 O OD2 . ASP A 1 1250 ? 154.963 169.417 118.201 1.00 56.84  ? 1250 ASP A OD2 1 
ATOM   6324 N N   . PHE A 1 1251 ? 159.614 169.728 114.499 1.00 44.08  ? 1251 PHE A N   1 
ATOM   6325 C CA  . PHE A 1 1251 ? 160.325 169.030 113.439 1.00 39.59  ? 1251 PHE A CA  1 
ATOM   6326 C C   . PHE A 1 1251 ? 161.634 169.739 113.136 1.00 50.88  ? 1251 PHE A C   1 
ATOM   6327 O O   . PHE A 1 1251 ? 161.699 170.970 113.146 1.00 60.82  ? 1251 PHE A O   1 
ATOM   6328 C CB  . PHE A 1 1251 ? 159.471 168.931 112.175 1.00 38.56  ? 1251 PHE A CB  1 
ATOM   6329 C CG  . PHE A 1 1251 ? 158.235 168.105 112.352 1.00 49.42  ? 1251 PHE A CG  1 
ATOM   6330 C CD1 . PHE A 1 1251 ? 158.263 166.743 112.132 1.00 48.45  ? 1251 PHE A CD1 1 
ATOM   6331 C CD2 . PHE A 1 1251 ? 157.047 168.688 112.743 1.00 46.57  ? 1251 PHE A CD2 1 
ATOM   6332 C CE1 . PHE A 1 1251 ? 157.133 165.980 112.298 1.00 43.46  ? 1251 PHE A CE1 1 
ATOM   6333 C CE2 . PHE A 1 1251 ? 155.915 167.928 112.908 1.00 47.00  ? 1251 PHE A CE2 1 
ATOM   6334 C CZ  . PHE A 1 1251 ? 155.958 166.573 112.684 1.00 43.03  ? 1251 PHE A CZ  1 
ATOM   6335 N N   . VAL A 1 1252 ? 162.675 168.952 112.875 1.00 36.15  ? 1252 VAL A N   1 
ATOM   6336 C CA  . VAL A 1 1252 ? 163.999 169.466 112.556 1.00 26.68  ? 1252 VAL A CA  1 
ATOM   6337 C C   . VAL A 1 1252 ? 164.493 168.783 111.291 1.00 31.68  ? 1252 VAL A C   1 
ATOM   6338 O O   . VAL A 1 1252 ? 164.618 167.553 111.253 1.00 51.41  ? 1252 VAL A O   1 
ATOM   6339 C CB  . VAL A 1 1252 ? 164.994 169.241 113.707 1.00 22.40  ? 1252 VAL A CB  1 
ATOM   6340 C CG1 . VAL A 1 1252 ? 166.378 169.680 113.289 1.00 25.74  ? 1252 VAL A CG1 1 
ATOM   6341 C CG2 . VAL A 1 1252 ? 164.550 169.994 114.943 1.00 32.11  ? 1252 VAL A CG2 1 
ATOM   6342 N N   . PHE A 1 1253 ? 164.783 169.576 110.267 1.00 31.98  ? 1253 PHE A N   1 
ATOM   6343 C CA  . PHE A 1 1253 ? 165.337 169.084 109.015 1.00 25.88  ? 1253 PHE A CA  1 
ATOM   6344 C C   . PHE A 1 1253 ? 166.756 169.604 108.867 1.00 45.10  ? 1253 PHE A C   1 
ATOM   6345 O O   . PHE A 1 1253 ? 166.994 170.808 108.987 1.00 65.99  ? 1253 PHE A O   1 
ATOM   6346 C CB  . PHE A 1 1253 ? 164.499 169.531 107.816 1.00 42.24  ? 1253 PHE A CB  1 
ATOM   6347 C CG  . PHE A 1 1253 ? 163.116 168.955 107.786 1.00 37.28  ? 1253 PHE A CG  1 
ATOM   6348 C CD1 . PHE A 1 1253 ? 162.084 169.562 108.474 1.00 38.88  ? 1253 PHE A CD1 1 
ATOM   6349 C CD2 . PHE A 1 1253 ? 162.846 167.817 107.053 1.00 42.21  ? 1253 PHE A CD2 1 
ATOM   6350 C CE1 . PHE A 1 1253 ? 160.812 169.037 108.441 1.00 36.93  ? 1253 PHE A CE1 1 
ATOM   6351 C CE2 . PHE A 1 1253 ? 161.576 167.288 107.015 1.00 41.45  ? 1253 PHE A CE2 1 
ATOM   6352 C CZ  . PHE A 1 1253 ? 160.559 167.899 107.711 1.00 44.99  ? 1253 PHE A CZ  1 
ATOM   6353 N N   . LEU A 1 1254 ? 167.694 168.700 108.607 1.00 39.12  ? 1254 LEU A N   1 
ATOM   6354 C CA  . LEU A 1 1254 ? 169.076 169.054 108.316 1.00 41.35  ? 1254 LEU A CA  1 
ATOM   6355 C C   . LEU A 1 1254 ? 169.423 168.523 106.936 1.00 50.83  ? 1254 LEU A C   1 
ATOM   6356 O O   . LEU A 1 1254 ? 169.257 167.328 106.671 1.00 64.13  ? 1254 LEU A O   1 
ATOM   6357 C CB  . LEU A 1 1254 ? 170.027 168.483 109.367 1.00 40.34  ? 1254 LEU A CB  1 
ATOM   6358 C CG  . LEU A 1 1254 ? 171.513 168.597 109.036 1.00 47.10  ? 1254 LEU A CG  1 
ATOM   6359 C CD1 . LEU A 1 1254 ? 171.895 170.044 108.815 1.00 49.44  ? 1254 LEU A CD1 1 
ATOM   6360 C CD2 . LEU A 1 1254 ? 172.355 167.989 110.138 1.00 51.45  ? 1254 LEU A CD2 1 
ATOM   6361 N N   . ASN A 1 1255 ? 169.891 169.411 106.060 1.00 54.45  ? 1255 ASN A N   1 
ATOM   6362 C CA  . ASN A 1 1255 ? 170.299 169.050 104.704 1.00 58.69  ? 1255 ASN A CA  1 
ATOM   6363 C C   . ASN A 1 1255 ? 169.204 168.289 103.965 1.00 62.68  ? 1255 ASN A C   1 
ATOM   6364 O O   . ASN A 1 1255 ? 169.485 167.358 103.210 1.00 66.33  ? 1255 ASN A O   1 
ATOM   6365 C CB  . ASN A 1 1255 ? 171.594 168.237 104.714 1.00 58.64  ? 1255 ASN A CB  1 
ATOM   6366 C CG  . ASN A 1 1255 ? 172.731 168.967 105.390 1.00 62.19  ? 1255 ASN A CG  1 
ATOM   6367 O OD1 . ASN A 1 1255 ? 172.768 170.195 105.410 1.00 64.68  ? 1255 ASN A OD1 1 
ATOM   6368 N ND2 . ASN A 1 1255 ? 173.666 168.213 105.952 1.00 60.08  ? 1255 ASN A ND2 1 
ATOM   6369 N N   . GLY A 1 1256 ? 167.949 168.670 104.185 1.00 58.00  ? 1256 GLY A N   1 
ATOM   6370 C CA  . GLY A 1 1256 ? 166.838 168.031 103.512 1.00 54.96  ? 1256 GLY A CA  1 
ATOM   6371 C C   . GLY A 1 1256 ? 166.379 166.720 104.106 1.00 49.30  ? 1256 GLY A C   1 
ATOM   6372 O O   . GLY A 1 1256 ? 165.518 166.063 103.513 1.00 51.46  ? 1256 GLY A O   1 
ATOM   6373 N N   . LYS A 1 1257 ? 166.920 166.313 105.250 1.00 50.66  ? 1257 LYS A N   1 
ATOM   6374 C CA  . LYS A 1 1257 ? 166.537 165.068 105.898 1.00 47.26  ? 1257 LYS A CA  1 
ATOM   6375 C C   . LYS A 1 1257 ? 165.973 165.356 107.280 1.00 46.80  ? 1257 LYS A C   1 
ATOM   6376 O O   . LYS A 1 1257 ? 166.562 166.116 108.052 1.00 58.04  ? 1257 LYS A O   1 
ATOM   6377 C CB  . LYS A 1 1257 ? 167.726 164.116 106.020 1.00 50.01  ? 1257 LYS A CB  1 
ATOM   6378 C CG  . LYS A 1 1257 ? 168.243 163.599 104.695 1.00 50.58  ? 1257 LYS A CG  1 
ATOM   6379 C CD  . LYS A 1 1257 ? 169.397 162.637 104.903 1.00 54.15  ? 1257 LYS A CD  1 
ATOM   6380 C CE  . LYS A 1 1257 ? 169.848 162.030 103.589 1.00 56.31  ? 1257 LYS A CE  1 
ATOM   6381 N NZ  . LYS A 1 1257 ? 171.005 161.112 103.768 1.00 63.17  ? 1257 LYS A NZ  1 
ATOM   6382 N N   . LEU A 1 1258 ? 164.835 164.745 107.591 1.00 37.57  ? 1258 LEU A N   1 
ATOM   6383 C CA  . LEU A 1 1258 ? 164.230 164.891 108.910 1.00 40.39  ? 1258 LEU A CA  1 
ATOM   6384 C C   . LEU A 1 1258 ? 165.094 164.172 109.937 1.00 37.51  ? 1258 LEU A C   1 
ATOM   6385 O O   . LEU A 1 1258 ? 165.088 162.940 110.007 1.00 56.50  ? 1258 LEU A O   1 
ATOM   6386 C CB  . LEU A 1 1258 ? 162.811 164.333 108.899 1.00 38.77  ? 1258 LEU A CB  1 
ATOM   6387 C CG  . LEU A 1 1258 ? 162.034 164.403 110.210 1.00 36.54  ? 1258 LEU A CG  1 
ATOM   6388 C CD1 . LEU A 1 1258 ? 161.847 165.840 110.642 1.00 43.86  ? 1258 LEU A CD1 1 
ATOM   6389 C CD2 . LEU A 1 1258 ? 160.694 163.717 110.064 1.00 36.46  ? 1258 LEU A CD2 1 
ATOM   6390 N N   . VAL A 1 1259 ? 165.840 164.931 110.735 1.00 34.37  ? 1259 VAL A N   1 
ATOM   6391 C CA  . VAL A 1 1259 ? 166.803 164.317 111.645 1.00 40.81  ? 1259 VAL A CA  1 
ATOM   6392 C C   . VAL A 1 1259 ? 166.237 164.169 113.050 1.00 42.19  ? 1259 VAL A C   1 
ATOM   6393 O O   . VAL A 1 1259 ? 166.699 163.329 113.823 1.00 61.75  ? 1259 VAL A O   1 
ATOM   6394 C CB  . VAL A 1 1259 ? 168.119 165.118 111.652 1.00 43.18  ? 1259 VAL A CB  1 
ATOM   6395 C CG1 . VAL A 1 1259 ? 168.760 165.087 110.278 1.00 40.88  ? 1259 VAL A CG1 1 
ATOM   6396 C CG2 . VAL A 1 1259 ? 167.871 166.540 112.097 1.00 48.79  ? 1259 VAL A CG2 1 
ATOM   6397 N N   . ALA A 1 1260 ? 165.244 164.972 113.414 1.00 29.47  ? 1260 ALA A N   1 
ATOM   6398 C CA  . ALA A 1 1260 ? 164.634 164.851 114.728 1.00 30.40  ? 1260 ALA A CA  1 
ATOM   6399 C C   . ALA A 1 1260 ? 163.213 165.382 114.669 1.00 38.31  ? 1260 ALA A C   1 
ATOM   6400 O O   . ALA A 1 1260 ? 162.919 166.324 113.931 1.00 48.18  ? 1260 ALA A O   1 
ATOM   6401 C CB  . ALA A 1 1260 ? 165.433 165.603 115.795 1.00 28.79  ? 1260 ALA A CB  1 
ATOM   6402 N N   . TRP A 1 1261 ? 162.336 164.767 115.456 1.00 36.78  ? 1261 TRP A N   1 
ATOM   6403 C CA  . TRP A 1 1261 ? 160.964 165.254 115.558 1.00 29.88  ? 1261 TRP A CA  1 
ATOM   6404 C C   . TRP A 1 1261 ? 160.338 164.715 116.832 1.00 32.30  ? 1261 TRP A C   1 
ATOM   6405 O O   . TRP A 1 1261 ? 160.966 163.963 117.579 1.00 45.41  ? 1261 TRP A O   1 
ATOM   6406 C CB  . TRP A 1 1261 ? 160.124 164.874 114.335 1.00 25.70  ? 1261 TRP A CB  1 
ATOM   6407 C CG  . TRP A 1 1261 ? 159.941 163.414 114.117 1.00 40.46  ? 1261 TRP A CG  1 
ATOM   6408 C CD1 . TRP A 1 1261 ? 160.845 162.548 113.587 1.00 48.64  ? 1261 TRP A CD1 1 
ATOM   6409 C CD2 . TRP A 1 1261 ? 158.764 162.648 114.389 1.00 47.81  ? 1261 TRP A CD2 1 
ATOM   6410 N NE1 . TRP A 1 1261 ? 160.314 161.285 113.527 1.00 46.90  ? 1261 TRP A NE1 1 
ATOM   6411 C CE2 . TRP A 1 1261 ? 159.035 161.322 114.013 1.00 40.43  ? 1261 TRP A CE2 1 
ATOM   6412 C CE3 . TRP A 1 1261 ? 157.511 162.955 114.921 1.00 45.96  ? 1261 TRP A CE3 1 
ATOM   6413 C CZ2 . TRP A 1 1261 ? 158.101 160.304 114.154 1.00 35.37  ? 1261 TRP A CZ2 1 
ATOM   6414 C CZ3 . TRP A 1 1261 ? 156.587 161.943 115.058 1.00 36.85  ? 1261 TRP A CZ3 1 
ATOM   6415 C CH2 . TRP A 1 1261 ? 156.885 160.635 114.676 1.00 33.41  ? 1261 TRP A CH2 1 
ATOM   6416 N N   . ARG A 1 1262 ? 159.097 165.125 117.084 1.00 34.60  ? 1262 ARG A N   1 
ATOM   6417 C CA  . ARG A 1 1262 ? 158.438 164.763 118.328 1.00 32.19  ? 1262 ARG A CA  1 
ATOM   6418 C C   . ARG A 1 1262 ? 156.932 164.897 118.187 1.00 43.98  ? 1262 ARG A C   1 
ATOM   6419 O O   . ARG A 1 1262 ? 156.422 165.540 117.268 1.00 53.39  ? 1262 ARG A O   1 
ATOM   6420 C CB  . ARG A 1 1262 ? 158.916 165.635 119.489 1.00 29.00  ? 1262 ARG A CB  1 
ATOM   6421 C CG  . ARG A 1 1262 ? 158.485 167.082 119.370 1.00 37.08  ? 1262 ARG A CG  1 
ATOM   6422 C CD  . ARG A 1 1262 ? 158.932 167.890 120.568 1.00 42.22  ? 1262 ARG A CD  1 
ATOM   6423 N NE  . ARG A 1 1262 ? 158.698 169.315 120.378 1.00 42.70  ? 1262 ARG A NE  1 
ATOM   6424 C CZ  . ARG A 1 1262 ? 159.122 170.257 121.207 1.00 45.43  ? 1262 ARG A CZ  1 
ATOM   6425 N NH1 . ARG A 1 1262 ? 159.803 169.959 122.300 1.00 50.41  ? 1262 ARG A NH1 1 
ATOM   6426 N NH2 . ARG A 1 1262 ? 158.858 171.530 120.932 1.00 43.52  ? 1262 ARG A NH2 1 
ATOM   6427 N N   . PHE A 1 1263 ? 156.229 164.273 119.126 1.00 39.48  ? 1263 PHE A N   1 
ATOM   6428 C CA  . PHE A 1 1263 ? 154.809 164.509 119.331 1.00 34.83  ? 1263 PHE A CA  1 
ATOM   6429 C C   . PHE A 1 1263 ? 154.503 164.324 120.809 1.00 45.30  ? 1263 PHE A C   1 
ATOM   6430 O O   . PHE A 1 1263 ? 155.383 163.997 121.606 1.00 54.59  ? 1263 PHE A O   1 
ATOM   6431 C CB  . PHE A 1 1263 ? 153.937 163.598 118.456 1.00 44.30  ? 1263 PHE A CB  1 
ATOM   6432 C CG  . PHE A 1 1263 ? 153.944 162.155 118.864 1.00 39.09  ? 1263 PHE A CG  1 
ATOM   6433 C CD1 . PHE A 1 1263 ? 154.886 161.284 118.358 1.00 43.65  ? 1263 PHE A CD1 1 
ATOM   6434 C CD2 . PHE A 1 1263 ? 152.984 161.662 119.727 1.00 43.77  ? 1263 PHE A CD2 1 
ATOM   6435 C CE1 . PHE A 1 1263 ? 154.883 159.955 118.722 1.00 47.70  ? 1263 PHE A CE1 1 
ATOM   6436 C CE2 . PHE A 1 1263 ? 152.979 160.337 120.094 1.00 45.08  ? 1263 PHE A CE2 1 
ATOM   6437 C CZ  . PHE A 1 1263 ? 153.928 159.483 119.590 1.00 49.94  ? 1263 PHE A CZ  1 
ATOM   6438 N N   . HIS A 1 1264 ? 153.250 164.562 121.178 1.00 53.52  ? 1264 HIS A N   1 
ATOM   6439 C CA  . HIS A 1 1264 ? 152.849 164.537 122.575 1.00 45.98  ? 1264 HIS A CA  1 
ATOM   6440 C C   . HIS A 1 1264 ? 151.511 163.833 122.721 1.00 49.47  ? 1264 HIS A C   1 
ATOM   6441 O O   . HIS A 1 1264 ? 150.719 163.761 121.780 1.00 57.02  ? 1264 HIS A O   1 
ATOM   6442 C CB  . HIS A 1 1264 ? 152.748 165.951 123.146 1.00 49.78  ? 1264 HIS A CB  1 
ATOM   6443 C CG  . HIS A 1 1264 ? 153.938 166.807 122.854 1.00 62.04  ? 1264 HIS A CG  1 
ATOM   6444 N ND1 . HIS A 1 1264 ? 155.007 166.917 123.717 1.00 58.40  ? 1264 HIS A ND1 1 
ATOM   6445 C CD2 . HIS A 1 1264 ? 154.230 167.595 121.794 1.00 63.35  ? 1264 HIS A CD2 1 
ATOM   6446 C CE1 . HIS A 1 1264 ? 155.905 167.735 123.202 1.00 52.96  ? 1264 HIS A CE1 1 
ATOM   6447 N NE2 . HIS A 1 1264 ? 155.458 168.161 122.035 1.00 61.61  ? 1264 HIS A NE2 1 
ATOM   6448 N N   . TYR A 1 1265 ? 151.263 163.311 123.919 1.00 45.82  ? 1265 TYR A N   1 
ATOM   6449 C CA  . TYR A 1 1265 ? 149.951 162.749 124.204 1.00 40.57  ? 1265 TYR A CA  1 
ATOM   6450 C C   . TYR A 1 1265 ? 149.697 162.784 125.702 1.00 47.53  ? 1265 TYR A C   1 
ATOM   6451 O O   . TYR A 1 1265 ? 150.627 162.708 126.509 1.00 54.42  ? 1265 TYR A O   1 
ATOM   6452 C CB  . TYR A 1 1265 ? 149.815 161.320 123.667 1.00 45.31  ? 1265 TYR A CB  1 
ATOM   6453 C CG  . TYR A 1 1265 ? 150.601 160.284 124.428 1.00 47.01  ? 1265 TYR A CG  1 
ATOM   6454 C CD1 . TYR A 1 1265 ? 151.921 160.019 124.111 1.00 50.80  ? 1265 TYR A CD1 1 
ATOM   6455 C CD2 . TYR A 1 1265 ? 150.017 159.561 125.455 1.00 53.43  ? 1265 TYR A CD2 1 
ATOM   6456 C CE1 . TYR A 1 1265 ? 152.638 159.071 124.800 1.00 52.35  ? 1265 TYR A CE1 1 
ATOM   6457 C CE2 . TYR A 1 1265 ? 150.728 158.613 126.151 1.00 55.59  ? 1265 TYR A CE2 1 
ATOM   6458 C CZ  . TYR A 1 1265 ? 152.036 158.372 125.819 1.00 54.73  ? 1265 TYR A CZ  1 
ATOM   6459 O OH  . TYR A 1 1265 ? 152.748 157.426 126.514 1.00 61.28  ? 1265 TYR A OH  1 
ATOM   6460 N N   . PHE A 1 1266 ? 148.423 162.887 126.059 1.00 59.98  ? 1266 PHE A N   1 
ATOM   6461 C CA  . PHE A 1 1266 ? 148.012 162.929 127.451 1.00 59.14  ? 1266 PHE A CA  1 
ATOM   6462 C C   . PHE A 1 1266 ? 147.659 161.536 127.954 1.00 57.34  ? 1266 PHE A C   1 
ATOM   6463 O O   . PHE A 1 1266 ? 147.124 160.697 127.227 1.00 65.01  ? 1266 PHE A O   1 
ATOM   6464 C CB  . PHE A 1 1266 ? 146.822 163.867 127.636 1.00 60.45  ? 1266 PHE A CB  1 
ATOM   6465 C CG  . PHE A 1 1266 ? 147.175 165.314 127.520 1.00 60.19  ? 1266 PHE A CG  1 
ATOM   6466 C CD1 . PHE A 1 1266 ? 147.618 166.019 128.621 1.00 57.29  ? 1266 PHE A CD1 1 
ATOM   6467 C CD2 . PHE A 1 1266 ? 147.067 165.970 126.309 1.00 61.22  ? 1266 PHE A CD2 1 
ATOM   6468 C CE1 . PHE A 1 1266 ? 147.944 167.351 128.520 1.00 60.38  ? 1266 PHE A CE1 1 
ATOM   6469 C CE2 . PHE A 1 1266 ? 147.393 167.303 126.200 1.00 63.11  ? 1266 PHE A CE2 1 
ATOM   6470 C CZ  . PHE A 1 1266 ? 147.831 167.995 127.307 1.00 60.82  ? 1266 PHE A CZ  1 
ATOM   6471 N N   . GLN A 1 1267 ? 147.966 161.305 129.222 1.00 66.23  ? 1267 GLN A N   1 
ATOM   6472 C CA  . GLN A 1 1267 ? 147.769 160.020 129.870 1.00 67.80  ? 1267 GLN A CA  1 
ATOM   6473 C C   . GLN A 1 1267 ? 146.959 160.222 131.140 1.00 71.09  ? 1267 GLN A C   1 
ATOM   6474 O O   . GLN A 1 1267 ? 147.210 161.162 131.900 1.00 77.54  ? 1267 GLN A O   1 
ATOM   6475 C CB  . GLN A 1 1267 ? 149.115 159.365 130.190 1.00 66.09  ? 1267 GLN A CB  1 
ATOM   6476 C CG  . GLN A 1 1267 ? 149.041 158.188 131.134 1.00 69.00  ? 1267 GLN A CG  1 
ATOM   6477 C CD  . GLN A 1 1267 ? 150.400 157.578 131.397 1.00 76.25  ? 1267 GLN A CD  1 
ATOM   6478 O OE1 . GLN A 1 1267 ? 151.265 157.567 130.523 1.00 79.95  ? 1267 GLN A OE1 1 
ATOM   6479 N NE2 . GLN A 1 1267 ? 150.600 157.073 132.607 1.00 79.38  ? 1267 GLN A NE2 1 
ATOM   6480 N N   . LYS A 1 1268 ? 145.981 159.346 131.358 1.00 74.33  ? 1268 LYS A N   1 
ATOM   6481 C CA  . LYS A 1 1268 ? 145.152 159.430 132.553 1.00 76.90  ? 1268 LYS A CA  1 
ATOM   6482 C C   . LYS A 1 1268 ? 146.009 159.319 133.804 1.00 79.97  ? 1268 LYS A C   1 
ATOM   6483 O O   . LYS A 1 1268 ? 146.890 158.461 133.895 1.00 84.92  ? 1268 LYS A O   1 
ATOM   6484 C CB  . LYS A 1 1268 ? 144.095 158.329 132.545 1.00 79.03  ? 1268 LYS A CB  1 
ATOM   6485 C CG  . LYS A 1 1268 ? 142.945 158.569 131.591 1.00 80.69  ? 1268 LYS A CG  1 
ATOM   6486 C CD  . LYS A 1 1268 ? 141.907 157.468 131.706 1.00 77.61  ? 1268 LYS A CD  1 
ATOM   6487 C CE  . LYS A 1 1268 ? 140.664 157.792 130.896 1.00 78.29  ? 1268 LYS A CE  1 
ATOM   6488 N NZ  . LYS A 1 1268 ? 139.989 159.023 131.389 1.00 80.86  ? 1268 LYS A NZ  1 
ATOM   6489 N N   . ASN A 1 1269 ? 145.751 160.194 134.770 1.00 78.40  ? 1269 ASN A N   1 
ATOM   6490 C CA  . ASN A 1 1269 ? 146.483 160.160 136.026 1.00 77.04  ? 1269 ASN A CA  1 
ATOM   6491 C C   . ASN A 1 1269 ? 145.940 159.041 136.903 1.00 79.98  ? 1269 ASN A C   1 
ATOM   6492 O O   . ASN A 1 1269 ? 144.725 158.851 137.003 1.00 83.01  ? 1269 ASN A O   1 
ATOM   6493 C CB  . ASN A 1 1269 ? 146.379 161.503 136.744 1.00 79.04  ? 1269 ASN A CB  1 
ATOM   6494 C CG  . ASN A 1 1269 ? 147.474 161.697 137.773 1.00 82.96  ? 1269 ASN A CG  1 
ATOM   6495 O OD1 . ASN A 1 1269 ? 147.853 160.763 138.478 1.00 79.65  ? 1269 ASN A OD1 1 
ATOM   6496 N ND2 . ASN A 1 1269 ? 147.997 162.915 137.857 1.00 82.62  ? 1269 ASN A ND2 1 
ATOM   6497 N N   . VAL A 1 1270 ? 146.844 158.301 137.536 1.00 88.02  ? 1270 VAL A N   1 
ATOM   6498 C CA  . VAL A 1 1270 ? 146.484 157.162 138.370 1.00 88.12  ? 1270 VAL A CA  1 
ATOM   6499 C C   . VAL A 1 1270 ? 147.320 157.214 139.641 1.00 93.48  ? 1270 VAL A C   1 
ATOM   6500 O O   . VAL A 1 1270 ? 148.459 157.693 139.629 1.00 93.33  ? 1270 VAL A O   1 
ATOM   6501 C CB  . VAL A 1 1270 ? 146.686 155.833 137.613 1.00 87.03  ? 1270 VAL A CB  1 
ATOM   6502 C CG1 . VAL A 1 1270 ? 148.149 155.639 137.261 1.00 87.96  ? 1270 VAL A CG1 1 
ATOM   6503 C CG2 . VAL A 1 1270 ? 146.150 154.660 138.419 1.00 88.96  ? 1270 VAL A CG2 1 
ATOM   6504 N N   . ASP A 1 1271 ? 146.748 156.731 140.744 1.00 106.73 ? 1271 ASP A N   1 
ATOM   6505 C CA  . ASP A 1 1271 ? 147.407 156.798 142.042 1.00 105.52 ? 1271 ASP A CA  1 
ATOM   6506 C C   . ASP A 1 1271 ? 148.455 155.712 142.242 1.00 104.35 ? 1271 ASP A C   1 
ATOM   6507 O O   . ASP A 1 1271 ? 149.204 155.776 143.222 1.00 104.17 ? 1271 ASP A O   1 
ATOM   6508 C CB  . ASP A 1 1271 ? 146.368 156.712 143.161 1.00 107.37 ? 1271 ASP A CB  1 
ATOM   6509 C CG  . ASP A 1 1271 ? 145.292 157.770 143.038 1.00 108.48 ? 1271 ASP A CG  1 
ATOM   6510 O OD1 . ASP A 1 1271 ? 145.578 158.847 142.476 1.00 109.07 ? 1271 ASP A OD1 1 
ATOM   6511 O OD2 . ASP A 1 1271 ? 144.160 157.523 143.502 1.00 107.23 ? 1271 ASP A OD2 1 
ATOM   6512 N N   . ASP A 1 1272 ? 148.526 154.725 141.356 1.00 99.25  ? 1272 ASP A N   1 
ATOM   6513 C CA  . ASP A 1 1272 ? 149.480 153.631 141.475 1.00 97.59  ? 1272 ASP A CA  1 
ATOM   6514 C C   . ASP A 1 1272 ? 150.638 153.874 140.516 1.00 96.35  ? 1272 ASP A C   1 
ATOM   6515 O O   . ASP A 1 1272 ? 150.424 154.071 139.316 1.00 98.59  ? 1272 ASP A O   1 
ATOM   6516 C CB  . ASP A 1 1272 ? 148.807 152.290 141.184 1.00 95.53  ? 1272 ASP A CB  1 
ATOM   6517 C CG  . ASP A 1 1272 ? 149.734 151.111 141.401 1.00 97.18  ? 1272 ASP A CG  1 
ATOM   6518 O OD1 . ASP A 1 1272 ? 150.813 151.298 142.000 1.00 98.37  ? 1272 ASP A OD1 1 
ATOM   6519 O OD2 . ASP A 1 1272 ? 149.382 149.993 140.971 1.00 98.08  ? 1272 ASP A OD2 1 
ATOM   6520 N N   . SER A 1 1273 ? 151.861 153.865 141.047 1.00 87.39  ? 1273 SER A N   1 
ATOM   6521 C CA  . SER A 1 1273 ? 153.030 154.084 140.203 1.00 87.02  ? 1273 SER A CA  1 
ATOM   6522 C C   . SER A 1 1273 ? 153.320 152.884 139.313 1.00 88.62  ? 1273 SER A C   1 
ATOM   6523 O O   . SER A 1 1273 ? 153.833 153.051 138.201 1.00 91.27  ? 1273 SER A O   1 
ATOM   6524 C CB  . SER A 1 1273 ? 154.249 154.407 141.066 1.00 88.82  ? 1273 SER A CB  1 
ATOM   6525 O OG  . SER A 1 1273 ? 155.402 154.599 140.264 1.00 91.95  ? 1273 SER A OG  1 
ATOM   6526 N N   . GLU A 1 1274 ? 153.017 151.673 139.784 1.00 87.94  ? 1274 GLU A N   1 
ATOM   6527 C CA  . GLU A 1 1274 ? 153.334 150.479 139.008 1.00 85.47  ? 1274 GLU A CA  1 
ATOM   6528 C C   . GLU A 1 1274 ? 152.550 150.441 137.703 1.00 87.19  ? 1274 GLU A C   1 
ATOM   6529 O O   . GLU A 1 1274 ? 153.107 150.131 136.643 1.00 91.22  ? 1274 GLU A O   1 
ATOM   6530 C CB  . GLU A 1 1274 ? 153.057 149.228 139.841 1.00 86.87  ? 1274 GLU A CB  1 
ATOM   6531 C CG  . GLU A 1 1274 ? 153.480 147.931 139.174 1.00 90.83  ? 1274 GLU A CG  1 
ATOM   6532 C CD  . GLU A 1 1274 ? 153.277 146.723 140.069 1.00 96.32  ? 1274 GLU A CD  1 
ATOM   6533 O OE1 . GLU A 1 1274 ? 152.786 146.899 141.204 1.00 98.90  ? 1274 GLU A OE1 1 
ATOM   6534 O OE2 . GLU A 1 1274 ? 153.609 145.598 139.639 1.00 97.42  ? 1274 GLU A OE2 1 
ATOM   6535 N N   . ILE A 1 1275 ? 151.257 150.763 137.754 1.00 79.87  ? 1275 ILE A N   1 
ATOM   6536 C CA  . ILE A 1 1275 ? 150.453 150.747 136.538 1.00 77.72  ? 1275 ILE A CA  1 
ATOM   6537 C C   . ILE A 1 1275 ? 150.872 151.879 135.605 1.00 77.76  ? 1275 ILE A C   1 
ATOM   6538 O O   . ILE A 1 1275 ? 150.815 151.742 134.379 1.00 84.65  ? 1275 ILE A O   1 
ATOM   6539 C CB  . ILE A 1 1275 ? 148.954 150.798 136.884 1.00 76.33  ? 1275 ILE A CB  1 
ATOM   6540 C CG1 . ILE A 1 1275 ? 148.105 150.671 135.620 1.00 79.46  ? 1275 ILE A CG1 1 
ATOM   6541 C CG2 . ILE A 1 1275 ? 148.614 152.069 137.620 1.00 79.55  ? 1275 ILE A CG2 1 
ATOM   6542 C CD1 . ILE A 1 1275 ? 146.621 150.599 135.892 1.00 82.01  ? 1275 ILE A CD1 1 
ATOM   6543 N N   . SER A 1 1276 ? 151.309 153.009 136.164 1.00 75.60  ? 1276 SER A N   1 
ATOM   6544 C CA  . SER A 1 1276 ? 151.827 154.087 135.328 1.00 73.36  ? 1276 SER A CA  1 
ATOM   6545 C C   . SER A 1 1276 ? 153.096 153.659 134.602 1.00 75.73  ? 1276 SER A C   1 
ATOM   6546 O O   . SER A 1 1276 ? 153.276 153.957 133.415 1.00 81.94  ? 1276 SER A O   1 
ATOM   6547 C CB  . SER A 1 1276 ? 152.086 155.329 136.177 1.00 78.40  ? 1276 SER A CB  1 
ATOM   6548 O OG  . SER A 1 1276 ? 152.630 156.374 135.393 1.00 80.57  ? 1276 SER A OG  1 
ATOM   6549 N N   . SER A 1 1277 ? 153.991 152.961 135.303 1.00 72.37  ? 1277 SER A N   1 
ATOM   6550 C CA  . SER A 1 1277 ? 155.185 152.434 134.652 1.00 74.87  ? 1277 SER A CA  1 
ATOM   6551 C C   . SER A 1 1277 ? 154.816 151.422 133.577 1.00 75.62  ? 1277 SER A C   1 
ATOM   6552 O O   . SER A 1 1277 ? 155.440 151.380 132.510 1.00 73.54  ? 1277 SER A O   1 
ATOM   6553 C CB  . SER A 1 1277 ? 156.111 151.804 135.689 1.00 77.92  ? 1277 SER A CB  1 
