data_2PN5
# 
_entry.id   2PN5 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.287 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   2PN5         
RCSB  RCSB042562   
WWPDB D_1000042562 
# 
_pdbx_database_status.entry_id                        2PN5 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.recvd_initial_deposition_date   2007-04-23 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
# 
_audit_author.name           'Baxter, R.H.G.' 
_audit_author.pdbx_ordinal   1 
# 
_citation.id                        primary 
_citation.title                     
'Structural basis for conserved complement factor-like function in the antimalarial protein TEP1' 
_citation.journal_abbrev            Proc.Natl.Acad.Sci.Usa 
_citation.journal_volume            104 
_citation.page_first                11615 
_citation.page_last                 11620 
_citation.year                      2007 
_citation.journal_id_ASTM           PNASA6 
_citation.country                   US 
_citation.journal_id_ISSN           0027-8424 
_citation.journal_id_CSD            0040 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   17606907 
_citation.pdbx_database_id_DOI      10.1073/pnas.0704967104 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Baxter, R.H.G.'  1 
primary 'Chang, C.I.'     2 
primary 'Chelliah, Y.'    3 
primary 'Blandin, S.'     4 
primary 'Levashina, E.A.' 5 
primary 'Deisenhofer, J.' 6 
# 
_cell.entry_id           2PN5 
_cell.length_a           150.515 
_cell.length_b           150.515 
_cell.length_c           226.315 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         2PN5 
_symmetry.space_group_name_H-M             'P 43 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                96 
_symmetry.space_group_name_Hall            ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Thioester-containing protein I' 150532.516 1   ? ? 'residues 22-1338' ? 
2 non-polymer man N-ACETYL-D-GLUCOSAMINE           221.208    5   ? ? ?                  ? 
3 non-polymer syn 'SODIUM ION'                     22.990     3   ? ? ?                  ? 
4 water       nat water                            18.015     140 ? ? ?                  ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        TEP1r 
# 
_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       
;LLVVGPKFIRANQEYTLVISNFNSQLSKVDLLLKLEGETDNGLSVLNVTKMVDVRRNMNRMINFNMPEDLTAGNYKITID
GQRGFSFHKEAELVYLSKSISGLIQVDKPVFKPGDTVNFRVIVLDTELKPPARVKSVYVTIRDPQRNVIRKWSTAKLYAG
VFESDLQIAPTPMLGVWNISVEVEGEELVSKTFEVKEYVLSTFDVQVMPSVIPLEEHQAVNLTIEANYHFGKPVQGVAKV
ELYLDDDKLKLKKELTVYGKGQVELRFDNFAMDADQQDVPVKVSFVEQYTNRTVVKQSQITVYRYAYRVELIKESPQFRP
GLPFKCALQFTHHDGTPAKGISGKVEVSDVRFETTTTSDNDGLIKLELQPSEGTEQLSIHFNAVDGFFFYEDVNKVETVT
DAYIKLELKSPIKRNKLMRFMVTCTERMTFFVYYVMSKGNIIDAGFMRPNKQPKYLLQLNATEKMIPRAKILIATVAGRT
VVYDFADLAFQELRNNFDLSIDEQEIKPGRQIELSMSGRPGAYVGLAAYDKALLLFNKNHDLFWEDIGQVFDGFHAINEN
EFDIFHSLGLFARTLDDILFDSANEKTGRNALQSGKPIGKLVSYRTNFQESWLWKNVSIGRSGSRKLIEVVPDTTTSWYL
TGFSIDPVYGLGIIKKPIQFTTVQPFYIVENLPYSIKRGEAVVLQFTLFNNLGAEYIADVTLYNVANQTEFVGRPNTDLS
YTKSVSVPPKVGVPISFLIKARKLGEMAVRVKASIMLGHETDALEKVIRVMPESLVQPRMDTRFFCFDDHKNQTFPINLD
INKKADSGSTKIEFRLNPNLLTTVIKNLDHLLGVPTGCGEQNMVKFVPNILVLDYLHAIGSKEQHLIDKATNLLRQGYQN
QMRYRQTDGSFGLWETTNGSVFLTAFVGTSMQTAVKYISDIDAAMVEKALDWLASKQHFSGRFDKAGAEYHKEMQGGLRN
GVALTSYVLMALLENDIAKAKHAEVIQKGMTYLSNQFGSINNAYDLSIATYAMMLNGHTMKEEALNKLIDMSFIDADKNE
RFWNTTNPIETTAYALLSFVMAEKYTDGIPVMNWLVNQRYVTGSFPSTQDTFVGLKALTKMAEKISPSRNDYTVQLKYKK
SAKYFKINSEQIDVENFVDIPEDTKKLEINVGGIGFGLLEVVYQFNLNLVNFENRFQLDLEKQNTGSDYELRLKVCASYI
PQLTDRRSNMALIEVTLPSGYVVDRNPISEQTKVNPIQKTEIRYGGTSVVLYYDNMGSERNCFTLTAYRRFKVALKRPAY
VVVYDYYNTNLNAIKVYEVDKQNLCEICDEEDCPAECGGHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;LLVVGPKFIRANQEYTLVISNFNSQLSKVDLLLKLEGETDNGLSVLNVTKMVDVRRNMNRMINFNMPEDLTAGNYKITID
GQRGFSFHKEAELVYLSKSISGLIQVDKPVFKPGDTVNFRVIVLDTELKPPARVKSVYVTIRDPQRNVIRKWSTAKLYAG
VFESDLQIAPTPMLGVWNISVEVEGEELVSKTFEVKEYVLSTFDVQVMPSVIPLEEHQAVNLTIEANYHFGKPVQGVAKV
ELYLDDDKLKLKKELTVYGKGQVELRFDNFAMDADQQDVPVKVSFVEQYTNRTVVKQSQITVYRYAYRVELIKESPQFRP
GLPFKCALQFTHHDGTPAKGISGKVEVSDVRFETTTTSDNDGLIKLELQPSEGTEQLSIHFNAVDGFFFYEDVNKVETVT
DAYIKLELKSPIKRNKLMRFMVTCTERMTFFVYYVMSKGNIIDAGFMRPNKQPKYLLQLNATEKMIPRAKILIATVAGRT
VVYDFADLAFQELRNNFDLSIDEQEIKPGRQIELSMSGRPGAYVGLAAYDKALLLFNKNHDLFWEDIGQVFDGFHAINEN
EFDIFHSLGLFARTLDDILFDSANEKTGRNALQSGKPIGKLVSYRTNFQESWLWKNVSIGRSGSRKLIEVVPDTTTSWYL
TGFSIDPVYGLGIIKKPIQFTTVQPFYIVENLPYSIKRGEAVVLQFTLFNNLGAEYIADVTLYNVANQTEFVGRPNTDLS
YTKSVSVPPKVGVPISFLIKARKLGEMAVRVKASIMLGHETDALEKVIRVMPESLVQPRMDTRFFCFDDHKNQTFPINLD
INKKADSGSTKIEFRLNPNLLTTVIKNLDHLLGVPTGCGEQNMVKFVPNILVLDYLHAIGSKEQHLIDKATNLLRQGYQN
QMRYRQTDGSFGLWETTNGSVFLTAFVGTSMQTAVKYISDIDAAMVEKALDWLASKQHFSGRFDKAGAEYHKEMQGGLRN
GVALTSYVLMALLENDIAKAKHAEVIQKGMTYLSNQFGSINNAYDLSIATYAMMLNGHTMKEEALNKLIDMSFIDADKNE
RFWNTTNPIETTAYALLSFVMAEKYTDGIPVMNWLVNQRYVTGSFPSTQDTFVGLKALTKMAEKISPSRNDYTVQLKYKK
SAKYFKINSEQIDVENFVDIPEDTKKLEINVGGIGFGLLEVVYQFNLNLVNFENRFQLDLEKQNTGSDYELRLKVCASYI
PQLTDRRSNMALIEVTLPSGYVVDRNPISEQTKVNPIQKTEIRYGGTSVVLYYDNMGSERNCFTLTAYRRFKVALKRPAY
VVVYDYYNTNLNAIKVYEVDKQNLCEICDEEDCPAECGGHHHHHH
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1    LEU n 
1 2    LEU n 
1 3    VAL n 
1 4    VAL n 
1 5    GLY n 
1 6    PRO n 
1 7    LYS n 
1 8    PHE n 
1 9    ILE n 
1 10   ARG n 
1 11   ALA n 
1 12   ASN n 
1 13   GLN n 
1 14   GLU n 
1 15   TYR n 
1 16   THR n 
1 17   LEU n 
1 18   VAL n 
1 19   ILE n 
1 20   SER n 
1 21   ASN n 
1 22   PHE n 
1 23   ASN n 
1 24   SER n 
1 25   GLN n 
1 26   LEU n 
1 27   SER n 
1 28   LYS n 
1 29   VAL n 
1 30   ASP n 
1 31   LEU n 
1 32   LEU n 
1 33   LEU n 
1 34   LYS n 
1 35   LEU n 
1 36   GLU n 
1 37   GLY n 
1 38   GLU n 
1 39   THR n 
1 40   ASP n 
1 41   ASN n 
1 42   GLY n 
1 43   LEU n 
1 44   SER n 
1 45   VAL n 
1 46   LEU n 
1 47   ASN n 
1 48   VAL n 
1 49   THR n 
1 50   LYS n 
1 51   MET n 
1 52   VAL n 
1 53   ASP n 
1 54   VAL n 
1 55   ARG n 
1 56   ARG n 
1 57   ASN n 
1 58   MET n 
1 59   ASN n 
1 60   ARG n 
1 61   MET n 
1 62   ILE n 
1 63   ASN n 
1 64   PHE n 
1 65   ASN n 
1 66   MET n 
1 67   PRO n 
1 68   GLU n 
1 69   ASP n 
1 70   LEU n 
1 71   THR n 
1 72   ALA n 
1 73   GLY n 
1 74   ASN n 
1 75   TYR n 
1 76   LYS n 
1 77   ILE n 
1 78   THR n 
1 79   ILE n 
1 80   ASP n 
1 81   GLY n 
1 82   GLN n 
1 83   ARG n 
1 84   GLY n 
1 85   PHE n 
1 86   SER n 
1 87   PHE n 
1 88   HIS n 
1 89   LYS n 
1 90   GLU n 
1 91   ALA n 
1 92   GLU n 
1 93   LEU n 
1 94   VAL n 
1 95   TYR n 
1 96   LEU n 
1 97   SER n 
1 98   LYS n 
1 99   SER n 
1 100  ILE n 
1 101  SER n 
1 102  GLY n 
1 103  LEU n 
1 104  ILE n 
1 105  GLN n 
1 106  VAL n 
1 107  ASP n 
1 108  LYS n 
1 109  PRO n 
1 110  VAL n 
1 111  PHE n 
1 112  LYS n 
1 113  PRO n 
1 114  GLY n 
1 115  ASP n 
1 116  THR n 
1 117  VAL n 
1 118  ASN n 
1 119  PHE n 
1 120  ARG n 
1 121  VAL n 
1 122  ILE n 
1 123  VAL n 
1 124  LEU n 
1 125  ASP n 
1 126  THR n 
1 127  GLU n 
1 128  LEU n 
1 129  LYS n 
1 130  PRO n 
1 131  PRO n 
1 132  ALA n 
1 133  ARG n 
1 134  VAL n 
1 135  LYS n 
1 136  SER n 
1 137  VAL n 
1 138  TYR n 
1 139  VAL n 
1 140  THR n 
1 141  ILE n 
1 142  ARG n 
1 143  ASP n 
1 144  PRO n 
1 145  GLN n 
1 146  ARG n 
1 147  ASN n 
1 148  VAL n 
1 149  ILE n 
1 150  ARG n 
1 151  LYS n 
1 152  TRP n 
1 153  SER n 
1 154  THR n 
1 155  ALA n 
1 156  LYS n 
1 157  LEU n 
1 158  TYR n 
1 159  ALA n 
1 160  GLY n 
1 161  VAL n 
1 162  PHE n 
1 163  GLU n 
1 164  SER n 
1 165  ASP n 
1 166  LEU n 
1 167  GLN n 
1 168  ILE n 
1 169  ALA n 
1 170  PRO n 
1 171  THR n 
1 172  PRO n 
1 173  MET n 
1 174  LEU n 
1 175  GLY n 
1 176  VAL n 
1 177  TRP n 
1 178  ASN n 
1 179  ILE n 
1 180  SER n 
1 181  VAL n 
1 182  GLU n 
1 183  VAL n 
1 184  GLU n 
1 185  GLY n 
1 186  GLU n 
1 187  GLU n 
1 188  LEU n 
1 189  VAL n 
1 190  SER n 
1 191  LYS n 
1 192  THR n 
1 193  PHE n 
1 194  GLU n 
1 195  VAL n 
1 196  LYS n 
1 197  GLU n 
1 198  TYR n 
1 199  VAL n 
1 200  LEU n 
1 201  SER n 
1 202  THR n 
1 203  PHE n 
1 204  ASP n 
1 205  VAL n 
1 206  GLN n 
1 207  VAL n 
1 208  MET n 
1 209  PRO n 
1 210  SER n 
1 211  VAL n 
1 212  ILE n 
1 213  PRO n 
1 214  LEU n 
1 215  GLU n 
1 216  GLU n 
1 217  HIS n 
1 218  GLN n 
1 219  ALA n 
1 220  VAL n 
1 221  ASN n 
1 222  LEU n 
1 223  THR n 
1 224  ILE n 
1 225  GLU n 
1 226  ALA n 
1 227  ASN n 
1 228  TYR n 
1 229  HIS n 
1 230  PHE n 
1 231  GLY n 
1 232  LYS n 
1 233  PRO n 
1 234  VAL n 
1 235  GLN n 
1 236  GLY n 
1 237  VAL n 
1 238  ALA n 
1 239  LYS n 
1 240  VAL n 
1 241  GLU n 
1 242  LEU n 
1 243  TYR n 
1 244  LEU n 
1 245  ASP n 
1 246  ASP n 
1 247  ASP n 
1 248  LYS n 
1 249  LEU n 
1 250  LYS n 
1 251  LEU n 
1 252  LYS n 
1 253  LYS n 
1 254  GLU n 
1 255  LEU n 
1 256  THR n 
1 257  VAL n 
1 258  TYR n 
1 259  GLY n 
1 260  LYS n 
1 261  GLY n 
1 262  GLN n 
1 263  VAL n 
1 264  GLU n 
1 265  LEU n 
1 266  ARG n 
1 267  PHE n 
1 268  ASP n 
1 269  ASN n 
1 270  PHE n 
1 271  ALA n 
1 272  MET n 
1 273  ASP n 
1 274  ALA n 
1 275  ASP n 
1 276  GLN n 
1 277  GLN n 
1 278  ASP n 
1 279  VAL n 
1 280  PRO n 
1 281  VAL n 
1 282  LYS n 
1 283  VAL n 
1 284  SER n 
1 285  PHE n 
1 286  VAL n 
1 287  GLU n 
1 288  GLN n 
1 289  TYR n 
1 290  THR n 
1 291  ASN n 
1 292  ARG n 
1 293  THR n 
1 294  VAL n 
1 295  VAL n 
1 296  LYS n 
1 297  GLN n 
1 298  SER n 
1 299  GLN n 
1 300  ILE n 
1 301  THR n 
1 302  VAL n 
1 303  TYR n 
1 304  ARG n 
1 305  TYR n 
1 306  ALA n 
1 307  TYR n 
1 308  ARG n 
1 309  VAL n 
1 310  GLU n 
1 311  LEU n 
1 312  ILE n 
1 313  LYS n 
1 314  GLU n 
1 315  SER n 
1 316  PRO n 
1 317  GLN n 
1 318  PHE n 
1 319  ARG n 
1 320  PRO n 
1 321  GLY n 
1 322  LEU n 
1 323  PRO n 
1 324  PHE n 
1 325  LYS n 
1 326  CYS n 
1 327  ALA n 
1 328  LEU n 
1 329  GLN n 
1 330  PHE n 
1 331  THR n 
1 332  HIS n 
1 333  HIS n 
1 334  ASP n 
1 335  GLY n 
1 336  THR n 
1 337  PRO n 
1 338  ALA n 
1 339  LYS n 
1 340  GLY n 
1 341  ILE n 
1 342  SER n 
1 343  GLY n 
1 344  LYS n 
1 345  VAL n 
1 346  GLU n 
1 347  VAL n 
1 348  SER n 
1 349  ASP n 
1 350  VAL n 
1 351  ARG n 
1 352  PHE n 
1 353  GLU n 
1 354  THR n 
1 355  THR n 
1 356  THR n 
1 357  THR n 
1 358  SER n 
1 359  ASP n 
1 360  ASN n 
1 361  ASP n 
1 362  GLY n 
1 363  LEU n 
1 364  ILE n 
1 365  LYS n 
1 366  LEU n 
1 367  GLU n 
1 368  LEU n 
1 369  GLN n 
1 370  PRO n 
1 371  SER n 
1 372  GLU n 
1 373  GLY n 
1 374  THR n 
1 375  GLU n 
1 376  GLN n 
1 377  LEU n 
1 378  SER n 
1 379  ILE n 
1 380  HIS n 
1 381  PHE n 
1 382  ASN n 
1 383  ALA n 
1 384  VAL n 
1 385  ASP n 
1 386  GLY n 
1 387  PHE n 
1 388  PHE n 
1 389  PHE n 
1 390  TYR n 
1 391  GLU n 
1 392  ASP n 
1 393  VAL n 
1 394  ASN n 
1 395  LYS n 
1 396  VAL n 
1 397  GLU n 
1 398  THR n 
1 399  VAL n 
1 400  THR n 
1 401  ASP n 
1 402  ALA n 
1 403  TYR n 
1 404  ILE n 
1 405  LYS n 
1 406  LEU n 
1 407  GLU n 
1 408  LEU n 
1 409  LYS n 
1 410  SER n 
1 411  PRO n 
1 412  ILE n 
1 413  LYS n 
1 414  ARG n 
1 415  ASN n 
1 416  LYS n 
1 417  LEU n 
1 418  MET n 
1 419  ARG n 
1 420  PHE n 
1 421  MET n 
1 422  VAL n 
1 423  THR n 
1 424  CYS n 
1 425  THR n 
1 426  GLU n 
1 427  ARG n 
1 428  MET n 
1 429  THR n 
1 430  PHE n 
1 431  PHE n 
1 432  VAL n 
1 433  TYR n 
1 434  TYR n 
1 435  VAL n 
1 436  MET n 
1 437  SER n 
1 438  LYS n 
1 439  GLY n 
1 440  ASN n 
1 441  ILE n 
1 442  ILE n 
1 443  ASP n 
1 444  ALA n 
1 445  GLY n 
1 446  PHE n 
1 447  MET n 
1 448  ARG n 
1 449  PRO n 
1 450  ASN n 
1 451  LYS n 
1 452  GLN n 
1 453  PRO n 
1 454  LYS n 
1 455  TYR n 
1 456  LEU n 
1 457  LEU n 
1 458  GLN n 
1 459  LEU n 
1 460  ASN n 
1 461  ALA n 
1 462  THR n 
1 463  GLU n 
1 464  LYS n 
1 465  MET n 
1 466  ILE n 
1 467  PRO n 
1 468  ARG n 
1 469  ALA n 
1 470  LYS n 
1 471  ILE n 
1 472  LEU n 
1 473  ILE n 
1 474  ALA n 
1 475  THR n 
1 476  VAL n 
1 477  ALA n 
1 478  GLY n 
1 479  ARG n 
1 480  THR n 
1 481  VAL n 
1 482  VAL n 
1 483  TYR n 
1 484  ASP n 
1 485  PHE n 
1 486  ALA n 
1 487  ASP n 
1 488  LEU n 
1 489  ALA n 
1 490  PHE n 
1 491  GLN n 
1 492  GLU n 
1 493  LEU n 
1 494  ARG n 
1 495  ASN n 
1 496  ASN n 
1 497  PHE n 
1 498  ASP n 
1 499  LEU n 
1 500  SER n 
1 501  ILE n 
1 502  ASP n 
1 503  GLU n 
1 504  GLN n 
1 505  GLU n 
1 506  ILE n 
1 507  LYS n 
1 508  PRO n 
1 509  GLY n 
1 510  ARG n 
1 511  GLN n 
1 512  ILE n 
1 513  GLU n 
1 514  LEU n 
1 515  SER n 
1 516  MET n 
1 517  SER n 
1 518  GLY n 
1 519  ARG n 
1 520  PRO n 
1 521  GLY n 
1 522  ALA n 
1 523  TYR n 
1 524  VAL n 
1 525  GLY n 
1 526  LEU n 
1 527  ALA n 
1 528  ALA n 
1 529  TYR n 
1 530  ASP n 
1 531  LYS n 
1 532  ALA n 
1 533  LEU n 
1 534  LEU n 
1 535  LEU n 
1 536  PHE n 
1 537  ASN n 
1 538  LYS n 
1 539  ASN n 
1 540  HIS n 
1 541  ASP n 
1 542  LEU n 
1 543  PHE n 
1 544  TRP n 
1 545  GLU n 
1 546  ASP n 
1 547  ILE n 
1 548  GLY n 
1 549  GLN n 
1 550  VAL n 
1 551  PHE n 
1 552  ASP n 
1 553  GLY n 
1 554  PHE n 
1 555  HIS n 
1 556  ALA n 
1 557  ILE n 
1 558  ASN n 
1 559  GLU n 
1 560  ASN n 
1 561  GLU n 
1 562  PHE n 
1 563  ASP n 
1 564  ILE n 
1 565  PHE n 
1 566  HIS n 
1 567  SER n 
1 568  LEU n 
1 569  GLY n 
1 570  LEU n 
1 571  PHE n 
1 572  ALA n 
1 573  ARG n 
1 574  THR n 
1 575  LEU n 
1 576  ASP n 
1 577  ASP n 
1 578  ILE n 
1 579  LEU n 
1 580  PHE n 
1 581  ASP n 
1 582  SER n 
1 583  ALA n 
1 584  ASN n 
1 585  GLU n 
1 586  LYS n 
1 587  THR n 
1 588  GLY n 
1 589  ARG n 
1 590  ASN n 
1 591  ALA n 
1 592  LEU n 
1 593  GLN n 
1 594  SER n 
1 595  GLY n 
1 596  LYS n 
1 597  PRO n 
1 598  ILE n 
1 599  GLY n 
1 600  LYS n 
1 601  LEU n 
1 602  VAL n 
1 603  SER n 
1 604  TYR n 
1 605  ARG n 
1 606  THR n 
1 607  ASN n 
1 608  PHE n 
1 609  GLN n 
1 610  GLU n 
1 611  SER n 
1 612  TRP n 
1 613  LEU n 
1 614  TRP n 
1 615  LYS n 
1 616  ASN n 
1 617  VAL n 
1 618  SER n 
1 619  ILE n 
1 620  GLY n 
1 621  ARG n 
1 622  SER n 
1 623  GLY n 
1 624  SER n 
1 625  ARG n 
1 626  LYS n 
1 627  LEU n 
1 628  ILE n 
1 629  GLU n 
1 630  VAL n 
1 631  VAL n 
1 632  PRO n 
1 633  ASP n 
1 634  THR n 
1 635  THR n 
1 636  THR n 
1 637  SER n 
1 638  TRP n 
1 639  TYR n 
1 640  LEU n 
1 641  THR n 
1 642  GLY n 
1 643  PHE n 
1 644  SER n 
1 645  ILE n 
1 646  ASP n 
1 647  PRO n 
1 648  VAL n 
1 649  TYR n 
1 650  GLY n 
1 651  LEU n 
1 652  GLY n 
1 653  ILE n 
1 654  ILE n 
1 655  LYS n 
1 656  LYS n 
1 657  PRO n 
1 658  ILE n 
1 659  GLN n 
1 660  PHE n 
1 661  THR n 
1 662  THR n 
1 663  VAL n 
1 664  GLN n 
1 665  PRO n 
1 666  PHE n 
1 667  TYR n 
1 668  ILE n 
1 669  VAL n 
1 670  GLU n 
1 671  ASN n 
1 672  LEU n 
1 673  PRO n 
1 674  TYR n 
1 675  SER n 
1 676  ILE n 
1 677  LYS n 
1 678  ARG n 
1 679  GLY n 
1 680  GLU n 
1 681  ALA n 
1 682  VAL n 
1 683  VAL n 
1 684  LEU n 
1 685  GLN n 
1 686  PHE n 
1 687  THR n 
1 688  LEU n 
1 689  PHE n 
1 690  ASN n 
1 691  ASN n 
1 692  LEU n 
1 693  GLY n 
1 694  ALA n 
1 695  GLU n 
1 696  TYR n 
1 697  ILE n 
1 698  ALA n 
1 699  ASP n 
1 700  VAL n 
1 701  THR n 
1 702  LEU n 
1 703  TYR n 
1 704  ASN n 
1 705  VAL n 
1 706  ALA n 
1 707  ASN n 
1 708  GLN n 
1 709  THR n 
1 710  GLU n 
1 711  PHE n 
1 712  VAL n 
1 713  GLY n 
1 714  ARG n 
1 715  PRO n 
1 716  ASN n 
1 717  THR n 
1 718  ASP n 
1 719  LEU n 
1 720  SER n 
1 721  TYR n 
1 722  THR n 
1 723  LYS n 
1 724  SER n 
1 725  VAL n 
1 726  SER n 
1 727  VAL n 
1 728  PRO n 
1 729  PRO n 
1 730  LYS n 
1 731  VAL n 
1 732  GLY n 
1 733  VAL n 
1 734  PRO n 
1 735  ILE n 
1 736  SER n 
1 737  PHE n 
1 738  LEU n 
1 739  ILE n 
1 740  LYS n 
1 741  ALA n 
1 742  ARG n 
1 743  LYS n 
1 744  LEU n 
1 745  GLY n 
1 746  GLU n 
1 747  MET n 
1 748  ALA n 
1 749  VAL n 
1 750  ARG n 
1 751  VAL n 
1 752  LYS n 
1 753  ALA n 
1 754  SER n 
1 755  ILE n 
1 756  MET n 
1 757  LEU n 
1 758  GLY n 
1 759  HIS n 
1 760  GLU n 
1 761  THR n 
1 762  ASP n 
1 763  ALA n 
1 764  LEU n 
1 765  GLU n 
1 766  LYS n 
1 767  VAL n 
1 768  ILE n 
1 769  ARG n 
1 770  VAL n 
1 771  MET n 
1 772  PRO n 
1 773  GLU n 
1 774  SER n 
1 775  LEU n 
1 776  VAL n 
1 777  GLN n 
1 778  PRO n 
1 779  ARG n 
1 780  MET n 
1 781  ASP n 
1 782  THR n 
1 783  ARG n 
1 784  PHE n 
1 785  PHE n 
1 786  CYS n 
1 787  PHE n 
1 788  ASP n 
1 789  ASP n 
1 790  HIS n 
1 791  LYS n 
1 792  ASN n 
1 793  GLN n 
1 794  THR n 
1 795  PHE n 
1 796  PRO n 
1 797  ILE n 
1 798  ASN n 
1 799  LEU n 
1 800  ASP n 
1 801  ILE n 
1 802  ASN n 
1 803  LYS n 
1 804  LYS n 
1 805  ALA n 
1 806  ASP n 
1 807  SER n 
1 808  GLY n 
1 809  SER n 
1 810  THR n 
1 811  LYS n 
1 812  ILE n 
1 813  GLU n 
1 814  PHE n 
1 815  ARG n 
1 816  LEU n 
1 817  ASN n 
1 818  PRO n 
1 819  ASN n 
1 820  LEU n 
1 821  LEU n 
1 822  THR n 
1 823  THR n 
1 824  VAL n 
1 825  ILE n 
1 826  LYS n 
1 827  ASN n 
1 828  LEU n 
1 829  ASP n 
1 830  HIS n 
1 831  LEU n 
1 832  LEU n 
1 833  GLY n 
1 834  VAL n 
1 835  PRO n 
1 836  THR n 
1 837  GLY n 
1 838  CYS n 
1 839  GLY n 
1 840  GLU n 
1 841  GLN n 
1 842  ASN n 
1 843  MET n 
1 844  VAL n 
1 845  LYS n 
1 846  PHE n 
1 847  VAL n 
1 848  PRO n 
1 849  ASN n 
1 850  ILE n 
1 851  LEU n 
1 852  VAL n 
1 853  LEU n 
1 854  ASP n 
1 855  TYR n 
1 856  LEU n 
1 857  HIS n 
1 858  ALA n 
1 859  ILE n 
1 860  GLY n 
1 861  SER n 
1 862  LYS n 
1 863  GLU n 
1 864  GLN n 
1 865  HIS n 
1 866  LEU n 
1 867  ILE n 
1 868  ASP n 
1 869  LYS n 
1 870  ALA n 
1 871  THR n 
1 872  ASN n 
1 873  LEU n 
1 874  LEU n 
1 875  ARG n 
1 876  GLN n 
1 877  GLY n 
1 878  TYR n 
1 879  GLN n 
1 880  ASN n 
1 881  GLN n 
1 882  MET n 
1 883  ARG n 
1 884  TYR n 
1 885  ARG n 
1 886  GLN n 
1 887  THR n 
1 888  ASP n 
1 889  GLY n 
1 890  SER n 
1 891  PHE n 
1 892  GLY n 
1 893  LEU n 
1 894  TRP n 
1 895  GLU n 
1 896  THR n 
1 897  THR n 
1 898  ASN n 
1 899  GLY n 
1 900  SER n 
1 901  VAL n 
1 902  PHE n 
1 903  LEU n 
1 904  THR n 
1 905  ALA n 
1 906  PHE n 
1 907  VAL n 
1 908  GLY n 
1 909  THR n 
1 910  SER n 
1 911  MET n 
1 912  GLN n 
1 913  THR n 
1 914  ALA n 
1 915  VAL n 
1 916  LYS n 
1 917  TYR n 
1 918  ILE n 
1 919  SER n 
1 920  ASP n 
1 921  ILE n 
1 922  ASP n 
1 923  ALA n 
1 924  ALA n 
1 925  MET n 
1 926  VAL n 
1 927  GLU n 
1 928  LYS n 
1 929  ALA n 
1 930  LEU n 
1 931  ASP n 
1 932  TRP n 
1 933  LEU n 
1 934  ALA n 
1 935  SER n 
1 936  LYS n 
1 937  GLN n 
1 938  HIS n 
1 939  PHE n 
1 940  SER n 
1 941  GLY n 
1 942  ARG n 
1 943  PHE n 
1 944  ASP n 
1 945  LYS n 
1 946  ALA n 
1 947  GLY n 
1 948  ALA n 
1 949  GLU n 
1 950  TYR n 
1 951  HIS n 
1 952  LYS n 
1 953  GLU n 
1 954  MET n 
1 955  GLN n 
1 956  GLY n 
1 957  GLY n 
1 958  LEU n 
1 959  ARG n 
1 960  ASN n 
1 961  GLY n 
1 962  VAL n 
1 963  ALA n 
1 964  LEU n 
1 965  THR n 
1 966  SER n 
1 967  TYR n 
1 968  VAL n 
1 969  LEU n 
1 970  MET n 
1 971  ALA n 
1 972  LEU n 
1 973  LEU n 
1 974  GLU n 
1 975  ASN n 
1 976  ASP n 
1 977  ILE n 
1 978  ALA n 
1 979  LYS n 
1 980  ALA n 
1 981  LYS n 
1 982  HIS n 
1 983  ALA n 
1 984  GLU n 
1 985  VAL n 
1 986  ILE n 
1 987  GLN n 
1 988  LYS n 
1 989  GLY n 
1 990  MET n 
1 991  THR n 
1 992  TYR n 
1 993  LEU n 
1 994  SER n 
1 995  ASN n 
1 996  GLN n 
1 997  PHE n 
1 998  GLY n 
1 999  SER n 
1 1000 ILE n 
1 1001 ASN n 
1 1002 ASN n 
1 1003 ALA n 
1 1004 TYR n 
1 1005 ASP n 
1 1006 LEU n 
1 1007 SER n 
1 1008 ILE n 
1 1009 ALA n 
1 1010 THR n 
1 1011 TYR n 
1 1012 ALA n 
1 1013 MET n 
1 1014 MET n 
1 1015 LEU n 
1 1016 ASN n 
1 1017 GLY n 
1 1018 HIS n 
1 1019 THR n 
1 1020 MET n 
1 1021 LYS n 
1 1022 GLU n 
1 1023 GLU n 
1 1024 ALA n 
1 1025 LEU n 
1 1026 ASN n 
1 1027 LYS n 
1 1028 LEU n 
1 1029 ILE n 
1 1030 ASP n 
1 1031 MET n 
1 1032 SER n 
1 1033 PHE n 
1 1034 ILE n 
1 1035 ASP n 
1 1036 ALA n 
1 1037 ASP n 
1 1038 LYS n 
1 1039 ASN n 
1 1040 GLU n 
1 1041 ARG n 
1 1042 PHE n 
1 1043 TRP n 
1 1044 ASN n 
1 1045 THR n 
1 1046 THR n 
1 1047 ASN n 
1 1048 PRO n 
1 1049 ILE n 
1 1050 GLU n 
1 1051 THR n 
1 1052 THR n 
1 1053 ALA n 
1 1054 TYR n 
1 1055 ALA n 
1 1056 LEU n 
1 1057 LEU n 
1 1058 SER n 
1 1059 PHE n 
1 1060 VAL n 
1 1061 MET n 
1 1062 ALA n 
1 1063 GLU n 
1 1064 LYS n 
1 1065 TYR n 
1 1066 THR n 
1 1067 ASP n 
1 1068 GLY n 
1 1069 ILE n 
1 1070 PRO n 
1 1071 VAL n 
1 1072 MET n 
1 1073 ASN n 
1 1074 TRP n 
1 1075 LEU n 
1 1076 VAL n 
1 1077 ASN n 
1 1078 GLN n 
1 1079 ARG n 
1 1080 TYR n 
1 1081 VAL n 
1 1082 THR n 
1 1083 GLY n 
1 1084 SER n 
1 1085 PHE n 
1 1086 PRO n 
1 1087 SER n 
1 1088 THR n 
1 1089 GLN n 
1 1090 ASP n 
1 1091 THR n 
1 1092 PHE n 
1 1093 VAL n 
1 1094 GLY n 
1 1095 LEU n 
1 1096 LYS n 
1 1097 ALA n 
1 1098 LEU n 
1 1099 THR n 
1 1100 LYS n 
1 1101 MET n 
1 1102 ALA n 
1 1103 GLU n 
1 1104 LYS n 
1 1105 ILE n 
1 1106 SER n 
1 1107 PRO n 
1 1108 SER n 
1 1109 ARG n 
1 1110 ASN n 
1 1111 ASP n 
1 1112 TYR n 
1 1113 THR n 
1 1114 VAL n 
1 1115 GLN n 
1 1116 LEU n 
1 1117 LYS n 
1 1118 TYR n 
1 1119 LYS n 
1 1120 LYS n 
1 1121 SER n 
1 1122 ALA n 
1 1123 LYS n 
1 1124 TYR n 
1 1125 PHE n 
1 1126 LYS n 
1 1127 ILE n 
1 1128 ASN n 
1 1129 SER n 
1 1130 GLU n 
1 1131 GLN n 
1 1132 ILE n 
1 1133 ASP n 
1 1134 VAL n 
1 1135 GLU n 
1 1136 ASN n 
1 1137 PHE n 
1 1138 VAL n 
1 1139 ASP n 
1 1140 ILE n 
1 1141 PRO n 
1 1142 GLU n 
1 1143 ASP n 
1 1144 THR n 
1 1145 LYS n 
1 1146 LYS n 
1 1147 LEU n 
1 1148 GLU n 
1 1149 ILE n 
1 1150 ASN n 
1 1151 VAL n 
1 1152 GLY n 
1 1153 GLY n 
1 1154 ILE n 
1 1155 GLY n 
1 1156 PHE n 
1 1157 GLY n 
1 1158 LEU n 
1 1159 LEU n 
1 1160 GLU n 
1 1161 VAL n 
1 1162 VAL n 
1 1163 TYR n 
1 1164 GLN n 
1 1165 PHE n 
1 1166 ASN n 
1 1167 LEU n 
1 1168 ASN n 
1 1169 LEU n 
1 1170 VAL n 
1 1171 ASN n 
1 1172 PHE n 
1 1173 GLU n 
1 1174 ASN n 
1 1175 ARG n 
1 1176 PHE n 
1 1177 GLN n 
1 1178 LEU n 
1 1179 ASP n 
1 1180 LEU n 
1 1181 GLU n 
1 1182 LYS n 
1 1183 GLN n 
1 1184 ASN n 
1 1185 THR n 
1 1186 GLY n 
1 1187 SER n 
1 1188 ASP n 
1 1189 TYR n 
1 1190 GLU n 
1 1191 LEU n 
1 1192 ARG n 
1 1193 LEU n 
1 1194 LYS n 
1 1195 VAL n 
1 1196 CYS n 
1 1197 ALA n 
1 1198 SER n 
1 1199 TYR n 
1 1200 ILE n 
1 1201 PRO n 
1 1202 GLN n 
1 1203 LEU n 
1 1204 THR n 
1 1205 ASP n 
1 1206 ARG n 
1 1207 ARG n 
1 1208 SER n 
1 1209 ASN n 
1 1210 MET n 
1 1211 ALA n 
1 1212 LEU n 
1 1213 ILE n 
1 1214 GLU n 
1 1215 VAL n 
1 1216 THR n 
1 1217 LEU n 
1 1218 PRO n 
1 1219 SER n 
1 1220 GLY n 
1 1221 TYR n 
1 1222 VAL n 
1 1223 VAL n 
1 1224 ASP n 
1 1225 ARG n 
1 1226 ASN n 
1 1227 PRO n 
1 1228 ILE n 
1 1229 SER n 
1 1230 GLU n 
1 1231 GLN n 
1 1232 THR n 
1 1233 LYS n 
1 1234 VAL n 
1 1235 ASN n 
1 1236 PRO n 
1 1237 ILE n 
1 1238 GLN n 
1 1239 LYS n 
1 1240 THR n 
1 1241 GLU n 
1 1242 ILE n 
1 1243 ARG n 
1 1244 TYR n 
1 1245 GLY n 
1 1246 GLY n 
1 1247 THR n 
1 1248 SER n 
1 1249 VAL n 
1 1250 VAL n 
1 1251 LEU n 
1 1252 TYR n 
1 1253 TYR n 
1 1254 ASP n 
1 1255 ASN n 
1 1256 MET n 
1 1257 GLY n 
1 1258 SER n 
1 1259 GLU n 
1 1260 ARG n 
1 1261 ASN n 
1 1262 CYS n 
1 1263 PHE n 
1 1264 THR n 
1 1265 LEU n 
1 1266 THR n 
1 1267 ALA n 
1 1268 TYR n 
1 1269 ARG n 
1 1270 ARG n 
1 1271 PHE n 
1 1272 LYS n 
1 1273 VAL n 
1 1274 ALA n 
1 1275 LEU n 
1 1276 LYS n 
1 1277 ARG n 
1 1278 PRO n 
1 1279 ALA n 
1 1280 TYR n 
1 1281 VAL n 
1 1282 VAL n 
1 1283 VAL n 
1 1284 TYR n 
1 1285 ASP n 
1 1286 TYR n 
1 1287 TYR n 
1 1288 ASN n 
1 1289 THR n 
1 1290 ASN n 
1 1291 LEU n 
1 1292 ASN n 
1 1293 ALA n 
1 1294 ILE n 
1 1295 LYS n 
1 1296 VAL n 
1 1297 TYR n 
1 1298 GLU n 
1 1299 VAL n 
1 1300 ASP n 
1 1301 LYS n 
1 1302 GLN n 
1 1303 ASN n 
1 1304 LEU n 
1 1305 CYS n 
1 1306 GLU n 
1 1307 ILE n 
1 1308 CYS n 
1 1309 ASP n 
1 1310 GLU n 
1 1311 GLU n 
1 1312 ASP n 
1 1313 CYS n 
1 1314 PRO n 
1 1315 ALA n 
1 1316 GLU n 
1 1317 CYS n 
1 1318 GLY n 
1 1319 GLY n 
1 1320 HIS n 
1 1321 HIS n 
1 1322 HIS n 
1 1323 HIS n 
1 1324 HIS n 
1 1325 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                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               'African malaria mosquito' 
_entity_src_gen.gene_src_genus                     Anopheles 
_entity_src_gen.pdbx_gene_src_gene                 TEP-I 
_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      'Anopheles gambiae' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     7165 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     Escherichia 
_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            'High-Five(TM)' 
_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          baculovirus 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pFastBac1 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   'Expression in BAC-TO-BAC system by INVITROGEN' 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q9GYW4_ANOGA 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_db_accession          Q9GYW4 
_struct_ref.pdbx_align_begin           ? 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_db_isoform            ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              2PN5 
_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                 1317 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q9GYW4 
_struct_ref_seq.db_align_beg                  22 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1338 
_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       1317 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE               ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE             ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'        ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE               ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE              ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'        ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE              ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                  ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE             ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                 ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE             ? 'C5 H11 N O2 S'  149.211 
NA  non-polymer         . 'SODIUM ION'           ? 'Na 1'           22.990  
NAG D-saccharide        . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6'    221.208 
PHE 'L-peptide linking' y PHENYLALANINE          ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                 ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE              ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN             ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE               ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                 ? 'C5 H11 N O2'    117.146 
# 
_exptl.crystals_number   1 
_exptl.entry_id          2PN5 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      4.26 
_exptl_crystal.density_percent_sol   71.10 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              6.5 
_exptl_crystal_grow.temp            294 
_exptl_crystal_grow.pdbx_details    
'2 M NaH2/K2H PO4, 0.2 M NaCl, 0.1 M imidazole pH 8.0, 50 mM NaK tartrate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
loop_
_diffrn.id 
_diffrn.ambient_temp 
_diffrn.ambient_temp_details 
_diffrn.crystal_id 
1 100 ? 1 
2 ?   ? 1 
3 ?   ? 1 
4 ?   ? 1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   APS-1 
_diffrn_detector.pdbx_collection_date   2006-11-11 
_diffrn_detector.details                'SAGITALLY FOCUSING. 2ND            CRYSTAL, ROSENBAUM-ROCK VERTICAL FOCUSING MIRROR' 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    'ROSENBAUM-ROCK DOUBLE-CRYSTAL MONOCHROMATOR' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9791 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'APS BEAMLINE 19-BM' 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        0.9791 
_diffrn_source.pdbx_synchrotron_site       APS 
_diffrn_source.pdbx_synchrotron_beamline   19-BM 
# 
_reflns.entry_id                     2PN5 
_reflns.d_resolution_high            2.698 
_reflns.d_resolution_low             50.000 
_reflns.number_obs                   71959 
_reflns.pdbx_Rmerge_I_obs            0.080 
_reflns.pdbx_netI_over_sigmaI        10.100 
_reflns.pdbx_chi_squared             1.172 
_reflns.pdbx_redundancy              7.800 
_reflns.percent_possible_obs         99.900 
_reflns.observed_criterion_sigma_F   -1.0 
_reflns.observed_criterion_sigma_I   -1.0 
_reflns.number_all                   72031 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        69.24 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high             2.698 
_reflns_shell.d_res_low              2.75 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.Rmerge_I_obs           0.898 
_reflns_shell.meanI_over_sigI_obs    2.1 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.pdbx_chi_squared       1.033 
_reflns_shell.pdbx_redundancy        7.50 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      3537 
_reflns_shell.percent_possible_all   99.90 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.pdbx_diffrn_id         1 
# 
_refine.entry_id                                 2PN5 
_refine.ls_d_res_high                            2.698 
_refine.ls_d_res_low                             45.880 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.ls_percent_reflns_obs                    100.000 
_refine.ls_number_reflns_obs                     71859 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_work                       0.239 
_refine.ls_R_factor_R_free                       0.275 
_refine.ls_percent_reflns_R_free                 5.100 
_refine.ls_number_reflns_R_free                  3631 
_refine.B_iso_mean                               52.085 
_refine.aniso_B[1][1]                            1.230 
_refine.aniso_B[2][2]                            1.230 
_refine.aniso_B[3][3]                            -2.470 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            0.000 
_refine.aniso_B[2][3]                            0.000 
_refine.correlation_coeff_Fo_to_Fc               0.922 
_refine.correlation_coeff_Fo_to_Fc_free          0.901 
_refine.pdbx_overall_ESU_R                       0.417 
_refine.pdbx_overall_ESU_R_Free                  0.297 
_refine.overall_SU_ML                            0.225 
_refine.overall_SU_B                             22.325 
_refine.solvent_model_details                    MASK 
_refine.pdbx_solvent_vdw_probe_radii             1.400 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_refine.pdbx_method_to_determine_struct          MIRAS 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_ls_sigma_I                          ? 
_refine.ls_number_reflns_all                     71859 
_refine.ls_R_factor_all                          ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_TLS_residual_ADP_flag               'LIKELY RESIDUAL' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        10270 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         73 
_refine_hist.number_atoms_solvent             140 
_refine_hist.number_atoms_total               10483 
_refine_hist.d_res_high                       2.698 
_refine_hist.d_res_low                        45.880 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d         10629 0.009  0.022  ? 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg      14408 1.188  1.969  ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg   1293  5.962  5.000  ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg   497   37.850 24.688 ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg   1885  18.161 15.000 ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg   55    19.750 15.000 ? 'X-RAY DIFFRACTION' ? 
r_chiral_restr           1630  0.083  0.200  ? 'X-RAY DIFFRACTION' ? 
r_gen_planes_refined     7968  0.003  0.020  ? 'X-RAY DIFFRACTION' ? 
r_nbd_refined            4386  0.209  0.200  ? 'X-RAY DIFFRACTION' ? 
r_nbtor_refined          7188  0.309  0.200  ? 'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined    413   0.125  0.200  ? 'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined   49    0.191  0.200  ? 'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined 9     0.142  0.200  ? 'X-RAY DIFFRACTION' ? 
r_mcbond_it              6431  0.503  1.500  ? 'X-RAY DIFFRACTION' ? 
r_mcangle_it             10463 0.958  2.000  ? 'X-RAY DIFFRACTION' ? 
r_scbond_it              4304  1.217  3.000  ? 'X-RAY DIFFRACTION' ? 
r_scangle_it             3945  2.159  4.500  ? 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.d_res_high                       2.698 
_refine_ls_shell.d_res_low                        2.768 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               100.000 
_refine_ls_shell.number_reflns_R_work             4919 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.352 
_refine_ls_shell.R_factor_R_free                  0.398 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             241 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                5160 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  2PN5 
_struct.title                     'Crystal Structure of TEP1r' 
_struct.pdbx_descriptor           'Thioester-containing protein I' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            N 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        2PN5 
_struct_keywords.pdbx_keywords   'IMMUNE SYSTEM' 
_struct_keywords.text            'full-length mature peptide, IMMUNE SYSTEM' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 3 ? 
H N N 3 ? 
I N N 3 ? 
J N N 4 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  1  LEU A 214  ? HIS A 217  ? LEU A 214  HIS A 217  5 ? 4  
HELX_P HELX_P2  2  ASP A 349  ? ARG A 351  ? ASP A 349  ARG A 351  5 ? 3  
HELX_P HELX_P3  3  THR A 462  ? ILE A 466  ? THR A 462  ILE A 466  5 ? 5  
HELX_P HELX_P4  4  GLN A 491  ? ARG A 494  ? GLN A 491  ARG A 494  5 ? 4  
HELX_P HELX_P5  5  LYS A 531  ? ASN A 537  ? LYS A 531  ASN A 537  1 ? 7  
HELX_P HELX_P6  6  LEU A 542  ? ASP A 552  ? LEU A 542  ASP A 552  1 ? 11 
HELX_P HELX_P7  7  ASP A 563  ? GLY A 569  ? ASP A 563  GLY A 569  1 ? 7  
HELX_P HELX_P8  8  VAL A 705  ? ASN A 707  ? VAL A 705  ASN A 707  5 ? 3  
HELX_P HELX_P9  9  LEU A 821  ? ASN A 827  ? LEU A 821  ASN A 827  1 ? 7  
HELX_P HELX_P10 10 GLU A 840  ? LYS A 845  ? GLU A 840  LYS A 845  5 ? 6  
HELX_P HELX_P11 11 PHE A 846  ? ILE A 859  ? PHE A 846  ILE A 859  1 ? 14 
HELX_P HELX_P12 12 GLU A 863  ? MET A 882  ? GLU A 863  MET A 882  1 ? 20 
HELX_P HELX_P13 13 ARG A 883  ? ARG A 885  ? ARG A 883  ARG A 885  5 ? 3  
HELX_P HELX_P14 14 SER A 900  ? VAL A 915  ? SER A 900  VAL A 915  1 ? 16 
HELX_P HELX_P15 15 ASP A 922  ? LYS A 936  ? ASP A 922  LYS A 936  1 ? 15 
HELX_P HELX_P16 16 HIS A 951  ? GLY A 956  ? HIS A 951  GLY A 956  1 ? 6  
HELX_P HELX_P17 17 GLY A 961  ? GLU A 974  ? GLY A 961  GLU A 974  1 ? 14 
HELX_P HELX_P18 18 ASN A 975  ? HIS A 982  ? ASN A 975  HIS A 982  1 ? 8  
HELX_P HELX_P19 19 HIS A 982  ? PHE A 997  ? HIS A 982  PHE A 997  1 ? 16 
HELX_P HELX_P20 20 GLY A 998  ? ILE A 1000 ? GLY A 998  ILE A 1000 5 ? 3  
HELX_P HELX_P21 21 ASN A 1002 ? GLY A 1017 ? ASN A 1002 GLY A 1017 1 ? 16 
HELX_P HELX_P22 22 MET A 1020 ? MET A 1031 ? MET A 1020 MET A 1031 1 ? 12 
HELX_P HELX_P23 23 ASN A 1047 ? ALA A 1062 ? ASN A 1047 ALA A 1062 1 ? 16 
HELX_P HELX_P24 24 LYS A 1064 ? ASN A 1077 ? LYS A 1064 ASN A 1077 1 ? 14 
HELX_P HELX_P25 25 SER A 1087 ? SER A 1106 ? SER A 1087 SER A 1106 1 ? 20 
HELX_P HELX_P26 26 ASN A 1303 ? CYS A 1308 ? ASN A 1303 CYS A 1308 1 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1 disulf ? ? A CYS 1196 SG  ? ? ? 1_555 A CYS 1262 SG ? ? A CYS 1196 A CYS 1262 1_555 ? ? ? ? ? ? ? 2.072 ? 
disulf2 disulf ? ? A CYS 1305 SG  ? ? ? 1_555 A CYS 1317 SG ? ? A CYS 1305 A CYS 1317 1_555 ? ? ? ? ? ? ? 2.043 ? 
disulf3 disulf ? ? A CYS 1308 SG  ? ? ? 1_555 A CYS 1313 SG ? ? A CYS 1308 A CYS 1313 1_555 ? ? ? ? ? ? ? 2.047 ? 
covale1 covale ? ? A CYS 838  SG  ? ? ? 1_555 A GLN 841  CD ? ? A CYS 838  A GLN 841  1_555 ? ? ? ? ? ? ? 1.751 ? 
covale2 covale ? ? A ASN 178  ND2 ? ? ? 1_555 B NAG .    C1 ? ? A ASN 178  A NAG 1326 1_555 ? ? ? ? ? ? ? 1.447 ? 
covale3 covale ? ? A ASN 221  ND2 ? ? ? 1_555 C NAG .    C1 ? ? A ASN 221  A NAG 1327 1_555 ? ? ? ? ? ? ? 1.448 ? 
covale4 covale ? ? A ASN 291  ND2 ? ? ? 1_555 D NAG .    C1 ? ? A ASN 291  A NAG 1328 1_555 ? ? ? ? ? ? ? 1.443 ? 
covale5 covale ? ? A ASN 616  ND2 ? ? ? 1_555 E NAG .    C1 ? ? A ASN 616  A NAG 1329 1_555 ? ? ? ? ? ? ? 1.442 ? 
covale6 covale ? ? E NAG .    O4  ? ? ? 1_555 F NAG .    C1 ? ? A NAG 1329 A NAG 1330 1_555 ? ? ? ? ? ? ? 1.447 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          ILE 
_struct_mon_prot_cis.label_seq_id           466 
_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           ILE 
_struct_mon_prot_cis.auth_seq_id            466 
_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    467 
_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     467 
_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       0.53 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 4 ? 
B ? 5 ? 
C ? 3 ? 
D ? 5 ? 
E ? 3 ? 
F ? 4 ? 
G ? 3 ? 
H ? 4 ? 
I ? 3 ? 
J ? 5 ? 
K ? 3 ? 
L ? 4 ? 
M ? 4 ? 
N ? 4 ? 
O ? 3 ? 
P ? 5 ? 
Q ? 4 ? 
R ? 4 ? 
S ? 2 ? 
T ? 6 ? 
U ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2 ? anti-parallel 
A 2 3 ? anti-parallel 
A 3 4 ? anti-parallel 
B 1 2 ? parallel      
B 2 3 ? anti-parallel 
B 3 4 ? anti-parallel 
B 4 5 ? anti-parallel 
C 1 2 ? anti-parallel 
C 2 3 ? anti-parallel 
D 1 2 ? parallel      
D 2 3 ? anti-parallel 
D 3 4 ? anti-parallel 
D 4 5 ? anti-parallel 
E 1 2 ? anti-parallel 
E 2 3 ? anti-parallel 
F 1 2 ? anti-parallel 
F 2 3 ? anti-parallel 
F 3 4 ? anti-parallel 
G 1 2 ? anti-parallel 
G 2 3 ? anti-parallel 
H 1 2 ? anti-parallel 
H 2 3 ? anti-parallel 
H 3 4 ? anti-parallel 
I 1 2 ? anti-parallel 
I 2 3 ? anti-parallel 
J 1 2 ? anti-parallel 
J 2 3 ? anti-parallel 
J 3 4 ? anti-parallel 
J 4 5 ? parallel      
K 1 2 ? anti-parallel 
K 2 3 ? anti-parallel 
L 1 2 ? anti-parallel 
L 2 3 ? anti-parallel 
L 3 4 ? anti-parallel 
M 1 2 ? anti-parallel 
M 2 3 ? anti-parallel 
M 3 4 ? anti-parallel 
N 1 2 ? anti-parallel 
N 2 3 ? anti-parallel 
N 3 4 ? anti-parallel 
O 1 2 ? anti-parallel 
O 2 3 ? anti-parallel 
P 1 2 ? parallel      
P 2 3 ? anti-parallel 
P 3 4 ? anti-parallel 
P 4 5 ? anti-parallel 
Q 1 2 ? anti-parallel 
Q 2 3 ? anti-parallel 
Q 3 4 ? anti-parallel 
R 1 2 ? anti-parallel 
R 2 3 ? anti-parallel 
R 3 4 ? anti-parallel 
S 1 2 ? anti-parallel 
T 1 2 ? anti-parallel 
T 2 3 ? anti-parallel 
T 3 4 ? anti-parallel 
T 4 5 ? anti-parallel 
T 5 6 ? anti-parallel 
U 1 2 ? anti-parallel 
U 2 3 ? anti-parallel 
U 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1 MET A 58   ? ASN A 65   ? MET A 58   ASN A 65   
A 2 GLU A 14   ? ASN A 21   ? GLU A 14   ASN A 21   
A 3 LEU A 2    ? PRO A 6    ? LEU A 2    PRO A 6    
A 4 LEU A 570  ? THR A 574  ? LEU A 570  THR A 574  
B 1 PHE A 8    ? ILE A 9    ? PHE A 8    ILE A 9    
B 2 HIS A 88   ? TYR A 95   ? HIS A 88   TYR A 95   
B 3 TYR A 75   ? GLN A 82   ? TYR A 75   GLN A 82   
B 4 LYS A 28   ? LEU A 35   ? LYS A 28   LEU A 35   
B 5 VAL A 48   ? ARG A 55   ? VAL A 48   ARG A 55   
C 1 ILE A 100  ? VAL A 106  ? ILE A 100  VAL A 106  
C 2 THR A 116  ? ASP A 125  ? THR A 116  ASP A 125  
C 3 VAL A 161  ? GLN A 167  ? VAL A 161  GLN A 167  
D 1 VAL A 110  ? PHE A 111  ? VAL A 110  PHE A 111  
D 2 GLU A 186  ? VAL A 195  ? GLU A 186  VAL A 195  
D 3 GLY A 175  ? VAL A 183  ? GLY A 175  VAL A 183  
D 4 SER A 136  ? ARG A 142  ? SER A 136  ARG A 142  
D 5 VAL A 148  ? LYS A 156  ? VAL A 148  LYS A 156  
E 1 PHE A 203  ? PRO A 209  ? PHE A 203  PRO A 209  
E 2 ALA A 219  ? TYR A 228  ? ALA A 219  TYR A 228  
E 3 LYS A 260  ? ARG A 266  ? LYS A 260  ARG A 266  
F 1 LEU A 249  ? TYR A 258  ? LEU A 249  TYR A 258  
F 2 GLN A 235  ? LEU A 244  ? GLN A 235  LEU A 244  
F 3 GLN A 276  ? GLU A 287  ? GLN A 276  GLU A 287  
F 4 THR A 293  ? TYR A 303  ? THR A 293  TYR A 303  
G 1 ARG A 308  ? LYS A 313  ? ARG A 308  LYS A 313  
G 2 PHE A 324  ? THR A 331  ? PHE A 324  THR A 331  
G 3 LEU A 363  ? LEU A 368  ? LEU A 363  LEU A 368  
H 1 PHE A 352  ? THR A 357  ? PHE A 352  THR A 357  
H 2 SER A 342  ? VAL A 347  ? SER A 342  VAL A 347  
H 3 GLN A 376  ? ASN A 382  ? GLN A 376  ASN A 382  
H 4 PHE A 388  ? ASN A 394  ? PHE A 388  ASN A 394  
I 1 ILE A 404  ? LEU A 408  ? ILE A 404  LEU A 408  
I 2 LEU A 417  ? MET A 428  ? LEU A 417  MET A 428  
I 3 GLN A 452  ? ASN A 460  ? GLN A 452  ASN A 460  
J 1 ILE A 441  ? MET A 447  ? ILE A 441  MET A 447  
J 2 PHE A 431  ? MET A 436  ? PHE A 431  MET A 436  
J 3 ARG A 468  ? ALA A 477  ? ARG A 468  ALA A 477  
J 4 THR A 480  ? ALA A 489  ? THR A 480  ALA A 489  
J 5 LEU A 579  ? PHE A 580  ? LEU A 579  PHE A 580  
K 1 ASP A 498  ? ILE A 501  ? ASP A 498  ILE A 501  
K 2 GLN A 511  ? SER A 517  ? GLN A 511  SER A 517  
K 3 SER A 624  ? VAL A 630  ? SER A 624  VAL A 630  
L 1 ASN A 616  ? SER A 618  ? ASN A 616  SER A 618  
L 2 TYR A 523  ? ASP A 530  ? TYR A 523  ASP A 530  
L 3 THR A 636  ? ASP A 646  ? THR A 636  ASP A 646  
L 4 GLY A 650  ? ILE A 653  ? GLY A 650  ILE A 653  
M 1 ASN A 616  ? SER A 618  ? ASN A 616  SER A 618  
M 2 TYR A 523  ? ASP A 530  ? TYR A 523  ASP A 530  
M 3 THR A 636  ? ASP A 646  ? THR A 636  ASP A 646  
M 4 ILE A 658  ? THR A 662  ? ILE A 658  THR A 662  
N 1 PHE A 666  ? ASN A 671  ? PHE A 666  ASN A 671  
N 2 ALA A 681  ? ASN A 690  ? ALA A 681  ASN A 690  
N 3 VAL A 733  ? ALA A 741  ? VAL A 733  ALA A 741  
N 4 THR A 709  ? PHE A 711  ? THR A 709  PHE A 711  
O 1 PHE A 666  ? ASN A 671  ? PHE A 666  ASN A 671  
O 2 ALA A 681  ? ASN A 690  ? ALA A 681  ASN A 690  
O 3 VAL A 1273 ? ALA A 1274 ? VAL A 1273 ALA A 1274 
P 1 SER A 675  ? LYS A 677  ? SER A 675  LYS A 677  
P 2 THR A 761  ? MET A 771  ? THR A 761  MET A 771  
P 3 GLY A 745  ? SER A 754  ? GLY A 745  SER A 754  
P 4 TYR A 696  ? TYR A 703  ? TYR A 696  TYR A 703  
P 5 SER A 720  ? VAL A 727  ? SER A 720  VAL A 727  
Q 1 ARG A 779  ? ASN A 798  ? ARG A 779  ASN A 798  
Q 2 LYS A 1146 ? GLN A 1164 ? LYS A 1146 GLN A 1164 
Q 3 ASP A 1111 ? TYR A 1118 ? ASP A 1111 TYR A 1118 
Q 4 SER A 1121 ? ILE A 1127 ? SER A 1121 ILE A 1127 
R 1 ARG A 779  ? ASN A 798  ? ARG A 779  ASN A 798  
R 2 LYS A 1146 ? GLN A 1164 ? LYS A 1146 GLN A 1164 
R 3 LYS A 811  ? ASN A 817  ? LYS A 811  ASN A 817  
R 4 VAL A 1138 ? ASP A 1139 ? VAL A 1138 ASP A 1139 
S 1 PHE A 1033 ? ASP A 1035 ? PHE A 1033 ASP A 1035 
S 2 GLU A 1040 ? PHE A 1042 ? GLU A 1040 PHE A 1042 
T 1 PHE A 1172 ? ASN A 1174 ? PHE A 1172 ASN A 1174 
T 2 ASN A 1288 ? TYR A 1297 ? ASN A 1288 TYR A 1297 
T 3 ALA A 1279 ? ASP A 1285 ? ALA A 1279 ASP A 1285 
T 4 ALA A 1211 ? THR A 1216 ? ALA A 1211 THR A 1216 
T 5 SER A 1248 ? TYR A 1253 ? SER A 1248 TYR A 1253 
T 6 LYS A 1239 ? ARG A 1243 ? LYS A 1239 ARG A 1243 
U 1 PHE A 1176 ? GLN A 1183 ? PHE A 1176 GLN A 1183 
U 2 GLU A 1190 ? TYR A 1199 ? GLU A 1190 TYR A 1199 
U 3 ASN A 1261 ? ARG A 1269 ? ASN A 1261 ARG A 1269 
U 4 TYR A 1221 ? SER A 1229 ? TYR A 1221 SER A 1229 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2 O PHE A 64   ? O PHE A 64   N TYR A 15   ? N TYR A 15   
A 2 3 O VAL A 18   ? O VAL A 18   N VAL A 4    ? N VAL A 4    
A 3 4 N GLY A 5    ? N GLY A 5    O PHE A 571  ? O PHE A 571  
B 1 2 N ILE A 9    ? N ILE A 9    O VAL A 94   ? O VAL A 94   
B 2 3 O LYS A 89   ? O LYS A 89   N ILE A 79   ? N ILE A 79   
B 3 4 O THR A 78   ? O THR A 78   N LYS A 34   ? N LYS A 34   
B 4 5 N VAL A 29   ? N VAL A 29   O VAL A 54   ? O VAL A 54   
C 1 2 N LEU A 103  ? N LEU A 103  O ILE A 122  ? O ILE A 122  
C 2 3 N VAL A 117  ? N VAL A 117  O LEU A 166  ? O LEU A 166  
D 1 2 N PHE A 111  ? N PHE A 111  O GLU A 194  ? O GLU A 194  
D 2 3 O LYS A 191  ? O LYS A 191  N ILE A 179  ? N ILE A 179  
D 3 4 O GLU A 182  ? O GLU A 182  N TYR A 138  ? N TYR A 138  
D 4 5 N VAL A 137  ? N VAL A 137  O ALA A 155  ? O ALA A 155  
E 1 2 N GLN A 206  ? N GLN A 206  O GLU A 225  ? O GLU A 225  
E 2 3 N LEU A 222  ? N LEU A 222  O VAL A 263  ? O VAL A 263  
F 1 2 O LYS A 253  ? O LYS A 253  N VAL A 240  ? N VAL A 240  
F 2 3 N GLU A 241  ? N GLU A 241  O LYS A 282  ? O LYS A 282  
F 3 4 N PHE A 285  ? N PHE A 285  O VAL A 294  ? O VAL A 294  
G 1 2 N GLU A 310  ? N GLU A 310  O GLN A 329  ? O GLN A 329  
G 2 3 N CYS A 326  ? N CYS A 326  O LEU A 366  ? O LEU A 366  
H 1 2 O THR A 354  ? O THR A 354  N VAL A 345  ? N VAL A 345  
H 2 3 N LYS A 344  ? N LYS A 344  O ASN A 382  ? O ASN A 382  
H 3 4 N LEU A 377  ? N LEU A 377  O VAL A 393  ? O VAL A 393  
I 1 2 N LYS A 405  ? N LYS A 405  O THR A 423  ? O THR A 423  
I 2 3 N VAL A 422  ? N VAL A 422  O TYR A 455  ? O TYR A 455  
J 1 2 O ASP A 443  ? O ASP A 443  N VAL A 435  ? N VAL A 435  
J 2 3 N VAL A 432  ? N VAL A 432  O ALA A 474  ? O ALA A 474  
J 3 4 N ALA A 469  ? N ALA A 469  O LEU A 488  ? O LEU A 488  
J 4 5 N VAL A 481  ? N VAL A 481  O LEU A 579  ? O LEU A 579  
K 1 2 N SER A 500  ? N SER A 500  O SER A 515  ? O SER A 515  
K 2 3 N LEU A 514  ? N LEU A 514  O LEU A 627  ? O LEU A 627  
L 1 2 O VAL A 617  ? O VAL A 617  N VAL A 524  ? N VAL A 524  
L 2 3 N ALA A 527  ? N ALA A 527  O THR A 641  ? O THR A 641  
L 3 4 N SER A 644  ? N SER A 644  O GLY A 652  ? O GLY A 652  
M 1 2 O VAL A 617  ? O VAL A 617  N VAL A 524  ? N VAL A 524  
M 2 3 N ALA A 527  ? N ALA A 527  O THR A 641  ? O THR A 641  
M 3 4 N LEU A 640  ? N LEU A 640  O ILE A 658  ? O ILE A 658  
N 1 2 N VAL A 669  ? N VAL A 669  O THR A 687  ? O THR A 687  
N 2 3 N VAL A 682  ? N VAL A 682  O ILE A 739  ? O ILE A 739  
N 3 4 O LYS A 740  ? O LYS A 740  N GLU A 710  ? N GLU A 710  
O 1 2 N VAL A 669  ? N VAL A 669  O THR A 687  ? O THR A 687  
O 2 3 N ALA A 681  ? N ALA A 681  O ALA A 1274 ? O ALA A 1274 
P 1 2 N ILE A 676  ? N ILE A 676  O MET A 771  ? O MET A 771  
P 2 3 O VAL A 770  ? O VAL A 770  N GLY A 745  ? N GLY A 745  
P 3 4 O LYS A 752  ? O LYS A 752  N THR A 701  ? N THR A 701  
P 4 5 N ALA A 698  ? N ALA A 698  O VAL A 725  ? O VAL A 725  
Q 1 2 N PHE A 795  ? N PHE A 795  O ILE A 1149 ? O ILE A 1149 
Q 2 3 O ILE A 1154 ? O ILE A 1154 N ASP A 1111 ? N ASP A 1111 
Q 3 4 N LEU A 1116 ? N LEU A 1116 O LYS A 1123 ? O LYS A 1123 
R 1 2 N PHE A 795  ? N PHE A 795  O ILE A 1149 ? O ILE A 1149 
R 2 3 O VAL A 1162 ? O VAL A 1162 N GLU A 813  ? N GLU A 813  
R 3 4 N PHE A 814  ? N PHE A 814  O ASP A 1139 ? O ASP A 1139 
S 1 2 N PHE A 1033 ? N PHE A 1033 O PHE A 1042 ? O PHE A 1042 
T 1 2 N ASN A 1174 ? N ASN A 1174 O ASN A 1292 ? O ASN A 1292 
T 2 3 O TYR A 1297 ? O TYR A 1297 N ALA A 1279 ? N ALA A 1279 
T 3 4 O VAL A 1282 ? O VAL A 1282 N GLU A 1214 ? N GLU A 1214 
T 4 5 N ILE A 1213 ? N ILE A 1213 O LEU A 1251 ? O LEU A 1251 
T 5 6 O VAL A 1250 ? O VAL A 1250 N GLU A 1241 ? N GLU A 1241 
U 1 2 N GLU A 1181 ? N GLU A 1181 O LYS A 1194 ? O LYS A 1194 
U 2 3 N ALA A 1197 ? N ALA A 1197 O ASN A 1261 ? O ASN A 1261 
U 3 4 O TYR A 1268 ? O TYR A 1268 N VAL A 1222 ? N VAL A 1222 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG A 1326' 
AC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG A 1327' 
AC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG A 1328' 
AC4 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG A 1329' 
AC5 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG A 1330' 
AC6 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NA A 1331'  
AC7 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NA A 1332'  
AC8 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NA A 1333'  
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 4 ARG A 146  ? ARG A 146  . ? 1_555 ? 