ATOM   6554 O OG  . SER A 1 1277 ? 155.467 150.735 136.358 1.00 84.21  ? 1277 SER A OG  1 
ATOM   6555 N N   . LYS A 1 1278 ? 153.806 150.593 133.846 1.00 77.29  ? 1278 LYS A N   1 
ATOM   6556 C CA  . LYS A 1 1278 ? 153.327 149.656 132.836 1.00 73.18  ? 1278 LYS A CA  1 
ATOM   6557 C C   . LYS A 1 1278 ? 152.818 150.390 131.603 1.00 74.96  ? 1278 LYS A C   1 
ATOM   6558 O O   . LYS A 1 1278 ? 153.089 149.980 130.469 1.00 76.82  ? 1278 LYS A O   1 
ATOM   6559 C CB  . LYS A 1 1278 ? 152.227 148.773 133.420 1.00 72.87  ? 1278 LYS A CB  1 
ATOM   6560 C CG  . LYS A 1 1278 ? 151.462 147.976 132.381 1.00 78.12  ? 1278 LYS A CG  1 
ATOM   6561 C CD  . LYS A 1 1278 ? 150.190 147.385 132.962 1.00 78.48  ? 1278 LYS A CD  1 
ATOM   6562 C CE  . LYS A 1 1278 ? 149.346 146.734 131.880 1.00 77.72  ? 1278 LYS A CE  1 
ATOM   6563 N NZ  . LYS A 1 1278 ? 148.058 146.216 132.415 1.00 78.64  ? 1278 LYS A NZ  1 
ATOM   6564 N N   . TRP A 1 1279 ? 152.073 151.477 131.808 1.00 69.51  ? 1279 TRP A N   1 
ATOM   6565 C CA  . TRP A 1 1279 ? 151.580 152.267 130.685 1.00 62.32  ? 1279 TRP A CA  1 
ATOM   6566 C C   . TRP A 1 1279 ? 152.727 152.871 129.889 1.00 64.60  ? 1279 TRP A C   1 
ATOM   6567 O O   . TRP A 1 1279 ? 152.697 152.884 128.653 1.00 69.77  ? 1279 TRP A O   1 
ATOM   6568 C CB  . TRP A 1 1279 ? 150.645 153.364 131.188 1.00 61.88  ? 1279 TRP A CB  1 
ATOM   6569 C CG  . TRP A 1 1279 ? 149.343 152.849 131.686 1.00 64.90  ? 1279 TRP A CG  1 
ATOM   6570 C CD1 . TRP A 1 1279 ? 148.857 151.586 131.546 1.00 68.92  ? 1279 TRP A CD1 1 
ATOM   6571 C CD2 . TRP A 1 1279 ? 148.353 153.582 132.413 1.00 67.65  ? 1279 TRP A CD2 1 
ATOM   6572 N NE1 . TRP A 1 1279 ? 147.622 151.485 132.137 1.00 71.88  ? 1279 TRP A NE1 1 
ATOM   6573 C CE2 . TRP A 1 1279 ? 147.291 152.699 132.678 1.00 68.97  ? 1279 TRP A CE2 1 
ATOM   6574 C CE3 . TRP A 1 1279 ? 148.260 154.900 132.863 1.00 65.94  ? 1279 TRP A CE3 1 
ATOM   6575 C CZ2 . TRP A 1 1279 ? 146.153 153.090 133.372 1.00 69.08  ? 1279 TRP A CZ2 1 
ATOM   6576 C CZ3 . TRP A 1 1279 ? 147.131 155.286 133.552 1.00 65.48  ? 1279 TRP A CZ3 1 
ATOM   6577 C CH2 . TRP A 1 1279 ? 146.092 154.385 133.800 1.00 68.22  ? 1279 TRP A CH2 1 
ATOM   6578 N N   . LEU A 1 1280 ? 153.746 153.385 130.579 1.00 64.22  ? 1280 LEU A N   1 
ATOM   6579 C CA  . LEU A 1 1280 ? 154.891 153.952 129.873 1.00 67.11  ? 1280 LEU A CA  1 
ATOM   6580 C C   . LEU A 1 1280 ? 155.627 152.890 129.066 1.00 68.86  ? 1280 LEU A C   1 
ATOM   6581 O O   . LEU A 1 1280 ? 156.042 153.141 127.929 1.00 69.63  ? 1280 LEU A O   1 
ATOM   6582 C CB  . LEU A 1 1280 ? 155.838 154.633 130.857 1.00 67.57  ? 1280 LEU A CB  1 
ATOM   6583 C CG  . LEU A 1 1280 ? 155.497 156.091 131.160 1.00 69.69  ? 1280 LEU A CG  1 
ATOM   6584 C CD1 . LEU A 1 1280 ? 156.569 156.725 132.021 1.00 72.73  ? 1280 LEU A CD1 1 
ATOM   6585 C CD2 . LEU A 1 1280 ? 155.325 156.864 129.868 1.00 71.08  ? 1280 LEU A CD2 1 
ATOM   6586 N N   . LYS A 1 1281 ? 155.801 151.697 129.636 1.00 76.65  ? 1281 LYS A N   1 
ATOM   6587 C CA  . LYS A 1 1281 ? 156.466 150.627 128.898 1.00 71.22  ? 1281 LYS A CA  1 
ATOM   6588 C C   . LYS A 1 1281 ? 155.634 150.186 127.701 1.00 65.94  ? 1281 LYS A C   1 
ATOM   6589 O O   . LYS A 1 1281 ? 156.178 149.888 126.631 1.00 70.86  ? 1281 LYS A O   1 
ATOM   6590 C CB  . LYS A 1 1281 ? 156.755 149.446 129.824 1.00 72.03  ? 1281 LYS A CB  1 
ATOM   6591 C CG  . LYS A 1 1281 ? 157.727 149.772 130.945 1.00 71.52  ? 1281 LYS A CG  1 
ATOM   6592 C CD  . LYS A 1 1281 ? 158.123 148.529 131.723 1.00 76.28  ? 1281 LYS A CD  1 
ATOM   6593 C CE  . LYS A 1 1281 ? 158.903 147.560 130.852 1.00 75.80  ? 1281 LYS A CE  1 
ATOM   6594 N NZ  . LYS A 1 1281 ? 159.367 146.373 131.622 1.00 72.04  ? 1281 LYS A NZ  1 
ATOM   6595 N N   . ALA A 1 1282 ? 154.310 150.142 127.859 1.00 69.61  ? 1282 ALA A N   1 
ATOM   6596 C CA  . ALA A 1 1282 ? 153.445 149.821 126.731 1.00 74.47  ? 1282 ALA A CA  1 
ATOM   6597 C C   . ALA A 1 1282 ? 153.566 150.871 125.636 1.00 77.21  ? 1282 ALA A C   1 
ATOM   6598 O O   . ALA A 1 1282 ? 153.582 150.540 124.446 1.00 77.67  ? 1282 ALA A O   1 
ATOM   6599 C CB  . ALA A 1 1282 ? 151.995 149.694 127.197 1.00 72.38  ? 1282 ALA A CB  1 
ATOM   6600 N N   . CYS A 1 1283 ? 153.648 152.145 126.020 1.00 76.06  ? 1283 CYS A N   1 
ATOM   6601 C CA  . CYS A 1 1283 ? 153.840 153.201 125.033 1.00 70.24  ? 1283 CYS A CA  1 
ATOM   6602 C C   . CYS A 1 1283 ? 155.171 153.047 124.312 1.00 73.21  ? 1283 CYS A C   1 
ATOM   6603 O O   . CYS A 1 1283 ? 155.250 153.228 123.092 1.00 81.34  ? 1283 CYS A O   1 
ATOM   6604 C CB  . CYS A 1 1283 ? 153.757 154.568 125.704 1.00 73.93  ? 1283 CYS A CB  1 
ATOM   6605 S SG  . CYS A 1 1283 ? 154.083 155.947 124.591 1.00 81.20  ? 1283 CYS A SG  1 
ATOM   6606 N N   . LYS A 1 1284 ? 156.232 152.721 125.054 1.00 67.63  ? 1284 LYS A N   1 
ATOM   6607 C CA  . LYS A 1 1284 ? 157.531 152.505 124.426 1.00 59.50  ? 1284 LYS A CA  1 
ATOM   6608 C C   . LYS A 1 1284 ? 157.474 151.343 123.446 1.00 65.54  ? 1284 LYS A C   1 
ATOM   6609 O O   . LYS A 1 1284 ? 158.090 151.392 122.375 1.00 71.53  ? 1284 LYS A O   1 
ATOM   6610 C CB  . LYS A 1 1284 ? 158.599 152.253 125.489 1.00 59.93  ? 1284 LYS A CB  1 
ATOM   6611 C CG  . LYS A 1 1284 ? 158.876 153.441 126.388 1.00 69.04  ? 1284 LYS A CG  1 
ATOM   6612 C CD  . LYS A 1 1284 ? 159.867 153.080 127.480 1.00 70.41  ? 1284 LYS A CD  1 
ATOM   6613 C CE  . LYS A 1 1284 ? 160.102 154.248 128.422 1.00 67.73  ? 1284 LYS A CE  1 
ATOM   6614 N NZ  . LYS A 1 1284 ? 161.008 153.877 129.542 1.00 71.98  ? 1284 LYS A NZ  1 
ATOM   6615 N N   . GLN A 1 1285 ? 156.747 150.285 123.801 1.00 71.03  ? 1285 GLN A N   1 
ATOM   6616 C CA  . GLN A 1 1285 ? 156.579 149.163 122.884 1.00 69.58  ? 1285 GLN A CA  1 
ATOM   6617 C C   . GLN A 1 1285 ? 155.795 149.573 121.644 1.00 63.95  ? 1285 GLN A C   1 
ATOM   6618 O O   . GLN A 1 1285 ? 156.102 149.128 120.533 1.00 64.02  ? 1285 GLN A O   1 
ATOM   6619 C CB  . GLN A 1 1285 ? 155.888 148.002 123.596 1.00 70.15  ? 1285 GLN A CB  1 
ATOM   6620 C CG  . GLN A 1 1285 ? 155.770 146.750 122.749 1.00 75.27  ? 1285 GLN A CG  1 
ATOM   6621 C CD  . GLN A 1 1285 ? 157.119 146.223 122.303 1.00 76.95  ? 1285 GLN A CD  1 
ATOM   6622 O OE1 . GLN A 1 1285 ? 158.097 146.277 123.049 1.00 73.65  ? 1285 GLN A OE1 1 
ATOM   6623 N NE2 . GLN A 1 1285 ? 157.180 145.715 121.078 1.00 74.00  ? 1285 GLN A NE2 1 
ATOM   6624 N N   . ILE A 1 1286 ? 154.773 150.410 121.817 1.00 63.58  ? 1286 ILE A N   1 
ATOM   6625 C CA  . ILE A 1 1286 ? 153.965 150.847 120.682 1.00 65.09  ? 1286 ILE A CA  1 
ATOM   6626 C C   . ILE A 1 1286 ? 154.792 151.696 119.728 1.00 67.24  ? 1286 ILE A C   1 
ATOM   6627 O O   . ILE A 1 1286 ? 154.710 151.537 118.504 1.00 70.68  ? 1286 ILE A O   1 
ATOM   6628 C CB  . ILE A 1 1286 ? 152.717 151.600 121.173 1.00 71.59  ? 1286 ILE A CB  1 
ATOM   6629 C CG1 . ILE A 1 1286 ? 151.753 150.636 121.862 1.00 70.98  ? 1286 ILE A CG1 1 
ATOM   6630 C CG2 . ILE A 1 1286 ? 152.031 152.298 120.017 1.00 69.80  ? 1286 ILE A CG2 1 
ATOM   6631 C CD1 . ILE A 1 1286 ? 150.518 151.300 122.413 1.00 68.78  ? 1286 ILE A CD1 1 
ATOM   6632 N N   . THR A 1 1287 ? 155.601 152.609 120.266 1.00 66.70  ? 1287 THR A N   1 
ATOM   6633 C CA  . THR A 1 1287 ? 156.419 153.479 119.428 1.00 57.19  ? 1287 THR A CA  1 
ATOM   6634 C C   . THR A 1 1287 ? 157.517 152.729 118.687 1.00 58.77  ? 1287 THR A C   1 
ATOM   6635 O O   . THR A 1 1287 ? 158.059 153.265 117.716 1.00 59.59  ? 1287 THR A O   1 
ATOM   6636 C CB  . THR A 1 1287 ? 157.045 154.585 120.273 1.00 48.14  ? 1287 THR A CB  1 
ATOM   6637 O OG1 . THR A 1 1287 ? 157.801 153.998 121.337 1.00 60.48  ? 1287 THR A OG1 1 
ATOM   6638 C CG2 . THR A 1 1287 ? 155.971 155.475 120.862 1.00 53.58  ? 1287 THR A CG2 1 
ATOM   6639 N N   . LYS A 1 1288 ? 157.854 151.516 119.113 1.00 68.71  ? 1288 LYS A N   1 
ATOM   6640 C CA  . LYS A 1 1288 ? 158.904 150.748 118.459 1.00 66.01  ? 1288 LYS A CA  1 
ATOM   6641 C C   . LYS A 1 1288 ? 158.468 150.337 117.059 1.00 65.15  ? 1288 LYS A C   1 
ATOM   6642 O O   . LYS A 1 1288 ? 157.365 149.819 116.866 1.00 67.10  ? 1288 LYS A O   1 
ATOM   6643 C CB  . LYS A 1 1288 ? 159.241 149.514 119.293 1.00 67.26  ? 1288 LYS A CB  1 
ATOM   6644 C CG  . LYS A 1 1288 ? 160.262 148.584 118.669 1.00 70.25  ? 1288 LYS A CG  1 
ATOM   6645 C CD  . LYS A 1 1288 ? 161.662 149.159 118.759 1.00 73.78  ? 1288 LYS A CD  1 
ATOM   6646 C CE  . LYS A 1 1288 ? 162.696 148.177 118.235 1.00 72.03  ? 1288 LYS A CE  1 
ATOM   6647 N NZ  . LYS A 1 1288 ? 164.077 148.716 118.358 1.00 75.41  ? 1288 LYS A NZ  1 
ATOM   6648 N N   . LEU A 1 1289 ? 159.338 150.568 116.080 1.00 66.82  ? 1289 LEU A N   1 
ATOM   6649 C CA  . LEU A 1 1289 ? 159.110 150.173 114.691 1.00 67.20  ? 1289 LEU A CA  1 
ATOM   6650 C C   . LEU A 1 1289 ? 160.356 149.428 114.222 1.00 70.18  ? 1289 LEU A C   1 
ATOM   6651 O O   . LEU A 1 1289 ? 161.261 150.018 113.628 1.00 67.58  ? 1289 LEU A O   1 
ATOM   6652 C CB  . LEU A 1 1289 ? 158.812 151.384 113.813 1.00 63.46  ? 1289 LEU A CB  1 
ATOM   6653 C CG  . LEU A 1 1289 ? 157.572 152.197 114.183 1.00 61.74  ? 1289 LEU A CG  1 
ATOM   6654 C CD1 . LEU A 1 1289 ? 157.436 153.409 113.282 1.00 60.04  ? 1289 LEU A CD1 1 
ATOM   6655 C CD2 . LEU A 1 1289 ? 156.332 151.330 114.101 1.00 70.86  ? 1289 LEU A CD2 1 
ATOM   6656 N N   . GLU A 1 1290 ? 160.394 148.121 114.484 1.00 91.35  ? 1290 GLU A N   1 
ATOM   6657 C CA  . GLU A 1 1290 ? 161.590 147.343 114.178 1.00 91.66  ? 1290 GLU A CA  1 
ATOM   6658 C C   . GLU A 1 1290 ? 161.746 147.102 112.684 1.00 90.53  ? 1290 GLU A C   1 
ATOM   6659 O O   . GLU A 1 1290 ? 162.855 146.825 112.216 1.00 91.33  ? 1290 GLU A O   1 
ATOM   6660 C CB  . GLU A 1 1290 ? 161.561 146.011 114.929 1.00 88.51  ? 1290 GLU A CB  1 
ATOM   6661 C CG  . GLU A 1 1290 ? 160.503 145.030 114.444 1.00 91.30  ? 1290 GLU A CG  1 
ATOM   6662 C CD  . GLU A 1 1290 ? 159.101 145.407 114.879 1.00 93.84  ? 1290 GLU A CD  1 
ATOM   6663 O OE1 . GLU A 1 1290 ? 158.962 146.315 115.724 1.00 92.38  ? 1290 GLU A OE1 1 
ATOM   6664 O OE2 . GLU A 1 1290 ? 158.137 144.796 114.373 1.00 93.35  ? 1290 GLU A OE2 1 
ATOM   6665 N N   . ASN A 1 1291 ? 160.655 147.191 111.922 1.00 82.53  ? 1291 ASN A N   1 
ATOM   6666 C CA  . ASN A 1 1291 ? 160.743 146.942 110.487 1.00 79.88  ? 1291 ASN A CA  1 
ATOM   6667 C C   . ASN A 1 1291 ? 161.557 148.013 109.776 1.00 84.30  ? 1291 ASN A C   1 
ATOM   6668 O O   . ASN A 1 1291 ? 162.175 147.735 108.742 1.00 87.03  ? 1291 ASN A O   1 
ATOM   6669 C CB  . ASN A 1 1291 ? 159.345 146.849 109.880 1.00 79.88  ? 1291 ASN A CB  1 
ATOM   6670 C CG  . ASN A 1 1291 ? 158.623 145.585 110.282 1.00 86.09  ? 1291 ASN A CG  1 
ATOM   6671 O OD1 . ASN A 1 1291 ? 159.250 144.583 110.623 1.00 88.95  ? 1291 ASN A OD1 1 
ATOM   6672 N ND2 . ASN A 1 1291 ? 157.296 145.621 110.241 1.00 86.94  ? 1291 ASN A ND2 1 
ATOM   6673 N N   . HIS A 1 1292 ? 161.570 149.236 110.303 1.00 75.50  ? 1292 HIS A N   1 
ATOM   6674 C CA  . HIS A 1 1292 ? 162.268 150.345 109.669 1.00 75.42  ? 1292 HIS A CA  1 
ATOM   6675 C C   . HIS A 1 1292 ? 163.375 150.921 110.546 1.00 75.45  ? 1292 HIS A C   1 
ATOM   6676 O O   . HIS A 1 1292 ? 163.823 152.047 110.308 1.00 75.07  ? 1292 HIS A O   1 
ATOM   6677 C CB  . HIS A 1 1292 ? 161.272 151.436 109.278 1.00 76.10  ? 1292 HIS A CB  1 
ATOM   6678 C CG  . HIS A 1 1292 ? 160.255 150.990 108.275 1.00 76.78  ? 1292 HIS A CG  1 
ATOM   6679 N ND1 . HIS A 1 1292 ? 159.321 150.014 108.545 1.00 78.07  ? 1292 HIS A ND1 1 
ATOM   6680 C CD2 . HIS A 1 1292 ? 160.030 151.383 106.999 1.00 81.14  ? 1292 HIS A CD2 1 
ATOM   6681 C CE1 . HIS A 1 1292 ? 158.562 149.827 107.481 1.00 78.73  ? 1292 HIS A CE1 1 
ATOM   6682 N NE2 . HIS A 1 1292 ? 158.971 150.646 106.529 1.00 80.36  ? 1292 HIS A NE2 1 
ATOM   6683 N N   . ASN A 1 1293 ? 163.828 150.169 111.548 1.00 74.65  ? 1293 ASN A N   1 
ATOM   6684 C CA  . ASN A 1 1293 ? 164.925 150.581 112.422 1.00 73.89  ? 1293 ASN A CA  1 
ATOM   6685 C C   . ASN A 1 1293 ? 164.626 151.913 113.105 1.00 72.95  ? 1293 ASN A C   1 
ATOM   6686 O O   . ASN A 1 1293 ? 165.460 152.817 113.155 1.00 78.29  ? 1293 ASN A O   1 
ATOM   6687 C CB  . ASN A 1 1293 ? 166.240 150.654 111.648 1.00 75.36  ? 1293 ASN A CB  1 
ATOM   6688 C CG  . ASN A 1 1293 ? 166.650 149.318 111.073 1.00 77.00  ? 1293 ASN A CG  1 
ATOM   6689 O OD1 . ASN A 1 1293 ? 165.859 148.377 111.033 1.00 74.74  ? 1293 ASN A OD1 1 
ATOM   6690 N ND2 . ASN A 1 1293 ? 167.894 149.227 110.619 1.00 77.57  ? 1293 ASN A ND2 1 
ATOM   6691 N N   . VAL A 1 1294 ? 163.414 152.031 113.640 1.00 67.53  ? 1294 VAL A N   1 
ATOM   6692 C CA  . VAL A 1 1294 ? 162.975 153.249 114.311 1.00 54.87  ? 1294 VAL A CA  1 
ATOM   6693 C C   . VAL A 1 1294 ? 162.449 152.888 115.690 1.00 50.14  ? 1294 VAL A C   1 
ATOM   6694 O O   . VAL A 1 1294 ? 161.607 151.995 115.824 1.00 64.80  ? 1294 VAL A O   1 
ATOM   6695 C CB  . VAL A 1 1294 ? 161.887 153.992 113.514 1.00 52.75  ? 1294 VAL A CB  1 
ATOM   6696 C CG1 . VAL A 1 1294 ? 161.471 155.248 114.249 1.00 57.13  ? 1294 VAL A CG1 1 
ATOM   6697 C CG2 . VAL A 1 1294 ? 162.386 154.326 112.130 1.00 58.82  ? 1294 VAL A CG2 1 
ATOM   6698 N N   . GLN A 1 1295 ? 162.941 153.580 116.711 1.00 60.94  ? 1295 GLN A N   1 
ATOM   6699 C CA  . GLN A 1 1295 ? 162.385 153.489 118.052 1.00 68.27  ? 1295 GLN A CA  1 
ATOM   6700 C C   . GLN A 1 1295 ? 162.418 154.871 118.674 1.00 72.36  ? 1295 GLN A C   1 
ATOM   6701 O O   . GLN A 1 1295 ? 163.474 155.508 118.721 1.00 77.94  ? 1295 GLN A O   1 
ATOM   6702 C CB  . GLN A 1 1295 ? 163.156 152.500 118.927 1.00 66.16  ? 1295 GLN A CB  1 
ATOM   6703 C CG  . GLN A 1 1295 ? 162.607 152.393 120.337 1.00 70.99  ? 1295 GLN A CG  1 
ATOM   6704 C CD  . GLN A 1 1295 ? 163.387 151.422 121.193 1.00 78.01  ? 1295 GLN A CD  1 
ATOM   6705 O OE1 . GLN A 1 1295 ? 164.452 150.948 120.801 1.00 79.40  ? 1295 GLN A OE1 1 
ATOM   6706 N NE2 . GLN A 1 1295 ? 162.859 151.119 122.373 1.00 77.13  ? 1295 GLN A NE2 1 
ATOM   6707 N N   . MET A 1 1296 ? 161.270 155.327 119.155 1.00 51.26  ? 1296 MET A N   1 
ATOM   6708 C CA  . MET A 1 1296 ? 161.122 156.680 119.664 1.00 44.89  ? 1296 MET A CA  1 
ATOM   6709 C C   . MET A 1 1296 ? 161.129 156.659 121.185 1.00 51.37  ? 1296 MET A C   1 
ATOM   6710 O O   . MET A 1 1296 ? 160.474 155.817 121.804 1.00 59.71  ? 1296 MET A O   1 
ATOM   6711 C CB  . MET A 1 1296 ? 159.835 157.308 119.135 1.00 49.78  ? 1296 MET A CB  1 
ATOM   6712 C CG  . MET A 1 1296 ? 159.734 157.291 117.622 1.00 52.22  ? 1296 MET A CG  1 
ATOM   6713 S SD  . MET A 1 1296 ? 158.280 158.151 117.009 1.00 67.68  ? 1296 MET A SD  1 
ATOM   6714 C CE  . MET A 1 1296 ? 158.545 159.778 117.697 1.00 45.91  ? 1296 MET A CE  1 
ATOM   6715 N N   . VAL A 1 1297 ? 161.878 157.580 121.778 1.00 50.99  ? 1297 VAL A N   1 
ATOM   6716 C CA  . VAL A 1 1297 ? 162.021 157.644 123.226 1.00 48.57  ? 1297 VAL A CA  1 
ATOM   6717 C C   . VAL A 1 1297 ? 160.826 158.377 123.817 1.00 47.50  ? 1297 VAL A C   1 
ATOM   6718 O O   . VAL A 1 1297 ? 160.502 159.495 123.404 1.00 58.44  ? 1297 VAL A O   1 
ATOM   6719 C CB  . VAL A 1 1297 ? 163.335 158.339 123.608 1.00 45.20  ? 1297 VAL A CB  1 
ATOM   6720 C CG1 . VAL A 1 1297 ? 163.600 158.180 125.089 1.00 53.23  ? 1297 VAL A CG1 1 
ATOM   6721 C CG2 . VAL A 1 1297 ? 164.481 157.780 122.791 1.00 54.38  ? 1297 VAL A CG2 1 
ATOM   6722 N N   . CYS A 1 1298 ? 160.171 157.753 124.788 1.00 62.94  ? 1298 CYS A N   1 
ATOM   6723 C CA  . CYS A 1 1298 ? 159.067 158.367 125.511 1.00 68.17  ? 1298 CYS A CA  1 
ATOM   6724 C C   . CYS A 1 1298 ? 159.601 158.958 126.805 1.00 67.68  ? 1298 CYS A C   1 
ATOM   6725 O O   . CYS A 1 1298 ? 160.325 158.284 127.544 1.00 80.39  ? 1298 CYS A O   1 
ATOM   6726 C CB  . CYS A 1 1298 ? 157.971 157.343 125.806 1.00 73.76  ? 1298 CYS A CB  1 
ATOM   6727 S SG  . CYS A 1 1298 ? 157.531 156.307 124.395 1.00 82.95  ? 1298 CYS A SG  1 
ATOM   6728 N N   . PHE A 1 1299 ? 159.253 160.212 127.079 1.00 59.58  ? 1299 PHE A N   1 
ATOM   6729 C CA  . PHE A 1 1299 ? 159.806 160.929 128.214 1.00 57.63  ? 1299 PHE A CA  1 
ATOM   6730 C C   . PHE A 1 1299 ? 158.715 161.657 128.982 1.00 60.26  ? 1299 PHE A C   1 
ATOM   6731 O O   . PHE A 1 1299 ? 157.721 162.116 128.405 1.00 69.39  ? 1299 PHE A O   1 
ATOM   6732 C CB  . PHE A 1 1299 ? 160.874 161.930 127.772 1.00 61.30  ? 1299 PHE A CB  1 
ATOM   6733 C CG  . PHE A 1 1299 ? 161.533 162.647 128.911 1.00 66.20  ? 1299 PHE A CG  1 
ATOM   6734 C CD1 . PHE A 1 1299 ? 162.536 162.037 129.639 1.00 68.06  ? 1299 PHE A CD1 1 
ATOM   6735 C CD2 . PHE A 1 1299 ? 161.146 163.928 129.257 1.00 64.99  ? 1299 PHE A CD2 1 
ATOM   6736 C CE1 . PHE A 1 1299 ? 163.143 162.690 130.689 1.00 64.78  ? 1299 PHE A CE1 1 
ATOM   6737 C CE2 . PHE A 1 1299 ? 161.749 164.586 130.307 1.00 66.88  ? 1299 PHE A CE2 1 
ATOM   6738 C CZ  . PHE A 1 1299 ? 162.748 163.966 131.023 1.00 68.21  ? 1299 PHE A CZ  1 
ATOM   6739 N N   . HIS A 1 1300 ? 158.922 161.751 130.293 1.00 67.74  ? 1300 HIS A N   1 
ATOM   6740 C CA  . HIS A 1 1300 ? 158.079 162.511 131.199 1.00 68.82  ? 1300 HIS A CA  1 
ATOM   6741 C C   . HIS A 1 1300 ? 158.873 162.760 132.472 1.00 77.94  ? 1300 HIS A C   1 
ATOM   6742 O O   . HIS A 1 1300 ? 159.927 162.160 132.692 1.00 81.21  ? 1300 HIS A O   1 
ATOM   6743 C CB  . HIS A 1 1300 ? 156.771 161.777 131.506 1.00 67.61  ? 1300 HIS A CB  1 
ATOM   6744 C CG  . HIS A 1 1300 ? 155.819 162.567 132.345 1.00 70.19  ? 1300 HIS A CG  1 
ATOM   6745 N ND1 . HIS A 1 1300 ? 155.578 163.907 132.132 1.00 71.20  ? 1300 HIS A ND1 1 
ATOM   6746 C CD2 . HIS A 1 1300 ? 155.054 162.211 133.403 1.00 72.13  ? 1300 HIS A CD2 1 
ATOM   6747 C CE1 . HIS A 1 1300 ? 154.701 164.341 133.020 1.00 73.33  ? 1300 HIS A CE1 1 
ATOM   6748 N NE2 . HIS A 1 1300 ? 154.367 163.331 133.802 1.00 77.44  ? 1300 HIS A NE2 1 
ATOM   6749 N N   . LEU A 1 1301 ? 158.362 163.663 133.309 1.00 81.97  ? 1301 LEU A N   1 
ATOM   6750 C CA  . LEU A 1 1301 ? 159.004 163.925 134.592 1.00 82.06  ? 1301 LEU A CA  1 
ATOM   6751 C C   . LEU A 1 1301 ? 159.061 162.662 135.440 1.00 81.67  ? 1301 LEU A C   1 
ATOM   6752 O O   . LEU A 1 1301 ? 160.065 162.390 136.108 1.00 79.33  ? 1301 LEU A O   1 
ATOM   6753 C CB  . LEU A 1 1301 ? 158.258 165.036 135.330 1.00 81.22  ? 1301 LEU A CB  1 
ATOM   6754 C CG  . LEU A 1 1301 ? 158.746 165.340 136.745 1.00 85.11  ? 1301 LEU A CG  1 
ATOM   6755 C CD1 . LEU A 1 1301 ? 160.200 165.777 136.719 1.00 85.91  ? 1301 LEU A CD1 1 
ATOM   6756 C CD2 . LEU A 1 1301 ? 157.874 166.400 137.396 1.00 83.57  ? 1301 LEU A CD2 1 
ATOM   6757 N N   . SER A 1 1302 ? 157.992 161.866 135.411 1.00 77.70  ? 1302 SER A N   1 
ATOM   6758 C CA  . SER A 1 1302 ? 157.919 160.681 136.257 1.00 74.64  ? 1302 SER A CA  1 
ATOM   6759 C C   . SER A 1 1302 ? 158.830 159.566 135.765 1.00 73.71  ? 1302 SER A C   1 
ATOM   6760 O O   . SER A 1 1302 ? 158.945 158.529 136.427 1.00 83.89  ? 1302 SER A O   1 
ATOM   6761 C CB  . SER A 1 1302 ? 156.477 160.184 136.330 1.00 79.97  ? 1302 SER A CB  1 
ATOM   6762 O OG  . SER A 1 1302 ? 156.016 159.791 135.050 1.00 78.50  ? 1302 SER A OG  1 
ATOM   6763 N N   . SER A 1 1303 ? 159.454 159.739 134.598 1.00 74.33  ? 1303 SER A N   1 
ATOM   6764 C CA  . SER A 1 1303 ? 160.299 158.684 134.046 1.00 81.82  ? 1303 SER A CA  1 
ATOM   6765 C C   . SER A 1 1303 ? 161.488 158.393 134.950 1.00 78.79  ? 1303 SER A C   1 
ATOM   6766 O O   . SER A 1 1303 ? 161.889 157.235 135.112 1.00 84.27  ? 1303 SER A O   1 
ATOM   6767 C CB  . SER A 1 1303 ? 160.773 159.073 132.646 1.00 78.84  ? 1303 SER A CB  1 
ATOM   6768 O OG  . SER A 1 1303 ? 161.602 158.067 132.094 1.00 76.80  ? 1303 SER A OG  1 
ATOM   6769 N N   . ILE A 1 1304 ? 162.067 159.436 135.547 1.00 67.43  ? 1304 ILE A N   1 
ATOM   6770 C CA  . ILE A 1 1304 ? 163.200 159.255 136.452 1.00 71.17  ? 1304 ILE A CA  1 
ATOM   6771 C C   . ILE A 1 1304 ? 162.796 158.393 137.639 1.00 75.49  ? 1304 ILE A C   1 
ATOM   6772 O O   . ILE A 1 1304 ? 163.493 157.441 138.018 1.00 79.90  ? 1304 ILE A O   1 
ATOM   6773 C CB  . ILE A 1 1304 ? 163.727 160.623 136.915 1.00 73.57  ? 1304 ILE A CB  1 
ATOM   6774 C CG1 . ILE A 1 1304 ? 163.820 161.582 135.731 1.00 78.32  ? 1304 ILE A CG1 1 
ATOM   6775 C CG2 . ILE A 1 1304 ? 165.069 160.471 137.593 1.00 67.38  ? 1304 ILE A CG2 1 
ATOM   6776 C CD1 . ILE A 1 1304 ? 163.892 163.029 136.136 1.00 74.74  ? 1304 ILE A CD1 1 
ATOM   6777 N N   . PHE A 1 1305 ? 161.655 158.719 138.244 1.00 73.07  ? 1305 PHE A N   1 
ATOM   6778 C CA  . PHE A 1 1305 ? 161.203 157.979 139.414 1.00 66.60  ? 1305 PHE A CA  1 
ATOM   6779 C C   . PHE A 1 1305 ? 160.817 156.554 139.045 1.00 66.00  ? 1305 PHE A C   1 
ATOM   6780 O O   . PHE A 1 1305 ? 161.041 155.622 139.826 1.00 74.04  ? 1305 PHE A O   1 
ATOM   6781 C CB  . PHE A 1 1305 ? 160.040 158.716 140.069 1.00 65.53  ? 1305 PHE A CB  1 
ATOM   6782 C CG  . PHE A 1 1305 ? 160.290 160.185 140.256 1.00 67.59  ? 1305 PHE A CG  1 
ATOM   6783 C CD1 . PHE A 1 1305 ? 161.318 160.627 141.067 1.00 67.90  ? 1305 PHE A CD1 1 
ATOM   6784 C CD2 . PHE A 1 1305 ? 159.498 161.123 139.620 1.00 69.31  ? 1305 PHE A CD2 1 
ATOM   6785 C CE1 . PHE A 1 1305 ? 161.552 161.975 141.240 1.00 67.07  ? 1305 PHE A CE1 1 
ATOM   6786 C CE2 . PHE A 1 1305 ? 159.728 162.472 139.791 1.00 70.73  ? 1305 PHE A CE2 1 
ATOM   6787 C CZ  . PHE A 1 1305 ? 160.756 162.897 140.602 1.00 68.57  ? 1305 PHE A CZ  1 
ATOM   6788 N N   . ASN A 1 1306 ? 160.243 156.360 137.857 1.00 66.88  ? 1306 ASN A N   1 
ATOM   6789 C CA  . ASN A 1 1306 ? 159.937 155.008 137.403 1.00 68.38  ? 1306 ASN A CA  1 
ATOM   6790 C C   . ASN A 1 1306 ? 161.208 154.190 137.227 1.00 73.11  ? 1306 ASN A C   1 
ATOM   6791 O O   . ASN A 1 1306 ? 161.258 153.012 137.602 1.00 78.73  ? 1306 ASN A O   1 
ATOM   6792 C CB  . ASN A 1 1306 ? 159.142 155.058 136.099 1.00 70.77  ? 1306 ASN A CB  1 
ATOM   6793 C CG  . ASN A 1 1306 ? 157.779 155.693 136.271 1.00 78.06  ? 1306 ASN A CG  1 
ATOM   6794 O OD1 . ASN A 1 1306 ? 157.164 155.592 137.331 1.00 81.63  ? 1306 ASN A OD1 1 
ATOM   6795 N ND2 . ASN A 1 1306 ? 157.299 156.355 135.227 1.00 76.89  ? 1306 ASN A ND2 1 
ATOM   6796 N N   . GLU A 1 1307 ? 162.250 154.801 136.662 1.00 73.87  ? 1307 GLU A N   1 
ATOM   6797 C CA  . GLU A 1 1307 ? 163.527 154.110 136.516 1.00 75.25  ? 1307 GLU A CA  1 
ATOM   6798 C C   . GLU A 1 1307 ? 164.102 153.734 137.874 1.00 75.75  ? 1307 GLU A C   1 
ATOM   6799 O O   . GLU A 1 1307 ? 164.614 152.622 138.065 1.00 81.42  ? 1307 GLU A O   1 
ATOM   6800 C CB  . GLU A 1 1307 ? 164.505 154.991 135.742 1.00 78.89  ? 1307 GLU A CB  1 
ATOM   6801 C CG  . GLU A 1 1307 ? 165.894 154.405 135.610 1.00 81.79  ? 1307 GLU A CG  1 
ATOM   6802 C CD  . GLU A 1 1307 ? 166.878 155.383 135.009 1.00 81.41  ? 1307 GLU A CD  1 
ATOM   6803 O OE1 . GLU A 1 1307 ? 166.576 156.594 134.992 1.00 82.19  ? 1307 GLU A OE1 1 
ATOM   6804 O OE2 . GLU A 1 1307 ? 167.952 154.943 134.550 1.00 78.87  ? 1307 GLU A OE2 1 
ATOM   6805 N N   . THR A 1 1308 ? 164.030 154.656 138.835 1.00 68.78  ? 1308 THR A N   1 
ATOM   6806 C CA  . THR A 1 1308 ? 164.530 154.358 140.173 1.00 71.35  ? 1308 THR A CA  1 
ATOM   6807 C C   . THR A 1 1308 ? 163.751 153.214 140.811 1.00 73.82  ? 1308 THR A C   1 
ATOM   6808 O O   . THR A 1 1308 ? 164.340 152.321 141.432 1.00 77.78  ? 1308 THR A O   1 
ATOM   6809 C CB  . THR A 1 1308 ? 164.462 155.606 141.049 1.00 69.80  ? 1308 THR A CB  1 
ATOM   6810 O OG1 . THR A 1 1308 ? 165.324 156.615 140.511 1.00 74.53  ? 1308 THR A OG1 1 
ATOM   6811 C CG2 . THR A 1 1308 ? 164.897 155.283 142.464 1.00 67.91  ? 1308 THR A CG2 1 
ATOM   6812 N N   . ASP A 1 1309 ? 162.423 153.226 140.670 1.00 75.92  ? 1309 ASP A N   1 
ATOM   6813 C CA  . ASP A 1 1309 ? 161.606 152.158 141.235 1.00 69.97  ? 1309 ASP A CA  1 
ATOM   6814 C C   . ASP A 1 1309 ? 161.880 150.825 140.556 1.00 75.51  ? 1309 ASP A C   1 
ATOM   6815 O O   . ASP A 1 1309 ? 161.738 149.770 141.181 1.00 79.41  ? 1309 ASP A O   1 
ATOM   6816 C CB  . ASP A 1 1309 ? 160.125 152.516 141.124 1.00 76.04  ? 1309 ASP A CB  1 
ATOM   6817 C CG  . ASP A 1 1309 ? 159.765 153.754 141.918 1.00 81.28  ? 1309 ASP A CG  1 
ATOM   6818 O OD1 . ASP A 1 1309 ? 160.641 154.273 142.639 1.00 77.94  ? 1309 ASP A OD1 1 
ATOM   6819 O OD2 . ASP A 1 1309 ? 158.606 154.209 141.820 1.00 81.34  ? 1309 ASP A OD2 1 
ATOM   6820 N N   . GLU A 1 1310 ? 162.250 150.847 139.278 1.00 82.95  ? 1310 GLU A N   1 
ATOM   6821 C CA  . GLU A 1 1310 ? 162.592 149.604 138.600 1.00 79.71  ? 1310 GLU A CA  1 
ATOM   6822 C C   . GLU A 1 1310 ? 163.966 149.090 139.011 1.00 85.03  ? 1310 GLU A C   1 
ATOM   6823 O O   . GLU A 1 1310 ? 164.189 147.876 139.024 1.00 86.86  ? 1310 GLU A O   1 
ATOM   6824 C CB  . GLU A 1 1310 ? 162.530 149.798 137.085 1.00 84.88  ? 1310 GLU A CB  1 
ATOM   6825 C CG  . GLU A 1 1310 ? 162.655 148.511 136.288 1.00 88.00  ? 1310 GLU A CG  1 
ATOM   6826 C CD  . GLU A 1 1310 ? 162.448 148.725 134.802 1.00 91.40  ? 1310 GLU A CD  1 
ATOM   6827 O OE1 . GLU A 1 1310 ? 162.079 149.851 134.407 1.00 91.92  ? 1310 GLU A OE1 1 
ATOM   6828 O OE2 . GLU A 1 1310 ? 162.653 147.767 134.027 1.00 89.82  ? 1310 GLU A OE2 1 
ATOM   6829 N N   . SER A 1 1311 ? 164.895 149.988 139.343 1.00 82.49  ? 1311 SER A N   1 
ATOM   6830 C CA  . SER A 1 1311 ? 166.242 149.557 139.710 1.00 80.71  ? 1311 SER A CA  1 
ATOM   6831 C C   . SER A 1 1311 ? 166.366 149.190 141.185 1.00 80.79  ? 1311 SER A C   1 
ATOM   6832 O O   . SER A 1 1311 ? 167.296 148.457 141.562 1.00 83.10  ? 1311 SER A O   1 
ATOM   6833 C CB  . SER A 1 1311 ? 167.251 150.651 139.367 1.00 79.12  ? 1311 SER A CB  1 
ATOM   6834 O OG  . SER A 1 1311 ? 168.556 150.284 139.778 1.00 84.17  ? 1311 SER A OG  1 
ATOM   6835 N N   . ILE A 1 1312 ? 165.455 149.691 142.024 1.00 74.33  ? 1312 ILE A N   1 
ATOM   6836 C CA  . ILE A 1 1312 ? 165.600 149.521 143.467 1.00 73.03  ? 1312 ILE A CA  1 
ATOM   6837 C C   . ILE A 1 1312 ? 165.545 148.048 143.848 1.00 77.06  ? 1312 ILE A C   1 
ATOM   6838 O O   . ILE A 1 1312 ? 166.213 147.618 144.793 1.00 81.78  ? 1312 ILE A O   1 
ATOM   6839 C CB  . ILE A 1 1312 ? 164.539 150.348 144.218 1.00 72.18  ? 1312 ILE A CB  1 
ATOM   6840 C CG1 . ILE A 1 1312 ? 164.833 150.361 145.717 1.00 78.88  ? 1312 ILE A CG1 1 
ATOM   6841 C CG2 . ILE A 1 1312 ? 163.149 149.802 143.976 1.00 73.06  ? 1312 ILE A CG2 1 
ATOM   6842 C CD1 . ILE A 1 1312 ? 166.170 150.967 146.070 1.00 76.19  ? 1312 ILE A CD1 1 
ATOM   6843 N N   . ILE A 1 1313 ? 164.759 147.249 143.124 1.00 77.00  ? 1313 ILE A N   1 
ATOM   6844 C CA  . ILE A 1 1313 ? 164.646 145.834 143.465 1.00 76.84  ? 1313 ILE A CA  1 
ATOM   6845 C C   . ILE A 1 1313 ? 165.992 145.137 143.318 1.00 77.79  ? 1313 ILE A C   1 
ATOM   6846 O O   . ILE A 1 1313 ? 166.433 144.413 144.218 1.00 76.62  ? 1313 ILE A O   1 
ATOM   6847 C CB  . ILE A 1 1313 ? 163.556 145.160 142.611 1.00 79.00  ? 1313 ILE A CB  1 
ATOM   6848 C CG1 . ILE A 1 1313 ? 163.731 143.640 142.615 1.00 79.45  ? 1313 ILE A CG1 1 
ATOM   6849 C CG2 . ILE A 1 1313 ? 163.572 145.701 141.197 1.00 77.29  ? 1313 ILE A CG2 1 
ATOM   6850 C CD1 . ILE A 1 1313 ? 163.469 142.993 143.954 1.00 77.54  ? 1313 ILE A CD1 1 
ATOM   6851 N N   . GLU A 1 1314 ? 166.672 145.348 142.190 1.00 82.38  ? 1314 GLU A N   1 
ATOM   6852 C CA  . GLU A 1 1314 ? 167.975 144.725 141.983 1.00 80.62  ? 1314 GLU A CA  1 
ATOM   6853 C C   . GLU A 1 1314 ? 168.999 145.263 142.974 1.00 75.52  ? 1314 GLU A C   1 
ATOM   6854 O O   . GLU A 1 1314 ? 169.791 144.499 143.548 1.00 80.60  ? 1314 GLU A O   1 
ATOM   6855 C CB  . GLU A 1 1314 ? 168.440 144.956 140.546 1.00 82.89  ? 1314 GLU A CB  1 
ATOM   6856 C CG  . GLU A 1 1314 ? 169.709 144.212 140.162 1.00 83.10  ? 1314 GLU A CG  1 
ATOM   6857 C CD  . GLU A 1 1314 ? 169.457 142.759 139.800 1.00 84.85  ? 1314 GLU A CD  1 
ATOM   6858 O OE1 . GLU A 1 1314 ? 168.305 142.296 139.937 1.00 86.39  ? 1314 GLU A OE1 1 
ATOM   6859 O OE2 . GLU A 1 1314 ? 170.413 142.079 139.372 1.00 81.86  ? 1314 GLU A OE2 1 
ATOM   6860 N N   . VAL A 1 1315 ? 168.992 146.581 143.194 1.00 67.30  ? 1315 VAL A N   1 
ATOM   6861 C CA  . VAL A 1 1315 ? 169.956 147.177 144.117 1.00 70.99  ? 1315 VAL A CA  1 
ATOM   6862 C C   . VAL A 1 1315 ? 169.797 146.571 145.505 1.00 68.55  ? 1315 VAL A C   1 
ATOM   6863 O O   . VAL A 1 1315 ? 170.778 146.194 146.158 1.00 70.52  ? 1315 VAL A O   1 
ATOM   6864 C CB  . VAL A 1 1315 ? 169.796 148.707 144.148 1.00 72.02  ? 1315 VAL A CB  1 
ATOM   6865 C CG1 . VAL A 1 1315 ? 170.646 149.305 145.252 1.00 69.26  ? 1315 VAL A CG1 1 
ATOM   6866 C CG2 . VAL A 1 1315 ? 170.172 149.304 142.805 1.00 69.78  ? 1315 VAL A CG2 1 
ATOM   6867 N N   . THR A 1 1316 ? 168.553 146.449 145.965 1.00 66.59  ? 1316 THR A N   1 
ATOM   6868 C CA  . THR A 1 1316 ? 168.289 145.895 147.285 1.00 68.81  ? 1316 THR A CA  1 
ATOM   6869 C C   . THR A 1 1316 ? 168.629 144.415 147.347 1.00 71.30  ? 1316 THR A C   1 
ATOM   6870 O O   . THR A 1 1316 ? 169.167 143.937 148.347 1.00 79.66  ? 1316 THR A O   1 
ATOM   6871 C CB  . THR A 1 1316 ? 166.829 146.117 147.653 1.00 68.30  ? 1316 THR A CB  1 
ATOM   6872 O OG1 . THR A 1 1316 ? 166.501 147.492 147.436 1.00 70.78  ? 1316 THR A OG1 1 
ATOM   6873 C CG2 . THR A 1 1316 ? 166.599 145.758 149.108 1.00 68.55  ? 1316 THR A CG2 1 
ATOM   6874 N N   . LEU A 1 1317 ? 168.302 143.665 146.296 1.00 57.71  ? 1317 LEU A N   1 
ATOM   6875 C CA  . LEU A 1 1317 ? 168.604 142.241 146.312 1.00 54.98  ? 1317 LEU A CA  1 
ATOM   6876 C C   . LEU A 1 1317 ? 170.101 141.981 146.337 1.00 57.66  ? 1317 LEU A C   1 
ATOM   6877 O O   . LEU A 1 1317 ? 170.529 140.933 146.832 1.00 64.96  ? 1317 LEU A O   1 
ATOM   6878 C CB  . LEU A 1 1317 ? 167.967 141.554 145.107 1.00 63.27  ? 1317 LEU A CB  1 
ATOM   6879 C CG  . LEU A 1 1317 ? 167.817 140.040 145.238 1.00 66.61  ? 1317 LEU A CG  1 
ATOM   6880 C CD1 . LEU A 1 1317 ? 166.989 139.704 146.465 1.00 61.29  ? 1317 LEU A CD1 1 
ATOM   6881 C CD2 . LEU A 1 1317 ? 167.190 139.452 143.987 1.00 66.10  ? 1317 LEU A CD2 1 
ATOM   6882 N N   . ILE A 1 1318 ? 170.907 142.906 145.820 1.00 54.86  ? 1318 ILE A N   1 
ATOM   6883 C CA  . ILE A 1 1318 ? 172.357 142.761 145.930 1.00 51.08  ? 1318 ILE A CA  1 
ATOM   6884 C C   . ILE A 1 1318 ? 172.838 143.188 147.313 1.00 57.47  ? 1318 ILE A C   1 
ATOM   6885 O O   . ILE A 1 1318 ? 173.627 142.487 147.964 1.00 55.56  ? 1318 ILE A O   1 
ATOM   6886 C CB  . ILE A 1 1318 ? 173.064 143.559 144.821 1.00 57.14  ? 1318 ILE A CB  1 
ATOM   6887 C CG1 . ILE A 1 1318 ? 172.696 142.999 143.448 1.00 60.33  ? 1318 ILE A CG1 1 
ATOM   6888 C CG2 . ILE A 1 1318 ? 174.566 143.526 145.019 1.00 62.58  ? 1318 ILE A CG2 1 
ATOM   6889 C CD1 . ILE A 1 1318 ? 173.341 143.736 142.302 1.00 60.46  ? 1318 ILE A CD1 1 
ATOM   6890 N N   . ASN A 1 1319 ? 172.369 144.349 147.777 1.00 62.88  ? 1319 ASN A N   1 
ATOM   6891 C CA  . ASN A 1 1319 ? 172.839 144.890 149.048 1.00 57.36  ? 1319 ASN A CA  1 
ATOM   6892 C C   . ASN A 1 1319 ? 172.469 143.980 150.208 1.00 58.92  ? 1319 ASN A C   1 
ATOM   6893 O O   . ASN A 1 1319 ? 173.251 143.807 151.146 1.00 65.41  ? 1319 ASN A O   1 
ATOM   6894 C CB  . ASN A 1 1319 ? 172.270 146.291 149.265 1.00 59.29  ? 1319 ASN A CB  1 
ATOM   6895 C CG  . ASN A 1 1319 ? 172.970 147.337 148.430 1.00 65.22  ? 1319 ASN A CG  1 
ATOM   6896 O OD1 . ASN A 1 1319 ? 174.124 147.167 148.043 1.00 65.64  ? 1319 ASN A OD1 1 
ATOM   6897 N ND2 . ASN A 1 1319 ? 172.276 148.432 148.153 1.00 66.49  ? 1319 ASN A ND2 1 
ATOM   6898 N N   . LEU A 1 1320 ? 171.268 143.404 150.172 1.00 51.07  ? 1320 LEU A N   1 
ATOM   6899 C CA  . LEU A 1 1320 ? 170.824 142.528 151.248 1.00 50.74  ? 1320 LEU A CA  1 
ATOM   6900 C C   . LEU A 1 1320 ? 171.710 141.298 151.351 1.00 54.86  ? 1320 LEU A C   1 
ATOM   6901 O O   . LEU A 1 1320 ? 172.093 140.886 152.450 1.00 64.67  ? 1320 LEU A O   1 
ATOM   6902 C CB  . LEU A 1 1320 ? 169.369 142.126 151.017 1.00 55.47  ? 1320 LEU A CB  1 
ATOM   6903 C CG  . LEU A 1 1320 ? 168.787 141.129 152.016 1.00 54.39  ? 1320 LEU A CG  1 
ATOM   6904 C CD1 . LEU A 1 1320 ? 168.847 141.696 153.419 1.00 55.99  ? 1320 LEU A CD1 1 
ATOM   6905 C CD2 . LEU A 1 1320 ? 167.361 140.778 151.639 1.00 51.62  ? 1320 LEU A CD2 1 
ATOM   6906 N N   . GLY A 1 1321 ? 172.050 140.701 150.215 1.00 54.29  ? 1321 GLY A N   1 
ATOM   6907 C CA  . GLY A 1 1321 ? 172.930 139.553 150.211 1.00 55.35  ? 1321 GLY A CA  1 
ATOM   6908 C C   . GLY A 1 1321 ? 174.307 139.895 150.734 1.00 55.09  ? 1321 GLY A C   1 
ATOM   6909 O O   . GLY A 1 1321 ? 174.874 139.157 151.550 1.00 56.93  ? 1321 GLY A O   1 
ATOM   6910 N N   . ILE A 1 1322 ? 174.853 141.024 150.276 1.00 54.20  ? 1322 ILE A N   1 
ATOM   6911 C CA  . ILE A 1 1322 ? 176.168 141.438 150.751 1.00 52.60  ? 1322 ILE A CA  1 
ATOM   6912 C C   . ILE A 1 1322 ? 176.156 141.696 152.250 1.00 57.45  ? 1322 ILE A C   1 
ATOM   6913 O O   . ILE A 1 1322 ? 177.094 141.310 152.954 1.00 59.44  ? 1322 ILE A O   1 
ATOM   6914 C CB  . ILE A 1 1322 ? 176.655 142.681 149.984 1.00 49.88  ? 1322 ILE A CB  1 
ATOM   6915 C CG1 . ILE A 1 1322 ? 176.806 142.361 148.498 1.00 51.18  ? 1322 ILE A CG1 1 
ATOM   6916 C CG2 . ILE A 1 1322 ? 177.973 143.174 150.551 1.00 45.72  ? 1322 ILE A CG2 1 
ATOM   6917 C CD1 . ILE A 1 1322 ? 177.288 143.528 147.674 1.00 50.04  ? 1322 ILE A CD1 1 
ATOM   6918 N N   . THR A 1 1323 ? 175.105 142.341 152.758 1.00 54.40  ? 1323 THR A N   1 
ATOM   6919 C CA  . THR A 1 1323 ? 174.995 142.606 154.187 1.00 51.54  ? 1323 THR A CA  1 
ATOM   6920 C C   . THR A 1 1323 ? 174.879 141.312 154.979 1.00 53.25  ? 1323 THR A C   1 
ATOM   6921 O O   . THR A 1 1323 ? 175.530 141.144 156.016 1.00 61.75  ? 1323 THR A O   1 
ATOM   6922 C CB  . THR A 1 1323 ? 173.790 143.508 154.455 1.00 46.07  ? 1323 THR A CB  1 
ATOM   6923 O OG1 . THR A 1 1323 ? 174.018 144.797 153.876 1.00 53.99  ? 1323 THR A OG1 1 
ATOM   6924 C CG2 . THR A 1 1323 ? 173.560 143.665 155.941 1.00 45.74  ? 1323 THR A CG2 1 
ATOM   6925 N N   . ILE A 1 1324 ? 174.046 140.383 154.505 1.00 51.69  ? 1324 ILE A N   1 
ATOM   6926 C CA  . ILE A 1 1324 ? 173.819 139.137 155.233 1.00 51.52  ? 1324 ILE A CA  1 
ATOM   6927 C C   . ILE A 1 1324 ? 175.106 138.332 155.317 1.00 52.37  ? 1324 ILE A C   1 
ATOM   6928 O O   . ILE A 1 1324 ? 175.462 137.805 156.375 1.00 64.02  ? 1324 ILE A O   1 
ATOM   6929 C CB  . ILE A 1 1324 ? 172.691 138.323 154.579 1.00 56.45  ? 1324 ILE A CB  1 
ATOM   6930 C CG1 . ILE A 1 1324 ? 171.333 138.942 154.905 1.00 57.83  ? 1324 ILE A CG1 1 
ATOM   6931 C CG2 . ILE A 1 1324 ? 172.736 136.880 155.045 1.00 55.75  ? 1324 ILE A CG2 1 
ATOM   6932 C CD1 . ILE A 1 1324 ? 170.160 138.136 154.401 1.00 59.22  ? 1324 ILE A CD1 1 
ATOM   6933 N N   . LEU A 1 1325 ? 175.828 138.228 154.199 1.00 55.04  ? 1325 LEU A N   1 
ATOM   6934 C CA  . LEU A 1 1325 ? 177.067 137.457 154.201 1.00 60.35  ? 1325 LEU A CA  1 
ATOM   6935 C C   . LEU A 1 1325 ? 178.076 138.037 155.186 1.00 56.61  ? 1325 LEU A C   1 
ATOM   6936 O O   . LEU A 1 1325 ? 178.673 137.309 155.991 1.00 56.69  ? 1325 LEU A O   1 
ATOM   6937 C CB  . LEU A 1 1325 ? 177.657 137.415 152.793 1.00 59.60  ? 1325 LEU A CB  1 
ATOM   6938 C CG  . LEU A 1 1325 ? 179.008 136.714 152.679 1.00 59.83  ? 1325 LEU A CG  1 
ATOM   6939 C CD1 . LEU A 1 1325 ? 178.885 135.267 153.118 1.00 63.09  ? 1325 LEU A CD1 1 
ATOM   6940 C CD2 . LEU A 1 1325 ? 179.540 136.805 151.260 1.00 60.46  ? 1325 LEU A CD2 1 
ATOM   6941 N N   . THR A 1 1326 ? 178.263 139.356 155.145 1.00 47.40  ? 1326 THR A N   1 
ATOM   6942 C CA  . THR A 1 1326 ? 179.231 140.003 156.021 1.00 50.14  ? 1326 THR A CA  1 
ATOM   6943 C C   . THR A 1 1326 ? 178.841 139.851 157.484 1.00 60.10  ? 1326 THR A C   1 
ATOM   6944 O O   . THR A 1 1326 ? 179.683 139.548 158.337 1.00 66.71  ? 1326 THR A O   1 
ATOM   6945 C CB  . THR A 1 1326 ? 179.357 141.479 155.654 1.00 50.82  ? 1326 THR A CB  1 
ATOM   6946 O OG1 . THR A 1 1326 ? 179.464 141.607 154.232 1.00 64.97  ? 1326 THR A OG1 1 
ATOM   6947 C CG2 . THR A 1 1326 ? 180.589 142.078 156.300 1.00 51.19  ? 1326 THR A CG2 1 
ATOM   6948 N N   . ILE A 1 1327 ? 177.560 140.059 157.794 1.00 56.58  ? 1327 ILE A N   1 
ATOM   6949 C CA  . ILE A 1 1327 ? 177.107 139.954 159.176 1.00 46.03  ? 1327 ILE A CA  1 
ATOM   6950 C C   . ILE A 1 1327 ? 177.259 138.528 159.679 1.00 47.41  ? 1327 ILE A C   1 
ATOM   6951 O O   . ILE A 1 1327 ? 177.661 138.301 160.826 1.00 56.70  ? 1327 ILE A O   1 
ATOM   6952 C CB  . ILE A 1 1327 ? 175.656 140.451 159.303 1.00 46.82  ? 1327 ILE A CB  1 
ATOM   6953 C CG1 . ILE A 1 1327 ? 175.598 141.965 159.120 1.00 49.12  ? 1327 ILE A CG1 1 
ATOM   6954 C CG2 . ILE A 1 1327 ? 175.073 140.062 160.645 1.00 53.84  ? 1327 ILE A CG2 1 
ATOM   6955 C CD1 . ILE A 1 1327 ? 174.219 142.538 159.315 1.00 59.98  ? 1327 ILE A CD1 1 
ATOM   6956 N N   . LEU A 1 1328 ? 176.936 137.543 158.839 1.00 49.16  ? 1328 LEU A N   1 
ATOM   6957 C CA  . LEU A 1 1328 ? 177.094 136.153 159.247 1.00 49.45  ? 1328 LEU A CA  1 
ATOM   6958 C C   . LEU A 1 1328 ? 178.555 135.821 159.512 1.00 53.77  ? 1328 LEU A C   1 
ATOM   6959 O O   . LEU A 1 1328 ? 178.870 135.136 160.489 1.00 62.59  ? 1328 LEU A O   1 
ATOM   6960 C CB  . LEU A 1 1328 ? 176.509 135.220 158.191 1.00 53.42  ? 1328 LEU A CB  1 
ATOM   6961 C CG  . LEU A 1 1328 ? 174.983 135.156 158.163 1.00 54.42  ? 1328 LEU A CG  1 
ATOM   6962 C CD1 . LEU A 1 1328 ? 174.506 134.138 157.144 1.00 54.33  ? 1328 LEU A CD1 1 
ATOM   6963 C CD2 . LEU A 1 1328 ? 174.446 134.828 159.542 1.00 52.92  ? 1328 LEU A CD2 1 
ATOM   6964 N N   . VAL A 1 1329 ? 179.464 136.307 158.665 1.00 51.09  ? 1329 VAL A N   1 
ATOM   6965 C CA  . VAL A 1 1329 ? 180.886 136.073 158.908 1.00 53.34  ? 1329 VAL A CA  1 
ATOM   6966 C C   . VAL A 1 1329 ? 181.309 136.700 160.233 1.00 55.47  ? 1329 VAL A C   1 
ATOM   6967 O O   . VAL A 1 1329 ? 181.984 136.067 161.059 1.00 57.02  ? 1329 VAL A O   1 
ATOM   6968 C CB  . VAL A 1 1329 ? 181.728 136.610 157.738 1.00 57.67  ? 1329 VAL A CB  1 
ATOM   6969 C CG1 . VAL A 1 1329 ? 183.198 136.630 158.111 1.00 51.21  ? 1329 VAL A CG1 1 
ATOM   6970 C CG2 . VAL A 1 1329 ? 181.508 135.760 156.500 1.00 60.38  ? 1329 VAL A CG2 1 
ATOM   6971 N N   . VAL A 1 1330 ? 180.901 137.950 160.462 1.00 56.21  ? 1330 VAL A N   1 
ATOM   6972 C CA  . VAL A 1 1330 ? 181.306 138.655 161.676 1.00 53.44  ? 1330 VAL A CA  1 
ATOM   6973 C C   . VAL A 1 1330 ? 180.786 137.933 162.911 1.00 58.44  ? 1330 VAL A C   1 
ATOM   6974 O O   . VAL A 1 1330 ? 181.519 137.727 163.885 1.00 67.09  ? 1330 VAL A O   1 
ATOM   6975 C CB  . VAL A 1 1330 ? 180.827 140.116 161.633 1.00 52.49  ? 1330 VAL A CB  1 
ATOM   6976 C CG1 . VAL A 1 1330 ? 181.013 140.772 162.988 1.00 53.77  ? 1330 VAL A CG1 1 
ATOM   6977 C CG2 . VAL A 1 1330 ? 181.581 140.884 160.569 1.00 54.73  ? 1330 VAL A CG2 1 
ATOM   6978 N N   . THR A 1 1331 ? 179.516 137.526 162.889 1.00 58.23  ? 1331 THR A N   1 
ATOM   6979 C CA  . THR A 1 1331 ? 178.939 136.887 164.066 1.00 55.52  ? 1331 THR A CA  1 
ATOM   6980 C C   . THR A 1 1331 ? 179.511 135.490 164.271 1.00 59.85  ? 1331 THR A C   1 
ATOM   6981 O O   . THR A 1 1331 ? 179.687 135.050 165.412 1.00 63.68  ? 1331 THR A O   1 
ATOM   6982 C CB  . THR A 1 1331 ? 177.411 136.849 163.967 1.00 57.84  ? 1331 THR A CB  1 
ATOM   6983 O OG1 . THR A 1 1331 ? 176.863 136.432 165.222 1.00 64.36  ? 1331 THR A OG1 1 
ATOM   6984 C CG2 . THR A 1 1331 ? 176.945 135.891 162.888 1.00 59.73  ? 1331 THR A CG2 1 
ATOM   6985 N N   . ALA A 1 1332 ? 179.829 134.781 163.185 1.00 57.98  ? 1332 ALA A N   1 
ATOM   6986 C CA  . ALA A 1 1332 ? 180.473 133.485 163.325 1.00 59.43  ? 1332 ALA A CA  1 
ATOM   6987 C C   . ALA A 1 1332 ? 181.870 133.618 163.900 1.00 67.41  ? 1332 ALA A C   1 
ATOM   6988 O O   . ALA A 1 1332 ? 182.354 132.687 164.551 1.00 71.26  ? 1332 ALA A O   1 
ATOM   6989 C CB  . ALA A 1 1332 ? 180.524 132.769 161.975 1.00 62.81  ? 1332 ALA A CB  1 
ATOM   6990 N N   . TYR A 1 1333 ? 182.526 134.754 163.679 1.00 67.99  ? 1333 TYR A N   1 
ATOM   6991 C CA  . TYR A 1 1333 ? 183.819 134.986 164.306 1.00 69.63  ? 1333 TYR A CA  1 
ATOM   6992 C C   . TYR A 1 1333 ? 183.732 135.152 165.819 1.00 76.73  ? 1333 TYR A C   1 
ATOM   6993 O O   . TYR A 1 1333 ? 184.755 135.028 166.499 1.00 81.05  ? 1333 TYR A O   1 
ATOM   6994 C CB  . TYR A 1 1333 ? 184.492 136.221 163.700 1.00 70.28  ? 1333 TYR A CB  1 
ATOM   6995 C CG  . TYR A 1 1333 ? 185.813 136.568 164.348 1.00 75.04  ? 1333 TYR A CG  1 
ATOM   6996 C CD1 . TYR A 1 1333 ? 186.946 135.810 164.100 1.00 75.98  ? 1333 TYR A CD1 1 
ATOM   6997 C CD2 . TYR A 1 1333 ? 185.922 137.643 165.218 1.00 72.71  ? 1333 TYR A CD2 1 
ATOM   6998 C CE1 . TYR A 1 1333 ? 188.153 136.116 164.693 1.00 75.24  ? 1333 TYR A CE1 1 
ATOM   6999 C CE2 . TYR A 1 1333 ? 187.125 137.957 165.816 1.00 74.30  ? 1333 TYR A CE2 1 
ATOM   7000 C CZ  . TYR A 1 1333 ? 188.236 137.191 165.550 1.00 76.30  ? 1333 TYR A CZ  1 
ATOM   7001 O OH  . TYR A 1 1333 ? 189.437 137.501 166.143 1.00 79.70  ? 1333 TYR A OH  1 
ATOM   7002 N N   . ILE A 1 1334 ? 182.549 135.419 166.371 1.00 66.41  ? 1334 ILE A N   1 
ATOM   7003 C CA  . ILE A 1 1334 ? 182.455 135.713 167.798 1.00 60.46  ? 1334 ILE A CA  1 
ATOM   7004 C C   . ILE A 1 1334 ? 181.539 134.728 168.512 1.00 65.98  ? 1334 ILE A C   1 
ATOM   7005 O O   . ILE A 1 1334 ? 181.634 134.557 169.732 1.00 66.60  ? 1334 ILE A O   1 
ATOM   7006 C CB  . ILE A 1 1334 ? 181.986 137.159 168.034 1.00 58.03  ? 1334 ILE A CB  1 
ATOM   7007 C CG1 . ILE A 1 1334 ? 180.574 137.367 167.490 1.00 65.40  ? 1334 ILE A CG1 1 
ATOM   7008 C CG2 . ILE A 1 1334 ? 182.949 138.138 167.395 1.00 59.34  ? 1334 ILE A CG2 1 
ATOM   7009 C CD1 . ILE A 1 1334 ? 179.534 137.582 168.566 1.00 66.77  ? 1334 ILE A CD1 1 
ATOM   7010 N N   . ILE A 1 1335 ? 180.645 134.078 167.775 1.00 63.16  ? 1335 ILE A N   1 
ATOM   7011 C CA  . ILE A 1 1335 ? 179.699 133.148 168.384 1.00 64.05  ? 1335 ILE A CA  1 
ATOM   7012 C C   . ILE A 1 1335 ? 180.398 131.820 168.640 1.00 65.20  ? 1335 ILE A C   1 
ATOM   7013 O O   . ILE A 1 1335 ? 181.029 131.255 167.741 1.00 65.68  ? 1335 ILE A O   1 
ATOM   7014 C CB  . ILE A 1 1335 ? 178.456 132.959 167.504 1.00 64.27  ? 1335 ILE A CB  1 