2  AC1 4 ASN A 178  ? ASN A 178  . ? 1_555 ? 
3  AC1 4 GLU A 187  ? GLU A 187  . ? 1_555 ? 
4  AC1 4 SER A 190  ? SER A 190  . ? 1_555 ? 
5  AC2 4 VAL A 211  ? VAL A 211  . ? 1_555 ? 
6  AC2 4 HIS A 217  ? HIS A 217  . ? 1_555 ? 
7  AC2 4 ASN A 221  ? ASN A 221  . ? 1_555 ? 
8  AC2 4 GLU A 264  ? GLU A 264  . ? 1_555 ? 
9  AC3 4 TYR A 289  ? TYR A 289  . ? 1_555 ? 
10 AC3 4 ASN A 291  ? ASN A 291  . ? 1_555 ? 
11 AC3 4 SER A 1187 ? SER A 1187 . ? 1_555 ? 
12 AC3 4 TYR A 1189 ? TYR A 1189 . ? 1_555 ? 
13 AC4 4 TYR A 158  ? TYR A 158  . ? 1_555 ? 
14 AC4 4 ASN A 616  ? ASN A 616  . ? 1_555 ? 
15 AC4 4 VAL A 617  ? VAL A 617  . ? 1_555 ? 
16 AC4 4 NAG F .    ? NAG A 1330 . ? 1_555 ? 
17 AC5 1 NAG E .    ? NAG A 1329 . ? 1_555 ? 
18 AC6 6 SER A 900  ? SER A 900  . ? 1_555 ? 
19 AC6 6 VAL A 901  ? VAL A 901  . ? 1_555 ? 
20 AC6 6 PHE A 902  ? PHE A 902  . ? 1_555 ? 
21 AC6 6 LYS A 945  ? LYS A 945  . ? 1_555 ? 
22 AC6 6 ALA A 946  ? ALA A 946  . ? 1_555 ? 
23 AC6 6 GLN A 955  ? GLN A 955  . ? 1_555 ? 
24 AC7 1 GLU A 1040 ? GLU A 1040 . ? 1_555 ? 
25 AC8 4 LEU A 1275 ? LEU A 1275 . ? 1_555 ? 
26 AC8 4 LYS A 1276 ? LYS A 1276 . ? 1_555 ? 
27 AC8 4 LYS A 1301 ? LYS A 1301 . ? 1_555 ? 
28 AC8 4 GLN A 1302 ? GLN A 1302 . ? 1_555 ? 
# 
_atom_sites.entry_id                    2PN5 
_atom_sites.fract_transf_matrix[1][1]   0.006644 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.006644 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.004419 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
NA 
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   . LEU A 1 1    ? 39.732  84.365  141.075 1.00 75.76  ? 1    LEU A N   1 
ATOM   2     C  CA  . LEU A 1 1    ? 40.214  82.957  140.993 1.00 75.41  ? 1    LEU A CA  1 
ATOM   3     C  C   . LEU A 1 1    ? 41.746  82.913  140.978 1.00 73.27  ? 1    LEU A C   1 
ATOM   4     O  O   . LEU A 1 1    ? 42.390  83.776  140.381 1.00 73.15  ? 1    LEU A O   1 
ATOM   5     C  CB  . LEU A 1 1    ? 39.639  82.291  139.740 1.00 78.12  ? 1    LEU A CB  1 
ATOM   6     C  CG  . LEU A 1 1    ? 39.313  80.795  139.743 1.00 79.09  ? 1    LEU A CG  1 
ATOM   7     C  CD1 . LEU A 1 1    ? 38.132  80.484  140.653 1.00 79.79  ? 1    LEU A CD1 1 
ATOM   8     C  CD2 . LEU A 1 1    ? 39.022  80.321  138.333 1.00 81.36  ? 1    LEU A CD2 1 
ATOM   9     N  N   . LEU A 1 2    ? 42.322  81.925  141.662 1.00 71.90  ? 2    LEU A N   1 
ATOM   10    C  CA  . LEU A 1 2    ? 43.775  81.730  141.674 1.00 70.04  ? 2    LEU A CA  1 
ATOM   11    C  C   . LEU A 1 2    ? 44.131  80.288  141.326 1.00 70.27  ? 2    LEU A C   1 
ATOM   12    O  O   . LEU A 1 2    ? 43.772  79.355  142.048 1.00 70.36  ? 2    LEU A O   1 
ATOM   13    C  CB  . LEU A 1 2    ? 44.386  82.127  143.028 1.00 67.79  ? 2    LEU A CB  1 
ATOM   14    C  CG  . LEU A 1 2    ? 45.905  81.940  143.249 1.00 66.04  ? 2    LEU A CG  1 
ATOM   15    C  CD1 . LEU A 1 2    ? 46.759  82.616  142.179 1.00 65.46  ? 2    LEU A CD1 1 
ATOM   16    C  CD2 . LEU A 1 2    ? 46.320  82.434  144.631 1.00 64.60  ? 2    LEU A CD2 1 
ATOM   17    N  N   . VAL A 1 3    ? 44.839  80.122  140.214 1.00 70.53  ? 3    VAL A N   1 
ATOM   18    C  CA  . VAL A 1 3    ? 45.175  78.800  139.701 1.00 71.23  ? 3    VAL A CA  1 
ATOM   19    C  C   . VAL A 1 3    ? 46.670  78.596  139.830 1.00 69.17  ? 3    VAL A C   1 
ATOM   20    O  O   . VAL A 1 3    ? 47.455  79.389  139.313 1.00 68.41  ? 3    VAL A O   1 
ATOM   21    C  CB  . VAL A 1 3    ? 44.767  78.631  138.209 1.00 73.98  ? 3    VAL A CB  1 
ATOM   22    C  CG1 . VAL A 1 3    ? 45.080  77.226  137.726 1.00 74.94  ? 3    VAL A CG1 1 
ATOM   23    C  CG2 . VAL A 1 3    ? 43.287  78.936  138.002 1.00 76.21  ? 3    VAL A CG2 1 
ATOM   24    N  N   . VAL A 1 4    ? 47.060  77.531  140.520 1.00 68.45  ? 4    VAL A N   1 
ATOM   25    C  CA  . VAL A 1 4    ? 48.470  77.227  140.717 1.00 66.65  ? 4    VAL A CA  1 
ATOM   26    C  C   . VAL A 1 4    ? 48.727  75.748  140.460 1.00 68.06  ? 4    VAL A C   1 
ATOM   27    O  O   . VAL A 1 4    ? 48.128  74.886  141.108 1.00 68.87  ? 4    VAL A O   1 
ATOM   28    C  CB  . VAL A 1 4    ? 48.943  77.613  142.148 1.00 64.21  ? 4    VAL A CB  1 
ATOM   29    C  CG1 . VAL A 1 4    ? 50.368  77.146  142.404 1.00 61.87  ? 4    VAL A CG1 1 
ATOM   30    C  CG2 . VAL A 1 4    ? 48.822  79.114  142.379 1.00 62.90  ? 4    VAL A CG2 1 
ATOM   31    N  N   . GLY A 1 5    ? 49.605  75.468  139.501 1.00 68.66  ? 5    GLY A N   1 
ATOM   32    C  CA  . GLY A 1 5    ? 50.115  74.119  139.275 1.00 70.21  ? 5    GLY A CA  1 
ATOM   33    C  C   . GLY A 1 5    ? 51.613  74.132  138.999 1.00 69.58  ? 5    GLY A C   1 
ATOM   34    O  O   . GLY A 1 5    ? 52.186  75.199  138.758 1.00 67.91  ? 5    GLY A O   1 
ATOM   35    N  N   . PRO A 1 6    ? 52.260  72.947  139.031 1.00 70.60  ? 6    PRO A N   1 
ATOM   36    C  CA  . PRO A 1 6    ? 53.676  72.827  138.666 1.00 70.35  ? 6    PRO A CA  1 
ATOM   37    C  C   . PRO A 1 6    ? 53.910  73.194  137.198 1.00 72.55  ? 6    PRO A C   1 
ATOM   38    O  O   . PRO A 1 6    ? 52.982  73.122  136.387 1.00 74.77  ? 6    PRO A O   1 
ATOM   39    C  CB  . PRO A 1 6    ? 53.982  71.341  138.893 1.00 71.20  ? 6    PRO A CB  1 
ATOM   40    C  CG  . PRO A 1 6    ? 52.880  70.833  139.762 1.00 71.48  ? 6    PRO A CG  1 
ATOM   41    C  CD  . PRO A 1 6    ? 51.682  71.649  139.425 1.00 72.00  ? 6    PRO A CD  1 
ATOM   42    N  N   . LYS A 1 7    ? 55.134  73.594  136.863 1.00 72.33  ? 7    LYS A N   1 
ATOM   43    C  CA  . LYS A 1 7    ? 55.446  73.982  135.490 1.00 74.72  ? 7    LYS A CA  1 
ATOM   44    C  C   . LYS A 1 7    ? 56.128  72.851  134.730 1.00 76.65  ? 7    LYS A C   1 
ATOM   45    O  O   . LYS A 1 7    ? 56.168  72.844  133.498 1.00 78.40  ? 7    LYS A O   1 
ATOM   46    C  CB  . LYS A 1 7    ? 56.316  75.242  135.462 1.00 72.95  ? 7    LYS A CB  1 
ATOM   47    C  CG  . LYS A 1 7    ? 56.334  75.919  134.103 1.00 75.35  ? 7    LYS A CG  1 
ATOM   48    C  CD  . LYS A 1 7    ? 56.948  77.307  134.160 1.00 75.98  ? 7    LYS A CD  1 
ATOM   49    C  CE  . LYS A 1 7    ? 56.827  78.016  132.805 1.00 78.20  ? 7    LYS A CE  1 
ATOM   50    N  NZ  . LYS A 1 7    ? 55.470  78.593  132.571 1.00 79.27  ? 7    LYS A NZ  1 
ATOM   51    N  N   . PHE A 1 8    ? 56.651  71.888  135.477 1.00 76.86  ? 8    PHE A N   1 
ATOM   52    C  CA  . PHE A 1 8    ? 57.460  70.832  134.896 1.00 78.80  ? 8    PHE A CA  1 
ATOM   53    C  C   . PHE A 1 8    ? 56.748  69.479  134.965 1.00 81.37  ? 8    PHE A C   1 
ATOM   54    O  O   . PHE A 1 8    ? 56.161  69.122  135.993 1.00 81.21  ? 8    PHE A O   1 
ATOM   55    C  CB  . PHE A 1 8    ? 58.839  70.803  135.563 1.00 76.62  ? 8    PHE A CB  1 
ATOM   56    C  CG  . PHE A 1 8    ? 59.631  72.076  135.369 1.00 76.03  ? 8    PHE A CG  1 
ATOM   57    C  CD1 . PHE A 1 8    ? 59.353  73.217  136.128 1.00 75.20  ? 8    PHE A CD1 1 
ATOM   58    C  CD2 . PHE A 1 8    ? 60.653  72.142  134.417 1.00 77.17  ? 8    PHE A CD2 1 
ATOM   59    C  CE1 . PHE A 1 8    ? 60.081  74.403  135.945 1.00 74.23  ? 8    PHE A CE1 1 
ATOM   60    C  CE2 . PHE A 1 8    ? 61.388  73.321  134.226 1.00 75.64  ? 8    PHE A CE2 1 
ATOM   61    C  CZ  . PHE A 1 8    ? 61.102  74.452  134.991 1.00 74.35  ? 8    PHE A CZ  1 
ATOM   62    N  N   . ILE A 1 9    ? 56.798  68.747  133.853 1.00 84.15  ? 9    ILE A N   1 
ATOM   63    C  CA  . ILE A 1 9    ? 56.056  67.500  133.686 1.00 87.35  ? 9    ILE A CA  1 
ATOM   64    C  C   . ILE A 1 9    ? 56.986  66.299  133.510 1.00 88.54  ? 9    ILE A C   1 
ATOM   65    O  O   . ILE A 1 9    ? 58.012  66.401  132.834 1.00 88.19  ? 9    ILE A O   1 
ATOM   66    C  CB  . ILE A 1 9    ? 55.062  67.615  132.494 1.00 90.25  ? 9    ILE A CB  1 
ATOM   67    C  CG1 . ILE A 1 9    ? 53.692  68.089  132.981 1.00 90.75  ? 9    ILE A CG1 1 
ATOM   68    C  CG2 . ILE A 1 9    ? 54.895  66.295  131.759 1.00 93.66  ? 9    ILE A CG2 1 
ATOM   69    C  CD1 . ILE A 1 9    ? 53.618  69.563  133.288 1.00 88.88  ? 9    ILE A CD1 1 
ATOM   70    N  N   . ARG A 1 10   ? 56.616  65.173  134.126 1.00 90.26  ? 10   ARG A N   1 
ATOM   71    C  CA  . ARG A 1 10   ? 57.368  63.917  133.996 1.00 92.09  ? 10   ARG A CA  1 
ATOM   72    C  C   . ARG A 1 10   ? 56.530  62.715  133.532 1.00 96.20  ? 10   ARG A C   1 
ATOM   73    O  O   . ARG A 1 10   ? 55.315  62.816  133.365 1.00 97.80  ? 10   ARG A O   1 
ATOM   74    C  CB  . ARG A 1 10   ? 58.114  63.589  135.291 1.00 90.01  ? 10   ARG A CB  1 
ATOM   75    C  CG  . ARG A 1 10   ? 59.389  64.368  135.446 1.00 87.23  ? 10   ARG A CG  1 
ATOM   76    C  CD  . ARG A 1 10   ? 60.325  63.709  136.422 1.00 87.17  ? 10   ARG A CD  1 
ATOM   77    N  NE  . ARG A 1 10   ? 61.536  64.505  136.605 1.00 85.66  ? 10   ARG A NE  1 
ATOM   78    C  CZ  . ARG A 1 10   ? 61.643  65.539  137.436 1.00 83.80  ? 10   ARG A CZ  1 
ATOM   79    N  NH1 . ARG A 1 10   ? 60.610  65.921  138.181 1.00 83.76  ? 10   ARG A NH1 1 
ATOM   80    N  NH2 . ARG A 1 10   ? 62.792  66.195  137.528 1.00 81.96  ? 10   ARG A NH2 1 
ATOM   81    N  N   . ALA A 1 11   ? 57.204  61.582  133.336 1.00 98.20  ? 11   ALA A N   1 
ATOM   82    C  CA  . ALA A 1 11   ? 56.613  60.390  132.722 1.00 102.59 ? 11   ALA A CA  1 
ATOM   83    C  C   . ALA A 1 11   ? 55.563  59.671  133.574 1.00 104.51 ? 11   ALA A C   1 
ATOM   84    O  O   . ALA A 1 11   ? 54.608  59.109  133.032 1.00 107.96 ? 11   ALA A O   1 
ATOM   85    C  CB  . ALA A 1 11   ? 57.711  59.419  132.296 1.00 103.83 ? 11   ALA A CB  1 
ATOM   86    N  N   . ASN A 1 12   ? 55.735  59.676  134.894 1.00 102.57 ? 12   ASN A N   1 
ATOM   87    C  CA  . ASN A 1 12   ? 54.810  58.949  135.770 1.00 104.38 ? 12   ASN A CA  1 
ATOM   88    C  C   . ASN A 1 12   ? 54.213  59.756  136.912 1.00 101.98 ? 12   ASN A C   1 
ATOM   89    O  O   . ASN A 1 12   ? 53.113  59.446  137.375 1.00 103.67 ? 12   ASN A O   1 
ATOM   90    C  CB  . ASN A 1 12   ? 55.464  57.678  136.319 1.00 105.78 ? 12   ASN A CB  1 
ATOM   91    C  CG  . ASN A 1 12   ? 55.181  56.461  135.462 1.00 110.39 ? 12   ASN A CG  1 
ATOM   92    O  OD1 . ASN A 1 12   ? 56.094  55.862  134.895 1.00 112.07 ? 12   ASN A OD1 1 
ATOM   93    N  ND2 . ASN A 1 12   ? 53.910  56.090  135.360 1.00 113.27 ? 12   ASN A ND2 1 
ATOM   94    N  N   . GLN A 1 13   ? 54.937  60.782  137.361 1.00 98.25  ? 13   GLN A N   1 
ATOM   95    C  CA  . GLN A 1 13   ? 54.492  61.632  138.467 1.00 95.78  ? 13   GLN A CA  1 
ATOM   96    C  C   . GLN A 1 13   ? 53.062  62.138  138.269 1.00 96.36  ? 13   GLN A C   1 
ATOM   97    O  O   . GLN A 1 13   ? 52.675  62.514  137.159 1.00 97.43  ? 13   GLN A O   1 
ATOM   98    C  CB  . GLN A 1 13   ? 55.450  62.821  138.671 1.00 92.40  ? 13   GLN A CB  1 
ATOM   99    C  CG  . GLN A 1 13   ? 56.736  62.486  139.432 1.00 91.91  ? 13   GLN A CG  1 
ATOM   100   C  CD  . GLN A 1 13   ? 57.472  63.724  139.951 1.00 90.42  ? 13   GLN A CD  1 
ATOM   101   O  OE1 . GLN A 1 13   ? 57.012  64.404  140.873 1.00 89.98  ? 13   GLN A OE1 1 
ATOM   102   N  NE2 . GLN A 1 13   ? 58.635  64.004  139.373 1.00 90.06  ? 13   GLN A NE2 1 
ATOM   103   N  N   . GLU A 1 14   ? 52.281  62.125  139.349 1.00 95.62  ? 14   GLU A N   1 
ATOM   104   C  CA  . GLU A 1 14   ? 50.952  62.730  139.343 1.00 95.63  ? 14   GLU A CA  1 
ATOM   105   C  C   . GLU A 1 14   ? 51.054  64.252  139.317 1.00 92.02  ? 14   GLU A C   1 
ATOM   106   O  O   . GLU A 1 14   ? 51.741  64.855  140.148 1.00 89.19  ? 14   GLU A O   1 
ATOM   107   C  CB  . GLU A 1 14   ? 50.120  62.259  140.540 1.00 96.56  ? 14   GLU A CB  1 
ATOM   108   C  CG  . GLU A 1 14   ? 49.377  60.941  140.280 1.00 101.56 ? 14   GLU A CG  1 
ATOM   109   C  CD  . GLU A 1 14   ? 48.237  60.672  141.260 1.00 103.55 ? 14   GLU A CD  1 
ATOM   110   O  OE1 . GLU A 1 14   ? 47.969  61.527  142.135 1.00 101.75 ? 14   GLU A OE1 1 
ATOM   111   O  OE2 . GLU A 1 14   ? 47.607  59.596  141.150 1.00 106.86 ? 14   GLU A OE2 1 
ATOM   112   N  N   . TYR A 1 15   ? 50.392  64.862  138.337 1.00 92.04  ? 15   TYR A N   1 
ATOM   113   C  CA  . TYR A 1 15   ? 50.376  66.314  138.208 1.00 88.78  ? 15   TYR A CA  1 
ATOM   114   C  C   . TYR A 1 15   ? 49.169  66.871  138.946 1.00 88.04  ? 15   TYR A C   1 
ATOM   115   O  O   . TYR A 1 15   ? 48.024  66.575  138.597 1.00 90.48  ? 15   TYR A O   1 
ATOM   116   C  CB  . TYR A 1 15   ? 50.358  66.735  136.734 1.00 90.01  ? 15   TYR A CB  1 
ATOM   117   C  CG  . TYR A 1 15   ? 50.408  68.234  136.517 1.00 87.49  ? 15   TYR A CG  1 
ATOM   118   C  CD1 . TYR A 1 15   ? 51.627  68.896  136.378 1.00 85.01  ? 15   TYR A CD1 1 
ATOM   119   C  CD2 . TYR A 1 15   ? 49.235  68.990  136.451 1.00 87.61  ? 15   TYR A CD2 1 
ATOM   120   C  CE1 . TYR A 1 15   ? 51.677  70.272  136.180 1.00 83.53  ? 15   TYR A CE1 1 
ATOM   121   C  CE2 . TYR A 1 15   ? 49.271  70.362  136.254 1.00 85.81  ? 15   TYR A CE2 1 
ATOM   122   C  CZ  . TYR A 1 15   ? 50.493  70.998  136.117 1.00 84.29  ? 15   TYR A CZ  1 
ATOM   123   O  OH  . TYR A 1 15   ? 50.531  72.361  135.926 1.00 83.00  ? 15   TYR A OH  1 
ATOM   124   N  N   . THR A 1 16   ? 49.434  67.678  139.967 1.00 84.50  ? 16   THR A N   1 
ATOM   125   C  CA  . THR A 1 16   ? 48.373  68.212  140.808 1.00 83.56  ? 16   THR A CA  1 
ATOM   126   C  C   . THR A 1 16   ? 48.166  69.705  140.591 1.00 81.41  ? 16   THR A C   1 
ATOM   127   O  O   . THR A 1 16   ? 49.007  70.519  140.971 1.00 78.79  ? 16   THR A O   1 
ATOM   128   C  CB  . THR A 1 16   ? 48.640  67.931  142.304 1.00 82.12  ? 16   THR A CB  1 
ATOM   129   O  OG1 . THR A 1 16   ? 48.784  66.519  142.509 1.00 84.04  ? 16   THR A OG1 1 
ATOM   130   C  CG2 . THR A 1 16   ? 47.488  68.443  143.161 1.00 82.10  ? 16   THR A CG2 1 
ATOM   131   N  N   . LEU A 1 17   ? 47.039  70.053  139.982 1.00 82.44  ? 17   LEU A N   1 
ATOM   132   C  CA  . LEU A 1 17   ? 46.642  71.445  139.864 1.00 80.83  ? 17   LEU A CA  1 
ATOM   133   C  C   . LEU A 1 17   ? 45.808  71.843  141.066 1.00 79.93  ? 17   LEU A C   1 
ATOM   134   O  O   . LEU A 1 17   ? 45.016  71.052  141.578 1.00 81.27  ? 17   LEU A O   1 
ATOM   135   C  CB  . LEU A 1 17   ? 45.846  71.681  138.581 1.00 83.36  ? 17   LEU A CB  1 
ATOM   136   C  CG  . LEU A 1 17   ? 45.472  73.127  138.235 1.00 82.35  ? 17   LEU A CG  1 
ATOM   137   C  CD1 . LEU A 1 17   ? 46.694  73.923  137.803 1.00 79.90  ? 17   LEU A CD1 1 
ATOM   138   C  CD2 . LEU A 1 17   ? 44.404  73.155  137.154 1.00 85.01  ? 17   LEU A CD2 1 
ATOM   139   N  N   . VAL A 1 18   ? 46.002  73.075  141.519 1.00 77.57  ? 18   VAL A N   1 
ATOM   140   C  CA  . VAL A 1 18   ? 45.185  73.637  142.586 1.00 76.73  ? 18   VAL A CA  1 
ATOM   141   C  C   . VAL A 1 18   ? 44.517  74.909  142.073 1.00 77.17  ? 18   VAL A C   1 
ATOM   142   O  O   . VAL A 1 18   ? 45.177  75.800  141.521 1.00 76.23  ? 18   VAL A O   1 
ATOM   143   C  CB  . VAL A 1 18   ? 46.013  73.925  143.869 1.00 73.92  ? 18   VAL A CB  1 
ATOM   144   C  CG1 . VAL A 1 18   ? 45.144  74.554  144.950 1.00 72.91  ? 18   VAL A CG1 1 
ATOM   145   C  CG2 . VAL A 1 18   ? 46.657  72.650  144.386 1.00 73.33  ? 18   VAL A CG2 1 
ATOM   146   N  N   . ILE A 1 19   ? 43.202  74.966  142.237 1.00 78.79  ? 19   ILE A N   1 
ATOM   147   C  CA  . ILE A 1 19   ? 42.418  76.136  141.876 1.00 79.56  ? 19   ILE A CA  1 
ATOM   148   C  C   . ILE A 1 19   ? 41.769  76.654  143.151 1.00 78.90  ? 19   ILE A C   1 
ATOM   149   O  O   . ILE A 1 19   ? 41.120  75.892  143.858 1.00 79.65  ? 19   ILE A O   1 
ATOM   150   C  CB  . ILE A 1 19   ? 41.325  75.772  140.838 1.00 82.76  ? 19   ILE A CB  1 
ATOM   151   C  CG1 . ILE A 1 19   ? 41.961  75.283  139.531 1.00 83.50  ? 19   ILE A CG1 1 
ATOM   152   C  CG2 . ILE A 1 19   ? 40.382  76.954  140.593 1.00 83.72  ? 19   ILE A CG2 1 
ATOM   153   C  CD1 . ILE A 1 19   ? 40.987  74.622  138.567 1.00 86.58  ? 19   ILE A CD1 1 
ATOM   154   N  N   . SER A 1 20   ? 41.948  77.939  143.447 1.00 77.75  ? 20   SER A N   1 
ATOM   155   C  CA  . SER A 1 20   ? 41.356  78.537  144.642 1.00 77.41  ? 20   SER A CA  1 
ATOM   156   C  C   . SER A 1 20   ? 40.325  79.591  144.270 1.00 79.00  ? 20   SER A C   1 
ATOM   157   O  O   . SER A 1 20   ? 40.629  80.533  143.539 1.00 78.83  ? 20   SER A O   1 
ATOM   158   C  CB  . SER A 1 20   ? 42.432  79.136  145.552 1.00 74.79  ? 20   SER A CB  1 
ATOM   159   O  OG  . SER A 1 20   ? 43.558  78.274  145.668 1.00 74.46  ? 20   SER A OG  1 
ATOM   160   N  N   . ASN A 1 21   ? 39.104  79.415  144.774 1.00 80.91  ? 21   ASN A N   1 
ATOM   161   C  CA  . ASN A 1 21   ? 37.995  80.322  144.480 1.00 82.87  ? 21   ASN A CA  1 
ATOM   162   C  C   . ASN A 1 21   ? 37.683  81.230  145.658 1.00 82.15  ? 21   ASN A C   1 
ATOM   163   O  O   . ASN A 1 21   ? 37.085  80.806  146.645 1.00 82.50  ? 21   ASN A O   1 
ATOM   164   C  CB  . ASN A 1 21   ? 36.746  79.535  144.052 1.00 85.71  ? 21   ASN A CB  1 
ATOM   165   C  CG  . ASN A 1 21   ? 35.601  80.436  143.596 1.00 87.43  ? 21   ASN A CG  1 
ATOM   166   O  OD1 . ASN A 1 21   ? 35.795  81.619  143.309 1.00 86.51  ? 21   ASN A OD1 1 
ATOM   167   N  ND2 . ASN A 1 21   ? 34.398  79.870  143.527 1.00 89.87  ? 21   ASN A ND2 1 
ATOM   168   N  N   . PHE A 1 22   ? 38.095  82.485  145.540 1.00 81.86  ? 22   PHE A N   1 
ATOM   169   C  CA  . PHE A 1 22   ? 37.897  83.474  146.591 1.00 81.65  ? 22   PHE A CA  1 
ATOM   170   C  C   . PHE A 1 22   ? 36.888  84.524  146.156 1.00 84.12  ? 22   PHE A C   1 
ATOM   171   O  O   . PHE A 1 22   ? 36.689  85.526  146.846 1.00 83.65  ? 22   PHE A O   1 
ATOM   172   C  CB  . PHE A 1 22   ? 39.227  84.135  146.957 1.00 79.15  ? 22   PHE A CB  1 
ATOM   173   C  CG  . PHE A 1 22   ? 40.038  84.560  145.768 1.00 79.02  ? 22   PHE A CG  1 
ATOM   174   C  CD1 . PHE A 1 22   ? 41.015  83.717  145.241 1.00 77.84  ? 22   PHE A CD1 1 
ATOM   175   C  CD2 . PHE A 1 22   ? 39.821  85.798  145.162 1.00 79.86  ? 22   PHE A CD2 1 
ATOM   176   C  CE1 . PHE A 1 22   ? 41.770  84.103  144.136 1.00 77.38  ? 22   PHE A CE1 1 
ATOM   177   C  CE2 . PHE A 1 22   ? 40.569  86.188  144.054 1.00 79.43  ? 22   PHE A CE2 1 
ATOM   178   C  CZ  . PHE A 1 22   ? 41.548  85.338  143.543 1.00 78.40  ? 22   PHE A CZ  1 
ATOM   179   N  N   . ASN A 1 23   ? 36.268  84.291  145.000 1.00 87.34  ? 23   ASN A N   1 
ATOM   180   C  CA  . ASN A 1 23   ? 35.203  85.150  144.482 1.00 90.50  ? 23   ASN A CA  1 
ATOM   181   C  C   . ASN A 1 23   ? 33.917  85.001  145.277 1.00 92.26  ? 23   ASN A C   1 
ATOM   182   O  O   . ASN A 1 23   ? 33.424  83.888  145.460 1.00 93.17  ? 23   ASN A O   1 
ATOM   183   C  CB  . ASN A 1 23   ? 34.930  84.825  143.021 1.00 92.83  ? 23   ASN A CB  1 
ATOM   184   C  CG  . ASN A 1 23   ? 36.124  85.073  142.149 1.00 92.50  ? 23   ASN A CG  1 
ATOM   185   O  OD1 . ASN A 1 23   ? 36.836  84.140  141.771 1.00 92.64  ? 23   ASN A OD1 1 
ATOM   186   N  ND2 . ASN A 1 23   ? 36.370  86.341  141.834 1.00 93.24  ? 23   ASN A ND2 1 
ATOM   187   N  N   . SER A 1 24   ? 33.379  86.128  145.734 1.00 93.36  ? 24   SER A N   1 
ATOM   188   C  CA  . SER A 1 24   ? 32.200  86.138  146.605 1.00 95.23  ? 24   SER A CA  1 
ATOM   189   C  C   . SER A 1 24   ? 30.877  86.409  145.870 1.00 98.52  ? 24   SER A C   1 
ATOM   190   O  O   . SER A 1 24   ? 29.809  86.417  146.489 1.00 99.80  ? 24   SER A O   1 
ATOM   191   C  CB  . SER A 1 24   ? 32.398  87.136  147.759 1.00 93.90  ? 24   SER A CB  1 
ATOM   192   O  OG  . SER A 1 24   ? 32.875  88.386  147.277 1.00 94.83  ? 24   SER A OG  1 
ATOM   193   N  N   . GLN A 1 25   ? 30.950  86.617  144.555 1.00 100.37 ? 25   GLN A N   1 
ATOM   194   C  CA  . GLN A 1 25   ? 29.754  86.873  143.750 1.00 103.98 ? 25   GLN A CA  1 
ATOM   195   C  C   . GLN A 1 25   ? 28.892  85.612  143.666 1.00 105.99 ? 25   GLN A C   1 
ATOM   196   O  O   . GLN A 1 25   ? 27.835  85.531  144.302 1.00 107.30 ? 25   GLN A O   1 
ATOM   197   C  CB  . GLN A 1 25   ? 30.112  87.380  142.344 1.00 105.26 ? 25   GLN A CB  1 
ATOM   198   C  CG  . GLN A 1 25   ? 30.882  88.700  142.300 1.00 104.30 ? 25   GLN A CG  1 
ATOM   199   C  CD  . GLN A 1 25   ? 32.395  88.513  142.398 1.00 101.37 ? 25   GLN A CD  1 
ATOM   200   O  OE1 . GLN A 1 25   ? 32.931  88.213  143.465 1.00 98.79  ? 25   GLN A OE1 1 
ATOM   201   N  NE2 . GLN A 1 25   ? 33.087  88.704  141.281 1.00 101.71 ? 25   GLN A NE2 1 
ATOM   202   N  N   . LEU A 1 26   ? 29.362  84.628  142.899 1.00 106.42 ? 26   LEU A N   1 
ATOM   203   C  CA  . LEU A 1 26   ? 28.661  83.355  142.729 1.00 108.40 ? 26   LEU A CA  1 
ATOM   204   C  C   . LEU A 1 26   ? 28.810  82.437  143.944 1.00 106.71 ? 26   LEU A C   1 
ATOM   205   O  O   . LEU A 1 26   ? 29.608  82.707  144.852 1.00 103.86 ? 26   LEU A O   1 
ATOM   206   C  CB  . LEU A 1 26   ? 29.158  82.641  141.469 1.00 109.57 ? 26   LEU A CB  1 
ATOM   207   C  CG  . LEU A 1 26   ? 28.600  83.119  140.125 1.00 113.01 ? 26   LEU A CG  1 
ATOM   208   C  CD1 . LEU A 1 26   ? 29.660  82.999  139.032 1.00 113.26 ? 26   LEU A CD1 1 
ATOM   209   C  CD2 . LEU A 1 26   ? 27.324  82.366  139.745 1.00 116.46 ? 26   LEU A CD2 1 
ATOM   210   N  N   . SER A 1 27   ? 28.028  81.359  143.953 1.00 108.63 ? 27   SER A N   1 
ATOM   211   C  CA  . SER A 1 27   ? 28.131  80.327  144.984 1.00 107.54 ? 27   SER A CA  1 
ATOM   212   C  C   . SER A 1 27   ? 29.087  79.215  144.552 1.00 106.72 ? 27   SER A C   1 
ATOM   213   O  O   . SER A 1 27   ? 29.653  78.512  145.393 1.00 105.00 ? 27   SER A O   1 
ATOM   214   C  CB  . SER A 1 27   ? 26.754  79.749  145.320 1.00 110.42 ? 27   SER A CB  1 
ATOM   215   O  OG  . SER A 1 27   ? 26.192  79.090  144.199 1.00 113.56 ? 27   SER A OG  1 
ATOM   216   N  N   . LYS A 1 28   ? 29.243  79.059  143.239 1.00 108.00 ? 28   LYS A N   1 
ATOM   217   C  CA  . LYS A 1 28   ? 30.193  78.111  142.662 1.00 107.46 ? 28   LYS A CA  1 
ATOM   218   C  C   . LYS A 1 28   ? 30.678  78.617  141.305 1.00 107.96 ? 28   LYS A C   1 
ATOM   219   O  O   . LYS A 1 28   ? 30.024  79.457  140.686 1.00 109.85 ? 28   LYS A O   1 
ATOM   220   C  CB  . LYS A 1 28   ? 29.574  76.710  142.536 1.00 110.13 ? 28   LYS A CB  1 
ATOM   221   C  CG  . LYS A 1 28   ? 28.404  76.602  141.567 1.00 114.24 ? 28   LYS A CG  1 
ATOM   222   C  CD  . LYS A 1 28   ? 27.955  75.156  141.397 1.00 117.30 ? 28   LYS A CD  1 
ATOM   223   C  CE  . LYS A 1 28   ? 26.980  75.018  140.235 1.00 121.75 ? 28   LYS A CE  1 
ATOM   224   N  NZ  . LYS A 1 28   ? 26.597  73.602  139.980 1.00 125.08 ? 28   LYS A NZ  1 
ATOM   225   N  N   . VAL A 1 29   ? 31.828  78.116  140.860 1.00 106.41 ? 29   VAL A N   1 
ATOM   226   C  CA  . VAL A 1 29   ? 32.367  78.444  139.539 1.00 106.92 ? 29   VAL A CA  1 
ATOM   227   C  C   . VAL A 1 29   ? 32.601  77.152  138.751 1.00 108.59 ? 29   VAL A C   1 
ATOM   228   O  O   . VAL A 1 29   ? 33.039  76.143  139.312 1.00 107.65 ? 29   VAL A O   1 
ATOM   229   C  CB  . VAL A 1 29   ? 33.672  79.303  139.637 1.00 103.74 ? 29   VAL A CB  1 
ATOM   230   C  CG1 . VAL A 1 29   ? 34.345  79.477  138.276 1.00 104.23 ? 29   VAL A CG1 1 
ATOM   231   C  CG2 . VAL A 1 29   ? 33.371  80.670  140.248 1.00 102.72 ? 29   VAL A CG2 1 
ATOM   232   N  N   . ASP A 1 30   ? 32.286  77.189  137.457 1.00 111.19 ? 30   ASP A N   1 
ATOM   233   C  CA  . ASP A 1 30   ? 32.455  76.042  136.570 1.00 113.30 ? 30   ASP A CA  1 
ATOM   234   C  C   . ASP A 1 30   ? 33.624  76.266  135.619 1.00 112.23 ? 30   ASP A C   1 
ATOM   235   O  O   . ASP A 1 30   ? 33.793  77.362  135.085 1.00 112.01 ? 30   ASP A O   1 
ATOM   236   C  CB  . ASP A 1 30   ? 31.163  75.780  135.794 1.00 117.87 ? 30   ASP A CB  1 
ATOM   237   C  CG  . ASP A 1 30   ? 30.047  75.261  136.684 1.00 119.41 ? 30   ASP A CG  1 
ATOM   238   O  OD1 . ASP A 1 30   ? 30.131  74.092  137.119 1.00 119.91 ? 30   ASP A OD1 1 
ATOM   239   O  OD2 . ASP A 1 30   ? 29.086  76.019  136.949 1.00 120.55 ? 30   ASP A OD2 1 
ATOM   240   N  N   . LEU A 1 31   ? 34.433  75.229  135.415 1.00 111.72 ? 31   LEU A N   1 
ATOM   241   C  CA  . LEU A 1 31   ? 35.669  75.363  134.644 1.00 110.35 ? 31   LEU A CA  1 
ATOM   242   C  C   . LEU A 1 31   ? 35.944  74.186  133.713 1.00 112.78 ? 31   LEU A C   1 
ATOM   243   O  O   . LEU A 1 31   ? 35.633  73.036  134.029 1.00 114.02 ? 31   LEU A O   1 
ATOM   244   C  CB  . LEU A 1 31   ? 36.871  75.574  135.579 1.00 105.98 ? 31   LEU A CB  1 
ATOM   245   C  CG  . LEU A 1 31   ? 36.932  76.830  136.460 1.00 102.98 ? 31   LEU A CG  1 
ATOM   246   C  CD1 . LEU A 1 31   ? 37.851  76.610  137.652 1.00 99.61  ? 31   LEU A CD1 1 
ATOM   247   C  CD2 . LEU A 1 31   ? 37.363  78.057  135.673 1.00 102.17 ? 31   LEU A CD2 1 
ATOM   248   N  N   . LEU A 1 32   ? 36.531  74.498  132.561 1.00 113.63 ? 32   LEU A N   1 
ATOM   249   C  CA  . LEU A 1 32   ? 37.006  73.498  131.614 1.00 115.76 ? 32   LEU A CA  1 
ATOM   250   C  C   . LEU A 1 32   ? 38.525  73.472  131.690 1.00 112.67 ? 32   LEU A C   1 
ATOM   251   O  O   . LEU A 1 32   ? 39.170  74.522  131.677 1.00 110.23 ? 32   LEU A O   1 
ATOM   252   C  CB  . LEU A 1 32   ? 36.540  73.838  130.192 1.00 119.41 ? 32   LEU A CB  1 
ATOM   253   C  CG  . LEU A 1 32   ? 36.813  72.849  129.053 1.00 122.36 ? 32   LEU A CG  1 
ATOM   254   C  CD1 . LEU A 1 32   ? 35.896  71.635  129.139 1.00 125.63 ? 32   LEU A CD1 1 
ATOM   255   C  CD2 . LEU A 1 32   ? 36.658  73.535  127.705 1.00 124.82 ? 32   LEU A CD2 1 
ATOM   256   N  N   . LEU A 1 33   ? 39.091  72.272  131.776 1.00 113.03 ? 33   LEU A N   1 
ATOM   257   C  CA  . LEU A 1 33   ? 40.530  72.117  131.979 1.00 110.43 ? 33   LEU A CA  1 
ATOM   258   C  C   . LEU A 1 33   ? 41.195  71.284  130.884 1.00 112.79 ? 33   LEU A C   1 
ATOM   259   O  O   . LEU A 1 33   ? 41.344  70.068  131.020 1.00 114.03 ? 33   LEU A O   1 
ATOM   260   C  CB  . LEU A 1 33   ? 40.820  71.509  133.360 1.00 107.87 ? 33   LEU A CB  1 
ATOM   261   C  CG  . LEU A 1 33   ? 40.176  72.122  134.610 1.00 105.75 ? 33   LEU A CG  1 
ATOM   262   C  CD1 . LEU A 1 33   ? 40.367  71.201  135.801 1.00 104.41 ? 33   LEU A CD1 1 
ATOM   263   C  CD2 . LEU A 1 33   ? 40.718  73.509  134.915 1.00 102.27 ? 33   LEU A CD2 1 
ATOM   264   N  N   . LYS A 1 34   ? 41.590  71.944  129.799 1.00 113.88 ? 34   LYS A N   1 
ATOM   265   C  CA  . LYS A 1 34   ? 42.311  71.282  128.717 1.00 115.96 ? 34   LYS A CA  1 
ATOM   266   C  C   . LYS A 1 34   ? 43.791  71.146  129.062 1.00 112.73 ? 34   LYS A C   1 
ATOM   267   O  O   . LYS A 1 34   ? 44.428  72.115  129.477 1.00 109.62 ? 34   LYS A O   1 
ATOM   268   C  CB  . LYS A 1 34   ? 42.147  72.052  127.404 1.00 118.43 ? 34   LYS A CB  1 
ATOM   269   C  CG  . LYS A 1 34   ? 40.827  71.808  126.682 1.00 123.50 ? 34   LYS A CG  1 
ATOM   270   C  CD  . LYS A 1 34   ? 40.872  72.358  125.256 1.00 126.82 ? 34   LYS A CD  1 
ATOM   271   C  CE  . LYS A 1 34   ? 39.696  71.861  124.410 1.00 132.69 ? 34   LYS A CE  1 
ATOM   272   N  NZ  . LYS A 1 34   ? 38.392  72.487  124.782 1.00 133.61 ? 34   LYS A NZ  1 
ATOM   273   N  N   . LEU A 1 35   ? 44.326  69.939  128.897 1.00 113.81 ? 35   LEU A N   1 
ATOM   274   C  CA  . LEU A 1 35   ? 45.754  69.686  129.094 1.00 111.26 ? 35   LEU A CA  1 
ATOM   275   C  C   . LEU A 1 35   ? 46.306  68.969  127.862 1.00 114.06 ? 35   LEU A C   1 
ATOM   276   O  O   . LEU A 1 35   ? 46.064  67.773  127.666 1.00 116.68 ? 35   LEU A O   1 
ATOM   277   C  CB  . LEU A 1 35   ? 45.982  68.854  130.357 1.00 109.32 ? 35   LEU A CB  1 
ATOM   278   C  CG  . LEU A 1 35   ? 47.314  68.976  131.100 1.00 105.36 ? 35   LEU A CG  1 
ATOM   279   C  CD1 . LEU A 1 35   ? 47.169  68.361  132.471 1.00 104.18 ? 35   LEU A CD1 1 
ATOM   280   C  CD2 . LEU A 1 35   ? 48.481  68.333  130.357 1.00 105.67 ? 35   LEU A CD2 1 
ATOM   281   N  N   . GLU A 1 36   ? 47.041  69.711  127.035 1.00 113.72 ? 36   GLU A N   1 
ATOM   282   C  CA  . GLU A 1 36   ? 47.454  69.226  125.716 1.00 116.78 ? 36   GLU A CA  1 
ATOM   283   C  C   . GLU A 1 36   ? 48.951  69.395  125.491 1.00 114.47 ? 36   GLU A C   1 
ATOM   284   O  O   . GLU A 1 36   ? 49.764  68.866  126.247 1.00 112.12 ? 36   GLU A O   1 
ATOM   285   C  CB  . GLU A 1 36   ? 46.669  69.946  124.610 1.00 119.85 ? 36   GLU A CB  1 
ATOM   286   C  CG  . GLU A 1 36   ? 45.142  69.878  124.762 1.00 122.80 ? 36   GLU A CG  1 
ATOM   287   C  CD  . GLU A 1 36   ? 44.384  70.459  123.567 1.00 127.46 ? 36   GLU A CD  1 
ATOM   288   O  OE1 . GLU A 1 36   ? 44.820  71.496  123.019 1.00 127.23 ? 36   GLU A OE1 1 
ATOM   289   O  OE2 . GLU A 1 36   ? 43.342  69.880  123.181 1.00 130.90 ? 36   GLU A OE2 1 
ATOM   290   N  N   . LEU A 1 43   ? 53.429  68.457  120.507 1.00 132.12 ? 43   LEU A N   1 
ATOM   291   C  CA  . LEU A 1 43   ? 52.901  67.325  119.748 1.00 136.54 ? 43   LEU A CA  1 
ATOM   292   C  C   . LEU A 1 43   ? 51.618  66.771  120.384 1.00 137.83 ? 43   LEU A C   1 
ATOM   293   O  O   . LEU A 1 43   ? 51.333  67.033  121.559 1.00 134.79 ? 43   LEU A O   1 
ATOM   294   C  CB  . LEU A 1 43   ? 53.971  66.231  119.594 1.00 136.78 ? 43   LEU A CB  1 
ATOM   295   C  CG  . LEU A 1 43   ? 55.181  66.517  118.689 1.00 136.71 ? 43   LEU A CG  1 
ATOM   296   C  CD1 . LEU A 1 43   ? 56.368  65.633  119.055 1.00 134.67 ? 43   LEU A CD1 1 
ATOM   297   C  CD2 . LEU A 1 43   ? 54.830  66.372  117.203 1.00 141.72 ? 43   LEU A CD2 1 
ATOM   298   N  N   . SER A 1 44   ? 50.852  66.008  119.602 1.00 142.45 ? 44   SER A N   1 
ATOM   299   C  CA  . SER A 1 44   ? 49.538  65.498  120.030 1.00 144.49 ? 44   SER A CA  1 
ATOM   300   C  C   . SER A 1 44   ? 49.604  64.142  120.751 1.00 144.72 ? 44   SER A C   1 
ATOM   301   O  O   . SER A 1 44   ? 49.020  63.150  120.297 1.00 148.78 ? 44   SER A O   1 
ATOM   302   C  CB  . SER A 1 44   ? 48.571  65.438  118.838 1.00 149.69 ? 44   SER A CB  1 
ATOM   303   O  OG  . SER A 1 44   ? 49.147  64.742  117.747 1.00 152.73 ? 44   SER A OG  1 
ATOM   304   N  N   . VAL A 1 45   ? 50.305  64.121  121.886 1.00 140.44 ? 45   VAL A N   1 
ATOM   305   C  CA  . VAL A 1 45   ? 50.516  62.896  122.672 1.00 140.16 ? 45   VAL A CA  1 
ATOM   306   C  C   . VAL A 1 45   ? 49.620  62.847  123.923 1.00 138.53 ? 45   VAL A C   1 
ATOM   307   O  O   . VAL A 1 45   ? 49.183  61.770  124.341 1.00 140.48 ? 45   VAL A O   1 
ATOM   308   C  CB  . VAL A 1 45   ? 52.019  62.704  123.044 1.00 137.07 ? 45   VAL A CB  1 
ATOM   309   C  CG1 . VAL A 1 45   ? 52.227  61.445  123.886 1.00 137.35 ? 45   VAL A CG1 1 
ATOM   310   C  CG2 . VAL A 1 45   ? 52.885  62.643  121.781 1.00 138.74 ? 45   VAL A CG2 1 
ATOM   311   N  N   . LEU A 1 46   ? 49.352  64.012  124.509 1.00 135.03 ? 46   LEU A N   1 
ATOM   312   C  CA  . LEU A 1 46   ? 48.380  64.126  125.597 1.00 133.59 ? 46   LEU A CA  1 
ATOM   313   C  C   . LEU A 1 46   ? 47.103  64.819  125.145 1.00 135.36 ? 46   LEU A C   1 
ATOM   314   O  O   . LEU A 1 46   ? 47.150  65.792  124.392 1.00 135.41 ? 46   LEU A O   1 
ATOM   315   C  CB  . LEU A 1 46   ? 48.970  64.880  126.791 1.00 128.62 ? 46   LEU A CB  1 
ATOM   316   C  CG  . LEU A 1 46   ? 49.501  64.068  127.975 1.00 126.65 ? 46   LEU A CG  1 
ATOM   317   C  CD1 . LEU A 1 46   ? 49.955  65.014  129.069 1.00 121.96 ? 46   LEU A CD1 1 
ATOM   318   C  CD2 . LEU A 1 46   ? 48.453  63.093  128.515 1.00 129.27 ? 46   LEU A CD2 1 
ATOM   319   N  N   . ASN A 1 47   ? 45.966  64.316  125.619 1.00 136.81 ? 47   ASN A N   1 
ATOM   320   C  CA  . ASN A 1 47   ? 44.670  64.905  125.304 1.00 138.62 ? 47   ASN A CA  1 
ATOM   321   C  C   . ASN A 1 47   ? 43.660  64.657  126.419 1.00 138.09 ? 47   ASN A C   1 
ATOM   322   O  O   . ASN A 1 47   ? 42.661  63.962  126.228 1.00 141.82 ? 47   ASN A O   1 
ATOM   323   C  CB  . ASN A 1 47   ? 44.148  64.375  123.962 1.00 144.06 ? 47   ASN A CB  1 
ATOM   324   C  CG  . ASN A 1 47   ? 43.133  65.305  123.317 1.00 146.28 ? 47   ASN A CG  1 
ATOM   325   O  OD1 . ASN A 1 47   ? 43.120  66.510  123.579 1.00 143.69 ? 47   ASN A OD1 1 
ATOM   326   N  ND2 . ASN A 1 47   ? 42.278  64.748  122.460 1.00 151.25 ? 47   ASN A ND2 1 
ATOM   327   N  N   . VAL A 1 48   ? 43.932  65.237  127.586 1.00 133.48 ? 48   VAL A N   1 
ATOM   328   C  CA  . VAL A 1 48   ? 43.097  65.033  128.771 1.00 132.49 ? 48   VAL A CA  1 
ATOM   329   C  C   . VAL A 1 48   ? 42.320  66.303  129.138 1.00 130.67 ? 48   VAL A C   1 
ATOM   330   O  O   . VAL A 1 48   ? 42.899  67.387  129.258 1.00 127.40 ? 48   VAL A O   1 
ATOM   331   C  CB  . VAL A 1 48   ? 43.936  64.533  129.980 1.00 129.26 ? 48   VAL A CB  1 
ATOM   332   C  CG1 . VAL A 1 48   ? 43.046  64.232  131.179 1.00 129.28 ? 48   VAL A CG1 1 
ATOM   333   C  CG2 . VAL A 1 48   ? 44.734  63.291  129.603 1.00 131.00 ? 48   VAL A CG2 1 
ATOM   334   N  N   . THR A 1 49   ? 41.007  66.148  129.306 1.00 132.81 ? 49   THR A N   1 
ATOM   335   C  CA  . THR A 1 49   ? 40.111  67.247  129.671 1.00 131.60 ? 49   THR A CA  1 
ATOM   336   C  C   . THR A 1 49   ? 39.233  66.842  130.856 1.00 131.28 ? 49   THR A C   1 
ATOM   337   O  O   . THR A 1 49   ? 38.874  65.671  130.995 1.00 133.80 ? 49   THR A O   1 
ATOM   338   C  CB  . THR A 1 49   ? 39.202  67.651  128.489 1.00 135.52 ? 49   THR A CB  1 
ATOM   339   O  OG1 . THR A 1 49   ? 39.934  67.563  127.260 1.00 137.02 ? 49   THR A OG1 1 
ATOM   340   C  CG2 . THR A 1 49   ? 38.680  69.073  128.664 1.00 134.07 ? 49   THR A CG2 1 
ATOM   341   N  N   . LYS A 1 50   ? 38.894  67.812  131.704 1.00 128.27 ? 50   LYS A N   1 
ATOM   342   C  CA  . LYS A 1 50   ? 38.051  67.567  132.875 1.00 127.77 ? 50   LYS A CA  1 
ATOM   343   C  C   . LYS A 1 50   ? 37.075  68.711  133.155 1.00 127.13 ? 50   LYS A C   1 
ATOM   344   O  O   . LYS A 1 50   ? 37.484  69.851  133.383 1.00 124.03 ? 50   LYS A O   1 
ATOM   345   C  CB  . LYS A 1 50   ? 38.908  67.279  134.117 1.00 124.19 ? 50   LYS A CB  1 
ATOM   346   C  CG  . LYS A 1 50   ? 39.387  65.835  134.230 1.00 125.77 ? 50   LYS A CG  1 
ATOM   347   C  CD  . LYS A 1 50   ? 40.231  65.600  135.477 1.00 122.48 ? 50   LYS A CD  1 
ATOM   348   C  CE  . LYS A 1 50   ? 40.579  64.123  135.625 1.00 124.53 ? 50   LYS A CE  1 
ATOM   349   N  NZ  . LYS A 1 50   ? 41.318  63.828  136.883 1.00 121.54 ? 50   LYS A NZ  1 
ATOM   350   N  N   . MET A 1 51   ? 35.783  68.392  133.125 1.00 130.16 ? 51   MET A N   1 
ATOM   351   C  CA  . MET A 1 51   ? 34.730  69.332  133.511 1.00 129.89 ? 51   MET A CA  1 
ATOM   352   C  C   . MET A 1 51   ? 34.660  69.416  135.037 1.00 126.50 ? 51   MET A C   1 
ATOM   353   O  O   . MET A 1 51   ? 34.223  68.477  135.703 1.00 127.67 ? 51   MET A O   1 
ATOM   354   C  CB  . MET A 1 51   ? 33.377  68.925  132.899 1.00 134.99 ? 51   MET A CB  1 
ATOM   355   C  CG  . MET A 1 51   ? 33.052  67.425  132.961 1.00 138.77 ? 51   MET A CG  1 
ATOM   356   S  SD  . MET A 1 51   ? 31.368  67.013  132.440 1.00 146.70 ? 51   MET A SD  1 
ATOM   357   C  CE  . MET A 1 51   ? 31.543  66.869  130.657 1.00 149.92 ? 51   MET A CE  1 
ATOM   358   N  N   . VAL A 1 52   ? 35.100  70.544  135.587 1.00 122.37 ? 52   VAL A N   1 
ATOM   359   C  CA  . VAL A 1 52   ? 35.349  70.641  137.026 1.00 118.69 ? 52   VAL A CA  1 
ATOM   360   C  C   . VAL A 1 52   ? 34.582  71.754  137.737 1.00 117.21 ? 52   VAL A C   1 
ATOM   361   O  O   . VAL A 1 52   ? 34.366  72.833  137.184 1.00 117.03 ? 52   VAL A O   1 
ATOM   362   C  CB  . VAL A 1 52   ? 36.875  70.697  137.318 1.00 115.11 ? 52   VAL A CB  1 
ATOM   363   C  CG1 . VAL A 1 52   ? 37.196  71.509  138.571 1.00 111.43 ? 52   VAL A CG1 1 
ATOM   364   C  CG2 . VAL A 1 52   ? 37.436  69.285  137.423 1.00 115.81 ? 52   VAL A CG2 1 
ATOM   365   N  N   . ASP A 1 53   ? 34.188  71.463  138.975 1.00 116.14 ? 53   ASP A N   1 
ATOM   366   C  CA  . ASP A 1 53   ? 33.379  72.345  139.807 1.00 115.10 ? 53   ASP A CA  1 
ATOM   367   C  C   . ASP A 1 53   ? 34.192  72.836  141.012 1.00 110.86 ? 53   ASP A C   1 
ATOM   368   O  O   . ASP A 1 53   ? 34.836  72.036  141.695 1.00 109.70 ? 53   ASP A O   1 
ATOM   369   C  CB  . ASP A 1 53   ? 32.141  71.570  140.280 1.00 118.06 ? 53   ASP A CB  1 
ATOM   370   C  CG  . ASP A 1 53   ? 31.079  72.459  140.911 1.00 118.44 ? 53   ASP A CG  1 
ATOM   371   O  OD1 . ASP A 1 53   ? 31.261  73.695  140.953 1.00 116.95 ? 53   ASP A OD1 1 
ATOM   372   O  OD2 . ASP A 1 53   ? 30.049  71.911  141.365 1.00 120.73 ? 53   ASP A OD2 1 
ATOM   373   N  N   . VAL A 1 54   ? 34.172  74.147  141.262 1.00 108.68 ? 54   VAL A N   1 
ATOM   374   C  CA  . VAL A 1 54   ? 34.826  74.719  142.451 1.00 104.93 ? 54   VAL A CA  1 
ATOM   375   C  C   . VAL A 1 54   ? 33.900  75.683  143.197 1.00 104.58 ? 54   VAL A C   1 
ATOM   376   O  O   . VAL A 1 54   ? 33.450  76.688  142.644 1.00 105.03 ? 54   VAL A O   1 
ATOM   377   C  CB  . VAL A 1 54   ? 36.170  75.435  142.130 1.00 102.21 ? 54   VAL A CB  1 
ATOM   378   C  CG1 . VAL A 1 54   ? 36.931  75.740  143.418 1.00 98.71  ? 54   VAL A CG1 1 
ATOM   379   C  CG2 . VAL A 1 54   ? 37.040  74.598  141.200 1.00 102.77 ? 54   VAL A CG2 1 
ATOM   380   N  N   . ARG A 1 55   ? 33.635  75.367  144.461 1.00 103.82 ? 55   ARG A N   1 
ATOM   381   C  CA  . ARG A 1 55   ? 32.725  76.152  145.290 1.00 103.82 ? 55   ARG A CA  1 
ATOM   382   C  C   . ARG A 1 55   ? 33.400  77.392  145.862 1.00 100.66 ? 55   ARG A C   1 
ATOM   383   O  O   . ARG A 1 55   ? 34.626  77.448  145.955 1.00 98.34  ? 55   ARG A O   1 
ATOM   384   C  CB  . ARG A 1 55   ? 32.138  75.280  146.407 1.00 104.69 ? 55   ARG A CB  1 
ATOM   385   C  CG  . ARG A 1 55   ? 31.175  74.220  145.889 1.00 108.90 ? 55   ARG A CG  1 
ATOM   386   C  CD  . ARG A 1 55   ? 30.696  73.279  146.981 1.00 111.04 ? 55   ARG A CD  1 
ATOM   387   N  NE  . ARG A 1 55   ? 29.699  72.336  146.469 1.00 115.78 ? 55   ARG A NE  1 
ATOM   388   C  CZ  . ARG A 1 55   ? 29.131  71.364  147.182 1.00 117.93 ? 55   ARG A CZ  1 
ATOM   389   N  NH1 . ARG A 1 55   ? 29.453  71.185  148.459 1.00 116.72 ? 55   ARG A NH1 1 
ATOM   390   N  NH2 . ARG A 1 55   ? 28.238  70.563  146.615 1.00 121.40 ? 55   ARG A NH2 1 
ATOM   391   N  N   . ARG A 1 56   ? 32.592  78.383  146.237 1.00 100.82 ? 56   ARG A N   1 
ATOM   392   C  CA  . ARG A 1 56   ? 33.103  79.635  146.790 1.00 98.51  ? 56   ARG A CA  1 
ATOM   393   C  C   . ARG A 1 56   ? 33.781  79.410  148.139 1.00 95.84  ? 56   ARG A C   1 
ATOM   394   O  O   . ARG A 1 56   ? 33.422  78.495  148.881 1.00 96.30  ? 56   ARG A O   1 
ATOM   395   C  CB  . ARG A 1 56   ? 31.994  80.695  146.893 1.00 99.93  ? 56   ARG A CB  1 
ATOM   396   C  CG  . ARG A 1 56   ? 31.140  80.621  148.149 1.00 102.02 ? 56   ARG A CG  1 
ATOM   397   C  CD  . ARG A 1 56   ? 29.738  81.171  147.916 1.00 107.61 ? 56   ARG A CD  1 
ATOM   398   N  NE  . ARG A 1 56   ? 29.649  82.625  148.061 1.00 108.68 ? 56   ARG A NE  1 
ATOM   399   C  CZ  . ARG A 1 56   ? 28.912  83.248  148.981 1.00 109.73 ? 56   ARG A CZ  1 
ATOM   400   N  NH1 . ARG A 1 56   ? 28.183  82.555  149.853 1.00 110.39 ? 56   ARG A NH1 1 
ATOM   401   N  NH2 . ARG A 1 56   ? 28.900  84.575  149.026 1.00 109.72 ? 56   ARG A NH2 1 
ATOM   402   N  N   . ASN A 1 57   ? 34.775  80.244  148.432 1.00 93.18  ? 57   ASN A N   1 
ATOM   403   C  CA  . ASN A 1 57   ? 35.558  80.150  149.660 1.00 90.60  ? 57   ASN A CA  1 
ATOM   404   C  C   . ASN A 1 57   ? 36.162  78.764  149.889 1.00 90.26  ? 57   ASN A C   1 
ATOM   405   O  O   . ASN A 1 57   ? 36.233  78.288  151.026 1.00 89.86  ? 57   ASN A O   1 
ATOM   406   C  CB  . ASN A 1 57   ? 34.727  80.602  150.867 1.00 90.77  ? 57   ASN A CB  1 
ATOM   407   C  CG  . ASN A 1 57   ? 34.402  82.085  150.834 1.00 90.24  ? 57   ASN A CG  1 
ATOM   408   O  OD1 . ASN A 1 57   ? 34.771  82.798  149.904 1.00 89.46  ? 57   ASN A OD1 1 
ATOM   409   N  ND2 . ASN A 1 57   ? 33.711  82.556  151.862 1.00 90.52  ? 57   ASN A ND2 1 
ATOM   410   N  N   . MET A 1 58   ? 36.590  78.125  148.799 1.00 90.57  ? 58   MET A N   1 
ATOM   411   C  CA  . MET A 1 58   ? 37.222  76.804  148.843 1.00 90.50  ? 58   MET A CA  1 
ATOM   412   C  C   . MET A 1 58   ? 38.241  76.647  147.722 1.00 89.65  ? 58   MET A C   1 
ATOM   413   O  O   . MET A 1 58   ? 38.275  77.450  146.786 1.00 89.67  ? 58   MET A O   1 
ATOM   414   C  CB  . MET A 1 58   ? 36.176  75.695  148.699 1.00 93.46  ? 58   MET A CB  1 
ATOM   415   C  CG  . MET A 1 58   ? 35.275  75.481  149.902 1.00 95.11  ? 58   MET A CG  1 
ATOM   416   S  SD  . MET A 1 58   ? 34.203  74.052  149.671 1.00 100.72 ? 58   MET A SD  1 
ATOM   417   C  CE  . MET A 1 58   ? 35.276  72.735  150.252 1.00 100.06 ? 58   MET A CE  1 
ATOM   418   N  N   . ASN A 1 59   ? 39.070  75.611  147.820 1.00 88.88  ? 59   ASN A N   1 
ATOM   419   C  CA  . ASN A 1 59   ? 39.864  75.186  146.672 1.00 88.78  ? 59   ASN A CA  1 
ATOM   420   C  C   . ASN A 1 59   ? 39.730  73.709  146.320 1.00 90.68  ? 59   ASN A C   1 
ATOM   421   O  O   . ASN A 1 59   ? 39.579  72.859  147.197 1.00 91.29  ? 59   ASN A O   1 
ATOM   422   C  CB  . ASN A 1 59   ? 41.342  75.667  146.742 1.00 86.17  ? 59   ASN A CB  1 
ATOM   423   C  CG  . ASN A 1 59   ? 42.167  75.004  147.840 1.00 84.13  ? 59   ASN A CG  1 
ATOM   424   O  OD1 . ASN A 1 59   ? 42.980  75.667  148.482 1.00 81.14  ? 59   ASN A OD1 1 
ATOM   425   N  ND2 . ASN A 1 59   ? 42.004  73.698  148.026 1.00 85.61  ? 59   ASN A ND2 1 
ATOM   426   N  N   . ARG A 1 60   ? 39.750  73.421  145.025 1.00 92.03  ? 60   ARG A N   1 
ATOM   427   C  CA  . ARG A 1 60   ? 39.796  72.051  144.539 1.00 93.99  ? 60   ARG A CA  1 
ATOM   428   C  C   . ARG A 1 60   ? 41.214  71.661  144.165 1.00 92.35  ? 60   ARG A C   1 
ATOM   429   O  O   . ARG A 1 60   ? 42.017  72.502  143.763 1.00 90.52  ? 60   ARG A O   1 
ATOM   430   C  CB  . ARG A 1 60   ? 38.887  71.865  143.326 1.00 97.15  ? 60   ARG A CB  1 
ATOM   431   C  CG  . ARG A 1 60   ? 37.592  71.127  143.622 1.00 100.79 ? 60   ARG A CG  1 
ATOM   432   C  CD  . ARG A 1 60   ? 37.384  70.024  142.596 1.00 104.79 ? 60   ARG A CD  1 
ATOM   433   N  NE  . ARG A 1 60   ? 36.025  69.490  142.589 1.00 108.76 ? 60   ARG A NE  1 
ATOM   434   C  CZ  . ARG A 1 60   ? 35.603  68.540  141.756 1.00 112.79 ? 60   ARG A CZ  1 
ATOM   435   N  NH1 . ARG A 1 60   ? 36.437  68.012  140.865 1.00 113.10 ? 60   ARG A NH1 1 
ATOM   436   N  NH2 . ARG A 1 60   ? 34.346  68.114  141.810 1.00 116.19 ? 60   ARG A NH2 1 
ATOM   437   N  N   . MET A 1 61   ? 41.514  70.377  144.309 1.00 93.20  ? 61   MET A N   1 
ATOM   438   C  CA  . MET A 1 61   ? 42.775  69.819  143.857 1.00 92.20  ? 61   MET A CA  1 
ATOM   439   C  C   . MET A 1 61   ? 42.463  68.770  142.805 1.00 95.31  ? 61   MET A C   1 
ATOM   440   O  O   . MET A 1 61   ? 41.724  67.821  143.067 1.00 97.64  ? 61   MET A O   1 
ATOM   441   C  CB  . MET A 1 61   ? 43.553  69.207  145.023 1.00 90.67  ? 61   MET A CB  1 
ATOM   442   C  CG  . MET A 1 61   ? 43.946  70.214  146.098 1.00 87.67  ? 61   MET A CG  1 
ATOM   443   S  SD  . MET A 1 61   ? 44.799  69.510  147.525 1.00 86.06  ? 61   MET A SD  1 
ATOM   444   C  CE  . MET A 1 61   ? 46.345  68.971  146.795 1.00 85.50  ? 61   MET A CE  1 
ATOM   445   N  N   . ILE A 1 62   ? 43.009  68.959  141.608 1.00 95.59  ? 62   ILE A N   1 
ATOM   446   C  CA  . ILE A 1 62   ? 42.751  68.057  140.495 1.00 98.86  ? 62   ILE A CA  1 
ATOM   447   C  C   . ILE A 1 62   ? 44.015  67.299  140.114 1.00 98.66  ? 62   ILE A C   1 
ATOM   448   O  O   . ILE A 1 62   ? 45.018  67.903  139.731 1.00 96.62  ? 62   ILE A O   1 
ATOM   449   C  CB  . ILE A 1 62   ? 42.185  68.799  139.260 1.00 100.25 ? 62   ILE A CB  1 
ATOM   450   C  CG1 . ILE A 1 62   ? 40.944  69.620  139.627 1.00 100.49 ? 62   ILE A CG1 1 
ATOM   451   C  CG2 . ILE A 1 62   ? 41.829  67.808  138.162 1.00 104.21 ? 62   ILE A CG2 1 
ATOM   452   C  CD1 . ILE A 1 62   ? 41.233  71.065  139.956 1.00 97.42  ? 62   ILE A CD1 1 
ATOM   453   N  N   . ASN A 1 63   ? 43.957  65.973  140.222 1.00 101.17 ? 63   ASN A N   1 
ATOM   454   C  CA  . ASN A 1 63   ? 45.104  65.122  139.912 1.00 101.58 ? 63   ASN A CA  1 
ATOM   455   C  C   . ASN A 1 63   ? 45.112  64.627  138.471 1.00 104.54 ? 63   ASN A C   1 
ATOM   456   O  O   . ASN A 1 63   ? 44.062  64.318  137.901 1.00 107.65 ? 63   ASN A O   1 
ATOM   457   C  CB  . ASN A 1 63   ? 45.182  63.936  140.877 1.00 102.50 ? 63   ASN A CB  1 
ATOM   458   C  CG  . ASN A 1 63   ? 45.566  64.350  142.290 1.00 99.88  ? 63   ASN A CG  1 
ATOM   459   O  OD1 . ASN A 1 63   ? 46.429  65.215  142.495 1.00 96.87  ? 63   ASN A OD1 1 
ATOM   460   N  ND2 . ASN A 1 63   ? 44.931  63.723  143.277 1.00 101.08 ? 63   ASN A ND2 1 
ATOM   461   N  N   . PHE A 1 64   ? 46.310  64.559  137.896 1.00 103.74 ? 64   PHE A N   1 
ATOM   462   C  CA  . PHE A 1 64   ? 46.506  64.081  136.534 1.00 106.47 ? 64   PHE A CA  1 
ATOM   463   C  C   . PHE A 1 64   ? 47.561  62.983  136.504 1.00 107.21 ? 64   PHE A C   1 
ATOM   464   O  O   . PHE A 1 64   ? 48.681  63.183  136.976 1.00 104.53 ? 64   PHE A O   1 
ATOM   465   C  CB  . PHE A 1 64   ? 46.942  65.230  135.625 1.00 104.96 ? 64   PHE A CB  1 
ATOM   466   C  CG  . PHE A 1 64   ? 45.851  66.212  135.312 1.00 105.31 ? 64   PHE A CG  1 
ATOM   467   C  CD1 . PHE A 1 64   ? 45.695  67.364  136.073 1.00 102.42 ? 64   PHE A CD1 1 
ATOM   468   C  CD2 . PHE A 1 64   ? 44.991  65.996  134.241 1.00 108.71 ? 64   PHE A CD2 1 
ATOM   469   C  CE1 . PHE A 1 64   ? 44.691  68.281  135.780 1.00 103.05 ? 64   PHE A CE1 1 
ATOM   470   C  CE2 . PHE A 1 64   ? 43.985  66.907  133.940 1.00 109.46 ? 64   PHE A CE2 1 
ATOM   471   C  CZ  . PHE A 1 64   ? 43.835  68.052  134.709 1.00 106.44 ? 64   PHE A CZ  1 
ATOM   472   N  N   . ASN A 1 65   ? 47.196  61.828  135.954 1.00 111.25 ? 65   ASN A N   1 
ATOM   473   C  CA  . ASN A 1 65   ? 48.131  60.720  135.777 1.00 112.68 ? 65   ASN A CA  1 
ATOM   474   C  C   . ASN A 1 65   ? 48.852  60.842  134.441 1.00 113.47 ? 65   ASN A C   1 
ATOM   475   O  O   . ASN A 1 65   ? 48.236  60.705  133.382 1.00 116.61 ? 65   ASN A O   1 
ATOM   476   C  CB  . ASN A 1 65   ? 47.403  59.370  135.846 1.00 116.92 ? 65   ASN A CB  1 
ATOM   477   C  CG  . ASN A 1 65   ? 46.652  59.161  137.154 1.00 116.98 ? 65   ASN A CG  1 
ATOM   478   O  OD1 . ASN A 1 65   ? 46.975  59.761  138.181 1.00 114.12 ? 65   ASN A OD1 1 
ATOM   479   N  ND2 . ASN A 1 65   ? 45.647  58.294  137.119 1.00 120.70 ? 65   ASN A ND2 1 
ATOM   480   N  N   . MET A 1 66   ? 50.154  61.107  134.490 1.00 110.93 ? 66   MET A N   1 
ATOM   481   C  CA  . MET A 1 66   ? 50.954  61.215  133.276 1.00 111.60 ? 66   MET A CA  1 
ATOM   482   C  C   . MET A 1 66   ? 51.294  59.822  132.755 1.00 115.11 ? 66   MET A C   1 
ATOM   483   O  O   . MET A 1 66   ? 51.825  59.002  133.508 1.00 115.02 ? 66   MET A O   1 
ATOM   484   C  CB  . MET A 1 66   ? 52.235  62.013  133.535 1.00 107.64 ? 66   MET A CB  1 
ATOM   485   C  CG  . MET A 1 66   ? 52.025  63.475  133.940 1.00 104.52 ? 66   MET A CG  1 
ATOM   486   S  SD  . MET A 1 66   ? 51.436  64.565  132.623 1.00 105.44 ? 66   MET A SD  1 
ATOM   487   C  CE  . MET A 1 66   ? 49.659  64.512  132.872 1.00 107.28 ? 66   MET A CE  1 
ATOM   488   N  N   . PRO A 1 67   ? 50.983  59.549  131.467 1.00 118.57 ? 67   PRO A N   1 
ATOM   489   C  CA  . PRO A 1 67   ? 51.229  58.234  130.872 1.00 122.29 ? 67   PRO A CA  1 
ATOM   490   C  C   . PRO A 1 67   ? 52.720  57.985  130.689 1.00 120.90 ? 67   PRO A C   1 
ATOM   491   O  O   . PRO A 1 67   ? 53.465  58.909  130.350 1.00 118.15 ? 67   PRO A O   1 
ATOM   492   C  CB  . PRO A 1 67   ? 50.523  58.318  129.514 1.00 125.81 ? 67   PRO A CB  1 
ATOM   493   C  CG  . PRO A 1 67   ? 50.494  59.759  129.186 1.00 123.11 ? 67   PRO A CG  1 
ATOM   494   C  CD  . PRO A 1 67   ? 50.385  60.486  130.497 1.00 119.32 ? 67   PRO A CD  1 
ATOM   495   N  N   . GLU A 1 68   ? 53.140  56.744  130.914 1.00 122.95 ? 68   GLU A N   1 
ATOM   496   C  CA  . GLU A 1 68   ? 54.560  56.395  130.938 1.00 121.74 ? 68   GLU A CA  1 
ATOM   497   C  C   . GLU A 1 68   ? 55.307  56.788  129.657 1.00 121.80 ? 68   GLU A C   1 
ATOM   498   O  O   . GLU A 1 68   ? 56.420  57.314  129.727 1.00 118.75 ? 68   GLU A O   1 
ATOM   499   C  CB  . GLU A 1 68   ? 54.743  54.903  131.228 1.00 124.89 ? 68   GLU A CB  1 
ATOM   500   C  CG  . GLU A 1 68   ? 56.157  54.527  131.678 1.00 123.48 ? 68   GLU A CG  1 
ATOM   501   C  CD  . GLU A 1 68   ? 56.638  53.211  131.080 1.00 127.77 ? 68   GLU A CD  1 
ATOM   502   O  OE1 . GLU A 1 68   ? 55.801  52.310  130.850 1.00 131.83 ? 68   GLU A OE1 1 
ATOM   503   O  OE2 . GLU A 1 68   ? 57.859  53.080  130.840 1.00 126.86 ? 68   GLU A OE2 1 
ATOM   504   N  N   . ASP A 1 69   ? 54.690  56.536  128.501 1.00 125.37 ? 69   ASP A N   1 
ATOM   505   C  CA  . ASP A 1 69   ? 55.316  56.816  127.204 1.00 126.09 ? 69   ASP A CA  1 
ATOM   506   C  C   . ASP A 1 69   ? 55.142  58.273  126.755 1.00 123.70 ? 69   ASP A C   1 
ATOM   507   O  O   . ASP A 1 69   ? 54.466  58.563  125.765 1.00 126.16 ? 69   ASP A O   1 
ATOM   508   C  CB  . ASP A 1 69   ? 54.842  55.823  126.123 1.00 131.56 ? 69   ASP A CB  1 
ATOM   509   C  CG  . ASP A 1 69   ? 53.324  55.810  125.940 1.00 134.79 ? 69   ASP A CG  1 
ATOM   510   O  OD1 . ASP A 1 69   ? 52.606  56.445  126.745 1.00 133.22 ? 69   ASP A OD1 1 
ATOM   511   O  OD2 . ASP A 1 69   ? 52.849  55.155  124.982 1.00 139.32 ? 69   ASP A OD2 1 
ATOM   512   N  N   . LEU A 1 70   ? 55.760  59.183  127.503 1.00 119.06 ? 70   LEU A N   1 
ATOM   513   C  CA  . LEU A 1 70   ? 55.788  60.595  127.138 1.00 116.60 ? 70   LEU A CA  1 
ATOM   514   C  C   . LEU A 1 70   ? 57.145  60.974  126.577 1.00 114.74 ? 70   LEU A C   1 
ATOM   515   O  O   . LEU A 1 70   ? 58.166  60.868  127.262 1.00 112.11 ? 70   LEU A O   1 
ATOM   516   C  CB  . LEU A 1 70   ? 55.456  61.494  128.334 1.00 113.08 ? 70   LEU A CB  1 
ATOM   517   C  CG  . LEU A 1 70   ? 53.996  61.789  128.691 1.00 114.26 ? 70   LEU A CG  1 
ATOM   518   C  CD1 . LEU A 1 70   ? 53.955  62.800  129.826 1.00 110.59 ? 70   LEU A CD1 1 
ATOM   519   C  CD2 . LEU A 1 70   ? 53.197  62.300  127.493 1.00 116.95 ? 70   LEU A CD2 1 
ATOM   520   N  N   . THR A 1 71   ? 57.140  61.411  125.322 1.00 116.23 ? 71   THR A N   1 
ATOM   521   C  CA  . THR A 1 71   ? 58.339  61.910  124.652 1.00 114.76 ? 71   THR A CA  1 
ATOM   522   C  C   . THR A 1 71   ? 58.412  63.440  124.771 1.00 111.33 ? 71   THR A C   1 
ATOM   523   O  O   . THR A 1 71   ? 57.471  64.074  125.259 1.00 110.48 ? 71   THR A O   1 
ATOM   524   C  CB  . THR A 1 71   ? 58.397  61.437  123.160 1.00 118.89 ? 71   THR A CB  1 
ATOM   525   O  OG1 . THR A 1 71   ? 59.609  61.892  122.548 1.00 117.81 ? 71   THR A OG1 1 
ATOM   526   C  CG2 . THR A 1 71   ? 57.191  61.940  122.349 1.00 121.63 ? 71   THR A CG2 1 
ATOM   527   N  N   . ALA A 1 72   ? 59.533  64.022  124.346 1.00 109.27 ? 72   ALA A N   1 
ATOM   528   C  CA  . ALA A 1 72   ? 59.666  65.476  124.259 1.00 106.63 ? 72   ALA A CA  1 
ATOM   529   C  C   . ALA A 1 72   ? 58.642  66.056  123.282 1.00 109.02 ? 72   ALA A C   1 
ATOM   530   O  O   . ALA A 1 72   ? 58.246  65.392  122.318 1.00 112.79 ? 72   ALA A O   1 
ATOM   531   C  CB  . ALA A 1 72   ? 61.076  65.855  123.841 1.00 105.21 ? 72   ALA A CB  1 
ATOM   532   N  N   . GLY A 1 73   ? 58.207  67.288  123.536 1.00 106.92 ? 73   GLY A N   1 
ATOM   533   C  CA  . GLY A 1 73   ? 57.221  67.943  122.678 1.00 108.81 ? 73   GLY A CA  1 
ATOM   534   C  C   . GLY A 1 73   ? 56.771  69.288  123.203 1.00 106.13 ? 73   GLY A C   1 
ATOM   535   O  O   . GLY A 1 73   ? 57.501  69.951  123.943 1.00 102.67 ? 73   GLY A O   1 
ATOM   536   N  N   . ASN A 1 74   ? 55.569  69.693  122.804 1.00 107.85 ? 74   ASN A N   1 
ATOM   537   C  CA  . ASN A 1 74   ? 54.970  70.935  123.278 1.00 105.82 ? 74   ASN A CA  1 
ATOM   538   C  C   . ASN A 1 74   ? 53.749  70.666  124.140 1.00 105.57 ? 74   ASN A C   1 
ATOM   539   O  O   . ASN A 1 74   ? 52.771  70.063  123.683 1.00 108.80 ? 74   ASN A O   1 
ATOM   540   C  CB  . ASN A 1 74   ? 54.608  71.851  122.107 1.00 108.31 ? 74   ASN A CB  1 
ATOM   541   C  CG  . ASN A 1 74   ? 55.825  72.507  121.480 1.00 107.58 ? 74   ASN A CG  1 
ATOM   542   O  OD1 . ASN A 1 74   ? 56.878  72.638  122.108 1.00 104.80 ? 74   ASN A OD1 1 
ATOM   543   N  ND2 . ASN A 1 74   ? 55.680  72.933  120.234 1.00 110.56 ? 74   ASN A ND2 1 
ATOM   544   N  N   . TYR A 1 75   ? 53.816  71.115  125.389 1.00 101.77 ? 75   TYR A N   1 
ATOM   545   C  CA  . TYR A 1 75   ? 52.763  70.843  126.362 1.00 100.98 ? 75   TYR A CA  1 
ATOM   546   C  C   . TYR A 1 75   ? 52.133  72.119  126.904 1.00 99.28  ? 75   TYR A C   1 
ATOM   547   O  O   . TYR A 1 75   ? 52.812  73.130  127.101 1.00 96.69  ? 75   TYR A O   1 
ATOM   548   C  CB  . TYR A 1 75   ? 53.300  69.974  127.498 1.00 98.57  ? 75   TYR A CB  1 
ATOM   549   C  CG  . TYR A 1 75   ? 53.734  68.588  127.066 1.00 100.16 ? 75   TYR A CG  1 
ATOM   550   C  CD1 . TYR A 1 75   ? 52.814  67.538  126.991 1.00 102.71 ? 75   TYR A CD1 1 
ATOM   551   C  CD2 . TYR A 1 75   ? 55.064  68.323  126.739 1.00 98.82  ? 75   TYR A CD2 1 
ATOM   552   C  CE1 . TYR A 1 75   ? 53.208  66.260  126.600 1.00 104.44 ? 75   TYR A CE1 1 
ATOM   553   C  CE2 . TYR A 1 75   ? 55.466  67.049  126.343 1.00 100.67 ? 75   TYR A CE2 1 
ATOM   554   C  CZ  . TYR A 1 75   ? 54.535  66.026  126.279 1.00 103.48 ? 75   TYR A CZ  1 
ATOM   555   O  OH  . TYR A 1 75   ? 54.932  64.770  125.894 1.00 105.86 ? 75   TYR A OH  1 
ATOM   556   N  N   . LYS A 1 76   ? 50.826  72.055  127.142 1.00 100.76 ? 76   LYS A N   1 
ATOM   557   C  CA  . LYS A 1 76   ? 50.040  73.221  127.532 1.00 100.00 ? 76   LYS A CA  1 
ATOM   558   C  C   . LYS A 1 76   ? 48.991  72.847  128.579 1.00 99.57  ? 76   LYS A C   1 
ATOM   559   O  O   . LYS A 1 76   ? 48.633  71.678  128.721 1.00 101.23 ? 76   LYS A O   1 
ATOM   560   C  CB  . LYS A 1 76   ? 49.355  73.805  126.290 1.00 103.32 ? 76   LYS A CB  1 
ATOM   561   C  CG  . LYS A 1 76   ? 48.965  75.277  126.390 1.00 102.92 ? 76   LYS A CG  1 
ATOM   562   C  CD  . LYS A 1 76   ? 47.860  75.644  125.390 1.00 107.71 ? 76   LYS A CD  1 
ATOM   563   C  CE  . LYS A 1 76   ? 48.404  76.084  124.032 1.00 109.97 ? 76   LYS A CE  1 
ATOM   564   N  NZ  . LYS A 1 76   ? 48.662  74.941  123.118 1.00 113.24 ? 76   LYS A NZ  1 
ATOM   565   N  N   . ILE A 1 77   ? 48.512  73.839  129.321 1.00 97.61  ? 77   ILE A N   1 
ATOM   566   C  CA  . ILE A 1 77   ? 47.323  73.669  130.158 1.00 97.69  ? 77   ILE A CA  1 
ATOM   567   C  C   . ILE A 1 77   ? 46.406  74.886  130.036 1.00 98.24  ? 77   ILE A C   1 
ATOM   568   O  O   . ILE A 1 77   ? 46.859  76.029  130.116 1.00 96.64  ? 77   ILE A O   1 
ATOM   569   C  CB  . ILE A 1 77   ? 47.659  73.319  131.645 1.00 94.68  ? 77   ILE A CB  1 
ATOM   570   C  CG1 . ILE A 1 77   ? 46.373  73.060  132.448 1.00 95.13  ? 77   ILE A CG1 1 
ATOM   571   C  CG2 . ILE A 1 77   ? 48.546  74.390  132.292 1.00 90.95  ? 77   ILE A CG2 1 
ATOM   572   C  CD1 . ILE A 1 77   ? 46.519  72.030  133.546 1.00 93.34  ? 77   ILE A CD1 1 
ATOM   573   N  N   . THR A 1 78   ? 45.121  74.627  129.829 1.00 100.70 ? 78   THR A N   1 
ATOM   574   C  CA  . THR A 1 78   ? 44.162  75.681  129.549 1.00 101.88 ? 78   THR A CA  1 
ATOM   575   C  C   . THR A 1 78   ? 43.020  75.633  130.554 1.00 101.78 ? 78   THR A C   1 
ATOM   576   O  O   . THR A 1 78   ? 42.441  74.571  130.797 1.00 103.20 ? 78   THR A O   1 
ATOM   577   C  CB  . THR A 1 78   ? 43.611  75.560  128.102 1.00 106.12 ? 78   THR A CB  1 
ATOM   578   O  OG1 . THR A 1 78   ? 44.693  75.316  127.190 1.00 106.13 ? 78   THR A OG1 1 
ATOM   579   C  CG2 . THR A 1 78   ? 42.878  76.832  127.686 1.00 107.21 ? 78   THR A CG2 1 
ATOM   580   N  N   . ILE A 1 79   ? 42.706  76.788  131.137 1.00 100.21 ? 79   ILE A N   1 
ATOM   581   C  CA  . ILE A 1 79   ? 41.629  76.900  132.124 1.00 100.00 ? 79   ILE A CA  1 
ATOM   582   C  C   . ILE A 1 79   ? 40.589  77.923  131.663 1.00 102.18 ? 79   ILE A C   1 
ATOM   583   O  O   . ILE A 1 79   ? 40.838  79.133  131.665 1.00 100.93 ? 79   ILE A O   1 
ATOM   584   C  CB  . ILE A 1 79   ? 42.181  77.251  133.530 1.00 96.07  ? 79   ILE A CB  1 
ATOM   585   C  CG1 . ILE A 1 79   ? 43.224  76.220  133.957 1.00 94.21  ? 79   ILE A CG1 1 
ATOM   586   C  CG2 . ILE A 1 79   ? 41.075  77.278  134.563 1.00 95.78  ? 79   ILE A CG2 1 
ATOM   587   C  CD1 . ILE A 1 79   ? 44.570  76.814  134.237 1.00 91.45  ? 79   ILE A CD1 1 
ATOM   588   N  N   . ASP A 1 80   ? 39.426  77.418  131.263 1.00 105.70 ? 80   ASP A N   1 
ATOM   589   C  CA  . ASP A 1 80   ? 38.355  78.258  130.737 1.00 108.55 ? 80   ASP A CA  1 
ATOM   590   C  C   . ASP A 1 80   ? 37.146  78.287  131.656 1.00 109.12 ? 80   ASP A C   1 
ATOM   591   O  O   . ASP A 1 80   ? 36.638  77.242  132.060 1.00 110.06 ? 80   ASP A O   1 
ATOM   592   C  CB  . ASP A 1 80   ? 37.936  77.787  129.343 1.00 112.72 ? 80   ASP A CB  1 
ATOM   593   C  CG  . ASP A 1 80   ? 38.998  78.045  128.299 1.00 112.64 ? 80   ASP A CG  1 
ATOM   594   O  OD1 . ASP A 1 80   ? 39.288  79.228  128.022 1.00 111.77 ? 80   ASP A OD1 1 
ATOM   595   O  OD2 . ASP A 1 80   ? 39.537  77.063  127.750 1.00 113.37 ? 80   ASP A OD2 1 
ATOM   596   N  N   . GLY A 1 81   ? 36.695  79.496  131.978 1.00 108.90 ? 81   GLY A N   1 
ATOM   597   C  CA  . GLY A 1 81   ? 35.507  79.690  132.801 1.00 109.81 ? 81   GLY A CA  1 
ATOM   598   C  C   . GLY A 1 81   ? 34.255  79.458  131.988 1.00 114.56 ? 81   GLY A C   1 
ATOM   599   O  O   . GLY A 1 81   ? 33.935  80.238  131.091 1.00 116.85 ? 81   GLY A O   1 
ATOM   600   N  N   . GLN A 1 82   ? 33.552  78.373  132.293 1.00 116.43 ? 82   GLN A N   1 
ATOM   601   C  CA  . GLN A 1 82   ? 32.322  78.038  131.584 1.00 121.21 ? 82   GLN A CA  1 
ATOM   602   C  C   . GLN A 1 82   ? 31.099  78.670  132.243 1.00 122.06 ? 82   GLN A C   1 
ATOM   603   O  O   . GLN A 1 82   ? 31.129  79.017  133.429 1.00 119.09 ? 82   GLN A O   1 
ATOM   604   C  CB  . GLN A 1 82   ? 32.164  76.522  131.463 1.00 123.20 ? 82   GLN A CB  1 
ATOM   605   C  CG  . GLN A 1 82   ? 33.142  75.890  130.472 1.00 124.55 ? 82   GLN A CG  1 
ATOM   606   C  CD  . GLN A 1 82   ? 32.973  74.386  130.349 1.00 127.68 ? 82   GLN A CD  1 
ATOM   607   O  OE1 . GLN A 1 82   ? 32.857  73.672  131.349 1.00 127.17 ? 82   GLN A OE1 1 
ATOM   608   N  NE2 . GLN A 1 82   ? 32.971  73.894  129.116 1.00 131.24 ? 82   GLN A NE2 1 
ATOM   609   N  N   . ARG A 1 83   ? 30.034  78.813  131.451 1.00 126.44 ? 83   ARG A N   1 
ATOM   610   C  CA  . ARG A 1 83   ? 28.772  79.447  131.867 1.00 128.10 ? 83   ARG A CA  1 
ATOM   611   C  C   . ARG A 1 83   ? 28.911  80.970  132.014 1.00 126.68 ? 83   ARG A C   1 
ATOM   612   O  O   . ARG A 1 83   ? 29.717  81.591  131.311 1.00 126.24 ? 83   ARG A O   1 
ATOM   613   C  CB  . ARG A 1 83   ? 28.208  78.796  133.137 1.00 126.90 ? 83   ARG A CB  1 
ATOM   614   C  CG  . ARG A 1 83   ? 27.829  77.339  132.954 1.00 129.58 ? 83   ARG A CG  1 
ATOM   615   C  CD  . ARG A 1 83   ? 27.293  76.755  134.239 1.00 129.27 ? 83   ARG A CD  1 
ATOM   616   N  NE  . ARG A 1 83   ? 26.334  75.680  133.989 1.00 133.74 ? 83   ARG A NE  1 
ATOM   617   C  CZ  . ARG A 1 83   ? 25.642  75.049  134.934 1.00 134.28 ? 83   ARG A CZ  1 
ATOM   618   N  NH1 . ARG A 1 83   ? 25.793  75.371  136.215 1.00 130.95 ? 83   ARG A NH1 1 
ATOM   619   N  NH2 . ARG A 1 83   ? 24.794  74.089  134.595 1.00 138.50 ? 83   ARG A NH2 1 
ATOM   620   N  N   . GLY A 1 84   ? 28.129  81.567  132.914 1.00 126.17 ? 84   GLY A N   1 
ATOM   621   C  CA  . GLY A 1 84   ? 28.139  83.019  133.113 1.00 125.10 ? 84   GLY A CA  1 
ATOM   622   C  C   . GLY A 1 84   ? 29.335  83.524  133.905 1.00 120.52 ? 84   GLY A C   1 
ATOM   623   O  O   . GLY A 1 84   ? 29.163  84.168  134.945 1.00 118.69 ? 84   GLY A O   1 
ATOM   624   N  N   . PHE A 1 85   ? 30.539  83.235  133.405 1.00 118.84 ? 85   PHE A N   1 
ATOM   625   C  CA  . PHE A 1 85   ? 31.797  83.579  134.077 1.00 114.46 ? 85   PHE A CA  1 
ATOM   626   C  C   . PHE A 1 85   ? 32.965  83.537  133.090 1.00 113.90 ? 85   PHE A C   1 
ATOM   627   O  O   . PHE A 1 85   ? 33.455  82.460  132.754 1.00 113.74 ? 85   PHE A O   1 
ATOM   628   C  CB  . PHE A 1 85   ? 32.059  82.622  135.252 1.00 111.84 ? 85   PHE A CB  1 
ATOM   629   C  CG  . PHE A 1 85   ? 33.331  82.912  136.010 1.00 108.13 ? 85   PHE A CG  1 
ATOM   630   C  CD1 . PHE A 1 85   ? 33.331  83.810  137.078 1.00 106.16 ? 85   PHE A CD1 1 
ATOM   631   C  CD2 . PHE A 1 85   ? 34.527  82.281  135.668 1.00 106.49 ? 85   PHE A CD2 1 
ATOM   632   C  CE1 . PHE A 1 85   ? 34.501  84.084  137.783 1.00 102.03 ? 85   PHE A CE1 1 
ATOM   633   C  CE2 . PHE A 1 85   ? 35.698  82.548  136.367 1.00 102.56 ? 85   PHE A CE2 1 
ATOM   634   C  CZ  . PHE A 1 85   ? 35.685  83.452  137.424 1.00 100.70 ? 85   PHE A CZ  1 
ATOM   635   N  N   . SER A 1 86   ? 33.406  84.707  132.632 1.00 113.65 ? 86   SER A N   1 
ATOM   636   C  CA  . SER A 1 86   ? 34.508  84.794  131.667 1.00 113.49 ? 86   SER A CA  1 
ATOM   637   C  C   . SER A 1 86   ? 35.865  84.614  132.335 1.00 109.25 ? 86   SER A C   1 
ATOM   638   O  O   . SER A 1 86   ? 36.169  85.279  133.328 1.00 106.58 ? 86   SER A O   1 
ATOM   639   C  CB  . SER A 1 86   ? 34.471  86.116  130.897 1.00 115.29 ? 86   SER A CB  1 
ATOM   640   O  OG  . SER A 1 86   ? 33.511  86.071  129.857 1.00 120.02 ? 86   SER A OG  1 
ATOM   641   N  N   . PHE A 1 87   ? 36.669  83.710  131.777 1.00 108.76 ? 87   PHE A N   1 
ATOM   642   C  CA  . PHE A 1 87   ? 37.990  83.379  132.307 1.00 105.03 ? 87   PHE A CA  1 
ATOM   643   C  C   . PHE A 1 87   ? 38.763  82.567  131.287 1.00 105.82 ? 87   PHE A C   1 
ATOM   644   O  O   . PHE A 1 87   ? 38.357  81.465  130.924 1.00 107.63 ? 87   PHE A O   1 
ATOM   645   C  CB  . PHE A 1 87   ? 37.864  82.572  133.602 1.00 102.78 ? 87   PHE A CB  1 
ATOM   646   C  CG  . PHE A 1 87   ? 39.161  82.395  134.353 1.00 98.96  ? 87   PHE A CG  1 
ATOM   647   C  CD1 . PHE A 1 87   ? 39.475  83.224  135.428 1.00 96.12  ? 87   PHE A CD1 1 
ATOM   648   C  CD2 . PHE A 1 87   ? 40.059  81.386  134.003 1.00 98.34  ? 87   PHE A CD2 1 
ATOM   649   C  CE1 . PHE A 1 87   ? 40.669  83.060  136.137 1.00 92.34  ? 87   PHE A CE1 1 
ATOM   650   C  CE2 . PHE A 1 87   ? 41.254  81.214  134.707 1.00 94.77  ? 87   PHE A CE2 1 
ATOM   651   C  CZ  . PHE A 1 87   ? 41.557  82.053  135.776 1.00 91.60  ? 87   PHE A CZ  1 
ATOM   652   N  N   . HIS A 1 88   ? 39.878  83.115  130.823 1.00 104.64 ? 88   HIS A N   1 
ATOM   653   C  CA  . HIS A 1 88   ? 40.788  82.362  129.974 1.00 104.99 ? 88   HIS A CA  1 
ATOM   654   C  C   . HIS A 1 88   ? 42.228  82.515  130.439 1.00 101.43 ? 88   HIS A C   1 
ATOM   655   O  O   . HIS A 1 88   ? 42.835  83.575  130.274 1.00 100.61 ? 88   HIS A O   1 
ATOM   656   C  CB  . HIS A 1 88   ? 40.657  82.764  128.501 1.00 108.42 ? 88   HIS A CB  1 
ATOM   657   C  CG  . HIS A 1 88   ? 41.646  82.081  127.609 1.00 108.93 ? 88   HIS A CG  1 
ATOM   658   N  ND1 . HIS A 1 88   ? 41.495  80.776  127.192 1.00 110.58 ? 88   HIS A ND1 1 
ATOM   659   C  CD2 . HIS A 1 88   ? 42.813  82.514  127.075 1.00 108.54 ? 88   HIS A CD2 1 
ATOM   660   C  CE1 . HIS A 1 88   ? 42.519  80.438  126.430 1.00 111.02 ? 88   HIS A CE1 1 
ATOM   661   N  NE2 . HIS A 1 88   ? 43.334  81.473  126.344 1.00 109.88 ? 88   HIS A NE2 1 
ATOM   662   N  N   . LYS A 1 89   ? 42.763  81.447  131.022 1.00 99.50  ? 89   LYS A N   1 
ATOM   663   C  CA  . LYS A 1 89   ? 44.171  81.395  131.390 1.00 96.56  ? 89   LYS A CA  1 
ATOM   664   C  C   . LYS A 1 89   ? 44.878  80.150  130.844 1.00 97.04  ? 89   LYS A C   1 
ATOM   665   O  O   . LYS A 1 89   ? 44.268  79.085  130.692 1.00 98.66  ? 89   LYS A O   1 
ATOM   666   C  CB  . LYS A 1 89   ? 44.351  81.546  132.904 1.00 93.26  ? 89   LYS A CB  1 
ATOM   667   C  CG  . LYS A 1 89   ? 44.810  82.942  133.334 1.00 91.20  ? 89   LYS A CG  1 
ATOM   668   C  CD  . LYS A 1 89   ? 43.726  84.012  133.251 1.00 91.68  ? 89   LYS A CD  1 
ATOM   669   C  CE  . LYS A 1 89   ? 44.352  85.376  132.980 1.00 90.92  ? 89   LYS A CE  1 
ATOM   670   N  NZ  . LYS A 1 89   ? 43.391  86.497  133.150 1.00 91.48  ? 89   LYS A NZ  1 
ATOM   671   N  N   . GLU A 1 90   ? 46.170  80.308  130.559 1.00 95.72  ? 90   GLU A N   1 
ATOM   672   C  CA  . GLU A 1 90   ? 46.942  79.335  129.798 1.00 96.74  ? 90   GLU A CA  1 
ATOM   673   C  C   . GLU A 1 90   ? 48.379  79.285  130.295 1.00 93.73  ? 90   GLU A C   1 
ATOM   674   O  O   . GLU A 1 90   ? 48.949  80.317  130.644 1.00 91.89  ? 90   GLU A O   1 
ATOM   675   C  CB  . GLU A 1 90   ? 46.920  79.749  128.331 1.00 99.89  ? 90   GLU A CB  1 
ATOM   676   C  CG  . GLU A 1 90   ? 47.543  78.776  127.357 1.00 102.02 ? 90   GLU A CG  1 
ATOM   677   C  CD  . GLU A 1 90   ? 47.400  79.241  125.919 1.00 106.27 ? 90   GLU A CD  1 
ATOM   678   O  OE1 . GLU A 1 90   ? 46.276  79.620  125.510 1.00 108.83 ? 90   GLU A OE1 1 
ATOM   679   O  OE2 . GLU A 1 90   ? 48.417  79.226  125.197 1.00 107.12 ? 90   GLU A OE2 1 
ATOM   680   N  N   . ALA A 1 91   ? 48.969  78.092  130.320 1.00 93.62  ? 91   ALA A N   1 
ATOM   681   C  CA  . ALA A 1 91   ? 50.350  77.943  130.785 1.00 91.41  ? 91   ALA A CA  1 
ATOM   682   C  C   . ALA A 1 91   ? 51.178  76.953  129.978 1.00 92.76  ? 91   ALA A C   1 
ATOM   683   O  O   . ALA A 1 91   ? 50.709  75.866  129.626 1.00 94.79  ? 91   ALA A O   1 
ATOM   684   C  CB  . ALA A 1 91   ? 50.384  77.573  132.261 1.00 88.85  ? 91   ALA A CB  1 
ATOM   685   N  N   . GLU A 1 92   ? 52.416  77.349  129.695 1.00 91.97  ? 92   GLU A N   1 
ATOM   686   C  CA  . GLU A 1 92   ? 53.402  76.474  129.065 1.00 92.99  ? 92   GLU A CA  1 
ATOM   687   C  C   . GLU A 1 92   ? 53.906  75.480  130.113 1.00 91.01  ? 92   GLU A C   1 
ATOM   688   O  O   . GLU A 1 92   ? 54.195  75.864  131.246 1.00 88.52  ? 92   GLU A O   1 
ATOM   689   C  CB  . GLU A 1 92   ? 54.582  77.280  128.490 1.00 92.42  ? 92   GLU A CB  1 
ATOM   690   C  CG  . GLU A 1 92   ? 54.309  78.777  128.199 1.00 93.80  ? 92   GLU A CG  1 
ATOM   691   C  CD  . GLU A 1 92   ? 54.711  79.715  129.356 1.00 91.88  ? 92   GLU A CD  1 
ATOM   692   O  OE1 . GLU A 1 92   ? 54.152  79.591  130.471 1.00 89.54  ? 92   GLU A OE1 1 
ATOM   693   O  OE2 . GLU A 1 92   ? 55.585  80.588  129.136 1.00 91.73  ? 92   GLU A OE2 1 
ATOM   694   N  N   . LEU A 1 93   ? 54.000  74.208  129.738 1.00 92.59  ? 93   LEU A N   1 
ATOM   695   C  CA  . LEU A 1 93   ? 54.438  73.153  130.655 1.00 91.16  ? 93   LEU A CA  1 
ATOM   696   C  C   . LEU A 1 93   ? 55.651  72.424  130.091 1.00 91.35  ? 93   LEU A C   1 
ATOM   697   O  O   . LEU A 1 93   ? 55.566  71.758  129.060 1.00 94.08  ? 93   LEU A O   1 
ATOM   698   C  CB  . LEU A 1 93   ? 53.303  72.158  130.931 1.00 92.97  ? 93   LEU A CB  1 
ATOM   699   C  CG  . LEU A 1 93   ? 51.997  72.633  131.577 1.00 93.09  ? 93   LEU A CG  1 
ATOM   700   C  CD1 . LEU A 1 93   ? 50.969  71.516  131.572 1.00 95.92  ? 93   LEU A CD1 1 
ATOM   701   C  CD2 . LEU A 1 93   ? 52.216  73.130  132.989 1.00 90.00  ? 93   LEU A CD2 1 
ATOM   702   N  N   . VAL A 1 94   ? 56.781  72.551  130.773 1.00 88.77  ? 94   VAL A N   1 
ATOM   703   C  CA  . VAL A 1 94   ? 58.033  71.993  130.277 1.00 88.80  ? 94   VAL A CA  1 
ATOM   704   C  C   . VAL A 1 94   ? 58.230  70.548  130.730 1.00 89.45  ? 94   VAL A C   1 
ATOM   705   O  O   . VAL A 1 94   ? 58.344  70.262  131.922 1.00 87.90  ? 94   VAL A O   1 
ATOM   706   C  CB  . VAL A 1 94   ? 59.241  72.860  130.680 1.00 85.99  ? 94   VAL A CB  1 
ATOM   707   C  CG1 . VAL A 1 94   ? 60.525  72.301  130.086 1.00 86.02  ? 94   VAL A CG1 1 
ATOM   708   C  CG2 . VAL A 1 94   ? 59.026  74.297  130.232 1.00 85.86  ? 94   VAL A CG2 1 
ATOM   709   N  N   . TYR A 1 95   ? 58.265  69.649  129.753 1.00 92.26  ? 95   TYR A N   1 
ATOM   710   C  CA  . TYR A 1 95   ? 58.499  68.230  129.979 1.00 93.48  ? 95   TYR A CA  1 
ATOM   711   C  C   . TYR A 1 95   ? 59.960  67.967  130.352 1.00 91.52  ? 95   TYR A C   1 
ATOM   712   O  O   . TYR A 1 95   ? 60.868  68.573  129.783 1.00 90.82  ? 95   TYR A O   1 
ATOM   713   C  CB  . TYR A 1 95   ? 58.108  67.454  128.713 1.00 97.38  ? 95   TYR A CB  1 
ATOM   714   C  CG  . TYR A 1 95   ? 58.668  66.054  128.609 1.00 99.14  ? 95   TYR A CG  1 
ATOM   715   C  CD1 . TYR A 1 95   ? 58.041  64.981  129.241 1.00 100.55 ? 95   TYR A CD1 1 
ATOM   716   C  CD2 . TYR A 1 95   ? 59.824  65.800  127.866 1.00 99.88  ? 95   TYR A CD2 1 
ATOM   717   C  CE1 . TYR A 1 95   ? 58.553  63.690  129.144 1.00 102.75 ? 95   TYR A CE1 1 
ATOM   718   C  CE2 . TYR A 1 95   ? 60.346  64.514  127.763 1.00 101.77 ? 95   TYR A CE2 1 
ATOM   719   C  CZ  . TYR A 1 95   ? 59.705  63.464  128.402 1.00 103.26 ? 95   TYR A CZ  1 
ATOM   720   O  OH  . TYR A 1 95   ? 60.214  62.190  128.300 1.00 105.08 ? 95   TYR A OH  1 
ATOM   721   N  N   . LEU A 1 96   ? 60.178  67.068  131.310 1.00 90.89  ? 96   LEU A N   1 
ATOM   722   C  CA  . LEU A 1 96   ? 61.528  66.654  131.685 1.00 89.46  ? 96   LEU A CA  1 
ATOM   723   C  C   . LEU A 1 96   ? 61.755  65.183  131.381 1.00 91.86  ? 96   LEU A C   1 
ATOM   724   O  O   . LEU A 1 96   ? 60.965  64.326  131.784 1.00 93.36  ? 96   LEU A O   1 
ATOM   725   C  CB  . LEU A 1 96   ? 61.796  66.934  133.159 1.00 86.68  ? 96   LEU A CB  1 
ATOM   726   C  CG  . LEU A 1 96   ? 61.827  68.400  133.592 1.00 84.58  ? 96   LEU A CG  1 
ATOM   727   C  CD1 . LEU A 1 96   ? 61.804  68.497  135.113 1.00 83.04  ? 96   LEU A CD1 1 
ATOM   728   C  CD2 . LEU A 1 96   ? 63.036  69.130  133.019 1.00 83.17  ? 96   LEU A CD2 1 
ATOM   729   N  N   . SER A 1 97   ? 62.840  64.904  130.663 1.00 92.42  ? 97   SER A N   1 
ATOM   730   C  CA  . SER A 1 97   ? 63.175  63.544  130.235 1.00 94.90  ? 97   SER A CA  1 
ATOM   731   C  C   . SER A 1 97   ? 63.732  62.723  131.392 1.00 93.77  ? 97   SER A C   1 
ATOM   732   O  O   . SER A 1 97   ? 63.336  61.575  131.597 1.00 95.89  ? 97   SER A O   1 
ATOM   733   C  CB  . SER A 1 97   ? 64.199  63.574  129.092 1.00 95.73  ? 97   SER A CB  1 
ATOM   734   O  OG  . SER A 1 97   ? 63.829  64.495  128.080 1.00 96.65  ? 97   SER A OG  1 
ATOM   735   N  N   . LYS A 1 98   ? 64.647  63.331  132.144 1.00 90.65  ? 98   LYS A N   1 
ATOM   736   C  CA  . LYS A 1 98   ? 65.393  62.643  133.192 1.00 89.52  ? 98   LYS A CA  1 
ATOM   737   C  C   . LYS A 1 98   ? 64.951  63.042  134.592 1.00 87.08  ? 98   LYS A C   1 
ATOM   738   O  O   . LYS A 1 98   ? 64.325  64.083  134.790 1.00 85.52  ? 98   LYS A O   1 
ATOM   739   C  CB  . LYS A 1 98   ? 66.905  62.882  133.023 1.00 88.32  ? 98   LYS A CB  1 
ATOM   740   C  CG  . LYS A 1 98   ? 67.533  62.148  131.828 1.00 91.30  ? 98   LYS A CG  1 
ATOM   741   C  CD  . LYS A 1 98   ? 67.290  60.638  131.920 1.00 95.06  ? 98   LYS A CD  1 
ATOM   742   C  CE  . LYS A 1 98   ? 66.844  60.065  130.578 1.00 98.82  ? 98   LYS A CE  1 
ATOM   743   N  NZ  . LYS A 1 98   ? 65.901  58.914  130.757 1.00 101.59 ? 98   LYS A NZ  1 
ATOM   744   N  N   . SER A 1 99   ? 65.287  62.190  135.556 1.00 86.71  ? 99   SER A N   1 
ATOM   745   C  CA  . SER A 1 99   ? 64.985  62.423  136.959 1.00 84.60  ? 99   SER A CA  1 
ATOM   746   C  C   . SER A 1 99   ? 66.223  62.939  137.700 1.00 81.50  ? 99   SER A C   1 
ATOM   747   O  O   . SER A 1 99   ? 66.169  63.250  138.893 1.00 80.04  ? 99   SER A O   1 
ATOM   748   C  CB  . SER A 1 99   ? 64.481  61.123  137.594 1.00 86.90  ? 99   SER A CB  1 
ATOM   749   O  OG  . SER A 1 99   ? 64.176  61.300  138.967 1.00 86.65  ? 99   SER A OG  1 
ATOM   750   N  N   . ILE A 1 100  ? 67.337  63.037  136.981 1.00 80.39  ? 100  ILE A N   1 
ATOM   751   C  CA  . ILE A 1 100  ? 68.618  63.377  137.592 1.00 77.56  ? 100  ILE A CA  1 
ATOM   752   C  C   . ILE A 1 100  ? 69.174  64.693  137.060 1.00 75.10  ? 100  ILE A C   1 
ATOM   753   O  O   . ILE A 1 100  ? 68.728  65.198  136.029 1.00 75.63  ? 100  ILE A O   1 
ATOM   754   C  CB  . ILE A 1 100  ? 69.652  62.230  137.421 1.00 79.03  ? 100  ILE A CB  1 
ATOM   755   C  CG1 . ILE A 1 100  ? 69.742  61.792  135.953 1.00 80.73  ? 100  ILE A CG1 1 
ATOM   756   C  CG2 . ILE A 1 100  ? 69.282  61.048  138.318 1.00 80.52  ? 100  ILE A CG2 1 
ATOM   757   C  CD1 . ILE A 1 100  ? 70.743  60.685  135.685 1.00 82.27  ? 100  ILE A CD1 1 
ATOM   758   N  N   . SER A 1 101  ? 70.136  65.253  137.782 1.00 72.28  ? 101  SER A N   1 
ATOM   759   C  CA  . SER A 1 101  ? 70.782  66.488  137.365 1.00 69.94  ? 101  SER A CA  1 
ATOM   760   C  C   . SER A 1 101  ? 72.293  66.365  137.513 1.00 68.71  ? 101  SER A C   1 
ATOM   761   O  O   . SER A 1 101  ? 72.788  65.572  138.318 1.00 68.93  ? 101  SER A O   1 
ATOM   762   C  CB  . SER A 1 101  ? 70.258  67.669  138.176 1.00 68.11  ? 101  SER A CB  1 
ATOM   763   O  OG  . SER A 1 101  ? 70.378  67.403  139.556 1.00 67.59  ? 101  SER A OG  1 
ATOM   764   N  N   . GLY A 1 102  ? 73.018  67.152  136.727 1.00 67.27  ? 102  GLY A N   1 
ATOM   765   C  CA  . GLY A 1 102  ? 74.463  67.052  136.679 1.00 65.67  ? 102  GLY A CA  1 
ATOM   766   C  C   . GLY A 1 102  ? 75.162  68.377  136.853 1.00 63.34  ? 102  GLY A C   1 
ATOM   767   O  O   . GLY A 1 102  ? 74.645  69.431  136.471 1.00 62.82  ? 102  GLY A O   1 
ATOM   768   N  N   . LEU A 1 103  ? 76.354  68.314  137.432 1.00 61.93  ? 103  LEU A N   1 
ATOM   769   C  CA  . LEU A 1 103  ? 77.180  69.487  137.641 1.00 59.65  ? 103  LEU A CA  1 
ATOM   770   C  C   . LEU A 1 103  ? 78.620  69.153  137.307 1.00 59.17  ? 103  LEU A C   1 
ATOM   771   O  O   . LEU A 1 103  ? 79.077  68.039  137.564 1.00 60.18  ? 103  LEU A O   1 
ATOM   772   C  CB  . LEU A 1 103  ? 77.107  69.901  139.098 1.00 58.70  ? 103  LEU A CB  1 
ATOM   773   C  CG  . LEU A 1 103  ? 75.764  70.395  139.610 1.00 59.09  ? 103  LEU A CG  1 
ATOM   774   C  CD1 . LEU A 1 103  ? 75.530  69.838  141.011 1.00 59.01  ? 103  LEU A CD1 1 
ATOM   775   C  CD2 . LEU A 1 103  ? 75.719  71.931  139.578 1.00 58.32  ? 103  LEU A CD2 1 
ATOM   776   N  N   . ILE A 1 104  ? 79.335  70.115  136.734 1.00 57.38  ? 104  ILE A N   1 
ATOM   777   C  CA  . ILE A 1 104  ? 80.766  69.957  136.508 1.00 56.27  ? 104  ILE A CA  1 
ATOM   778   C  C   . ILE A 1 104  ? 81.523  71.053  137.244 1.00 54.46  ? 104  ILE A C   1 
ATOM   779   O  O   . ILE A 1 104  ? 81.194  72.238  137.136 1.00 53.46  ? 104  ILE A O   1 
ATOM   780   C  CB  . ILE A 1 104  ? 81.137  69.971  135.005 1.00 57.39  ? 104  ILE A CB  1 
ATOM   781   C  CG1 . ILE A 1 104  ? 80.491  68.783  134.283 1.00 58.16  ? 104  ILE A CG1 1 
ATOM   782   C  CG2 . ILE A 1 104  ? 82.670  69.962  134.826 1.00 57.16  ? 104  ILE A CG2 1 
ATOM   783   C  CD1 . ILE A 1 104  ? 80.395  68.930  132.778 1.00 59.23  ? 104  ILE A CD1 1 
ATOM   784   N  N   . GLN A 1 105  ? 82.532  70.640  138.002 1.00 53.58  ? 105  GLN A N   1 
ATOM   785   C  CA  . GLN A 1 105  ? 83.380  71.571  138.715 1.00 51.93  ? 105  GLN A CA  1 
ATOM   786   C  C   . GLN A 1 105  ? 84.785  71.501  138.120 1.00 52.68  ? 105  GLN A C   1 
ATOM   787   O  O   . GLN A 1 105  ? 85.370  70.422  138.041 1.00 53.51  ? 105  GLN A O   1 
ATOM   788   C  CB  . GLN A 1 105  ? 83.395  71.229  140.207 1.00 51.04  ? 105  GLN A CB  1 
ATOM   789   C  CG  . GLN A 1 105  ? 84.091  72.264  141.066 1.00 48.39  ? 105  GLN A CG  1 
ATOM   790   C  CD  . GLN A 1 105  ? 84.321  71.801  142.486 1.00 46.77  ? 105  GLN A CD  1 
ATOM   791   O  OE1 . GLN A 1 105  ? 84.207  70.615  142.796 1.00 46.39  ? 105  GLN A OE1 1 
ATOM   792   N  NE2 . GLN A 1 105  ? 84.656  72.742  143.364 1.00 45.98  ? 105  GLN A NE2 1 
ATOM   793   N  N   . VAL A 1 106  ? 85.310  72.652  137.699 1.00 52.38  ? 106  VAL A N   1 
ATOM   794   C  CA  . VAL A 1 106  ? 86.648  72.747  137.119 1.00 53.24  ? 106  VAL A CA  1 
ATOM   795   C  C   . VAL A 1 106  ? 87.495  73.624  138.024 1.00 53.07  ? 106  VAL A C   1 
ATOM   796   O  O   . VAL A 1 106  ? 87.064  74.714  138.392 1.00 52.77  ? 106  VAL A O   1 
ATOM   797   C  CB  . VAL A 1 106  ? 86.623  73.393  135.705 1.00 53.70  ? 106  VAL A CB  1 
ATOM   798   C  CG1 . VAL A 1 106  ? 87.939  73.178  134.996 1.00 54.91  ? 106  VAL A CG1 1 
ATOM   799   C  CG2 . VAL A 1 106  ? 85.495  72.834  134.859 1.00 54.00  ? 106  VAL A CG2 1 
ATOM   800   N  N   . ASP A 1 107  ? 88.701  73.170  138.366 1.00 53.78  ? 107  ASP A N   1 
ATOM   801   C  CA  . ASP A 1 107  ? 89.571  73.919  139.292 1.00 53.84  ? 107  ASP A CA  1 
ATOM   802   C  C   . ASP A 1 107  ? 89.999  75.313  138.823 1.00 54.06  ? 107  ASP A C   1 
ATOM   803   O  O   . ASP A 1 107  ? 90.391  76.131  139.646 1.00 54.91  ? 107  ASP A O   1 
ATOM   804   C  CB  . ASP A 1 107  ? 90.797  73.098  139.715 1.00 54.67  ? 107  ASP A CB  1 
ATOM   805   C  CG  . ASP A 1 107  ? 91.679  72.678  138.537 1.00 56.67  ? 107  ASP A CG  1 
ATOM   806   O  OD1 . ASP A 1 107  ? 91.393  73.062  137.376 1.00 57.03  ? 107  ASP A OD1 1 
ATOM   807   O  OD2 . ASP A 1 107  ? 92.674  71.955  138.780 1.00 57.61  ? 107  ASP A OD2 1 
ATOM   808   N  N   . LYS A 1 108  ? 89.931  75.588  137.524 1.00 54.13  ? 108  LYS A N   1 
ATOM   809   C  CA  . LYS A 1 108  ? 90.194  76.931  137.005 1.00 54.44  ? 108  LYS A CA  1 
ATOM   810   C  C   . LYS A 1 108  ? 89.295  77.217  135.800 1.00 54.20  ? 108  LYS A C   1 
ATOM   811   O  O   . LYS A 1 108  ? 88.861  76.284  135.129 1.00 54.65  ? 108  LYS A O   1 
ATOM   812   C  CB  . LYS A 1 108  ? 91.658  77.077  136.565 1.00 55.97  ? 108  LYS A CB  1 
ATOM   813   C  CG  . LYS A 1 108  ? 92.725  76.989  137.652 1.00 56.92  ? 108  LYS A CG  1 
ATOM   814   C  CD  . LYS A 1 108  ? 94.112  77.136  137.021 1.00 59.69  ? 108  LYS A CD  1 
ATOM   815   C  CE  . LYS A 1 108  ? 95.230  76.747  137.985 1.00 61.34  ? 108  LYS A CE  1 
ATOM   816   N  NZ  . LYS A 1 108  ? 96.496  76.416  137.251 1.00 63.39  ? 108  LYS A NZ  1 
ATOM   817   N  N   . PRO A 1 109  ? 89.004  78.505  135.518 1.00 53.86  ? 109  PRO A N   1 
ATOM   818   C  CA  . PRO A 1 109  ? 88.321  78.856  134.258 1.00 53.81  ? 109  PRO A CA  1 
ATOM   819   C  C   . PRO A 1 109  ? 89.258  79.011  133.051 1.00 54.87  ? 109  PRO A C   1 
ATOM   820   O  O   . PRO A 1 109  ? 88.847  78.762  131.914 1.00 55.77  ? 109  PRO A O   1 
ATOM   821   C  CB  . PRO A 1 109  ? 87.653  80.200  134.573 1.00 53.58  ? 109  PRO A CB  1 
ATOM   822   C  CG  . PRO A 1 109  ? 88.127  80.600  135.963 1.00 53.43  ? 109  PRO A CG  1 
ATOM   823   C  CD  . PRO A 1 109  ? 89.235  79.690  136.363 1.00 53.74  ? 109  PRO A CD  1 
ATOM   824   N  N   . VAL A 1 110  ? 90.493  79.450  133.289 1.00 54.64  ? 110  VAL A N   1 
ATOM   825   C  CA  . VAL A 1 110  ? 91.480  79.584  132.220 1.00 54.98  ? 110  VAL A CA  1 
ATOM   826   C  C   . VAL A 1 110  ? 92.712  78.760  132.567 1.00 54.33  ? 110  VAL A C   1 
ATOM   827   O  O   . VAL A 1 110  ? 93.160  78.742  133.713 1.00 53.98  ? 110  VAL A O   1 
ATOM   828   C  CB  . VAL A 1 110  ? 91.868  81.064  131.948 1.00 56.09  ? 110  VAL A CB  1 
ATOM   829   C  CG1 . VAL A 1 110  ? 92.904  81.151  130.858 1.00 57.99  ? 110  VAL A CG1 1 
ATOM   830   C  CG2 . VAL A 1 110  ? 90.650  81.868  131.521 1.00 56.66  ? 110  VAL A CG2 1 
ATOM   831   N  N   . PHE A 1 111  ? 93.232  78.063  131.567 1.00 54.04  ? 111  PHE A N   1 
ATOM   832   C  CA  . PHE A 1 111  ? 94.437  77.274  131.721 1.00 53.49  ? 111  PHE A CA  1 
ATOM   833   C  C   . PHE A 1 111  ? 95.505  77.760  130.745 1.00 54.93  ? 111  PHE A C   1 
ATOM   834   O  O   . PHE A 1 111  ? 95.203  78.402  129.734 1.00 55.52  ? 111  PHE A O   1 
ATOM   835   C  CB  . PHE A 1 111  ? 94.117  75.794  131.500 1.00 52.95  ? 111  PHE A CB  1 