ATOM   7015 C CG1 . ILE A 1 1335 ? 177.522 134.160 167.644 1.00 62.74  ? 1335 ILE A CG1 1 
ATOM   7016 C CG2 . ILE A 1 1335 ? 177.728 131.682 167.878 1.00 63.65  ? 1335 ILE A CG2 1 
ATOM   7017 C CD1 . ILE A 1 1335 ? 177.001 134.359 169.044 1.00 61.65  ? 1335 ILE A CD1 1 
ATOM   7018 N N   . LYS A 1 1336 ? 180.289 131.324 169.869 1.00 78.79  ? 1336 LYS A N   1 
ATOM   7019 C CA  . LYS A 1 1336 ? 180.864 130.033 170.216 1.00 77.90  ? 1336 LYS A CA  1 
ATOM   7020 C C   . LYS A 1 1336 ? 180.105 128.913 169.517 1.00 76.87  ? 1336 LYS A C   1 
ATOM   7021 O O   . LYS A 1 1336 ? 178.873 128.861 169.561 1.00 76.40  ? 1336 LYS A O   1 
ATOM   7022 C CB  . LYS A 1 1336 ? 180.828 129.835 171.730 1.00 77.37  ? 1336 LYS A CB  1 
ATOM   7023 C CG  . LYS A 1 1336 ? 181.184 128.434 172.189 1.00 79.15  ? 1336 LYS A CG  1 
ATOM   7024 C CD  . LYS A 1 1336 ? 180.969 128.282 173.685 1.00 78.84  ? 1336 LYS A CD  1 
ATOM   7025 C CE  . LYS A 1 1336 ? 181.215 126.855 174.140 1.00 81.22  ? 1336 LYS A CE  1 
ATOM   7026 N NZ  . LYS A 1 1336 ? 180.948 126.688 175.595 1.00 81.36  ? 1336 LYS A NZ  1 
ATOM   7027 N N   . GLY A 1 1337 ? 180.843 128.016 168.872 1.00 75.09  ? 1337 GLY A N   1 
ATOM   7028 C CA  . GLY A 1 1337 ? 180.255 126.892 168.179 1.00 76.37  ? 1337 GLY A CA  1 
ATOM   7029 C C   . GLY A 1 1337 ? 179.810 127.236 166.769 1.00 77.77  ? 1337 GLY A C   1 
ATOM   7030 O O   . GLY A 1 1337 ? 179.760 128.395 166.353 1.00 79.15  ? 1337 GLY A O   1 
ATOM   7031 N N   . PHE A 1 1338 ? 179.483 126.187 166.017 1.00 75.13  ? 1338 PHE A N   1 
ATOM   7032 C CA  . PHE A 1 1338 ? 179.009 126.331 164.647 1.00 74.94  ? 1338 PHE A CA  1 
ATOM   7033 C C   . PHE A 1 1338 ? 177.510 126.127 164.506 1.00 75.86  ? 1338 PHE A C   1 
ATOM   7034 O O   . PHE A 1 1338 ? 176.879 126.802 163.688 1.00 75.46  ? 1338 PHE A O   1 
ATOM   7035 C CB  . PHE A 1 1338 ? 179.739 125.344 163.729 1.00 78.72  ? 1338 PHE A CB  1 
ATOM   7036 C CG  . PHE A 1 1338 ? 179.148 125.245 162.350 1.00 80.85  ? 1338 PHE A CG  1 
ATOM   7037 C CD1 . PHE A 1 1338 ? 179.369 126.240 161.414 1.00 77.64  ? 1338 PHE A CD1 1 
ATOM   7038 C CD2 . PHE A 1 1338 ? 178.380 124.150 161.987 1.00 77.47  ? 1338 PHE A CD2 1 
ATOM   7039 C CE1 . PHE A 1 1338 ? 178.830 126.149 160.146 1.00 74.86  ? 1338 PHE A CE1 1 
ATOM   7040 C CE2 . PHE A 1 1338 ? 177.838 124.055 160.721 1.00 75.42  ? 1338 PHE A CE2 1 
ATOM   7041 C CZ  . PHE A 1 1338 ? 178.064 125.055 159.800 1.00 74.56  ? 1338 PHE A CZ  1 
ATOM   7042 N N   . TYR A 1 1339 ? 176.929 125.210 165.282 1.00 72.88  ? 1339 TYR A N   1 
ATOM   7043 C CA  . TYR A 1 1339 ? 175.490 124.981 165.211 1.00 69.42  ? 1339 TYR A CA  1 
ATOM   7044 C C   . TYR A 1 1339 ? 174.719 126.225 165.629 1.00 74.72  ? 1339 TYR A C   1 
ATOM   7045 O O   . TYR A 1 1339 ? 173.661 126.535 165.064 1.00 78.03  ? 1339 TYR A O   1 
ATOM   7046 C CB  . TYR A 1 1339 ? 175.119 123.786 166.087 1.00 69.36  ? 1339 TYR A CB  1 
ATOM   7047 C CG  . TYR A 1 1339 ? 173.714 123.278 165.884 1.00 72.64  ? 1339 TYR A CG  1 
ATOM   7048 C CD1 . TYR A 1 1339 ? 173.348 122.649 164.705 1.00 75.90  ? 1339 TYR A CD1 1 
ATOM   7049 C CD2 . TYR A 1 1339 ? 172.758 123.413 166.879 1.00 75.24  ? 1339 TYR A CD2 1 
ATOM   7050 C CE1 . TYR A 1 1339 ? 172.064 122.178 164.517 1.00 78.96  ? 1339 TYR A CE1 1 
ATOM   7051 C CE2 . TYR A 1 1339 ? 171.473 122.945 166.701 1.00 75.62  ? 1339 TYR A CE2 1 
ATOM   7052 C CZ  . TYR A 1 1339 ? 171.131 122.329 165.518 1.00 77.61  ? 1339 TYR A CZ  1 
ATOM   7053 O OH  . TYR A 1 1339 ? 169.850 121.862 165.338 1.00 77.98  ? 1339 TYR A OH  1 
ATOM   7054 N N   . SER A 1 1340 ? 175.242 126.955 166.615 1.00 64.36  ? 1340 SER A N   1 
ATOM   7055 C CA  . SER A 1 1340 ? 174.614 128.204 167.026 1.00 61.57  ? 1340 SER A CA  1 
ATOM   7056 C C   . SER A 1 1340 ? 174.581 129.204 165.879 1.00 64.93  ? 1340 SER A C   1 
ATOM   7057 O O   . SER A 1 1340 ? 173.607 129.949 165.724 1.00 73.58  ? 1340 SER A O   1 
ATOM   7058 C CB  . SER A 1 1340 ? 175.354 128.785 168.227 1.00 61.66  ? 1340 SER A CB  1 
ATOM   7059 O OG  . SER A 1 1340 ? 175.319 127.889 169.324 1.00 68.21  ? 1340 SER A OG  1 
ATOM   7060 N N   . CYS A 1 1341 ? 175.636 129.236 165.064 1.00 66.60  ? 1341 CYS A N   1 
ATOM   7061 C CA  . CYS A 1 1341 ? 175.640 130.113 163.898 1.00 69.59  ? 1341 CYS A CA  1 
ATOM   7062 C C   . CYS A 1 1341 ? 174.544 129.724 162.913 1.00 66.87  ? 1341 CYS A C   1 
ATOM   7063 O O   . CYS A 1 1341 ? 173.894 130.593 162.321 1.00 70.91  ? 1341 CYS A O   1 
ATOM   7064 C CB  . CYS A 1 1341 ? 177.008 130.081 163.222 1.00 70.55  ? 1341 CYS A CB  1 
ATOM   7065 S SG  . CYS A 1 1341 ? 177.122 131.094 161.732 1.00 90.58  ? 1341 CYS A SG  1 
ATOM   7066 N N   . VAL A 1 1342 ? 174.327 128.421 162.722 1.00 50.16  ? 1342 VAL A N   1 
ATOM   7067 C CA  . VAL A 1 1342 ? 173.256 127.968 161.838 1.00 52.87  ? 1342 VAL A CA  1 
ATOM   7068 C C   . VAL A 1 1342 ? 171.900 128.398 162.380 1.00 60.56  ? 1342 VAL A C   1 
ATOM   7069 O O   . VAL A 1 1342 ? 171.023 128.840 161.626 1.00 62.10  ? 1342 VAL A O   1 
ATOM   7070 C CB  . VAL A 1 1342 ? 173.333 126.443 161.646 1.00 54.69  ? 1342 VAL A CB  1 
ATOM   7071 C CG1 . VAL A 1 1342 ? 172.165 125.953 160.810 1.00 53.48  ? 1342 VAL A CG1 1 
ATOM   7072 C CG2 . VAL A 1 1342 ? 174.648 126.063 160.995 1.00 61.28  ? 1342 VAL A CG2 1 
ATOM   7073 N N   . ILE A 1 1343 ? 171.701 128.269 163.694 1.00 59.62  ? 1343 ILE A N   1 
ATOM   7074 C CA  . ILE A 1 1343 ? 170.438 128.693 164.295 1.00 47.48  ? 1343 ILE A CA  1 
ATOM   7075 C C   . ILE A 1 1343 ? 170.235 130.189 164.102 1.00 52.77  ? 1343 ILE A C   1 
ATOM   7076 O O   . ILE A 1 1343 ? 169.132 130.647 163.775 1.00 62.35  ? 1343 ILE A O   1 
ATOM   7077 C CB  . ILE A 1 1343 ? 170.396 128.304 165.782 1.00 47.35  ? 1343 ILE A CB  1 
ATOM   7078 C CG1 . ILE A 1 1343 ? 170.495 126.788 165.936 1.00 53.96  ? 1343 ILE A CG1 1 
ATOM   7079 C CG2 . ILE A 1 1343 ? 169.125 128.813 166.429 1.00 53.76  ? 1343 ILE A CG2 1 
ATOM   7080 C CD1 . ILE A 1 1343 ? 170.501 126.329 167.369 1.00 55.06  ? 1343 ILE A CD1 1 
ATOM   7081 N N   . ILE A 1 1344 ? 171.295 130.973 164.302 1.00 53.72  ? 1344 ILE A N   1 
ATOM   7082 C CA  . ILE A 1 1344 ? 171.206 132.418 164.113 1.00 49.50  ? 1344 ILE A CA  1 
ATOM   7083 C C   . ILE A 1 1344 ? 170.837 132.747 162.675 1.00 53.80  ? 1344 ILE A C   1 
ATOM   7084 O O   . ILE A 1 1344 ? 169.991 133.612 162.418 1.00 57.05  ? 1344 ILE A O   1 
ATOM   7085 C CB  . ILE A 1 1344 ? 172.528 133.091 164.520 1.00 44.70  ? 1344 ILE A CB  1 
ATOM   7086 C CG1 . ILE A 1 1344 ? 172.731 133.007 166.029 1.00 50.61  ? 1344 ILE A CG1 1 
ATOM   7087 C CG2 . ILE A 1 1344 ? 172.546 134.530 164.072 1.00 47.47  ? 1344 ILE A CG2 1 
ATOM   7088 C CD1 . ILE A 1 1344 ? 174.005 133.662 166.502 1.00 54.81  ? 1344 ILE A CD1 1 
ATOM   7089 N N   . ALA A 1 1345 ? 171.472 132.074 161.714 1.00 51.60  ? 1345 ALA A N   1 
ATOM   7090 C CA  . ALA A 1 1345 ? 171.173 132.336 160.311 1.00 53.71  ? 1345 ALA A CA  1 
ATOM   7091 C C   . ALA A 1 1345 ? 169.727 131.992 159.981 1.00 53.01  ? 1345 ALA A C   1 
ATOM   7092 O O   . ALA A 1 1345 ? 169.050 132.740 159.266 1.00 56.86  ? 1345 ALA A O   1 
ATOM   7093 C CB  . ALA A 1 1345 ? 172.129 131.552 159.415 1.00 51.16  ? 1345 ALA A CB  1 
ATOM   7094 N N   . LEU A 1 1346 ? 169.236 130.862 160.493 1.00 48.08  ? 1346 LEU A N   1 
ATOM   7095 C CA  . LEU A 1 1346 ? 167.848 130.489 160.244 1.00 49.31  ? 1346 LEU A CA  1 
ATOM   7096 C C   . LEU A 1 1346 ? 166.890 131.518 160.829 1.00 51.20  ? 1346 LEU A C   1 
ATOM   7097 O O   . LEU A 1 1346 ? 165.902 131.896 160.186 1.00 51.35  ? 1346 LEU A O   1 
ATOM   7098 C CB  . LEU A 1 1346 ? 167.562 129.105 160.820 1.00 52.26  ? 1346 LEU A CB  1 
ATOM   7099 C CG  . LEU A 1 1346 ? 166.123 128.614 160.662 1.00 50.97  ? 1346 LEU A CG  1 
ATOM   7100 C CD1 . LEU A 1 1346 ? 165.761 128.501 159.192 1.00 48.86  ? 1346 LEU A CD1 1 
ATOM   7101 C CD2 . LEU A 1 1346 ? 165.927 127.283 161.367 1.00 55.45  ? 1346 LEU A CD2 1 
ATOM   7102 N N   . ILE A 1 1347 ? 167.171 131.989 162.045 1.00 49.48  ? 1347 ILE A N   1 
ATOM   7103 C CA  . ILE A 1 1347 ? 166.309 132.991 162.664 1.00 42.61  ? 1347 ILE A CA  1 
ATOM   7104 C C   . ILE A 1 1347 ? 166.332 134.284 161.862 1.00 48.87  ? 1347 ILE A C   1 
ATOM   7105 O O   . ILE A 1 1347 ? 165.296 134.927 161.667 1.00 60.32  ? 1347 ILE A O   1 
ATOM   7106 C CB  . ILE A 1 1347 ? 166.720 133.224 164.128 1.00 41.75  ? 1347 ILE A CB  1 
ATOM   7107 C CG1 . ILE A 1 1347 ? 166.384 131.995 164.968 1.00 50.38  ? 1347 ILE A CG1 1 
ATOM   7108 C CG2 . ILE A 1 1347 ? 166.016 134.439 164.691 1.00 45.19  ? 1347 ILE A CG2 1 
ATOM   7109 C CD1 . ILE A 1 1347 ? 164.912 131.671 164.998 1.00 49.94  ? 1347 ILE A CD1 1 
ATOM   7110 N N   . ILE A 1 1348 ? 167.510 134.687 161.382 1.00 55.64  ? 1348 ILE A N   1 
ATOM   7111 C CA  . ILE A 1 1348 ? 167.612 135.912 160.594 1.00 54.54  ? 1348 ILE A CA  1 
ATOM   7112 C C   . ILE A 1 1348 ? 166.804 135.791 159.310 1.00 52.73  ? 1348 ILE A C   1 
ATOM   7113 O O   . ILE A 1 1348 ? 166.081 136.719 158.921 1.00 48.46  ? 1348 ILE A O   1 
ATOM   7114 C CB  . ILE A 1 1348 ? 169.089 136.238 160.304 1.00 50.57  ? 1348 ILE A CB  1 
ATOM   7115 C CG1 . ILE A 1 1348 ? 169.792 136.699 161.579 1.00 54.13  ? 1348 ILE A CG1 1 
ATOM   7116 C CG2 . ILE A 1 1348 ? 169.201 137.296 159.225 1.00 48.48  ? 1348 ILE A CG2 1 
ATOM   7117 C CD1 . ILE A 1 1348 ? 169.176 137.927 162.197 1.00 56.30  ? 1348 ILE A CD1 1 
ATOM   7118 N N   . PHE A 1 1349 ? 166.914 134.649 158.629 1.00 63.47  ? 1349 PHE A N   1 
ATOM   7119 C CA  . PHE A 1 1349 ? 166.156 134.454 157.397 1.00 60.98  ? 1349 PHE A CA  1 
ATOM   7120 C C   . PHE A 1 1349 ? 164.655 134.468 157.661 1.00 64.22  ? 1349 PHE A C   1 
ATOM   7121 O O   . PHE A 1 1349 ? 163.891 135.067 156.896 1.00 68.43  ? 1349 PHE A O   1 
ATOM   7122 C CB  . PHE A 1 1349 ? 166.574 133.150 156.722 1.00 64.78  ? 1349 PHE A CB  1 
ATOM   7123 C CG  . PHE A 1 1349 ? 167.760 133.293 155.814 1.00 70.78  ? 1349 PHE A CG  1 
ATOM   7124 C CD1 . PHE A 1 1349 ? 169.022 133.527 156.331 1.00 66.89  ? 1349 PHE A CD1 1 
ATOM   7125 C CD2 . PHE A 1 1349 ? 167.614 133.190 154.442 1.00 75.02  ? 1349 PHE A CD2 1 
ATOM   7126 C CE1 . PHE A 1 1349 ? 170.116 133.659 155.498 1.00 68.42  ? 1349 PHE A CE1 1 
ATOM   7127 C CE2 . PHE A 1 1349 ? 168.704 133.320 153.603 1.00 73.51  ? 1349 PHE A CE2 1 
ATOM   7128 C CZ  . PHE A 1 1349 ? 169.957 133.555 154.133 1.00 70.87  ? 1349 PHE A CZ  1 
ATOM   7129 N N   . LEU A 1 1350 ? 164.213 133.820 158.742 1.00 58.72  ? 1350 LEU A N   1 
ATOM   7130 C CA  . LEU A 1 1350 ? 162.790 133.832 159.069 1.00 52.33  ? 1350 LEU A CA  1 
ATOM   7131 C C   . LEU A 1 1350 ? 162.308 135.239 159.398 1.00 54.10  ? 1350 LEU A C   1 
ATOM   7132 O O   . LEU A 1 1350 ? 161.207 135.635 158.998 1.00 57.78  ? 1350 LEU A O   1 
ATOM   7133 C CB  . LEU A 1 1350 ? 162.509 132.884 160.232 1.00 51.82  ? 1350 LEU A CB  1 
ATOM   7134 C CG  . LEU A 1 1350 ? 162.653 131.400 159.905 1.00 60.19  ? 1350 LEU A CG  1 
ATOM   7135 C CD1 . LEU A 1 1350 ? 162.305 130.551 161.113 1.00 56.86  ? 1350 LEU A CD1 1 
ATOM   7136 C CD2 . LEU A 1 1350 ? 161.778 131.035 158.721 1.00 55.72  ? 1350 LEU A CD2 1 
ATOM   7137 N N   . ILE A 1 1351 ? 163.118 136.007 160.128 1.00 52.21  ? 1351 ILE A N   1 
ATOM   7138 C CA  . ILE A 1 1351 ? 162.746 137.378 160.463 1.00 43.42  ? 1351 ILE A CA  1 
ATOM   7139 C C   . ILE A 1 1351 ? 162.615 138.217 159.201 1.00 53.79  ? 1351 ILE A C   1 
ATOM   7140 O O   . ILE A 1 1351 ? 161.660 138.985 159.049 1.00 58.88  ? 1351 ILE A O   1 
ATOM   7141 C CB  . ILE A 1 1351 ? 163.768 137.986 161.440 1.00 44.13  ? 1351 ILE A CB  1 
ATOM   7142 C CG1 . ILE A 1 1351 ? 163.651 137.333 162.814 1.00 50.23  ? 1351 ILE A CG1 1 
ATOM   7143 C CG2 . ILE A 1 1351 ? 163.567 139.479 161.562 1.00 48.69  ? 1351 ILE A CG2 1 
ATOM   7144 C CD1 . ILE A 1 1351 ? 164.658 137.846 163.811 1.00 52.93  ? 1351 ILE A CD1 1 
ATOM   7145 N N   . ASP A 1 1352 ? 163.572 138.090 158.279 1.00 61.55  ? 1352 ASP A N   1 
ATOM   7146 C CA  . ASP A 1 1352 ? 163.489 138.845 157.031 1.00 57.67  ? 1352 ASP A CA  1 
ATOM   7147 C C   . ASP A 1 1352 ? 162.267 138.440 156.220 1.00 55.68  ? 1352 ASP A C   1 
ATOM   7148 O O   . ASP A 1 1352 ? 161.584 139.295 155.641 1.00 57.81  ? 1352 ASP A O   1 
ATOM   7149 C CB  . ASP A 1 1352 ? 164.760 138.650 156.209 1.00 54.12  ? 1352 ASP A CB  1 
ATOM   7150 C CG  . ASP A 1 1352 ? 165.894 139.529 156.677 1.00 61.49  ? 1352 ASP A CG  1 
ATOM   7151 O OD1 . ASP A 1 1352 ? 165.686 140.315 157.623 1.00 68.60  ? 1352 ASP A OD1 1 
ATOM   7152 O OD2 . ASP A 1 1352 ? 166.993 139.436 156.095 1.00 62.73  ? 1352 ASP A OD2 1 
ATOM   7153 N N   . LEU A 1 1353 ? 161.979 137.139 156.162 1.00 54.13  ? 1353 LEU A N   1 
ATOM   7154 C CA  . LEU A 1 1353 ? 160.803 136.681 155.433 1.00 55.76  ? 1353 LEU A CA  1 
ATOM   7155 C C   . LEU A 1 1353 ? 159.532 137.268 156.026 1.00 62.27  ? 1353 LEU A C   1 
ATOM   7156 O O   . LEU A 1 1353 ? 158.663 137.752 155.292 1.00 66.13  ? 1353 LEU A O   1 
ATOM   7157 C CB  . LEU A 1 1353 ? 160.740 135.156 155.442 1.00 54.41  ? 1353 LEU A CB  1 
ATOM   7158 C CG  . LEU A 1 1353 ? 159.426 134.549 154.955 1.00 54.78  ? 1353 LEU A CG  1 
ATOM   7159 C CD1 . LEU A 1 1353 ? 159.183 134.904 153.501 1.00 56.35  ? 1353 LEU A CD1 1 
ATOM   7160 C CD2 . LEU A 1 1353 ? 159.429 133.046 155.149 1.00 58.15  ? 1353 LEU A CD2 1 
ATOM   7161 N N   . CYS A 1 1354 ? 159.411 137.248 157.354 1.00 59.57  ? 1354 CYS A N   1 
ATOM   7162 C CA  . CYS A 1 1354 ? 158.224 137.805 157.993 1.00 51.49  ? 1354 CYS A CA  1 
ATOM   7163 C C   . CYS A 1 1354 ? 158.124 139.307 157.764 1.00 56.14  ? 1354 CYS A C   1 
ATOM   7164 O O   . CYS A 1 1354 ? 157.033 139.830 157.512 1.00 64.42  ? 1354 CYS A O   1 
ATOM   7165 C CB  . CYS A 1 1354 ? 158.231 137.487 159.486 1.00 46.44  ? 1354 CYS A CB  1 
ATOM   7166 S SG  . CYS A 1 1354 ? 157.863 135.765 159.869 1.00 68.44  ? 1354 CYS A SG  1 
ATOM   7167 N N   . ILE A 1 1355 ? 159.250 140.017 157.845 1.00 51.22  ? 1355 ILE A N   1 
ATOM   7168 C CA  . ILE A 1 1355 ? 159.233 141.462 157.640 1.00 43.80  ? 1355 ILE A CA  1 
ATOM   7169 C C   . ILE A 1 1355 ? 158.746 141.791 156.238 1.00 47.04  ? 1355 ILE A C   1 
ATOM   7170 O O   . ILE A 1 1355 ? 157.867 142.640 156.052 1.00 57.31  ? 1355 ILE A O   1 
ATOM   7171 C CB  . ILE A 1 1355 ? 160.625 142.061 157.900 1.00 46.83  ? 1355 ILE A CB  1 
ATOM   7172 C CG1 . ILE A 1 1355 ? 160.967 142.002 159.385 1.00 46.82  ? 1355 ILE A CG1 1 
ATOM   7173 C CG2 . ILE A 1 1355 ? 160.684 143.492 157.405 1.00 49.13  ? 1355 ILE A CG2 1 
ATOM   7174 C CD1 . ILE A 1 1355 ? 162.404 142.338 159.677 1.00 44.16  ? 1355 ILE A CD1 1 
ATOM   7175 N N   . PHE A 1 1356 ? 159.306 141.121 155.229 1.00 56.83  ? 1356 PHE A N   1 
ATOM   7176 C CA  . PHE A 1 1356 ? 158.890 141.395 153.858 1.00 55.80  ? 1356 PHE A CA  1 
ATOM   7177 C C   . PHE A 1 1356 ? 157.433 141.013 153.638 1.00 57.86  ? 1356 PHE A C   1 
ATOM   7178 O O   . PHE A 1 1356 ? 156.673 141.765 153.012 1.00 65.72  ? 1356 PHE A O   1 
ATOM   7179 C CB  . PHE A 1 1356 ? 159.792 140.658 152.872 1.00 53.27  ? 1356 PHE A CB  1 
ATOM   7180 C CG  . PHE A 1 1356 ? 159.465 140.939 151.437 1.00 56.79  ? 1356 PHE A CG  1 
ATOM   7181 C CD1 . PHE A 1 1356 ? 159.924 142.089 150.823 1.00 60.49  ? 1356 PHE A CD1 1 
ATOM   7182 C CD2 . PHE A 1 1356 ? 158.698 140.056 150.701 1.00 60.32  ? 1356 PHE A CD2 1 
ATOM   7183 C CE1 . PHE A 1 1356 ? 159.624 142.352 149.503 1.00 60.15  ? 1356 PHE A CE1 1 
ATOM   7184 C CE2 . PHE A 1 1356 ? 158.394 140.313 149.381 1.00 62.49  ? 1356 PHE A CE2 1 
ATOM   7185 C CZ  . PHE A 1 1356 ? 158.859 141.463 148.782 1.00 62.09  ? 1356 PHE A CZ  1 
ATOM   7186 N N   . GLY A 1 1357 ? 157.021 139.855 154.154 1.00 52.57  ? 1357 GLY A N   1 
ATOM   7187 C CA  . GLY A 1 1357 ? 155.649 139.425 153.969 1.00 51.46  ? 1357 GLY A CA  1 
ATOM   7188 C C   . GLY A 1 1357 ? 154.650 140.384 154.579 1.00 57.42  ? 1357 GLY A C   1 
ATOM   7189 O O   . GLY A 1 1357 ? 153.627 140.698 153.971 1.00 69.12  ? 1357 GLY A O   1 
ATOM   7190 N N   . PHE A 1 1358 ? 154.936 140.876 155.783 1.00 49.96  ? 1358 PHE A N   1 
ATOM   7191 C CA  . PHE A 1 1358 ? 154.001 141.786 156.428 1.00 49.63  ? 1358 PHE A CA  1 
ATOM   7192 C C   . PHE A 1 1358 ? 154.067 143.191 155.849 1.00 52.60  ? 1358 PHE A C   1 
ATOM   7193 O O   . PHE A 1 1358 ? 153.050 143.891 155.842 1.00 58.89  ? 1358 PHE A O   1 
ATOM   7194 C CB  . PHE A 1 1358 ? 154.240 141.810 157.934 1.00 50.49  ? 1358 PHE A CB  1 
ATOM   7195 C CG  . PHE A 1 1358 ? 153.405 140.819 158.682 1.00 46.61  ? 1358 PHE A CG  1 
ATOM   7196 C CD1 . PHE A 1 1358 ? 153.686 139.469 158.616 1.00 52.28  ? 1358 PHE A CD1 1 
ATOM   7197 C CD2 . PHE A 1 1358 ? 152.326 141.236 159.437 1.00 54.53  ? 1358 PHE A CD2 1 
ATOM   7198 C CE1 . PHE A 1 1358 ? 152.916 138.555 159.297 1.00 55.89  ? 1358 PHE A CE1 1 
ATOM   7199 C CE2 . PHE A 1 1358 ? 151.551 140.324 160.120 1.00 59.65  ? 1358 PHE A CE2 1 
ATOM   7200 C CZ  . PHE A 1 1358 ? 151.848 138.983 160.049 1.00 56.60  ? 1358 PHE A CZ  1 
ATOM   7201 N N   . MET A 1 1359 ? 155.228 143.630 155.357 1.00 60.55  ? 1359 MET A N   1 
ATOM   7202 C CA  . MET A 1 1359 ? 155.266 144.926 154.691 1.00 57.16  ? 1359 MET A CA  1 
ATOM   7203 C C   . MET A 1 1359 ? 154.477 144.883 153.391 1.00 62.80  ? 1359 MET A C   1 
ATOM   7204 O O   . MET A 1 1359 ? 153.841 145.873 153.013 1.00 67.74  ? 1359 MET A O   1 
ATOM   7205 C CB  . MET A 1 1359 ? 156.711 145.372 154.447 1.00 54.95  ? 1359 MET A CB  1 
ATOM   7206 C CG  . MET A 1 1359 ? 157.346 144.849 153.171 1.00 59.87  ? 1359 MET A CG  1 
ATOM   7207 S SD  . MET A 1 1359 ? 158.738 145.850 152.624 1.00 68.67  ? 1359 MET A SD  1 
ATOM   7208 C CE  . MET A 1 1359 ? 159.826 145.707 154.035 1.00 60.87  ? 1359 MET A CE  1 
ATOM   7209 N N   . CYS A 1 1360 ? 154.495 143.743 152.696 1.00 67.83  ? 1360 CYS A N   1 
ATOM   7210 C CA  . CYS A 1 1360 ? 153.641 143.602 151.523 1.00 61.61  ? 1360 CYS A CA  1 
ATOM   7211 C C   . CYS A 1 1360 ? 152.178 143.471 151.924 1.00 69.80  ? 1360 CYS A C   1 
ATOM   7212 O O   . CYS A 1 1360 ? 151.287 143.958 151.220 1.00 78.92  ? 1360 CYS A O   1 
ATOM   7213 C CB  . CYS A 1 1360 ? 154.084 142.402 150.692 1.00 63.07  ? 1360 CYS A CB  1 
ATOM   7214 S SG  . CYS A 1 1360 ? 155.706 142.590 149.927 1.00 87.97  ? 1360 CYS A SG  1 
ATOM   7215 N N   . LEU A 1 1361 ? 151.914 142.818 153.056 1.00 65.23  ? 1361 LEU A N   1 
ATOM   7216 C CA  . LEU A 1 1361 ? 150.540 142.612 153.499 1.00 68.44  ? 1361 LEU A CA  1 
ATOM   7217 C C   . LEU A 1 1361 ? 149.914 143.910 153.995 1.00 66.28  ? 1361 LEU A C   1 
ATOM   7218 O O   . LEU A 1 1361 ? 148.715 144.138 153.805 1.00 70.61  ? 1361 LEU A O   1 
ATOM   7219 C CB  . LEU A 1 1361 ? 150.506 141.543 154.589 1.00 67.87  ? 1361 LEU A CB  1 
ATOM   7220 C CG  . LEU A 1 1361 ? 149.137 141.122 155.117 1.00 71.00  ? 1361 LEU A CG  1 
ATOM   7221 C CD1 . LEU A 1 1361 ? 148.268 140.608 153.986 1.00 72.17  ? 1361 LEU A CD1 1 
ATOM   7222 C CD2 . LEU A 1 1361 ? 149.294 140.064 156.193 1.00 68.15  ? 1361 LEU A CD2 1 
ATOM   7223 N N   . CYS A 1 1362 ? 150.704 144.768 154.633 1.00 57.95  ? 1362 CYS A N   1 
ATOM   7224 C CA  . CYS A 1 1362 ? 150.197 146.024 155.169 1.00 61.06  ? 1362 CYS A CA  1 
ATOM   7225 C C   . CYS A 1 1362 ? 150.091 147.119 154.119 1.00 60.92  ? 1362 CYS A C   1 
ATOM   7226 O O   . CYS A 1 1362 ? 149.801 148.266 154.471 1.00 66.79  ? 1362 CYS A O   1 
ATOM   7227 C CB  . CYS A 1 1362 ? 151.080 146.500 156.325 1.00 61.69  ? 1362 CYS A CB  1 
ATOM   7228 S SG  . CYS A 1 1362 ? 151.010 145.456 157.794 1.00 73.49  ? 1362 CYS A SG  1 
ATOM   7229 N N   . GLY A 1 1363 ? 150.321 146.802 152.850 1.00 55.98  ? 1363 GLY A N   1 
ATOM   7230 C CA  . GLY A 1 1363 ? 150.200 147.776 151.790 1.00 59.45  ? 1363 GLY A CA  1 
ATOM   7231 C C   . GLY A 1 1363 ? 151.455 148.562 151.479 1.00 66.02  ? 1363 GLY A C   1 
ATOM   7232 O O   . GLY A 1 1363 ? 151.437 149.376 150.547 1.00 70.28  ? 1363 GLY A O   1 
ATOM   7233 N N   . ILE A 1 1364 ? 152.540 148.354 152.222 1.00 61.00  ? 1364 ILE A N   1 
ATOM   7234 C CA  . ILE A 1 1364 ? 153.787 149.043 151.921 1.00 55.44  ? 1364 ILE A CA  1 
ATOM   7235 C C   . ILE A 1 1364 ? 154.398 148.443 150.665 1.00 60.53  ? 1364 ILE A C   1 
ATOM   7236 O O   . ILE A 1 1364 ? 154.533 147.219 150.544 1.00 66.86  ? 1364 ILE A O   1 
ATOM   7237 C CB  . ILE A 1 1364 ? 154.754 148.953 153.109 1.00 58.44  ? 1364 ILE A CB  1 
ATOM   7238 C CG1 . ILE A 1 1364 ? 154.080 149.461 154.381 1.00 56.86  ? 1364 ILE A CG1 1 
ATOM   7239 C CG2 . ILE A 1 1364 ? 156.012 149.749 152.827 1.00 52.30  ? 1364 ILE A CG2 1 
ATOM   7240 C CD1 . ILE A 1 1364 ? 154.947 149.349 155.607 1.00 54.02  ? 1364 ILE A CD1 1 
ATOM   7241 N N   . THR A 1 1365 ? 154.765 149.301 149.719 1.00 67.99  ? 1365 THR A N   1 
ATOM   7242 C CA  . THR A 1 1365 ? 155.315 148.853 148.453 1.00 66.58  ? 1365 THR A CA  1 
ATOM   7243 C C   . THR A 1 1365 ? 156.832 148.719 148.550 1.00 68.31  ? 1365 THR A C   1 
ATOM   7244 O O   . THR A 1 1365 ? 157.468 149.207 149.486 1.00 72.88  ? 1365 THR A O   1 