ATOM   836   C  CG  . PHE A 1 111  ? 93.140  75.233  132.494 1.00 50.32  ? 111  PHE A CG  1 
ATOM   837   C  CD1 . PHE A 1 111  ? 93.587  74.639  133.667 1.00 48.34  ? 111  PHE A CD1 1 
ATOM   838   C  CD2 . PHE A 1 111  ? 91.771  75.308  132.262 1.00 48.71  ? 111  PHE A CD2 1 
ATOM   839   C  CE1 . PHE A 1 111  ? 92.691  74.132  134.592 1.00 46.34  ? 111  PHE A CE1 1 
ATOM   840   C  CE2 . PHE A 1 111  ? 90.864  74.801  133.187 1.00 46.56  ? 111  PHE A CE2 1 
ATOM   841   C  CZ  . PHE A 1 111  ? 91.327  74.216  134.356 1.00 45.49  ? 111  PHE A CZ  1 
ATOM   842   N  N   . LYS A 1 112  ? 96.760  77.478  131.064 1.00 55.33  ? 112  LYS A N   1 
ATOM   843   C  CA  . LYS A 1 112  ? 97.851  77.771  130.145 1.00 57.01  ? 112  LYS A CA  1 
ATOM   844   C  C   . LYS A 1 112  ? 98.480  76.457  129.629 1.00 57.29  ? 112  LYS A C   1 
ATOM   845   O  O   . LYS A 1 112  ? 98.288  75.396  130.240 1.00 56.36  ? 112  LYS A O   1 
ATOM   846   C  CB  . LYS A 1 112  ? 98.875  78.725  130.791 1.00 57.75  ? 112  LYS A CB  1 
ATOM   847   C  CG  . LYS A 1 112  ? 99.589  78.180  132.013 1.00 58.34  ? 112  LYS A CG  1 
ATOM   848   C  CD  . LYS A 1 112  ? 100.768 79.066  132.432 1.00 61.90  ? 112  LYS A CD  1 
ATOM   849   C  CE  . LYS A 1 112  ? 101.524 78.479  133.638 1.00 62.35  ? 112  LYS A CE  1 
ATOM   850   N  NZ  . LYS A 1 112  ? 100.676 78.428  134.882 1.00 60.60  ? 112  LYS A NZ  1 
ATOM   851   N  N   . PRO A 1 113  ? 99.195  76.514  128.489 1.00 58.60  ? 113  PRO A N   1 
ATOM   852   C  CA  . PRO A 1 113  ? 99.812  75.349  127.854 1.00 59.54  ? 113  PRO A CA  1 
ATOM   853   C  C   . PRO A 1 113  ? 100.389 74.283  128.785 1.00 59.20  ? 113  PRO A C   1 
ATOM   854   O  O   . PRO A 1 113  ? 100.135 73.094  128.597 1.00 59.24  ? 113  PRO A O   1 
ATOM   855   C  CB  . PRO A 1 113  ? 100.900 75.977  126.995 1.00 61.27  ? 113  PRO A CB  1 
ATOM   856   C  CG  . PRO A 1 113  ? 100.256 77.219  126.514 1.00 61.47  ? 113  PRO A CG  1 
ATOM   857   C  CD  . PRO A 1 113  ? 99.424  77.726  127.680 1.00 59.94  ? 113  PRO A CD  1 
ATOM   858   N  N   . GLY A 1 114  ? 101.151 74.681  129.783 1.00 59.33  ? 114  GLY A N   1 
ATOM   859   C  CA  . GLY A 1 114  ? 101.710 73.690  130.694 1.00 60.02  ? 114  GLY A CA  1 
ATOM   860   C  C   . GLY A 1 114  ? 100.756 72.784  131.477 1.00 59.07  ? 114  GLY A C   1 
ATOM   861   O  O   . GLY A 1 114  ? 101.046 71.603  131.655 1.00 59.40  ? 114  GLY A O   1 
ATOM   862   N  N   . ASP A 1 115  ? 99.618  73.314  131.931 1.00 57.91  ? 115  ASP A N   1 
ATOM   863   C  CA  . ASP A 1 115  ? 99.013  72.781  133.155 1.00 57.37  ? 115  ASP A CA  1 
ATOM   864   C  C   . ASP A 1 115  ? 97.936  71.697  133.060 1.00 56.39  ? 115  ASP A C   1 
ATOM   865   O  O   . ASP A 1 115  ? 97.579  71.245  131.974 1.00 56.91  ? 115  ASP A O   1 
ATOM   866   C  CB  . ASP A 1 115  ? 98.610  73.920  134.128 1.00 57.12  ? 115  ASP A CB  1 
ATOM   867   C  CG  . ASP A 1 115  ? 97.883  75.078  133.439 1.00 58.56  ? 115  ASP A CG  1 
ATOM   868   O  OD1 . ASP A 1 115  ? 96.797  74.851  132.870 1.00 60.31  ? 115  ASP A OD1 1 
ATOM   869   O  OD2 . ASP A 1 115  ? 98.381  76.225  133.499 1.00 60.17  ? 115  ASP A OD2 1 
ATOM   870   N  N   . THR A 1 116  ? 97.468  71.258  134.230 1.00 55.18  ? 116  THR A N   1 
ATOM   871   C  CA  . THR A 1 116  ? 96.519  70.158  134.353 1.00 54.38  ? 116  THR A CA  1 
ATOM   872   C  C   . THR A 1 116  ? 95.129  70.664  134.693 1.00 52.68  ? 116  THR A C   1 
ATOM   873   O  O   . THR A 1 116  ? 94.953  71.424  135.643 1.00 51.86  ? 116  THR A O   1 
ATOM   874   C  CB  . THR A 1 116  ? 96.957  69.147  135.439 1.00 54.67  ? 116  THR A CB  1 
ATOM   875   O  OG1 . THR A 1 116  ? 98.229  68.585  135.095 1.00 57.08  ? 116  THR A OG1 1 
ATOM   876   C  CG2 . THR A 1 116  ? 95.957  68.023  135.556 1.00 54.17  ? 116  THR A CG2 1 
ATOM   877   N  N   . VAL A 1 117  ? 94.146  70.241  133.905 1.00 52.38  ? 117  VAL A N   1 
ATOM   878   C  CA  . VAL A 1 117  ? 92.754  70.487  134.231 1.00 50.73  ? 117  VAL A CA  1 
ATOM   879   C  C   . VAL A 1 117  ? 92.286  69.383  135.162 1.00 50.64  ? 117  VAL A C   1 
ATOM   880   O  O   . VAL A 1 117  ? 92.337  68.207  134.815 1.00 51.66  ? 117  VAL A O   1 
ATOM   881   C  CB  . VAL A 1 117  ? 91.847  70.501  132.980 1.00 51.04  ? 117  VAL A CB  1 
ATOM   882   C  CG1 . VAL A 1 117  ? 90.378  70.720  133.386 1.00 49.53  ? 117  VAL A CG1 1 
ATOM   883   C  CG2 . VAL A 1 117  ? 92.299  71.560  131.983 1.00 50.69  ? 117  VAL A CG2 1 
ATOM   884   N  N   . ASN A 1 118  ? 91.853  69.776  136.350 1.00 49.76  ? 118  ASN A N   1 
ATOM   885   C  CA  . ASN A 1 118  ? 91.156  68.883  137.267 1.00 49.75  ? 118  ASN A CA  1 
ATOM   886   C  C   . ASN A 1 118  ? 89.669  69.204  137.279 1.00 48.38  ? 118  ASN A C   1 
ATOM   887   O  O   . ASN A 1 118  ? 89.268  70.371  137.342 1.00 47.13  ? 118  ASN A O   1 
ATOM   888   C  CB  . ASN A 1 118  ? 91.734  68.994  138.682 1.00 49.86  ? 118  ASN A CB  1 
ATOM   889   C  CG  . ASN A 1 118  ? 93.179  68.533  138.758 1.00 52.05  ? 118  ASN A CG  1 
ATOM   890   O  OD1 . ASN A 1 118  ? 93.468  67.332  138.772 1.00 53.88  ? 118  ASN A OD1 1 
ATOM   891   N  ND2 . ASN A 1 118  ? 94.094  69.489  138.805 1.00 52.84  ? 118  ASN A ND2 1 
ATOM   892   N  N   . PHE A 1 119  ? 88.855  68.162  137.211 1.00 48.65  ? 119  PHE A N   1 
ATOM   893   C  CA  . PHE A 1 119  ? 87.418  68.337  137.209 1.00 48.04  ? 119  PHE A CA  1 
ATOM   894   C  C   . PHE A 1 119  ? 86.711  67.244  137.994 1.00 48.86  ? 119  PHE A C   1 
ATOM   895   O  O   . PHE A 1 119  ? 87.243  66.141  138.179 1.00 49.78  ? 119  PHE A O   1 
ATOM   896   C  CB  . PHE A 1 119  ? 86.882  68.377  135.781 1.00 48.43  ? 119  PHE A CB  1 
ATOM   897   C  CG  . PHE A 1 119  ? 87.015  67.070  135.049 1.00 49.55  ? 119  PHE A CG  1 
ATOM   898   C  CD1 . PHE A 1 119  ? 88.144  66.798  134.289 1.00 49.39  ? 119  PHE A CD1 1 
ATOM   899   C  CD2 . PHE A 1 119  ? 86.015  66.111  135.127 1.00 49.86  ? 119  PHE A CD2 1 
ATOM   900   C  CE1 . PHE A 1 119  ? 88.273  65.600  133.625 1.00 51.11  ? 119  PHE A CE1 1 
ATOM   901   C  CE2 . PHE A 1 119  ? 86.138  64.900  134.460 1.00 51.47  ? 119  PHE A CE2 1 
ATOM   902   C  CZ  . PHE A 1 119  ? 87.269  64.649  133.708 1.00 52.41  ? 119  PHE A CZ  1 
ATOM   903   N  N   . ARG A 1 120  ? 85.504  67.580  138.447 1.00 48.51  ? 120  ARG A N   1 
ATOM   904   C  CA  . ARG A 1 120  ? 84.627  66.670  139.160 1.00 49.25  ? 120  ARG A CA  1 
ATOM   905   C  C   . ARG A 1 120  ? 83.239  66.739  138.520 1.00 49.67  ? 120  ARG A C   1 
ATOM   906   O  O   . ARG A 1 120  ? 82.765  67.821  138.125 1.00 48.61  ? 120  ARG A O   1 
ATOM   907   C  CB  . ARG A 1 120  ? 84.566  67.031  140.656 1.00 48.33  ? 120  ARG A CB  1 
ATOM   908   C  CG  . ARG A 1 120  ? 85.930  67.023  141.353 1.00 49.24  ? 120  ARG A CG  1 
ATOM   909   C  CD  . ARG A 1 120  ? 85.850  66.994  142.871 1.00 49.34  ? 120  ARG A CD  1 
ATOM   910   N  NE  . ARG A 1 120  ? 85.751  68.322  143.469 1.00 48.95  ? 120  ARG A NE  1 
ATOM   911   C  CZ  . ARG A 1 120  ? 86.619  68.842  144.340 1.00 49.40  ? 120  ARG A CZ  1 
ATOM   912   N  NH1 . ARG A 1 120  ? 87.688  68.157  144.748 1.00 49.50  ? 120  ARG A NH1 1 
ATOM   913   N  NH2 . ARG A 1 120  ? 86.406  70.064  144.816 1.00 48.29  ? 120  ARG A NH2 1 
ATOM   914   N  N   . VAL A 1 121  ? 82.601  65.578  138.405 1.00 51.37  ? 121  VAL A N   1 
ATOM   915   C  CA  . VAL A 1 121  ? 81.269  65.478  137.832 1.00 52.27  ? 121  VAL A CA  1 
ATOM   916   C  C   . VAL A 1 121  ? 80.324  65.036  138.930 1.00 53.09  ? 121  VAL A C   1 
ATOM   917   O  O   . VAL A 1 121  ? 80.472  63.945  139.481 1.00 54.20  ? 121  VAL A O   1 
ATOM   918   C  CB  . VAL A 1 121  ? 81.221  64.484  136.645 1.00 54.09  ? 121  VAL A CB  1 
ATOM   919   C  CG1 . VAL A 1 121  ? 79.787  64.288  136.156 1.00 54.22  ? 121  VAL A CG1 1 
ATOM   920   C  CG2 . VAL A 1 121  ? 82.107  64.964  135.519 1.00 53.20  ? 121  VAL A CG2 1 
ATOM   921   N  N   . ILE A 1 122  ? 79.367  65.903  139.254 1.00 53.09  ? 122  ILE A N   1 
ATOM   922   C  CA  . ILE A 1 122  ? 78.401  65.647  140.316 1.00 54.08  ? 122  ILE A CA  1 
ATOM   923   C  C   . ILE A 1 122  ? 77.109  65.153  139.699 1.00 55.73  ? 122  ILE A C   1 
ATOM   924   O  O   . ILE A 1 122  ? 76.544  65.828  138.834 1.00 55.68  ? 122  ILE A O   1 
ATOM   925   C  CB  . ILE A 1 122  ? 78.072  66.933  141.101 1.00 52.47  ? 122  ILE A CB  1 
ATOM   926   C  CG1 . ILE A 1 122  ? 79.329  67.766  141.382 1.00 52.13  ? 122  ILE A CG1 1 
ATOM   927   C  CG2 . ILE A 1 122  ? 77.304  66.603  142.387 1.00 52.79  ? 122  ILE A CG2 1 
ATOM   928   C  CD1 . ILE A 1 122  ? 80.058  67.373  142.642 1.00 52.77  ? 122  ILE A CD1 1 
ATOM   929   N  N   . VAL A 1 123  ? 76.639  63.987  140.135 1.00 58.01  ? 123  VAL A N   1 
ATOM   930   C  CA  . VAL A 1 123  ? 75.350  63.464  139.670 1.00 60.11  ? 123  VAL A CA  1 
ATOM   931   C  C   . VAL A 1 123  ? 74.408  63.205  140.844 1.00 61.07  ? 123  VAL A C   1 
ATOM   932   O  O   . VAL A 1 123  ? 74.650  62.311  141.657 1.00 62.30  ? 123  VAL A O   1 
ATOM   933   C  CB  . VAL A 1 123  ? 75.496  62.169  138.849 1.00 62.24  ? 123  VAL A CB  1 
ATOM   934   C  CG1 . VAL A 1 123  ? 74.169  61.820  138.186 1.00 63.39  ? 123  VAL A CG1 1 
ATOM   935   C  CG2 . VAL A 1 123  ? 76.587  62.307  137.807 1.00 62.31  ? 123  VAL A CG2 1 
ATOM   936   N  N   . LEU A 1 124  ? 73.335  63.989  140.924 1.00 61.15  ? 124  LEU A N   1 
ATOM   937   C  CA  . LEU A 1 124  ? 72.351  63.852  142.000 1.00 62.17  ? 124  LEU A CA  1 
ATOM   938   C  C   . LEU A 1 124  ? 70.945  63.654  141.446 1.00 64.01  ? 124  LEU A C   1 
ATOM   939   O  O   . LEU A 1 124  ? 70.581  64.269  140.436 1.00 64.20  ? 124  LEU A O   1 
ATOM   940   C  CB  . LEU A 1 124  ? 72.383  65.082  142.915 1.00 59.79  ? 124  LEU A CB  1 
ATOM   941   C  CG  . LEU A 1 124  ? 73.736  65.443  143.542 1.00 59.23  ? 124  LEU A CG  1 
ATOM   942   C  CD1 . LEU A 1 124  ? 73.770  66.893  144.027 1.00 57.33  ? 124  LEU A CD1 1 
ATOM   943   C  CD2 . LEU A 1 124  ? 74.128  64.484  144.660 1.00 59.37  ? 124  LEU A CD2 1 
ATOM   944   N  N   . ASP A 1 125  ? 70.149  62.809  142.100 1.00 66.03  ? 125  ASP A N   1 
ATOM   945   C  CA  . ASP A 1 125  ? 68.746  62.655  141.704 1.00 67.86  ? 125  ASP A CA  1 
ATOM   946   C  C   . ASP A 1 125  ? 67.838  63.758  142.280 1.00 66.72  ? 125  ASP A C   1 
ATOM   947   O  O   . ASP A 1 125  ? 68.324  64.746  142.839 1.00 64.63  ? 125  ASP A O   1 
ATOM   948   C  CB  . ASP A 1 125  ? 68.224  61.254  142.045 1.00 70.44  ? 125  ASP A CB  1 
ATOM   949   C  CG  . ASP A 1 125  ? 68.108  61.007  143.538 1.00 70.64  ? 125  ASP A CG  1 
ATOM   950   O  OD1 . ASP A 1 125  ? 68.165  61.976  144.328 1.00 68.25  ? 125  ASP A OD1 1 
ATOM   951   O  OD2 . ASP A 1 125  ? 67.950  59.823  143.913 1.00 73.20  ? 125  ASP A OD2 1 
ATOM   952   N  N   . THR A 1 126  ? 66.524  63.576  142.132 1.00 68.48  ? 126  THR A N   1 
ATOM   953   C  CA  . THR A 1 126  ? 65.501  64.532  142.607 1.00 67.78  ? 126  THR A CA  1 
ATOM   954   C  C   . THR A 1 126  ? 65.579  64.795  144.108 1.00 66.78  ? 126  THR A C   1 
ATOM   955   O  O   . THR A 1 126  ? 65.193  65.867  144.585 1.00 65.28  ? 126  THR A O   1 
ATOM   956   C  CB  . THR A 1 126  ? 64.075  64.024  142.304 1.00 69.67  ? 126  THR A CB  1 
ATOM   957   O  OG1 . THR A 1 126  ? 63.992  62.629  142.613 1.00 71.79  ? 126  THR A OG1 1 
ATOM   958   C  CG2 . THR A 1 126  ? 63.723  64.231  140.840 1.00 71.10  ? 126  THR A CG2 1 
ATOM   959   N  N   . GLU A 1 127  ? 66.080  63.804  144.839 1.00 67.90  ? 127  GLU A N   1 
ATOM   960   C  CA  . GLU A 1 127  ? 66.229  63.881  146.284 1.00 67.55  ? 127  GLU A CA  1 
ATOM   961   C  C   . GLU A 1 127  ? 67.577  64.520  146.678 1.00 65.75  ? 127  GLU A C   1 
ATOM   962   O  O   . GLU A 1 127  ? 67.906  64.618  147.866 1.00 65.29  ? 127  GLU A O   1 
ATOM   963   C  CB  . GLU A 1 127  ? 66.102  62.469  146.858 1.00 70.11  ? 127  GLU A CB  1 
ATOM   964   C  CG  . GLU A 1 127  ? 65.457  62.377  148.223 1.00 71.76  ? 127  GLU A CG  1 
ATOM   965   C  CD  . GLU A 1 127  ? 65.055  60.951  148.572 1.00 76.73  ? 127  GLU A CD  1 
ATOM   966   O  OE1 . GLU A 1 127  ? 64.090  60.438  147.961 1.00 79.04  ? 127  GLU A OE1 1 
ATOM   967   O  OE2 . GLU A 1 127  ? 65.697  60.347  149.463 1.00 78.41  ? 127  GLU A OE2 1 
ATOM   968   N  N   . LEU A 1 128  ? 68.338  64.957  145.667 1.00 64.79  ? 128  LEU A N   1 
ATOM   969   C  CA  . LEU A 1 128  ? 69.681  65.541  145.826 1.00 63.09  ? 128  LEU A CA  1 
ATOM   970   C  C   . LEU A 1 128  ? 70.661  64.587  146.510 1.00 64.10  ? 128  LEU A C   1 
ATOM   971   O  O   . LEU A 1 128  ? 71.417  64.981  147.398 1.00 63.46  ? 128  LEU A O   1 
ATOM   972   C  CB  . LEU A 1 128  ? 69.633  66.909  146.529 1.00 61.14  ? 128  LEU A CB  1 
ATOM   973   C  CG  . LEU A 1 128  ? 68.700  68.009  145.989 1.00 60.06  ? 128  LEU A CG  1 
ATOM   974   C  CD1 . LEU A 1 128  ? 68.854  69.292  146.791 1.00 57.96  ? 128  LEU A CD1 1 
ATOM   975   C  CD2 . LEU A 1 128  ? 68.914  68.294  144.509 1.00 60.37  ? 128  LEU A CD2 1 
ATOM   976   N  N   . LYS A 1 129  ? 70.628  63.326  146.084 1.00 66.05  ? 129  LYS A N   1 
ATOM   977   C  CA  . LYS A 1 129  ? 71.543  62.288  146.561 1.00 67.45  ? 129  LYS A CA  1 
ATOM   978   C  C   . LYS A 1 129  ? 72.070  61.489  145.359 1.00 68.68  ? 129  LYS A C   1 
ATOM   979   O  O   . LYS A 1 129  ? 71.546  61.641  144.250 1.00 68.71  ? 129  LYS A O   1 
ATOM   980   C  CB  . LYS A 1 129  ? 70.838  61.364  147.567 1.00 69.34  ? 129  LYS A CB  1 
ATOM   981   C  CG  . LYS A 1 129  ? 69.507  60.804  147.084 1.00 71.47  ? 129  LYS A CG  1 
ATOM   982   C  CD  . LYS A 1 129  ? 69.145  59.476  147.741 1.00 74.71  ? 129  LYS A CD  1 
ATOM   983   C  CE  . LYS A 1 129  ? 67.818  58.972  147.181 1.00 76.89  ? 129  LYS A CE  1 
ATOM   984   N  NZ  . LYS A 1 129  ? 67.575  57.531  147.445 1.00 80.96  ? 129  LYS A NZ  1 
ATOM   985   N  N   . PRO A 1 130  ? 73.109  60.646  145.564 1.00 69.84  ? 130  PRO A N   1 
ATOM   986   C  CA  . PRO A 1 130  ? 73.582  59.836  144.440 1.00 71.36  ? 130  PRO A CA  1 
ATOM   987   C  C   . PRO A 1 130  ? 72.466  58.922  143.972 1.00 73.50  ? 130  PRO A C   1 
ATOM   988   O  O   . PRO A 1 130  ? 71.836  58.274  144.804 1.00 74.89  ? 130  PRO A O   1 
ATOM   989   C  CB  . PRO A 1 130  ? 74.715  58.997  145.046 1.00 72.55  ? 130  PRO A CB  1 
ATOM   990   C  CG  . PRO A 1 130  ? 75.106  59.694  146.285 1.00 71.14  ? 130  PRO A CG  1 
ATOM   991   C  CD  . PRO A 1 130  ? 73.884  60.385  146.791 1.00 70.09  ? 130  PRO A CD  1 
ATOM   992   N  N   . PRO A 1 131  ? 72.202  58.887  142.654 1.00 74.20  ? 131  PRO A N   1 
ATOM   993   C  CA  . PRO A 1 131  ? 71.153  58.023  142.136 1.00 76.65  ? 131  PRO A CA  1 
ATOM   994   C  C   . PRO A 1 131  ? 71.544  56.581  142.390 1.00 79.62  ? 131  PRO A C   1 
ATOM   995   O  O   . PRO A 1 131  ? 72.702  56.214  142.180 1.00 80.21  ? 131  PRO A O   1 
ATOM   996   C  CB  . PRO A 1 131  ? 71.156  58.314  140.633 1.00 76.64  ? 131  PRO A CB  1 
ATOM   997   C  CG  . PRO A 1 131  ? 71.876  59.584  140.477 1.00 74.21  ? 131  PRO A CG  1 
ATOM   998   C  CD  . PRO A 1 131  ? 72.872  59.635  141.579 1.00 73.10  ? 131  PRO A CD  1 
ATOM   999   N  N   . ALA A 1 132  ? 70.596  55.785  142.869 1.00 81.80  ? 132  ALA A N   1 
ATOM   1000  C  CA  . ALA A 1 132  ? 70.851  54.380  143.145 1.00 85.19  ? 132  ALA A CA  1 
ATOM   1001  C  C   . ALA A 1 132  ? 71.045  53.614  141.845 1.00 87.63  ? 132  ALA A C   1 
ATOM   1002  O  O   . ALA A 1 132  ? 71.817  52.653  141.793 1.00 89.78  ? 132  ALA A O   1 
ATOM   1003  C  CB  . ALA A 1 132  ? 69.716  53.781  143.955 1.00 86.99  ? 132  ALA A CB  1 
ATOM   1004  N  N   . ARG A 1 133  ? 70.351  54.059  140.798 1.00 87.59  ? 133  ARG A N   1 
ATOM   1005  C  CA  . ARG A 1 133  ? 70.386  53.398  139.492 1.00 90.16  ? 133  ARG A CA  1 
ATOM   1006  C  C   . ARG A 1 133  ? 71.680  53.670  138.720 1.00 88.74  ? 133  ARG A C   1 
ATOM   1007  O  O   . ARG A 1 133  ? 72.280  52.750  138.164 1.00 91.13  ? 133  ARG A O   1 
ATOM   1008  C  CB  . ARG A 1 133  ? 69.163  53.791  138.650 1.00 90.83  ? 133  ARG A CB  1 
ATOM   1009  C  CG  . ARG A 1 133  ? 67.841  53.221  139.162 1.00 94.36  ? 133  ARG A CG  1 
ATOM   1010  C  CD  . ARG A 1 133  ? 66.685  53.550  138.218 1.00 97.44  ? 133  ARG A CD  1 
ATOM   1011  N  NE  . ARG A 1 133  ? 65.595  52.575  138.315 1.00 102.01 ? 133  ARG A NE  1 
ATOM   1012  C  CZ  . ARG A 1 133  ? 64.755  52.274  137.323 1.00 105.20 ? 133  ARG A CZ  1 
ATOM   1013  N  NH1 . ARG A 1 133  ? 64.867  52.862  136.136 1.00 104.76 ? 133  ARG A NH1 1 
ATOM   1014  N  NH2 . ARG A 1 133  ? 63.801  51.371  137.516 1.00 108.57 ? 133  ARG A NH2 1 
ATOM   1015  N  N   . VAL A 1 134  ? 72.107  54.932  138.703 1.00 84.90  ? 134  VAL A N   1 
ATOM   1016  C  CA  . VAL A 1 134  ? 73.261  55.361  137.909 1.00 83.16  ? 134  VAL A CA  1 
ATOM   1017  C  C   . VAL A 1 134  ? 74.573  55.041  138.616 1.00 82.13  ? 134  VAL A C   1 
ATOM   1018  O  O   . VAL A 1 134  ? 74.909  55.657  139.629 1.00 80.01  ? 134  VAL A O   1 
ATOM   1019  C  CB  . VAL A 1 134  ? 73.198  56.865  137.597 1.00 80.25  ? 134  VAL A CB  1 
ATOM   1020  C  CG1 . VAL A 1 134  ? 74.281  57.241  136.594 1.00 79.98  ? 134  VAL A CG1 1 
ATOM   1021  C  CG2 . VAL A 1 134  ? 71.819  57.241  137.064 1.00 80.76  ? 134  VAL A CG2 1 
ATOM   1022  N  N   . LYS A 1 135  ? 75.307  54.082  138.060 1.00 83.57  ? 135  LYS A N   1 
ATOM   1023  C  CA  . LYS A 1 135  ? 76.544  53.579  138.657 1.00 83.13  ? 135  LYS A CA  1 
ATOM   1024  C  C   . LYS A 1 135  ? 77.784  54.232  138.037 1.00 80.74  ? 135  LYS A C   1 
ATOM   1025  O  O   . LYS A 1 135  ? 78.827  54.349  138.689 1.00 79.76  ? 135  LYS A O   1 
ATOM   1026  C  CB  . LYS A 1 135  ? 76.606  52.055  138.509 1.00 87.08  ? 135  LYS A CB  1 
ATOM   1027  C  CG  . LYS A 1 135  ? 77.629  51.350  139.396 1.00 88.79  ? 135  LYS A CG  1 
ATOM   1028  C  CD  . LYS A 1 135  ? 77.694  49.853  139.056 1.00 94.48  ? 135  LYS A CD  1 
ATOM   1029  C  CE  . LYS A 1 135  ? 78.892  49.151  139.703 1.00 95.70  ? 135  LYS A CE  1 
ATOM   1030  N  NZ  . LYS A 1 135  ? 79.016  47.737  139.241 1.00 99.33  ? 135  LYS A NZ  1 
ATOM   1031  N  N   . SER A 1 136  ? 77.657  54.656  136.778 1.00 79.58  ? 136  SER A N   1 
ATOM   1032  C  CA  . SER A 1 136  ? 78.741  55.316  136.048 1.00 77.25  ? 136  SER A CA  1 
ATOM   1033  C  C   . SER A 1 136  ? 78.202  56.261  134.974 1.00 75.69  ? 136  SER A C   1 
ATOM   1034  O  O   . SER A 1 136  ? 77.024  56.192  134.604 1.00 76.40  ? 136  SER A O   1 
ATOM   1035  C  CB  . SER A 1 136  ? 79.671  54.285  135.405 1.00 79.69  ? 136  SER A CB  1 
ATOM   1036  O  OG  . SER A 1 136  ? 79.083  53.733  134.242 1.00 81.60  ? 136  SER A OG  1 
ATOM   1037  N  N   . VAL A 1 137  ? 79.078  57.139  134.481 1.00 73.22  ? 137  VAL A N   1 
ATOM   1038  C  CA  . VAL A 1 137  ? 78.738  58.080  133.414 1.00 71.64  ? 137  VAL A CA  1 
ATOM   1039  C  C   . VAL A 1 137  ? 79.725  58.033  132.236 1.00 72.18  ? 137  VAL A C   1 
ATOM   1040  O  O   . VAL A 1 137  ? 80.771  57.377  132.295 1.00 72.96  ? 137  VAL A O   1 
ATOM   1041  C  CB  . VAL A 1 137  ? 78.603  59.545  133.936 1.00 68.51  ? 137  VAL A CB  1 
ATOM   1042  C  CG1 . VAL A 1 137  ? 77.381  59.692  134.824 1.00 68.15  ? 137  VAL A CG1 1 
ATOM   1043  C  CG2 . VAL A 1 137  ? 79.858  59.992  134.670 1.00 66.34  ? 137  VAL A CG2 1 
ATOM   1044  N  N   . TYR A 1 138  ? 79.362  58.743  131.170 1.00 71.47  ? 138  TYR A N   1 
ATOM   1045  C  CA  . TYR A 1 138  ? 80.171  58.877  129.969 1.00 71.52  ? 138  TYR A CA  1 
ATOM   1046  C  C   . TYR A 1 138  ? 80.638  60.335  129.865 1.00 68.34  ? 138  TYR A C   1 
ATOM   1047  O  O   . TYR A 1 138  ? 79.840  61.237  129.599 1.00 67.20  ? 138  TYR A O   1 
ATOM   1048  C  CB  . TYR A 1 138  ? 79.331  58.502  128.744 1.00 74.07  ? 138  TYR A CB  1 
ATOM   1049  C  CG  . TYR A 1 138  ? 80.115  58.076  127.521 1.00 76.69  ? 138  TYR A CG  1 
ATOM   1050  C  CD1 . TYR A 1 138  ? 80.027  56.770  127.038 1.00 80.31  ? 138  TYR A CD1 1 
ATOM   1051  C  CD2 . TYR A 1 138  ? 80.928  58.974  126.833 1.00 76.32  ? 138  TYR A CD2 1 
ATOM   1052  C  CE1 . TYR A 1 138  ? 80.737  56.367  125.909 1.00 82.58  ? 138  TYR A CE1 1 
ATOM   1053  C  CE2 . TYR A 1 138  ? 81.646  58.577  125.703 1.00 78.66  ? 138  TYR A CE2 1 
ATOM   1054  C  CZ  . TYR A 1 138  ? 81.544  57.275  125.248 1.00 81.88  ? 138  TYR A CZ  1 
ATOM   1055  O  OH  . TYR A 1 138  ? 82.250  56.885  124.132 1.00 84.70  ? 138  TYR A OH  1 
ATOM   1056  N  N   . VAL A 1 139  ? 81.926  60.567  130.088 1.00 66.59  ? 139  VAL A N   1 
ATOM   1057  C  CA  . VAL A 1 139  ? 82.479  61.908  129.943 1.00 64.10  ? 139  VAL A CA  1 
ATOM   1058  C  C   . VAL A 1 139  ? 83.498  61.985  128.806 1.00 64.84  ? 139  VAL A C   1 
ATOM   1059  O  O   . VAL A 1 139  ? 84.363  61.123  128.678 1.00 66.28  ? 139  VAL A O   1 
ATOM   1060  C  CB  . VAL A 1 139  ? 83.022  62.480  131.291 1.00 61.76  ? 139  VAL A CB  1 
ATOM   1061  C  CG1 . VAL A 1 139  ? 83.504  61.379  132.204 1.00 62.59  ? 139  VAL A CG1 1 
ATOM   1062  C  CG2 . VAL A 1 139  ? 84.111  63.515  131.066 1.00 60.51  ? 139  VAL A CG2 1 
ATOM   1063  N  N   . THR A 1 140  ? 83.355  63.005  127.961 1.00 63.94  ? 140  THR A N   1 
ATOM   1064  C  CA  . THR A 1 140  ? 84.293  63.255  126.865 1.00 64.50  ? 140  THR A CA  1 
ATOM   1065  C  C   . THR A 1 140  ? 84.768  64.708  126.879 1.00 61.99  ? 140  THR A C   1 
ATOM   1066  O  O   . THR A 1 140  ? 83.971  65.626  127.076 1.00 60.73  ? 140  THR A O   1 
ATOM   1067  C  CB  . THR A 1 140  ? 83.688  62.964  125.464 1.00 66.87  ? 140  THR A CB  1 
ATOM   1068  O  OG1 . THR A 1 140  ? 82.883  64.073  125.050 1.00 67.08  ? 140  THR A OG1 1 
ATOM   1069  C  CG2 . THR A 1 140  ? 82.841  61.713  125.463 1.00 69.08  ? 140  THR A CG2 1 
ATOM   1070  N  N   . ILE A 1 141  ? 86.064  64.905  126.657 1.00 61.13  ? 141  ILE A N   1 
ATOM   1071  C  CA  . ILE A 1 141  ? 86.626  66.240  126.520 1.00 58.87  ? 141  ILE A CA  1 
ATOM   1072  C  C   . ILE A 1 141  ? 87.113  66.426  125.097 1.00 60.24  ? 141  ILE A C   1 
ATOM   1073  O  O   . ILE A 1 141  ? 87.787  65.554  124.550 1.00 61.86  ? 141  ILE A O   1 
ATOM   1074  C  CB  . ILE A 1 141  ? 87.782  66.480  127.504 1.00 57.46  ? 141  ILE A CB  1 
ATOM   1075  C  CG1 . ILE A 1 141  ? 87.311  66.219  128.944 1.00 55.53  ? 141  ILE A CG1 1 
ATOM   1076  C  CG2 . ILE A 1 141  ? 88.340  67.894  127.323 1.00 56.25  ? 141  ILE A CG2 1 
ATOM   1077  C  CD1 . ILE A 1 141  ? 88.323  66.564  130.025 1.00 53.68  ? 141  ILE A CD1 1 
ATOM   1078  N  N   . ARG A 1 142  ? 86.751  67.551  124.491 1.00 59.64  ? 142  ARG A N   1 
ATOM   1079  C  CA  . ARG A 1 142  ? 87.248  67.885  123.164 1.00 61.06  ? 142  ARG A CA  1 
ATOM   1080  C  C   . ARG A 1 142  ? 87.761  69.319  123.060 1.00 59.72  ? 142  ARG A C   1 
ATOM   1081  O  O   . ARG A 1 142  ? 87.349  70.193  123.827 1.00 58.02  ? 142  ARG A O   1 
ATOM   1082  C  CB  . ARG A 1 142  ? 86.214  67.548  122.084 1.00 63.46  ? 142  ARG A CB  1 
ATOM   1083  C  CG  . ARG A 1 142  ? 84.911  68.277  122.179 1.00 63.62  ? 142  ARG A CG  1 
ATOM   1084  C  CD  . ARG A 1 142  ? 83.749  67.289  122.160 1.00 65.56  ? 142  ARG A CD  1 
ATOM   1085  N  NE  . ARG A 1 142  ? 83.615  66.528  120.924 1.00 66.75  ? 142  ARG A NE  1 
ATOM   1086  C  CZ  . ARG A 1 142  ? 82.740  65.536  120.752 1.00 68.91  ? 142  ARG A CZ  1 
ATOM   1087  N  NH1 . ARG A 1 142  ? 81.930  65.174  121.746 1.00 66.22  ? 142  ARG A NH1 1 
ATOM   1088  N  NH2 . ARG A 1 142  ? 82.681  64.895  119.584 1.00 71.00  ? 142  ARG A NH2 1 
ATOM   1089  N  N   . ASP A 1 143  ? 88.685  69.544  122.128 1.00 60.40  ? 143  ASP A N   1 
ATOM   1090  C  CA  . ASP A 1 143  ? 89.339  70.843  121.988 1.00 59.35  ? 143  ASP A CA  1 
ATOM   1091  C  C   . ASP A 1 143  ? 88.452  71.853  121.256 1.00 59.83  ? 143  ASP A C   1 
ATOM   1092  O  O   . ASP A 1 143  ? 87.364  71.498  120.814 1.00 60.64  ? 143  ASP A O   1 
ATOM   1093  C  CB  . ASP A 1 143  ? 90.699  70.691  121.292 1.00 60.66  ? 143  ASP A CB  1 
ATOM   1094  C  CG  . ASP A 1 143  ? 90.593  70.130  119.881 1.00 62.83  ? 143  ASP A CG  1 
ATOM   1095  O  OD1 . ASP A 1 143  ? 91.606  69.588  119.399 1.00 63.42  ? 143  ASP A OD1 1 
ATOM   1096  O  OD2 . ASP A 1 143  ? 89.520  70.226  119.249 1.00 63.24  ? 143  ASP A OD2 1 
ATOM   1097  N  N   . PRO A 1 144  ? 88.906  73.117  121.143 1.00 59.60  ? 144  PRO A N   1 
ATOM   1098  C  CA  . PRO A 1 144  ? 88.181  74.186  120.453 1.00 60.45  ? 144  PRO A CA  1 
ATOM   1099  C  C   . PRO A 1 144  ? 87.682  73.852  119.049 1.00 63.01  ? 144  PRO A C   1 
ATOM   1100  O  O   . PRO A 1 144  ? 86.842  74.571  118.514 1.00 63.64  ? 144  PRO A O   1 
ATOM   1101  C  CB  . PRO A 1 144  ? 89.212  75.315  120.399 1.00 60.68  ? 144  PRO A CB  1 
ATOM   1102  C  CG  . PRO A 1 144  ? 90.012  75.112  121.623 1.00 58.64  ? 144  PRO A CG  1 
ATOM   1103  C  CD  . PRO A 1 144  ? 90.157  73.628  121.735 1.00 58.80  ? 144  PRO A CD  1 
ATOM   1104  N  N   . GLN A 1 145  ? 88.181  72.770  118.468 1.00 64.61  ? 145  GLN A N   1 
ATOM   1105  C  CA  . GLN A 1 145  ? 87.734  72.346  117.143 1.00 67.79  ? 145  GLN A CA  1 
ATOM   1106  C  C   . GLN A 1 145  ? 87.111  70.955  117.162 1.00 68.08  ? 145  GLN A C   1 
ATOM   1107  O  O   . GLN A 1 145  ? 87.039  70.265  116.129 1.00 70.49  ? 145  GLN A O   1 
ATOM   1108  C  CB  . GLN A 1 145  ? 88.858  72.474  116.104 1.00 70.05  ? 145  GLN A CB  1 
ATOM   1109  C  CG  . GLN A 1 145  ? 88.959  73.888  115.548 1.00 72.61  ? 145  GLN A CG  1 
ATOM   1110  C  CD  . GLN A 1 145  ? 90.088  74.072  114.560 1.00 77.96  ? 145  GLN A CD  1 
ATOM   1111  O  OE1 . GLN A 1 145  ? 90.916  73.177  114.352 1.00 80.07  ? 145  GLN A OE1 1 
ATOM   1112  N  NE2 . GLN A 1 145  ? 90.134  75.248  113.941 1.00 80.62  ? 145  GLN A NE2 1 
ATOM   1113  N  N   . ARG A 1 146  ? 86.673  70.564  118.359 1.00 65.55  ? 146  ARG A N   1 
ATOM   1114  C  CA  . ARG A 1 146  ? 85.793  69.413  118.569 1.00 65.86  ? 146  ARG A CA  1 
ATOM   1115  C  C   . ARG A 1 146  ? 86.444  68.028  118.386 1.00 66.65  ? 146  ARG A C   1 
ATOM   1116  O  O   . ARG A 1 146  ? 85.740  67.024  118.251 1.00 67.91  ? 146  ARG A O   1 
ATOM   1117  C  CB  . ARG A 1 146  ? 84.538  69.553  117.696 1.00 68.00  ? 146  ARG A CB  1 
ATOM   1118  C  CG  . ARG A 1 146  ? 83.654  70.755  118.038 1.00 68.03  ? 146  ARG A CG  1 
ATOM   1119  C  CD  . ARG A 1 146  ? 82.359  70.297  118.675 1.00 70.39  ? 146  ARG A CD  1 
ATOM   1120  N  NE  . ARG A 1 146  ? 81.656  69.356  117.800 1.00 75.74  ? 146  ARG A NE  1 
ATOM   1121  C  CZ  . ARG A 1 146  ? 80.676  68.539  118.187 1.00 76.98  ? 146  ARG A CZ  1 
ATOM   1122  N  NH1 . ARG A 1 146  ? 80.257  68.531  119.453 1.00 73.77  ? 146  ARG A NH1 1 
ATOM   1123  N  NH2 . ARG A 1 146  ? 80.113  67.726  117.295 1.00 80.16  ? 146  ARG A NH2 1 
ATOM   1124  N  N   . ASN A 1 147  ? 87.776  67.972  118.387 1.00 65.99  ? 147  ASN A N   1 
ATOM   1125  C  CA  . ASN A 1 147  ? 88.490  66.694  118.382 1.00 66.60  ? 147  ASN A CA  1 
ATOM   1126  C  C   . ASN A 1 147  ? 88.393  66.057  119.756 1.00 64.49  ? 147  ASN A C   1 
ATOM   1127  O  O   . ASN A 1 147  ? 88.610  66.725  120.755 1.00 62.06  ? 147  ASN A O   1 
ATOM   1128  C  CB  . ASN A 1 147  ? 89.968  66.878  118.044 1.00 66.66  ? 147  ASN A CB  1 
ATOM   1129  C  CG  . ASN A 1 147  ? 90.186  67.620  116.759 1.00 68.20  ? 147  ASN A CG  1 
ATOM   1130  O  OD1 . ASN A 1 147  ? 89.817  67.154  115.681 1.00 72.13  ? 147  ASN A OD1 1 
ATOM   1131  N  ND2 . ASN A 1 147  ? 90.817  68.774  116.856 1.00 66.30  ? 147  ASN A ND2 1 
ATOM   1132  N  N   . VAL A 1 148  ? 88.075  64.772  119.812 1.00 65.80  ? 148  VAL A N   1 
ATOM   1133  C  CA  . VAL A 1 148  ? 88.023  64.078  121.087 1.00 64.57  ? 148  VAL A CA  1 
ATOM   1134  C  C   . VAL A 1 148  ? 89.437  63.840  121.585 1.00 64.30  ? 148  VAL A C   1 
ATOM   1135  O  O   . VAL A 1 148  ? 90.234  63.162  120.933 1.00 66.33  ? 148  VAL A O   1 
ATOM   1136  C  CB  . VAL A 1 148  ? 87.242  62.747  121.005 1.00 66.40  ? 148  VAL A CB  1 
ATOM   1137  C  CG1 . VAL A 1 148  ? 87.200  62.064  122.373 1.00 64.96  ? 148  VAL A CG1 1 
ATOM   1138  C  CG2 . VAL A 1 148  ? 85.826  62.990  120.498 1.00 67.10  ? 148  VAL A CG2 1 
ATOM   1139  N  N   . ILE A 1 149  ? 89.741  64.413  122.743 1.00 62.34  ? 149  ILE A N   1 
ATOM   1140  C  CA  . ILE A 1 149  ? 91.073  64.304  123.330 1.00 62.20  ? 149  ILE A CA  1 
ATOM   1141  C  C   . ILE A 1 149  ? 91.096  63.305  124.476 1.00 62.10  ? 149  ILE A C   1 
ATOM   1142  O  O   . ILE A 1 149  ? 92.066  62.567  124.638 1.00 62.94  ? 149  ILE A O   1 
ATOM   1143  C  CB  . ILE A 1 149  ? 91.620  65.688  123.723 1.00 60.07  ? 149  ILE A CB  1 
ATOM   1144  C  CG1 . ILE A 1 149  ? 92.112  66.368  122.457 1.00 62.70  ? 149  ILE A CG1 1 
ATOM   1145  C  CG2 . ILE A 1 149  ? 92.779  65.587  124.693 1.00 58.03  ? 149  ILE A CG2 1 
ATOM   1146  C  CD1 . ILE A 1 149  ? 91.628  67.751  122.321 1.00 64.20  ? 149  ILE A CD1 1 
ATOM   1147  N  N   . ARG A 1 150  ? 90.017  63.261  125.245 1.00 61.63  ? 150  ARG A N   1 
ATOM   1148  C  CA  . ARG A 1 150  ? 89.914  62.284  126.310 1.00 62.58  ? 150  ARG A CA  1 
ATOM   1149  C  C   . ARG A 1 150  ? 88.483  61.786  126.498 1.00 63.21  ? 150  ARG A C   1 
ATOM   1150  O  O   . ARG A 1 150  ? 87.551  62.576  126.628 1.00 61.66  ? 150  ARG A O   1 
ATOM   1151  C  CB  . ARG A 1 150  ? 90.473  62.854  127.608 1.00 60.63  ? 150  ARG A CB  1 
ATOM   1152  C  CG  . ARG A 1 150  ? 90.970  61.799  128.581 1.00 62.99  ? 150  ARG A CG  1 
ATOM   1153  C  CD  . ARG A 1 150  ? 92.494  61.741  128.671 1.00 66.17  ? 150  ARG A CD  1 
ATOM   1154  N  NE  . ARG A 1 150  ? 92.940  61.876  130.064 1.00 67.43  ? 150  ARG A NE  1 
ATOM   1155  C  CZ  . ARG A 1 150  ? 92.868  60.919  130.996 1.00 69.16  ? 150  ARG A CZ  1 
ATOM   1156  N  NH1 . ARG A 1 150  ? 92.361  59.720  130.709 1.00 71.31  ? 150  ARG A NH1 1 
ATOM   1157  N  NH2 . ARG A 1 150  ? 93.300  61.166  132.230 1.00 67.90  ? 150  ARG A NH2 1 
ATOM   1158  N  N   . LYS A 1 151  ? 88.332  60.463  126.477 1.00 66.05  ? 151  LYS A N   1 
ATOM   1159  C  CA  . LYS A 1 151  ? 87.062  59.781  126.727 1.00 67.72  ? 151  LYS A CA  1 
ATOM   1160  C  C   . LYS A 1 151  ? 87.150  58.976  128.010 1.00 68.07  ? 151  LYS A C   1 
ATOM   1161  O  O   . LYS A 1 151  ? 88.163  58.333  128.283 1.00 69.15  ? 151  LYS A O   1 
ATOM   1162  C  CB  . LYS A 1 151  ? 86.730  58.807  125.594 1.00 70.75  ? 151  LYS A CB  1 
ATOM   1163  C  CG  . LYS A 1 151  ? 85.691  59.282  124.584 1.00 72.29  ? 151  LYS A CG  1 
ATOM   1164  C  CD  . LYS A 1 151  ? 85.345  58.177  123.559 1.00 77.29  ? 151  LYS A CD  1 
ATOM   1165  C  CE  . LYS A 1 151  ? 86.532  57.869  122.620 1.00 80.11  ? 151  LYS A CE  1 
ATOM   1166  N  NZ  . LYS A 1 151  ? 86.150  57.196  121.341 1.00 83.62  ? 151  LYS A NZ  1 
ATOM   1167  N  N   . TRP A 1 152  ? 86.087  59.015  128.797 1.00 67.79  ? 152  TRP A N   1 
ATOM   1168  C  CA  . TRP A 1 152  ? 85.878  58.016  129.822 1.00 69.25  ? 152  TRP A CA  1 
ATOM   1169  C  C   . TRP A 1 152  ? 84.527  57.372  129.526 1.00 71.56  ? 152  TRP A C   1 
ATOM   1170  O  O   . TRP A 1 152  ? 83.482  57.933  129.855 1.00 70.44  ? 152  TRP A O   1 
ATOM   1171  C  CB  . TRP A 1 152  ? 85.886  58.645  131.207 1.00 66.60  ? 152  TRP A CB  1 
ATOM   1172  C  CG  . TRP A 1 152  ? 87.209  59.184  131.670 1.00 65.43  ? 152  TRP A CG  1 
ATOM   1173  C  CD1 . TRP A 1 152  ? 88.128  58.539  132.444 1.00 65.77  ? 152  TRP A CD1 1 
ATOM   1174  C  CD2 . TRP A 1 152  ? 87.738  60.499  131.436 1.00 63.92  ? 152  TRP A CD2 1 
ATOM   1175  N  NE1 . TRP A 1 152  ? 89.198  59.363  132.702 1.00 64.15  ? 152  TRP A NE1 1 
ATOM   1176  C  CE2 . TRP A 1 152  ? 88.986  60.571  132.092 1.00 63.07  ? 152  TRP A CE2 1 
ATOM   1177  C  CE3 . TRP A 1 152  ? 87.282  61.622  130.732 1.00 62.91  ? 152  TRP A CE3 1 
ATOM   1178  C  CZ2 . TRP A 1 152  ? 89.784  61.719  132.060 1.00 61.71  ? 152  TRP A CZ2 1 
ATOM   1179  C  CZ3 . TRP A 1 152  ? 88.081  62.766  130.705 1.00 60.88  ? 152  TRP A CZ3 1 
ATOM   1180  C  CH2 . TRP A 1 152  ? 89.313  62.803  131.364 1.00 60.25  ? 152  TRP A CH2 1 
ATOM   1181  N  N   . SER A 1 153  ? 84.553  56.211  128.874 1.00 75.49  ? 153  SER A N   1 
ATOM   1182  C  CA  . SER A 1 153  ? 83.325  55.542  128.444 1.00 78.52  ? 153  SER A CA  1 
ATOM   1183  C  C   . SER A 1 153  ? 82.462  55.136  129.635 1.00 79.05  ? 153  SER A C   1 
ATOM   1184  O  O   . SER A 1 153  ? 81.232  55.207  129.580 1.00 79.59  ? 153  SER A O   1 
ATOM   1185  C  CB  . SER A 1 153  ? 83.641  54.315  127.587 1.00 81.87  ? 153  SER A CB  1 
ATOM   1186  O  OG  . SER A 1 153  ? 84.071  53.231  128.389 1.00 82.80  ? 153  SER A OG  1 
ATOM   1187  N  N   . THR A 1 154  ? 83.116  54.714  130.711 1.00 79.44  ? 154  THR A N   1 
ATOM   1188  C  CA  . THR A 1 154  ? 82.411  54.227  131.886 1.00 80.32  ? 154  THR A CA  1 
ATOM   1189  C  C   . THR A 1 154  ? 83.068  54.769  133.158 1.00 78.34  ? 154  THR A C   1 
ATOM   1190  O  O   . THR A 1 154  ? 83.768  54.061  133.881 1.00 79.43  ? 154  THR A O   1 
ATOM   1191  C  CB  . THR A 1 154  ? 82.265  52.673  131.862 1.00 83.93  ? 154  THR A CB  1 
ATOM   1192  O  OG1 . THR A 1 154  ? 81.777  52.213  133.125 1.00 84.56  ? 154  THR A OG1 1 
ATOM   1193  C  CG2 . THR A 1 154  ? 83.591  51.979  131.538 1.00 85.81  ? 154  THR A CG2 1 
ATOM   1194  N  N   . ALA A 1 155  ? 82.832  56.054  133.401 1.00 76.07  ? 155  ALA A N   1 
ATOM   1195  C  CA  . ALA A 1 155  ? 83.438  56.786  134.500 1.00 74.23  ? 155  ALA A CA  1 
ATOM   1196  C  C   . ALA A 1 155  ? 82.619  56.631  135.784 1.00 74.28  ? 155  ALA A C   1 
ATOM   1197  O  O   . ALA A 1 155  ? 81.538  57.222  135.914 1.00 73.08  ? 155  ALA A O   1 
ATOM   1198  C  CB  . ALA A 1 155  ? 83.560  58.240  134.121 1.00 71.56  ? 155  ALA A CB  1 
ATOM   1199  N  N   . LYS A 1 156  ? 83.148  55.846  136.727 1.00 75.93  ? 156  LYS A N   1 
ATOM   1200  C  CA  . LYS A 1 156  ? 82.423  55.471  137.952 1.00 76.71  ? 156  LYS A CA  1 
ATOM   1201  C  C   . LYS A 1 156  ? 82.142  56.626  138.893 1.00 74.15  ? 156  LYS A C   1 
ATOM   1202  O  O   . LYS A 1 156  ? 82.998  57.481  139.128 1.00 72.54  ? 156  LYS A O   1 
ATOM   1203  C  CB  . LYS A 1 156  ? 83.169  54.381  138.729 1.00 78.76  ? 156  LYS A CB  1 
ATOM   1204  C  CG  . LYS A 1 156  ? 82.856  52.960  138.297 1.00 82.90  ? 156  LYS A CG  1 
ATOM   1205  C  CD  . LYS A 1 156  ? 83.593  51.950  139.173 1.00 86.07  ? 156  LYS A CD  1 
ATOM   1206  C  CE  . LYS A 1 156  ? 83.737  50.599  138.468 1.00 89.94  ? 156  LYS A CE  1 
ATOM   1207  N  NZ  . LYS A 1 156  ? 84.735  49.719  139.142 1.00 91.77  ? 156  LYS A NZ  1 
ATOM   1208  N  N   . LEU A 1 157  ? 80.929  56.631  139.431 1.00 74.37  ? 157  LEU A N   1 
ATOM   1209  C  CA  . LEU A 1 157  ? 80.543  57.563  140.479 1.00 72.48  ? 157  LEU A CA  1 
ATOM   1210  C  C   . LEU A 1 157  ? 80.941  57.009  141.840 1.00 73.53  ? 157  LEU A C   1 
ATOM   1211  O  O   . LEU A 1 157  ? 80.737  55.827  142.133 1.00 76.04  ? 157  LEU A O   1 
ATOM   1212  C  CB  . LEU A 1 157  ? 79.037  57.813  140.432 1.00 71.97  ? 157  LEU A CB  1 
ATOM   1213  C  CG  . LEU A 1 157  ? 78.499  58.971  139.585 1.00 70.30  ? 157  LEU A CG  1 
ATOM   1214  C  CD1 . LEU A 1 157  ? 79.430  59.372  138.457 1.00 69.45  ? 157  LEU A CD1 1 
ATOM   1215  C  CD2 . LEU A 1 157  ? 77.120  58.623  139.048 1.00 71.31  ? 157  LEU A CD2 1 
ATOM   1216  N  N   . TYR A 1 158  ? 81.538  57.861  142.660 1.00 72.10  ? 158  TYR A N   1 
ATOM   1217  C  CA  . TYR A 1 158  ? 81.809  57.509  144.040 1.00 73.13  ? 158  TYR A CA  1 
ATOM   1218  C  C   . TYR A 1 158  ? 81.129  58.557  144.896 1.00 70.56  ? 158  TYR A C   1 
ATOM   1219  O  O   . TYR A 1 158  ? 81.565  59.705  144.943 1.00 68.52  ? 158  TYR A O   1 
ATOM   1220  C  CB  . TYR A 1 158  ? 83.317  57.445  144.298 1.00 74.30  ? 158  TYR A CB  1 
ATOM   1221  C  CG  . TYR A 1 158  ? 83.714  57.294  145.759 1.00 76.37  ? 158  TYR A CG  1 
ATOM   1222  C  CD1 . TYR A 1 158  ? 83.384  56.142  146.484 1.00 79.89  ? 158  TYR A CD1 1 
ATOM   1223  C  CD2 . TYR A 1 158  ? 84.438  58.303  146.410 1.00 76.52  ? 158  TYR A CD2 1 
ATOM   1224  C  CE1 . TYR A 1 158  ? 83.757  56.003  147.830 1.00 81.44  ? 158  TYR A CE1 1 
ATOM   1225  C  CE2 . TYR A 1 158  ? 84.820  58.173  147.751 1.00 77.92  ? 158  TYR A CE2 1 
ATOM   1226  C  CZ  . TYR A 1 158  ? 84.474  57.023  148.452 1.00 80.07  ? 158  TYR A CZ  1 
ATOM   1227  O  OH  . TYR A 1 158  ? 84.849  56.899  149.767 1.00 80.13  ? 158  TYR A OH  1 
ATOM   1228  N  N   . ALA A 1 159  ? 80.043  58.147  145.548 1.00 70.84  ? 159  ALA A N   1 
ATOM   1229  C  CA  . ALA A 1 159  ? 79.125  59.055  146.247 1.00 68.62  ? 159  ALA A CA  1 
ATOM   1230  C  C   . ALA A 1 159  ? 78.582  60.147  145.318 1.00 66.21  ? 159  ALA A C   1 
ATOM   1231  O  O   . ALA A 1 159  ? 78.405  61.290  145.727 1.00 64.25  ? 159  ALA A O   1 
ATOM   1232  C  CB  . ALA A 1 159  ? 79.778  59.654  147.508 1.00 67.60  ? 159  ALA A CB  1 
ATOM   1233  N  N   . GLY A 1 160  ? 78.320  59.775  144.066 1.00 66.64  ? 160  GLY A N   1 
ATOM   1234  C  CA  . GLY A 1 160  ? 77.746  60.683  143.071 1.00 64.79  ? 160  GLY A CA  1 
ATOM   1235  C  C   . GLY A 1 160  ? 78.772  61.456  142.262 1.00 63.38  ? 160  GLY A C   1 
ATOM   1236  O  O   . GLY A 1 160  ? 78.428  62.101  141.271 1.00 62.83  ? 160  GLY A O   1 
ATOM   1237  N  N   . VAL A 1 161  ? 80.033  61.373  142.679 1.00 63.01  ? 161  VAL A N   1 
ATOM   1238  C  CA  . VAL A 1 161  ? 81.111  62.169  142.110 1.00 61.44  ? 161  VAL A CA  1 
ATOM   1239  C  C   . VAL A 1 161  ? 82.061  61.312  141.288 1.00 62.70  ? 161  VAL A C   1 
ATOM   1240  O  O   . VAL A 1 161  ? 82.423  60.208  141.694 1.00 64.57  ? 161  VAL A O   1 
ATOM   1241  C  CB  . VAL A 1 161  ? 81.939  62.859  143.224 1.00 60.48  ? 161  VAL A CB  1 
ATOM   1242  C  CG1 . VAL A 1 161  ? 82.929  63.857  142.635 1.00 59.31  ? 161  VAL A CG1 1 
ATOM   1243  C  CG2 . VAL A 1 161  ? 81.028  63.552  144.228 1.00 59.45  ? 161  VAL A CG2 1 
ATOM   1244  N  N   . PHE A 1 162  ? 82.461  61.834  140.132 1.00 61.77  ? 162  PHE A N   1 
ATOM   1245  C  CA  . PHE A 1 162  ? 83.575  61.278  139.374 1.00 62.56  ? 162  PHE A CA  1 
ATOM   1246  C  C   . PHE A 1 162  ? 84.629  62.347  139.182 1.00 60.81  ? 162  PHE A C   1 
ATOM   1247  O  O   . PHE A 1 162  ? 84.335  63.424  138.683 1.00 59.35  ? 162  PHE A O   1 
ATOM   1248  C  CB  . PHE A 1 162  ? 83.133  60.770  138.002 1.00 64.00  ? 162  PHE A CB  1 
ATOM   1249  C  CG  . PHE A 1 162  ? 84.280  60.476  137.076 1.00 64.97  ? 162  PHE A CG  1 
ATOM   1250  C  CD1 . PHE A 1 162  ? 85.044  59.324  137.240 1.00 67.24  ? 162  PHE A CD1 1 
ATOM   1251  C  CD2 . PHE A 1 162  ? 84.611  61.360  136.058 1.00 64.58  ? 162  PHE A CD2 1 
ATOM   1252  C  CE1 . PHE A 1 162  ? 86.119  59.046  136.393 1.00 68.63  ? 162  PHE A CE1 1 
ATOM   1253  C  CE2 . PHE A 1 162  ? 85.684  61.098  135.204 1.00 66.12  ? 162  PHE A CE2 1 
ATOM   1254  C  CZ  . PHE A 1 162  ? 86.439  59.932  135.370 1.00 67.93  ? 162  PHE A CZ  1 
ATOM   1255  N  N   . GLU A 1 163  ? 85.861  62.036  139.559 1.00 61.18  ? 163  GLU A N   1 
ATOM   1256  C  CA  . GLU A 1 163  ? 86.947  63.000  139.454 1.00 60.01  ? 163  GLU A CA  1 
ATOM   1257  C  C   . GLU A 1 163  ? 88.075  62.483  138.576 1.00 60.76  ? 163  GLU A C   1 
ATOM   1258  O  O   . GLU A 1 163  ? 88.437  61.305  138.639 1.00 62.69  ? 163  GLU A O   1 
ATOM   1259  C  CB  . GLU A 1 163  ? 87.483  63.365  140.837 1.00 59.67  ? 163  GLU A CB  1 
ATOM   1260  C  CG  . GLU A 1 163  ? 88.551  64.445  140.816 1.00 59.90  ? 163  GLU A CG  1 
ATOM   1261  C  CD  . GLU A 1 163  ? 89.045  64.811  142.198 1.00 61.31  ? 163  GLU A CD  1 
ATOM   1262  O  OE1 . GLU A 1 163  ? 88.243  64.786  143.162 1.00 61.52  ? 163  GLU A OE1 1 
ATOM   1263  O  OE2 . GLU A 1 163  ? 90.245  65.132  142.314 1.00 62.58  ? 163  GLU A OE2 1 
ATOM   1264  N  N   . SER A 1 164  ? 88.622  63.374  137.757 1.00 59.08  ? 164  SER A N   1 
ATOM   1265  C  CA  . SER A 1 164  ? 89.744  63.039  136.911 1.00 59.43  ? 164  SER A CA  1 
ATOM   1266  C  C   . SER A 1 164  ? 90.407  64.305  136.382 1.00 57.97  ? 164  SER A C   1 
ATOM   1267  O  O   . SER A 1 164  ? 89.978  65.422  136.687 1.00 56.29  ? 164  SER A O   1 
ATOM   1268  C  CB  . SER A 1 164  ? 89.293  62.138  135.761 1.00 61.08  ? 164  SER A CB  1 
ATOM   1269  O  OG  . SER A 1 164  ? 90.378  61.378  135.259 1.00 62.35  ? 164  SER A OG  1 
ATOM   1270  N  N   . ASP A 1 165  ? 91.456  64.123  135.588 1.00 58.36  ? 165  ASP A N   1 
ATOM   1271  C  CA  . ASP A 1 165  ? 92.224  65.242  135.077 1.00 57.47  ? 165  ASP A CA  1 
ATOM   1272  C  C   . ASP A 1 165  ? 92.634  65.061  133.624 1.00 58.10  ? 165  ASP A C   1 
ATOM   1273  O  O   . ASP A 1 165  ? 92.578  63.951  133.089 1.00 59.79  ? 165  ASP A O   1 
ATOM   1274  C  CB  . ASP A 1 165  ? 93.459  65.489  135.955 1.00 57.79  ? 165  ASP A CB  1 
ATOM   1275  C  CG  . ASP A 1 165  ? 94.311  64.239  136.159 1.00 60.31  ? 165  ASP A CG  1 
ATOM   1276  O  OD1 . ASP A 1 165  ? 94.428  63.411  135.233 1.00 62.64  ? 165  ASP A OD1 1 
ATOM   1277  O  OD2 . ASP A 1 165  ? 94.887  64.094  137.257 1.00 62.26  ? 165  ASP A OD2 1 
ATOM   1278  N  N   . LEU A 1 166  ? 93.033  66.162  132.993 1.00 56.85  ? 166  LEU A N   1 
ATOM   1279  C  CA  . LEU A 1 166  ? 93.594  66.138  131.645 1.00 57.40  ? 166  LEU A CA  1 
ATOM   1280  C  C   . LEU A 1 166  ? 94.842  67.010  131.595 1.00 56.91  ? 166  LEU A C   1 
ATOM   1281  O  O   . LEU A 1 166  ? 94.829  68.160  132.041 1.00 55.55  ? 166  LEU A O   1 
ATOM   1282  C  CB  . LEU A 1 166  ? 92.564  66.605  130.605 1.00 57.20  ? 166  LEU A CB  1 
ATOM   1283  C  CG  . LEU A 1 166  ? 93.049  66.986  129.194 1.00 58.99  ? 166  LEU A CG  1 
ATOM   1284  C  CD1 . LEU A 1 166  ? 93.707  65.814  128.438 1.00 61.17  ? 166  LEU A CD1 1 
ATOM   1285  C  CD2 . LEU A 1 166  ? 91.912  67.582  128.366 1.00 58.80  ? 166  LEU A CD2 1 
ATOM   1286  N  N   . GLN A 1 167  ? 95.926  66.458  131.064 1.00 58.01  ? 167  GLN A N   1 
ATOM   1287  C  CA  . GLN A 1 167  ? 97.140  67.239  130.908 1.00 57.98  ? 167  GLN A CA  1 
ATOM   1288  C  C   . GLN A 1 167  ? 97.083  68.036  129.608 1.00 57.50  ? 167  GLN A C   1 
ATOM   1289  O  O   . GLN A 1 167  ? 96.832  67.485  128.545 1.00 58.82  ? 167  GLN A O   1 
ATOM   1290  C  CB  . GLN A 1 167  ? 98.388  66.357  130.980 1.00 59.45  ? 167  GLN A CB  1 
ATOM   1291  C  CG  . GLN A 1 167  ? 99.662  67.169  131.236 1.00 62.42  ? 167  GLN A CG  1 
ATOM   1292  C  CD  . GLN A 1 167  ? 100.856 66.314  131.628 1.00 67.54  ? 167  GLN A CD  1 
ATOM   1293  O  OE1 . GLN A 1 167  ? 101.222 65.362  130.921 1.00 70.80  ? 167  GLN A OE1 1 
ATOM   1294  N  NE2 . GLN A 1 167  ? 101.480 66.654  132.758 1.00 67.63  ? 167  GLN A NE2 1 
ATOM   1295  N  N   . ILE A 1 168  ? 97.286  69.340  129.697 1.00 55.96  ? 168  ILE A N   1 
ATOM   1296  C  CA  . ILE A 1 168  ? 97.292  70.162  128.504 1.00 56.18  ? 168  ILE A CA  1 
ATOM   1297  C  C   . ILE A 1 168  ? 98.681  70.109  127.882 1.00 57.79  ? 168  ILE A C   1 
ATOM   1298  O  O   . ILE A 1 168  ? 99.690  70.138  128.597 1.00 58.21  ? 168  ILE A O   1 
ATOM   1299  C  CB  . ILE A 1 168  ? 96.836  71.602  128.807 1.00 54.90  ? 168  ILE A CB  1 
ATOM   1300  C  CG1 . ILE A 1 168  ? 95.339  71.602  129.089 1.00 53.60  ? 168  ILE A CG1 1 
ATOM   1301  C  CG2 . ILE A 1 168  ? 97.145  72.556  127.649 1.00 55.33  ? 168  ILE A CG2 1 
ATOM   1302  C  CD1 . ILE A 1 168  ? 94.808  72.932  129.501 1.00 53.98  ? 168  ILE A CD1 1 
ATOM   1303  N  N   . ALA A 1 169  ? 98.725  70.007  126.556 1.00 58.75  ? 169  ALA A N   1 
ATOM   1304  C  CA  . ALA A 1 169  ? 99.983  69.899  125.832 1.00 60.15  ? 169  ALA A CA  1 
ATOM   1305  C  C   . ALA A 1 169  ? 100.753 71.215  125.875 1.00 60.17  ? 169  ALA A C   1 
ATOM   1306  O  O   . ALA A 1 169  ? 100.152 72.279  125.999 1.00 59.26  ? 169  ALA A O   1 
ATOM   1307  C  CB  . ALA A 1 169  ? 99.728  69.474  124.395 1.00 61.65  ? 169  ALA A CB  1 
ATOM   1308  N  N   . PRO A 1 170  ? 102.092 71.144  125.788 1.00 61.42  ? 170  PRO A N   1 
ATOM   1309  C  CA  . PRO A 1 170  ? 102.947 72.326  125.683 1.00 62.03  ? 170  PRO A CA  1 
ATOM   1310  C  C   . PRO A 1 170  ? 102.534 73.257  124.547 1.00 62.66  ? 170  PRO A C   1 
ATOM   1311  O  O   . PRO A 1 170  ? 102.666 74.469  124.676 1.00 62.90  ? 170  PRO A O   1 
ATOM   1312  C  CB  . PRO A 1 170  ? 104.319 71.729  125.372 1.00 63.71  ? 170  PRO A CB  1 
ATOM   1313  C  CG  . PRO A 1 170  ? 104.285 70.392  125.988 1.00 63.49  ? 170  PRO A CG  1 
ATOM   1314  C  CD  . PRO A 1 170  ? 102.885 69.901  125.807 1.00 62.58  ? 170  PRO A CD  1 
ATOM   1315  N  N   . THR A 1 171  ? 102.054 72.688  123.445 1.00 63.23  ? 171  THR A N   1 
ATOM   1316  C  CA  . THR A 1 171  ? 101.564 73.478  122.321 1.00 64.03  ? 171  THR A CA  1 
ATOM   1317  C  C   . THR A 1 171  ? 100.149 73.017  121.955 1.00 63.22  ? 171  THR A C   1 
ATOM   1318  O  O   . THR A 1 171  ? 99.968  72.271  120.991 1.00 64.62  ? 171  THR A O   1 
ATOM   1319  C  CB  . THR A 1 171  ? 102.504 73.360  121.105 1.00 66.41  ? 171  THR A CB  1 
ATOM   1320  O  OG1 . THR A 1 171  ? 103.850 73.207  121.563 1.00 67.70  ? 171  THR A OG1 1 
ATOM   1321  C  CG2 . THR A 1 171  ? 102.403 74.588  120.208 1.00 67.12  ? 171  THR A CG2 1 
ATOM   1322  N  N   . PRO A 1 172  ? 99.140  73.457  122.730 1.00 61.08  ? 172  PRO A N   1 
ATOM   1323  C  CA  . PRO A 1 172  ? 97.783  72.949  122.584 1.00 60.15  ? 172  PRO A CA  1 
ATOM   1324  C  C   . PRO A 1 172  ? 96.943  73.800  121.636 1.00 60.76  ? 172  PRO A C   1 
ATOM   1325  O  O   . PRO A 1 172  ? 97.416  74.834  121.142 1.00 61.81  ? 172  PRO A O   1 
ATOM   1326  C  CB  . PRO A 1 172  ? 97.244  73.081  124.000 1.00 57.81  ? 172  PRO A CB  1 
ATOM   1327  C  CG  . PRO A 1 172  ? 97.871  74.354  124.490 1.00 57.65  ? 172  PRO A CG  1 
ATOM   1328  C  CD  . PRO A 1 172  ? 99.217  74.460  123.813 1.00 59.83  ? 172  PRO A CD  1 
ATOM   1329  N  N   A MET A 1 173  ? 95.712  73.355  121.392 0.50 60.38  ? 173  MET A N   1 
ATOM   1330  N  N   B MET A 1 173  ? 95.712  73.370  121.368 0.50 60.45  ? 173  MET A N   1 
ATOM   1331  C  CA  A MET A 1 173  ? 94.727  74.141  120.663 0.50 60.90  ? 173  MET A CA  1 
ATOM   1332  C  CA  B MET A 1 173  ? 94.795  74.192  120.586 0.50 61.13  ? 173  MET A CA  1 
ATOM   1333  C  C   A MET A 1 173  ? 94.134  75.224  121.566 0.50 59.17  ? 173  MET A C   1 
ATOM   1334  C  C   B MET A 1 173  ? 94.095  75.217  121.481 0.50 59.34  ? 173  MET A C   1 
ATOM   1335  O  O   A MET A 1 173  ? 93.428  74.925  122.536 0.50 57.13  ? 173  MET A O   1 
ATOM   1336  O  O   B MET A 1 173  ? 93.302  74.871  122.365 0.50 57.40  ? 173  MET A O   1 
ATOM   1337  C  CB  A MET A 1 173  ? 93.612  73.243  120.130 0.50 61.42  ? 173  MET A CB  1 
ATOM   1338  C  CB  B MET A 1 173  ? 93.798  73.342  119.793 0.50 62.13  ? 173  MET A CB  1 
ATOM   1339  C  CG  A MET A 1 173  ? 93.828  72.742  118.722 0.50 64.04  ? 173  MET A CG  1 
ATOM   1340  C  CG  B MET A 1 173  ? 94.410  72.650  118.583 0.50 64.87  ? 173  MET A CG  1 
ATOM   1341  S  SD  A MET A 1 173  ? 92.261  72.511  117.855 0.50 65.12  ? 173  MET A SD  1 
ATOM   1342  S  SD  B MET A 1 173  ? 94.993  73.759  117.274 0.50 68.15  ? 173  MET A SD  1 
ATOM   1343  C  CE  A MET A 1 173  ? 91.685  74.205  117.791 0.50 66.03  ? 173  MET A CE  1 
ATOM   1344  C  CE  B MET A 1 173  ? 93.487  74.041  116.347 0.50 69.07  ? 173  MET A CE  1 
ATOM   1345  N  N   . LEU A 1 174  ? 94.424  76.481  121.241 1.00 59.90  ? 174  LEU A N   1 
ATOM   1346  C  CA  . LEU A 1 174  ? 93.924  77.598  122.023 1.00 58.90  ? 174  LEU A CA  1 
ATOM   1347  C  C   . LEU A 1 174  ? 92.452  77.879  121.724 1.00 59.17  ? 174  LEU A C   1 
ATOM   1348  O  O   . LEU A 1 174  ? 92.004  77.771  120.572 1.00 61.02  ? 174  LEU A O   1 
ATOM   1349  C  CB  . LEU A 1 174  ? 94.788  78.845  121.788 1.00 59.81  ? 174  LEU A CB  1 
ATOM   1350  C  CG  . LEU A 1 174  ? 96.300  78.668  122.022 1.00 60.28  ? 174  LEU A CG  1 
ATOM   1351  C  CD1 . LEU A 1 174  ? 97.081  79.917  121.642 1.00 60.92  ? 174  LEU A CD1 1 
ATOM   1352  C  CD2 . LEU A 1 174  ? 96.618  78.247  123.458 1.00 57.75  ? 174  LEU A CD2 1 
ATOM   1353  N  N   . GLY A 1 175  ? 91.710  78.229  122.773 1.00 57.31  ? 175  GLY A N   1 
ATOM   1354  C  CA  . GLY A 1 175  ? 90.298  78.541  122.652 1.00 57.55  ? 175  GLY A CA  1 
ATOM   1355  C  C   . GLY A 1 175  ? 89.446  77.869  123.713 1.00 55.82  ? 175  GLY A C   1 
ATOM   1356  O  O   . GLY A 1 175  ? 89.891  77.640  124.844 1.00 54.19  ? 175  GLY A O   1 
ATOM   1357  N  N   . VAL A 1 176  ? 88.217  77.535  123.336 1.00 56.32  ? 176  VAL A N   1 
ATOM   1358  C  CA  . VAL A 1 176  ? 87.241  77.038  124.298 1.00 54.95  ? 176  VAL A CA  1 
ATOM   1359  C  C   . VAL A 1 176  ? 87.080  75.524  124.183 1.00 55.29  ? 176  VAL A C   1 
ATOM   1360  O  O   . VAL A 1 176  ? 86.692  74.999  123.139 1.00 57.03  ? 176  VAL A O   1 
ATOM   1361  C  CB  . VAL A 1 176  ? 85.871  77.762  124.150 1.00 55.00  ? 176  VAL A CB  1 
ATOM   1362  C  CG1 . VAL A 1 176  ? 84.901  77.273  125.208 1.00 53.15  ? 176  VAL A CG1 1 
ATOM   1363  C  CG2 . VAL A 1 176  ? 86.042  79.283  124.246 1.00 54.32  ? 176  VAL A CG2 1 
ATOM   1364  N  N   . TRP A 1 177  ? 87.392  74.837  125.272 1.00 53.89  ? 177  TRP A N   1 
ATOM   1365  C  CA  . TRP A 1 177  ? 87.284  73.391  125.349 1.00 54.28  ? 177  TRP A CA  1 
ATOM   1366  C  C   . TRP A 1 177  ? 85.963  73.015  126.009 1.00 54.08  ? 177  TRP A C   1 
ATOM   1367  O  O   . TRP A 1 177  ? 85.377  73.810  126.730 1.00 52.56  ? 177  TRP A O   1 
ATOM   1368  C  CB  . TRP A 1 177  ? 88.435  72.835  126.185 1.00 52.89  ? 177  TRP A CB  1 
ATOM   1369  C  CG  . TRP A 1 177  ? 89.791  72.912  125.540 1.00 53.52  ? 177  TRP A CG  1 
ATOM   1370  C  CD1 . TRP A 1 177  ? 90.416  74.028  125.059 1.00 53.23  ? 177  TRP A CD1 1 
ATOM   1371  C  CD2 . TRP A 1 177  ? 90.700  71.826  125.337 1.00 53.48  ? 177  TRP A CD2 1 
ATOM   1372  N  NE1 . TRP A 1 177  ? 91.647  73.700  124.548 1.00 54.57  ? 177  TRP A NE1 1 
ATOM   1373  C  CE2 . TRP A 1 177  ? 91.849  72.355  124.711 1.00 54.64  ? 177  TRP A CE2 1 
ATOM   1374  C  CE3 . TRP A 1 177  ? 90.651  70.455  125.614 1.00 52.95  ? 177  TRP A CE3 1 
ATOM   1375  C  CZ2 . TRP A 1 177  ? 92.940  71.562  124.363 1.00 55.38  ? 177  TRP A CZ2 1 
ATOM   1376  C  CZ3 . TRP A 1 177  ? 91.733  69.670  125.268 1.00 54.58  ? 177  TRP A CZ3 1 
ATOM   1377  C  CH2 . TRP A 1 177  ? 92.862  70.224  124.647 1.00 55.41  ? 177  TRP A CH2 1 
ATOM   1378  N  N   . ASN A 1 178  ? 85.522  71.785  125.790 1.00 55.82  ? 178  ASN A N   1 
ATOM   1379  C  CA  . ASN A 1 178  ? 84.225  71.351  126.248 1.00 56.51  ? 178  ASN A CA  1 
ATOM   1380  C  C   . ASN A 1 178  ? 84.322  70.038  127.020 1.00 56.06  ? 178  ASN A C   1 
ATOM   1381  O  O   . ASN A 1 178  ? 84.785  69.035  126.488 1.00 57.41  ? 178  ASN A O   1 
ATOM   1382  C  CB  . ASN A 1 178  ? 83.318  71.192  125.029 1.00 59.44  ? 178  ASN A CB  1 
ATOM   1383  C  CG  . ASN A 1 178  ? 81.850  71.283  125.363 1.00 62.79  ? 178  ASN A CG  1 
ATOM   1384  O  OD1 . ASN A 1 178  ? 81.467  71.455  126.520 1.00 62.14  ? 178  ASN A OD1 1 
ATOM   1385  N  ND2 . ASN A 1 178  ? 81.015  71.168  124.330 1.00 71.87  ? 178  ASN A ND2 1 
ATOM   1386  N  N   . ILE A 1 179  ? 83.924  70.063  128.288 1.00 54.54  ? 179  ILE A N   1 
ATOM   1387  C  CA  . ILE A 1 179  ? 83.739  68.844  129.066 1.00 54.65  ? 179  ILE A CA  1 
ATOM   1388  C  C   . ILE A 1 179  ? 82.275  68.458  128.929 1.00 55.76  ? 179  ILE A C   1 
ATOM   1389  O  O   . ILE A 1 179  ? 81.385  69.241  129.268 1.00 55.16  ? 179  ILE A O   1 
ATOM   1390  C  CB  . ILE A 1 179  ? 84.074  69.051  130.558 1.00 52.65  ? 179  ILE A CB  1 
ATOM   1391  C  CG1 . ILE A 1 179  ? 85.506  69.565  130.723 1.00 51.84  ? 179  ILE A CG1 1 
ATOM   1392  C  CG2 . ILE A 1 179  ? 83.856  67.756  131.348 1.00 52.46  ? 179  ILE A CG2 1 
ATOM   1393  C  CD1 . ILE A 1 179  ? 85.969  69.670  132.177 1.00 48.27  ? 179  ILE A CD1 1 
ATOM   1394  N  N   . SER A 1 180  ? 82.028  67.252  128.443 1.00 58.09  ? 180  SER A N   1 
ATOM   1395  C  CA  . SER A 1 180  ? 80.677  66.813  128.124 1.00 60.07  ? 180  SER A CA  1 
ATOM   1396  C  C   . SER A 1 180  ? 80.326  65.529  128.872 1.00 60.96  ? 180  SER A C   1 
ATOM   1397  O  O   . SER A 1 180  ? 81.036  64.533  128.773 1.00 62.11  ? 180  SER A O   1 
ATOM   1398  C  CB  . SER A 1 180  ? 80.556  66.593  126.618 1.00 62.46  ? 180  SER A CB  1 
ATOM   1399  O  OG  . SER A 1 180  ? 79.200  66.559  126.222 1.00 64.82  ? 180  SER A OG  1 
ATOM   1400  N  N   . VAL A 1 181  ? 79.233  65.561  129.627 1.00 60.96  ? 181  VAL A N   1 
ATOM   1401  C  CA  . VAL A 1 181  ? 78.806  64.404  130.413 1.00 62.15  ? 181  VAL A CA  1 
ATOM   1402  C  C   . VAL A 1 181  ? 77.513  63.823  129.862 1.00 64.59  ? 181  VAL A C   1 
ATOM   1403  O  O   . VAL A 1 181  ? 76.553  64.547  129.599 1.00 64.36  ? 181  VAL A O   1 
ATOM   1404  C  CB  . VAL A 1 181  ? 78.625  64.744  131.906 1.00 59.92  ? 181  VAL A CB  1 
ATOM   1405  C  CG1 . VAL A 1 181  ? 78.232  63.498  132.693 1.00 60.71  ? 181  VAL A CG1 1 
ATOM   1406  C  CG2 . VAL A 1 181  ? 79.895  65.341  132.471 1.00 57.96  ? 181  VAL A CG2 1 
ATOM   1407  N  N   . GLU A 1 182  ? 77.496  62.507  129.715 1.00 67.48  ? 182  GLU A N   1 
ATOM   1408  C  CA  . GLU A 1 182  ? 76.399  61.827  129.071 1.00 70.82  ? 182  GLU A CA  1 
ATOM   1409  C  C   . GLU A 1 182  ? 75.901  60.679  129.928 1.00 72.38  ? 182  GLU A C   1 
ATOM   1410  O  O   . GLU A 1 182  ? 76.695  59.940  130.513 1.00 72.54  ? 182  GLU A O   1 
ATOM   1411  C  CB  . GLU A 1 182  ? 76.880  61.286  127.739 1.00 73.44  ? 182  GLU A CB  1 
ATOM   1412  C  CG  . GLU A 1 182  ? 75.907  61.460  126.620 1.00 76.51  ? 182  GLU A CG  1 
ATOM   1413  C  CD  . GLU A 1 182  ? 76.531  61.134  125.292 1.00 80.50  ? 182  GLU A CD  1 
ATOM   1414  O  OE1 . GLU A 1 182  ? 76.979  62.080  124.613 1.00 80.86  ? 182  GLU A OE1 1 
ATOM   1415  O  OE2 . GLU A 1 182  ? 76.595  59.934  124.938 1.00 84.24  ? 182  GLU A OE2 1 
ATOM   1416  N  N   . VAL A 1 183  ? 74.581  60.545  130.004 1.00 74.08  ? 183  VAL A N   1 
ATOM   1417  C  CA  . VAL A 1 183  ? 73.949  59.426  130.695 1.00 76.48  ? 183  VAL A CA  1 
ATOM   1418  C  C   . VAL A 1 183  ? 73.028  58.697  129.724 1.00 80.42  ? 183  VAL A C   1 
ATOM   1419  O  O   . VAL A 1 183  ? 72.165  59.313  129.089 1.00 80.82  ? 183  VAL A O   1 
ATOM   1420  C  CB  . VAL A 1 183  ? 73.160  59.883  131.946 1.00 74.47  ? 183  VAL A CB  1 
ATOM   1421  C  CG1 . VAL A 1 183  ? 72.363  58.727  132.538 1.00 76.72  ? 183  VAL A CG1 1 
ATOM   1422  C  CG2 . VAL A 1 183  ? 74.101  60.450  132.990 1.00 71.77  ? 183  VAL A CG2 1 
ATOM   1423  N  N   . GLU A 1 184  ? 73.227  57.387  129.605 1.00 83.93  ? 184  GLU A N   1 
ATOM   1424  C  CA  . GLU A 1 184  ? 72.426  56.562  128.708 1.00 88.51  ? 184  GLU A CA  1 
ATOM   1425  C  C   . GLU A 1 184  ? 72.327  57.230  127.334 1.00 89.57  ? 184  GLU A C   1 
ATOM   1426  O  O   . GLU A 1 184  ? 71.233  57.469  126.823 1.00 91.08  ? 184  GLU A O   1 
ATOM   1427  C  CB  . GLU A 1 184  ? 71.026  56.305  129.303 1.00 89.43  ? 184  GLU A CB  1 
ATOM   1428  C  CG  . GLU A 1 184  ? 71.005  55.380  130.522 1.00 90.72  ? 184  GLU A CG  1 
ATOM   1429  C  CD  . GLU A 1 184  ? 71.424  53.955  130.184 1.00 95.70  ? 184  GLU A CD  1 
ATOM   1430  O  OE1 . GLU A 1 184  ? 70.791  53.332  129.301 1.00 99.52  ? 184  GLU A OE1 1 
ATOM   1431  O  OE2 . GLU A 1 184  ? 72.386  53.455  130.806 1.00 96.12  ? 184  GLU A OE2 1 
ATOM   1432  N  N   . GLY A 1 185  ? 73.481  57.557  126.759 1.00 89.24  ? 185  GLY A N   1 
ATOM   1433  C  CA  . GLY A 1 185  ? 73.545  58.219  125.462 1.00 90.20  ? 185  GLY A CA  1 
ATOM   1434  C  C   . GLY A 1 185  ? 72.815  59.550  125.354 1.00 88.55  ? 185  GLY A C   1 
ATOM   1435  O  O   . GLY A 1 185  ? 72.433  59.951  124.257 1.00 90.17  ? 185  GLY A O   1 
ATOM   1436  N  N   . GLU A 1 186  ? 72.606  60.232  126.478 1.00 85.63  ? 186  GLU A N   1 
ATOM   1437  C  CA  . GLU A 1 186  ? 72.028  61.578  126.450 1.00 84.16  ? 186  GLU A CA  1 
ATOM   1438  C  C   . GLU A 1 186  ? 72.765  62.569  127.338 1.00 80.49  ? 186  GLU A C   1 
ATOM   1439  O  O   . GLU A 1 186  ? 73.073  62.282  128.496 1.00 79.05  ? 186  GLU A O   1 
ATOM   1440  C  CB  . GLU A 1 186  ? 70.541  61.567  126.792 1.00 84.82  ? 186  GLU A CB  1 
ATOM   1441  C  CG  . GLU A 1 186  ? 69.660  61.301  125.580 1.00 89.86  ? 186  GLU A CG  1 
ATOM   1442  C  CD  . GLU A 1 186  ? 68.374  62.117  125.576 1.00 91.54  ? 186  GLU A CD  1 
ATOM   1443  O  OE1 . GLU A 1 186  ? 68.067  62.782  126.597 1.00 89.71  ? 186  GLU A OE1 1 
ATOM   1444  O  OE2 . GLU A 1 186  ? 67.673  62.090  124.540 1.00 94.35  ? 186  GLU A OE2 1 
ATOM   1445  N  N   . GLU A 1 187  ? 73.048  63.739  126.777 1.00 79.29  ? 187  GLU A N   1 
ATOM   1446  C  CA  . GLU A 1 187  ? 73.806  64.752  127.479 1.00 76.22  ? 187  GLU A CA  1 
ATOM   1447  C  C   . GLU A 1 187  ? 73.091  65.170  128.760 1.00 73.69  ? 187  GLU A C   1 
ATOM   1448  O  O   . GLU A 1 187  ? 71.913  65.526  128.734 1.00 73.88  ? 187  GLU A O   1 
ATOM   1449  C  CB  . GLU A 1 187  ? 74.071  65.957  126.572 1.00 76.11  ? 187  GLU A CB  1 
ATOM   1450  C  CG  . GLU A 1 187  ? 74.748  67.127  127.290 1.00 74.82  ? 187  GLU A CG  1 
ATOM   1451  C  CD  . GLU A 1 187  ? 75.972  67.642  126.562 1.00 76.81  ? 187  GLU A CD  1 
ATOM   1452  O  OE1 . GLU A 1 187  ? 76.701  68.472  127.141 1.00 75.94  ? 187  GLU A OE1 1 
ATOM   1453  O  OE2 . GLU A 1 187  ? 76.219  67.205  125.418 1.00 80.64  ? 187  GLU A OE2 1 
ATOM   1454  N  N   . LEU A 1 188  ? 73.818  65.098  129.873 1.00 71.26  ? 188  LEU A N   1 
ATOM   1455  C  CA  . LEU A 1 188  ? 73.313  65.510  131.171 1.00 68.68  ? 188  LEU A CA  1 
ATOM   1456  C  C   . LEU A 1 188  ? 73.899  66.860  131.548 1.00 66.20  ? 188  LEU A C   1 
ATOM   1457  O  O   . LEU A 1 188  ? 73.184  67.724  132.053 1.00 65.08  ? 188  LEU A O   1 
ATOM   1458  C  CB  . LEU A 1 188  ? 73.659  64.471  132.240 1.00 68.47  ? 188  LEU A CB  1 
ATOM   1459  C  CG  . LEU A 1 188  ? 73.236  64.744  133.686 1.00 66.49  ? 188  LEU A CG  1 
ATOM   1460  C  CD1 . LEU A 1 188  ? 71.724  64.598  133.860 1.00 67.41  ? 188  LEU A CD1 1 
ATOM   1461  C  CD2 . LEU A 1 188  ? 73.982  63.823  134.644 1.00 65.94  ? 188  LEU A CD2 1 
ATOM   1462  N  N   . VAL A 1 189  ? 75.204  67.028  131.321 1.00 65.44  ? 189  VAL A N   1 
ATOM   1463  C  CA  . VAL A 1 189  ? 75.900  68.277  131.640 1.00 62.92  ? 189  VAL A CA  1 
ATOM   1464  C  C   . VAL A 1 189  ? 77.012  68.567  130.660 1.00 63.38  ? 189  VAL A C   1 
ATOM   1465  O  O   . VAL A 1 189  ? 77.717  67.665  130.217 1.00 64.49  ? 189  VAL A O   1 
ATOM   1466  C  CB  . VAL A 1 189  ? 76.600  68.257  133.012 1.00 61.16  ? 189  VAL A CB  1 
ATOM   1467  C  CG1 . VAL A 1 189  ? 76.416  69.597  133.704 1.00 58.61  ? 189  VAL A CG1 1 
ATOM   1468  C  CG2 . VAL A 1 189  ? 76.131  67.109  133.868 1.00 61.48  ? 189  VAL A CG2 1 
ATOM   1469  N  N   . SER A 1 190  ? 77.179  69.849  130.367 1.00 62.56  ? 190  SER A N   1 
ATOM   1470  C  CA  . SER A 1 190  ? 78.273  70.344  129.562 1.00 62.74  ? 190  SER A CA  1 
ATOM   1471  C  C   . SER A 1 190  ? 78.894  71.495  130.324 1.00 60.90  ? 190  SER A C   1 
ATOM   1472  O  O   . SER A 1 190  ? 78.190  72.242  131.001 1.00 59.89  ? 190  SER A O   1 
ATOM   1473  C  CB  . SER A 1 190  ? 77.753  70.831  128.214 1.00 64.14  ? 190  SER A CB  1 
ATOM   1474  O  OG  . SER A 1 190  ? 78.657  71.731  127.609 1.00 64.57  ? 190  SER A OG  1 
ATOM   1475  N  N   . LYS A 1 191  ? 80.212  71.623  130.227 1.00 60.76  ? 191  LYS A N   1 
ATOM   1476  C  CA  . LYS A 1 191  ? 80.927  72.753  130.805 1.00 59.29  ? 191  LYS A CA  1 
ATOM   1477  C  C   . LYS A 1 191  ? 82.135  73.064  129.929 1.00 59.85  ? 191  LYS A C   1 
ATOM   1478  O  O   . LYS A 1 191  ? 82.806  72.155  129.443 1.00 60.76  ? 191  LYS A O   1 
ATOM   1479  C  CB  . LYS A 1 191  ? 81.363  72.424  132.232 1.00 58.05  ? 191  LYS A CB  1 
ATOM   1480  C  CG  . LYS A 1 191  ? 82.127  73.526  132.957 1.00 58.72  ? 191  LYS A CG  1 
ATOM   1481  C  CD  . LYS A 1 191  ? 81.210  74.416  133.768 1.00 61.38  ? 191  LYS A CD  1 
ATOM   1482  C  CE  . LYS A 1 191  ? 81.997  75.515  134.463 1.00 63.79  ? 191  LYS A CE  1 
ATOM   1483  N  NZ  . LYS A 1 191  ? 81.175  76.218  135.504 1.00 65.14  ? 191  LYS A NZ  1 
ATOM   1484  N  N   . THR A 1 192  ? 82.401  74.345  129.715 1.00 59.25  ? 192  THR A N   1 
ATOM   1485  C  CA  . THR A 1 192  ? 83.576  74.737  128.962 1.00 59.86  ? 192  THR A CA  1 
ATOM   1486  C  C   . THR A 1 192  ? 84.683  75.251  129.876 1.00 58.85  ? 192  THR A C   1 
ATOM   1487  O  O   . THR A 1 192  ? 84.453  75.527  131.056 1.00 57.45  ? 192  THR A O   1 
ATOM   1488  C  CB  . THR A 1 192  ? 83.277  75.810  127.894 1.00 60.97  ? 192  THR A CB  1 
ATOM   1489  O  OG1 . THR A 1 192  ? 83.168  77.094  128.514 1.00 60.56  ? 192  THR A OG1 1 
ATOM   1490  C  CG2 . THR A 1 192  ? 82.016  75.492  127.106 1.00 61.85  ? 192  THR A CG2 1 
ATOM   1491  N  N   . PHE A 1 193  ? 85.891  75.339  129.318 1.00 59.44  ? 193  PHE A N   1 
ATOM   1492  C  CA  . PHE A 1 193  ? 87.005  76.046  129.930 1.00 58.69  ? 193  PHE A CA  1 
ATOM   1493  C  C   . PHE A 1 193  ? 87.888  76.571  128.816 1.00 60.52  ? 193  PHE A C   1 
ATOM   1494  O  O   . PHE A 1 193  ? 87.822  76.094  127.683 1.00 61.78  ? 193  PHE A O   1 
ATOM   1495  C  CB  . PHE A 1 193  ? 87.791  75.165  130.916 1.00 57.69  ? 193  PHE A CB  1 
ATOM   1496  C  CG  . PHE A 1 193  ? 88.441  73.957  130.292 1.00 58.15  ? 193  PHE A CG  1 
ATOM   1497  C  CD1 . PHE A 1 193  ? 87.781  72.733  130.259 1.00 57.65  ? 193  PHE A CD1 1 
ATOM   1498  C  CD2 . PHE A 1 193  ? 89.729  74.034  129.759 1.00 58.09  ? 193  PHE A CD2 1 
ATOM   1499  C  CE1 . PHE A 1 193  ? 88.387  71.610  129.688 1.00 58.39  ? 193  PHE A CE1 1 
ATOM   1500  C  CE2 . PHE A 1 193  ? 90.338  72.918  129.192 1.00 58.12  ? 193  PHE A CE2 1 
ATOM   1501  C  CZ  . PHE A 1 193  ? 89.668  71.705  129.157 1.00 58.16  ? 193  PHE A CZ  1 
ATOM   1502  N  N   . GLU A 1 194  ? 88.696  77.572  129.131 1.00 60.99  ? 194  GLU A N   1 
ATOM   1503  C  CA  . GLU A 1 194  ? 89.555  78.167  128.138 1.00 63.38  ? 194  GLU A CA  1 
ATOM   1504  C  C   . GLU A 1 194  ? 90.995  77.746  128.344 1.00 64.18  ? 194  GLU A C   1 
ATOM   1505  O  O   . GLU A 1 194  ? 91.427  77.484  129.471 1.00 63.21  ? 194  GLU A O   1 
ATOM   1506  C  CB  . GLU A 1 194  ? 89.452  79.688  128.173 1.00 63.75  ? 194  GLU A CB  1 
ATOM   1507  C  CG  . GLU A 1 194  ? 88.376  80.264  127.289 1.00 65.49  ? 194  GLU A CG  1 
ATOM   1508  C  CD  . GLU A 1 194  ? 88.359  81.788  127.325 1.00 68.22  ? 194  GLU A CD  1 
ATOM   1509  O  OE1 . GLU A 1 194  ? 89.221  82.434  126.668 1.00 69.57  ? 194  GLU A OE1 1 
ATOM   1510  O  OE2 . GLU A 1 194  ? 87.472  82.335  128.016 1.00 67.69  ? 194  GLU A OE2 1 
ATOM   1511  N  N   . VAL A 1 195  ? 91.722  77.665  127.234 1.00 66.36  ? 195  VAL A N   1 
ATOM   1512  C  CA  . VAL A 1 195  ? 93.166  77.564  127.254 1.00 67.72  ? 195  VAL A CA  1 
ATOM   1513  C  C   . VAL A 1 195  ? 93.673  78.782  126.496 1.00 70.12  ? 195  VAL A C   1 
ATOM   1514  O  O   . VAL A 1 195  ? 93.308  78.997  125.342 1.00 71.35  ? 195  VAL A O   1 
ATOM   1515  C  CB  . VAL A 1 195  ? 93.660  76.251  126.612 1.00 68.31  ? 195  VAL A CB  1 
ATOM   1516  C  CG1 . VAL A 1 195  ? 95.171  76.159  126.669 1.00 68.87  ? 195  VAL A CG1 1 
ATOM   1517  C  CG2 . VAL A 1 195  ? 93.054  75.056  127.318 1.00 66.67  ? 195  VAL A CG2 1 
ATOM   1518  N  N   . LYS A 1 196  ? 94.488  79.592  127.164 1.00 71.51  ? 196  LYS A N   1 
ATOM   1519  C  CA  . LYS A 1 196  ? 94.981  80.844  126.591 1.00 74.62  ? 196  LYS A CA  1 
ATOM   1520  C  C   . LYS A 1 196  ? 96.499  80.980  126.679 1.00 76.66  ? 196  LYS A C   1 
ATOM   1521  O  O   . LYS A 1 196  ? 97.142  80.370  127.531 1.00 75.74  ? 196  LYS A O   1 
ATOM   1522  C  CB  . LYS A 1 196  ? 94.316  82.050  127.268 1.00 74.07  ? 196  LYS A CB  1 
ATOM   1523  C  CG  . LYS A 1 196  ? 92.929  82.395  126.747 1.00 74.88  ? 196  LYS A CG  1 
ATOM   1524  C  CD  . LYS A 1 196  ? 92.586  83.867  127.000 1.00 77.04  ? 196  LYS A CD  1 
ATOM   1525  C  CE  . LYS A 1 196  ? 93.314  84.791  126.014 1.00 80.83  ? 196  LYS A CE  1 
ATOM   1526  N  NZ  . LYS A 1 196  ? 93.084  86.236  126.304 1.00 82.68  ? 196  LYS A NZ  1 
ATOM   1527  N  N   . GLU A 1 197  ? 97.057  81.792  125.787 1.00 80.32  ? 197  GLU A N   1 
ATOM   1528  C  CA  . GLU A 1 197  ? 98.486  82.085  125.791 1.00 83.57  ? 197  GLU A CA  1 
ATOM   1529  C  C   . GLU A 1 197  ? 98.825  83.294  126.648 1.00 84.92  ? 197  GLU A C   1 
ATOM   1530  O  O   . GLU A 1 197  ? 98.062  84.261  126.716 1.00 85.08  ? 197  GLU A O   1 
ATOM   1531  C  CB  . GLU A 1 197  ? 99.002  82.312  124.369 1.00 85.90  ? 197  GLU A CB  1 
ATOM   1532  C  CG  . GLU A 1 197  ? 99.872  81.186  123.827 1.00 87.48  ? 197  GLU A CG  1 
ATOM   1533  C  CD  . GLU A 1 197  ? 100.442 81.492  122.445 1.00 91.64  ? 197  GLU A CD  1 
ATOM   1534  O  OE1 . GLU A 1 197  ? 101.246 80.675  121.941 1.00 93.08  ? 197  GLU A OE1 1 
ATOM   1535  O  OE2 . GLU A 1 197  ? 100.093 82.546  121.862 1.00 93.43  ? 197  GLU A OE2 1 
ATOM   1536  N  N   . TYR A 1 198  ? 99.991  83.231  127.284 1.00 86.85  ? 198  TYR A N   1 
ATOM   1537  C  CA  . TYR A 1 198  ? 100.487 84.322  128.122 1.00 88.87  ? 198  TYR A CA  1 
ATOM   1538  C  C   . TYR A 1 198  ? 101.090 85.457  127.284 1.00 91.73  ? 198  TYR A C   1 
ATOM   1539  O  O   . TYR A 1 198  ? 101.381 86.531  127.814 1.00 92.86  ? 198  TYR A O   1 
ATOM   1540  C  CB  . TYR A 1 198  ? 101.521 83.792  129.137 1.00 89.19  ? 198  TYR A CB  1 
ATOM   1541  C  CG  . TYR A 1 198  ? 102.958 83.732  128.623 1.00 91.89  ? 198  TYR A CG  1 
ATOM   1542  C  CD1 . TYR A 1 198  ? 103.373 82.715  127.758 1.00 93.15  ? 198  TYR A CD1 1 
ATOM   1543  C  CD2 . TYR A 1 198  ? 103.906 84.690  129.017 1.00 94.48  ? 198  TYR A CD2 1 
ATOM   1544  C  CE1 . TYR A 1 198  ? 104.699 82.658  127.283 1.00 95.68  ? 198  TYR A CE1 1 
ATOM   1545  C  CE2 . TYR A 1 198  ? 105.231 84.641  128.553 1.00 96.91  ? 198  TYR A CE2 1 
ATOM   1546  C  CZ  . TYR A 1 198  ? 105.617 83.621  127.686 1.00 97.36  ? 198  TYR A CZ  1 
ATOM   1547  O  OH  . TYR A 1 198  ? 106.916 83.560  127.221 1.00 98.86  ? 198  TYR A OH  1 
ATOM   1548  N  N   . VAL A 1 199  ? 101.264 85.212  125.983 1.00 93.39  ? 199  VAL A N   1 
ATOM   1549  C  CA  . VAL A 1 199  ? 101.966 86.137  125.074 1.00 96.50  ? 199  VAL A CA  1 
ATOM   1550  C  C   . VAL A 1 199  ? 101.267 87.514  124.939 1.00 97.81  ? 199  VAL A C   1 
ATOM   1551  O  O   . VAL A 1 199  ? 101.692 88.369  124.142 1.00 100.50 ? 199  VAL A O   1 
ATOM   1552  C  CB  . VAL A 1 199  ? 102.256 85.485  123.675 1.00 97.71  ? 199  VAL A CB  1 
ATOM   1553  C  CG1 . VAL A 1 199  ? 103.394 86.220  122.945 1.00 100.90 ? 199  VAL A CG1 1 
ATOM   1554  C  CG2 . VAL A 1 199  ? 102.623 84.013  123.824 1.00 96.19  ? 199  VAL A CG2 1 
ATOM   1555  N  N   . LEU A 1 200  ? 100.210 87.717  125.734 1.00 96.02  ? 200  LEU A N   1 
ATOM   1556  C  CA  . LEU A 1 200  ? 99.608  89.039  125.937 1.00 96.96  ? 200  LEU A CA  1 
ATOM   1557  C  C   . LEU A 1 200  ? 100.626 89.992  126.589 1.00 98.39  ? 200  LEU A C   1 
ATOM   1558  O  O   . LEU A 1 200  ? 100.546 90.256  127.797 1.00 97.69  ? 200  LEU A O   1 
ATOM   1559  C  CB  . LEU A 1 200  ? 98.357  88.936  126.830 1.00 94.85  ? 200  LEU A CB  1 
ATOM   1560  C  CG  . LEU A 1 200  ? 97.108  88.132  126.427 1.00 93.75  ? 200  LEU A CG  1 
ATOM   1561  C  CD1 . LEU A 1 200  ? 96.321  87.682  127.668 1.00 91.09  ? 200  LEU A CD1 1 
ATOM   1562  C  CD2 . LEU A 1 200  ? 96.210  88.917  125.460 1.00 95.76  ? 200  LEU A CD2 1 
ATOM   1563  N  N   . SER A 1 201  ? 101.577 90.502  125.797 1.00 63.60  ? 201  SER A N   1 
ATOM   1564  C  CA  . SER A 1 201  ? 102.627 91.402  126.318 1.00 62.99  ? 201  SER A CA  1 
ATOM   1565  C  C   . SER A 1 201  ? 102.072 92.762  126.774 1.00 61.89  ? 201  SER A C   1 
ATOM   1566  O  O   . SER A 1 201  ? 102.760 93.518  127.496 1.00 62.04  ? 201  SER A O   1 
ATOM   1567  C  CB  . SER A 1 201  ? 103.798 91.576  125.324 1.00 63.30  ? 201  SER A CB  1 
ATOM   1568  O  OG  . SER A 1 201  ? 103.343 91.848  124.001 1.00 64.67  ? 201  SER A OG  1 
ATOM   1569  N  N   . THR A 1 202  ? 100.834 93.071  126.361 1.00 59.98  ? 202  THR A N   1 
ATOM   1570  C  CA  . THR A 1 202  ? 100.154 94.270  126.865 1.00 57.87  ? 202  THR A CA  1 
ATOM   1571  C  C   . THR A 1 202  ? 99.848  94.095  128.354 1.00 55.58  ? 202  THR A C   1 
ATOM   1572  O  O   . THR A 1 202  ? 99.636  92.973  128.820 1.00 55.83  ? 202  THR A O   1 
ATOM   1573  C  CB  . THR A 1 202  ? 98.885  94.657  126.045 1.00 58.25  ? 202  THR A CB  1 
ATOM   1574  O  OG1 . THR A 1 202  ? 98.448  95.978  126.424 1.00 58.49  ? 202  THR A OG1 1 
ATOM   1575  C  CG2 . THR A 1 202  ? 97.756  93.639  126.248 1.00 58.45  ? 202  THR A CG2 1 
ATOM   1576  N  N   . PHE A 1 203  ? 99.860  95.204  129.089 1.00 52.49  ? 203  PHE A N   1 
ATOM   1577  C  CA  . PHE A 1 203  ? 99.761  95.184  130.538 1.00 49.23  ? 203  PHE A CA  1 
ATOM   1578  C  C   . PHE A 1 203  ? 98.545  95.978  130.991 1.00 48.40  ? 203  PHE A C   1 
ATOM   1579  O  O   . PHE A 1 203  ? 98.045  96.827  130.246 1.00 48.27  ? 203  PHE A O   1 
ATOM   1580  C  CB  . PHE A 1 203  ? 101.043 95.753  131.153 1.00 48.71  ? 203  PHE A CB  1 
ATOM   1581  C  CG  . PHE A 1 203  ? 101.374 97.149  130.704 1.00 45.35  ? 203  PHE A CG  1 
ATOM   1582  C  CD1 . PHE A 1 203  ? 102.074 97.368  129.533 1.00 42.53  ? 203  PHE A CD1 1 
ATOM   1583  C  CD2 . PHE A 1 203  ? 101.003 98.243  131.471 1.00 43.97  ? 203  PHE A CD2 1 
ATOM   1584  C  CE1 . PHE A 1 203  ? 102.381 98.646  129.116 1.00 42.58  ? 203  PHE A CE1 1 
ATOM   1585  C  CE2 . PHE A 1 203  ? 101.303 99.533  131.065 1.00 43.63  ? 203  PHE A CE2 1 
ATOM   1586  C  CZ  . PHE A 1 203  ? 101.997 99.740  129.885 1.00 43.34  ? 203  PHE A CZ  1 
ATOM   1587  N  N   A ASP A 1 204  ? 98.057  95.710  132.199 0.50 47.82  ? 204  ASP A N   1 
ATOM   1588  N  N   B ASP A 1 204  ? 98.072  95.693  132.199 0.50 47.81  ? 204  ASP A N   1 
ATOM   1589  C  CA  A ASP A 1 204  ? 96.931  96.487  132.724 0.50 47.41  ? 204  ASP A CA  1 
ATOM   1590  C  CA  B ASP A 1 204  ? 96.960  96.438  132.781 0.50 47.42  ? 204  ASP A CA  1 
ATOM   1591  C  C   A ASP A 1 204  ? 97.299  97.355  133.926 0.50 47.00  ? 204  ASP A C   1 
ATOM   1592  C  C   B ASP A 1 204  ? 97.463  97.453  133.805 0.50 46.97  ? 204  ASP A C   1 
ATOM   1593  O  O   A ASP A 1 204  ? 98.069  96.946  134.794 0.50 47.20  ? 204  ASP A O   1 
ATOM   1594  O  O   B ASP A 1 204  ? 98.508  97.252  134.423 0.50 47.12  ? 204  ASP A O   1 
ATOM   1595  C  CB  A ASP A 1 204  ? 95.700  95.613  133.006 0.50 47.39  ? 204  ASP A CB  1 
ATOM   1596  C  CB  B ASP A 1 204  ? 95.929  95.488  133.403 0.50 47.38  ? 204  ASP A CB  1 
ATOM   1597  C  CG  A ASP A 1 204  ? 95.809  94.839  134.295 0.50 47.70  ? 204  ASP A CG  1 
ATOM   1598  C  CG  B ASP A 1 204  ? 95.178  94.662  132.355 0.50 47.86  ? 204  ASP A CG  1 
ATOM   1599  O  OD1 A ASP A 1 204  ? 95.021  95.133  135.223 0.50 48.12  ? 204  ASP A OD1 1 
ATOM   1600  O  OD1 B ASP A 1 204  ? 94.714  95.233  131.339 0.50 47.83  ? 204  ASP A OD1 1 
ATOM   1601  O  OD2 A ASP A 1 204  ? 96.677  93.940  134.378 0.50 48.12  ? 204  ASP A OD2 1 
ATOM   1602  O  OD2 B ASP A 1 204  ? 95.040  93.435  132.557 0.50 48.67  ? 204  ASP A OD2 1 
ATOM   1603  N  N   . VAL A 1 205  ? 96.732  98.557  133.949 1.00 46.51  ? 205  VAL A N   1 
ATOM   1604  C  CA  . VAL A 1 205  ? 97.046  99.571  134.942 1.00 45.64  ? 205  VAL A CA  1 
ATOM   1605  C  C   . VAL A 1 205  ? 95.881  99.704  135.913 1.00 45.11  ? 205  VAL A C   1 
ATOM   1606  O  O   . VAL A 1 205  ? 94.734  99.773  135.501 1.00 44.74  ? 205  VAL A O   1 
ATOM   1607  C  CB  . VAL A 1 205  ? 97.333  100.930 134.273 1.00 45.60  ? 205  VAL A CB  1 
ATOM   1608  C  CG1 . VAL A 1 205  ? 97.699  101.984 135.308 1.00 45.17  ? 205  VAL A CG1 1 
ATOM   1609  C  CG2 . VAL A 1 205  ? 98.447  100.786 133.257 1.00 45.48  ? 205  VAL A CG2 1 
ATOM   1610  N  N   . GLN A 1 206  ? 96.189  99.726  137.202 1.00 44.95  ? 206  GLN A N   1 
ATOM   1611  C  CA  . GLN A 1 206  ? 95.187  99.932  138.243 1.00 45.03  ? 206  GLN A CA  1 
ATOM   1612  C  C   . GLN A 1 206  ? 95.430  101.240 138.980 1.00 44.41  ? 206  GLN A C   1 
ATOM   1613  O  O   . GLN A 1 206  ? 96.564  101.593 139.288 1.00 44.26  ? 206  GLN A O   1 
ATOM   1614  C  CB  . GLN A 1 206  ? 95.161  98.756  139.219 1.00 45.36  ? 206  GLN A CB  1 
ATOM   1615  C  CG  . GLN A 1 206  ? 94.428  97.529  138.684 1.00 48.94  ? 206  GLN A CG  1 
ATOM   1616  C  CD  . GLN A 1 206  ? 94.550  96.302  139.606 1.00 56.11  ? 206  GLN A CD  1 
ATOM   1617  O  OE1 . GLN A 1 206  ? 95.178  95.302  139.233 1.00 59.39  ? 206  GLN A OE1 1 
ATOM   1618  N  NE2 . GLN A 1 206  ? 93.946  96.371  140.809 1.00 56.79  ? 206  GLN A NE2 1 
ATOM   1619  N  N   . VAL A 1 207  ? 94.347  101.964 139.240 1.00 44.09  ? 207  VAL A N   1 
ATOM   1620  C  CA  . VAL A 1 207  ? 94.402  103.229 139.961 1.00 43.65  ? 207  VAL A CA  1 
ATOM   1621  C  C   . VAL A 1 207  ? 93.302  103.281 141.017 1.00 43.55  ? 207  VAL A C   1 
ATOM   1622  O  O   . VAL A 1 207  ? 92.119  103.348 140.696 1.00 43.49  ? 207  VAL A O   1 
ATOM   1623  C  CB  . VAL A 1 207  ? 94.274  104.413 139.002 1.00 43.47  ? 207  VAL A CB  1 
ATOM   1624  C  CG1 . VAL A 1 207  ? 94.418  105.741 139.747 1.00 43.64  ? 207  VAL A CG1 1 
ATOM   1625  C  CG2 . VAL A 1 207  ? 95.324  104.298 137.932 1.00 44.32  ? 207  VAL A CG2 1 
ATOM   1626  N  N   A MET A 1 208  ? 93.697  103.249 142.280 0.50 43.62  ? 208  MET A N   1 
ATOM   1627  N  N   B MET A 1 208  ? 93.715  103.253 142.278 0.50 43.66  ? 208  MET A N   1 
ATOM   1628  C  CA  A MET A 1 208  ? 92.739  103.344 143.377 0.50 43.80  ? 208  MET A CA  1 
ATOM   1629  C  CA  B MET A 1 208  ? 92.795  103.286 143.413 0.50 43.87  ? 208  MET A CA  1 
ATOM   1630  C  C   A MET A 1 208  ? 93.345  104.167 144.505 0.50 43.82  ? 208  MET A C   1 
ATOM   1631  C  C   B MET A 1 208  ? 93.368  104.196 144.499 0.50 43.86  ? 208  MET A C   1 
ATOM   1632  O  O   A MET A 1 208  ? 94.568  104.197 144.655 0.50 43.95  ? 208  MET A O   1 
ATOM   1633  O  O   B MET A 1 208  ? 94.589  104.326 144.605 0.50 44.02  ? 208  MET A O   1 
ATOM   1634  C  CB  A MET A 1 208  ? 92.333  101.949 143.870 0.50 43.85  ? 208  MET A CB  1 
ATOM   1635  C  CB  B MET A 1 208  ? 92.567  101.867 143.959 0.50 43.97  ? 208  MET A CB  1 
ATOM   1636  C  CG  A MET A 1 208  ? 93.470  101.158 144.492 0.50 44.99  ? 208  MET A CG  1 
ATOM   1637  C  CG  B MET A 1 208  ? 93.822  101.184 144.534 0.50 45.25  ? 208  MET A CG  1 
ATOM   1638  S  SD  A MET A 1 208  ? 93.087  99.430  144.771 0.50 47.54  ? 208  MET A SD  1 
ATOM   1639  S  SD  B MET A 1 208  ? 95.044  100.653 143.302 0.50 47.40  ? 208  MET A SD  1 
ATOM   1640  C  CE  A MET A 1 208  ? 94.653  98.853  145.442 0.50 46.95  ? 208  MET A CE  1 
ATOM   1641  C  CE  B MET A 1 208  ? 94.322  99.086  142.807 0.50 47.61  ? 208  MET A CE  1 
ATOM   1642  N  N   . PRO A 1 209  ? 92.498  104.847 145.299 1.00 43.92  ? 209  PRO A N   1 
ATOM   1643  C  CA  . PRO A 1 209  ? 92.997  105.609 146.452 1.00 43.86  ? 209  PRO A CA  1 
ATOM   1644  C  C   . PRO A 1 209  ? 93.663  104.660 147.441 1.00 43.82  ? 209  PRO A C   1 
ATOM   1645  O  O   . PRO A 1 209  ? 93.180  103.540 147.629 1.00 43.73  ? 209  PRO A O   1 
ATOM   1646  C  CB  . PRO A 1 209  ? 91.720  106.179 147.065 1.00 43.93  ? 209  PRO A CB  1 
ATOM   1647  C  CG  . PRO A 1 209  ? 90.740  106.180 145.963 1.00 43.42  ? 209  PRO A CG  1 
ATOM   1648  C  CD  . PRO A 1 209  ? 91.032  104.950 145.186 1.00 43.48  ? 209  PRO A CD  1 
ATOM   1649  N  N   . SER A 1 210  ? 94.771  105.078 148.044 1.00 44.09  ? 210  SER A N   1 
ATOM   1650  C  CA  . SER A 1 210  ? 95.479  104.210 148.991 1.00 44.34  ? 210  SER A CA  1 
ATOM   1651  C  C   . SER A 1 210  ? 94.938  104.361 150.407 1.00 44.85  ? 210  SER A C   1 
ATOM   1652  O  O   . SER A 1 210  ? 95.210  103.547 151.278 1.00 45.52  ? 210  SER A O   1 
ATOM   1653  C  CB  . SER A 1 210  ? 96.981  104.471 148.953 1.00 44.51  ? 210  SER A CB  1 
ATOM   1654  O  OG  . SER A 1 210  ? 97.278  105.804 149.304 1.00 46.25  ? 210  SER A OG  1 
ATOM   1655  N  N   . VAL A 1 211  ? 94.195  105.435 150.629 1.00 45.00  ? 211  VAL A N   1 
ATOM   1656  C  CA  . VAL A 1 211  ? 93.421  105.645 151.842 1.00 45.16  ? 211  VAL A CA  1 
ATOM   1657  C  C   . VAL A 1 211  ? 92.174  106.373 151.338 1.00 45.29  ? 211  VAL A C   1 
ATOM   1658  O  O   . VAL A 1 211  ? 92.257  107.108 150.343 1.00 45.11  ? 211  VAL A O   1 
ATOM   1659  C  CB  . VAL A 1 211  ? 94.215  106.477 152.914 1.00 45.70  ? 211  VAL A CB  1 
ATOM   1660  C  CG1 . VAL A 1 211  ? 94.445  107.926 152.464 1.00 45.19  ? 211  VAL A CG1 1 
ATOM   1661  C  CG2 . VAL A 1 211  ? 93.511  106.449 154.258 1.00 45.57  ? 211  VAL A CG2 1 
ATOM   1662  N  N   . ILE A 1 212  ? 91.022  106.174 151.975 1.00 45.26  ? 212  ILE A N   1 
ATOM   1663  C  CA  . ILE A 1 212  ? 89.818  106.814 151.454 1.00 45.47  ? 212  ILE A CA  1 
ATOM   1664  C  C   . ILE A 1 212  ? 89.868  108.350 151.639 1.00 45.62  ? 212  ILE A C   1 
ATOM   1665  O  O   . ILE A 1 212  ? 90.155  108.836 152.728 1.00 46.45  ? 212  ILE A O   1 
ATOM   1666  C  CB  . ILE A 1 212  ? 88.488  106.149 151.951 1.00 45.85  ? 212  ILE A CB  1 
ATOM   1667  C  CG1 . ILE A 1 212  ? 87.744  107.038 152.930 1.00 46.56  ? 212  ILE A CG1 1 
ATOM   1668  C  CG2 . ILE A 1 212  ? 88.712  104.710 152.499 1.00 46.72  ? 212  ILE A CG2 1 
ATOM   1669  C  CD1 . ILE A 1 212  ? 86.285  106.976 152.726 1.00 48.03  ? 212  ILE A CD1 1 
ATOM   1670  N  N   . PRO A 1 213  ? 89.640  109.114 150.554 1.00 45.31  ? 213  PRO A N   1 
ATOM   1671  C  CA  . PRO A 1 213  ? 89.778  110.573 150.598 1.00 45.59  ? 213  PRO A CA  1 
ATOM   1672  C  C   . PRO A 1 213  ? 88.691  111.270 151.402 1.00 46.37  ? 213  PRO A C   1 
ATOM   1673  O  O   . PRO A 1 213  ? 87.496  111.107 151.111 1.00 46.55  ? 213  PRO A O   1 
ATOM   1674  C  CB  . PRO A 1 213  ? 89.663  110.988 149.121 1.00 45.03  ? 213  PRO A CB  1 
ATOM   1675  C  CG  . PRO A 1 213  ? 89.786  109.734 148.337 1.00 44.11  ? 213  PRO A CG  1 
ATOM   1676  C  CD  . PRO A 1 213  ? 89.259  108.653 149.208 1.00 44.53  ? 213  PRO A CD  1 
ATOM   1677  N  N   . LEU A 1 214  ? 89.108  112.042 152.402 1.00 47.01  ? 214  LEU A N   1 
ATOM   1678  C  CA  . LEU A 1 214  ? 88.194  112.887 153.160 1.00 47.58  ? 214  LEU A CA  1 
ATOM   1679  C  C   . LEU A 1 214  ? 88.510  114.346 152.877 1.00 48.05  ? 214  LEU A C   1 
ATOM   1680  O  O   . LEU A 1 214  ? 89.670  114.707 152.703 1.00 48.28  ? 214  LEU A O   1 
ATOM   1681  C  CB  . LEU A 1 214  ? 88.312  112.615 154.653 1.00 48.27  ? 214  LEU A CB  1 
ATOM   1682  C  CG  . LEU A 1 214  ? 88.150  111.200 155.208 1.00 48.74  ? 214  LEU A CG  1 
ATOM   1683  C  CD1 . LEU A 1 214  ? 88.494  111.201 156.688 1.00 49.03  ? 214  LEU A CD1 1 
ATOM   1684  C  CD2 . LEU A 1 214  ? 86.742  110.634 154.987 1.00 49.52  ? 214  LEU A CD2 1 
ATOM   1685  N  N   . GLU A 1 215  ? 87.474  115.176 152.822 1.00 48.49  ? 215  GLU A N   1 
ATOM   1686  C  CA  . GLU A 1 215  ? 87.606  116.597 152.520 1.00 49.37  ? 215  GLU A CA  1 
ATOM   1687  C  C   . GLU A 1 215  ? 88.666  117.295 153.372 1.00 50.23  ? 215  GLU A C   1 
ATOM   1688  O  O   . GLU A 1 215  ? 89.416  118.138 152.878 1.00 50.32  ? 215  GLU A O   1 