ATOM   7245 C CB  . THR A 1 1365 ? 154.921 149.814 147.335 1.00 66.32  ? 1365 THR A CB  1 
ATOM   7246 O OG1 . THR A 1 1365 ? 155.392 151.129 147.650 1.00 71.42  ? 1365 THR A OG1 1 
ATOM   7247 C CG2 . THR A 1 1365 ? 153.412 149.853 147.178 1.00 71.30  ? 1365 THR A CG2 1 
ATOM   7248 N N   . MET A 1 1366 ? 157.424 148.050 147.563 1.00 79.55  ? 1366 MET A N   1 
ATOM   7249 C CA  . MET A 1 1366 ? 158.873 147.870 147.506 1.00 77.60  ? 1366 MET A CA  1 
ATOM   7250 C C   . MET A 1 1366 ? 159.482 149.140 146.930 1.00 79.21  ? 1366 MET A C   1 
ATOM   7251 O O   . MET A 1 1366 ? 159.747 149.243 145.733 1.00 83.79  ? 1366 MET A O   1 
ATOM   7252 C CB  . MET A 1 1366 ? 159.238 146.650 146.674 1.00 75.12  ? 1366 MET A CB  1 
ATOM   7253 C CG  . MET A 1 1366 ? 158.717 145.342 147.226 1.00 81.13  ? 1366 MET A CG  1 
ATOM   7254 S SD  . MET A 1 1366 ? 159.300 143.936 146.265 1.00 100.70 ? 1366 MET A SD  1 
ATOM   7255 C CE  . MET A 1 1366 ? 161.069 144.101 146.475 1.00 84.48  ? 1366 MET A CE  1 
ATOM   7256 N N   . ASN A 1 1367 ? 159.712 150.120 147.799 1.00 56.63  ? 1367 ASN A N   1 
ATOM   7257 C CA  . ASN A 1 1367 ? 160.294 151.386 147.379 1.00 59.08  ? 1367 ASN A CA  1 
ATOM   7258 C C   . ASN A 1 1367 ? 161.638 151.600 148.059 1.00 64.34  ? 1367 ASN A C   1 
ATOM   7259 O O   . ASN A 1 1367 ? 162.140 150.701 148.737 1.00 68.61  ? 1367 ASN A O   1 
ATOM   7260 C CB  . ASN A 1 1367 ? 159.342 152.540 147.685 1.00 55.21  ? 1367 ASN A CB  1 
ATOM   7261 C CG  . ASN A 1 1367 ? 158.784 152.475 149.086 1.00 58.28  ? 1367 ASN A CG  1 
ATOM   7262 O OD1 . ASN A 1 1367 ? 159.353 151.831 149.964 1.00 66.13  ? 1367 ASN A OD1 1 
ATOM   7263 N ND2 . ASN A 1 1367 ? 157.660 153.142 149.304 1.00 64.83  ? 1367 ASN A ND2 1 
ATOM   7264 N N   . ILE A 1 1368 ? 162.223 152.785 147.888 1.00 57.01  ? 1368 ILE A N   1 
ATOM   7265 C CA  . ILE A 1 1368 ? 163.566 153.035 148.406 1.00 52.07  ? 1368 ILE A CA  1 
ATOM   7266 C C   . ILE A 1 1368 ? 163.597 152.881 149.922 1.00 61.37  ? 1368 ILE A C   1 
ATOM   7267 O O   . ILE A 1 1368 ? 164.467 152.199 150.477 1.00 68.78  ? 1368 ILE A O   1 
ATOM   7268 C CB  . ILE A 1 1368 ? 164.052 154.427 147.968 1.00 55.21  ? 1368 ILE A CB  1 
ATOM   7269 C CG1 . ILE A 1 1368 ? 164.624 154.370 146.554 1.00 62.36  ? 1368 ILE A CG1 1 
ATOM   7270 C CG2 . ILE A 1 1368 ? 165.084 154.959 148.931 1.00 62.53  ? 1368 ILE A CG2 1 
ATOM   7271 C CD1 . ILE A 1 1368 ? 165.276 155.658 146.117 1.00 57.93  ? 1368 ILE A CD1 1 
ATOM   7272 N N   . ILE A 1 1369 ? 162.638 153.499 150.614 1.00 61.02  ? 1369 ILE A N   1 
ATOM   7273 C CA  . ILE A 1 1369 ? 162.663 153.506 152.074 1.00 58.64  ? 1369 ILE A CA  1 
ATOM   7274 C C   . ILE A 1 1369 ? 162.504 152.092 152.616 1.00 57.78  ? 1369 ILE A C   1 
ATOM   7275 O O   . ILE A 1 1369 ? 163.289 151.635 153.458 1.00 67.09  ? 1369 ILE A O   1 
ATOM   7276 C CB  . ILE A 1 1369 ? 161.572 154.439 152.625 1.00 56.53  ? 1369 ILE A CB  1 
ATOM   7277 C CG1 . ILE A 1 1369 ? 161.498 155.728 151.808 1.00 56.53  ? 1369 ILE A CG1 1 
ATOM   7278 C CG2 . ILE A 1 1369 ? 161.838 154.756 154.079 1.00 59.04  ? 1369 ILE A CG2 1 
ATOM   7279 C CD1 . ILE A 1 1369 ? 160.346 155.768 150.828 1.00 54.88  ? 1369 ILE A CD1 1 
ATOM   7280 N N   . SER A 1 1370 ? 161.486 151.378 152.133 1.00 54.77  ? 1370 SER A N   1 
ATOM   7281 C CA  . SER A 1 1370 ? 161.220 150.035 152.633 1.00 55.40  ? 1370 SER A CA  1 
ATOM   7282 C C   . SER A 1 1370 ? 162.378 149.100 152.329 1.00 55.85  ? 1370 SER A C   1 
ATOM   7283 O O   . SER A 1 1370 ? 162.742 148.263 153.158 1.00 68.44  ? 1370 SER A O   1 
ATOM   7284 C CB  . SER A 1 1370 ? 159.925 149.495 152.033 1.00 54.06  ? 1370 SER A CB  1 
ATOM   7285 O OG  . SER A 1 1370 ? 160.010 149.432 150.622 1.00 61.65  ? 1370 SER A OG  1 
ATOM   7286 N N   . MET A 1 1371 ? 162.973 149.230 151.145 1.00 60.51  ? 1371 MET A N   1 
ATOM   7287 C CA  . MET A 1 1371 ? 164.086 148.361 150.780 1.00 61.30  ? 1371 MET A CA  1 
ATOM   7288 C C   . MET A 1 1371 ? 165.312 148.633 151.643 1.00 64.17  ? 1371 MET A C   1 
ATOM   7289 O O   . MET A 1 1371 ? 165.998 147.701 152.078 1.00 66.62  ? 1371 MET A O   1 
ATOM   7290 C CB  . MET A 1 1371 ? 164.409 148.536 149.300 1.00 62.75  ? 1371 MET A CB  1 
ATOM   7291 C CG  . MET A 1 1371 ? 163.395 147.899 148.356 1.00 71.82  ? 1371 MET A CG  1 
ATOM   7292 S SD  . MET A 1 1371 ? 163.114 146.143 148.654 1.00 85.17  ? 1371 MET A SD  1 
ATOM   7293 C CE  . MET A 1 1371 ? 161.551 146.180 149.527 1.00 69.34  ? 1371 MET A CE  1 
ATOM   7294 N N   . VAL A 1 1372 ? 165.607 149.907 151.904 1.00 59.29  ? 1372 VAL A N   1 
ATOM   7295 C CA  . VAL A 1 1372 ? 166.747 150.230 152.758 1.00 63.66  ? 1372 VAL A CA  1 
ATOM   7296 C C   . VAL A 1 1372 ? 166.529 149.692 154.166 1.00 66.00  ? 1372 VAL A C   1 
ATOM   7297 O O   . VAL A 1 1372 ? 167.444 149.129 154.784 1.00 67.02  ? 1372 VAL A O   1 
ATOM   7298 C CB  . VAL A 1 1372 ? 167.001 151.748 152.761 1.00 57.08  ? 1372 VAL A CB  1 
ATOM   7299 C CG1 . VAL A 1 1372 ? 167.993 152.116 153.846 1.00 58.32  ? 1372 VAL A CG1 1 
ATOM   7300 C CG2 . VAL A 1 1372 ? 167.516 152.189 151.408 1.00 58.35  ? 1372 VAL A CG2 1 
ATOM   7301 N N   . ILE A 1 1373 ? 165.315 149.848 154.696 1.00 54.83  ? 1373 ILE A N   1 
ATOM   7302 C CA  . ILE A 1 1373 ? 165.039 149.334 156.032 1.00 51.26  ? 1373 ILE A CA  1 
ATOM   7303 C C   . ILE A 1 1373 ? 165.095 147.812 156.044 1.00 53.48  ? 1373 ILE A C   1 
ATOM   7304 O O   . ILE A 1 1373 ? 165.522 147.203 157.029 1.00 59.24  ? 1373 ILE A O   1 
ATOM   7305 C CB  . ILE A 1 1373 ? 163.691 149.862 156.541 1.00 48.23  ? 1373 ILE A CB  1 
ATOM   7306 C CG1 . ILE A 1 1373 ? 163.705 151.383 156.539 1.00 49.90  ? 1373 ILE A CG1 1 
ATOM   7307 C CG2 . ILE A 1 1373 ? 163.425 149.365 157.945 1.00 53.56  ? 1373 ILE A CG2 1 
ATOM   7308 C CD1 . ILE A 1 1373 ? 162.342 151.975 156.573 1.00 62.18  ? 1373 ILE A CD1 1 
ATOM   7309 N N   . LEU A 1 1374 ? 164.668 147.171 154.957 1.00 49.48  ? 1374 LEU A N   1 
ATOM   7310 C CA  . LEU A 1 1374 ? 164.786 145.721 154.865 1.00 53.53  ? 1374 LEU A CA  1 
ATOM   7311 C C   . LEU A 1 1374 ? 166.245 145.291 154.886 1.00 56.56  ? 1374 LEU A C   1 
ATOM   7312 O O   . LEU A 1 1374 ? 166.592 144.274 155.496 1.00 65.99  ? 1374 LEU A O   1 
ATOM   7313 C CB  . LEU A 1 1374 ? 164.093 145.221 153.599 1.00 58.01  ? 1374 LEU A CB  1 
ATOM   7314 C CG  . LEU A 1 1374 ? 164.141 143.716 153.342 1.00 57.04  ? 1374 LEU A CG  1 
ATOM   7315 C CD1 . LEU A 1 1374 ? 163.567 142.957 154.520 1.00 56.47  ? 1374 LEU A CD1 1 
ATOM   7316 C CD2 . LEU A 1 1374 ? 163.388 143.377 152.071 1.00 58.99  ? 1374 LEU A CD2 1 
ATOM   7317 N N   . VAL A 1 1375 ? 167.113 146.050 154.218 1.00 58.58  ? 1375 VAL A N   1 
ATOM   7318 C CA  . VAL A 1 1375 ? 168.543 145.758 154.267 1.00 56.91  ? 1375 VAL A CA  1 
ATOM   7319 C C   . VAL A 1 1375 ? 169.068 145.897 155.690 1.00 59.50  ? 1375 VAL A C   1 
ATOM   7320 O O   . VAL A 1 1375 ? 169.802 145.034 156.184 1.00 63.43  ? 1375 VAL A O   1 
ATOM   7321 C CB  . VAL A 1 1375 ? 169.309 146.671 153.293 1.00 54.73  ? 1375 VAL A CB  1 
ATOM   7322 C CG1 . VAL A 1 1375 ? 170.802 146.572 153.539 1.00 58.97  ? 1375 VAL A CG1 1 
ATOM   7323 C CG2 . VAL A 1 1375 ? 168.984 146.303 151.861 1.00 58.93  ? 1375 VAL A CG2 1 
ATOM   7324 N N   . LEU A 1 1376 ? 168.695 146.978 156.375 1.00 59.08  ? 1376 LEU A N   1 
ATOM   7325 C CA  . LEU A 1 1376 ? 169.187 147.221 157.729 1.00 53.50  ? 1376 LEU A CA  1 
ATOM   7326 C C   . LEU A 1 1376 ? 168.546 146.311 158.772 1.00 61.78  ? 1376 LEU A C   1 
ATOM   7327 O O   . LEU A 1 1376 ? 169.035 146.249 159.909 1.00 63.87  ? 1376 LEU A O   1 
ATOM   7328 C CB  . LEU A 1 1376 ? 168.955 148.682 158.105 1.00 57.97  ? 1376 LEU A CB  1 
ATOM   7329 C CG  . LEU A 1 1376 ? 169.557 149.690 157.127 1.00 62.73  ? 1376 LEU A CG  1 
ATOM   7330 C CD1 . LEU A 1 1376 ? 168.984 151.072 157.364 1.00 67.25  ? 1376 LEU A CD1 1 
ATOM   7331 C CD2 . LEU A 1 1376 ? 171.069 149.711 157.246 1.00 63.41  ? 1376 LEU A CD2 1 
ATOM   7332 N N   . SER A 1 1377 ? 167.460 145.625 158.415 1.00 56.50  ? 1377 SER A N   1 
ATOM   7333 C CA  . SER A 1 1377 ? 166.783 144.753 159.366 1.00 55.69  ? 1377 SER A CA  1 
ATOM   7334 C C   . SER A 1 1377 ? 167.695 143.634 159.840 1.00 60.16  ? 1377 SER A C   1 
ATOM   7335 O O   . SER A 1 1377 ? 167.593 143.186 160.986 1.00 68.90  ? 1377 SER A O   1 
ATOM   7336 C CB  . SER A 1 1377 ? 165.519 144.176 158.733 1.00 61.19  ? 1377 SER A CB  1 
ATOM   7337 O OG  . SER A 1 1377 ? 165.841 143.363 157.620 1.00 61.24  ? 1377 SER A OG  1 
ATOM   7338 N N   . VAL A 1 1378 ? 168.584 143.156 158.969 1.00 52.49  ? 1378 VAL A N   1 
ATOM   7339 C CA  . VAL A 1 1378 ? 169.520 142.113 159.372 1.00 55.29  ? 1378 VAL A CA  1 
ATOM   7340 C C   . VAL A 1 1378 ? 170.414 142.616 160.495 1.00 55.39  ? 1378 VAL A C   1 
ATOM   7341 O O   . VAL A 1 1378 ? 170.571 141.960 161.531 1.00 65.82  ? 1378 VAL A O   1 
ATOM   7342 C CB  . VAL A 1 1378 ? 170.348 141.639 158.166 1.00 56.18  ? 1378 VAL A CB  1 
ATOM   7343 C CG1 . VAL A 1 1378 ? 171.221 140.466 158.559 1.00 54.79  ? 1378 VAL A CG1 1 
ATOM   7344 C CG2 . VAL A 1 1378 ? 169.434 141.271 157.019 1.00 62.09  ? 1378 VAL A CG2 1 
ATOM   7345 N N   . GLY A 1 1379 ? 170.999 143.799 160.309 1.00 51.17  ? 1379 GLY A N   1 
ATOM   7346 C CA  . GLY A 1 1379 ? 171.846 144.368 161.339 1.00 49.45  ? 1379 GLY A CA  1 
ATOM   7347 C C   . GLY A 1 1379 ? 171.101 144.667 162.622 1.00 55.16  ? 1379 GLY A C   1 
ATOM   7348 O O   . GLY A 1 1379 ? 171.674 144.588 163.710 1.00 54.80  ? 1379 GLY A O   1 
ATOM   7349 N N   . PHE A 1 1380 ? 169.824 145.034 162.518 1.00 63.81  ? 1380 PHE A N   1 
ATOM   7350 C CA  . PHE A 1 1380 ? 169.065 145.316 163.734 1.00 63.36  ? 1380 PHE A CA  1 
ATOM   7351 C C   . PHE A 1 1380 ? 168.707 144.039 164.489 1.00 61.09  ? 1380 PHE A C   1 
ATOM   7352 O O   . PHE A 1 1380 ? 168.842 143.984 165.716 1.00 61.48  ? 1380 PHE A O   1 
ATOM   7353 C CB  . PHE A 1 1380 ? 167.812 146.121 163.403 1.00 63.41  ? 1380 PHE A CB  1 
ATOM   7354 C CG  . PHE A 1 1380 ? 168.076 147.583 163.216 1.00 70.87  ? 1380 PHE A CG  1 
ATOM   7355 C CD1 . PHE A 1 1380 ? 169.239 148.149 163.705 1.00 67.21  ? 1380 PHE A CD1 1 
ATOM   7356 C CD2 . PHE A 1 1380 ? 167.171 148.389 162.553 1.00 68.09  ? 1380 PHE A CD2 1 
ATOM   7357 C CE1 . PHE A 1 1380 ? 169.495 149.490 163.538 1.00 65.56  ? 1380 PHE A CE1 1 
ATOM   7358 C CE2 . PHE A 1 1380 ? 167.423 149.734 162.383 1.00 69.39  ? 1380 PHE A CE2 1 
ATOM   7359 C CZ  . PHE A 1 1380 ? 168.587 150.283 162.876 1.00 68.92  ? 1380 PHE A CZ  1 
ATOM   7360 N N   . SER A 1 1381 ? 168.254 143.004 163.782 1.00 57.31  ? 1381 SER A N   1 
ATOM   7361 C CA  . SER A 1 1381 ? 167.771 141.797 164.445 1.00 58.06  ? 1381 SER A CA  1 
ATOM   7362 C C   . SER A 1 1381 ? 168.901 140.883 164.897 1.00 58.75  ? 1381 SER A C   1 
ATOM   7363 O O   . SER A 1 1381 ? 168.720 140.099 165.846 1.00 65.00  ? 1381 SER A O   1 
ATOM   7364 C CB  . SER A 1 1381 ? 166.831 141.034 163.514 1.00 59.02  ? 1381 SER A CB  1 
ATOM   7365 O OG  . SER A 1 1381 ? 167.467 140.742 162.285 1.00 58.93  ? 1381 SER A OG  1 
ATOM   7366 N N   . ILE A 1 1382 ? 170.057 140.955 164.231 1.00 44.57  ? 1382 ILE A N   1 
ATOM   7367 C CA  . ILE A 1 1382 ? 171.175 140.099 164.600 1.00 42.80  ? 1382 ILE A CA  1 
ATOM   7368 C C   . ILE A 1 1382 ? 171.612 140.376 166.026 1.00 53.93  ? 1382 ILE A C   1 
ATOM   7369 O O   . ILE A 1 1382 ? 172.095 139.476 166.714 1.00 61.94  ? 1382 ILE A O   1 
ATOM   7370 C CB  . ILE A 1 1382 ? 172.335 140.284 163.605 1.00 50.17  ? 1382 ILE A CB  1 
ATOM   7371 C CG1 . ILE A 1 1382 ? 173.432 139.254 163.853 1.00 58.19  ? 1382 ILE A CG1 1 
ATOM   7372 C CG2 . ILE A 1 1382 ? 172.903 141.672 163.710 1.00 56.30  ? 1382 ILE A CG2 1 
ATOM   7373 C CD1 . ILE A 1 1382 ? 173.154 137.925 163.220 1.00 58.45  ? 1382 ILE A CD1 1 
ATOM   7374 N N   . ASP A 1 1383 ? 171.426 141.606 166.507 1.00 62.59  ? 1383 ASP A N   1 
ATOM   7375 C CA  . ASP A 1 1383 ? 171.838 141.930 167.867 1.00 59.83  ? 1383 ASP A CA  1 
ATOM   7376 C C   . ASP A 1 1383 ? 171.065 141.103 168.886 1.00 57.35  ? 1383 ASP A C   1 
ATOM   7377 O O   . ASP A 1 1383 ? 171.660 140.417 169.725 1.00 65.09  ? 1383 ASP A O   1 
ATOM   7378 C CB  . ASP A 1 1383 ? 171.645 143.423 168.125 1.00 62.81  ? 1383 ASP A CB  1 
ATOM   7379 C CG  . ASP A 1 1383 ? 172.377 144.286 167.118 1.00 73.02  ? 1383 ASP A CG  1 
ATOM   7380 O OD1 . ASP A 1 1383 ? 173.452 143.866 166.643 1.00 71.82  ? 1383 ASP A OD1 1 
ATOM   7381 O OD2 . ASP A 1 1383 ? 171.877 145.385 166.801 1.00 72.25  ? 1383 ASP A OD2 1 
ATOM   7382 N N   . HIS A 1 1384 ? 169.734 141.130 168.806 1.00 48.12  ? 1384 HIS A N   1 
ATOM   7383 C CA  . HIS A 1 1384 ? 168.924 140.368 169.750 1.00 45.55  ? 1384 HIS A CA  1 
ATOM   7384 C C   . HIS A 1 1384 ? 169.131 138.871 169.572 1.00 43.83  ? 1384 HIS A C   1 
ATOM   7385 O O   . HIS A 1 1384 ? 169.257 138.130 170.561 1.00 53.77  ? 1384 HIS A O   1 
ATOM   7386 C CB  . HIS A 1 1384 ? 167.449 140.724 169.580 1.00 50.61  ? 1384 HIS A CB  1 
ATOM   7387 C CG  . HIS A 1 1384 ? 167.183 142.194 169.521 1.00 55.20  ? 1384 HIS A CG  1 
ATOM   7388 N ND1 . HIS A 1 1384 ? 167.207 142.908 168.343 1.00 54.73  ? 1384 HIS A ND1 1 
ATOM   7389 C CD2 . HIS A 1 1384 ? 166.884 143.086 170.494 1.00 55.45  ? 1384 HIS A CD2 1 
ATOM   7390 C CE1 . HIS A 1 1384 ? 166.935 144.175 168.592 1.00 52.26  ? 1384 HIS A CE1 1 
ATOM   7391 N NE2 . HIS A 1 1384 ? 166.736 144.310 169.890 1.00 53.94  ? 1384 HIS A NE2 1 
ATOM   7392 N N   . THR A 1 1385 ? 169.164 138.403 168.321 1.00 47.18  ? 1385 THR A N   1 
ATOM   7393 C CA  . THR A 1 1385 ? 169.333 136.973 168.095 1.00 42.54  ? 1385 THR A CA  1 
ATOM   7394 C C   . THR A 1 1385 ? 170.667 136.484 168.644 1.00 43.77  ? 1385 THR A C   1 
ATOM   7395 O O   . THR A 1 1385 ? 170.730 135.441 169.306 1.00 49.77  ? 1385 THR A O   1 
ATOM   7396 C CB  . THR A 1 1385 ? 169.213 136.659 166.606 1.00 48.73  ? 1385 THR A CB  1 
ATOM   7397 O OG1 . THR A 1 1385 ? 167.946 137.122 166.125 1.00 50.01  ? 1385 THR A OG1 1 
ATOM   7398 C CG2 . THR A 1 1385 ? 169.313 135.167 166.374 1.00 48.26  ? 1385 THR A CG2 1 
ATOM   7399 N N   . SER A 1 1386 ? 171.742 137.235 168.397 1.00 49.15  ? 1386 SER A N   1 
ATOM   7400 C CA  . SER A 1 1386 ? 173.054 136.863 168.903 1.00 50.01  ? 1386 SER A CA  1 
ATOM   7401 C C   . SER A 1 1386 ? 173.100 136.922 170.420 1.00 58.75  ? 1386 SER A C   1 
ATOM   7402 O O   . SER A 1 1386 ? 173.716 136.062 171.052 1.00 66.03  ? 1386 SER A O   1 
ATOM   7403 C CB  . SER A 1 1386 ? 174.121 137.771 168.298 1.00 55.86  ? 1386 SER A CB  1 
ATOM   7404 O OG  . SER A 1 1386 ? 175.394 137.492 168.849 1.00 64.24  ? 1386 SER A OG  1 
ATOM   7405 N N   . HIS A 1 1387 ? 172.464 137.928 171.025 1.00 54.77  ? 1387 HIS A N   1 
ATOM   7406 C CA  . HIS A 1 1387 ? 172.423 137.986 172.482 1.00 45.09  ? 1387 HIS A CA  1 
ATOM   7407 C C   . HIS A 1 1387 ? 171.818 136.715 173.055 1.00 51.16  ? 1387 HIS A C   1 
ATOM   7408 O O   . HIS A 1 1387 ? 172.420 136.054 173.910 1.00 60.73  ? 1387 HIS A O   1 
ATOM   7409 C CB  . HIS A 1 1387 ? 171.628 139.205 172.945 1.00 52.56  ? 1387 HIS A CB  1 
ATOM   7410 C CG  . HIS A 1 1387 ? 172.347 140.502 172.763 1.00 57.70  ? 1387 HIS A CG  1 
ATOM   7411 N ND1 . HIS A 1 1387 ? 171.791 141.714 173.110 1.00 54.09  ? 1387 HIS A ND1 1 
ATOM   7412 C CD2 . HIS A 1 1387 ? 173.577 140.779 172.273 1.00 60.87  ? 1387 HIS A CD2 1 
ATOM   7413 C CE1 . HIS A 1 1387 ? 172.646 142.682 172.839 1.00 58.08  ? 1387 HIS A CE1 1 
ATOM   7414 N NE2 . HIS A 1 1387 ? 173.739 142.142 172.331 1.00 64.73  ? 1387 HIS A NE2 1 
ATOM   7415 N N   . ILE A 1 1388 ? 170.634 136.340 172.568 1.00 46.94  ? 1388 ILE A N   1 
ATOM   7416 C CA  . ILE A 1 1388 ? 169.960 135.167 173.120 1.00 42.08  ? 1388 ILE A CA  1 
ATOM   7417 C C   . ILE A 1 1388 ? 170.766 133.902 172.849 1.00 48.70  ? 1388 ILE A C   1 
ATOM   7418 O O   . ILE A 1 1388 ? 170.936 133.056 173.735 1.00 53.59  ? 1388 ILE A O   1 
ATOM   7419 C CB  . ILE A 1 1388 ? 168.529 135.057 172.568 1.00 54.48  ? 1388 ILE A CB  1 
ATOM   7420 C CG1 . ILE A 1 1388 ? 167.684 136.224 173.070 1.00 53.68  ? 1388 ILE A CG1 1 
ATOM   7421 C CG2 . ILE A 1 1388 ? 167.901 133.747 172.991 1.00 51.44  ? 1388 ILE A CG2 1 
ATOM   7422 C CD1 . ILE A 1 1388 ? 167.515 136.245 174.566 1.00 49.61  ? 1388 ILE A CD1 1 
ATOM   7423 N N   . VAL A 1 1389 ? 171.286 133.755 171.628 1.00 47.09  ? 1389 VAL A N   1 
ATOM   7424 C CA  . VAL A 1 1389 ? 171.990 132.528 171.273 1.00 48.98  ? 1389 VAL A CA  1 
ATOM   7425 C C   . VAL A 1 1389 ? 173.282 132.389 172.068 1.00 51.53  ? 1389 VAL A C   1 
ATOM   7426 O O   . VAL A 1 1389 ? 173.612 131.299 172.549 1.00 54.69  ? 1389 VAL A O   1 
ATOM   7427 C CB  . VAL A 1 1389 ? 172.245 132.482 169.758 1.00 48.81  ? 1389 VAL A CB  1 
ATOM   7428 C CG1 . VAL A 1 1389 ? 173.243 131.401 169.427 1.00 43.66  ? 1389 VAL A CG1 1 
ATOM   7429 C CG2 . VAL A 1 1389 ? 170.945 132.229 169.029 1.00 54.30  ? 1389 VAL A CG2 1 
ATOM   7430 N N   . GLN A 1 1390 ? 174.038 133.477 172.217 1.00 55.67  ? 1390 GLN A N   1 
ATOM   7431 C CA  . GLN A 1 1390 ? 175.276 133.411 172.982 1.00 52.13  ? 1390 GLN A CA  1 
ATOM   7432 C C   . GLN A 1 1390 ? 174.998 133.161 174.456 1.00 58.08  ? 1390 GLN A C   1 
ATOM   7433 O O   . GLN A 1 1390 ? 175.741 132.421 175.113 1.00 64.69  ? 1390 GLN A O   1 
ATOM   7434 C CB  . GLN A 1 1390 ? 176.080 134.695 172.790 1.00 53.80  ? 1390 GLN A CB  1 
ATOM   7435 C CG  . GLN A 1 1390 ? 177.463 134.638 173.398 1.00 59.12  ? 1390 GLN A CG  1 
ATOM   7436 C CD  . GLN A 1 1390 ? 178.514 135.277 172.518 1.00 65.76  ? 1390 GLN A CD  1 
ATOM   7437 O OE1 . GLN A 1 1390 ? 178.201 136.074 171.635 1.00 66.87  ? 1390 GLN A OE1 1 
ATOM   7438 N NE2 . GLN A 1 1390 ? 179.773 134.924 172.748 1.00 66.88  ? 1390 GLN A NE2 1 
ATOM   7439 N N   . ALA A 1 1391 ? 173.935 133.763 174.997 1.00 56.27  ? 1391 ALA A N   1 
ATOM   7440 C CA  . ALA A 1 1391 ? 173.564 133.475 176.377 1.00 49.27  ? 1391 ALA A CA  1 
ATOM   7441 C C   . ALA A 1 1391 ? 173.222 132.003 176.552 1.00 53.17  ? 1391 ALA A C   1 
ATOM   7442 O O   . ALA A 1 1391 ? 173.583 131.389 177.561 1.00 56.75  ? 1391 ALA A O   1 
ATOM   7443 C CB  . ALA A 1 1391 ? 172.392 134.356 176.803 1.00 49.62  ? 1391 ALA A CB  1 
ATOM   7444 N N   . PHE A 1 1392 ? 172.522 131.421 175.578 1.00 52.63  ? 1392 PHE A N   1 
ATOM   7445 C CA  . PHE A 1 1392 ? 172.211 129.997 175.642 1.00 54.85  ? 1392 PHE A CA  1 
ATOM   7446 C C   . PHE A 1 1392 ? 173.478 129.154 175.575 1.00 55.24  ? 1392 PHE A C   1 
ATOM   7447 O O   . PHE A 1 1392 ? 173.639 128.193 176.334 1.00 60.51  ? 1392 PHE A O   1 
ATOM   7448 C CB  . PHE A 1 1392 ? 171.254 129.624 174.510 1.00 51.02  ? 1392 PHE A CB  1 
ATOM   7449 C CG  . PHE A 1 1392 ? 170.873 128.176 174.490 1.00 46.11  ? 1392 PHE A CG  1 
ATOM   7450 C CD1 . PHE A 1 1392 ? 169.836 127.711 175.273 1.00 51.12  ? 1392 PHE A CD1 1 
ATOM   7451 C CD2 . PHE A 1 1392 ? 171.545 127.281 173.680 1.00 51.36  ? 1392 PHE A CD2 1 
ATOM   7452 C CE1 . PHE A 1 1392 ? 169.479 126.383 175.253 1.00 56.05  ? 1392 PHE A CE1 1 
ATOM   7453 C CE2 . PHE A 1 1392 ? 171.194 125.950 173.659 1.00 52.21  ? 1392 PHE A CE2 1 
ATOM   7454 C CZ  . PHE A 1 1392 ? 170.158 125.502 174.446 1.00 53.67  ? 1392 PHE A CZ  1 
ATOM   7455 N N   . SER A 1 1393 ? 174.391 129.502 174.669 1.00 57.39  ? 1393 SER A N   1 
ATOM   7456 C CA  . SER A 1 1393 ? 175.574 128.676 174.456 1.00 54.10  ? 1393 SER A CA  1 
ATOM   7457 C C   . SER A 1 1393 ? 176.517 128.726 175.651 1.00 57.09  ? 1393 SER A C   1 
ATOM   7458 O O   . SER A 1 1393 ? 177.070 127.696 176.052 1.00 61.98  ? 1393 SER A O   1 
ATOM   7459 C CB  . SER A 1 1393 ? 176.298 129.115 173.186 1.00 60.18  ? 1393 SER A CB  1 
ATOM   7460 O OG  . SER A 1 1393 ? 175.479 128.930 172.045 1.00 60.61  ? 1393 SER A OG  1 
ATOM   7461 N N   . HIS A 1 1394 ? 176.716 129.907 176.233 1.00 71.97  ? 1394 HIS A N   1 
ATOM   7462 C CA  . HIS A 1 1394 ? 177.659 130.050 177.334 1.00 71.49  ? 1394 HIS A CA  1 
ATOM   7463 C C   . HIS A 1 1394 ? 177.145 129.483 178.651 1.00 74.92  ? 1394 HIS A C   1 
ATOM   7464 O O   . HIS A 1 1394 ? 177.937 129.329 179.585 1.00 78.68  ? 1394 HIS A O   1 
ATOM   7465 C CB  . HIS A 1 1394 ? 178.024 131.521 177.530 1.00 75.79  ? 1394 HIS A CB  1 
ATOM   7466 C CG  . HIS A 1 1394 ? 179.177 131.975 176.693 1.00 80.66  ? 1394 HIS A CG  1 
ATOM   7467 N ND1 . HIS A 1 1394 ? 180.488 131.832 177.094 1.00 81.08  ? 1394 HIS A ND1 1 
ATOM   7468 C CD2 . HIS A 1 1394 ? 179.218 132.572 175.480 1.00 79.17  ? 1394 HIS A CD2 1 
ATOM   7469 C CE1 . HIS A 1 1394 ? 181.286 132.320 176.162 1.00 84.11  ? 1394 HIS A CE1 1 
ATOM   7470 N NE2 . HIS A 1 1394 ? 180.541 132.775 175.172 1.00 81.45  ? 1394 HIS A NE2 1 
ATOM   7471 N N   . SER A 1 1395 ? 175.857 129.173 178.754 1.00 73.97  ? 1395 SER A N   1 
ATOM   7472 C CA  . SER A 1 1395 ? 175.312 128.674 180.005 1.00 69.56  ? 1395 SER A CA  1 
ATOM   7473 C C   . SER A 1 1395 ? 175.834 127.271 180.301 1.00 74.05  ? 1395 SER A C   1 
ATOM   7474 O O   . SER A 1 1395 ? 176.313 126.555 179.419 1.00 78.36  ? 1395 SER A O   1 
ATOM   7475 C CB  . SER A 1 1395 ? 173.786 128.664 179.961 1.00 64.76  ? 1395 SER A CB  1 
ATOM   7476 O OG  . SER A 1 1395 ? 173.320 127.809 178.936 1.00 72.09  ? 1395 SER A OG  1 
ATOM   7477 N N   . MET A 1 1396 ? 175.737 126.883 181.573 1.00 88.60  ? 1396 MET A N   1 
ATOM   7478 C CA  . MET A 1 1396 ? 176.224 125.591 182.036 1.00 90.21  ? 1396 MET A CA  1 
ATOM   7479 C C   . MET A 1 1396 ? 175.097 124.667 182.480 1.00 92.15  ? 1396 MET A C   1 
ATOM   7480 O O   . MET A 1 1396 ? 175.333 123.738 183.258 1.00 94.84  ? 1396 MET A O   1 
ATOM   7481 C CB  . MET A 1 1396 ? 177.231 125.779 183.170 1.00 90.16  ? 1396 MET A CB  1 
ATOM   7482 C CG  . MET A 1 1396 ? 178.521 126.454 182.744 1.00 95.02  ? 1396 MET A CG  1 
ATOM   7483 S SD  . MET A 1 1396 ? 179.691 126.643 184.102 1.00 103.62 ? 1396 MET A SD  1 
ATOM   7484 C CE  . MET A 1 1396 ? 181.092 127.351 183.242 1.00 90.73  ? 1396 MET A CE  1 
ATOM   7485 N N   . GLY A 1 1397 ? 173.876 124.906 182.009 1.00 79.23  ? 1397 GLY A N   1 
ATOM   7486 C CA  . GLY A 1 1397 ? 172.777 124.029 182.362 1.00 76.91  ? 1397 GLY A CA  1 
ATOM   7487 C C   . GLY A 1 1397 ? 172.964 122.637 181.790 1.00 81.46  ? 1397 GLY A C   1 
ATOM   7488 O O   . GLY A 1 1397 ? 173.634 122.439 180.776 1.00 84.18  ? 1397 GLY A O   1 
ATOM   7489 N N   . ARG A 1 1398 ? 172.359 121.656 182.459 1.00 83.16  ? 1398 ARG A N   1 
ATOM   7490 C CA  . ARG A 1 1398 ? 172.501 120.270 182.030 1.00 82.29  ? 1398 ARG A CA  1 
ATOM   7491 C C   . ARG A 1 1398 ? 171.595 119.967 180.843 1.00 81.27  ? 1398 ARG A C   1 
ATOM   7492 O O   . ARG A 1 1398 ? 172.069 119.616 179.758 1.00 81.68  ? 1398 ARG A O   1 
ATOM   7493 C CB  . ARG A 1 1398 ? 172.198 119.330 183.197 1.00 82.50  ? 1398 ARG A CB  1 
ATOM   7494 C CG  . ARG A 1 1398 ? 172.956 119.667 184.467 1.00 83.43  ? 1398 ARG A CG  1 
ATOM   7495 C CD  . ARG A 1 1398 ? 172.581 118.726 185.596 1.00 86.27  ? 1398 ARG A CD  1 
ATOM   7496 N NE  . ARG A 1 1398 ? 173.224 119.099 186.850 1.00 85.14  ? 1398 ARG A NE  1 
ATOM   7497 C CZ  . ARG A 1 1398 ? 173.105 118.421 187.983 1.00 87.88  ? 1398 ARG A CZ  1 
ATOM   7498 N NH1 . ARG A 1 1398 ? 172.375 117.320 188.056 1.00 89.34  ? 1398 ARG A NH1 1 
ATOM   7499 N NH2 . ARG A 1 1398 ? 173.733 118.859 189.070 1.00 87.10  ? 1398 ARG A NH2 1 
ATOM   7500 N N   . THR A 1 1399 ? 170.288 120.096 181.032 1.00 80.95  ? 1399 THR A N   1 
ATOM   7501 C CA  . THR A 1 1399 ? 169.335 119.903 179.953 1.00 82.33  ? 1399 THR A CA  1 
ATOM   7502 C C   . THR A 1 1399 ? 169.223 121.173 179.117 1.00 80.55  ? 1399 THR A C   1 
ATOM   7503 O O   . THR A 1 1399 ? 169.756 122.227 179.463 1.00 82.21  ? 1399 THR A O   1 
ATOM   7504 C CB  . THR A 1 1399 ? 167.964 119.514 180.506 1.00 82.00  ? 1399 THR A CB  1 
ATOM   7505 O OG1 . THR A 1 1399 ? 167.436 120.596 181.282 1.00 83.70  ? 1399 THR A OG1 1 
ATOM   7506 C CG2 . THR A 1 1399 ? 168.076 118.281 181.386 1.00 80.39  ? 1399 THR A CG2 1 
ATOM   7507 N N   . ARG A 1 1400 ? 168.519 121.060 177.990 1.00 77.38  ? 1400 ARG A N   1 
ATOM   7508 C CA  . ARG A 1 1400 ? 168.270 122.236 177.165 1.00 74.39  ? 1400 ARG A CA  1 
ATOM   7509 C C   . ARG A 1 1400 ? 167.386 123.238 177.892 1.00 70.84  ? 1400 ARG A C   1 
ATOM   7510 O O   . ARG A 1 1400 ? 167.564 124.453 177.744 1.00 78.28  ? 1400 ARG A O   1 
ATOM   7511 C CB  . ARG A 1 1400 ? 167.639 121.829 175.836 1.00 73.94  ? 1400 ARG A CB  1 
ATOM   7512 C CG  . ARG A 1 1400 ? 168.584 121.105 174.897 1.00 70.28  ? 1400 ARG A CG  1 
ATOM   7513 C CD  . ARG A 1 1400 ? 167.920 120.801 173.568 1.00 68.86  ? 1400 ARG A CD  1 
ATOM   7514 N NE  . ARG A 1 1400 ? 168.853 120.191 172.631 1.00 74.29  ? 1400 ARG A NE  1 
ATOM   7515 C CZ  . ARG A 1 1400 ? 169.099 118.891 172.561 1.00 77.51  ? 1400 ARG A CZ  1 
ATOM   7516 N NH1 . ARG A 1 1400 ? 168.487 118.029 173.356 1.00 77.06  ? 1400 ARG A NH1 1 
ATOM   7517 N NH2 . ARG A 1 1400 ? 169.983 118.444 171.674 1.00 74.77  ? 1400 ARG A NH2 1 
ATOM   7518 N N   . ASP A 1 1401 ? 166.421 122.750 178.673 1.00 68.51  ? 1401 ASP A N   1 
ATOM   7519 C CA  . ASP A 1 1401 ? 165.517 123.652 179.377 1.00 73.04  ? 1401 ASP A CA  1 
ATOM   7520 C C   . ASP A 1 1401 ? 166.264 124.518 180.381 1.00 74.51  ? 1401 ASP A C   1 
ATOM   7521 O O   . ASP A 1 1401 ? 165.985 125.714 180.501 1.00 78.34  ? 1401 ASP A O   1 
ATOM   7522 C CB  . ASP A 1 1401 ? 164.412 122.858 180.070 1.00 75.73  ? 1401 ASP A CB  1 
ATOM   7523 C CG  . ASP A 1 1401 ? 163.312 122.442 179.119 1.00 80.20  ? 1401 ASP A CG  1 
ATOM   7524 O OD1 . ASP A 1 1401 ? 163.069 123.172 178.136 1.00 78.42  ? 1401 ASP A OD1 1 
ATOM   7525 O OD2 . ASP A 1 1401 ? 162.686 121.387 179.354 1.00 85.56  ? 1401 ASP A OD2 1 
ATOM   7526 N N   . GLU A 1 1402 ? 167.210 123.933 181.117 1.00 70.20  ? 1402 GLU A N   1 
ATOM   7527 C CA  . GLU A 1 1402 ? 167.975 124.719 182.080 1.00 68.25  ? 1402 GLU A CA  1 
ATOM   7528 C C   . GLU A 1 1402 ? 168.798 125.792 181.383 1.00 73.05  ? 1402 GLU A C   1 
ATOM   7529 O O   . GLU A 1 1402 ? 168.878 126.932 181.857 1.00 80.09  ? 1402 GLU A O   1 
ATOM   7530 C CB  . GLU A 1 1402 ? 168.876 123.806 182.908 1.00 72.97  ? 1402 GLU A CB  1 
ATOM   7531 C CG  . GLU A 1 1402 ? 168.126 122.815 183.777 1.00 78.33  ? 1402 GLU A CG  1 
ATOM   7532 C CD  . GLU A 1 1402 ? 169.054 121.930 184.585 1.00 82.98  ? 1402 GLU A CD  1 
ATOM   7533 O OE1 . GLU A 1 1402 ? 170.281 121.989 184.357 1.00 83.09  ? 1402 GLU A OE1 1 
ATOM   7534 O OE2 . GLU A 1 1402 ? 168.559 121.177 185.448 1.00 82.13  ? 1402 GLU A OE2 1 
ATOM   7535 N N   . LYS A 1 1403 ? 169.420 125.445 180.256 1.00 67.23  ? 1403 LYS A N   1 
ATOM   7536 C CA  . LYS A 1 1403 ? 170.196 126.429 179.511 1.00 58.99  ? 1403 LYS A CA  1 
ATOM   7537 C C   . LYS A 1 1403 ? 169.304 127.546 178.988 1.00 59.93  ? 1403 LYS A C   1 
ATOM   7538 O O   . LYS A 1 1403 ? 169.694 128.718 179.004 1.00 66.29  ? 1403 LYS A O   1 
ATOM   7539 C CB  . LYS A 1 1403 ? 170.946 125.750 178.366 1.00 57.32  ? 1403 LYS A CB  1 
ATOM   7540 C CG  . LYS A 1 1403 ? 171.862 124.625 178.816 1.00 60.77  ? 1403 LYS A CG  1 
ATOM   7541 C CD  . LYS A 1 1403 ? 172.677 124.067 177.665 1.00 58.82  ? 1403 LYS A CD  1 
ATOM   7542 C CE  . LYS A 1 1403 ? 173.693 125.077 177.175 1.00 56.89  ? 1403 LYS A CE  1 
ATOM   7543 N NZ  . LYS A 1 1403 ? 174.546 124.525 176.091 1.00 57.48  ? 1403 LYS A NZ  1 
ATOM   7544 N N   . MET A 1 1404 ? 168.102 127.205 178.521 1.00 56.87  ? 1404 MET A N   1 
ATOM   7545 C CA  . MET A 1 1404 ? 167.171 128.233 178.067 1.00 50.56  ? 1404 MET A CA  1 
ATOM   7546 C C   . MET A 1 1404 ? 166.743 129.134 179.217 1.00 60.40  ? 1404 MET A C   1 
ATOM   7547 O O   . MET A 1 1404 ? 166.644 130.357 179.053 1.00 73.05  ? 1404 MET A O   1 
ATOM   7548 C CB  . MET A 1 1404 ? 165.956 127.585 177.408 1.00 60.18  ? 1404 MET A CB  1 
ATOM   7549 C CG  . MET A 1 1404 ? 164.983 128.571 176.796 1.00 66.04  ? 1404 MET A CG  1 
ATOM   7550 S SD  . MET A 1 1404 ? 163.574 128.918 177.859 1.00 78.11  ? 1404 MET A SD  1 
ATOM   7551 C CE  . MET A 1 1404 ? 162.754 127.329 177.854 1.00 65.17  ? 1404 MET A CE  1 
ATOM   7552 N N   . LYS A 1 1405 ? 166.483 128.548 180.388 1.00 65.62  ? 1405 LYS A N   1 
ATOM   7553 C CA  . LYS A 1 1405 ? 166.133 129.347 181.559 1.00 61.54  ? 1405 LYS A CA  1 
ATOM   7554 C C   . LYS A 1 1405 ? 167.248 130.323 181.899 1.00 63.28  ? 1405 LYS A C   1 
ATOM   7555 O O   . LYS A 1 1405 ? 166.998 131.508 182.148 1.00 69.53  ? 1405 LYS A O   1 
ATOM   7556 C CB  . LYS A 1 1405 ? 165.850 128.443 182.759 1.00 61.59  ? 1405 LYS A CB  1 
ATOM   7557 C CG  . LYS A 1 1405 ? 164.647 127.538 182.621 1.00 67.75  ? 1405 LYS A CG  1 
ATOM   7558 C CD  . LYS A 1 1405 ? 164.358 126.826 183.933 1.00 68.67  ? 1405 LYS A CD  1 
ATOM   7559 C CE  . LYS A 1 1405 ? 163.180 125.877 183.807 1.00 68.87  ? 1405 LYS A CE  1 
ATOM   7560 N NZ  . LYS A 1 1405 ? 163.453 124.775 182.845 1.00 71.03  ? 1405 LYS A NZ  1 
ATOM   7561 N N   . GLU A 1 1406 ? 168.489 129.837 181.918 1.00 70.86  ? 1406 GLU A N   1 
ATOM   7562 C CA  . GLU A 1 1406 ? 169.613 130.708 182.241 1.00 67.37  ? 1406 GLU A CA  1 
ATOM   7563 C C   . GLU A 1 1406 ? 169.781 131.800 181.195 1.00 69.93  ? 1406 GLU A C   1 
ATOM   7564 O O   . GLU A 1 1406 ? 170.008 132.966 181.537 1.00 78.51  ? 1406 GLU A O   1 
ATOM   7565 C CB  . GLU A 1 1406 ? 170.893 129.888 182.377 1.00 67.49  ? 1406 GLU A CB  1 
ATOM   7566 C CG  . GLU A 1 1406 ? 170.841 128.861 183.491 1.00 75.59  ? 1406 GLU A CG  1 
ATOM   7567 C CD  . GLU A 1 1406 ? 172.155 128.134 183.678 1.00 85.15  ? 1406 GLU A CD  1 
ATOM   7568 O OE1 . GLU A 1 1406 ? 173.179 128.606 183.140 1.00 87.68  ? 1406 GLU A OE1 1 
ATOM   7569 O OE2 . GLU A 1 1406 ? 172.166 127.089 184.363 1.00 84.00  ? 1406 GLU A OE2 1 
ATOM   7570 N N   . SER A 1 1407 ? 169.659 131.447 179.915 1.00 48.04  ? 1407 SER A N   1 
ATOM   7571 C CA  . SER A 1 1407 ? 169.818 132.438 178.858 1.00 43.47  ? 1407 SER A CA  1 
ATOM   7572 C C   . SER A 1 1407 ? 168.771 133.534 178.968 1.00 42.57  ? 1407 SER A C   1 
ATOM   7573 O O   . SER A 1 1407 ? 169.090 134.722 178.843 1.00 56.83  ? 1407 SER A O   1 
ATOM   7574 C CB  . SER A 1 1407 ? 169.737 131.763 177.494 1.00 52.37  ? 1407 SER A CB  1 
ATOM   7575 O OG  . SER A 1 1407 ? 168.469 131.163 177.305 1.00 62.40  ? 1407 SER A OG  1 
ATOM   7576 N N   . LEU A 1 1408 ? 167.512 133.157 179.197 1.00 50.70  ? 1408 LEU A N   1 
ATOM   7577 C CA  . LEU A 1 1408 ? 166.474 134.166 179.368 1.00 54.45  ? 1408 LEU A CA  1 
ATOM   7578 C C   . LEU A 1 1408 ? 166.748 135.022 180.595 1.00 57.39  ? 1408 LEU A C   1 
ATOM   7579 O O   . LEU A 1 1408 ? 166.827 136.251 180.499 1.00 61.20  ? 1408 LEU A O   1 
ATOM   7580 C CB  . LEU A 1 1408 ? 165.102 133.505 179.464 1.00 44.48  ? 1408 LEU A CB  1 
ATOM   7581 C CG  . LEU A 1 1408 ? 164.585 132.914 178.155 1.00 48.94  ? 1408 LEU A CG  1 
ATOM   7582 C CD1 . LEU A 1 1408 ? 163.158 132.444 178.318 1.00 61.03  ? 1408 LEU A CD1 1 
ATOM   7583 C CD2 . LEU A 1 1408 ? 164.685 133.938 177.045 1.00 48.68  ? 1408 LEU A CD2 1 
ATOM   7584 N N   . HIS A 1 1409 ? 166.963 134.380 181.747 1.00 59.76  ? 1409 HIS A N   1 
ATOM   7585 C CA  . HIS A 1 1409 ? 167.179 135.104 182.994 1.00 53.91  ? 1409 HIS A CA  1 
ATOM   7586 C C   . HIS A 1 1409 ? 168.367 136.049 182.902 1.00 60.55  ? 1409 HIS A C   1 
ATOM   7587 O O   . HIS A 1 1409 ? 168.415 137.055 183.617 1.00 70.86  ? 1409 HIS A O   1 
ATOM   7588 C CB  . HIS A 1 1409 ? 167.379 134.104 184.132 1.00 55.81  ? 1409 HIS A CB  1 
ATOM   7589 C CG  . HIS A 1 1409 ? 167.556 134.737 185.474 1.00 64.88  ? 1409 HIS A CG  1 
ATOM   7590 N ND1 . HIS A 1 1409 ? 168.760 135.256 185.899 1.00 66.46  ? 1409 HIS A ND1 1 
ATOM   7591 C CD2 . HIS A 1 1409 ? 166.686 134.921 186.494 1.00 65.85  ? 1409 HIS A CD2 1 
ATOM   7592 C CE1 . HIS A 1 1409 ? 168.621 135.739 187.120 1.00 68.03  ? 1409 HIS A CE1 1 
ATOM   7593 N NE2 . HIS A 1 1409 ? 167.372 135.549 187.504 1.00 70.35  ? 1409 HIS A NE2 1 
ATOM   7594 N N   . LEU A 1 1410 ? 169.331 135.751 182.032 1.00 59.76  ? 1410 LEU A N   1 
ATOM   7595 C CA  . LEU A 1 1410 ? 170.483 136.632 181.899 1.00 54.10  ? 1410 LEU A CA  1 
ATOM   7596 C C   . LEU A 1 1410 ? 170.221 137.759 180.909 1.00 55.70  ? 1410 LEU A C   1 
ATOM   7597 O O   . LEU A 1 1410 ? 170.418 138.934 181.234 1.00 61.26  ? 1410 LEU A O   1 
ATOM   7598 C CB  . LEU A 1 1410 ? 171.713 135.832 181.476 1.00 54.13  ? 1410 LEU A CB  1 
ATOM   7599 C CG  . LEU A 1 1410 ? 172.293 134.898 182.534 1.00 58.24  ? 1410 LEU A CG  1 
ATOM   7600 C CD1 . LEU A 1 1410 ? 173.480 134.144 181.972 1.00 60.78  ? 1410 LEU A CD1 1 
ATOM   7601 C CD2 . LEU A 1 1410 ? 172.685 135.678 183.772 1.00 60.84  ? 1410 LEU A CD2 1 
ATOM   7602 N N   . MET A 1 1411 ? 169.772 137.430 179.695 1.00 50.26  ? 1411 MET A N   1 
ATOM   7603 C CA  . MET A 1 1411 ? 169.775 138.395 178.603 1.00 48.15  ? 1411 MET A CA  1 
ATOM   7604 C C   . MET A 1 1411 ? 168.401 138.615 177.981 1.00 54.12  ? 1411 MET A C   1 
ATOM   7605 O O   . MET A 1 1411 ? 168.318 138.876 176.779 1.00 61.59  ? 1411 MET A O   1 
ATOM   7606 C CB  . MET A 1 1411 ? 170.768 137.962 177.524 1.00 46.27  ? 1411 MET A CB  1 
ATOM   7607 C CG  . MET A 1 1411 ? 172.213 137.946 177.976 1.00 53.70  ? 1411 MET A CG  1 
ATOM   7608 S SD  . MET A 1 1411 ? 172.911 139.598 178.126 1.00 79.08  ? 1411 MET A SD  1 
ATOM   7609 C CE  . MET A 1 1411 ? 172.812 140.155 176.428 1.00 56.68  ? 1411 MET A CE  1 
ATOM   7610 N N   . ILE A 1 1412 ? 167.319 138.523 178.749 1.00 38.34  ? 1412 ILE A N   1 
ATOM   7611 C CA  . ILE A 1 1412 ? 166.032 138.905 178.185 1.00 37.95  ? 1412 ILE A CA  1 
ATOM   7612 C C   . ILE A 1 1412 ? 165.684 140.351 178.519 1.00 53.91  ? 1412 ILE A C   1 
ATOM   7613 O O   . ILE A 1 1412 ? 164.860 140.961 177.832 1.00 61.38  ? 1412 ILE A O   1 
ATOM   7614 C CB  . ILE A 1 1412 ? 164.921 137.951 178.646 1.00 46.12  ? 1412 ILE A CB  1 
ATOM   7615 C CG1 . ILE A 1 1412 ? 163.768 137.969 177.643 1.00 42.55  ? 1412 ILE A CG1 1 
ATOM   7616 C CG2 . ILE A 1 1412 ? 164.420 138.340 180.022 1.00 56.06  ? 1412 ILE A CG2 1 
ATOM   7617 C CD1 . ILE A 1 1412 ? 162.660 137.006 177.973 1.00 49.53  ? 1412 ILE A CD1 1 
ATOM   7618 N N   . GLY A 1 1413 ? 166.293 140.913 179.556 1.00 47.77  ? 1413 GLY A N   1 
ATOM   7619 C CA  . GLY A 1 1413 ? 166.122 142.307 179.875 1.00 36.18  ? 1413 GLY A CA  1 
ATOM   7620 C C   . GLY A 1 1413 ? 166.690 143.210 178.800 1.00 37.52  ? 1413 GLY A C   1 
ATOM   7621 O O   . GLY A 1 1413 ? 165.980 144.029 178.209 1.00 45.78  ? 1413 GLY A O   1 
ATOM   7622 N N   . PRO A 1 1414 ? 167.994 143.085 178.533 1.00 35.74  ? 1414 PRO A N   1 
ATOM   7623 C CA  . PRO A 1 1414 ? 168.597 143.910 177.476 1.00 40.46  ? 1414 PRO A CA  1 
ATOM   7624 C C   . PRO A 1 1414 ? 167.953 143.729 176.118 1.00 44.10  ? 1414 PRO A C   1 
ATOM   7625 O O   . PRO A 1 1414 ? 167.828 144.704 175.372 1.00 43.38  ? 1414 PRO A O   1 
ATOM   7626 C CB  . PRO A 1 1414 ? 170.057 143.447 177.469 1.00 36.84  ? 1414 PRO A CB  1 
ATOM   7627 C CG  . PRO A 1 1414 ? 170.292 142.971 178.829 1.00 38.28  ? 1414 PRO A CG  1 
ATOM   7628 C CD  . PRO A 1 1414 ? 169.016 142.346 179.291 1.00 36.01  ? 1414 PRO A CD  1 
ATOM   7629 N N   . VAL A 1 1415 ? 167.540 142.511 175.769 1.00 46.61  ? 1415 VAL A N   1 
ATOM   7630 C CA  . VAL A 1 1415 ? 166.948 142.284 174.454 1.00 41.08  ? 1415 VAL A CA  1 
ATOM   7631 C C   . VAL A 1 1415 ? 165.641 143.053 174.319 1.00 47.76  ? 1415 VAL A C   1 
ATOM   7632 O O   . VAL A 1 1415 ? 165.399 143.729 173.313 1.00 52.34  ? 1415 VAL A O   1 
ATOM   7633 C CB  . VAL A 1 1415 ? 166.749 140.780 174.207 1.00 43.73  ? 1415 VAL A CB  1 
ATOM   7634 C CG1 . VAL A 1 1415 ? 165.748 140.557 173.093 1.00 46.66  ? 1415 VAL A CG1 1 
ATOM   7635 C CG2 . VAL A 1 1415 ? 168.071 140.137 173.854 1.00 47.26  ? 1415 VAL A CG2 1 
ATOM   7636 N N   . LEU A 1 1416 ? 164.781 142.968 175.334 1.00 50.66  ? 1416 LEU A N   1 
ATOM   7637 C CA  . LEU A 1 1416 ? 163.530 143.714 175.293 1.00 46.39  ? 1416 LEU A CA  1 
ATOM   7638 C C   . LEU A 1 1416 ? 163.780 145.214 175.320 1.00 49.04  ? 1416 LEU A C   1 
ATOM   7639 O O   . LEU A 1 1416 ? 163.116 145.973 174.604 1.00 56.74  ? 1416 LEU A O   1 
ATOM   7640 C CB  . LEU A 1 1416 ? 162.630 143.305 176.456 1.00 45.75  ? 1416 LEU A CB  1 
ATOM   7641 C CG  . LEU A 1 1416 ? 161.693 142.135 176.179 1.00 46.25  ? 1416 LEU A CG  1 
ATOM   7642 C CD1 . LEU A 1 1416 ? 160.759 141.919 177.348 1.00 51.52  ? 1416 LEU A CD1 1 
ATOM   7643 C CD2 . LEU A 1 1416 ? 160.903 142.398 174.919 1.00 50.33  ? 1416 LEU A CD2 1 
ATOM   7644 N N   . HIS A 1 1417 ? 164.722 145.661 176.151 1.00 42.29  ? 1417 HIS A N   1 
ATOM   7645 C CA  . HIS A 1 1417 ? 164.957 147.093 176.292 1.00 40.07  ? 1417 HIS A CA  1 
ATOM   7646 C C   . HIS A 1 1417 ? 165.525 147.695 175.014 1.00 50.05  ? 1417 HIS A C   1 
ATOM   7647 O O   . HIS A 1 1417 ? 165.118 148.786 174.608 1.00 57.42  ? 1417 HIS A O   1 
ATOM   7648 C CB  . HIS A 1 1417 ? 165.888 147.355 177.473 1.00 44.85  ? 1417 HIS A CB  1 
ATOM   7649 C CG  . HIS A 1 1417 ? 165.311 146.947 178.791 1.00 49.45  ? 1417 HIS A CG  1 
ATOM   7650 N ND1 . HIS A 1 1417 ? 163.987 146.604 178.947 1.00 53.55  ? 1417 HIS A ND1 1 
ATOM   7651 C CD2 . HIS A 1 1417 ? 165.879 146.823 180.013 1.00 51.68  ? 1417 HIS A CD2 1 
ATOM   7652 C CE1 . HIS A 1 1417 ? 163.762 146.289 180.209 1.00 53.41  ? 1417 HIS A CE1 1 
ATOM   7653 N NE2 . HIS A 1 1417 ? 164.893 146.413 180.878 1.00 57.54  ? 1417 HIS A NE2 1 
ATOM   7654 N N   . SER A 1 1418 ? 166.452 146.999 174.359 1.00 47.87  ? 1418 SER A N   1 
ATOM   7655 C CA  . SER A 1 1418 ? 167.082 147.525 173.157 1.00 42.47  ? 1418 SER A CA  1 
ATOM   7656 C C   . SER A 1 1418 ? 166.115 147.659 171.992 1.00 55.47  ? 1418 SER A C   1 
ATOM   7657 O O   . SER A 1 1418 ? 166.406 148.407 171.054 1.00 58.92  ? 1418 SER A O   1 
ATOM   7658 C CB  . SER A 1 1418 ? 168.251 146.629 172.753 1.00 50.90  ? 1418 SER A CB  1 
ATOM   7659 O OG  . SER A 1 1418 ? 167.814 145.306 172.509 1.00 56.90  ? 1418 SER A OG  1 
ATOM   7660 N N   . GLY A 1 1419 ? 164.983 146.965 172.028 1.00 46.58  ? 1419 GLY A N   1 
ATOM   7661 C CA  . GLY A 1 1419 ? 163.991 147.095 170.982 1.00 34.47  ? 1419 GLY A CA  1 
ATOM   7662 C C   . GLY A 1 1419 ? 162.900 148.068 171.366 1.00 40.81  ? 1419 GLY A C   1 
ATOM   7663 O O   . GLY A 1 1419 ? 162.455 148.874 170.542 1.00 56.96  ? 1419 GLY A O   1 
ATOM   7664 N N   . LEU A 1 1420 ? 162.466 148.010 172.626 1.00 43.43  ? 1420 LEU A N   1 
ATOM   7665 C CA  . LEU A 1 1420 ? 161.441 148.936 173.088 1.00 49.16  ? 1420 LEU A CA  1 
ATOM   7666 C C   . LEU A 1 1420 ? 161.948 150.370 173.073 1.00 56.70  ? 1420 LEU A C   1 
ATOM   7667 O O   . LEU A 1 1420 ? 161.192 151.291 172.755 1.00 65.50  ? 1420 LEU A O   1 
ATOM   7668 C CB  . LEU A 1 1420 ? 160.963 148.544 174.483 1.00 45.66  ? 1420 LEU A CB  1 
ATOM   7669 C CG  . LEU A 1 1420 ? 160.061 147.313 174.530 1.00 46.44  ? 1420 LEU A CG  1 
ATOM   7670 C CD1 . LEU A 1 1420 ? 159.543 147.086 175.937 1.00 54.86  ? 1420 LEU A CD1 1 
ATOM   7671 C CD2 . LEU A 1 1420 ? 158.911 147.467 173.555 1.00 43.46  ? 1420 LEU A CD2 1 
ATOM   7672 N N   . SER A 1 1421 ? 163.222 150.582 173.407 1.00 48.49  ? 1421 SER A N   1 
ATOM   7673 C CA  . SER A 1 1421 ? 163.790 151.922 173.349 1.00 46.00  ? 1421 SER A CA  1 
ATOM   7674 C C   . SER A 1 1421 ? 163.774 152.465 171.929 1.00 48.27  ? 1421 SER A C   1 
ATOM   7675 O O   . SER A 1 1421 ? 163.360 153.609 171.692 1.00 63.52  ? 1421 SER A O   1 
ATOM   7676 C CB  . SER A 1 1421 ? 165.216 151.894 173.891 1.00 50.09  ? 1421 SER A CB  1 
ATOM   7677 O OG  . SER A 1 1421 ? 166.009 150.968 173.171 1.00 56.24  ? 1421 SER A OG  1 
ATOM   7678 N N   . THR A 1 1422 ? 164.219 151.655 170.968 1.00 37.51  ? 1422 THR A N   1 
ATOM   7679 C CA  . THR A 1 1422 ? 164.243 152.098 169.582 1.00 40.58  ? 1422 THR A CA  1 
ATOM   7680 C C   . THR A 1 1422 ? 162.837 152.395 169.087 1.00 44.73  ? 1422 THR A C   1 
ATOM   7681 O O   . THR A 1 1422 ? 162.600 153.417 168.434 1.00 62.20  ? 1422 THR A O   1 
ATOM   7682 C CB  . THR A 1 1422 ? 164.912 151.043 168.705 1.00 50.17  ? 1422 THR A CB  1 
ATOM   7683 O OG1 . THR A 1 1422 ? 166.179 150.689 169.269 1.00 58.42  ? 1422 THR A OG1 1 
ATOM   7684 C CG2 . THR A 1 1422 ? 165.128 151.586 167.307 1.00 42.05  ? 1422 THR A CG2 1 
ATOM   7685 N N   . TRP A 1 1423 ? 161.880 151.522 169.409 1.00 33.19  ? 1423 TRP A N   1 
ATOM   7686 C CA  . TRP A 1 1423 ? 160.517 151.765 168.956 1.00 35.43  ? 1423 TRP A CA  1 
ATOM   7687 C C   . TRP A 1 1423 ? 159.908 152.985 169.627 1.00 42.39  ? 1423 TRP A C   1 
ATOM   7688 O O   . TRP A 1 1423 ? 159.136 153.708 168.996 1.00 59.41  ? 1423 TRP A O   1 
ATOM   7689 C CB  . TRP A 1 1423 ? 159.632 150.547 169.195 1.00 41.34  ? 1423 TRP A CB  1 
ATOM   7690 C CG  . TRP A 1 1423 ? 158.299 150.706 168.545 1.00 49.47  ? 1423 TRP A CG  1 
ATOM   7691 C CD1 . TRP A 1 1423 ? 157.974 150.388 167.262 1.00 50.81  ? 1423 TRP A CD1 1 
ATOM   7692 C CD2 . TRP A 1 1423 ? 157.117 151.253 169.135 1.00 43.70  ? 1423 TRP A CD2 1 
ATOM   7693 N NE1 . TRP A 1 1423 ? 156.659 150.690 167.018 1.00 48.39  ? 1423 TRP A NE1 1 
ATOM   7694 C CE2 . TRP A 1 1423 ? 156.110 151.223 168.153 1.00 41.89  ? 1423 TRP A CE2 1 
ATOM   7695 C CE3 . TRP A 1 1423 ? 156.809 151.758 170.399 1.00 46.21  ? 1423 TRP A CE3 1 
ATOM   7696 C CZ2 . TRP A 1 1423 ? 154.819 151.678 168.396 1.00 39.45  ? 1423 TRP A CZ2 1 
ATOM   7697 C CZ3 . TRP A 1 1423 ? 155.527 152.209 170.638 1.00 49.82  ? 1423 TRP A CZ3 1 
ATOM   7698 C CH2 . TRP A 1 1423 ? 154.549 152.166 169.641 1.00 43.39  ? 1423 TRP A CH2 1 
ATOM   7699 N N   . PHE A 1 1424 ? 160.227 153.230 170.897 1.00 43.11  ? 1424 PHE A N   1 
ATOM   7700 C CA  . PHE A 1 1424 ? 159.699 154.410 171.568 1.00 42.26  ? 1424 PHE A CA  1 
ATOM   7701 C C   . PHE A 1 1424 ? 160.256 155.686 170.958 1.00 44.02  ? 1424 PHE A C   1 
ATOM   7702 O O   . PHE A 1 1424 ? 159.533 156.677 170.817 1.00 52.10  ? 1424 PHE A O   1 
ATOM   7703 C CB  . PHE A 1 1424 ? 160.002 154.345 173.063 1.00 44.15  ? 1424 PHE A CB  1 
ATOM   7704 C CG  . PHE A 1 1424 ? 159.036 153.498 173.834 1.00 50.49  ? 1424 PHE A CG  1 
ATOM   7705 C CD1 . PHE A 1 1424 ? 157.729 153.365 173.409 1.00 50.52  ? 1424 PHE A CD1 1 