ATOM   1689  C  CB  . GLU A 1 215  ? 86.261  117.276 152.728 1.00 49.82  ? 215  GLU A CB  1 
ATOM   1690  C  CG  . GLU A 1 215  ? 86.198  118.721 152.291 1.00 51.32  ? 215  GLU A CG  1 
ATOM   1691  C  CD  . GLU A 1 215  ? 84.826  119.319 152.504 1.00 53.54  ? 215  GLU A CD  1 
ATOM   1692  O  OE1 . GLU A 1 215  ? 84.292  119.202 153.631 1.00 54.61  ? 215  GLU A OE1 1 
ATOM   1693  O  OE2 . GLU A 1 215  ? 84.278  119.905 151.544 1.00 54.73  ? 215  GLU A OE2 1 
ATOM   1694  N  N   . GLU A 1 216  ? 88.708  116.928 154.650 1.00 51.12  ? 216  GLU A N   1 
ATOM   1695  C  CA  . GLU A 1 216  ? 89.638  117.479 155.634 1.00 52.39  ? 216  GLU A CA  1 
ATOM   1696  C  C   . GLU A 1 216  ? 91.099  117.239 155.236 1.00 52.03  ? 216  GLU A C   1 
ATOM   1697  O  O   . GLU A 1 216  ? 91.969  118.046 155.569 1.00 52.75  ? 216  GLU A O   1 
ATOM   1698  C  CB  . GLU A 1 216  ? 89.348  116.895 157.040 1.00 53.21  ? 216  GLU A CB  1 
ATOM   1699  C  CG  . GLU A 1 216  ? 89.487  115.352 157.134 1.00 54.80  ? 216  GLU A CG  1 
ATOM   1700  C  CD  . GLU A 1 216  ? 88.981  114.752 158.441 1.00 58.04  ? 216  GLU A CD  1 
ATOM   1701  O  OE1 . GLU A 1 216  ? 87.747  114.720 158.650 1.00 59.93  ? 216  GLU A OE1 1 
ATOM   1702  O  OE2 . GLU A 1 216  ? 89.816  114.273 159.247 1.00 59.05  ? 216  GLU A OE2 1 
ATOM   1703  N  N   . HIS A 1 217  ? 91.357  116.137 154.530 1.00 51.12  ? 217  HIS A N   1 
ATOM   1704  C  CA  . HIS A 1 217  ? 92.696  115.809 154.038 1.00 50.91  ? 217  HIS A CA  1 
ATOM   1705  C  C   . HIS A 1 217  ? 93.222  116.835 153.027 1.00 50.87  ? 217  HIS A C   1 
ATOM   1706  O  O   . HIS A 1 217  ? 94.429  116.981 152.866 1.00 50.79  ? 217  HIS A O   1 
ATOM   1707  C  CB  . HIS A 1 217  ? 92.715  114.436 153.366 1.00 50.34  ? 217  HIS A CB  1 
ATOM   1708  C  CG  . HIS A 1 217  ? 92.383  113.293 154.271 1.00 50.73  ? 217  HIS A CG  1 
ATOM   1709  N  ND1 . HIS A 1 217  ? 91.865  112.108 153.798 1.00 50.52  ? 217  HIS A ND1 1 
ATOM   1710  C  CD2 . HIS A 1 217  ? 92.504  113.142 155.612 1.00 52.87  ? 217  HIS A CD2 1 
ATOM   1711  C  CE1 . HIS A 1 217  ? 91.681  111.273 154.805 1.00 51.48  ? 217  HIS A CE1 1 
ATOM   1712  N  NE2 . HIS A 1 217  ? 92.056  111.878 155.919 1.00 53.06  ? 217  HIS A NE2 1 
ATOM   1713  N  N   . GLN A 1 218  ? 92.309  117.520 152.338 1.00 50.81  ? 218  GLN A N   1 
ATOM   1714  C  CA  . GLN A 1 218  ? 92.650  118.499 151.301 1.00 50.91  ? 218  GLN A CA  1 
ATOM   1715  C  C   . GLN A 1 218  ? 93.592  117.914 150.251 1.00 50.79  ? 218  GLN A C   1 
ATOM   1716  O  O   . GLN A 1 218  ? 94.362  118.636 149.605 1.00 51.58  ? 218  GLN A O   1 
ATOM   1717  C  CB  . GLN A 1 218  ? 93.236  119.781 151.913 1.00 51.62  ? 218  GLN A CB  1 
ATOM   1718  C  CG  . GLN A 1 218  ? 92.213  120.681 152.619 1.00 51.78  ? 218  GLN A CG  1 
ATOM   1719  C  CD  . GLN A 1 218  ? 91.159  121.235 151.668 1.00 51.73  ? 218  GLN A CD  1 
ATOM   1720  O  OE1 . GLN A 1 218  ? 91.453  122.054 150.790 1.00 51.68  ? 218  GLN A OE1 1 
ATOM   1721  N  NE2 . GLN A 1 218  ? 89.924  120.780 151.835 1.00 51.10  ? 218  GLN A NE2 1 
ATOM   1722  N  N   . ALA A 1 219  ? 93.522  116.597 150.078 1.00 50.02  ? 219  ALA A N   1 
ATOM   1723  C  CA  . ALA A 1 219  ? 94.420  115.893 149.175 1.00 49.07  ? 219  ALA A CA  1 
ATOM   1724  C  C   . ALA A 1 219  ? 93.887  114.505 148.841 1.00 48.03  ? 219  ALA A C   1 
ATOM   1725  O  O   . ALA A 1 219  ? 93.041  113.959 149.556 1.00 48.31  ? 219  ALA A O   1 
ATOM   1726  C  CB  . ALA A 1 219  ? 95.827  115.791 149.796 1.00 49.39  ? 219  ALA A CB  1 
ATOM   1727  N  N   . VAL A 1 220  ? 94.395  113.937 147.755 1.00 46.84  ? 220  VAL A N   1 
ATOM   1728  C  CA  . VAL A 1 220  ? 94.096  112.557 147.391 1.00 45.61  ? 220  VAL A CA  1 
ATOM   1729  C  C   . VAL A 1 220  ? 95.408  111.791 147.253 1.00 45.11  ? 220  VAL A C   1 
ATOM   1730  O  O   . VAL A 1 220  ? 96.315  112.231 146.535 1.00 45.05  ? 220  VAL A O   1 
ATOM   1731  C  CB  . VAL A 1 220  ? 93.245  112.493 146.090 1.00 45.21  ? 220  VAL A CB  1 
ATOM   1732  C  CG1 . VAL A 1 220  ? 93.148  111.077 145.551 1.00 44.19  ? 220  VAL A CG1 1 
ATOM   1733  C  CG2 . VAL A 1 220  ? 91.855  113.046 146.353 1.00 45.01  ? 220  VAL A CG2 1 
ATOM   1734  N  N   . ASN A 1 221  ? 95.513  110.671 147.966 1.00 44.74  ? 221  ASN A N   1 
ATOM   1735  C  CA  . ASN A 1 221  ? 96.655  109.755 147.834 1.00 44.74  ? 221  ASN A CA  1 
ATOM   1736  C  C   . ASN A 1 221  ? 96.267  108.603 146.924 1.00 43.42  ? 221  ASN A C   1 
ATOM   1737  O  O   . ASN A 1 221  ? 95.251  107.958 147.150 1.00 43.14  ? 221  ASN A O   1 
ATOM   1738  C  CB  . ASN A 1 221  ? 97.094  109.204 149.200 1.00 45.42  ? 221  ASN A CB  1 
ATOM   1739  C  CG  . ASN A 1 221  ? 97.608  110.281 150.150 1.00 47.92  ? 221  ASN A CG  1 
ATOM   1740  O  OD1 . ASN A 1 221  ? 97.715  111.457 149.790 1.00 48.80  ? 221  ASN A OD1 1 
ATOM   1741  N  ND2 . ASN A 1 221  ? 97.932  109.869 151.379 1.00 51.64  ? 221  ASN A ND2 1 
ATOM   1742  N  N   . LEU A 1 222  ? 97.063  108.342 145.897 1.00 42.93  ? 222  LEU A N   1 
ATOM   1743  C  CA  . LEU A 1 222  ? 96.709  107.306 144.912 1.00 42.05  ? 222  LEU A CA  1 
ATOM   1744  C  C   . LEU A 1 222  ? 97.760  106.237 144.732 1.00 41.63  ? 222  LEU A C   1 
ATOM   1745  O  O   . LEU A 1 222  ? 98.935  106.540 144.572 1.00 42.00  ? 222  LEU A O   1 
ATOM   1746  C  CB  . LEU A 1 222  ? 96.409  107.923 143.545 1.00 41.56  ? 222  LEU A CB  1 
ATOM   1747  C  CG  . LEU A 1 222  ? 95.201  108.837 143.358 1.00 41.30  ? 222  LEU A CG  1 
ATOM   1748  C  CD1 . LEU A 1 222  ? 95.203  109.360 141.947 1.00 40.94  ? 222  LEU A CD1 1 
ATOM   1749  C  CD2 . LEU A 1 222  ? 93.892  108.114 143.659 1.00 40.75  ? 222  LEU A CD2 1 
ATOM   1750  N  N   . THR A 1 223  ? 97.316  104.989 144.751 1.00 41.43  ? 223  THR A N   1 
ATOM   1751  C  CA  . THR A 1 223  ? 98.131  103.848 144.369 1.00 41.54  ? 223  THR A CA  1 
ATOM   1752  C  C   . THR A 1 223  ? 97.990  103.619 142.870 1.00 41.73  ? 223  THR A C   1 
ATOM   1753  O  O   . THR A 1 223  ? 96.884  103.445 142.365 1.00 41.62  ? 223  THR A O   1 
ATOM   1754  C  CB  . THR A 1 223  ? 97.701  102.588 145.139 1.00 41.14  ? 223  THR A CB  1 
ATOM   1755  O  OG1 . THR A 1 223  ? 97.899  102.815 146.539 1.00 42.88  ? 223  THR A OG1 1 
ATOM   1756  C  CG2 . THR A 1 223  ? 98.511  101.358 144.721 1.00 39.60  ? 223  THR A CG2 1 
ATOM   1757  N  N   . ILE A 1 224  ? 99.113  103.644 142.164 1.00 42.63  ? 224  ILE A N   1 
ATOM   1758  C  CA  . ILE A 1 224  ? 99.149  103.287 140.752 1.00 43.28  ? 224  ILE A CA  1 
ATOM   1759  C  C   . ILE A 1 224  ? 99.879  101.971 140.623 1.00 44.25  ? 224  ILE A C   1 
ATOM   1760  O  O   . ILE A 1 224  ? 100.947 101.780 141.213 1.00 44.79  ? 224  ILE A O   1 
ATOM   1761  C  CB  . ILE A 1 224  ? 99.870  104.330 139.907 1.00 43.18  ? 224  ILE A CB  1 
ATOM   1762  C  CG1 . ILE A 1 224  ? 99.161  105.677 140.026 1.00 43.32  ? 224  ILE A CG1 1 
ATOM   1763  C  CG2 . ILE A 1 224  ? 99.911  103.889 138.453 1.00 42.84  ? 224  ILE A CG2 1 
ATOM   1764  C  CD1 . ILE A 1 224  ? 100.012 106.818 139.563 1.00 43.74  ? 224  ILE A CD1 1 
ATOM   1765  N  N   . GLU A 1 225  ? 99.306  101.064 139.843 1.00 44.92  ? 225  GLU A N   1 
ATOM   1766  C  CA  . GLU A 1 225  ? 99.836  99.724  139.752 1.00 45.89  ? 225  GLU A CA  1 
ATOM   1767  C  C   . GLU A 1 225  ? 99.813  99.263  138.309 1.00 45.97  ? 225  GLU A C   1 
ATOM   1768  O  O   . GLU A 1 225  ? 98.791  99.390  137.648 1.00 45.96  ? 225  GLU A O   1 
ATOM   1769  C  CB  . GLU A 1 225  ? 99.006  98.806  140.631 1.00 45.99  ? 225  GLU A CB  1 
ATOM   1770  C  CG  . GLU A 1 225  ? 99.667  97.491  140.953 1.00 48.53  ? 225  GLU A CG  1 
ATOM   1771  C  CD  . GLU A 1 225  ? 98.897  96.703  142.002 1.00 52.33  ? 225  GLU A CD  1 
ATOM   1772  O  OE1 . GLU A 1 225  ? 98.111  97.329  142.780 1.00 51.74  ? 225  GLU A OE1 1 
ATOM   1773  O  OE2 . GLU A 1 225  ? 99.088  95.453  142.036 1.00 53.34  ? 225  GLU A OE2 1 
ATOM   1774  N  N   . ALA A 1 226  ? 100.940 98.737  137.826 1.00 46.74  ? 226  ALA A N   1 
ATOM   1775  C  CA  . ALA A 1 226  ? 101.061 98.257  136.446 1.00 47.31  ? 226  ALA A CA  1 
ATOM   1776  C  C   . ALA A 1 226  ? 101.673 96.852  136.364 1.00 48.20  ? 226  ALA A C   1 
ATOM   1777  O  O   . ALA A 1 226  ? 102.790 96.635  136.816 1.00 48.35  ? 226  ALA A O   1 
ATOM   1778  C  CB  . ALA A 1 226  ? 101.865 99.232  135.632 1.00 47.13  ? 226  ALA A CB  1 
ATOM   1779  N  N   . ASN A 1 227  ? 100.936 95.905  135.786 1.00 49.44  ? 227  ASN A N   1 
ATOM   1780  C  CA  . ASN A 1 227  ? 101.387 94.509  135.684 1.00 51.19  ? 227  ASN A CA  1 
ATOM   1781  C  C   . ASN A 1 227  ? 101.096 93.848  134.331 1.00 52.00  ? 227  ASN A C   1 
ATOM   1782  O  O   . ASN A 1 227  ? 100.067 94.138  133.717 1.00 51.76  ? 227  ASN A O   1 
ATOM   1783  C  CB  . ASN A 1 227  ? 100.728 93.663  136.770 1.00 51.39  ? 227  ASN A CB  1 
ATOM   1784  C  CG  . ASN A 1 227  ? 101.218 93.996  138.149 1.00 52.80  ? 227  ASN A CG  1 
ATOM   1785  O  OD1 . ASN A 1 227  ? 102.170 93.394  138.637 1.00 54.37  ? 227  ASN A OD1 1 
ATOM   1786  N  ND2 . ASN A 1 227  ? 100.573 94.963  138.794 1.00 55.03  ? 227  ASN A ND2 1 
ATOM   1787  N  N   . TYR A 1 228  ? 101.985 92.953  133.887 1.00 53.47  ? 228  TYR A N   1 
ATOM   1788  C  CA  . TYR A 1 228  ? 101.673 92.040  132.776 1.00 55.33  ? 228  TYR A CA  1 
ATOM   1789  C  C   . TYR A 1 228  ? 100.768 90.923  133.312 1.00 56.83  ? 228  TYR A C   1 
ATOM   1790  O  O   . TYR A 1 228  ? 100.683 90.733  134.522 1.00 57.26  ? 228  TYR A O   1 
ATOM   1791  C  CB  . TYR A 1 228  ? 102.940 91.464  132.124 1.00 55.18  ? 228  TYR A CB  1 
ATOM   1792  C  CG  . TYR A 1 228  ? 104.000 92.494  131.794 1.00 55.60  ? 228  TYR A CG  1 
ATOM   1793  C  CD1 . TYR A 1 228  ? 105.087 92.689  132.643 1.00 56.73  ? 228  TYR A CD1 1 
ATOM   1794  C  CD2 . TYR A 1 228  ? 103.917 93.281  130.641 1.00 55.47  ? 228  TYR A CD2 1 
ATOM   1795  C  CE1 . TYR A 1 228  ? 106.075 93.646  132.368 1.00 56.60  ? 228  TYR A CE1 1 
ATOM   1796  C  CE2 . TYR A 1 228  ? 104.897 94.244  130.350 1.00 55.86  ? 228  TYR A CE2 1 
ATOM   1797  C  CZ  . TYR A 1 228  ? 105.976 94.419  131.225 1.00 56.67  ? 228  TYR A CZ  1 
ATOM   1798  O  OH  . TYR A 1 228  ? 106.962 95.359  130.970 1.00 55.97  ? 228  TYR A OH  1 
ATOM   1799  N  N   . HIS A 1 229  ? 100.086 90.197  132.428 1.00 58.95  ? 229  HIS A N   1 
ATOM   1800  C  CA  . HIS A 1 229  ? 99.071  89.216  132.848 1.00 61.18  ? 229  HIS A CA  1 
ATOM   1801  C  C   . HIS A 1 229  ? 99.627  88.060  133.679 1.00 62.04  ? 229  HIS A C   1 
ATOM   1802  O  O   . HIS A 1 229  ? 99.062  87.719  134.721 1.00 62.24  ? 229  HIS A O   1 
ATOM   1803  C  CB  . HIS A 1 229  ? 98.269  88.709  131.650 1.00 61.79  ? 229  HIS A CB  1 
ATOM   1804  C  CG  . HIS A 1 229  ? 97.424  89.770  131.001 1.00 65.23  ? 229  HIS A CG  1 
ATOM   1805  N  ND1 . HIS A 1 229  ? 97.956  90.768  130.204 1.00 67.08  ? 229  HIS A ND1 1 
ATOM   1806  C  CD2 . HIS A 1 229  ? 96.085  89.991  131.036 1.00 67.46  ? 229  HIS A CD2 1 
ATOM   1807  C  CE1 . HIS A 1 229  ? 96.982  91.554  129.776 1.00 68.25  ? 229  HIS A CE1 1 
ATOM   1808  N  NE2 . HIS A 1 229  ? 95.837  91.105  130.265 1.00 69.24  ? 229  HIS A NE2 1 
ATOM   1809  N  N   . PHE A 1 230  ? 100.738 87.479  133.228 1.00 63.07  ? 230  PHE A N   1 
ATOM   1810  C  CA  . PHE A 1 230  ? 101.476 86.478  134.003 1.00 63.88  ? 230  PHE A CA  1 
ATOM   1811  C  C   . PHE A 1 230  ? 101.638 86.972  135.445 1.00 63.53  ? 230  PHE A C   1 
ATOM   1812  O  O   . PHE A 1 230  ? 101.287 86.251  136.388 1.00 64.42  ? 230  PHE A O   1 
ATOM   1813  C  CB  . PHE A 1 230  ? 102.846 86.200  133.355 1.00 64.79  ? 230  PHE A CB  1 
ATOM   1814  C  CG  . PHE A 1 230  ? 103.380 84.785  133.579 1.00 68.05  ? 230  PHE A CG  1 
ATOM   1815  C  CD1 . PHE A 1 230  ? 102.666 83.657  133.128 1.00 70.60  ? 230  PHE A CD1 1 
ATOM   1816  C  CD2 . PHE A 1 230  ? 104.630 84.581  134.199 1.00 70.79  ? 230  PHE A CD2 1 
ATOM   1817  C  CE1 . PHE A 1 230  ? 103.175 82.341  133.319 1.00 71.94  ? 230  PHE A CE1 1 
ATOM   1818  C  CE2 . PHE A 1 230  ? 105.153 83.268  134.395 1.00 71.86  ? 230  PHE A CE2 1 
ATOM   1819  C  CZ  . PHE A 1 230  ? 104.420 82.150  133.956 1.00 72.10  ? 230  PHE A CZ  1 
ATOM   1820  N  N   . GLY A 1 231  ? 102.150 88.196  135.620 1.00 62.40  ? 231  GLY A N   1 
ATOM   1821  C  CA  . GLY A 1 231  ? 102.240 88.805  136.958 1.00 60.51  ? 231  GLY A CA  1 
ATOM   1822  C  C   . GLY A 1 231  ? 103.372 89.803  137.197 1.00 59.35  ? 231  GLY A C   1 
ATOM   1823  O  O   . GLY A 1 231  ? 103.285 90.635  138.118 1.00 59.50  ? 231  GLY A O   1 
ATOM   1824  N  N   . LYS A 1 232  ? 104.430 89.728  136.380 1.00 57.42  ? 232  LYS A N   1 
ATOM   1825  C  CA  . LYS A 1 232  ? 105.615 90.586  136.550 1.00 55.30  ? 232  LYS A CA  1 
ATOM   1826  C  C   . LYS A 1 232  ? 105.309 92.080  136.417 1.00 53.46  ? 232  LYS A C   1 
ATOM   1827  O  O   . LYS A 1 232  ? 104.604 92.484  135.494 1.00 53.17  ? 232  LYS A O   1 
ATOM   1828  C  CB  . LYS A 1 232  ? 106.715 90.195  135.557 1.00 55.70  ? 232  LYS A CB  1 
ATOM   1829  C  CG  . LYS A 1 232  ? 107.583 89.021  136.007 1.00 54.97  ? 232  LYS A CG  1 
ATOM   1830  C  CD  . LYS A 1 232  ? 108.823 88.904  135.131 1.00 54.36  ? 232  LYS A CD  1 
ATOM   1831  C  CE  . LYS A 1 232  ? 109.429 87.524  135.236 1.00 54.53  ? 232  LYS A CE  1 
ATOM   1832  N  NZ  . LYS A 1 232  ? 109.379 87.060  136.642 1.00 55.55  ? 232  LYS A NZ  1 
ATOM   1833  N  N   . PRO A 1 233  ? 105.831 92.899  137.349 1.00 51.75  ? 233  PRO A N   1 
ATOM   1834  C  CA  . PRO A 1 233  ? 105.675 94.352  137.360 1.00 50.24  ? 233  PRO A CA  1 
ATOM   1835  C  C   . PRO A 1 233  ? 106.214 95.028  136.102 1.00 48.82  ? 233  PRO A C   1 
ATOM   1836  O  O   . PRO A 1 233  ? 107.157 94.517  135.485 1.00 48.96  ? 233  PRO A O   1 
ATOM   1837  C  CB  . PRO A 1 233  ? 106.528 94.782  138.564 1.00 50.69  ? 233  PRO A CB  1 
ATOM   1838  C  CG  . PRO A 1 233  ? 107.441 93.651  138.819 1.00 51.36  ? 233  PRO A CG  1 
ATOM   1839  C  CD  . PRO A 1 233  ? 106.634 92.447  138.496 1.00 52.08  ? 233  PRO A CD  1 
ATOM   1840  N  N   . VAL A 1 234  ? 105.620 96.160  135.727 1.00 46.74  ? 234  VAL A N   1 
ATOM   1841  C  CA  . VAL A 1 234  ? 106.157 96.953  134.632 1.00 45.14  ? 234  VAL A CA  1 
ATOM   1842  C  C   . VAL A 1 234  ? 106.783 98.249  135.118 1.00 44.86  ? 234  VAL A C   1 
ATOM   1843  O  O   . VAL A 1 234  ? 106.296 98.882  136.058 1.00 44.50  ? 234  VAL A O   1 
ATOM   1844  C  CB  . VAL A 1 234  ? 105.173 97.120  133.387 1.00 44.88  ? 234  VAL A CB  1 
ATOM   1845  C  CG1 . VAL A 1 234  ? 103.793 96.569  133.649 1.00 43.89  ? 234  VAL A CG1 1 
ATOM   1846  C  CG2 . VAL A 1 234  ? 105.124 98.538  132.859 1.00 44.18  ? 234  VAL A CG2 1 
ATOM   1847  N  N   . GLN A 1 235  ? 107.902 98.612  134.499 1.00 44.12  ? 235  GLN A N   1 
ATOM   1848  C  CA  . GLN A 1 235  ? 108.535 99.872  134.801 1.00 43.58  ? 235  GLN A CA  1 
ATOM   1849  C  C   . GLN A 1 235  ? 108.142 100.890 133.745 1.00 42.57  ? 235  GLN A C   1 
ATOM   1850  O  O   . GLN A 1 235  ? 108.253 100.632 132.548 1.00 42.32  ? 235  GLN A O   1 
ATOM   1851  C  CB  . GLN A 1 235  ? 110.052 99.729  134.874 1.00 44.04  ? 235  GLN A CB  1 
ATOM   1852  C  CG  . GLN A 1 235  ? 110.765 101.078 134.775 1.00 46.16  ? 235  GLN A CG  1 
ATOM   1853  C  CD  . GLN A 1 235  ? 112.188 101.048 135.262 1.00 48.76  ? 235  GLN A CD  1 
ATOM   1854  O  OE1 . GLN A 1 235  ? 112.630 100.076 135.884 1.00 51.16  ? 235  GLN A OE1 1 
ATOM   1855  N  NE2 . GLN A 1 235  ? 112.918 102.124 135.001 1.00 49.19  ? 235  GLN A NE2 1 
ATOM   1856  N  N   . GLY A 1 236  ? 107.689 102.050 134.193 1.00 41.69  ? 236  GLY A N   1 
ATOM   1857  C  CA  . GLY A 1 236  ? 107.362 103.117 133.274 1.00 40.80  ? 236  GLY A CA  1 
ATOM   1858  C  C   . GLY A 1 236  ? 107.199 104.415 134.007 1.00 40.87  ? 236  GLY A C   1 
ATOM   1859  O  O   . GLY A 1 236  ? 107.447 104.491 135.211 1.00 41.07  ? 236  GLY A O   1 
ATOM   1860  N  N   . VAL A 1 237  ? 106.793 105.440 133.269 1.00 40.85  ? 237  VAL A N   1 
ATOM   1861  C  CA  . VAL A 1 237  ? 106.524 106.756 133.835 1.00 41.39  ? 237  VAL A CA  1 
ATOM   1862  C  C   . VAL A 1 237  ? 105.026 106.995 133.757 1.00 41.59  ? 237  VAL A C   1 
ATOM   1863  O  O   . VAL A 1 237  ? 104.437 106.868 132.681 1.00 41.68  ? 237  VAL A O   1 
ATOM   1864  C  CB  . VAL A 1 237  ? 107.279 107.867 133.056 1.00 41.70  ? 237  VAL A CB  1 
ATOM   1865  C  CG1 . VAL A 1 237  ? 106.835 109.261 133.508 1.00 41.27  ? 237  VAL A CG1 1 
ATOM   1866  C  CG2 . VAL A 1 237  ? 108.781 107.696 133.204 1.00 41.00  ? 237  VAL A CG2 1 
ATOM   1867  N  N   . ALA A 1 238  ? 104.413 107.327 134.889 1.00 42.01  ? 238  ALA A N   1 
ATOM   1868  C  CA  . ALA A 1 238  ? 102.973 107.573 134.945 1.00 42.36  ? 238  ALA A CA  1 
ATOM   1869  C  C   . ALA A 1 238  ? 102.660 109.061 135.075 1.00 43.63  ? 238  ALA A C   1 
ATOM   1870  O  O   . ALA A 1 238  ? 103.087 109.708 136.043 1.00 44.30  ? 238  ALA A O   1 
ATOM   1871  C  CB  . ALA A 1 238  ? 102.353 106.803 136.096 1.00 41.93  ? 238  ALA A CB  1 
ATOM   1872  N  N   . LYS A 1 239  ? 101.934 109.602 134.097 1.00 44.42  ? 239  LYS A N   1 
ATOM   1873  C  CA  . LYS A 1 239  ? 101.394 110.961 134.195 1.00 45.98  ? 239  LYS A CA  1 
ATOM   1874  C  C   . LYS A 1 239  ? 99.987  110.919 134.788 1.00 46.02  ? 239  LYS A C   1 
ATOM   1875  O  O   . LYS A 1 239  ? 99.086  110.312 134.223 1.00 45.97  ? 239  LYS A O   1 
ATOM   1876  C  CB  . LYS A 1 239  ? 101.417 111.676 132.834 1.00 46.35  ? 239  LYS A CB  1 
ATOM   1877  C  CG  . LYS A 1 239  ? 102.796 112.291 132.487 1.00 49.58  ? 239  LYS A CG  1 
ATOM   1878  C  CD  . LYS A 1 239  ? 103.008 112.562 130.984 1.00 52.14  ? 239  LYS A CD  1 
ATOM   1879  C  CE  . LYS A 1 239  ? 104.027 113.702 130.769 1.00 53.76  ? 239  LYS A CE  1 
ATOM   1880  N  NZ  . LYS A 1 239  ? 103.997 114.275 129.378 1.00 53.76  ? 239  LYS A NZ  1 
ATOM   1881  N  N   . VAL A 1 240  ? 99.822  111.546 135.947 1.00 46.83  ? 240  VAL A N   1 
ATOM   1882  C  CA  . VAL A 1 240  ? 98.556  111.552 136.670 1.00 47.35  ? 240  VAL A CA  1 
ATOM   1883  C  C   . VAL A 1 240  ? 97.900  112.919 136.545 1.00 48.50  ? 240  VAL A C   1 
ATOM   1884  O  O   . VAL A 1 240  ? 98.522  113.943 136.847 1.00 48.94  ? 240  VAL A O   1 
ATOM   1885  C  CB  . VAL A 1 240  ? 98.759  111.216 138.166 1.00 47.34  ? 240  VAL A CB  1 
ATOM   1886  C  CG1 . VAL A 1 240  ? 97.431  111.132 138.889 1.00 47.20  ? 240  VAL A CG1 1 
ATOM   1887  C  CG2 . VAL A 1 240  ? 99.501  109.906 138.312 1.00 46.89  ? 240  VAL A CG2 1 
ATOM   1888  N  N   . GLU A 1 241  ? 96.651  112.926 136.077 1.00 49.22  ? 241  GLU A N   1 
ATOM   1889  C  CA  . GLU A 1 241  ? 95.855  114.150 135.999 1.00 50.48  ? 241  GLU A CA  1 
ATOM   1890  C  C   . GLU A 1 241  ? 94.572  114.015 136.803 1.00 50.83  ? 241  GLU A C   1 
ATOM   1891  O  O   . GLU A 1 241  ? 93.940  112.955 136.840 1.00 50.92  ? 241  GLU A O   1 
ATOM   1892  C  CB  . GLU A 1 241  ? 95.522  114.512 134.554 1.00 50.45  ? 241  GLU A CB  1 
ATOM   1893  C  CG  . GLU A 1 241  ? 96.727  114.835 133.704 1.00 52.73  ? 241  GLU A CG  1 
ATOM   1894  C  CD  . GLU A 1 241  ? 96.362  115.463 132.374 1.00 55.16  ? 241  GLU A CD  1 
ATOM   1895  O  OE1 . GLU A 1 241  ? 95.647  114.827 131.580 1.00 55.93  ? 241  GLU A OE1 1 
ATOM   1896  O  OE2 . GLU A 1 241  ? 96.806  116.597 132.113 1.00 58.13  ? 241  GLU A OE2 1 
ATOM   1897  N  N   . LEU A 1 242  ? 94.190  115.106 137.442 1.00 51.68  ? 242  LEU A N   1 
ATOM   1898  C  CA  . LEU A 1 242  ? 93.007  115.144 138.269 1.00 52.18  ? 242  LEU A CA  1 
ATOM   1899  C  C   . LEU A 1 242  ? 92.272  116.417 137.902 1.00 53.00  ? 242  LEU A C   1 
ATOM   1900  O  O   . LEU A 1 242  ? 92.875  117.479 137.861 1.00 53.47  ? 242  LEU A O   1 
ATOM   1901  C  CB  . LEU A 1 242  ? 93.438  115.141 139.721 1.00 52.25  ? 242  LEU A CB  1 
ATOM   1902  C  CG  . LEU A 1 242  ? 92.378  114.880 140.766 1.00 52.97  ? 242  LEU A CG  1 
ATOM   1903  C  CD1 . LEU A 1 242  ? 92.902  113.920 141.806 1.00 53.16  ? 242  LEU A CD1 1 
ATOM   1904  C  CD2 . LEU A 1 242  ? 92.011  116.211 141.382 1.00 55.72  ? 242  LEU A CD2 1 
ATOM   1905  N  N   . TYR A 1 243  ? 90.985  116.313 137.598 1.00 53.86  ? 243  TYR A N   1 
ATOM   1906  C  CA  . TYR A 1 243  ? 90.272  117.438 136.995 1.00 55.24  ? 243  TYR A CA  1 
ATOM   1907  C  C   . TYR A 1 243  ? 89.236  118.047 137.914 1.00 56.83  ? 243  TYR A C   1 
ATOM   1908  O  O   . TYR A 1 243  ? 88.320  117.363 138.377 1.00 56.84  ? 243  TYR A O   1 
ATOM   1909  C  CB  . TYR A 1 243  ? 89.612  117.027 135.672 1.00 54.81  ? 243  TYR A CB  1 
ATOM   1910  C  CG  . TYR A 1 243  ? 90.557  116.390 134.681 1.00 53.81  ? 243  TYR A CG  1 
ATOM   1911  C  CD1 . TYR A 1 243  ? 90.769  115.019 134.685 1.00 53.00  ? 243  TYR A CD1 1 
ATOM   1912  C  CD2 . TYR A 1 243  ? 91.243  117.156 133.750 1.00 53.84  ? 243  TYR A CD2 1 
ATOM   1913  C  CE1 . TYR A 1 243  ? 91.638  114.429 133.798 1.00 52.31  ? 243  TYR A CE1 1 
ATOM   1914  C  CE2 . TYR A 1 243  ? 92.122  116.568 132.847 1.00 53.08  ? 243  TYR A CE2 1 
ATOM   1915  C  CZ  . TYR A 1 243  ? 92.311  115.203 132.881 1.00 52.48  ? 243  TYR A CZ  1 
ATOM   1916  O  OH  . TYR A 1 243  ? 93.170  114.590 131.995 1.00 53.06  ? 243  TYR A OH  1 
ATOM   1917  N  N   . LEU A 1 244  ? 89.387  119.343 138.171 1.00 58.88  ? 244  LEU A N   1 
ATOM   1918  C  CA  . LEU A 1 244  ? 88.377  120.115 138.885 1.00 60.82  ? 244  LEU A CA  1 
ATOM   1919  C  C   . LEU A 1 244  ? 87.743  121.082 137.895 1.00 62.59  ? 244  LEU A C   1 
ATOM   1920  O  O   . LEU A 1 244  ? 88.357  122.070 137.505 1.00 63.06  ? 244  LEU A O   1 
ATOM   1921  C  CB  . LEU A 1 244  ? 89.001  120.840 140.070 1.00 60.84  ? 244  LEU A CB  1 
ATOM   1922  C  CG  . LEU A 1 244  ? 89.584  119.896 141.117 1.00 60.25  ? 244  LEU A CG  1 
ATOM   1923  C  CD1 . LEU A 1 244  ? 90.619  120.591 141.977 1.00 60.34  ? 244  LEU A CD1 1 
ATOM   1924  C  CD2 . LEU A 1 244  ? 88.471  119.303 141.965 1.00 60.76  ? 244  LEU A CD2 1 
ATOM   1925  N  N   . ASP A 1 245  ? 86.518  120.772 137.479 1.00 64.62  ? 245  ASP A N   1 
ATOM   1926  C  CA  . ASP A 1 245  ? 85.894  121.415 136.310 1.00 66.76  ? 245  ASP A CA  1 
ATOM   1927  C  C   . ASP A 1 245  ? 85.060  122.623 136.660 1.00 68.52  ? 245  ASP A C   1 
ATOM   1928  O  O   . ASP A 1 245  ? 84.901  123.535 135.845 1.00 69.00  ? 245  ASP A O   1 
ATOM   1929  C  CB  . ASP A 1 245  ? 85.029  120.417 135.546 1.00 66.28  ? 245  ASP A CB  1 
ATOM   1930  C  CG  . ASP A 1 245  ? 85.841  119.318 134.922 1.00 66.13  ? 245  ASP A CG  1 
ATOM   1931  O  OD1 . ASP A 1 245  ? 86.893  119.628 134.315 1.00 66.14  ? 245  ASP A OD1 1 
ATOM   1932  O  OD2 . ASP A 1 245  ? 85.422  118.145 135.039 1.00 66.38  ? 245  ASP A OD2 1 
ATOM   1933  N  N   . ASP A 1 246  ? 84.511  122.602 137.868 1.00 70.40  ? 246  ASP A N   1 
ATOM   1934  C  CA  . ASP A 1 246  ? 83.817  123.753 138.423 1.00 72.73  ? 246  ASP A CA  1 
ATOM   1935  C  C   . ASP A 1 246  ? 84.794  124.942 138.491 1.00 73.58  ? 246  ASP A C   1 
ATOM   1936  O  O   . ASP A 1 246  ? 84.371  126.101 138.433 1.00 74.55  ? 246  ASP A O   1 
ATOM   1937  C  CB  . ASP A 1 246  ? 83.244  123.412 139.814 1.00 73.15  ? 246  ASP A CB  1 
ATOM   1938  C  CG  . ASP A 1 246  ? 82.021  124.266 140.189 1.00 75.75  ? 246  ASP A CG  1 
ATOM   1939  O  OD1 . ASP A 1 246  ? 81.679  125.215 139.437 1.00 77.75  ? 246  ASP A OD1 1 
ATOM   1940  O  OD2 . ASP A 1 246  ? 81.399  123.985 141.246 1.00 77.12  ? 246  ASP A OD2 1 
ATOM   1941  N  N   . ASP A 1 247  ? 86.094  124.640 138.581 1.00 73.63  ? 247  ASP A N   1 
ATOM   1942  C  CA  . ASP A 1 247  ? 87.137  125.665 138.717 1.00 74.35  ? 247  ASP A CA  1 
ATOM   1943  C  C   . ASP A 1 247  ? 88.058  125.750 137.493 1.00 74.16  ? 247  ASP A C   1 
ATOM   1944  O  O   . ASP A 1 247  ? 89.062  126.477 137.512 1.00 74.51  ? 247  ASP A O   1 
ATOM   1945  C  CB  . ASP A 1 247  ? 88.002  125.410 139.966 1.00 74.48  ? 247  ASP A CB  1 
ATOM   1946  C  CG  . ASP A 1 247  ? 87.188  125.119 141.230 1.00 75.27  ? 247  ASP A CG  1 
ATOM   1947  O  OD1 . ASP A 1 247  ? 87.753  124.440 142.117 1.00 75.07  ? 247  ASP A OD1 1 
ATOM   1948  O  OD2 . ASP A 1 247  ? 86.018  125.564 141.357 1.00 76.02  ? 247  ASP A OD2 1 
ATOM   1949  N  N   . LYS A 1 248  ? 87.722  125.004 136.441 1.00 73.68  ? 248  LYS A N   1 
ATOM   1950  C  CA  . LYS A 1 248  ? 88.586  124.846 135.256 1.00 73.36  ? 248  LYS A CA  1 
ATOM   1951  C  C   . LYS A 1 248  ? 90.028  124.411 135.625 1.00 72.52  ? 248  LYS A C   1 
ATOM   1952  O  O   . LYS A 1 248  ? 90.979  124.709 134.897 1.00 72.64  ? 248  LYS A O   1 
ATOM   1953  C  CB  . LYS A 1 248  ? 88.604  126.130 134.395 1.00 74.27  ? 248  LYS A CB  1 
ATOM   1954  C  CG  . LYS A 1 248  ? 87.235  126.786 134.104 1.00 75.75  ? 248  LYS A CG  1 
ATOM   1955  C  CD  . LYS A 1 248  ? 86.625  126.355 132.757 1.00 77.51  ? 248  LYS A CD  1 
ATOM   1956  C  CE  . LYS A 1 248  ? 85.526  125.293 132.935 1.00 78.35  ? 248  LYS A CE  1 
ATOM   1957  N  NZ  . LYS A 1 248  ? 84.792  124.989 131.664 1.00 78.01  ? 248  LYS A NZ  1 
ATOM   1958  N  N   . LEU A 1 249  ? 90.175  123.705 136.749 1.00 71.41  ? 249  LEU A N   1 
ATOM   1959  C  CA  . LEU A 1 249  ? 91.488  123.298 137.265 1.00 70.52  ? 249  LEU A CA  1 
ATOM   1960  C  C   . LEU A 1 249  ? 91.936  121.917 136.789 1.00 69.13  ? 249  LEU A C   1 
ATOM   1961  O  O   . LEU A 1 249  ? 91.123  121.072 136.402 1.00 68.79  ? 249  LEU A O   1 
ATOM   1962  C  CB  . LEU A 1 249  ? 91.515  123.336 138.801 1.00 70.81  ? 249  LEU A CB  1 
ATOM   1963  C  CG  . LEU A 1 249  ? 91.537  124.682 139.538 1.00 72.08  ? 249  LEU A CG  1 
ATOM   1964  C  CD1 . LEU A 1 249  ? 91.334  124.466 141.043 1.00 72.97  ? 249  LEU A CD1 1 
ATOM   1965  C  CD2 . LEU A 1 249  ? 92.823  125.464 139.273 1.00 72.93  ? 249  LEU A CD2 1 
ATOM   1966  N  N   . LYS A 1 250  ? 93.246  121.702 136.843 1.00 68.02  ? 250  LYS A N   1 
ATOM   1967  C  CA  . LYS A 1 250  ? 93.865  120.448 136.446 1.00 66.46  ? 250  LYS A CA  1 
ATOM   1968  C  C   . LYS A 1 250  ? 95.141  120.256 137.271 1.00 65.46  ? 250  LYS A C   1 
ATOM   1969  O  O   . LYS A 1 250  ? 96.111  120.994 137.087 1.00 65.85  ? 250  LYS A O   1 
ATOM   1970  C  CB  . LYS A 1 250  ? 94.186  120.483 134.945 1.00 66.56  ? 250  LYS A CB  1 
ATOM   1971  C  CG  . LYS A 1 250  ? 94.503  119.133 134.311 1.00 66.93  ? 250  LYS A CG  1 
ATOM   1972  C  CD  . LYS A 1 250  ? 95.381  119.295 133.051 1.00 69.30  ? 250  LYS A CD  1 
ATOM   1973  C  CE  . LYS A 1 250  ? 94.595  119.239 131.729 1.00 70.96  ? 250  LYS A CE  1 
ATOM   1974  N  NZ  . LYS A 1 250  ? 93.719  120.428 131.470 1.00 72.14  ? 250  LYS A NZ  1 
ATOM   1975  N  N   . LEU A 1 251  ? 95.129  119.294 138.196 1.00 63.55  ? 251  LEU A N   1 
ATOM   1976  C  CA  . LEU A 1 251  ? 96.340  118.913 138.926 1.00 62.11  ? 251  LEU A CA  1 
ATOM   1977  C  C   . LEU A 1 251  ? 97.108  117.834 138.161 1.00 60.69  ? 251  LEU A C   1 
ATOM   1978  O  O   . LEU A 1 251  ? 96.516  116.872 137.675 1.00 60.01  ? 251  LEU A O   1 
ATOM   1979  C  CB  . LEU A 1 251  ? 96.018  118.413 140.335 1.00 62.12  ? 251  LEU A CB  1 
ATOM   1980  C  CG  . LEU A 1 251  ? 95.064  119.158 141.277 1.00 62.48  ? 251  LEU A CG  1 
ATOM   1981  C  CD1 . LEU A 1 251  ? 95.229  118.602 142.668 1.00 62.90  ? 251  LEU A CD1 1 
ATOM   1982  C  CD2 . LEU A 1 251  ? 95.271  120.662 141.299 1.00 63.37  ? 251  LEU A CD2 1 
ATOM   1983  N  N   . LYS A 1 252  ? 98.424  118.008 138.051 1.00 59.71  ? 252  LYS A N   1 
ATOM   1984  C  CA  . LYS A 1 252  ? 99.284  117.071 137.328 1.00 58.36  ? 252  LYS A CA  1 
ATOM   1985  C  C   . LYS A 1 252  ? 100.433 116.584 138.200 1.00 57.22  ? 252  LYS A C   1 
ATOM   1986  O  O   . LYS A 1 252  ? 101.004 117.359 138.957 1.00 57.52  ? 252  LYS A O   1 
ATOM   1987  C  CB  . LYS A 1 252  ? 99.899  117.743 136.098 1.00 58.94  ? 252  LYS A CB  1 
ATOM   1988  C  CG  . LYS A 1 252  ? 98.946  118.206 135.009 1.00 60.53  ? 252  LYS A CG  1 
ATOM   1989  C  CD  . LYS A 1 252  ? 99.712  119.066 133.993 1.00 64.43  ? 252  LYS A CD  1 
ATOM   1990  C  CE  . LYS A 1 252  ? 99.127  118.953 132.584 1.00 66.92  ? 252  LYS A CE  1 
ATOM   1991  N  NZ  . LYS A 1 252  ? 100.000 119.570 131.524 1.00 68.28  ? 252  LYS A NZ  1 
ATOM   1992  N  N   . LYS A 1 253  ? 100.778 115.305 138.078 1.00 55.52  ? 253  LYS A N   1 
ATOM   1993  C  CA  . LYS A 1 253  ? 102.036 114.775 138.622 1.00 54.53  ? 253  LYS A CA  1 
ATOM   1994  C  C   . LYS A 1 253  ? 102.611 113.644 137.772 1.00 53.10  ? 253  LYS A C   1 
ATOM   1995  O  O   . LYS A 1 253  ? 101.870 112.889 137.159 1.00 52.44  ? 253  LYS A O   1 
ATOM   1996  C  CB  . LYS A 1 253  ? 101.882 114.326 140.073 1.00 54.71  ? 253  LYS A CB  1 
ATOM   1997  C  CG  . LYS A 1 253  ? 101.810 115.482 141.050 1.00 56.41  ? 253  LYS A CG  1 
ATOM   1998  C  CD  . LYS A 1 253  ? 102.506 115.171 142.356 1.00 58.55  ? 253  LYS A CD  1 
ATOM   1999  C  CE  . LYS A 1 253  ? 102.469 116.378 143.262 1.00 60.00  ? 253  LYS A CE  1 
ATOM   2000  N  NZ  . LYS A 1 253  ? 102.653 115.966 144.679 1.00 62.55  ? 253  LYS A NZ  1 
ATOM   2001  N  N   . GLU A 1 254  ? 103.936 113.551 137.725 1.00 52.51  ? 254  GLU A N   1 
ATOM   2002  C  CA  . GLU A 1 254  ? 104.622 112.460 137.038 1.00 51.42  ? 254  GLU A CA  1 
ATOM   2003  C  C   . GLU A 1 254  ? 105.486 111.717 138.017 1.00 50.33  ? 254  GLU A C   1 
ATOM   2004  O  O   . GLU A 1 254  ? 106.043 112.316 138.931 1.00 50.75  ? 254  GLU A O   1 
ATOM   2005  C  CB  . GLU A 1 254  ? 105.545 112.973 135.953 1.00 52.03  ? 254  GLU A CB  1 
ATOM   2006  C  CG  . GLU A 1 254  ? 104.947 113.916 134.952 1.00 55.26  ? 254  GLU A CG  1 
ATOM   2007  C  CD  . GLU A 1 254  ? 105.971 114.284 133.900 1.00 60.20  ? 254  GLU A CD  1 
ATOM   2008  O  OE1 . GLU A 1 254  ? 106.291 113.409 133.056 1.00 60.81  ? 254  GLU A OE1 1 
ATOM   2009  O  OE2 . GLU A 1 254  ? 106.478 115.435 133.939 1.00 62.68  ? 254  GLU A OE2 1 
ATOM   2010  N  N   . LEU A 1 255  ? 105.617 110.412 137.817 1.00 48.50  ? 255  LEU A N   1 
ATOM   2011  C  CA  . LEU A 1 255  ? 106.505 109.619 138.646 1.00 47.13  ? 255  LEU A CA  1 
ATOM   2012  C  C   . LEU A 1 255  ? 106.893 108.367 137.913 1.00 45.85  ? 255  LEU A C   1 
ATOM   2013  O  O   . LEU A 1 255  ? 106.131 107.863 137.096 1.00 45.61  ? 255  LEU A O   1 
ATOM   2014  C  CB  . LEU A 1 255  ? 105.872 109.276 140.008 1.00 47.09  ? 255  LEU A CB  1 
ATOM   2015  C  CG  . LEU A 1 255  ? 104.701 108.292 140.115 1.00 46.47  ? 255  LEU A CG  1 
ATOM   2016  C  CD1 . LEU A 1 255  ? 104.670 107.643 141.475 1.00 46.08  ? 255  LEU A CD1 1 
ATOM   2017  C  CD2 . LEU A 1 255  ? 103.369 108.962 139.832 1.00 47.03  ? 255  LEU A CD2 1 
ATOM   2018  N  N   . THR A 1 256  ? 108.100 107.885 138.194 1.00 45.00  ? 256  THR A N   1 
ATOM   2019  C  CA  . THR A 1 256  ? 108.523 106.571 137.749 1.00 43.24  ? 256  THR A CA  1 
ATOM   2020  C  C   . THR A 1 256  ? 107.881 105.545 138.666 1.00 42.24  ? 256  THR A C   1 
ATOM   2021  O  O   . THR A 1 256  ? 107.892 105.682 139.884 1.00 42.30  ? 256  THR A O   1 
ATOM   2022  C  CB  . THR A 1 256  ? 110.051 106.443 137.743 1.00 43.55  ? 256  THR A CB  1 
ATOM   2023  O  OG1 . THR A 1 256  ? 110.596 107.544 137.012 1.00 44.00  ? 256  THR A OG1 1 
ATOM   2024  C  CG2 . THR A 1 256  ? 110.498 105.139 137.073 1.00 42.64  ? 256  THR A CG2 1 
ATOM   2025  N  N   . VAL A 1 257  ? 107.281 104.536 138.063 1.00 41.01  ? 257  VAL A N   1 
ATOM   2026  C  CA  . VAL A 1 257  ? 106.624 103.489 138.811 1.00 40.21  ? 257  VAL A CA  1 
ATOM   2027  C  C   . VAL A 1 257  ? 107.315 102.198 138.454 1.00 40.02  ? 257  VAL A C   1 
ATOM   2028  O  O   . VAL A 1 257  ? 107.452 101.860 137.276 1.00 40.24  ? 257  VAL A O   1 
ATOM   2029  C  CB  . VAL A 1 257  ? 105.105 103.414 138.484 1.00 39.57  ? 257  VAL A CB  1 
ATOM   2030  C  CG1 . VAL A 1 257  ? 104.455 102.207 139.138 1.00 38.98  ? 257  VAL A CG1 1 
ATOM   2031  C  CG2 . VAL A 1 257  ? 104.405 104.694 138.901 1.00 38.66  ? 257  VAL A CG2 1 
ATOM   2032  N  N   . TYR A 1 258  ? 107.772 101.501 139.482 1.00 39.97  ? 258  TYR A N   1 
ATOM   2033  C  CA  . TYR A 1 258  ? 108.360 100.196 139.334 1.00 39.79  ? 258  TYR A CA  1 
ATOM   2034  C  C   . TYR A 1 258  ? 107.315 99.205  139.787 1.00 39.38  ? 258  TYR A C   1 
ATOM   2035  O  O   . TYR A 1 258  ? 107.323 98.757  140.928 1.00 39.97  ? 258  TYR A O   1 
ATOM   2036  C  CB  . TYR A 1 258  ? 109.630 100.094 140.175 1.00 40.46  ? 258  TYR A CB  1 
ATOM   2037  C  CG  . TYR A 1 258  ? 110.666 101.141 139.816 1.00 41.24  ? 258  TYR A CG  1 
ATOM   2038  C  CD1 . TYR A 1 258  ? 110.671 102.394 140.442 1.00 40.79  ? 258  TYR A CD1 1 
ATOM   2039  C  CD2 . TYR A 1 258  ? 111.636 100.882 138.849 1.00 41.66  ? 258  TYR A CD2 1 
ATOM   2040  C  CE1 . TYR A 1 258  ? 111.605 103.349 140.117 1.00 41.98  ? 258  TYR A CE1 1 
ATOM   2041  C  CE2 . TYR A 1 258  ? 112.587 101.839 138.514 1.00 42.16  ? 258  TYR A CE2 1 
ATOM   2042  C  CZ  . TYR A 1 258  ? 112.574 103.068 139.151 1.00 43.64  ? 258  TYR A CZ  1 
ATOM   2043  O  OH  . TYR A 1 258  ? 113.523 104.023 138.809 1.00 44.60  ? 258  TYR A OH  1 
ATOM   2044  N  N   . GLY A 1 259  ? 106.389 98.886  138.894 1.00 39.05  ? 259  GLY A N   1 
ATOM   2045  C  CA  . GLY A 1 259  ? 105.273 97.998  139.222 1.00 38.69  ? 259  GLY A CA  1 
ATOM   2046  C  C   . GLY A 1 259  ? 104.194 98.661  140.070 1.00 38.87  ? 259  GLY A C   1 
ATOM   2047  O  O   . GLY A 1 259  ? 103.019 98.601  139.721 1.00 38.98  ? 259  GLY A O   1 
ATOM   2048  N  N   . LYS A 1 260  ? 104.586 99.290  141.183 1.00 38.93  ? 260  LYS A N   1 
ATOM   2049  C  CA  . LYS A 1 260  ? 103.634 99.918  142.115 1.00 38.61  ? 260  LYS A CA  1 
ATOM   2050  C  C   . LYS A 1 260  ? 104.186 101.223 142.667 1.00 38.50  ? 260  LYS A C   1 
ATOM   2051  O  O   . LYS A 1 260  ? 105.338 101.274 143.092 1.00 38.83  ? 260  LYS A O   1 
ATOM   2052  C  CB  . LYS A 1 260  ? 103.339 98.968  143.271 1.00 38.90  ? 260  LYS A CB  1 
ATOM   2053  C  CG  . LYS A 1 260  ? 102.232 99.410  144.188 1.00 39.55  ? 260  LYS A CG  1 
ATOM   2054  C  CD  . LYS A 1 260  ? 102.086 98.404  145.310 1.00 42.33  ? 260  LYS A CD  1 
ATOM   2055  C  CE  . LYS A 1 260  ? 100.703 97.797  145.338 1.00 42.68  ? 260  LYS A CE  1 
ATOM   2056  N  NZ  . LYS A 1 260  ? 100.531 96.968  146.557 1.00 44.44  ? 260  LYS A NZ  1 
ATOM   2057  N  N   . GLY A 1 261  ? 103.362 102.266 142.667 1.00 38.12  ? 261  GLY A N   1 
ATOM   2058  C  CA  . GLY A 1 261  ? 103.777 103.592 143.117 1.00 38.53  ? 261  GLY A CA  1 
ATOM   2059  C  C   . GLY A 1 261  ? 102.696 104.319 143.894 1.00 39.12  ? 261  GLY A C   1 
ATOM   2060  O  O   . GLY A 1 261  ? 101.507 103.976 143.800 1.00 38.90  ? 261  GLY A O   1 
ATOM   2061  N  N   . GLN A 1 262  ? 103.108 105.313 144.677 1.00 39.73  ? 262  GLN A N   1 
ATOM   2062  C  CA  . GLN A 1 262  ? 102.175 106.160 145.410 1.00 40.41  ? 262  GLN A CA  1 
ATOM   2063  C  C   . GLN A 1 262  ? 102.324 107.601 144.941 1.00 41.17  ? 262  GLN A C   1 
ATOM   2064  O  O   . GLN A 1 262  ? 103.419 108.032 144.597 1.00 41.52  ? 262  GLN A O   1 
ATOM   2065  C  CB  . GLN A 1 262  ? 102.430 106.079 146.910 1.00 40.65  ? 262  GLN A CB  1 
ATOM   2066  C  CG  . GLN A 1 262  ? 102.433 104.683 147.491 1.00 41.50  ? 262  GLN A CG  1 
ATOM   2067  C  CD  . GLN A 1 262  ? 101.094 103.976 147.376 1.00 43.57  ? 262  GLN A CD  1 
ATOM   2068  O  OE1 . GLN A 1 262  ? 100.035 104.608 147.391 1.00 45.88  ? 262  GLN A OE1 1 
ATOM   2069  N  NE2 . GLN A 1 262  ? 101.135 102.651 147.278 1.00 42.73  ? 262  GLN A NE2 1 
ATOM   2070  N  N   . VAL A 1 263  ? 101.222 108.339 144.910 1.00 41.70  ? 263  VAL A N   1 
ATOM   2071  C  CA  . VAL A 1 263  ? 101.254 109.731 144.503 1.00 42.80  ? 263  VAL A CA  1 
ATOM   2072  C  C   . VAL A 1 263  ? 100.214 110.515 145.289 1.00 43.94  ? 263  VAL A C   1 
ATOM   2073  O  O   . VAL A 1 263  ? 99.064  110.096 145.403 1.00 43.99  ? 263  VAL A O   1 
ATOM   2074  C  CB  . VAL A 1 263  ? 101.062 109.909 142.967 1.00 42.41  ? 263  VAL A CB  1 
ATOM   2075  C  CG1 . VAL A 1 263  ? 99.674  109.482 142.514 1.00 41.66  ? 263  VAL A CG1 1 
ATOM   2076  C  CG2 . VAL A 1 263  ? 101.314 111.352 142.552 1.00 43.45  ? 263  VAL A CG2 1 
ATOM   2077  N  N   . GLU A 1 264  ? 100.639 111.639 145.854 1.00 45.59  ? 264  GLU A N   1 
ATOM   2078  C  CA  . GLU A 1 264  ? 99.755  112.524 146.592 1.00 47.00  ? 264  GLU A CA  1 
ATOM   2079  C  C   . GLU A 1 264  ? 99.469  113.769 145.765 1.00 47.47  ? 264  GLU A C   1 
ATOM   2080  O  O   . GLU A 1 264  ? 100.388 114.443 145.295 1.00 47.84  ? 264  GLU A O   1 
ATOM   2081  C  CB  . GLU A 1 264  ? 100.366 112.896 147.949 1.00 47.80  ? 264  GLU A CB  1 
ATOM   2082  C  CG  . GLU A 1 264  ? 99.579  113.960 148.721 1.00 50.60  ? 264  GLU A CG  1 
ATOM   2083  C  CD  . GLU A 1 264  ? 99.817  113.944 150.232 1.00 53.75  ? 264  GLU A CD  1 
ATOM   2084  O  OE1 . GLU A 1 264  ? 99.160  114.733 150.938 1.00 54.18  ? 264  GLU A OE1 1 
ATOM   2085  O  OE2 . GLU A 1 264  ? 100.652 113.152 150.722 1.00 55.95  ? 264  GLU A OE2 1 
ATOM   2086  N  N   . LEU A 1 265  ? 98.187  114.056 145.571 1.00 48.04  ? 265  LEU A N   1 
ATOM   2087  C  CA  . LEU A 1 265  ? 97.768  115.275 144.893 1.00 48.80  ? 265  LEU A CA  1 
ATOM   2088  C  C   . LEU A 1 265  ? 97.052  116.157 145.903 1.00 50.24  ? 265  LEU A C   1 
ATOM   2089  O  O   . LEU A 1 265  ? 96.080  115.730 146.526 1.00 50.26  ? 265  LEU A O   1 
ATOM   2090  C  CB  . LEU A 1 265  ? 96.868  114.940 143.710 1.00 47.69  ? 265  LEU A CB  1 
ATOM   2091  C  CG  . LEU A 1 265  ? 97.607  114.229 142.582 1.00 46.57  ? 265  LEU A CG  1 
ATOM   2092  C  CD1 . LEU A 1 265  ? 96.805  113.078 142.037 1.00 44.84  ? 265  LEU A CD1 1 
ATOM   2093  C  CD2 . LEU A 1 265  ? 97.976  115.213 141.485 1.00 47.53  ? 265  LEU A CD2 1 
ATOM   2094  N  N   . ARG A 1 266  ? 97.550  117.377 146.073 1.00 52.02  ? 266  ARG A N   1 
ATOM   2095  C  CA  . ARG A 1 266  ? 97.043  118.292 147.093 1.00 53.99  ? 266  ARG A CA  1 
ATOM   2096  C  C   . ARG A 1 266  ? 96.092  119.336 146.524 1.00 54.90  ? 266  ARG A C   1 
ATOM   2097  O  O   . ARG A 1 266  ? 96.412  120.019 145.550 1.00 54.88  ? 266  ARG A O   1 
ATOM   2098  C  CB  . ARG A 1 266  ? 98.201  118.968 147.824 1.00 54.62  ? 266  ARG A CB  1 
ATOM   2099  C  CG  . ARG A 1 266  ? 99.034  118.001 148.640 1.00 56.02  ? 266  ARG A CG  1 
ATOM   2100  C  CD  . ARG A 1 266  ? 100.141 118.714 149.393 1.00 59.56  ? 266  ARG A CD  1 
ATOM   2101  N  NE  . ARG A 1 266  ? 100.754 117.838 150.390 1.00 62.29  ? 266  ARG A NE  1 
ATOM   2102  C  CZ  . ARG A 1 266  ? 100.293 117.662 151.630 1.00 64.45  ? 266  ARG A CZ  1 
ATOM   2103  N  NH1 . ARG A 1 266  ? 99.196  118.293 152.052 1.00 64.29  ? 266  ARG A NH1 1 
ATOM   2104  N  NH2 . ARG A 1 266  ? 100.927 116.838 152.457 1.00 65.86  ? 266  ARG A NH2 1 
ATOM   2105  N  N   . PHE A 1 267  ? 94.917  119.441 147.135 1.00 56.24  ? 267  PHE A N   1 
ATOM   2106  C  CA  . PHE A 1 267  ? 93.928  120.425 146.728 1.00 57.88  ? 267  PHE A CA  1 
ATOM   2107  C  C   . PHE A 1 267  ? 94.263  121.780 147.323 1.00 59.60  ? 267  PHE A C   1 
ATOM   2108  O  O   . PHE A 1 267  ? 95.012  121.869 148.297 1.00 59.91  ? 267  PHE A O   1 
ATOM   2109  C  CB  . PHE A 1 267  ? 92.524  120.004 147.177 1.00 57.82  ? 267  PHE A CB  1 
ATOM   2110  C  CG  . PHE A 1 267  ? 91.995  118.773 146.484 1.00 57.74  ? 267  PHE A CG  1 
ATOM   2111  C  CD1 . PHE A 1 267  ? 91.477  117.713 147.226 1.00 57.71  ? 267  PHE A CD1 1 
ATOM   2112  C  CD2 . PHE A 1 267  ? 92.005  118.674 145.092 1.00 58.02  ? 267  PHE A CD2 1 
ATOM   2113  C  CE1 . PHE A 1 267  ? 90.981  116.575 146.602 1.00 56.82  ? 267  PHE A CE1 1 
ATOM   2114  C  CE2 . PHE A 1 267  ? 91.510  117.535 144.457 1.00 57.86  ? 267  PHE A CE2 1 