ATOM   7706 C CD2 . PHE A 1 1424 ? 159.433 152.835 174.977 1.00 49.64  ? 1424 PHE A CD2 1 
ATOM   7707 C CE1 . PHE A 1 1424 ? 156.835 152.590 174.110 1.00 49.00  ? 1424 PHE A CE1 1 
ATOM   7708 C CE2 . PHE A 1 1424 ? 158.542 152.056 175.683 1.00 49.66  ? 1424 PHE A CE2 1 
ATOM   7709 C CZ  . PHE A 1 1424 ? 157.242 151.934 175.248 1.00 49.96  ? 1424 PHE A CZ  1 
ATOM   7710 N N   . VAL A 1 1425 ? 161.538 155.685 170.589 1.00 47.42  ? 1425 VAL A N   1 
ATOM   7711 C CA  . VAL A 1 1425 ? 162.081 156.867 169.928 1.00 41.26  ? 1425 VAL A CA  1 
ATOM   7712 C C   . VAL A 1 1425 ? 161.471 157.038 168.541 1.00 49.90  ? 1425 VAL A C   1 
ATOM   7713 O O   . VAL A 1 1425 ? 161.177 158.162 168.120 1.00 55.63  ? 1425 VAL A O   1 
ATOM   7714 C CB  . VAL A 1 1425 ? 163.615 156.799 169.859 1.00 38.33  ? 1425 VAL A CB  1 
ATOM   7715 C CG1 . VAL A 1 1425 ? 164.161 158.039 169.187 1.00 49.47  ? 1425 VAL A CG1 1 
ATOM   7716 C CG2 . VAL A 1 1425 ? 164.199 156.659 171.246 1.00 48.59  ? 1425 VAL A CG2 1 
ATOM   7717 N N   . ILE A 1 1426 ? 161.263 155.940 167.815 1.00 51.47  ? 1426 ILE A N   1 
ATOM   7718 C CA  . ILE A 1 1426 ? 160.742 156.013 166.454 1.00 41.88  ? 1426 ILE A CA  1 
ATOM   7719 C C   . ILE A 1 1426 ? 159.261 156.375 166.381 1.00 50.32  ? 1426 ILE A C   1 
ATOM   7720 O O   . ILE A 1 1426 ? 158.852 157.072 165.442 1.00 57.21  ? 1426 ILE A O   1 
ATOM   7721 C CB  . ILE A 1 1426 ? 161.002 154.677 165.733 1.00 44.65  ? 1426 ILE A CB  1 
ATOM   7722 C CG1 . ILE A 1 1426 ? 162.497 154.500 165.489 1.00 59.11  ? 1426 ILE A CG1 1 
ATOM   7723 C CG2 . ILE A 1 1426 ? 160.261 154.602 164.418 1.00 45.93  ? 1426 ILE A CG2 1 
ATOM   7724 C CD1 . ILE A 1 1426 ? 163.117 155.626 164.702 1.00 52.74  ? 1426 ILE A CD1 1 
ATOM   7725 N N   . SER A 1 1427 ? 158.454 155.957 167.360 1.00 52.50  ? 1427 SER A N   1 
ATOM   7726 C CA  . SER A 1 1427 ? 157.002 156.022 167.225 1.00 44.44  ? 1427 SER A CA  1 
ATOM   7727 C C   . SER A 1 1427 ? 156.500 157.434 166.965 1.00 51.00  ? 1427 SER A C   1 
ATOM   7728 O O   . SER A 1 1427 ? 155.433 157.608 166.368 1.00 63.47  ? 1427 SER A O   1 
ATOM   7729 C CB  . SER A 1 1427 ? 156.339 155.458 168.479 1.00 48.21  ? 1427 SER A CB  1 
ATOM   7730 O OG  . SER A 1 1427 ? 156.685 156.223 169.617 1.00 50.88  ? 1427 SER A OG  1 
ATOM   7731 N N   . THR A 1 1428 ? 157.242 158.451 167.400 1.00 46.90  ? 1428 THR A N   1 
ATOM   7732 C CA  . THR A 1 1428 ? 156.814 159.820 167.149 1.00 49.72  ? 1428 THR A CA  1 
ATOM   7733 C C   . THR A 1 1428 ? 156.771 160.145 165.663 1.00 53.17  ? 1428 THR A C   1 
ATOM   7734 O O   . THR A 1 1428 ? 156.083 161.090 165.268 1.00 57.71  ? 1428 THR A O   1 
ATOM   7735 C CB  . THR A 1 1428 ? 157.733 160.799 167.872 1.00 50.52  ? 1428 THR A CB  1 
ATOM   7736 O OG1 . THR A 1 1428 ? 159.090 160.553 167.488 1.00 65.02  ? 1428 THR A OG1 1 
ATOM   7737 C CG2 . THR A 1 1428 ? 157.600 160.628 169.370 1.00 44.66  ? 1428 THR A CG2 1 
ATOM   7738 N N   . LEU A 1 1429 ? 157.479 159.381 164.831 1.00 48.58  ? 1429 LEU A N   1 
ATOM   7739 C CA  . LEU A 1 1429 ? 157.441 159.597 163.391 1.00 45.26  ? 1429 LEU A CA  1 
ATOM   7740 C C   . LEU A 1 1429 ? 156.103 159.223 162.773 1.00 46.09  ? 1429 LEU A C   1 
ATOM   7741 O O   . LEU A 1 1429 ? 155.874 159.541 161.603 1.00 61.78  ? 1429 LEU A O   1 
ATOM   7742 C CB  . LEU A 1 1429 ? 158.557 158.808 162.710 1.00 47.79  ? 1429 LEU A CB  1 
ATOM   7743 C CG  . LEU A 1 1429 ? 159.979 159.200 163.097 1.00 46.44  ? 1429 LEU A CG  1 
ATOM   7744 C CD1 . LEU A 1 1429 ? 160.982 158.358 162.337 1.00 46.92  ? 1429 LEU A CD1 1 
ATOM   7745 C CD2 . LEU A 1 1429 ? 160.208 160.676 162.837 1.00 48.55  ? 1429 LEU A CD2 1 
ATOM   7746 N N   . PHE A 1 1430 ? 155.223 158.553 163.519 1.00 41.93  ? 1430 PHE A N   1 
ATOM   7747 C CA  . PHE A 1 1430 ? 153.926 158.176 162.969 1.00 48.50  ? 1430 PHE A CA  1 
ATOM   7748 C C   . PHE A 1 1430 ? 153.098 159.396 162.595 1.00 56.58  ? 1430 PHE A C   1 
ATOM   7749 O O   . PHE A 1 1430 ? 152.227 159.311 161.722 1.00 59.33  ? 1430 PHE A O   1 
ATOM   7750 C CB  . PHE A 1 1430 ? 153.169 157.305 163.970 1.00 47.56  ? 1430 PHE A CB  1 
ATOM   7751 C CG  . PHE A 1 1430 ? 151.767 156.981 163.553 1.00 52.59  ? 1430 PHE A CG  1 
ATOM   7752 C CD1 . PHE A 1 1430 ? 151.525 156.096 162.521 1.00 53.09  ? 1430 PHE A CD1 1 
ATOM   7753 C CD2 . PHE A 1 1430 ? 150.689 157.556 164.199 1.00 58.21  ? 1430 PHE A CD2 1 
ATOM   7754 C CE1 . PHE A 1 1430 ? 150.238 155.793 162.138 1.00 54.82  ? 1430 PHE A CE1 1 
ATOM   7755 C CE2 . PHE A 1 1430 ? 149.398 157.257 163.821 1.00 57.06  ? 1430 PHE A CE2 1 
ATOM   7756 C CZ  . PHE A 1 1430 ? 149.173 156.374 162.789 1.00 58.01  ? 1430 PHE A CZ  1 
ATOM   7757 N N   . PHE A 1 1431 ? 153.354 160.535 163.231 1.00 60.88  ? 1431 PHE A N   1 
ATOM   7758 C CA  . PHE A 1 1431 ? 152.617 161.761 162.967 1.00 57.20  ? 1431 PHE A CA  1 
ATOM   7759 C C   . PHE A 1 1431 ? 153.361 162.705 162.034 1.00 57.69  ? 1431 PHE A C   1 
ATOM   7760 O O   . PHE A 1 1431 ? 152.928 163.846 161.853 1.00 64.00  ? 1431 PHE A O   1 
ATOM   7761 C CB  . PHE A 1 1431 ? 152.294 162.470 164.282 1.00 53.18  ? 1431 PHE A CB  1 
ATOM   7762 C CG  . PHE A 1 1431 ? 151.665 161.577 165.307 1.00 54.96  ? 1431 PHE A CG  1 
ATOM   7763 C CD1 . PHE A 1 1431 ? 150.341 161.198 165.192 1.00 58.95  ? 1431 PHE A CD1 1 
ATOM   7764 C CD2 . PHE A 1 1431 ? 152.399 161.112 166.382 1.00 55.72  ? 1431 PHE A CD2 1 
ATOM   7765 C CE1 . PHE A 1 1431 ? 149.760 160.373 166.131 1.00 57.35  ? 1431 PHE A CE1 1 
ATOM   7766 C CE2 . PHE A 1 1431 ? 151.823 160.288 167.324 1.00 59.56  ? 1431 PHE A CE2 1 
ATOM   7767 C CZ  . PHE A 1 1431 ? 150.502 159.918 167.198 1.00 59.89  ? 1431 PHE A CZ  1 
ATOM   7768 N N   . SER A 1 1432 ? 154.467 162.261 161.442 1.00 57.41  ? 1432 SER A N   1 
ATOM   7769 C CA  . SER A 1 1432 ? 155.223 163.119 160.542 1.00 59.41  ? 1432 SER A CA  1 
ATOM   7770 C C   . SER A 1 1432 ? 154.414 163.419 159.288 1.00 58.88  ? 1432 SER A C   1 
ATOM   7771 O O   . SER A 1 1432 ? 153.764 162.537 158.722 1.00 52.74  ? 1432 SER A O   1 
ATOM   7772 C CB  . SER A 1 1432 ? 156.549 162.461 160.169 1.00 57.65  ? 1432 SER A CB  1 
ATOM   7773 O OG  . SER A 1 1432 ? 157.339 163.327 159.376 1.00 58.98  ? 1432 SER A OG  1 
ATOM   7774 N N   . ASN A 1 1433 ? 154.457 164.678 158.854 1.00 60.91  ? 1433 ASN A N   1 
ATOM   7775 C CA  . ASN A 1 1433 ? 153.672 165.118 157.709 1.00 56.98  ? 1433 ASN A CA  1 
ATOM   7776 C C   . ASN A 1 1433 ? 154.209 164.606 156.381 1.00 61.65  ? 1433 ASN A C   1 
ATOM   7777 O O   . ASN A 1 1433 ? 153.525 164.748 155.363 1.00 63.07  ? 1433 ASN A O   1 
ATOM   7778 C CB  . ASN A 1 1433 ? 153.605 166.645 157.679 1.00 57.31  ? 1433 ASN A CB  1 
ATOM   7779 C CG  . ASN A 1 1433 ? 154.964 167.288 157.821 1.00 62.50  ? 1433 ASN A CG  1 
ATOM   7780 O OD1 . ASN A 1 1433 ? 155.992 166.617 157.746 1.00 63.98  ? 1433 ASN A OD1 1 
ATOM   7781 N ND2 . ASN A 1 1433 ? 154.980 168.598 158.028 1.00 63.80  ? 1433 ASN A ND2 1 
ATOM   7782 N N   . LYS A 1 1434 ? 155.402 164.022 156.361 1.00 58.21  ? 1434 LYS A N   1 
ATOM   7783 C CA  . LYS A 1 1434 ? 156.000 163.501 155.140 1.00 47.13  ? 1434 LYS A CA  1 
ATOM   7784 C C   . LYS A 1 1434 ? 155.779 161.997 155.068 1.00 51.41  ? 1434 LYS A C   1 
ATOM   7785 O O   . LYS A 1 1434 ? 156.151 161.266 155.990 1.00 62.26  ? 1434 LYS A O   1 
ATOM   7786 C CB  . LYS A 1 1434 ? 157.491 163.832 155.086 1.00 42.04  ? 1434 LYS A CB  1 
ATOM   7787 C CG  . LYS A 1 1434 ? 157.776 165.263 154.666 1.00 43.58  ? 1434 LYS A CG  1 
ATOM   7788 C CD  . LYS A 1 1434 ? 159.161 165.710 155.085 1.00 47.64  ? 1434 LYS A CD  1 
ATOM   7789 C CE  . LYS A 1 1434 ? 159.232 165.916 156.583 1.00 50.19  ? 1434 LYS A CE  1 
ATOM   7790 N NZ  . LYS A 1 1434 ? 158.265 166.947 157.043 1.00 55.97  ? 1434 LYS A NZ  1 
ATOM   7791 N N   . ASP A 1 1435 ? 155.177 161.542 153.967 1.00 65.51  ? 1435 ASP A N   1 
ATOM   7792 C CA  . ASP A 1 1435 ? 154.769 160.146 153.865 1.00 63.95  ? 1435 ASP A CA  1 
ATOM   7793 C C   . ASP A 1 1435 ? 155.962 159.202 153.816 1.00 63.82  ? 1435 ASP A C   1 
ATOM   7794 O O   . ASP A 1 1435 ? 155.851 158.046 154.241 1.00 69.36  ? 1435 ASP A O   1 
ATOM   7795 C CB  . ASP A 1 1435 ? 153.884 159.947 152.637 1.00 69.16  ? 1435 ASP A CB  1 
ATOM   7796 C CG  . ASP A 1 1435 ? 153.044 158.689 152.723 1.00 75.80  ? 1435 ASP A CG  1 
ATOM   7797 O OD1 . ASP A 1 1435 ? 153.083 158.018 153.774 1.00 74.63  ? 1435 ASP A OD1 1 
ATOM   7798 O OD2 . ASP A 1 1435 ? 152.340 158.372 151.742 1.00 75.48  ? 1435 ASP A OD2 1 
ATOM   7799 N N   . PHE A 1 1436 ? 157.103 159.659 153.297 1.00 53.67  ? 1436 PHE A N   1 
ATOM   7800 C CA  . PHE A 1 1436 ? 158.296 158.820 153.320 1.00 53.27  ? 1436 PHE A CA  1 
ATOM   7801 C C   . PHE A 1 1436 ? 158.703 158.496 154.750 1.00 55.92  ? 1436 PHE A C   1 
ATOM   7802 O O   . PHE A 1 1436 ? 159.071 157.357 155.057 1.00 65.61  ? 1436 PHE A O   1 
ATOM   7803 C CB  . PHE A 1 1436 ? 159.445 159.502 152.580 1.00 56.44  ? 1436 PHE A CB  1 
ATOM   7804 C CG  . PHE A 1 1436 ? 159.401 159.323 151.091 1.00 62.36  ? 1436 PHE A CG  1 
ATOM   7805 C CD1 . PHE A 1 1436 ? 158.301 158.752 150.479 1.00 65.78  ? 1436 PHE A CD1 1 
ATOM   7806 C CD2 . PHE A 1 1436 ? 160.469 159.709 150.306 1.00 59.77  ? 1436 PHE A CD2 1 
ATOM   7807 C CE1 . PHE A 1 1436 ? 158.265 158.585 149.112 1.00 61.78  ? 1436 PHE A CE1 1 
ATOM   7808 C CE2 . PHE A 1 1436 ? 160.438 159.542 148.940 1.00 55.06  ? 1436 PHE A CE2 1 
ATOM   7809 C CZ  . PHE A 1 1436 ? 159.335 158.980 148.343 1.00 56.91  ? 1436 PHE A CZ  1 
ATOM   7810 N N   . THR A 1 1437 ? 158.637 159.485 155.642 1.00 47.33  ? 1437 THR A N   1 
ATOM   7811 C CA  . THR A 1 1437 ? 158.954 159.237 157.043 1.00 38.87  ? 1437 THR A CA  1 
ATOM   7812 C C   . THR A 1 1437 ? 157.953 158.275 157.669 1.00 47.33  ? 1437 THR A C   1 
ATOM   7813 O O   . THR A 1 1437 ? 158.320 157.446 158.508 1.00 61.13  ? 1437 THR A O   1 
ATOM   7814 C CB  . THR A 1 1437 ? 158.993 160.555 157.812 1.00 44.56  ? 1437 THR A CB  1 
ATOM   7815 O OG1 . THR A 1 1437 ? 159.922 161.445 157.183 1.00 51.38  ? 1437 THR A OG1 1 
ATOM   7816 C CG2 . THR A 1 1437 ? 159.433 160.321 159.240 1.00 48.69  ? 1437 THR A CG2 1 
ATOM   7817 N N   . VAL A 1 1438 ? 156.682 158.368 157.273 1.00 51.04  ? 1438 VAL A N   1 
ATOM   7818 C CA  . VAL A 1 1438 ? 155.675 157.445 157.790 1.00 47.55  ? 1438 VAL A CA  1 
ATOM   7819 C C   . VAL A 1 1438 ? 155.978 156.020 157.346 1.00 51.98  ? 1438 VAL A C   1 
ATOM   7820 O O   . VAL A 1 1438 ? 155.862 155.071 158.130 1.00 56.75  ? 1438 VAL A O   1 
ATOM   7821 C CB  . VAL A 1 1438 ? 154.269 157.887 157.352 1.00 47.91  ? 1438 VAL A CB  1 
ATOM   7822 C CG1 . VAL A 1 1438 ? 153.230 156.905 157.852 1.00 51.50  ? 1438 VAL A CG1 1 
ATOM   7823 C CG2 . VAL A 1 1438 ? 153.974 159.281 157.868 1.00 52.65  ? 1438 VAL A CG2 1 
ATOM   7824 N N   . ILE A 1 1439 ? 156.359 155.845 156.080 1.00 51.15  ? 1439 ILE A N   1 
ATOM   7825 C CA  . ILE A 1 1439 ? 156.734 154.519 155.597 1.00 48.49  ? 1439 ILE A CA  1 
ATOM   7826 C C   . ILE A 1 1439 ? 157.961 154.013 156.342 1.00 45.41  ? 1439 ILE A C   1 
ATOM   7827 O O   . ILE A 1 1439 ? 158.051 152.829 156.694 1.00 55.18  ? 1439 ILE A O   1 
ATOM   7828 C CB  . ILE A 1 1439 ? 156.967 154.550 154.075 1.00 49.33  ? 1439 ILE A CB  1 
ATOM   7829 C CG1 . ILE A 1 1439 ? 155.667 154.886 153.348 1.00 50.00  ? 1439 ILE A CG1 1 
ATOM   7830 C CG2 . ILE A 1 1439 ? 157.511 153.221 153.590 1.00 51.53  ? 1439 ILE A CG2 1 
ATOM   7831 C CD1 . ILE A 1 1439 ? 155.801 154.895 151.847 1.00 55.88  ? 1439 ILE A CD1 1 
ATOM   7832 N N   . PHE A 1 1440 ? 158.926 154.901 156.587 1.00 45.41  ? 1440 PHE A N   1 
ATOM   7833 C CA  . PHE A 1 1440 ? 160.099 154.534 157.371 1.00 46.11  ? 1440 PHE A CA  1 
ATOM   7834 C C   . PHE A 1 1440 ? 159.694 154.029 158.747 1.00 52.15  ? 1440 PHE A C   1 
ATOM   7835 O O   . PHE A 1 1440 ? 160.162 152.980 159.201 1.00 58.34  ? 1440 PHE A O   1 
ATOM   7836 C CB  . PHE A 1 1440 ? 161.038 155.734 157.489 1.00 43.46  ? 1440 PHE A CB  1 
ATOM   7837 C CG  . PHE A 1 1440 ? 162.187 155.523 158.434 1.00 51.05  ? 1440 PHE A CG  1 
ATOM   7838 C CD1 . PHE A 1 1440 ? 163.353 154.923 158.004 1.00 55.31  ? 1440 PHE A CD1 1 
ATOM   7839 C CD2 . PHE A 1 1440 ? 162.108 155.948 159.748 1.00 55.28  ? 1440 PHE A CD2 1 
ATOM   7840 C CE1 . PHE A 1 1440 ? 164.410 154.735 158.866 1.00 54.07  ? 1440 PHE A CE1 1 
ATOM   7841 C CE2 . PHE A 1 1440 ? 163.163 155.763 160.614 1.00 54.75  ? 1440 PHE A CE2 1 
ATOM   7842 C CZ  . PHE A 1 1440 ? 164.315 155.156 160.172 1.00 54.28  ? 1440 PHE A CZ  1 
ATOM   7843 N N   . PHE A 1 1441 ? 158.810 154.765 159.420 1.00 53.64  ? 1441 PHE A N   1 
ATOM   7844 C CA  . PHE A 1 1441 ? 158.361 154.358 160.745 1.00 47.56  ? 1441 PHE A CA  1 
ATOM   7845 C C   . PHE A 1 1441 ? 157.661 153.010 160.701 1.00 46.16  ? 1441 PHE A C   1 
ATOM   7846 O O   . PHE A 1 1441 ? 157.907 152.152 161.551 1.00 56.28  ? 1441 PHE A O   1 
ATOM   7847 C CB  . PHE A 1 1441 ? 157.427 155.408 161.339 1.00 43.63  ? 1441 PHE A CB  1 
ATOM   7848 C CG  . PHE A 1 1441 ? 156.437 154.846 162.314 1.00 49.46  ? 1441 PHE A CG  1 
ATOM   7849 C CD1 . PHE A 1 1441 ? 156.812 154.558 163.611 1.00 49.30  ? 1441 PHE A CD1 1 
ATOM   7850 C CD2 . PHE A 1 1441 ? 155.131 154.598 161.932 1.00 55.63  ? 1441 PHE A CD2 1 
ATOM   7851 C CE1 . PHE A 1 1441 ? 155.908 154.037 164.507 1.00 46.29  ? 1441 PHE A CE1 1 
ATOM   7852 C CE2 . PHE A 1 1441 ? 154.224 154.075 162.825 1.00 50.05  ? 1441 PHE A CE2 1 
ATOM   7853 C CZ  . PHE A 1 1441 ? 154.613 153.796 164.114 1.00 46.23  ? 1441 PHE A CZ  1 
ATOM   7854 N N   . GLN A 1 1442 ? 156.775 152.810 159.725 1.00 49.10  ? 1442 GLN A N   1 
ATOM   7855 C CA  . GLN A 1 1442 ? 156.020 151.563 159.662 1.00 48.36  ? 1442 GLN A CA  1 
ATOM   7856 C C   . GLN A 1 1442 ? 156.942 150.374 159.431 1.00 46.99  ? 1442 GLN A C   1 
ATOM   7857 O O   . GLN A 1 1442 ? 156.843 149.349 160.119 1.00 59.09  ? 1442 GLN A O   1 
ATOM   7858 C CB  . GLN A 1 1442 ? 154.962 151.651 158.564 1.00 48.25  ? 1442 GLN A CB  1 
ATOM   7859 C CG  . GLN A 1 1442 ? 153.884 152.684 158.832 1.00 50.94  ? 1442 GLN A CG  1 
ATOM   7860 C CD  . GLN A 1 1442 ? 152.922 152.831 157.675 1.00 53.86  ? 1442 GLN A CD  1 
ATOM   7861 O OE1 . GLN A 1 1442 ? 153.057 152.161 156.654 1.00 61.43  ? 1442 GLN A OE1 1 
ATOM   7862 N NE2 . GLN A 1 1442 ? 151.942 153.712 157.829 1.00 52.33  ? 1442 GLN A NE2 1 
ATOM   7863 N N   . THR A 1 1443 ? 157.859 150.498 158.472 1.00 39.81  ? 1443 THR A N   1 
ATOM   7864 C CA  . THR A 1 1443 ? 158.766 149.394 158.186 1.00 39.42  ? 1443 THR A CA  1 
ATOM   7865 C C   . THR A 1 1443 ? 159.691 149.120 159.364 1.00 47.37  ? 1443 THR A C   1 
ATOM   7866 O O   . THR A 1 1443 ? 159.949 147.959 159.704 1.00 49.12  ? 1443 THR A O   1 
ATOM   7867 C CB  . THR A 1 1443 ? 159.571 149.691 156.926 1.00 35.32  ? 1443 THR A CB  1 
ATOM   7868 O OG1 . THR A 1 1443 ? 158.689 150.153 155.898 1.00 45.59  ? 1443 THR A OG1 1 
ATOM   7869 C CG2 . THR A 1 1443 ? 160.270 148.438 156.445 1.00 46.20  ? 1443 THR A CG2 1 
ATOM   7870 N N   . LEU A 1 1444 ? 160.195 150.174 160.010 1.00 48.10  ? 1444 LEU A N   1 
ATOM   7871 C CA  . LEU A 1 1444 ? 161.080 149.973 161.150 1.00 39.25  ? 1444 LEU A CA  1 
ATOM   7872 C C   . LEU A 1 1444 ? 160.334 149.351 162.322 1.00 44.94  ? 1444 LEU A C   1 
ATOM   7873 O O   . LEU A 1 1444 ? 160.897 148.533 163.056 1.00 59.27  ? 1444 LEU A O   1 
ATOM   7874 C CB  . LEU A 1 1444 ? 161.717 151.297 161.558 1.00 39.48  ? 1444 LEU A CB  1 
ATOM   7875 C CG  . LEU A 1 1444 ? 163.010 151.164 162.354 1.00 49.26  ? 1444 LEU A CG  1 
ATOM   7876 C CD1 . LEU A 1 1444 ? 164.000 150.316 161.585 1.00 44.74  ? 1444 LEU A CD1 1 
ATOM   7877 C CD2 . LEU A 1 1444 ? 163.591 152.530 162.636 1.00 48.42  ? 1444 LEU A CD2 1 
ATOM   7878 N N   . SER A 1 1445 ? 159.071 149.731 162.520 1.00 32.07  ? 1445 SER A N   1 
ATOM   7879 C CA  . SER A 1 1445 ? 158.272 149.116 163.570 1.00 22.76  ? 1445 SER A CA  1 
ATOM   7880 C C   . SER A 1 1445 ? 158.050 147.640 163.290 1.00 30.49  ? 1445 SER A C   1 
ATOM   7881 O O   . SER A 1 1445 ? 158.116 146.814 164.204 1.00 45.21  ? 1445 SER A O   1 
ATOM   7882 C CB  . SER A 1 1445 ? 156.937 149.840 163.710 1.00 35.55  ? 1445 SER A CB  1 
ATOM   7883 O OG  . SER A 1 1445 ? 157.134 151.184 164.106 1.00 47.73  ? 1445 SER A OG  1 
ATOM   7884 N N   . LEU A 1 1446 ? 157.785 147.287 162.030 1.00 37.71  ? 1446 LEU A N   1 
ATOM   7885 C CA  . LEU A 1 1446 ? 157.678 145.873 161.685 1.00 41.80  ? 1446 LEU A CA  1 
ATOM   7886 C C   . LEU A 1 1446 ? 158.978 145.139 161.983 1.00 41.67  ? 1446 LEU A C   1 
ATOM   7887 O O   . LEU A 1 1446 ? 158.967 144.044 162.561 1.00 54.41  ? 1446 LEU A O   1 
ATOM   7888 C CB  . LEU A 1 1446 ? 157.306 145.711 160.213 1.00 42.98  ? 1446 LEU A CB  1 
ATOM   7889 C CG  . LEU A 1 1446 ? 155.893 146.117 159.809 1.00 45.56  ? 1446 LEU A CG  1 
ATOM   7890 C CD1 . LEU A 1 1446 ? 155.674 145.843 158.334 1.00 46.81  ? 1446 LEU A CD1 1 
ATOM   7891 C CD2 . LEU A 1 1446 ? 154.877 145.373 160.650 1.00 46.36  ? 1446 LEU A CD2 1 
ATOM   7892 N N   . VAL A 1 1447 ? 160.109 145.738 161.606 1.00 38.52  ? 1447 VAL A N   1 
ATOM   7893 C CA  . VAL A 1 1447 ? 161.407 145.112 161.847 1.00 37.95  ? 1447 VAL A CA  1 
ATOM   7894 C C   . VAL A 1 1447 ? 161.609 144.866 163.335 1.00 44.48  ? 1447 VAL A C   1 
ATOM   7895 O O   . VAL A 1 1447 ? 161.967 143.761 163.758 1.00 56.36  ? 1447 VAL A O   1 
ATOM   7896 C CB  . VAL A 1 1447 ? 162.537 145.980 161.269 1.00 39.05  ? 1447 VAL A CB  1 
ATOM   7897 C CG1 . VAL A 1 1447 ? 163.882 145.473 161.745 1.00 43.68  ? 1447 VAL A CG1 1 
ATOM   7898 C CG2 . VAL A 1 1447 ? 162.477 145.988 159.756 1.00 51.56  ? 1447 VAL A CG2 1 
ATOM   7899 N N   . LEU A 1 1448 ? 161.383 145.897 164.151 1.00 45.61  ? 1448 LEU A N   1 
ATOM   7900 C CA  . LEU A 1 1448 ? 161.607 145.771 165.586 1.00 40.49  ? 1448 LEU A CA  1 
ATOM   7901 C C   . LEU A 1 1448 ? 160.658 144.759 166.209 1.00 46.07  ? 1448 LEU A C   1 
ATOM   7902 O O   . LEU A 1 1448 ? 161.071 143.945 167.042 1.00 57.04  ? 1448 LEU A O   1 
ATOM   7903 C CB  . LEU A 1 1448 ? 161.457 147.131 166.261 1.00 35.07  ? 1448 LEU A CB  1 
ATOM   7904 C CG  . LEU A 1 1448 ? 162.493 148.173 165.855 1.00 36.02  ? 1448 LEU A CG  1 
ATOM   7905 C CD1 . LEU A 1 1448 ? 162.214 149.487 166.552 1.00 43.88  ? 1448 LEU A CD1 1 
ATOM   7906 C CD2 . LEU A 1 1448 ? 163.886 147.676 166.176 1.00 42.04  ? 1448 LEU A CD2 1 
ATOM   7907 N N   . PHE A 1 1449 ? 159.383 144.792 165.821 1.00 35.70  ? 1449 PHE A N   1 
ATOM   7908 C CA  . PHE A 1 1449 ? 158.415 143.863 166.387 1.00 36.54  ? 1449 PHE A CA  1 
ATOM   7909 C C   . PHE A 1 1449 ? 158.795 142.425 166.077 1.00 42.90  ? 1449 PHE A C   1 
ATOM   7910 O O   . PHE A 1 1449 ? 158.792 141.565 166.966 1.00 51.36  ? 1449 PHE A O   1 
ATOM   7911 C CB  . PHE A 1 1449 ? 157.017 144.175 165.856 1.00 42.79  ? 1449 PHE A CB  1 
ATOM   7912 C CG  . PHE A 1 1449 ? 155.987 143.152 166.229 1.00 45.11  ? 1449 PHE A CG  1 
ATOM   7913 C CD1 . PHE A 1 1449 ? 155.435 143.140 167.495 1.00 44.93  ? 1449 PHE A CD1 1 
ATOM   7914 C CD2 . PHE A 1 1449 ? 155.566 142.207 165.313 1.00 50.62  ? 1449 PHE A CD2 1 
ATOM   7915 C CE1 . PHE A 1 1449 ? 154.489 142.202 167.842 1.00 45.68  ? 1449 PHE A CE1 1 
ATOM   7916 C CE2 . PHE A 1 1449 ? 154.618 141.267 165.654 1.00 50.20  ? 1449 PHE A CE2 1 
ATOM   7917 C CZ  . PHE A 1 1449 ? 154.080 141.265 166.920 1.00 46.96  ? 1449 PHE A CZ  1 
ATOM   7918 N N   . PHE A 1 1450 ? 159.145 142.144 164.822 1.00 46.30  ? 1450 PHE A N   1 
ATOM   7919 C CA  . PHE A 1 1450 ? 159.468 140.768 164.469 1.00 44.82  ? 1450 PHE A CA  1 
ATOM   7920 C C   . PHE A 1 1450 ? 160.787 140.330 165.086 1.00 46.29  ? 1450 PHE A C   1 
ATOM   7921 O O   . PHE A 1 1450 ? 160.916 139.181 165.519 1.00 57.01  ? 1450 PHE A O   1 
ATOM   7922 C CB  . PHE A 1 1450 ? 159.478 140.597 162.954 1.00 38.83  ? 1450 PHE A CB  1 
ATOM   7923 C CG  . PHE A 1 1450 ? 158.112 140.422 162.373 1.00 42.59  ? 1450 PHE A CG  1 
ATOM   7924 C CD1 . PHE A 1 1450 ? 157.393 139.271 162.620 1.00 42.75  ? 1450 PHE A CD1 1 
ATOM   7925 C CD2 . PHE A 1 1450 ? 157.540 141.411 161.598 1.00 52.94  ? 1450 PHE A CD2 1 
ATOM   7926 C CE1 . PHE A 1 1450 ? 156.134 139.105 162.099 1.00 48.43  ? 1450 PHE A CE1 1 
ATOM   7927 C CE2 . PHE A 1 1450 ? 156.279 141.250 161.073 1.00 53.18  ? 1450 PHE A CE2 1 
ATOM   7928 C CZ  . PHE A 1 1450 ? 155.576 140.095 161.325 1.00 52.15  ? 1450 PHE A CZ  1 
ATOM   7929 N N   . SER A 1 1451 ? 161.768 141.230 165.164 1.00 38.85  ? 1451 SER A N   1 
ATOM   7930 C CA  . SER A 1 1451 ? 163.023 140.886 165.823 1.00 41.58  ? 1451 SER A CA  1 
ATOM   7931 C C   . SER A 1 1451 ? 162.791 140.537 167.286 1.00 47.55  ? 1451 SER A C   1 
ATOM   7932 O O   . SER A 1 1451 ? 163.289 139.519 167.781 1.00 54.22  ? 1451 SER A O   1 
ATOM   7933 C CB  . SER A 1 1451 ? 164.013 142.041 165.695 1.00 51.50  ? 1451 SER A CB  1 
ATOM   7934 O OG  . SER A 1 1451 ? 165.178 141.793 166.458 1.00 56.55  ? 1451 SER A OG  1 
ATOM   7935 N N   . ILE A 1 1452 ? 162.010 141.359 167.989 1.00 41.74  ? 1452 ILE A N   1 
ATOM   7936 C CA  . ILE A 1 1452 ? 161.756 141.112 169.404 1.00 38.78  ? 1452 ILE A CA  1 
ATOM   7937 C C   . ILE A 1 1452 ? 160.991 139.810 169.595 1.00 52.00  ? 1452 ILE A C   1 
ATOM   7938 O O   . ILE A 1 1452 ? 161.335 138.996 170.460 1.00 59.79  ? 1452 ILE A O   1 
ATOM   7939 C CB  . ILE A 1 1452 ? 161.006 142.303 170.024 1.00 34.51  ? 1452 ILE A CB  1 
ATOM   7940 C CG1 . ILE A 1 1452 ? 161.937 143.505 170.150 1.00 45.50  ? 1452 ILE A CG1 1 
ATOM   7941 C CG2 . ILE A 1 1452 ? 160.431 141.926 171.369 1.00 37.95  ? 1452 ILE A CG2 1 
ATOM   7942 C CD1 . ILE A 1 1452 ? 161.269 144.722 170.731 1.00 51.57  ? 1452 ILE A CD1 1 
ATOM   7943 N N   . THR A 1 1453 ? 159.946 139.587 168.795 1.00 49.50  ? 1453 THR A N   1 
ATOM   7944 C CA  . THR A 1 1453 ? 159.146 138.379 168.962 1.00 42.45  ? 1453 THR A CA  1 
ATOM   7945 C C   . THR A 1 1453 ? 159.951 137.125 168.646 1.00 49.95  ? 1453 THR A C   1 
ATOM   7946 O O   . THR A 1 1453 ? 159.853 136.125 169.364 1.00 59.31  ? 1453 THR A O   1 
ATOM   7947 C CB  . THR A 1 1453 ? 157.899 138.443 168.087 1.00 40.86  ? 1453 THR A CB  1 
ATOM   7948 O OG1 . THR A 1 1453 ? 158.272 138.789 166.749 1.00 51.96  ? 1453 THR A OG1 1 
ATOM   7949 C CG2 . THR A 1 1453 ? 156.929 139.478 168.622 1.00 45.25  ? 1453 THR A CG2 1 
ATOM   7950 N N   . PHE A 1 1454 ? 160.754 137.153 167.582 1.00 41.74  ? 1454 PHE A N   1 
ATOM   7951 C CA  . PHE A 1 1454 ? 161.531 135.981 167.211 1.00 44.69  ? 1454 PHE A CA  1 
ATOM   7952 C C   . PHE A 1 1454 ? 162.758 135.782 168.084 1.00 47.94  ? 1454 PHE A C   1 
ATOM   7953 O O   . PHE A 1 1454 ? 163.327 134.688 168.077 1.00 59.21  ? 1454 PHE A O   1 
ATOM   7954 C CB  . PHE A 1 1454 ? 161.957 136.071 165.747 1.00 44.75  ? 1454 PHE A CB  1 
ATOM   7955 C CG  . PHE A 1 1454 ? 160.917 135.588 164.786 1.00 46.23  ? 1454 PHE A CG  1 
ATOM   7956 C CD1 . PHE A 1 1454 ? 159.865 136.403 164.418 1.00 45.16  ? 1454 PHE A CD1 1 
ATOM   7957 C CD2 . PHE A 1 1454 ? 160.988 134.315 164.256 1.00 48.11  ? 1454 PHE A CD2 1 
ATOM   7958 C CE1 . PHE A 1 1454 ? 158.907 135.958 163.537 1.00 44.09  ? 1454 PHE A CE1 1 
ATOM   7959 C CE2 . PHE A 1 1454 ? 160.034 133.865 163.374 1.00 52.05  ? 1454 PHE A CE2 1 
ATOM   7960 C CZ  . PHE A 1 1454 ? 158.992 134.688 163.015 1.00 50.94  ? 1454 PHE A CZ  1 
ATOM   7961 N N   . SER A 1 1455 ? 163.188 136.801 168.825 1.00 45.76  ? 1455 SER A N   1 
ATOM   7962 C CA  . SER A 1 1455 ? 164.326 136.635 169.714 1.00 48.95  ? 1455 SER A CA  1 
ATOM   7963 C C   . SER A 1 1455 ? 163.927 136.317 171.146 1.00 51.03  ? 1455 SER A C   1 
ATOM   7964 O O   . SER A 1 1455 ? 164.722 135.715 171.873 1.00 55.52  ? 1455 SER A O   1 
ATOM   7965 C CB  . SER A 1 1455 ? 165.191 137.896 169.703 1.00 53.91  ? 1455 SER A CB  1 
ATOM   7966 O OG  . SER A 1 1455 ? 165.728 138.128 168.414 1.00 63.10  ? 1455 SER A OG  1 
ATOM   7967 N N   . SER A 1 1456 ? 162.724 136.700 171.569 1.00 46.90  ? 1456 SER A N   1 
ATOM   7968 C CA  . SER A 1 1456 ? 162.302 136.486 172.943 1.00 45.66  ? 1456 SER A CA  1 
ATOM   7969 C C   . SER A 1 1456 ? 161.270 135.384 173.107 1.00 54.68  ? 1456 SER A C   1 
ATOM   7970 O O   . SER A 1 1456 ? 161.095 134.892 174.224 1.00 59.39  ? 1456 SER A O   1 
ATOM   7971 C CB  . SER A 1 1456 ? 161.733 137.784 173.532 1.00 48.96  ? 1456 SER A CB  1 
ATOM   7972 O OG  . SER A 1 1456 ? 162.691 138.823 173.480 1.00 58.48  ? 1456 SER A OG  1 
ATOM   7973 N N   . MET A 1 1457 ? 160.575 134.996 172.040 1.00 55.17  ? 1457 MET A N   1 
ATOM   7974 C CA  . MET A 1 1457 ? 159.547 133.967 172.135 1.00 50.96  ? 1457 MET A CA  1 
ATOM   7975 C C   . MET A 1 1457 ? 159.870 132.750 171.279 1.00 56.76  ? 1457 MET A C   1 
ATOM   7976 O O   . MET A 1 1457 ? 159.887 131.630 171.796 1.00 62.80  ? 1457 MET A O   1 
ATOM   7977 C CB  . MET A 1 1457 ? 158.187 134.562 171.749 1.00 50.96  ? 1457 MET A CB  1 
ATOM   7978 C CG  . MET A 1 1457 ? 157.006 133.668 172.068 1.00 59.64  ? 1457 MET A CG  1 
ATOM   7979 S SD  . MET A 1 1457 ? 155.431 134.509 171.837 1.00 78.50  ? 1457 MET A SD  1 
ATOM   7980 C CE  . MET A 1 1457 ? 155.617 135.882 172.970 1.00 55.65  ? 1457 MET A CE  1 
ATOM   7981 N N   . PHE A 1 1458 ? 160.132 132.931 169.984 1.00 43.72  ? 1458 PHE A N   1 
ATOM   7982 C CA  . PHE A 1 1458 ? 160.365 131.781 169.117 1.00 37.17  ? 1458 PHE A CA  1 
ATOM   7983 C C   . PHE A 1 1458 ? 161.745 131.178 169.343 1.00 46.41  ? 1458 PHE A C   1 
ATOM   7984 O O   . PHE A 1 1458 ? 161.890 129.951 169.399 1.00 60.68  ? 1458 PHE A O   1 
ATOM   7985 C CB  . PHE A 1 1458 ? 160.191 132.184 167.656 1.00 41.79  ? 1458 PHE A CB  1 
ATOM   7986 C CG  . PHE A 1 1458 ? 160.275 131.036 166.698 1.00 47.80  ? 1458 PHE A CG  1 
ATOM   7987 C CD1 . PHE A 1 1458 ? 159.212 130.168 166.547 1.00 48.00  ? 1458 PHE A CD1 1 
ATOM   7988 C CD2 . PHE A 1 1458 ? 161.414 130.830 165.942 1.00 51.09  ? 1458 PHE A CD2 1 
ATOM   7989 C CE1 . PHE A 1 1458 ? 159.283 129.113 165.667 1.00 45.80  ? 1458 PHE A CE1 1 
ATOM   7990 C CE2 . PHE A 1 1458 ? 161.490 129.776 165.060 1.00 54.88  ? 1458 PHE A CE2 1 
ATOM   7991 C CZ  . PHE A 1 1458 ? 160.422 128.917 164.922 1.00 52.35  ? 1458 PHE A CZ  1 
ATOM   7992 N N   . LEU A 1 1459 ? 162.769 132.019 169.462 1.00 44.56  ? 1459 LEU A N   1 
ATOM   7993 C CA  . LEU A 1 1459 ? 164.128 131.509 169.637 1.00 39.08  ? 1459 LEU A CA  1 
ATOM   7994 C C   . LEU A 1 1459 ? 164.308 130.709 170.920 1.00 44.01  ? 1459 LEU A C   1 
ATOM   7995 O O   . LEU A 1 1459 ? 164.962 129.655 170.868 1.00 48.24  ? 1459 LEU A O   1 
ATOM   7996 C CB  . LEU A 1 1459 ? 165.130 132.663 169.558 1.00 39.18  ? 1459 LEU A CB  1 
ATOM   7997 C CG  . LEU A 1 1459 ? 166.605 132.270 169.590 1.00 40.87  ? 1459 LEU A CG  1 
ATOM   7998 C CD1 . LEU A 1 1459 ? 166.885 131.187 168.572 1.00 33.58  ? 1459 LEU A CD1 1 
ATOM   7999 C CD2 . LEU A 1 1459 ? 167.473 133.480 169.322 1.00 44.62  ? 1459 LEU A CD2 1 
ATOM   8000 N N   . PRO A 1 1460 ? 163.825 131.147 172.090 1.00 48.56  ? 1460 PRO A N   1 
ATOM   8001 C CA  . PRO A 1 1460 ? 163.987 130.296 173.281 1.00 46.26  ? 1460 PRO A CA  1 
ATOM   8002 C C   . PRO A 1 1460 ? 163.314 128.942 173.151 1.00 48.32  ? 1460 PRO A C   1 
ATOM   8003 O O   . PRO A 1 1460 ? 163.878 127.935 173.591 1.00 56.37  ? 1460 PRO A O   1 
ATOM   8004 C CB  . PRO A 1 1460 ? 163.367 131.141 174.402 1.00 43.33  ? 1460 PRO A CB  1 
ATOM   8005 C CG  . PRO A 1 1460 ? 162.489 132.104 173.711 1.00 46.57  ? 1460 PRO A CG  1 
ATOM   8006 C CD  . PRO A 1 1460 ? 163.182 132.424 172.436 1.00 51.70  ? 1460 PRO A CD  1 
ATOM   8007 N N   . VAL A 1 1461 ? 162.132 128.882 172.538 1.00 44.78  ? 1461 VAL A N   1 
ATOM   8008 C CA  . VAL A 1 1461 ? 161.467 127.597 172.347 1.00 42.25  ? 1461 VAL A CA  1 
ATOM   8009 C C   . VAL A 1 1461 ? 162.261 126.725 171.386 1.00 47.53  ? 1461 VAL A C   1 
ATOM   8010 O O   . VAL A 1 1461 ? 162.430 125.519 171.611 1.00 57.17  ? 1461 VAL A O   1 
ATOM   8011 C CB  . VAL A 1 1461 ? 160.025 127.811 171.859 1.00 41.84  ? 1461 VAL A CB  1 
ATOM   8012 C CG1 . VAL A 1 1461 ? 159.357 126.479 171.593 1.00 49.90  ? 1461 VAL A CG1 1 
ATOM   8013 C CG2 . VAL A 1 1461 ? 159.239 128.603 172.882 1.00 42.26  ? 1461 VAL A CG2 1 
ATOM   8014 N N   . LEU A 1 1462 ? 162.762 127.317 170.302 1.00 43.22  ? 1462 LEU A N   1 
ATOM   8015 C CA  . LEU A 1 1462 ? 163.552 126.551 169.346 1.00 45.04  ? 1462 LEU A CA  1 
ATOM   8016 C C   . LEU A 1 1462 ? 164.825 126.017 169.988 1.00 48.15  ? 1462 LEU A C   1 
ATOM   8017 O O   . LEU A 1 1462 ? 165.240 124.888 169.711 1.00 55.28  ? 1462 LEU A O   1 
ATOM   8018 C CB  . LEU A 1 1462 ? 163.880 127.415 168.132 1.00 49.90  ? 1462 LEU A CB  1 
ATOM   8019 C CG  . LEU A 1 1462 ? 164.581 126.704 166.978 1.00 53.59  ? 1462 LEU A CG  1 
ATOM   8020 C CD1 . LEU A 1 1462 ? 163.729 125.553 166.482 1.00 56.45  ? 1462 LEU A CD1 1 
ATOM   8021 C CD2 . LEU A 1 1462 ? 164.872 127.679 165.854 1.00 47.75  ? 1462 LEU A CD2 1 
ATOM   8022 N N   . LEU A 1 1463 ? 165.464 126.818 170.841 1.00 51.44  ? 1463 LEU A N   1 
ATOM   8023 C CA  . LEU A 1 1463 ? 166.667 126.359 171.529 1.00 46.69  ? 1463 LEU A CA  1 
ATOM   8024 C C   . LEU A 1 1463 ? 166.341 125.276 172.548 1.00 50.38  ? 1463 LEU A C   1 
ATOM   8025 O O   . LEU A 1 1463 ? 167.120 124.336 172.733 1.00 61.41  ? 1463 LEU A O   1 
ATOM   8026 C CB  . LEU A 1 1463 ? 167.369 127.536 172.200 1.00 46.64  ? 1463 LEU A CB  1 
ATOM   8027 C CG  . LEU A 1 1463 ? 167.952 128.580 171.250 1.00 48.54  ? 1463 LEU A CG  1 
ATOM   8028 C CD1 . LEU A 1 1463 ? 168.546 129.732 172.030 1.00 51.24  ? 1463 LEU A CD1 1 
ATOM   8029 C CD2 . LEU A 1 1463 ? 168.993 127.953 170.346 1.00 45.65  ? 1463 LEU A CD2 1 
ATOM   8030 N N   . SER A 1 1464 ? 165.202 125.395 173.228 1.00 56.17  ? 1464 SER A N   1 
ATOM   8031 C CA  . SER A 1 1464 ? 164.792 124.350 174.158 1.00 59.21  ? 1464 SER A CA  1 
ATOM   8032 C C   . SER A 1 1464 ? 164.540 123.039 173.428 1.00 60.66  ? 1464 SER A C   1 
ATOM   8033 O O   . SER A 1 1464 ? 164.835 121.959 173.952 1.00 64.75  ? 1464 SER A O   1 
ATOM   8034 C CB  . SER A 1 1464 ? 163.543 124.791 174.920 1.00 63.18  ? 1464 SER A CB  1 
ATOM   8035 O OG  . SER A 1 1464 ? 163.092 123.773 175.795 1.00 67.72  ? 1464 SER A OG  1 
ATOM   8036 N N   . SER A 1 1465 ? 163.996 123.114 172.214 1.00 59.61  ? 1465 SER A N   1 
ATOM   8037 C CA  . SER A 1 1465 ? 163.658 121.897 171.483 1.00 56.35  ? 1465 SER A CA  1 
ATOM   8038 C C   . SER A 1 1465 ? 164.888 121.271 170.832 1.00 62.79  ? 1465 SER A C   1 
ATOM   8039 O O   . SER A 1 1465 ? 165.164 120.083 171.026 1.00 64.74  ? 1465 SER A O   1 
ATOM   8040 C CB  . SER A 1 1465 ? 162.587 122.200 170.437 1.00 56.24  ? 1465 SER A CB  1 
ATOM   8041 O OG  . SER A 1 1465 ? 162.966 123.300 169.631 1.00 65.93  ? 1465 SER A OG  1 
ATOM   8042 N N   . PHE A 1 1466 ? 165.643 122.054 170.056 1.00 62.89  ? 1466 PHE A N   1 
ATOM   8043 C CA  . PHE A 1 1466 ? 166.739 121.518 169.257 1.00 59.10  ? 1466 PHE A CA  1 
ATOM   8044 C C   . PHE A 1 1466 ? 168.067 122.230 169.487 1.00 59.38  ? 1466 PHE A C   1 
ATOM   8045 O O   . PHE A 1 1466 ? 168.941 122.170 168.616 1.00 61.98  ? 1466 PHE A O   1 
ATOM   8046 C CB  . PHE A 1 1466 ? 166.399 121.578 167.763 1.00 56.75  ? 1466 PHE A CB  1 
ATOM   8047 C CG  . PHE A 1 1466 ? 165.025 121.083 167.430 1.00 57.79  ? 1466 PHE A CG  1 
ATOM   8048 C CD1 . PHE A 1 1466 ? 164.719 119.737 167.513 1.00 63.94  ? 1466 PHE A CD1 1 
ATOM   8049 C CD2 . PHE A 1 1466 ? 164.043 121.963 167.015 1.00 55.99  ? 1466 PHE A CD2 1 
ATOM   8050 C CE1 . PHE A 1 1466 ? 163.453 119.280 167.199 1.00 64.65  ? 1466 PHE A CE1 1 
ATOM   8051 C CE2 . PHE A 1 1466 ? 162.778 121.514 166.700 1.00 62.43  ? 1466 PHE A CE2 1 
ATOM   8052 C CZ  . PHE A 1 1466 ? 162.482 120.171 166.792 1.00 63.62  ? 1466 PHE A CZ  1 
ATOM   8053 N N   . GLY A 1 1467 ? 168.245 122.906 170.616 1.00 64.05  ? 1467 GLY A N   1 
ATOM   8054 C CA  . GLY A 1 1467 ? 169.469 123.626 170.876 1.00 65.94  ? 1467 GLY A CA  1 
ATOM   8055 C C   . GLY A 1 1467 ? 170.654 122.715 171.118 1.00 65.64  ? 1467 GLY A C   1 
ATOM   8056 O O   . GLY A 1 1467 ? 170.509 121.551 171.502 1.00 72.57  ? 1467 GLY A O   1 
ATOM   8057 N N   . PRO A 1 1468 ? 171.858 123.234 170.887 1.00 69.36  ? 1468 PRO A N   1 
ATOM   8058 C CA  . PRO A 1 1468 ? 173.063 122.439 171.140 1.00 76.43  ? 1468 PRO A CA  1 
ATOM   8059 C C   . PRO A 1 1468 ? 173.263 122.181 172.626 1.00 82.18  ? 1468 PRO A C   1 
ATOM   8060 O O   . PRO A 1 1468 ? 172.850 122.970 173.477 1.00 86.13  ? 1468 PRO A O   1 
ATOM   8061 C CB  . PRO A 1 1468 ? 174.186 123.309 170.567 1.00 75.70  ? 1468 PRO A CB  1 
ATOM   8062 C CG  . PRO A 1 1468 ? 173.651 124.695 170.645 1.00 73.49  ? 1468 PRO A CG  1 
ATOM   8063 C CD  . PRO A 1 1468 ? 172.177 124.582 170.393 1.00 72.44  ? 1468 PRO A CD  1 
ATOM   8064 N N   . LEU A 1 1469 ? 173.911 121.055 172.931 1.00 89.36  ? 1469 LEU A N   1 
ATOM   8065 C CA  . LEU A 1 1469 ? 174.207 120.682 174.307 1.00 87.38  ? 1469 LEU A CA  1 
ATOM   8066 C C   . LEU A 1 1469 ? 175.690 120.675 174.642 1.00 90.83  ? 1469 LEU A C   1 
ATOM   8067 O O   . LEU A 1 1469 ? 176.040 120.870 175.810 1.00 89.96  ? 1469 LEU A O   1 
ATOM   8068 C CB  . LEU A 1 1469 ? 173.627 119.296 174.621 1.00 86.25  ? 1469 LEU A CB  1 
ATOM   8069 C CG  . LEU A 1 1469 ? 172.131 119.268 174.918 1.00 89.66  ? 1469 LEU A CG  1 
ATOM   8070 C CD1 . LEU A 1 1469 ? 171.650 117.841 175.102 1.00 89.83  ? 1469 LEU A CD1 1 
ATOM   8071 C CD2 . LEU A 1 1469 ? 171.836 120.096 176.155 1.00 87.30  ? 1469 LEU A CD2 1 
ATOM   8072 N N   . HIS A 1 1470 ? 176.562 120.454 173.665 1.00 106.60 ? 1470 HIS A N   1 
ATOM   8073 C CA  . HIS A 1 1470 ? 178.000 120.444 173.907 1.00 105.91 ? 1470 HIS A CA  1 
ATOM   8074 C C   . HIS A 1 1470 ? 178.761 120.938 172.683 1.00 108.56 ? 1470 HIS A C   1 
ATOM   8075 O O   . HIS A 1 1470 ? 178.213 121.012 171.584 1.00 110.10 ? 1470 HIS A O   1 
ATOM   8076 C CB  . HIS A 1 1470 ? 178.479 119.041 174.286 1.00 106.46 ? 1470 HIS A CB  1 
ATOM   8077 C CG  . HIS A 1 1470 ? 178.155 118.649 175.694 1.00 106.93 ? 1470 HIS A CG  1 
ATOM   8078 N ND1 . HIS A 1 1470 ? 176.911 118.196 176.074 1.00 109.40 ? 1470 HIS A ND1 1 
ATOM   8079 C CD2 . HIS A 1 1470 ? 178.916 118.642 176.814 1.00 105.68 ? 1470 HIS A CD2 1 
ATOM   8080 C CE1 . HIS A 1 1470 ? 176.919 117.928 177.368 1.00 107.56 ? 1470 HIS A CE1 1 
ATOM   8081 N NE2 . HIS A 1 1470 ? 178.124 118.190 177.840 1.00 106.20 ? 1470 HIS A NE2 1 
ATOM   8082 O OXT . HIS A 1 1470 ? 179.942 121.271 172.765 1.00 107.84 ? 1470 HIS A OXT 1 
HETATM 8083 C C1  . NAG B 2 .    ? 166.904 174.822 93.079  1.00 112.21 ? 1501 NAG A C1  1 
HETATM 8084 C C2  . NAG B 2 .    ? 165.972 175.385 92.009  1.00 111.65 ? 1501 NAG A C2  1 
HETATM 8085 C C3  . NAG B 2 .    ? 166.372 174.861 90.634  1.00 112.67 ? 1501 NAG A C3  1 
HETATM 8086 C C4  . NAG B 2 .    ? 167.844 175.142 90.365  1.00 111.28 ? 1501 NAG A C4  1 
HETATM 8087 C C5  . NAG B 2 .    ? 168.704 174.601 91.503  1.00 110.72 ? 1501 NAG A C5  1 
HETATM 8088 C C6  . NAG B 2 .    ? 170.162 174.969 91.363  1.00 110.39 ? 1501 NAG A C6  1 
HETATM 8089 C C7  . NAG B 2 .    ? 163.662 175.975 92.587  1.00 110.46 ? 1501 NAG A C7  1 
HETATM 8090 C C8  . NAG B 2 .    ? 162.282 175.457 92.858  1.00 108.86 ? 1501 NAG A C8  1 
HETATM 8091 N N2  . NAG B 2 .    ? 164.586 175.054 92.298  1.00 109.56 ? 1501 NAG A N2  1 
HETATM 8092 O O3  . NAG B 2 .    ? 165.568 175.486 89.640  1.00 111.64 ? 1501 NAG A O3  1 
HETATM 8093 O O4  . NAG B 2 .    ? 168.242 174.525 89.146  1.00 109.31 ? 1501 NAG A O4  1 
HETATM 8094 O O5  . NAG B 2 .    ? 168.260 175.146 92.754  1.00 112.46 ? 1501 NAG A O5  1 
HETATM 8095 O O6  . NAG B 2 .    ? 170.320 176.342 91.033  1.00 112.61 ? 1501 NAG A O6  1 
HETATM 8096 O O7  . NAG B 2 .    ? 163.927 177.172 92.628  1.00 112.04 ? 1501 NAG A O7  1 
HETATM 8097 C C1  . CLR C 3 .    ? 149.778 170.230 122.567 1.00 20.00  ? 1502 CLR A C1  1 
HETATM 8098 C C2  . CLR C 3 .    ? 150.787 170.788 123.564 1.00 20.00  ? 1502 CLR A C2  1 
HETATM 8099 C C3  . CLR C 3 .    ? 151.999 171.350 122.849 1.00 20.00  ? 1502 CLR A C3  1 
HETATM 8100 C C4  . CLR C 3 .    ? 151.559 172.420 121.856 1.00 20.00  ? 1502 CLR A C4  1 
HETATM 8101 C C5  . CLR C 3 .    ? 150.502 171.914 120.910 1.00 20.00  ? 1502 CLR A C5  1 
HETATM 8102 C C6  . CLR C 3 .    ? 150.669 172.038 119.597 1.00 20.00  ? 1502 CLR A C6  1 
HETATM 8103 C C7  . CLR C 3 .    ? 149.653 171.670 118.571 1.00 20.00  ? 1502 CLR A C7  1 
HETATM 8104 C C8  . CLR C 3 .    ? 148.289 171.369 119.178 1.00 20.00  ? 1502 CLR A C8  1 
HETATM 8105 C C9  . CLR C 3 .    ? 148.453 170.525 120.447 1.00 20.00  ? 1502 CLR A C9  1 
HETATM 8106 C C10 . CLR C 3 .    ? 149.282 171.259 121.532 1.00 20.00  ? 1502 CLR A C10 1 
HETATM 8107 C C11 . CLR C 3 .    ? 147.099 170.007 120.948 1.00 20.00  ? 1502 CLR A C11 1 
HETATM 8108 C C12 . CLR C 3 .    ? 146.243 169.335 119.870 1.00 20.00  ? 1502 CLR A C12 1 
HETATM 8109 C C13 . CLR C 3 .    ? 146.024 170.257 118.670 1.00 20.00  ? 1502 CLR A C13 1 
HETATM 8110 C C14 . CLR C 3 .    ? 147.431 170.620 118.177 1.00 20.00  ? 1502 CLR A C14 1 
HETATM 8111 C C15 . CLR C 3 .    ? 147.195 171.258 116.821 1.00 20.00  ? 1502 CLR A C15 1 
HETATM 8112 C C16 . CLR C 3 .    ? 146.134 170.328 116.213 1.00 20.00  ? 1502 CLR A C16 1 
HETATM 8113 C C17 . CLR C 3 .    ? 145.404 169.626 117.392 1.00 20.00  ? 1502 CLR A C17 1 
HETATM 8114 C C18 . CLR C 3 .    ? 145.232 171.498 119.084 1.00 20.00  ? 1502 CLR A C18 1 
HETATM 8115 C C19 . CLR C 3 .    ? 148.457 172.343 122.240 1.00 20.00  ? 1502 CLR A C19 1 
HETATM 8116 C C20 . CLR C 3 .    ? 143.880 169.651 117.195 1.00 20.00  ? 1502 CLR A C20 1 
HETATM 8117 C C21 . CLR C 3 .    ? 143.141 168.630 118.054 1.00 20.00  ? 1502 CLR A C21 1 
HETATM 8118 C C22 . CLR C 3 .    ? 143.536 169.441 115.712 1.00 20.00  ? 1502 CLR A C22 1 
HETATM 8119 C C23 . CLR C 3 .    ? 142.719 170.549 115.056 1.00 20.00  ? 1502 CLR A C23 1 
HETATM 8120 C C24 . CLR C 3 .    ? 142.517 170.309 113.565 1.00 20.00  ? 1502 CLR A C24 1 
HETATM 8121 C C25 . CLR C 3 .    ? 141.061 170.151 113.124 1.00 20.00  ? 1502 CLR A C25 1 
HETATM 8122 C C26 . CLR C 3 .    ? 140.292 171.449 113.348 1.00 20.00  ? 1502 CLR A C26 1 
HETATM 8123 C C27 . CLR C 3 .    ? 140.944 169.715 111.667 1.00 20.00  ? 1502 CLR A C27 1 
HETATM 8124 O O1  . CLR C 3 .    ? 152.894 171.866 123.813 1.00 20.00  ? 1502 CLR A O1  1 
HETATM 8125 C C10 . Y6F D 4 .    ? 161.858 161.289 154.208 1.00 67.97  ? 1503 Y6F A C10 1 
HETATM 8126 C C12 . Y6F D 4 .    ? 162.989 159.099 154.948 1.00 59.04  ? 1503 Y6F A C12 1 
HETATM 8127 C C13 . Y6F D 4 .    ? 163.502 158.448 156.055 1.00 61.78  ? 1503 Y6F A C13 1 
HETATM 8128 C C14 . Y6F D 4 .    ? 164.411 157.413 155.900 1.00 66.08  ? 1503 Y6F A C14 1 
HETATM 8129 C C16 . Y6F D 4 .    ? 165.810 155.881 154.465 1.00 63.86  ? 1503 Y6F A C16 1 
HETATM 8130 C C17 . Y6F D 4 .    ? 164.297 157.667 153.524 1.00 68.05  ? 1503 Y6F A C17 1 
HETATM 8131 C C18 . Y6F D 4 .    ? 164.731 157.244 152.123 1.00 65.01  ? 1503 Y6F A C18 1 
HETATM 8132 C C19 . Y6F D 4 .    ? 163.387 158.700 153.682 1.00 63.67  ? 1503 Y6F A C19 1 
HETATM 8133 C C21 . Y6F D 4 .    ? 162.969 162.002 150.022 1.00 64.61  ? 1503 Y6F A C21 1 
HETATM 8134 C C22 . Y6F D 4 .    ? 163.355 162.309 148.729 1.00 62.64  ? 1503 Y6F A C22 1 
HETATM 8135 C C24 . Y6F D 4 .    ? 162.009 164.809 144.620 1.00 65.29  ? 1503 Y6F A C24 1 
HETATM 8136 C C03 . Y6F D 4 .    ? 163.205 163.601 148.259 1.00 59.44  ? 1503 Y6F A C03 1 
HETATM 8137 C C04 . Y6F D 4 .    ? 162.674 164.587 149.072 1.00 61.74  ? 1503 Y6F A C04 1 
HETATM 8138 C C05 . Y6F D 4 .    ? 162.288 164.280 150.369 1.00 65.97  ? 1503 Y6F A C05 1 
HETATM 8139 C C06 . Y6F D 4 .    ? 162.434 162.985 150.837 1.00 64.29  ? 1503 Y6F A C06 1 
HETATM 8140 C C07 . Y6F D 4 .    ? 162.014 162.618 152.261 1.00 59.20  ? 1503 Y6F A C07 1 
HETATM 8141 C C08 . Y6F D 4 .    ? 161.208 163.404 153.124 1.00 62.60  ? 1503 Y6F A C08 1 
HETATM 8142 C C15 . Y6F D 4 .    ? 164.808 157.022 154.634 1.00 65.01  ? 1503 Y6F A C15 1 
HETATM 8143 C C25 . Y6F D 4 .    ? 160.495 164.789 144.420 1.00 67.51  ? 1503 Y6F A C25 1 
HETATM 8144 C C26 . Y6F D 4 .    ? 162.203 162.354 145.017 1.00 64.94  ? 1503 Y6F A C26 1 
HETATM 8145 C C27 . Y6F D 4 .    ? 161.231 161.624 145.941 1.00 61.94  ? 1503 Y6F A C27 1 
HETATM 8146 N N11 . Y6F D 4 .    ? 162.030 160.183 155.146 1.00 66.24  ? 1503 Y6F A N11 1 
HETATM 8147 N N20 . Y6F D 4 .    ? 162.384 161.361 152.921 1.00 62.21  ? 1503 Y6F A N20 1 
HETATM 8148 N N23 . Y6F D 4 .    ? 162.429 163.712 145.474 1.00 67.32  ? 1503 Y6F A N23 1 
HETATM 8149 O O01 . Y6F D 4 .    ? 164.900 163.229 146.182 1.00 71.62  ? 1503 Y6F A O01 1 
HETATM 8150 O O28 . Y6F D 4 .    ? 164.209 165.366 146.459 1.00 76.71  ? 1503 Y6F A O28 1 
HETATM 8151 S S02 . Y6F D 4 .    ? 163.714 163.994 146.561 1.00 82.31  ? 1503 Y6F A S02 1 
HETATM 8152 S S09 . Y6F D 4 .    ? 161.005 162.634 154.514 1.00 71.58  ? 1503 Y6F A S09 1 
HETATM 8153 C C1  . NAG E 2 .    ? 190.128 167.541 109.713 1.00 30.00  ? 1504 NAG A C1  1 
HETATM 8154 C C2  . NAG E 2 .    ? 189.998 166.158 110.392 1.00 30.00  ? 1504 NAG A C2  1 
HETATM 8155 C C3  . NAG E 2 .    ? 189.201 165.180 109.520 1.00 30.00  ? 1504 NAG A C3  1 
HETATM 8156 C C4  . NAG E 2 .    ? 189.220 165.598 108.057 1.00 30.00  ? 1504 NAG A C4  1 
HETATM 8157 C C5  . NAG E 2 .    ? 190.590 166.161 107.710 1.00 30.00  ? 1504 NAG A C5  1 
HETATM 8158 C C6  . NAG E 2 .    ? 190.755 166.455 106.236 1.00 30.00  ? 1504 NAG A C6  1 
HETATM 8159 C C7  . NAG E 2 .    ? 191.592 165.055 111.907 1.00 30.00  ? 1504 NAG A C7  1 
HETATM 8160 C C8  . NAG E 2 .    ? 190.478 165.023 112.911 1.00 30.00  ? 1504 NAG A C8  1 
HETATM 8161 N N2  . NAG E 2 .    ? 191.303 165.607 110.724 1.00 30.00  ? 1504 NAG A N2  1 
HETATM 8162 O O3  . NAG E 2 .    ? 187.859 165.115 109.989 1.00 30.00  ? 1504 NAG A O3  1 
HETATM 8163 O O4  . NAG E 2 .    ? 188.945 164.477 107.225 1.00 30.00  ? 1504 NAG A O4  1 
HETATM 8164 O O5  . NAG E 2 .    ? 190.792 167.401 108.404 1.00 30.00  ? 1504 NAG A O5  1 
HETATM 8165 O O6  . NAG E 2 .    ? 189.661 167.206 105.728 1.00 30.00  ? 1504 NAG A O6  1 
HETATM 8166 O O7  . NAG E 2 .    ? 192.704 164.599 112.157 1.00 30.00  ? 1504 NAG A O7  1 
# 