ATOM   2115  C  CZ  . PHE A 1 267  ? 91.001  116.480 145.218 1.00 57.07  ? 267  PHE A CZ  1 
ATOM   2116  N  N   . ASP A 1 268  ? 93.698  122.829 146.732 1.00 61.39  ? 268  ASP A N   1 
ATOM   2117  C  CA  . ASP A 1 268  ? 93.831  124.185 147.252 1.00 63.57  ? 268  ASP A CA  1 
ATOM   2118  C  C   . ASP A 1 268  ? 92.775  124.451 148.310 1.00 64.61  ? 268  ASP A C   1 
ATOM   2119  O  O   . ASP A 1 268  ? 92.876  123.967 149.448 1.00 64.96  ? 268  ASP A O   1 
ATOM   2120  C  CB  . ASP A 1 268  ? 93.694  125.205 146.126 1.00 64.12  ? 268  ASP A CB  1 
ATOM   2121  C  CG  . ASP A 1 268  ? 94.461  126.486 146.400 1.00 66.38  ? 268  ASP A CG  1 
ATOM   2122  O  OD1 . ASP A 1 268  ? 94.324  127.052 147.514 1.00 68.77  ? 268  ASP A OD1 1 
ATOM   2123  O  OD2 . ASP A 1 268  ? 95.199  126.929 145.491 1.00 67.17  ? 268  ASP A OD2 1 
ATOM   2124  N  N   . ASN A 1 269  ? 91.765  125.236 147.946 1.00 65.55  ? 269  ASN A N   1 
ATOM   2125  C  CA  . ASN A 1 269  ? 90.665  125.499 148.875 1.00 66.57  ? 269  ASN A CA  1 
ATOM   2126  C  C   . ASN A 1 269  ? 89.488  124.595 148.512 1.00 65.54  ? 269  ASN A C   1 
ATOM   2127  O  O   . ASN A 1 269  ? 88.525  125.027 147.860 1.00 65.77  ? 269  ASN A O   1 
ATOM   2128  C  CB  . ASN A 1 269  ? 90.274  126.984 148.882 1.00 67.64  ? 269  ASN A CB  1 
ATOM   2129  C  CG  . ASN A 1 269  ? 89.264  127.318 149.981 1.00 70.56  ? 269  ASN A CG  1 
ATOM   2130  O  OD1 . ASN A 1 269  ? 89.627  127.873 151.026 1.00 73.37  ? 269  ASN A OD1 1 
ATOM   2131  N  ND2 . ASN A 1 269  ? 87.988  126.971 149.754 1.00 71.68  ? 269  ASN A ND2 1 
ATOM   2132  N  N   . PHE A 1 270  ? 89.589  123.332 148.920 1.00 64.37  ? 270  PHE A N   1 
ATOM   2133  C  CA  . PHE A 1 270  ? 88.613  122.326 148.523 1.00 63.08  ? 270  PHE A CA  1 
ATOM   2134  C  C   . PHE A 1 270  ? 87.454  122.260 149.509 1.00 63.07  ? 270  PHE A C   1 
ATOM   2135  O  O   . PHE A 1 270  ? 87.597  121.792 150.644 1.00 63.02  ? 270  PHE A O   1 
ATOM   2136  C  CB  . PHE A 1 270  ? 89.283  120.961 148.363 1.00 62.50  ? 270  PHE A CB  1 
ATOM   2137  C  CG  . PHE A 1 270  ? 88.435  119.947 147.657 1.00 61.10  ? 270  PHE A CG  1 
ATOM   2138  C  CD1 . PHE A 1 270  ? 88.291  119.985 146.275 1.00 60.33  ? 270  PHE A CD1 1 
ATOM   2139  C  CD2 . PHE A 1 270  ? 87.795  118.942 148.373 1.00 60.33  ? 270  PHE A CD2 1 
ATOM   2140  C  CE1 . PHE A 1 270  ? 87.513  119.046 145.612 1.00 59.95  ? 270  PHE A CE1 1 
ATOM   2141  C  CE2 . PHE A 1 270  ? 87.014  117.997 147.725 1.00 60.08  ? 270  PHE A CE2 1 
ATOM   2142  C  CZ  . PHE A 1 270  ? 86.867  118.048 146.340 1.00 59.81  ? 270  PHE A CZ  1 
ATOM   2143  N  N   . ALA A 1 271  ? 86.304  122.748 149.059 1.00 62.70  ? 271  ALA A N   1 
ATOM   2144  C  CA  . ALA A 1 271  ? 85.104  122.767 149.870 1.00 62.55  ? 271  ALA A CA  1 
ATOM   2145  C  C   . ALA A 1 271  ? 83.940  122.243 149.036 1.00 61.80  ? 271  ALA A C   1 
ATOM   2146  O  O   . ALA A 1 271  ? 83.503  122.889 148.086 1.00 61.91  ? 271  ALA A O   1 
ATOM   2147  C  CB  . ALA A 1 271  ? 84.835  124.183 150.391 1.00 63.35  ? 271  ALA A CB  1 
ATOM   2148  N  N   . MET A 1 272  ? 83.462  121.054 149.381 1.00 60.95  ? 272  MET A N   1 
ATOM   2149  C  CA  . MET A 1 272  ? 82.408  120.405 148.614 1.00 60.32  ? 272  MET A CA  1 
ATOM   2150  C  C   . MET A 1 272  ? 81.051  121.033 148.891 1.00 61.09  ? 272  MET A C   1 
ATOM   2151  O  O   . MET A 1 272  ? 80.766  121.459 150.015 1.00 61.74  ? 272  MET A O   1 
ATOM   2152  C  CB  . MET A 1 272  ? 82.355  118.915 148.931 1.00 59.60  ? 272  MET A CB  1 
ATOM   2153  C  CG  . MET A 1 272  ? 83.632  118.178 148.627 1.00 57.75  ? 272  MET A CG  1 
ATOM   2154  S  SD  . MET A 1 272  ? 83.542  116.438 149.039 1.00 55.54  ? 272  MET A SD  1 
ATOM   2155  C  CE  . MET A 1 272  ? 83.341  116.482 150.811 1.00 56.91  ? 272  MET A CE  1 
ATOM   2156  N  N   . ASP A 1 273  ? 80.217  121.088 147.859 1.00 61.02  ? 273  ASP A N   1 
ATOM   2157  C  CA  . ASP A 1 273  ? 78.856  121.590 148.008 1.00 61.56  ? 273  ASP A CA  1 
ATOM   2158  C  C   . ASP A 1 273  ? 77.962  120.565 148.707 1.00 60.93  ? 273  ASP A C   1 
ATOM   2159  O  O   . ASP A 1 273  ? 77.076  120.934 149.471 1.00 61.85  ? 273  ASP A O   1 
ATOM   2160  C  CB  . ASP A 1 273  ? 78.283  122.014 146.654 1.00 61.84  ? 273  ASP A CB  1 
ATOM   2161  C  CG  . ASP A 1 273  ? 78.992  123.241 146.080 1.00 63.63  ? 273  ASP A CG  1 
ATOM   2162  O  OD1 . ASP A 1 273  ? 79.007  124.296 146.758 1.00 65.97  ? 273  ASP A OD1 1 
ATOM   2163  O  OD2 . ASP A 1 273  ? 79.538  123.155 144.955 1.00 64.49  ? 273  ASP A OD2 1 
ATOM   2164  N  N   . ALA A 1 274  ? 78.210  119.285 148.453 1.00 59.45  ? 274  ALA A N   1 
ATOM   2165  C  CA  . ALA A 1 274  ? 77.492  118.207 149.121 1.00 58.52  ? 274  ALA A CA  1 
ATOM   2166  C  C   . ALA A 1 274  ? 78.420  117.465 150.084 1.00 57.82  ? 274  ALA A C   1 
ATOM   2167  O  O   . ALA A 1 274  ? 79.513  117.944 150.398 1.00 57.91  ? 274  ALA A O   1 
ATOM   2168  C  CB  . ALA A 1 274  ? 76.897  117.251 148.095 1.00 58.05  ? 274  ALA A CB  1 
ATOM   2169  N  N   . ASP A 1 275  ? 77.978  116.299 150.547 1.00 56.88  ? 275  ASP A N   1 
ATOM   2170  C  CA  . ASP A 1 275  ? 78.764  115.462 151.446 1.00 56.08  ? 275  ASP A CA  1 
ATOM   2171  C  C   . ASP A 1 275  ? 79.755  114.588 150.674 1.00 54.71  ? 275  ASP A C   1 
ATOM   2172  O  O   . ASP A 1 275  ? 80.593  113.907 151.277 1.00 54.62  ? 275  ASP A O   1 
ATOM   2173  C  CB  . ASP A 1 275  ? 77.830  114.580 152.288 1.00 56.49  ? 275  ASP A CB  1 
ATOM   2174  C  CG  . ASP A 1 275  ? 77.208  115.327 153.488 1.00 58.26  ? 275  ASP A CG  1 
ATOM   2175  O  OD1 . ASP A 1 275  ? 76.658  114.633 154.373 1.00 60.79  ? 275  ASP A OD1 1 
ATOM   2176  O  OD2 . ASP A 1 275  ? 77.261  116.582 153.568 1.00 58.20  ? 275  ASP A OD2 1 
ATOM   2177  N  N   . GLN A 1 276  ? 79.651  114.635 149.343 1.00 53.33  ? 276  GLN A N   1 
ATOM   2178  C  CA  . GLN A 1 276  ? 80.356  113.744 148.422 1.00 51.82  ? 276  GLN A CA  1 
ATOM   2179  C  C   . GLN A 1 276  ? 80.680  114.457 147.124 1.00 51.05  ? 276  GLN A C   1 
ATOM   2180  O  O   . GLN A 1 276  ? 79.858  115.219 146.612 1.00 51.60  ? 276  GLN A O   1 
ATOM   2181  C  CB  . GLN A 1 276  ? 79.472  112.556 148.066 1.00 51.39  ? 276  GLN A CB  1 
ATOM   2182  C  CG  . GLN A 1 276  ? 79.849  111.304 148.769 1.00 52.26  ? 276  GLN A CG  1 
ATOM   2183  C  CD  . GLN A 1 276  ? 79.072  110.089 148.292 1.00 53.02  ? 276  GLN A CD  1 
ATOM   2184  O  OE1 . GLN A 1 276  ? 78.385  109.439 149.083 1.00 54.90  ? 276  GLN A OE1 1 
ATOM   2185  N  NE2 . GLN A 1 276  ? 79.200  109.758 147.012 1.00 51.14  ? 276  GLN A NE2 1 
ATOM   2186  N  N   . GLN A 1 277  ? 81.860  114.198 146.574 1.00 49.64  ? 277  GLN A N   1 
ATOM   2187  C  CA  . GLN A 1 277  ? 82.194  114.725 145.257 1.00 48.68  ? 277  GLN A CA  1 
ATOM   2188  C  C   . GLN A 1 277  ? 83.072  113.766 144.461 1.00 47.40  ? 277  GLN A C   1 
ATOM   2189  O  O   . GLN A 1 277  ? 84.082  113.260 144.954 1.00 47.18  ? 277  GLN A O   1 
ATOM   2190  C  CB  . GLN A 1 277  ? 82.847  116.096 145.372 1.00 48.96  ? 277  GLN A CB  1 
ATOM   2191  C  CG  . GLN A 1 277  ? 82.723  116.928 144.119 1.00 50.03  ? 277  GLN A CG  1 
ATOM   2192  C  CD  . GLN A 1 277  ? 83.449  118.257 144.230 1.00 51.65  ? 277  GLN A CD  1 
ATOM   2193  O  OE1 . GLN A 1 277  ? 83.187  119.053 145.136 1.00 54.17  ? 277  GLN A OE1 1 
ATOM   2194  N  NE2 . GLN A 1 277  ? 84.361  118.507 143.302 1.00 51.36  ? 277  GLN A NE2 1 
ATOM   2195  N  N   . ASP A 1 278  ? 82.665  113.503 143.229 1.00 46.32  ? 278  ASP A N   1 
ATOM   2196  C  CA  . ASP A 1 278  ? 83.458  112.680 142.346 1.00 45.11  ? 278  ASP A CA  1 
ATOM   2197  C  C   . ASP A 1 278  ? 84.420  113.541 141.566 1.00 44.25  ? 278  ASP A C   1 
ATOM   2198  O  O   . ASP A 1 278  ? 84.029  114.521 140.929 1.00 44.55  ? 278  ASP A O   1 
ATOM   2199  C  CB  . ASP A 1 278  ? 82.565  111.865 141.418 1.00 45.21  ? 278  ASP A CB  1 
ATOM   2200  C  CG  . ASP A 1 278  ? 81.941  110.670 142.117 1.00 46.90  ? 278  ASP A CG  1 
ATOM   2201  O  OD1 . ASP A 1 278  ? 81.318  109.849 141.416 1.00 48.56  ? 278  ASP A OD1 1 
ATOM   2202  O  OD2 . ASP A 1 278  ? 82.075  110.533 143.363 1.00 49.20  ? 278  ASP A OD2 1 
ATOM   2203  N  N   . VAL A 1 279  ? 85.693  113.181 141.644 1.00 43.00  ? 279  VAL A N   1 
ATOM   2204  C  CA  . VAL A 1 279  ? 86.735  113.892 140.926 1.00 42.21  ? 279  VAL A CA  1 
ATOM   2205  C  C   . VAL A 1 279  ? 87.355  112.922 139.921 1.00 41.28  ? 279  VAL A C   1 
ATOM   2206  O  O   . VAL A 1 279  ? 87.865  111.866 140.310 1.00 41.20  ? 279  VAL A O   1 
ATOM   2207  C  CB  . VAL A 1 279  ? 87.797  114.445 141.903 1.00 42.34  ? 279  VAL A CB  1 
ATOM   2208  C  CG1 . VAL A 1 279  ? 88.889  115.140 141.158 1.00 42.26  ? 279  VAL A CG1 1 
ATOM   2209  C  CG2 . VAL A 1 279  ? 87.163  115.423 142.863 1.00 42.89  ? 279  VAL A CG2 1 
ATOM   2210  N  N   . PRO A 1 280  ? 87.292  113.259 138.622 1.00 40.73  ? 280  PRO A N   1 
ATOM   2211  C  CA  . PRO A 1 280  ? 87.822  112.358 137.588 1.00 40.18  ? 280  PRO A CA  1 
ATOM   2212  C  C   . PRO A 1 280  ? 89.356  112.361 137.507 1.00 39.99  ? 280  PRO A C   1 
ATOM   2213  O  O   . PRO A 1 280  ? 89.976  113.428 137.486 1.00 40.18  ? 280  PRO A O   1 
ATOM   2214  C  CB  . PRO A 1 280  ? 87.202  112.900 136.292 1.00 39.85  ? 280  PRO A CB  1 
ATOM   2215  C  CG  . PRO A 1 280  ? 86.897  114.307 136.556 1.00 40.05  ? 280  PRO A CG  1 
ATOM   2216  C  CD  . PRO A 1 280  ? 86.723  114.490 138.047 1.00 40.98  ? 280  PRO A CD  1 
ATOM   2217  N  N   . VAL A 1 281  ? 89.946  111.172 137.472 1.00 39.56  ? 281  VAL A N   1 
ATOM   2218  C  CA  . VAL A 1 281  ? 91.389  111.026 137.376 1.00 40.04  ? 281  VAL A CA  1 
ATOM   2219  C  C   . VAL A 1 281  ? 91.760  110.301 136.089 1.00 40.05  ? 281  VAL A C   1 
ATOM   2220  O  O   . VAL A 1 281  ? 91.059  109.368 135.685 1.00 40.06  ? 281  VAL A O   1 
ATOM   2221  C  CB  . VAL A 1 281  ? 91.957  110.259 138.585 1.00 40.11  ? 281  VAL A CB  1 
ATOM   2222  C  CG1 . VAL A 1 281  ? 93.426  109.941 138.385 1.00 40.01  ? 281  VAL A CG1 1 
ATOM   2223  C  CG2 . VAL A 1 281  ? 91.793  111.094 139.855 1.00 41.56  ? 281  VAL A CG2 1 
ATOM   2224  N  N   . LYS A 1 282  ? 92.840  110.746 135.437 1.00 40.01  ? 282  LYS A N   1 
ATOM   2225  C  CA  . LYS A 1 282  ? 93.405  110.024 134.288 1.00 39.86  ? 282  LYS A CA  1 
ATOM   2226  C  C   . LYS A 1 282  ? 94.876  109.688 134.520 1.00 39.41  ? 282  LYS A C   1 
ATOM   2227  O  O   . LYS A 1 282  ? 95.657  110.557 134.918 1.00 39.66  ? 282  LYS A O   1 
ATOM   2228  C  CB  . LYS A 1 282  ? 93.247  110.811 132.978 1.00 40.08  ? 282  LYS A CB  1 
ATOM   2229  C  CG  . LYS A 1 282  ? 93.872  110.099 131.772 1.00 40.74  ? 282  LYS A CG  1 
ATOM   2230  C  CD  . LYS A 1 282  ? 93.317  110.568 130.441 1.00 43.23  ? 282  LYS A CD  1 
ATOM   2231  C  CE  . LYS A 1 282  ? 93.913  111.901 130.041 1.00 46.50  ? 282  LYS A CE  1 
ATOM   2232  N  NZ  . LYS A 1 282  ? 93.525  112.252 128.647 1.00 48.72  ? 282  LYS A NZ  1 
ATOM   2233  N  N   . VAL A 1 283  ? 95.233  108.428 134.280 1.00 38.51  ? 283  VAL A N   1 
ATOM   2234  C  CA  . VAL A 1 283  ? 96.611  107.975 134.394 1.00 38.49  ? 283  VAL A CA  1 
ATOM   2235  C  C   . VAL A 1 283  ? 97.113  107.416 133.059 1.00 38.65  ? 283  VAL A C   1 
ATOM   2236  O  O   . VAL A 1 283  ? 96.568  106.433 132.540 1.00 38.29  ? 283  VAL A O   1 
ATOM   2237  C  CB  . VAL A 1 283  ? 96.788  106.902 135.498 1.00 38.30  ? 283  VAL A CB  1 
ATOM   2238  C  CG1 . VAL A 1 283  ? 98.239  106.408 135.523 1.00 38.68  ? 283  VAL A CG1 1 
ATOM   2239  C  CG2 . VAL A 1 283  ? 96.403  107.458 136.865 1.00 37.70  ? 283  VAL A CG2 1 
ATOM   2240  N  N   . SER A 1 284  ? 98.140  108.053 132.505 1.00 38.88  ? 284  SER A N   1 
ATOM   2241  C  CA  . SER A 1 284  ? 98.832  107.513 131.340 1.00 39.29  ? 284  SER A CA  1 
ATOM   2242  C  C   . SER A 1 284  ? 100.121 106.849 131.753 1.00 38.62  ? 284  SER A C   1 
ATOM   2243  O  O   . SER A 1 284  ? 101.032 107.495 132.237 1.00 38.48  ? 284  SER A O   1 
ATOM   2244  C  CB  . SER A 1 284  ? 99.122  108.597 130.314 1.00 39.61  ? 284  SER A CB  1 
ATOM   2245  O  OG  . SER A 1 284  ? 97.903  109.194 129.948 1.00 42.57  ? 284  SER A OG  1 
ATOM   2246  N  N   . PHE A 1 285  ? 100.173 105.545 131.559 1.00 38.38  ? 285  PHE A N   1 
ATOM   2247  C  CA  . PHE A 1 285  ? 101.341 104.781 131.894 1.00 38.79  ? 285  PHE A CA  1 
ATOM   2248  C  C   . PHE A 1 285  ? 102.158 104.450 130.632 1.00 38.99  ? 285  PHE A C   1 
ATOM   2249  O  O   . PHE A 1 285  ? 101.728 103.652 129.782 1.00 38.71  ? 285  PHE A O   1 
ATOM   2250  C  CB  . PHE A 1 285  ? 100.923 103.515 132.631 1.00 38.29  ? 285  PHE A CB  1 
ATOM   2251  C  CG  . PHE A 1 285  ? 102.002 102.940 133.469 1.00 39.09  ? 285  PHE A CG  1 
ATOM   2252  C  CD1 . PHE A 1 285  ? 102.012 103.148 134.836 1.00 39.81  ? 285  PHE A CD1 1 
ATOM   2253  C  CD2 . PHE A 1 285  ? 103.035 102.207 132.892 1.00 39.54  ? 285  PHE A CD2 1 
ATOM   2254  C  CE1 . PHE A 1 285  ? 103.029 102.623 135.620 1.00 40.91  ? 285  PHE A CE1 1 
ATOM   2255  C  CE2 . PHE A 1 285  ? 104.049 101.671 133.668 1.00 39.65  ? 285  PHE A CE2 1 
ATOM   2256  C  CZ  . PHE A 1 285  ? 104.049 101.878 135.036 1.00 40.61  ? 285  PHE A CZ  1 
ATOM   2257  N  N   . VAL A 1 286  ? 103.330 105.071 130.522 1.00 39.41  ? 286  VAL A N   1 
ATOM   2258  C  CA  . VAL A 1 286  ? 104.231 104.843 129.390 1.00 39.78  ? 286  VAL A CA  1 
ATOM   2259  C  C   . VAL A 1 286  ? 105.322 103.826 129.740 1.00 40.14  ? 286  VAL A C   1 
ATOM   2260  O  O   . VAL A 1 286  ? 106.221 104.130 130.520 1.00 40.52  ? 286  VAL A O   1 
ATOM   2261  C  CB  . VAL A 1 286  ? 104.879 106.174 128.904 1.00 39.83  ? 286  VAL A CB  1 
ATOM   2262  C  CG1 . VAL A 1 286  ? 105.790 105.927 127.720 1.00 39.45  ? 286  VAL A CG1 1 
ATOM   2263  C  CG2 . VAL A 1 286  ? 103.809 107.175 128.519 1.00 39.47  ? 286  VAL A CG2 1 
ATOM   2264  N  N   . GLU A 1 287  ? 105.250 102.631 129.157 1.00 40.42  ? 287  GLU A N   1 
ATOM   2265  C  CA  . GLU A 1 287  ? 106.257 101.597 129.414 1.00 41.30  ? 287  GLU A CA  1 
ATOM   2266  C  C   . GLU A 1 287  ? 107.659 102.059 128.993 1.00 42.59  ? 287  GLU A C   1 
ATOM   2267  O  O   . GLU A 1 287  ? 107.820 102.787 128.008 1.00 42.55  ? 287  GLU A O   1 
ATOM   2268  C  CB  . GLU A 1 287  ? 105.886 100.282 128.727 1.00 40.91  ? 287  GLU A CB  1 
ATOM   2269  C  CG  . GLU A 1 287  ? 106.803 99.115  129.058 1.00 41.33  ? 287  GLU A CG  1 
ATOM   2270  C  CD  . GLU A 1 287  ? 106.464 97.857  128.277 1.00 43.36  ? 287  GLU A CD  1 
ATOM   2271  O  OE1 . GLU A 1 287  ? 106.150 97.950  127.070 1.00 43.32  ? 287  GLU A OE1 1 
ATOM   2272  O  OE2 . GLU A 1 287  ? 106.515 96.758  128.876 1.00 45.42  ? 287  GLU A OE2 1 
ATOM   2273  N  N   . GLN A 1 288  ? 108.660 101.603 129.740 1.00 43.81  ? 288  GLN A N   1 
ATOM   2274  C  CA  . GLN A 1 288  ? 109.998 102.167 129.700 1.00 45.24  ? 288  GLN A CA  1 
ATOM   2275  C  C   . GLN A 1 288  ? 110.608 102.389 128.311 1.00 46.34  ? 288  GLN A C   1 
ATOM   2276  O  O   . GLN A 1 288  ? 110.809 103.550 127.888 1.00 47.63  ? 288  GLN A O   1 
ATOM   2277  C  CB  . GLN A 1 288  ? 110.950 101.378 130.597 1.00 45.22  ? 288  GLN A CB  1 
ATOM   2278  C  CG  . GLN A 1 288  ? 112.344 101.964 130.648 1.00 46.36  ? 288  GLN A CG  1 
ATOM   2279  C  CD  . GLN A 1 288  ? 113.193 101.402 131.779 1.00 48.34  ? 288  GLN A CD  1 
ATOM   2280  O  OE1 . GLN A 1 288  ? 112.951 100.294 132.277 1.00 49.57  ? 288  GLN A OE1 1 
ATOM   2281  N  NE2 . GLN A 1 288  ? 114.204 102.164 132.183 1.00 47.26  ? 288  GLN A NE2 1 
ATOM   2282  N  N   . TYR A 1 289  ? 110.932 101.318 127.602 1.00 46.38  ? 289  TYR A N   1 
ATOM   2283  C  CA  . TYR A 1 289  ? 111.748 101.498 126.403 1.00 46.70  ? 289  TYR A CA  1 
ATOM   2284  C  C   . TYR A 1 289  ? 110.866 101.503 125.177 1.00 46.45  ? 289  TYR A C   1 
ATOM   2285  O  O   . TYR A 1 289  ? 111.062 102.284 124.252 1.00 46.93  ? 289  TYR A O   1 
ATOM   2286  C  CB  . TYR A 1 289  ? 112.790 100.394 126.303 1.00 47.29  ? 289  TYR A CB  1 
ATOM   2287  C  CG  . TYR A 1 289  ? 113.704 100.309 127.502 1.00 48.25  ? 289  TYR A CG  1 
ATOM   2288  C  CD1 . TYR A 1 289  ? 114.665 101.292 127.741 1.00 49.42  ? 289  TYR A CD1 1 
ATOM   2289  C  CD2 . TYR A 1 289  ? 113.620 99.239  128.392 1.00 48.63  ? 289  TYR A CD2 1 
ATOM   2290  C  CE1 . TYR A 1 289  ? 115.510 101.216 128.834 1.00 50.17  ? 289  TYR A CE1 1 
ATOM   2291  C  CE2 . TYR A 1 289  ? 114.466 99.152  129.491 1.00 49.39  ? 289  TYR A CE2 1 
ATOM   2292  C  CZ  . TYR A 1 289  ? 115.409 100.144 129.703 1.00 50.25  ? 289  TYR A CZ  1 
ATOM   2293  O  OH  . TYR A 1 289  ? 116.250 100.071 130.789 1.00 51.04  ? 289  TYR A OH  1 
ATOM   2294  N  N   . THR A 1 290  ? 109.882 100.617 125.200 1.00 45.76  ? 290  THR A N   1 
ATOM   2295  C  CA  . THR A 1 290  ? 108.883 100.502 124.159 1.00 45.21  ? 290  THR A CA  1 
ATOM   2296  C  C   . THR A 1 290  ? 108.046 101.768 123.978 1.00 45.00  ? 290  THR A C   1 
ATOM   2297  O  O   . THR A 1 290  ? 107.574 102.050 122.883 1.00 45.02  ? 290  THR A O   1 
ATOM   2298  C  CB  . THR A 1 290  ? 107.932 99.366  124.502 1.00 44.64  ? 290  THR A CB  1 
ATOM   2299  O  OG1 . THR A 1 290  ? 107.094 99.783  125.583 1.00 44.30  ? 290  THR A OG1 1 
ATOM   2300  C  CG2 . THR A 1 290  ? 108.722 98.144  124.928 1.00 44.16  ? 290  THR A CG2 1 
ATOM   2301  N  N   . ASN A 1 291  ? 107.863 102.513 125.059 1.00 45.13  ? 291  ASN A N   1 
ATOM   2302  C  CA  . ASN A 1 291  ? 106.897 103.613 125.114 1.00 45.54  ? 291  ASN A CA  1 
ATOM   2303  C  C   . ASN A 1 291  ? 105.441 103.189 124.888 1.00 44.90  ? 291  ASN A C   1 
ATOM   2304  O  O   . ASN A 1 291  ? 104.585 104.023 124.602 1.00 44.92  ? 291  ASN A O   1 
ATOM   2305  C  CB  . ASN A 1 291  ? 107.294 104.770 124.192 1.00 45.94  ? 291  ASN A CB  1 
ATOM   2306  C  CG  . ASN A 1 291  ? 108.539 105.494 124.666 1.00 48.37  ? 291  ASN A CG  1 
ATOM   2307  O  OD1 . ASN A 1 291  ? 108.870 105.483 125.861 1.00 49.74  ? 291  ASN A OD1 1 
ATOM   2308  N  ND2 . ASN A 1 291  ? 109.228 106.151 123.726 1.00 51.58  ? 291  ASN A ND2 1 
ATOM   2309  N  N   . ARG A 1 292  ? 105.161 101.898 125.038 1.00 44.38  ? 292  ARG A N   1 
ATOM   2310  C  CA  . ARG A 1 292  ? 103.791 101.419 125.011 1.00 44.45  ? 292  ARG A CA  1 
ATOM   2311  C  C   . ARG A 1 292  ? 102.972 102.098 126.123 1.00 43.73  ? 292  ARG A C   1 
ATOM   2312  O  O   . ARG A 1 292  ? 103.281 101.978 127.313 1.00 43.70  ? 292  ARG A O   1 
ATOM   2313  C  CB  . ARG A 1 292  ? 103.739 99.901  125.143 1.00 44.77  ? 292  ARG A CB  1 
ATOM   2314  C  CG  . ARG A 1 292  ? 102.327 99.337  125.116 1.00 48.61  ? 292  ARG A CG  1 
ATOM   2315  C  CD  . ARG A 1 292  ? 102.325 97.815  125.198 1.00 55.50  ? 292  ARG A CD  1 
ATOM   2316  N  NE  . ARG A 1 292  ? 102.446 97.214  123.867 1.00 62.40  ? 292  ARG A NE  1 
ATOM   2317  C  CZ  . ARG A 1 292  ? 102.599 95.908  123.625 1.00 65.53  ? 292  ARG A CZ  1 
ATOM   2318  N  NH1 . ARG A 1 292  ? 102.659 95.029  124.627 1.00 66.61  ? 292  ARG A NH1 1 
ATOM   2319  N  NH2 . ARG A 1 292  ? 102.697 95.475  122.372 1.00 66.55  ? 292  ARG A NH2 1 
ATOM   2320  N  N   . THR A 1 293  ? 101.944 102.830 125.703 1.00 42.68  ? 293  THR A N   1 
ATOM   2321  C  CA  . THR A 1 293  ? 101.116 103.623 126.586 1.00 41.43  ? 293  THR A CA  1 
ATOM   2322  C  C   . THR A 1 293  ? 99.779  102.930 126.857 1.00 40.83  ? 293  THR A C   1 
ATOM   2323  O  O   . THR A 1 293  ? 99.094  102.468 125.934 1.00 40.63  ? 293  THR A O   1 
ATOM   2324  C  CB  . THR A 1 293  ? 100.897 105.016 125.989 1.00 41.46  ? 293  THR A CB  1 
ATOM   2325  O  OG1 . THR A 1 293  ? 102.170 105.604 125.713 1.00 42.49  ? 293  THR A OG1 1 
ATOM   2326  C  CG2 . THR A 1 293  ? 100.149 105.924 126.942 1.00 41.33  ? 293  THR A CG2 1 
ATOM   2327  N  N   . VAL A 1 294  ? 99.430  102.835 128.138 1.00 39.91  ? 294  VAL A N   1 
ATOM   2328  C  CA  . VAL A 1 294  ? 98.110  102.385 128.546 1.00 38.77  ? 294  VAL A CA  1 
ATOM   2329  C  C   . VAL A 1 294  ? 97.510  103.494 129.392 1.00 38.95  ? 294  VAL A C   1 
ATOM   2330  O  O   . VAL A 1 294  ? 98.193  104.063 130.265 1.00 38.85  ? 294  VAL A O   1 
ATOM   2331  C  CB  . VAL A 1 294  ? 98.166  101.079 129.344 1.00 38.61  ? 294  VAL A CB  1 
ATOM   2332  C  CG1 . VAL A 1 294  ? 96.842  100.821 130.056 1.00 37.18  ? 294  VAL A CG1 1 
ATOM   2333  C  CG2 . VAL A 1 294  ? 98.531  99.923  128.433 1.00 38.02  ? 294  VAL A CG2 1 
ATOM   2334  N  N   . VAL A 1 295  ? 96.244  103.806 129.114 1.00 38.33  ? 295  VAL A N   1 
ATOM   2335  C  CA  . VAL A 1 295  ? 95.547  104.878 129.792 1.00 37.86  ? 295  VAL A CA  1 
ATOM   2336  C  C   . VAL A 1 295  ? 94.441  104.299 130.629 1.00 38.08  ? 295  VAL A C   1 
ATOM   2337  O  O   . VAL A 1 295  ? 93.668  103.472 130.149 1.00 38.00  ? 295  VAL A O   1 
ATOM   2338  C  CB  . VAL A 1 295  ? 94.973  105.906 128.793 1.00 38.21  ? 295  VAL A CB  1 
ATOM   2339  C  CG1 . VAL A 1 295  ? 94.078  106.912 129.503 1.00 37.39  ? 295  VAL A CG1 1 
ATOM   2340  C  CG2 . VAL A 1 295  ? 96.099  106.611 128.047 1.00 36.35  ? 295  VAL A CG2 1 
ATOM   2341  N  N   . LYS A 1 296  ? 94.375  104.734 131.889 1.00 38.42  ? 296  LYS A N   1 
ATOM   2342  C  CA  . LYS A 1 296  ? 93.358  104.269 132.828 1.00 38.20  ? 296  LYS A CA  1 
ATOM   2343  C  C   . LYS A 1 296  ? 92.672  105.455 133.476 1.00 38.07  ? 296  LYS A C   1 
ATOM   2344  O  O   . LYS A 1 296  ? 93.328  106.379 133.938 1.00 38.33  ? 296  LYS A O   1 
ATOM   2345  C  CB  . LYS A 1 296  ? 93.998  103.392 133.903 1.00 38.53  ? 296  LYS A CB  1 
ATOM   2346  C  CG  . LYS A 1 296  ? 93.020  102.797 134.904 1.00 39.63  ? 296  LYS A CG  1 
ATOM   2347  C  CD  . LYS A 1 296  ? 92.284  101.625 134.282 1.00 42.79  ? 296  LYS A CD  1 
ATOM   2348  C  CE  . LYS A 1 296  ? 91.112  101.178 135.126 1.00 45.52  ? 296  LYS A CE  1 
ATOM   2349  N  NZ  . LYS A 1 296  ? 90.544  99.931  134.545 1.00 47.70  ? 296  LYS A NZ  1 
ATOM   2350  N  N   . GLN A 1 297  ? 91.345  105.417 133.508 1.00 38.04  ? 297  GLN A N   1 
ATOM   2351  C  CA  . GLN A 1 297  ? 90.541  106.495 134.079 1.00 37.96  ? 297  GLN A CA  1 
ATOM   2352  C  C   . GLN A 1 297  ? 89.658  105.979 135.192 1.00 37.87  ? 297  GLN A C   1 
ATOM   2353  O  O   . GLN A 1 297  ? 89.217  104.848 135.140 1.00 38.11  ? 297  GLN A O   1 
ATOM   2354  C  CB  . GLN A 1 297  ? 89.675  107.143 133.002 1.00 37.88  ? 297  GLN A CB  1 
ATOM   2355  C  CG  . GLN A 1 297  ? 90.468  107.975 132.019 1.00 38.24  ? 297  GLN A CG  1 
ATOM   2356  C  CD  . GLN A 1 297  ? 89.609  108.953 131.244 1.00 40.65  ? 297  GLN A CD  1 
ATOM   2357  O  OE1 . GLN A 1 297  ? 89.018  109.873 131.813 1.00 40.15  ? 297  GLN A OE1 1 
ATOM   2358  N  NE2 . GLN A 1 297  ? 89.556  108.774 129.923 1.00 41.92  ? 297  GLN A NE2 1 
ATOM   2359  N  N   . SER A 1 298  ? 89.428  106.794 136.217 1.00 38.10  ? 298  SER A N   1 
ATOM   2360  C  CA  . SER A 1 298  ? 88.377  106.497 137.189 1.00 38.56  ? 298  SER A CA  1 
ATOM   2361  C  C   . SER A 1 298  ? 87.833  107.739 137.878 1.00 38.55  ? 298  SER A C   1 
ATOM   2362  O  O   . SER A 1 298  ? 88.406  108.818 137.780 1.00 38.89  ? 298  SER A O   1 
ATOM   2363  C  CB  . SER A 1 298  ? 88.810  105.443 138.211 1.00 38.79  ? 298  SER A CB  1 
ATOM   2364  O  OG  . SER A 1 298  ? 89.528  106.023 139.273 1.00 40.61  ? 298  SER A OG  1 
ATOM   2365  N  N   . GLN A 1 299  ? 86.691  107.583 138.528 1.00 38.59  ? 299  GLN A N   1 
ATOM   2366  C  CA  . GLN A 1 299  ? 86.104  108.663 139.292 1.00 38.99  ? 299  GLN A CA  1 
ATOM   2367  C  C   . GLN A 1 299  ? 86.496  108.410 140.734 1.00 39.20  ? 299  GLN A C   1 
ATOM   2368  O  O   . GLN A 1 299  ? 86.217  107.340 141.292 1.00 38.79  ? 299  GLN A O   1 
ATOM   2369  C  CB  . GLN A 1 299  ? 84.574  108.701 139.134 1.00 38.83  ? 299  GLN A CB  1 
ATOM   2370  C  CG  . GLN A 1 299  ? 84.081  109.044 137.734 1.00 38.25  ? 299  GLN A CG  1 
ATOM   2371  C  CD  . GLN A 1 299  ? 84.151  110.535 137.403 1.00 38.88  ? 299  GLN A CD  1 
ATOM   2372  O  OE1 . GLN A 1 299  ? 84.424  111.364 138.273 1.00 40.53  ? 299  GLN A OE1 1 
ATOM   2373  N  NE2 . GLN A 1 299  ? 83.886  110.882 136.142 1.00 36.53  ? 299  GLN A NE2 1 
ATOM   2374  N  N   . ILE A 1 300  ? 87.168  109.383 141.331 1.00 39.75  ? 300  ILE A N   1 
ATOM   2375  C  CA  . ILE A 1 300  ? 87.540  109.246 142.723 1.00 40.64  ? 300  ILE A CA  1 
ATOM   2376  C  C   . ILE A 1 300  ? 86.691  110.125 143.616 1.00 41.00  ? 300  ILE A C   1 
ATOM   2377  O  O   . ILE A 1 300  ? 86.664  111.349 143.472 1.00 41.70  ? 300  ILE A O   1 
ATOM   2378  C  CB  . ILE A 1 300  ? 89.065  109.388 142.927 1.00 41.04  ? 300  ILE A CB  1 
ATOM   2379  C  CG1 . ILE A 1 300  ? 89.696  108.019 142.671 1.00 41.29  ? 300  ILE A CG1 1 
ATOM   2380  C  CG2 . ILE A 1 300  ? 89.406  109.836 144.351 1.00 40.99  ? 300  ILE A CG2 1 
ATOM   2381  C  CD1 . ILE A 1 300  ? 90.745  108.047 141.647 1.00 43.69  ? 300  ILE A CD1 1 
ATOM   2382  N  N   . THR A 1 301  ? 85.971  109.474 144.516 1.00 41.06  ? 301  THR A N   1 
ATOM   2383  C  CA  . THR A 1 301  ? 85.071  110.160 145.428 1.00 41.29  ? 301  THR A CA  1 
ATOM   2384  C  C   . THR A 1 301  ? 85.844  110.691 146.619 1.00 41.52  ? 301  THR A C   1 
ATOM   2385  O  O   . THR A 1 301  ? 86.559  109.945 147.295 1.00 41.23  ? 301  THR A O   1 
ATOM   2386  C  CB  . THR A 1 301  ? 83.931  109.223 145.935 1.00 41.15  ? 301  THR A CB  1 
ATOM   2387  O  OG1 . THR A 1 301  ? 83.366  108.515 144.829 1.00 40.64  ? 301  THR A OG1 1 
ATOM   2388  C  CG2 . THR A 1 301  ? 82.843  110.024 146.604 1.00 40.80  ? 301  THR A CG2 1 
ATOM   2389  N  N   . VAL A 1 302  ? 85.690  111.986 146.861 1.00 41.87  ? 302  VAL A N   1 
ATOM   2390  C  CA  . VAL A 1 302  ? 86.094  112.588 148.125 1.00 42.36  ? 302  VAL A CA  1 
ATOM   2391  C  C   . VAL A 1 302  ? 84.857  112.705 149.028 1.00 43.08  ? 302  VAL A C   1 
ATOM   2392  O  O   . VAL A 1 302  ? 83.806  113.199 148.594 1.00 43.13  ? 302  VAL A O   1 
ATOM   2393  C  CB  . VAL A 1 302  ? 86.752  113.964 147.908 1.00 42.30  ? 302  VAL A CB  1 
ATOM   2394  C  CG1 . VAL A 1 302  ? 87.225  114.541 149.225 1.00 42.54  ? 302  VAL A CG1 1 
ATOM   2395  C  CG2 . VAL A 1 302  ? 87.918  113.838 146.933 1.00 41.59  ? 302  VAL A CG2 1 
ATOM   2396  N  N   . TYR A 1 303  ? 84.993  112.251 150.275 1.00 43.57  ? 303  TYR A N   1 
ATOM   2397  C  CA  . TYR A 1 303  ? 83.882  112.208 151.234 1.00 44.10  ? 303  TYR A CA  1 
ATOM   2398  C  C   . TYR A 1 303  ? 84.072  113.170 152.396 1.00 45.11  ? 303  TYR A C   1 
ATOM   2399  O  O   . TYR A 1 303  ? 85.177  113.311 152.913 1.00 45.60  ? 303  TYR A O   1 
ATOM   2400  C  CB  . TYR A 1 303  ? 83.753  110.817 151.830 1.00 43.49  ? 303  TYR A CB  1 
ATOM   2401  C  CG  . TYR A 1 303  ? 83.518  109.700 150.843 1.00 43.09  ? 303  TYR A CG  1 
ATOM   2402  C  CD1 . TYR A 1 303  ? 84.585  108.922 150.378 1.00 42.35  ? 303  TYR A CD1 1 
ATOM   2403  C  CD2 . TYR A 1 303  ? 82.229  109.392 150.400 1.00 42.34  ? 303  TYR A CD2 1 
ATOM   2404  C  CE1 . TYR A 1 303  ? 84.379  107.871 149.501 1.00 42.28  ? 303  TYR A CE1 1 
ATOM   2405  C  CE2 . TYR A 1 303  ? 82.007  108.339 149.510 1.00 42.48  ? 303  TYR A CE2 1 
ATOM   2406  C  CZ  . TYR A 1 303  ? 83.086  107.583 149.067 1.00 42.83  ? 303  TYR A CZ  1 
ATOM   2407  O  OH  . TYR A 1 303  ? 82.890  106.554 148.179 1.00 42.09  ? 303  TYR A OH  1 
ATOM   2408  N  N   . ARG A 1 304  ? 82.990  113.801 152.839 1.00 45.79  ? 304  ARG A N   1 
ATOM   2409  C  CA  . ARG A 1 304  ? 83.062  114.651 154.023 1.00 46.62  ? 304  ARG A CA  1 
ATOM   2410  C  C   . ARG A 1 304  ? 83.227  113.854 155.318 1.00 46.92  ? 304  ARG A C   1 
ATOM   2411  O  O   . ARG A 1 304  ? 83.978  114.260 156.198 1.00 47.62  ? 304  ARG A O   1 
ATOM   2412  C  CB  . ARG A 1 304  ? 81.851  115.576 154.121 1.00 47.03  ? 304  ARG A CB  1 
ATOM   2413  C  CG  . ARG A 1 304  ? 81.959  116.581 155.240 1.00 47.53  ? 304  ARG A CG  1 
ATOM   2414  C  CD  . ARG A 1 304  ? 80.972  117.709 155.051 1.00 48.24  ? 304  ARG A CD  1 
ATOM   2415  N  NE  . ARG A 1 304  ? 81.449  118.668 154.067 1.00 47.55  ? 304  ARG A NE  1 
ATOM   2416  C  CZ  . ARG A 1 304  ? 80.664  119.325 153.221 1.00 48.19  ? 304  ARG A CZ  1 
ATOM   2417  N  NH1 . ARG A 1 304  ? 79.349  119.115 153.225 1.00 47.52  ? 304  ARG A NH1 1 
ATOM   2418  N  NH2 . ARG A 1 304  ? 81.198  120.182 152.356 1.00 47.16  ? 304  ARG A NH2 1 
ATOM   2419  N  N   . TYR A 1 305  ? 82.537  112.723 155.428 1.00 46.48  ? 305  TYR A N   1 
ATOM   2420  C  CA  . TYR A 1 305  ? 82.575  111.929 156.648 1.00 46.68  ? 305  TYR A CA  1 
ATOM   2421  C  C   . TYR A 1 305  ? 83.122  110.550 156.370 1.00 46.26  ? 305  TYR A C   1 
ATOM   2422  O  O   . TYR A 1 305  ? 83.040  110.071 155.249 1.00 45.80  ? 305  TYR A O   1 
ATOM   2423  C  CB  . TYR A 1 305  ? 81.177  111.816 157.255 1.00 47.01  ? 305  TYR A CB  1 
ATOM   2424  C  CG  . TYR A 1 305  ? 80.516  113.151 157.460 1.00 47.34  ? 305  TYR A CG  1 
ATOM   2425  C  CD1 . TYR A 1 305  ? 79.677  113.682 156.482 1.00 46.83  ? 305  TYR A CD1 1 
ATOM   2426  C  CD2 . TYR A 1 305  ? 80.741  113.894 158.624 1.00 47.11  ? 305  TYR A CD2 1 
ATOM   2427  C  CE1 . TYR A 1 305  ? 79.071  114.915 156.653 1.00 48.15  ? 305  TYR A CE1 1 
ATOM   2428  C  CE2 . TYR A 1 305  ? 80.135  115.133 158.807 1.00 48.29  ? 305  TYR A CE2 1 
ATOM   2429  C  CZ  . TYR A 1 305  ? 79.299  115.637 157.815 1.00 48.19  ? 305  TYR A CZ  1 
ATOM   2430  O  OH  . TYR A 1 305  ? 78.690  116.855 157.965 1.00 47.79  ? 305  TYR A OH  1 
ATOM   2431  N  N   . ALA A 1 306  ? 83.652  109.904 157.402 1.00 46.70  ? 306  ALA A N   1 
ATOM   2432  C  CA  . ALA A 1 306  ? 84.280  108.597 157.253 1.00 46.26  ? 306  ALA A CA  1 
ATOM   2433  C  C   . ALA A 1 306  ? 83.261  107.473 157.298 1.00 46.28  ? 306  ALA A C   1 
ATOM   2434  O  O   . ALA A 1 306  ? 83.619  106.299 157.245 1.00 46.22  ? 306  ALA A O   1 
ATOM   2435  C  CB  . ALA A 1 306  ? 85.346  108.400 158.319 1.00 46.50  ? 306  ALA A CB  1 
ATOM   2436  N  N   . TYR A 1 307  ? 81.988  107.833 157.393 1.00 46.92  ? 307  TYR A N   1 
ATOM   2437  C  CA  . TYR A 1 307  ? 80.932  106.836 157.475 1.00 47.31  ? 307  TYR A CA  1 
ATOM   2438  C  C   . TYR A 1 307  ? 79.689  107.264 156.702 1.00 47.80  ? 307  TYR A C   1 
ATOM   2439  O  O   . TYR A 1 307  ? 79.516  108.445 156.394 1.00 47.52  ? 307  TYR A O   1 
ATOM   2440  C  CB  . TYR A 1 307  ? 80.586  106.530 158.945 1.00 47.70  ? 307  TYR A CB  1 
ATOM   2441  C  CG  . TYR A 1 307  ? 80.123  107.729 159.749 1.00 47.76  ? 307  TYR A CG  1 
ATOM   2442  C  CD1 . TYR A 1 307  ? 81.037  108.502 160.477 1.00 47.55  ? 307  TYR A CD1 1 
ATOM   2443  C  CD2 . TYR A 1 307  ? 78.775  108.092 159.783 1.00 46.98  ? 307  TYR A CD2 1 
ATOM   2444  C  CE1 . TYR A 1 307  ? 80.621  109.607 161.209 1.00 47.76  ? 307  TYR A CE1 1 
ATOM   2445  C  CE2 . TYR A 1 307  ? 78.348  109.193 160.509 1.00 48.00  ? 307  TYR A CE2 1 
ATOM   2446  C  CZ  . TYR A 1 307  ? 79.273  109.945 161.225 1.00 49.61  ? 307  TYR A CZ  1 
ATOM   2447  O  OH  . TYR A 1 307  ? 78.845  111.037 161.961 1.00 51.61  ? 307  TYR A OH  1 
ATOM   2448  N  N   . ARG A 1 308  ? 78.841  106.280 156.395 1.00 48.68  ? 308  ARG A N   1 
ATOM   2449  C  CA  . ARG A 1 308  ? 77.524  106.503 155.795 1.00 49.81  ? 308  ARG A CA  1 
ATOM   2450  C  C   . ARG A 1 308  ? 76.449  105.674 156.511 1.00 50.25  ? 308  ARG A C   1 
ATOM   2451  O  O   . ARG A 1 308  ? 76.714  104.576 157.009 1.00 50.32  ? 308  ARG A O   1 
ATOM   2452  C  CB  . ARG A 1 308  ? 77.531  106.204 154.282 1.00 49.44  ? 308  ARG A CB  1 
ATOM   2453  C  CG  . ARG A 1 308  ? 77.805  104.752 153.916 1.00 51.52  ? 308  ARG A CG  1 
ATOM   2454  C  CD  . ARG A 1 308  ? 77.314  104.398 152.512 1.00 56.83  ? 308  ARG A CD  1 
ATOM   2455  N  NE  . ARG A 1 308  ? 77.294  102.947 152.302 1.00 60.74  ? 308  ARG A NE  1 
ATOM   2456  C  CZ  . ARG A 1 308  ? 78.308  102.226 151.815 1.00 62.81  ? 308  ARG A CZ  1 
ATOM   2457  N  NH1 . ARG A 1 308  ? 79.454  102.811 151.452 1.00 63.61  ? 308  ARG A NH1 1 
ATOM   2458  N  NH2 . ARG A 1 308  ? 78.174  100.908 151.686 1.00 62.77  ? 308  ARG A NH2 1 
ATOM   2459  N  N   . VAL A 1 309  ? 75.238  106.215 156.551 1.00 50.74  ? 309  VAL A N   1 
ATOM   2460  C  CA  . VAL A 1 309  ? 74.110  105.554 157.178 1.00 51.29  ? 309  VAL A CA  1 
ATOM   2461  C  C   . VAL A 1 309  ? 73.041  105.256 156.141 1.00 51.53  ? 309  VAL A C   1 
ATOM   2462  O  O   . VAL A 1 309  ? 72.739  106.095 155.281 1.00 51.33  ? 309  VAL A O   1 
ATOM   2463  C  CB  . VAL A 1 309  ? 73.468  106.441 158.270 1.00 52.19  ? 309  VAL A CB  1 
ATOM   2464  C  CG1 . VAL A 1 309  ? 72.476  105.644 159.109 1.00 52.48  ? 309  VAL A CG1 1 
ATOM   2465  C  CG2 . VAL A 1 309  ? 74.524  107.044 159.155 1.00 52.36  ? 309  VAL A CG2 1 
ATOM   2466  N  N   . GLU A 1 310  ? 72.473  104.057 156.225 1.00 51.91  ? 310  GLU A N   1 
ATOM   2467  C  CA  . GLU A 1 310  ? 71.219  103.760 155.547 1.00 52.84  ? 310  GLU A CA  1 
ATOM   2468  C  C   . GLU A 1 310  ? 70.211  103.125 156.521 1.00 53.23  ? 310  GLU A C   1 
ATOM   2469  O  O   . GLU A 1 310  ? 70.589  102.492 157.516 1.00 53.46  ? 310  GLU A O   1 
ATOM   2470  C  CB  . GLU A 1 310  ? 71.434  102.905 154.292 1.00 52.35  ? 310  GLU A CB  1 
ATOM   2471  C  CG  . GLU A 1 310  ? 72.020  101.533 154.556 1.00 55.43  ? 310  GLU A CG  1 
ATOM   2472  C  CD  . GLU A 1 310  ? 71.951  100.594 153.352 1.00 59.13  ? 310  GLU A CD  1 
ATOM   2473  O  OE1 . GLU A 1 310  ? 71.174  100.859 152.405 1.00 59.86  ? 310  GLU A OE1 1 
ATOM   2474  O  OE2 . GLU A 1 310  ? 72.677  99.572  153.369 1.00 60.68  ? 310  GLU A OE2 1 
ATOM   2475  N  N   . LEU A 1 311  ? 68.929  103.312 156.232 1.00 53.18  ? 311  LEU A N   1 
ATOM   2476  C  CA  . LEU A 1 311  ? 67.881  102.767 157.069 1.00 53.55  ? 311  LEU A CA  1 
ATOM   2477  C  C   . LEU A 1 311  ? 67.450  101.380 156.590 1.00 53.26  ? 311  LEU A C   1 
ATOM   2478  O  O   . LEU A 1 311  ? 66.979  101.223 155.471 1.00 53.22  ? 311  LEU A O   1 
ATOM   2479  C  CB  . LEU A 1 311  ? 66.692  103.719 157.087 1.00 54.01  ? 311  LEU A CB  1 
ATOM   2480  C  CG  . LEU A 1 311  ? 65.493  103.235 157.884 1.00 55.16  ? 311  LEU A CG  1 
ATOM   2481  C  CD1 . LEU A 1 311  ? 65.824  103.242 159.373 1.00 55.71  ? 311  LEU A CD1 1 
ATOM   2482  C  CD2 . LEU A 1 311  ? 64.296  104.111 157.568 1.00 55.70  ? 311  LEU A CD2 1 
ATOM   2483  N  N   . ILE A 1 312  ? 67.613  100.376 157.441 1.00 53.30  ? 312  ILE A N   1 
ATOM   2484  C  CA  . ILE A 1 312  ? 67.204  99.021  157.095 1.00 53.14  ? 312  ILE A CA  1 
ATOM   2485  C  C   . ILE A 1 312  ? 65.933  98.699  157.848 1.00 53.72  ? 312  ILE A C   1 
ATOM   2486  O  O   . ILE A 1 312  ? 65.907  98.749  159.070 1.00 54.33  ? 312  ILE A O   1 
ATOM   2487  C  CB  . ILE A 1 312  ? 68.322  97.985  157.376 1.00 52.93  ? 312  ILE A CB  1 
ATOM   2488  C  CG1 . ILE A 1 312  ? 69.580  98.367  156.566 1.00 52.84  ? 312  ILE A CG1 1 
ATOM   2489  C  CG2 . ILE A 1 312  ? 67.819  96.559  157.112 1.00 52.40  ? 312  ILE A CG2 1 
ATOM   2490  C  CD1 . ILE A 1 312  ? 70.249  97.246  155.784 1.00 54.12  ? 312  ILE A CD1 1 
ATOM   2491  N  N   . LYS A 1 313  ? 64.880  98.390  157.103 1.00 53.60  ? 313  LYS A N   1 
ATOM   2492  C  CA  . LYS A 1 313  ? 63.545  98.262  157.671 1.00 54.25  ? 313  LYS A CA  1 
ATOM   2493  C  C   . LYS A 1 313  ? 63.075  96.825  157.592 1.00 54.66  ? 313  LYS A C   1 
ATOM   2494  O  O   . LYS A 1 313  ? 63.430  96.109  156.660 1.00 53.92  ? 313  LYS A O   1 
ATOM   2495  C  CB  . LYS A 1 313  ? 62.563  99.161  156.920 1.00 54.50  ? 313  LYS A CB  1 
ATOM   2496  C  CG  . LYS A 1 313  ? 63.000  100.610 156.803 1.00 53.69  ? 313  LYS A CG  1 
ATOM   2497  C  CD  . LYS A 1 313  ? 62.053  101.411 155.936 1.00 53.48  ? 313  LYS A CD  1 
ATOM   2498  C  CE  . LYS A 1 313  ? 62.260  101.138 154.459 1.00 52.72  ? 313  LYS A CE  1 
ATOM   2499  N  NZ  . LYS A 1 313  ? 61.312  101.947 153.646 1.00 52.50  ? 313  LYS A NZ  1 
ATOM   2500  N  N   . GLU A 1 314  ? 62.278  96.398  158.568 1.00 55.89  ? 314  GLU A N   1 
ATOM   2501  C  CA  . GLU A 1 314  ? 61.780  95.029  158.567 1.00 56.73  ? 314  GLU A CA  1 
ATOM   2502  C  C   . GLU A 1 314  ? 60.816  94.850  157.404 1.00 56.92  ? 314  GLU A C   1 
ATOM   2503  O  O   . GLU A 1 314  ? 60.751  93.781  156.805 1.00 56.93  ? 314  GLU A O   1 
ATOM   2504  C  CB  . GLU A 1 314  ? 61.125  94.660  159.901 1.00 57.93  ? 314  GLU A CB  1 
ATOM   2505  C  CG  . GLU A 1 314  ? 59.764  95.311  160.178 1.00 60.09  ? 314  GLU A CG  1 
ATOM   2506  C  CD  . GLU A 1 314  ? 58.987  94.605  161.279 1.00 63.86  ? 314  GLU A CD  1 
ATOM   2507  O  OE1 . GLU A 1 314  ? 58.285  95.301  162.054 1.00 65.47  ? 314  GLU A OE1 1 
ATOM   2508  O  OE2 . GLU A 1 314  ? 59.084  93.353  161.380 1.00 65.14  ? 314  GLU A OE2 1 
ATOM   2509  N  N   . SER A 1 315  ? 60.089  95.917  157.089 1.00 57.26  ? 315  SER A N   1 
ATOM   2510  C  CA  . SER A 1 315  ? 59.161  95.945  155.972 1.00 57.90  ? 315  SER A CA  1 
ATOM   2511  C  C   . SER A 1 315  ? 59.062  97.380  155.457 1.00 57.81  ? 315  SER A C   1 
ATOM   2512  O  O   . SER A 1 315  ? 59.179  98.321  156.244 1.00 58.07  ? 315  SER A O   1 
ATOM   2513  C  CB  . SER A 1 315  ? 57.795  95.444  156.416 1.00 59.01  ? 315  SER A CB  1 
ATOM   2514  O  OG  . SER A 1 315  ? 57.272  96.273  157.438 1.00 60.66  ? 315  SER A OG  1 
ATOM   2515  N  N   . PRO A 1 316  ? 58.826  97.556  154.141 1.00 57.62  ? 316  PRO A N   1 
ATOM   2516  C  CA  . PRO A 1 316  ? 58.949  98.874  153.497 1.00 57.25  ? 316  PRO A CA  1 
ATOM   2517  C  C   . PRO A 1 316  ? 58.074  99.958  154.119 1.00 57.96  ? 316  PRO A C   1 
ATOM   2518  O  O   . PRO A 1 316  ? 58.468  101.123 154.142 1.00 58.07  ? 316  PRO A O   1 
ATOM   2519  C  CB  . PRO A 1 316  ? 58.511  98.607  152.055 1.00 57.05  ? 316  PRO A CB  1 
ATOM   2520  C  CG  . PRO A 1 316  ? 58.711  97.149  151.856 1.00 57.15  ? 316  PRO A CG  1 
ATOM   2521  C  CD  . PRO A 1 316  ? 58.402  96.521  153.180 1.00 57.74  ? 316  PRO A CD  1 
ATOM   2522  N  N   . GLN A 1 317  ? 56.899  99.578  154.604 1.00 58.61  ? 317  GLN A N   1 
ATOM   2523  C  CA  . GLN A 1 317  ? 56.006  100.512 155.260 1.00 59.60  ? 317  GLN A CA  1 
ATOM   2524  C  C   . GLN A 1 317  ? 55.599  99.944  156.609 1.00 60.54  ? 317  GLN A C   1 
ATOM   2525  O  O   . GLN A 1 317  ? 55.684  98.728  156.825 1.00 60.75  ? 317  GLN A O   1 
ATOM   2526  C  CB  . GLN A 1 317  ? 54.764  100.774 154.406 1.00 60.22  ? 317  GLN A CB  1 
ATOM   2527  C  CG  . GLN A 1 317  ? 54.976  101.740 153.240 1.00 59.82  ? 317  GLN A CG  1 
ATOM   2528  C  CD  . GLN A 1 317  ? 55.528  101.057 152.005 1.00 58.96  ? 317  GLN A CD  1 
ATOM   2529  O  OE1 . GLN A 1 317  ? 55.170  99.916  151.697 1.00 59.56  ? 317  GLN A OE1 1 
ATOM   2530  N  NE2 . GLN A 1 317  ? 56.407  101.751 151.290 1.00 56.71  ? 317  GLN A NE2 1 
ATOM   2531  N  N   . PHE A 1 318  ? 55.160  100.821 157.510 1.00 60.98  ? 318  PHE A N   1 
ATOM   2532  C  CA  . PHE A 1 318  ? 54.768  100.403 158.848 1.00 61.85  ? 318  PHE A CA  1 
ATOM   2533  C  C   . PHE A 1 318  ? 53.261  100.219 158.989 1.00 63.16  ? 318  PHE A C   1 
ATOM   2534  O  O   . PHE A 1 318  ? 52.476  100.733 158.185 1.00 63.51  ? 318  PHE A O   1 
ATOM   2535  C  CB  . PHE A 1 318  ? 55.287  101.389 159.904 1.00 62.05  ? 318  PHE A CB  1 
ATOM   2536  C  CG  . PHE A 1 318  ? 54.497  102.675 160.002 1.00 62.44  ? 318  PHE A CG  1 
ATOM   2537  C  CD1 . PHE A 1 318  ? 54.908  103.814 159.309 1.00 61.69  ? 318  PHE A CD1 1 
ATOM   2538  C  CD2 . PHE A 1 318  ? 53.364  102.754 160.813 1.00 62.81  ? 318  PHE A CD2 1 
ATOM   2539  C  CE1 . PHE A 1 318  ? 54.194  105.007 159.404 1.00 62.19  ? 318  PHE A CE1 1 
ATOM   2540  C  CE2 . PHE A 1 318  ? 52.640  103.941 160.919 1.00 63.88  ? 318  PHE A CE2 1 
ATOM   2541  C  CZ  . PHE A 1 318  ? 53.053  105.072 160.213 1.00 63.62  ? 318  PHE A CZ  1 
ATOM   2542  N  N   . ARG A 1 319  ? 52.871  99.493  160.029 1.00 63.92  ? 319  ARG A N   1 
ATOM   2543  C  CA  . ARG A 1 319  ? 51.472  99.235  160.311 1.00 65.08  ? 319  ARG A CA  1 
ATOM   2544  C  C   . ARG A 1 319  ? 51.035  100.104 161.486 1.00 66.20  ? 319  ARG A C   1 
ATOM   2545  O  O   . ARG A 1 319  ? 51.533  99.943  162.600 1.00 66.25  ? 319  ARG A O   1 
ATOM   2546  C  CB  . ARG A 1 319  ? 51.253  97.753  160.585 1.00 65.37  ? 319  ARG A CB  1 
ATOM   2547  C  CG  . ARG A 1 319  ? 51.652  96.864  159.418 1.00 64.30  ? 319  ARG A CG  1 
ATOM   2548  C  CD  . ARG A 1 319  ? 51.827  95.433  159.856 1.00 64.59  ? 319  ARG A CD  1 
ATOM   2549  N  NE  . ARG A 1 319  ? 52.919  95.283  160.817 1.00 64.35  ? 319  ARG A NE  1 
ATOM   2550  C  CZ  . ARG A 1 319  ? 53.094  94.218  161.594 1.00 63.64  ? 319  ARG A CZ  1 
ATOM   2551  N  NH1 . ARG A 1 319  ? 52.252  93.197  161.533 1.00 64.29  ? 319  ARG A NH1 1 
ATOM   2552  N  NH2 . ARG A 1 319  ? 54.115  94.175  162.435 1.00 62.87  ? 319  ARG A NH2 1 
ATOM   2553  N  N   . PRO A 1 320  ? 50.118  101.053 161.221 1.00 67.11  ? 320  PRO A N   1 
ATOM   2554  C  CA  . PRO A 1 320  ? 49.669  102.118 162.110 1.00 67.79  ? 320  PRO A CA  1 
ATOM   2555  C  C   . PRO A 1 320  ? 49.618  101.847 163.611 1.00 68.33  ? 320  PRO A C   1 
ATOM   2556  O  O   . PRO A 1 320  ? 49.857  102.774 164.380 1.00 69.30  ? 320  PRO A O   1 
ATOM   2557  C  CB  . PRO A 1 320  ? 48.282  102.445 161.565 1.00 68.82  ? 320  PRO A CB  1 
ATOM   2558  C  CG  . PRO A 1 320  ? 48.480  102.319 160.090 1.00 68.29  ? 320  PRO A CG  1 
ATOM   2559  C  CD  . PRO A 1 320  ? 49.448  101.158 159.908 1.00 67.34  ? 320  PRO A CD  1 
ATOM   2560  N  N   . GLY A 1 321  ? 49.321  100.624 164.041 1.00 67.77  ? 321  GLY A N   1 
ATOM   2561  C  CA  . GLY A 1 321  ? 49.213  100.371 165.481 1.00 67.54  ? 321  GLY A CA  1 
ATOM   2562  C  C   . GLY A 1 321  ? 50.204  99.380  166.073 1.00 66.49  ? 321  GLY A C   1 
ATOM   2563  O  O   . GLY A 1 321  ? 50.151  99.077  167.272 1.00 67.14  ? 321  GLY A O   1 
ATOM   2564  N  N   . LEU A 1 322  ? 51.115  98.886  165.239 1.00 64.50  ? 322  LEU A N   1 
ATOM   2565  C  CA  . LEU A 1 322  ? 51.959  97.753  165.596 1.00 63.23  ? 322  LEU A CA  1 
ATOM   2566  C  C   . LEU A 1 322  ? 53.431  98.133  165.714 1.00 61.89  ? 322  LEU A C   1 
ATOM   2567  O  O   . LEU A 1 322  ? 53.845  99.137  165.146 1.00 61.61  ? 322  LEU A O   1 
ATOM   2568  C  CB  . LEU A 1 322  ? 51.755  96.629  164.574 1.00 62.88  ? 322  LEU A CB  1 
ATOM   2569  C  CG  . LEU A 1 322  ? 50.380  95.943  164.633 1.00 63.17  ? 322  LEU A CG  1 
ATOM   2570  C  CD1 . LEU A 1 322  ? 50.097  95.162  163.362 1.00 62.33  ? 322  LEU A CD1 1 
ATOM   2571  C  CD2 . LEU A 1 322  ? 50.279  95.047  165.839 1.00 61.59  ? 322  LEU A CD2 1 
ATOM   2572  N  N   . PRO A 1 323  ? 54.233  97.340  166.460 1.00 61.44  ? 323  PRO A N   1 
ATOM   2573  C  CA  . PRO A 1 323  ? 55.641  97.725  166.568 1.00 60.24  ? 323  PRO A CA  1 
ATOM   2574  C  C   . PRO A 1 323  ? 56.348  97.631  165.218 1.00 59.03  ? 323  PRO A C   1 
ATOM   2575  O  O   . PRO A 1 323  ? 55.990  96.787  164.392 1.00 59.20  ? 323  PRO A O   1 
ATOM   2576  C  CB  . PRO A 1 323  ? 56.220  96.725  167.578 1.00 60.35  ? 323  PRO A CB  1 
ATOM   2577  C  CG  . PRO A 1 323  ? 55.252  95.617  167.663 1.00 60.91  ? 323  PRO A CG  1 
ATOM   2578  C  CD  . PRO A 1 323  ? 53.923  96.113  167.220 1.00 61.78  ? 323  PRO A CD  1 
ATOM   2579  N  N   . PHE A 1 324  ? 57.318  98.517  164.996 1.00 57.92  ? 324  PHE A N   1 
ATOM   2580  C  CA  . PHE A 1 324  ? 58.048  98.582  163.738 1.00 56.29  ? 324  PHE A CA  1 
ATOM   2581  C  C   . PHE A 1 324  ? 59.541  98.478  164.016 1.00 55.72  ? 324  PHE A C   1 
ATOM   2582  O  O   . PHE A 1 324  ? 60.116  99.323  164.715 1.00 55.23  ? 324  PHE A O   1 
ATOM   2583  C  CB  . PHE A 1 324  ? 57.718  99.885  162.998 1.00 55.94  ? 324  PHE A CB  1 
ATOM   2584  C  CG  . PHE A 1 324  ? 58.440  100.052 161.676 1.00 54.41  ? 324  PHE A CG  1 
ATOM   2585  C  CD1 . PHE A 1 324  ? 58.009  99.375  160.534 1.00 53.35  ? 324  PHE A CD1 1 
ATOM   2586  C  CD2 . PHE A 1 324  ? 59.547  100.909 161.569 1.00 53.08  ? 324  PHE A CD2 1 
ATOM   2587  C  CE1 . PHE A 1 324  ? 58.673  99.539  159.308 1.00 52.20  ? 324  PHE A CE1 1 
ATOM   2588  C  CE2 . PHE A 1 324  ? 60.219  101.079 160.352 1.00 50.95  ? 324  PHE A CE2 1 
ATOM   2589  C  CZ  . PHE A 1 324  ? 59.781  100.394 159.219 1.00 50.73  ? 324  PHE A CZ  1 
ATOM   2590  N  N   . LYS A 1 325  ? 60.156  97.428  163.466 1.00 55.41  ? 325  LYS A N   1 
ATOM   2591  C  CA  . LYS A 1 325  ? 61.579  97.153  163.665 1.00 54.89  ? 325  LYS A CA  1 
ATOM   2592  C  C   . LYS A 1 325  ? 62.416  97.620  162.500 1.00 53.55  ? 325  LYS A C   1 
ATOM   2593  O  O   . LYS A 1 325  ? 62.140  97.296  161.345 1.00 53.55  ? 325  LYS A O   1 
ATOM   2594  C  CB  . LYS A 1 325  ? 61.835  95.663  163.892 1.00 55.19  ? 325  LYS A CB  1 
ATOM   2595  C  CG  . LYS A 1 325  ? 61.526  95.158  165.300 1.00 57.91  ? 325  LYS A CG  1 
ATOM   2596  C  CD  . LYS A 1 325  ? 62.329  93.891  165.587 1.00 60.82  ? 325  LYS A CD  1 
ATOM   2597  C  CE  . LYS A 1 325  ? 61.608  92.964  166.554 1.00 64.06  ? 325  LYS A CE  1 
ATOM   2598  N  NZ  . LYS A 1 325  ? 62.302  91.639  166.638 1.00 65.66  ? 325  LYS A NZ  1 
ATOM   2599  N  N   . CYS A 1 326  ? 63.454  98.379  162.816 1.00 52.62  ? 326  CYS A N   1 
ATOM   2600  C  CA  . CYS A 1 326  ? 64.404  98.828  161.821 1.00 51.14  ? 326  CYS A CA  1 
ATOM   2601  C  C   . CYS A 1 326  ? 65.703  99.162  162.520 1.00 50.80  ? 326  CYS A C   1 
ATOM   2602  O  O   . CYS A 1 326  ? 65.784  99.126  163.744 1.00 51.47  ? 326  CYS A O   1 
ATOM   2603  C  CB  . CYS A 1 326  ? 63.869  100.055 161.088 1.00 51.14  ? 326  CYS A CB  1 
ATOM   2604  S  SG  . CYS A 1 326  ? 63.435  101.433 162.171 1.00 51.12  ? 326  CYS A SG  1 
ATOM   2605  N  N   . ALA A 1 327  ? 66.718  99.489  161.739 1.00 49.92  ? 327  ALA A N   1 
ATOM   2606  C  CA  . ALA A 1 327  ? 68.026  99.794  162.277 1.00 49.61  ? 327  ALA A CA  1 
ATOM   2607  C  C   . ALA A 1 327  ? 68.716  100.811 161.379 1.00 49.16  ? 327  ALA A C   1 
ATOM   2608  O  O   . ALA A 1 327  ? 68.527  100.794 160.161 1.00 48.50  ? 327  ALA A O   1 
ATOM   2609  C  CB  . ALA A 1 327  ? 68.848  98.530  162.372 1.00 49.02  ? 327  ALA A CB  1 
ATOM   2610  N  N   . LEU A 1 328  ? 69.493  101.703 161.986 1.00 49.50  ? 328  LEU A N   1 
ATOM   2611  C  CA  . LEU A 1 328  ? 70.349  102.598 161.227 1.00 49.57  ? 328  LEU A CA  1 
ATOM   2612  C  C   . LEU A 1 328  ? 71.663  101.878 161.003 1.00 49.40  ? 328  LEU A C   1 
ATOM   2613  O  O   . LEU A 1 328  ? 72.369  101.549 161.957 1.00 49.82  ? 328  LEU A O   1 
ATOM   2614  C  CB  . LEU A 1 328  ? 70.558  103.923 161.962 1.00 49.82  ? 328  LEU A CB  1 
ATOM   2615  C  CG  . LEU A 1 328  ? 69.327  104.834 162.085 1.00 50.69  ? 328  LEU A CG  1 
ATOM   2616  C  CD1 . LEU A 1 328  ? 69.557  105.933 163.107 1.00 50.86  ? 328  LEU A CD1 1 
ATOM   2617  C  CD2 . LEU A 1 328  ? 68.931  105.441 160.736 1.00 49.48  ? 328  LEU A CD2 1 
ATOM   2618  N  N   . GLN A 1 329  ? 71.970  101.595 159.743 1.00 49.34  ? 329  GLN A N   1 
ATOM   2619  C  CA  . GLN A 1 329  ? 73.164  100.824 159.408 1.00 49.34  ? 329  GLN A CA  1 
ATOM   2620  C  C   . GLN A 1 329  ? 74.330  101.729 159.038 1.00 48.90  ? 329  GLN A C   1 
ATOM   2621  O  O   . GLN A 1 329  ? 74.279  102.438 158.027 1.00 48.44  ? 329  GLN A O   1 
ATOM   2622  C  CB  . GLN A 1 329  ? 72.878  99.843  158.272 1.00 48.96  ? 329  GLN A CB  1 
ATOM   2623  C  CG  . GLN A 1 329  ? 74.048  98.943  157.947 1.00 49.81  ? 329  GLN A CG  1 
ATOM   2624  C  CD  . GLN A 1 329  ? 73.671  97.829  156.999 1.00 52.26  ? 329  GLN A CD  1 
ATOM   2625  O  OE1 . GLN A 1 329  ? 73.535  98.046  155.789 1.00 54.65  ? 329  GLN A OE1 1 
ATOM   2626  N  NE2 . GLN A 1 329  ? 73.508  96.622  157.536 1.00 52.40  ? 329  GLN A NE2 1 
ATOM   2627  N  N   . PHE A 1 330  ? 75.375  101.690 159.864 1.00 49.08  ? 330  PHE A N   1 
ATOM   2628  C  CA  . PHE A 1 330  ? 76.593  102.470 159.631 1.00 48.95  ? 330  PHE A CA  1 
ATOM   2629  C  C   . PHE A 1 330  ? 77.677  101.623 158.977 1.00 48.78  ? 330  PHE A C   1 
ATOM   2630  O  O   . PHE A 1 330  ? 77.990  100.518 159.441 1.00 48.96  ? 330  PHE A O   1 
ATOM   2631  C  CB  . PHE A 1 330  ? 77.136  103.046 160.938 1.00 49.15  ? 330  PHE A CB  1 
ATOM   2632  C  CG  . PHE A 1 330  ? 76.196  103.976 161.637 1.00 48.88  ? 330  PHE A CG  1 
ATOM   2633  C  CD1 . PHE A 1 330  ? 76.411  105.343 161.605 1.00 48.36  ? 330  PHE A CD1 1 
ATOM   2634  C  CD2 . PHE A 1 330  ? 75.112  103.483 162.360 1.00 49.05  ? 330  PHE A CD2 1 
ATOM   2635  C  CE1 . PHE A 1 330  ? 75.545  106.214 162.274 1.00 49.64  ? 330  PHE A CE1 1 
ATOM   2636  C  CE2 . PHE A 1 330  ? 74.241  104.341 163.022 1.00 49.16  ? 330  PHE A CE2 1 
ATOM   2637  C  CZ  . PHE A 1 330  ? 74.457  105.707 162.984 1.00 49.44  ? 330  PHE A CZ  1 
ATOM   2638  N  N   . THR A 1 331  ? 78.244  102.147 157.896 1.00 48.87  ? 331  THR A N   1 
ATOM   2639  C  CA  . THR A 1 331  ? 79.348  101.489 157.194 1.00 49.03  ? 331  THR A CA  1 
ATOM   2640  C  C   . THR A 1 331  ? 80.396  102.510 156.791 1.00 49.30  ? 331  THR A C   1 
ATOM   2641  O  O   . THR A 1 331  ? 80.074  103.681 156.557 1.00 49.40  ? 331  THR A O   1 
ATOM   2642  C  CB  . THR A 1 331  ? 78.880  100.787 155.910 1.00 48.41  ? 331  THR A CB  1 
ATOM   2643  O  OG1 . THR A 1 331  ? 78.032  101.676 155.168 1.00 49.54  ? 331  THR A OG1 1 
ATOM   2644  C  CG2 . THR A 1 331  ? 78.127  99.502  156.218 1.00 47.87  ? 331  THR A CG2 1 
ATOM   2645  N  N   . HIS A 1 332  ? 81.649  102.065 156.710 1.00 49.75  ? 332  HIS A N   1 
ATOM   2646  C  CA  . HIS A 1 332  ? 82.701  102.877 156.106 1.00 50.16  ? 332  HIS A CA  1 
ATOM   2647  C  C   . HIS A 1 332  ? 82.471  102.884 154.604 1.00 50.49  ? 332  HIS A C   1 
ATOM   2648  O  O   . HIS A 1 332  ? 81.618  102.147 154.097 1.00 50.49  ? 332  HIS A O   1 
ATOM   2649  C  CB  . HIS A 1 332  ? 84.082  102.337 156.464 1.00 49.78  ? 332  HIS A CB  1 
ATOM   2650  C  CG  . HIS A 1 332  ? 84.418  102.481 157.913 1.00 50.30  ? 332  HIS A CG  1 
ATOM   2651  N  ND1 . HIS A 1 332  ? 84.679  101.401 158.728 1.00 50.74  ? 332  HIS A ND1 1 
ATOM   2652  C  CD2 . HIS A 1 332  ? 84.499  103.580 158.705 1.00 50.36  ? 332  HIS A CD2 1 
ATOM   2653  C  CE1 . HIS A 1 332  ? 84.920  101.828 159.957 1.00 51.34  ? 332  HIS A CE1 1 
ATOM   2654  N  NE2 . HIS A 1 332  ? 84.819  103.146 159.969 1.00 51.30  ? 332  HIS A NE2 1 
ATOM   2655  N  N   . HIS A 1 333  ? 83.204  103.722 153.881 1.00 51.39  ? 333  HIS A N   1 
ATOM   2656  C  CA  . HIS A 1 333  ? 82.974  103.823 152.440 1.00 52.05  ? 333  HIS A CA  1 
ATOM   2657  C  C   . HIS A 1 333  ? 83.543  102.647 151.622 1.00 52.29  ? 333  HIS A C   1 
ATOM   2658  O  O   . HIS A 1 333  ? 83.391  102.609 150.406 1.00 52.07  ? 333  HIS A O   1 
ATOM   2659  C  CB  . HIS A 1 333  ? 83.388  105.195 151.906 1.00 51.78  ? 333  HIS A CB  1 
ATOM   2660  C  CG  . HIS A 1 333  ? 82.517  106.312 152.403 1.00 52.51  ? 333  HIS A CG  1 
ATOM   2661  N  ND1 . HIS A 1 333  ? 82.958  107.262 153.301 1.00 51.87  ? 333  HIS A ND1 1 
ATOM   2662  C  CD2 . HIS A 1 333  ? 81.219  106.610 152.147 1.00 52.33  ? 333  HIS A CD2 1 
ATOM   2663  C  CE1 . HIS A 1 333  ? 81.975  108.106 153.562 1.00 52.33  ? 333  HIS A CE1 1 
ATOM   2664  N  NE2 . HIS A 1 333  ? 80.909  107.733 152.877 1.00 52.37  ? 333  HIS A NE2 1 
ATOM   2665  N  N   . ASP A 1 334  ? 84.165  101.690 152.310 1.00 53.32  ? 334  ASP A N   1 
ATOM   2666  C  CA  . ASP A 1 334  ? 84.614  100.433 151.711 1.00 54.01  ? 334  ASP A CA  1 
ATOM   2667  C  C   . ASP A 1 334  ? 83.632  99.296  151.976 1.00 54.33  ? 334  ASP A C   1 
ATOM   2668  O  O   . ASP A 1 334  ? 83.940  98.132  151.715 1.00 54.32  ? 334  ASP A O   1 
ATOM   2669  C  CB  . ASP A 1 334  ? 85.960  100.046 152.294 1.00 54.49  ? 334  ASP A CB  1 
ATOM   2670  C  CG  . ASP A 1 334  ? 86.003  100.236 153.788 1.00 57.82  ? 334  ASP A CG  1 
ATOM   2671  O  OD1 . ASP A 1 334  ? 86.765  101.117 154.238 1.00 61.79  ? 334  ASP A OD1 1 
ATOM   2672  O  OD2 . ASP A 1 334  ? 85.249  99.546  154.512 1.00 60.22  ? 334  ASP A OD2 1 
ATOM   2673  N  N   . GLY A 1 335  ? 82.470  99.632  152.533 1.00 54.93  ? 335  GLY A N   1 
ATOM   2674  C  CA  . GLY A 1 335  ? 81.419  98.654  152.786 1.00 54.86  ? 335  GLY A CA  1 
ATOM   2675  C  C   . GLY A 1 335  ? 81.461  97.987  154.149 1.00 55.34  ? 335  GLY A C   1 
ATOM   2676  O  O   . GLY A 1 335  ? 80.461  97.387  154.564 1.00 55.85  ? 335  GLY A O   1 
ATOM   2677  N  N   . THR A 1 336  ? 82.600  98.074  154.844 1.00 54.99  ? 336  THR A N   1 
ATOM   2678  C  CA  . THR A 1 336  ? 82.745  97.448  156.170 1.00 55.29  ? 336  THR A CA  1 
ATOM   2679  C  C   . THR A 1 336  ? 81.947  98.175  157.265 1.00 55.66  ? 336  THR A C   1 
ATOM   2680  O  O   . THR A 1 336  ? 81.794  99.404  157.211 1.00 55.43  ? 336  THR A O   1 
ATOM   2681  C  CB  . THR A 1 336  ? 84.224  97.364  156.631 1.00 55.41  ? 336  THR A CB  1 
ATOM   2682  O  OG1 . THR A 1 336  ? 84.788  98.681  156.722 1.00 55.23  ? 336  THR A OG1 1 
ATOM   2683  C  CG2 . THR A 1 336  ? 85.049  96.495  155.684 1.00 55.09  ? 336  THR A CG2 1 
ATOM   2684  N  N   . PRO A 1 337  ? 81.440  97.420  158.264 1.00 55.95  ? 337  PRO A N   1 
ATOM   2685  C  CA  . PRO A 1 337  ? 80.723  98.009  159.400 1.00 56.37  ? 337  PRO A CA  1 
ATOM   2686  C  C   . PRO A 1 337  ? 81.540  99.083  160.109 1.00 56.50  ? 337  PRO A C   1 
ATOM   2687  O  O   . PRO A 1 337  ? 82.755  98.929  160.286 1.00 56.65  ? 337  PRO A O   1 
ATOM   2688  C  CB  . PRO A 1 337  ? 80.504  96.816  160.330 1.00 56.76  ? 337  PRO A CB  1 
ATOM   2689  C  CG  . PRO A 1 337  ? 80.464  95.644  159.418 1.00 56.54  ? 337  PRO A CG  1 
ATOM   2690  C  CD  . PRO A 1 337  ? 81.491  95.949  158.364 1.00 56.07  ? 337  PRO A CD  1 
ATOM   2691  N  N   . ALA A 1 338  ? 80.875  100.172 160.483 1.00 56.38  ? 338  ALA A N   1 
ATOM   2692  C  CA  . ALA A 1 338  ? 81.518  101.257 161.213 1.00 56.20  ? 338  ALA A CA  1 
ATOM   2693  C  C   . ALA A 1 338  ? 81.022  101.280 162.659 1.00 56.71  ? 338  ALA A C   1 
ATOM   2694  O  O   . ALA A 1 338  ? 79.901  101.690 162.935 1.00 56.87  ? 338  ALA A O   1 
ATOM   2695  C  CB  . ALA A 1 338  ? 81.263  102.582 160.521 1.00 55.92  ? 338  ALA A CB  1 
ATOM   2696  N  N   . LYS A 1 339  ? 81.875  100.824 163.570 1.00 56.98  ? 339  LYS A N   1 
ATOM   2697  C  CA  . LYS A 1 339  ? 81.511  100.614 164.971 1.00 57.72  ? 339  LYS A CA  1 
ATOM   2698  C  C   . LYS A 1 339  ? 81.804  101.845 165.809 1.00 57.82  ? 339  LYS A C   1 
ATOM   2699  O  O   . LYS A 1 339  ? 82.711  102.617 165.503 1.00 57.85  ? 339  LYS A O   1 
ATOM   2700  C  CB  . LYS A 1 339  ? 82.285  99.428  165.551 1.00 58.03  ? 339  LYS A CB  1 
ATOM   2701  C  CG  . LYS A 1 339  ? 82.499  98.267  164.581 1.00 59.17  ? 339  LYS A CG  1 
ATOM   2702  C  CD  . LYS A 1 339  ? 83.611  97.353  165.072 1.00 62.33  ? 339  LYS A CD  1 
ATOM   2703  C  CE  . LYS A 1 339  ? 83.688  96.053  164.276 1.00 63.39  ? 339  LYS A CE  1 
ATOM   2704  N  NZ  . LYS A 1 339  ? 84.407  95.013  165.078 1.00 64.78  ? 339  LYS A NZ  1 
ATOM   2705  N  N   . GLY A 1 340  ? 81.029  102.021 166.871 1.00 58.10  ? 340  GLY A N   1 
ATOM   2706  C  CA  . GLY A 1 340  ? 81.273  103.084 167.831 1.00 57.93  ? 340  GLY A CA  1 
ATOM   2707  C  C   . GLY A 1 340  ? 80.918  104.473 167.351 1.00 57.34  ? 340  GLY A C   1 
ATOM   2708  O  O   . GLY A 1 340  ? 81.271  105.450 168.004 1.00 57.86  ? 340  GLY A O   1 
ATOM   2709  N  N   . ILE A 1 341  ? 80.222  104.575 166.221 1.00 56.22  ? 341  ILE A N   1 
ATOM   2710  C  CA  . ILE A 1 341  ? 79.778  105.878 165.739 1.00 55.94  ? 341  ILE A CA  1 
ATOM   2711  C  C   . ILE A 1 341  ? 78.614  106.378 166.602 1.00 56.81  ? 341  ILE A C   1 
ATOM   2712  O  O   . ILE A 1 341  ? 77.594  105.695 166.767 1.00 56.91  ? 341  ILE A O   1 
ATOM   2713  C  CB  . ILE A 1 341  ? 79.479  105.896 164.210 1.00 55.03  ? 341  ILE A CB  1 
ATOM   2714  C  CG1 . ILE A 1 341  ? 80.770  106.124 163.409 1.00 54.25  ? 341  ILE A CG1 1 
ATOM   2715  C  CG2 . ILE A 1 341  ? 78.594  107.066 163.844 1.00 55.16  ? 341  ILE A CG2 1 
ATOM   2716  C  CD1 . ILE A 1 341  ? 81.708  104.942 163.308 1.00 53.54  ? 341  ILE A CD1 1 
ATOM   2717  N  N   . SER A 1 342  ? 78.798  107.563 167.178 1.00 57.22  ? 342  SER A N   1 
ATOM   2718  C  CA  . SER A 1 342  ? 77.857  108.086 168.150 1.00 58.20  ? 342  SER A CA  1 
ATOM   2719  C  C   . SER A 1 342  ? 77.078  109.269 167.606 1.00 58.09  ? 342  SER A C   1 
ATOM   2720  O  O   . SER A 1 342  ? 77.568  110.015 166.760 1.00 57.52  ? 342  SER A O   1 
ATOM   2721  C  CB  . SER A 1 342  ? 78.574  108.474 169.446 1.00 59.01  ? 342  SER A CB  1 
ATOM   2722  O  OG  . SER A 1 342  ? 79.186  109.741 169.333 1.00 59.73  ? 342  SER A OG  1 
ATOM   2723  N  N   . GLY A 1 343  ? 75.863  109.431 168.124 1.00 58.51  ? 343  GLY A N   1 
ATOM   2724  C  CA  . GLY A 1 343  ? 74.967  110.502 167.718 1.00 58.51  ? 343  GLY A CA  1 
ATOM   2725  C  C   . GLY A 1 343  ? 73.632  110.378 168.425 1.00 59.08  ? 343  GLY A C   1 
ATOM   2726  O  O   . GLY A 1 343  ? 73.463  109.545 169.310 1.00 59.51  ? 343  GLY A O   1 
ATOM   2727  N  N   . LYS A 1 344  ? 72.688  111.221 168.034 1.00 59.03  ? 344  LYS A N   1 
ATOM   2728  C  CA  . LYS A 1 344  ? 71.379  111.244 168.638 1.00 59.61  ? 344  LYS A CA  1 
ATOM   2729  C  C   . LYS A 1 344  ? 70.360  110.835 167.594 1.00 58.97  ? 344  LYS A C   1 
ATOM   2730  O  O   . LYS A 1 344  ? 70.289  111.429 166.514 1.00 58.59  ? 344  LYS A O   1 
ATOM   2731  C  CB  . LYS A 1 344  ? 71.078  112.645 169.167 1.00 60.72  ? 344  LYS A CB  1 
ATOM   2732  C  CG  . LYS A 1 344  ? 69.776  112.789 169.960 1.00 62.85  ? 344  LYS A CG  1 
ATOM   2733  C  CD  . LYS A 1 344  ? 69.910  113.933 170.969 1.00 66.33  ? 344  LYS A CD  1 
ATOM   2734  C  CE  . LYS A 1 344  ? 68.566  114.411 171.508 1.00 68.50  ? 344  LYS A CE  1 
ATOM   2735  N  NZ  . LYS A 1 344  ? 67.799  115.211 170.505 1.00 69.46  ? 344  LYS A NZ  1 
ATOM   2736  N  N   . VAL A 1 345  ? 69.592  109.801 167.915 1.00 58.72  ? 345  VAL A N   1 
ATOM   2737  C  CA  . VAL A 1 345  ? 68.481  109.375 167.082 1.00 58.05  ? 345  VAL A CA  1 
ATOM   2738  C  C   . VAL A 1 345  ? 67.245  110.011 167.676 1.00 58.96  ? 345  VAL A C   1 
ATOM   2739  O  O   . VAL A 1 345  ? 67.085  110.028 168.901 1.00 60.02  ? 345  VAL A O   1 
ATOM   2740  C  CB  . VAL A 1 345  ? 68.308  107.827 167.089 1.00 57.78  ? 345  VAL A CB  1 
ATOM   2741  C  CG1 . VAL A 1 345  ? 67.153  107.393 166.188 1.00 56.51  ? 345  VAL A CG1 1 
ATOM   2742  C  CG2 . VAL A 1 345  ? 69.604  107.129 166.676 1.00 56.63  ? 345  VAL A CG2 1 
ATOM   2743  N  N   . GLU A 1 346  ? 66.384  110.557 166.825 1.00 58.80  ? 346  GLU A N   1 
ATOM   2744  C  CA  . GLU A 1 346  ? 65.053  110.953 167.278 1.00 59.83  ? 346  GLU A CA  1 
ATOM   2745  C  C   . GLU A 1 346  ? 63.964  110.839 166.225 1.00 59.41  ? 346  GLU A C   1 
ATOM   2746  O  O   . GLU A 1 346  ? 64.168  111.147 165.041 1.00 58.25  ? 346  GLU A O   1 
ATOM   2747  C  CB  . GLU A 1 346  ? 65.039  112.328 167.959 1.00 60.64  ? 346  GLU A CB  1 
ATOM   2748  C  CG  . GLU A 1 346  ? 65.450  113.492 167.102 1.00 62.25  ? 346  GLU A CG  1 
ATOM   2749  C  CD  . GLU A 1 346  ? 65.111  114.832 167.740 1.00 66.04  ? 346  GLU A CD  1 
ATOM   2750  O  OE1 . GLU A 1 346  ? 64.474  114.847 168.830 1.00 66.53  ? 346  GLU A OE1 1 
ATOM   2751  O  OE2 . GLU A 1 346  ? 65.478  115.871 167.136 1.00 66.51  ? 346  GLU A OE2 1 
ATOM   2752  N  N   . VAL A 1 347  ? 62.821  110.340 166.691 1.00 60.08  ? 347  VAL A N   1 
ATOM   2753  C  CA  . VAL A 1 347  ? 61.614  110.221 165.897 1.00 60.47  ? 347  VAL A CA  1 
ATOM   2754  C  C   . VAL A 1 347  ? 60.570  111.021 166.650 1.00 62.04  ? 347  VAL A C   1 
ATOM   2755  O  O   . VAL A 1 347  ? 60.012  110.543 167.638 1.00 63.16  ? 347  VAL A O   1 
ATOM   2756  C  CB  . VAL A 1 347  ? 61.170  108.741 165.716 1.00 60.02  ? 347  VAL A CB  1 
ATOM   2757  C  CG1 . VAL A 1 347  ? 60.024  108.637 164.723 1.00 59.76  ? 347  VAL A CG1 1 
ATOM   2758  C  CG2 . VAL A 1 347  ? 62.329  107.874 165.250 1.00 58.51  ? 347  VAL A CG2 1 
ATOM   2759  N  N   . SER A 1 348  ? 60.327  112.250 166.201 1.00 62.88  ? 348  SER A N   1 
ATOM   2760  C  CA  . SER A 1 348  ? 59.486  113.188 166.958 1.00 64.69  ? 348  SER A CA  1 
ATOM   2761  C  C   . SER A 1 348  ? 58.006  112.813 166.973 1.00 65.69  ? 348  SER A C   1 
ATOM   2762  O  O   . SER A 1 348  ? 57.310  113.101 167.944 1.00 66.62  ? 348  SER A O   1 
ATOM   2763  C  CB  . SER A 1 348  ? 59.679  114.634 166.480 1.00 64.64  ? 348  SER A CB  1 
ATOM   2764  O  OG  . SER A 1 348  ? 59.109  114.840 165.198 1.00 65.00  ? 348  SER A OG  1 
ATOM   2765  N  N   . ASP A 1 349  ? 57.548  112.155 165.907 1.00 66.00  ? 349  ASP A N   1 
ATOM   2766  C  CA  . ASP A 1 349  ? 56.158  111.675 165.782 1.00 67.34  ? 349  ASP A CA  1 
ATOM   2767  C  C   . ASP A 1 349  ? 55.673  110.851 166.969 1.00 68.17  ? 349  ASP A C   1 
ATOM   2768  O  O   . ASP A 1 349  ? 54.484  110.841 167.261 1.00 69.32  ? 349  ASP A O   1 
ATOM   2769  C  CB  . ASP A 1 349  ? 55.980  110.827 164.517 1.00 66.94  ? 349  ASP A CB  1 
ATOM   2770  C  CG  . ASP A 1 349  ? 56.426  111.540 163.259 1.00 66.96  ? 349  ASP A CG  1 
ATOM   2771  O  OD1 . ASP A 1 349  ? 55.547  111.851 162.428 1.00 67.70  ? 349  ASP A OD1 1 
ATOM   2772  O  OD2 . ASP A 1 349  ? 57.649  111.778 163.098 1.00 67.78  ? 349  ASP A OD2 1 
ATOM   2773  N  N   . VAL A 1 350  ? 56.596  110.151 167.627 1.00 68.17  ? 350  VAL A N   1 
ATOM   2774  C  CA  . VAL A 1 350  ? 56.287  109.284 168.770 1.00 69.08  ? 350  VAL A CA  1 
ATOM   2775  C  C   . VAL A 1 350  ? 57.014  109.768 170.034 1.00 69.67  ? 350  VAL A C   1 
ATOM   2776  O  O   . VAL A 1 350  ? 56.975  109.114 171.082 1.00 70.15  ? 350  VAL A O   1 
ATOM   2777  C  CB  . VAL A 1 350  ? 56.649  107.804 168.453 1.00 68.50  ? 350  VAL A CB  1 
ATOM   2778  C  CG1 . VAL A 1 350  ? 56.503  106.902 169.693 1.00 70.15  ? 350  VAL A CG1 1 
ATOM   2779  C  CG2 . VAL A 1 350  ? 55.784  107.278 167.323 1.00 68.18  ? 350  VAL A CG2 1 
ATOM   2780  N  N   . ARG A 1 351  ? 57.654  110.932 169.931 1.00 69.90  ? 351  ARG A N   1 
ATOM   2781  C  CA  . ARG A 1 351  ? 58.504  111.477 170.996 1.00 70.55  ? 351  ARG A CA  1 
ATOM   2782  C  C   . ARG A 1 351  ? 59.523  110.435 171.433 1.00 69.70  ? 351  ARG A C   1 
ATOM   2783  O  O   . ARG A 1 351  ? 59.738  110.210 172.629 1.00 70.38  ? 351  ARG A O   1 
ATOM   2784  C  CB  . ARG A 1 351  ? 57.683  111.975 172.190 1.00 72.03  ? 351  ARG A CB  1 
ATOM   2785  C  CG  . ARG A 1 351  ? 56.719  113.103 171.866 1.00 75.12  ? 351  ARG A CG  1 
ATOM   2786  C  CD  . ARG A 1 351  ? 55.741  113.317 173.018 1.00 81.03  ? 351  ARG A CD  1 
ATOM   2787  N  NE  . ARG A 1 351  ? 56.080  114.466 173.863 1.00 84.71  ? 351  ARG A NE  1 
ATOM   2788  C  CZ  . ARG A 1 351  ? 55.879  114.520 175.182 1.00 87.64  ? 351  ARG A CZ  1 
ATOM   2789  N  NH1 . ARG A 1 351  ? 55.371  113.475 175.836 1.00 88.82  ? 351  ARG A NH1 1 
ATOM   2790  N  NH2 . ARG A 1 351  ? 56.210  115.615 175.858 1.00 88.74  ? 351  ARG A NH2 1 
ATOM   2791  N  N   . PHE A 1 352  ? 60.127  109.780 170.446 1.00 68.22  ? 352  PHE A N   1 
ATOM   2792  C  CA  . PHE A 1 352  ? 61.180  108.820 170.710 1.00 67.23  ? 352  PHE A CA  1 
ATOM   2793  C  C   . PHE A 1 352  ? 62.537  109.497 170.604 1.00 66.79  ? 352  PHE A C   1 
ATOM   2794  O  O   . PHE A 1 352  ? 62.738  110.396 169.778 1.00 66.40  ? 352  PHE A O   1 
ATOM   2795  C  CB  . PHE A 1 352  ? 61.104  107.630 169.751 1.00 66.24  ? 352  PHE A CB  1 
ATOM   2796  C  CG  . PHE A 1 352  ? 62.274  106.701 169.867 1.00 64.51  ? 352  PHE A CG  1 
ATOM   2797  C  CD1 . PHE A 1 352  ? 62.311  105.739 170.870 1.00 63.23  ? 352  PHE A CD1 1 
ATOM   2798  C  CD2 . PHE A 1 352  ? 63.363  106.823 169.003 1.00 63.23  ? 352  PHE A CD2 1 
ATOM   2799  C  CE1 . PHE A 1 352  ? 63.387  104.891 171.002 1.00 62.29  ? 352  PHE A CE1 1 
ATOM   2800  C  CE2 . PHE A 1 352  ? 64.455  105.981 169.126 1.00 62.68  ? 352  PHE A CE2 1 
ATOM   2801  C  CZ  . PHE A 1 352  ? 64.463  105.007 170.135 1.00 63.13  ? 352  PHE A CZ  1 
ATOM   2802  N  N   . GLU A 1 353  ? 63.472  109.046 171.434 1.00 66.85  ? 353  GLU A N   1 
ATOM   2803  C  CA  . GLU A 1 353  ? 64.799  109.631 171.478 1.00 66.55  ? 353  GLU A CA  1 
ATOM   2804  C  C   . GLU A 1 353  ? 65.795  108.658 172.105 1.00 65.88  ? 353  GLU A C   1 
ATOM   2805  O  O   . GLU A 1 353  ? 65.468  107.978 173.084 1.00 66.41  ? 353  GLU A O   1 
ATOM   2806  C  CB  . GLU A 1 353  ? 64.732  110.909 172.306 1.00 67.66  ? 353  GLU A CB  1 
ATOM   2807  C  CG  . GLU A 1 353  ? 65.945  111.784 172.232 1.00 68.71  ? 353  GLU A CG  1 
ATOM   2808  C  CD  . GLU A 1 353  ? 65.991  112.756 173.381 1.00 71.89  ? 353  GLU A CD  1 
ATOM   2809  O  OE1 . GLU A 1 353  ? 64.944  113.381 173.673 1.00 73.68  ? 353  GLU A OE1 1 
ATOM   2810  O  OE2 . GLU A 1 353  ? 67.070  112.887 173.998 1.00 73.13  ? 353  GLU A OE2 1 
ATOM   2811  N  N   . THR A 1 354  ? 67.000  108.599 171.536 1.00 64.37  ? 354  THR A N   1 
ATOM   2812  C  CA  . THR A 1 354  ? 68.113  107.839 172.116 1.00 63.72  ? 354  THR A CA  1 
ATOM   2813  C  C   . THR A 1 354  ? 69.472  108.361 171.670 1.00 63.10  ? 354  THR A C   1 
ATOM   2814  O  O   . THR A 1 354  ? 69.715  108.568 170.475 1.00 62.25  ? 354  THR A O   1 
ATOM   2815  C  CB  . THR A 1 354  ? 68.041  106.300 171.840 1.00 63.34  ? 354  THR A CB  1 
ATOM   2816  O  OG1 . THR A 1 354  ? 69.219  105.675 172.358 1.00 62.88  ? 354  THR A OG1 1 
ATOM   2817  C  CG2 . THR A 1 354  ? 67.934  105.968 170.347 1.00 61.74  ? 354  THR A CG2 1 
ATOM   2818  N  N   . THR A 1 355  ? 70.355  108.564 172.640 1.00 63.35  ? 355  THR A N   1 
ATOM   2819  C  CA  . THR A 1 355  ? 71.715  109.005 172.363 1.00 62.88  ? 355  THR A CA  1 
ATOM   2820  C  C   . THR A 1 355  ? 72.680  107.867 172.675 1.00 62.46  ? 355  THR A C   1 
ATOM   2821  O  O   . THR A 1 355  ? 72.964  107.583 173.843 1.00 63.14  ? 355  THR A O   1 
ATOM   2822  C  CB  . THR A 1 355  ? 72.070  110.273 173.163 1.00 63.64  ? 355  THR A CB  1 
ATOM   2823  O  OG1 . THR A 1 355  ? 71.085  111.281 172.906 1.00 64.83  ? 355  THR A OG1 1 
ATOM   2824  C  CG2 . THR A 1 355  ? 73.444  110.803 172.762 1.00 63.11  ? 355  THR A CG2 1 
ATOM   2825  N  N   . THR A 1 356  ? 73.174  107.228 171.616 1.00 61.17  ? 356  THR A N   1 
ATOM   2826  C  CA  . THR A 1 356  ? 73.935  105.992 171.731 1.00 60.85  ? 356  THR A CA  1 
ATOM   2827  C  C   . THR A 1 356  ? 74.980  105.867 170.618 1.00 60.09  ? 356  THR A C   1 
ATOM   2828  O  O   . THR A 1 356  ? 75.099  106.754 169.784 1.00 60.00  ? 356  THR A O   1 
ATOM   2829  C  CB  . THR A 1 356  ? 72.995  104.757 171.754 1.00 60.76  ? 356  THR A CB  1 
ATOM   2830  O  OG1 . THR A 1 356  ? 73.749  103.597 172.103 1.00 60.66  ? 356  THR A OG1 1 
ATOM   2831  C  CG2 . THR A 1 356  ? 72.317  104.532 170.400 1.00 59.41  ? 356  THR A CG2 1 
ATOM   2832  N  N   . THR A 1 357  ? 75.749  104.781 170.619 1.00 59.96  ? 357  THR A N   1 
ATOM   2833  C  CA  . THR A 1 357  ? 76.767  104.562 169.591 1.00 59.40  ? 357  THR A CA  1 
ATOM   2834  C  C   . THR A 1 357  ? 76.441  103.306 168.792 1.00 58.86  ? 357  THR A C   1 
ATOM   2835  O  O   . THR A 1 357  ? 75.854  102.363 169.333 1.00 59.12  ? 357  THR A O   1 
ATOM   2836  C  CB  . THR A 1 357  ? 78.201  104.441 170.184 1.00 59.57  ? 357  THR A CB  1 
ATOM   2837  O  OG1 . THR A 1 357  ? 78.319  103.235 170.951 1.00 60.18  ? 357  THR A OG1 1 
ATOM   2838  C  CG2 . THR A 1 357  ? 78.520  105.628 171.075 1.00 60.43  ? 357  THR A CG2 1 
ATOM   2839  N  N   . SER A 1 358  ? 76.815  103.297 167.511 1.00 57.82  ? 358  SER A N   1 
ATOM   2840  C  CA  . SER A 1 358  ? 76.592  102.122 166.666 1.00 57.24  ? 358  SER A CA  1 
ATOM   2841  C  C   . SER A 1 358  ? 77.296  100.907 167.257 1.00 57.39  ? 358  SER A C   1 
ATOM   2842  O  O   . SER A 1 358  ? 78.456  100.992 167.674 1.00 57.05  ? 358  SER A O   1 
ATOM   2843  C  CB  . SER A 1 358  ? 77.052  102.367 165.228 1.00 56.05  ? 358  SER A CB  1 
ATOM   2844  O  OG  . SER A 1 358  ? 78.426  102.702 165.186 1.00 55.82  ? 358  SER A OG  1 
ATOM   2845  N  N   . ASP A 1 359  ? 76.581  99.786  167.302 1.00 57.80  ? 359  ASP A N   1 
ATOM   2846  C  CA  . ASP A 1 359  ? 77.094  98.573  167.935 1.00 58.43  ? 359  ASP A CA  1 
ATOM   2847  C  C   . ASP A 1 359  ? 78.193  97.905  167.100 1.00 57.97  ? 359  ASP A C   1 
ATOM   2848  O  O   . ASP A 1 359  ? 78.566  98.404  166.036 1.00 57.28  ? 359  ASP A O   1 
ATOM   2849  C  CB  . ASP A 1 359  ? 75.953  97.600  168.295 1.00 58.69  ? 359  ASP A CB  1 
ATOM   2850  C  CG  . ASP A 1 359  ? 75.290  96.964  167.074 1.00 58.53  ? 359  ASP A CG  1 
ATOM   2851  O  OD1 . ASP A 1 359  ? 75.854  97.014  165.965 1.00 58.55  ? 359  ASP A OD1 1 
ATOM   2852  O  OD2 . ASP A 1 359  ? 74.190  96.392  167.227 1.00 59.23  ? 359  ASP A OD2 1 
ATOM   2853  N  N   . ASN A 1 360  ? 78.702  96.779  167.599 1.00 58.59  ? 360  ASN A N   1 
ATOM   2854  C  CA  . ASN A 1 360  ? 79.785  96.028  166.959 1.00 58.10  ? 360  ASN A CA  1 
ATOM   2855  C  C   . ASN A 1 360  ? 79.486  95.617  165.501 1.00 56.80  ? 360  ASN A C   1 
ATOM   2856  O  O   . ASN A 1 360  ? 80.405  95.434  164.698 1.00 56.42  ? 360  ASN A O   1 
ATOM   2857  C  CB  . ASN A 1 360  ? 80.169  94.827  167.841 1.00 58.95  ? 360  ASN A CB  1 
ATOM   2858  C  CG  . ASN A 1 360  ? 81.121  93.867  167.153 1.00 60.32  ? 360  ASN A CG  1 
ATOM   2859  O  OD1 . ASN A 1 360  ? 82.273  94.208  166.855 1.00 62.39  ? 360  ASN A OD1 1 
ATOM   2860  N  ND2 . ASN A 1 360  ? 80.640  92.656  166.885 1.00 61.78  ? 360  ASN A ND2 1 
ATOM   2861  N  N   . ASP A 1 361  ? 78.204  95.496  165.161 1.00 56.18  ? 361  ASP A N   1 
ATOM   2862  C  CA  . ASP A 1 361  ? 77.785  95.222  163.783 1.00 54.77  ? 361  ASP A CA  1 
ATOM   2863  C  C   . ASP A 1 361  ? 77.552  96.481  162.958 1.00 53.54  ? 361  ASP A C   1 
ATOM   2864  O  O   . ASP A 1 361  ? 77.195  96.393  161.782 1.00 53.06  ? 361  ASP A O   1 
ATOM   2865  C  CB  . ASP A 1 361  ? 76.499  94.406  163.776 1.00 55.45  ? 361  ASP A CB  1 
ATOM   2866  C  CG  . ASP A 1 361  ? 76.685  93.035  164.355 1.00 56.64  ? 361  ASP A CG  1 
ATOM   2867  O  OD1 . ASP A 1 361  ? 76.003  92.717  165.359 1.00 58.14  ? 361  ASP A OD1 1 
ATOM   2868  O  OD2 . ASP A 1 361  ? 77.519  92.285  163.805 1.00 57.39  ? 361  ASP A OD2 1 
ATOM   2869  N  N   . GLY A 1 362  ? 77.741  97.643  163.576 1.00 52.79  ? 362  GLY A N   1 
ATOM   2870  C  CA  . GLY A 1 362  ? 77.511  98.921  162.908 1.00 51.36  ? 362  GLY A CA  1 
ATOM   2871  C  C   . GLY A 1 362  ? 76.046  99.319  162.869 1.00 50.98  ? 362  GLY A C   1 
ATOM   2872  O  O   . GLY A 1 362  ? 75.641  100.163 162.059 1.00 50.76  ? 362  GLY A O   1 
ATOM   2873  N  N   . LEU A 1 363  ? 75.249  98.722  163.750 1.00 50.60  ? 363  LEU A N   1 
ATOM   2874  C  CA  . LEU A 1 363  ? 73.826  99.009  163.796 1.00 50.22  ? 363  LEU A CA  1 
ATOM   2875  C  C   . LEU A 1 363  ? 73.451  99.848  165.003 1.00 50.59  ? 363  LEU A C   1 
ATOM   2876  O  O   . LEU A 1 363  ? 74.112  99.793  166.035 1.00 50.95  ? 363  LEU A O   1 
ATOM   2877  C  CB  . LEU A 1 363  ? 73.019  97.710  163.803 1.00 50.15  ? 363  LEU A CB  1 
ATOM   2878  C  CG  . LEU A 1 363  ? 73.263  96.728  162.657 1.00 49.47  ? 363  LEU A CG  1 
ATOM   2879  C  CD1 . LEU A 1 363  ? 72.480  95.449  162.870 1.00 48.88  ? 363  LEU A CD1 1 
ATOM   2880  C  CD2 . LEU A 1 363  ? 72.944  97.345  161.286 1.00 48.90  ? 363  LEU A CD2 1 
ATOM   2881  N  N   . ILE A 1 364  ? 72.407  100.651 164.851 1.00 50.53  ? 364  ILE A N   1 
ATOM   2882  C  CA  . ILE A 1 364  ? 71.659  101.145 165.996 1.00 51.38  ? 364  ILE A CA  1 
ATOM   2883  C  C   . ILE A 1 364  ? 70.240  100.609 165.812 1.00 52.13  ? 364  ILE A C   1 
ATOM   2884  O  O   . ILE A 1 364  ? 69.492  101.069 164.947 1.00 51.99  ? 364  ILE A O   1 
ATOM   2885  C  CB  . ILE A 1 364  ? 71.698  102.681 166.132 1.00 51.36  ? 364  ILE A CB  1 
ATOM   2886  C  CG1 . ILE A 1 364  ? 73.087  103.131 166.575 1.00 50.18  ? 364  ILE A CG1 1 
ATOM   2887  C  CG2 . ILE A 1 364  ? 70.665  103.159 167.152 1.00 52.03  ? 364  ILE A CG2 1 
ATOM   2888  C  CD1 . ILE A 1 364  ? 73.311  104.617 166.468 1.00 48.88  ? 364  ILE A CD1 1 
ATOM   2889  N  N   . LYS A 1 365  ? 69.900  99.595  166.599 1.00 52.94  ? 365  LYS A N   1 
ATOM   2890  C  CA  . LYS A 1 365  ? 68.623  98.921  166.452 1.00 53.94  ? 365  LYS A CA  1 
ATOM   2891  C  C   . LYS A 1 365  ? 67.503  99.751  167.050 1.00 54.89  ? 365  LYS A C   1 
ATOM   2892  O  O   . LYS A 1 365  ? 67.644  100.325 168.133 1.00 55.57  ? 365  LYS A O   1 
ATOM   2893  C  CB  . LYS A 1 365  ? 68.659  97.531  167.087 1.00 54.36  ? 365  LYS A CB  1 
ATOM   2894  C  CG  . LYS A 1 365  ? 69.545  96.550  166.359 1.00 54.68  ? 365  LYS A CG  1 
ATOM   2895  C  CD  . LYS A 1 365  ? 69.027  95.152  166.573 1.00 57.38  ? 365  LYS A CD  1 
ATOM   2896  C  CE  . LYS A 1 365  ? 70.069  94.101  166.221 1.00 58.63  ? 365  LYS A CE  1 
ATOM   2897  N  NZ  . LYS A 1 365  ? 69.642  92.763  166.737 1.00 60.37  ? 365  LYS A NZ  1 
ATOM   2898  N  N   . LEU A 1 366  ? 66.390  99.811  166.330 1.00 55.18  ? 366  LEU A N   1 
ATOM   2899  C  CA  . LEU A 1 366  ? 65.246  100.583 166.764 1.00 56.33  ? 366  LEU A CA  1 
ATOM   2900  C  C   . LEU A 1 366  ? 63.990  99.734  166.745 1.00 57.52  ? 366  LEU A C   1 
ATOM   2901  O  O   . LEU A 1 366  ? 63.761  98.978  165.796 1.00 57.29  ? 366  LEU A O   1 
ATOM   2902  C  CB  . LEU A 1 366  ? 65.058  101.809 165.869 1.00 55.82  ? 366  LEU A CB  1 
ATOM   2903  C  CG  . LEU A 1 366  ? 66.169  102.860 165.817 1.00 54.96  ? 366  LEU A CG  1 
ATOM   2904  C  CD1 . LEU A 1 366  ? 65.748  103.973 164.880 1.00 53.77  ? 366  LEU A CD1 1 
ATOM   2905  C  CD2 . LEU A 1 366  ? 66.484  103.418 167.206 1.00 56.17  ? 366  LEU A CD2 1 
ATOM   2906  N  N   . GLU A 1 367  ? 63.202  99.846  167.812 1.00 59.08  ? 367  GLU A N   1 
ATOM   2907  C  CA  . GLU A 1 367  ? 61.843  99.328  167.843 1.00 60.54  ? 367  GLU A CA  1 
ATOM   2908  C  C   . GLU A 1 367  ? 60.928  100.500 168.146 1.00 61.50  ? 367  GLU A C   1 
ATOM   2909  O  O   . GLU A 1 367  ? 60.815  100.935 169.292 1.00 62.37  ? 367  GLU A O   1 
ATOM   2910  C  CB  . GLU A 1 367  ? 61.673  98.215  168.886 1.00 61.24  ? 367  GLU A CB  1 
ATOM   2911  C  CG  . GLU A 1 367  ? 60.274  97.580  168.873 1.00 63.20  ? 367  GLU A CG  1 
ATOM   2912  C  CD  . GLU A 1 367  ? 60.112  96.425  169.863 1.00 65.91  ? 367  GLU A CD  1 
ATOM   2913  O  OE1 . GLU A 1 367  ? 60.032  95.262  169.406 1.00 65.96  ? 367  GLU A OE1 1 
ATOM   2914  O  OE2 . GLU A 1 367  ? 60.061  96.676  171.093 1.00 67.28  ? 367  GLU A OE2 1 
ATOM   2915  N  N   . LEU A 1 368  ? 60.295  101.021 167.104 1.00 61.86  ? 368  LEU A N   1 
ATOM   2916  C  CA  . LEU A 1 368  ? 59.421  102.175 167.238 1.00 63.07  ? 368  LEU A CA  1 
ATOM   2917  C  C   . LEU A 1 368  ? 57.975  101.741 167.426 1.00 64.84  ? 368  LEU A C   1 
ATOM   2918  O  O   . LEU A 1 368  ? 57.586  100.642 167.016 1.00 64.79  ? 368  LEU A O   1 
ATOM   2919  C  CB  . LEU A 1 368  ? 59.564  103.088 166.023 1.00 62.05  ? 368  LEU A CB  1 
ATOM   2920  C  CG  . LEU A 1 368  ? 60.988  103.583 165.737 1.00 60.90  ? 368  LEU A CG  1 
ATOM   2921  C  CD1 . LEU A 1 368  ? 61.077  104.276 164.377 1.00 59.55  ? 368  LEU A CD1 1 
ATOM   2922  C  CD2 . LEU A 1 368  ? 61.495  104.494 166.847 1.00 60.18  ? 368  LEU A CD2 1 
ATOM   2923  N  N   . GLN A 1 369  ? 57.181  102.604 168.053 1.00 66.66  ? 369  GLN A N   1 
ATOM   2924  C  CA  . GLN A 1 369  ? 55.776  102.288 168.293 1.00 68.78  ? 369  GLN A CA  1 
ATOM   2925  C  C   . GLN A 1 369  ? 54.761  103.358 167.850 1.00 69.79  ? 369  GLN A C   1 
ATOM   2926  O  O   . GLN A 1 369  ? 54.365  104.223 168.647 1.00 70.50  ? 369  GLN A O   1 
ATOM   2927  C  CB  . GLN A 1 369  ? 55.553  101.880 169.749 1.00 69.67  ? 369  GLN A CB  1 
ATOM   2928  C  CG  . GLN A 1 369  ? 55.342  100.389 169.913 1.00 71.48  ? 369  GLN A CG  1 
ATOM   2929  C  CD  . GLN A 1 369  ? 53.965  99.921  169.439 1.00 73.83  ? 369  GLN A CD  1 
ATOM   2930  O  OE1 . GLN A 1 369  ? 53.741  98.724  169.263 1.00 74.82  ? 369  GLN A OE1 1 
ATOM   2931  N  NE2 . GLN A 1 369  ? 53.041  100.859 169.234 1.00 74.33  ? 369  GLN A NE2 1 
ATOM   2932  N  N   . PRO A 1 370  ? 54.328  103.285 166.576 1.00 69.97  ? 370  PRO A N   1 
ATOM   2933  C  CA  . PRO A 1 370  ? 53.276  104.153 166.071 1.00 71.13  ? 370  PRO A CA  1 
ATOM   2934  C  C   . PRO A 1 370  ? 51.921  103.816 166.678 1.00 73.21  ? 370  PRO A C   1 
ATOM   2935  O  O   . PRO A 1 370  ? 51.553  102.640 166.771 1.00 73.76  ? 370  PRO A O   1 
ATOM   2936  C  CB  . PRO A 1 370  ? 53.264  103.847 164.569 1.00 70.34  ? 370  PRO A CB  1 
ATOM   2937  C  CG  . PRO A 1 370  ? 53.807  102.480 164.452 1.00 69.37  ? 370  PRO A CG  1 
ATOM   2938  C  CD  . PRO A 1 370  ? 54.831  102.371 165.533 1.00 69.08  ? 370  PRO A CD  1 
ATOM   2939  N  N   . SER A 1 371  ? 51.200  104.847 167.110 1.00 74.89  ? 371  SER A N   1 
ATOM   2940  C  CA  . SER A 1 371  ? 49.788  104.718 167.427 1.00 76.97  ? 371  SER A CA  1 
ATOM   2941  C  C   . SER A 1 371  ? 49.045  104.793 166.101 1.00 77.56  ? 371  SER A C   1 
ATOM   2942  O  O   . SER A 1 371  ? 49.619  105.239 165.105 1.00 76.85  ? 371  SER A O   1 
ATOM   2943  C  CB  . SER A 1 371  ? 49.346  105.845 168.358 1.00 77.79  ? 371  SER A CB  1 
ATOM   2944  O  OG  . SER A 1 371  ? 49.559  107.108 167.756 1.00 77.76  ? 371  SER A OG  1 
ATOM   2945  N  N   . GLU A 1 372  ? 47.789  104.350 166.070 1.00 79.44  ? 372  GLU A N   1 
ATOM   2946  C  CA  . GLU A 1 372  ? 46.984  104.413 164.837 1.00 80.43  ? 372  GLU A CA  1 
ATOM   2947  C  C   . GLU A 1 372  ? 46.943  105.827 164.272 1.00 80.24  ? 372  GLU A C   1 
ATOM   2948  O  O   . GLU A 1 372  ? 46.998  106.010 163.054 1.00 80.03  ? 372  GLU A O   1 
ATOM   2949  C  CB  . GLU A 1 372  ? 45.560  103.890 165.045 1.00 82.07  ? 372  GLU A CB  1 
ATOM   2950  C  CG  . GLU A 1 372  ? 45.461  102.413 165.420 1.00 84.28  ? 372  GLU A CG  1 
ATOM   2951  C  CD  . GLU A 1 372  ? 45.450  102.186 166.929 1.00 87.83  ? 372  GLU A CD  1 
ATOM   2952  O  OE1 . GLU A 1 372  ? 44.443  101.627 167.440 1.00 89.79  ? 372  GLU A OE1 1 
ATOM   2953  O  OE2 . GLU A 1 372  ? 46.440  102.572 167.601 1.00 88.12  ? 372  GLU A OE2 1 
ATOM   2954  N  N   . GLY A 1 373  ? 46.869  106.819 165.160 1.00 80.67  ? 373  GLY A N   1 
ATOM   2955  C  CA  . GLY A 1 373  ? 46.971  108.225 164.764 1.00 80.67  ? 373  GLY A CA  1 
ATOM   2956  C  C   . GLY A 1 373  ? 48.137  108.492 163.819 1.00 79.35  ? 373  GLY A C   1 
ATOM   2957  O  O   . GLY A 1 373  ? 47.957  109.086 162.753 1.00 79.16  ? 373  GLY A O   1 
ATOM   2958  N  N   . THR A 1 374  ? 49.319  108.008 164.205 1.00 78.35  ? 374  THR A N   1 
ATOM   2959  C  CA  . THR A 1 374  ? 50.581  108.294 163.530 1.00 76.91  ? 374  THR A CA  1 
ATOM   2960  C  C   . THR A 1 374  ? 50.524  108.047 162.022 1.00 76.39  ? 374  THR A C   1 
ATOM   2961  O  O   . THR A 1 374  ? 50.186  106.945 161.581 1.00 76.56  ? 374  THR A O   1 
ATOM   2962  C  CB  . THR A 1 374  ? 51.729  107.482 164.157 1.00 76.14  ? 374  THR A CB  1 
ATOM   2963  O  OG1 . THR A 1 374  ? 51.672  107.605 165.582 1.00 76.49  ? 374  THR A OG1 1 
ATOM   2964  C  CG2 . THR A 1 374  ? 53.079  107.983 163.668 1.00 75.14  ? 374  THR A CG2 1 
ATOM   2965  N  N   . GLU A 1 375  ? 50.854  109.086 161.251 1.00 75.68  ? 375  GLU A N   1 
ATOM   2966  C  CA  . GLU A 1 375  ? 50.821  109.046 159.785 1.00 75.06  ? 375  GLU A CA  1 
ATOM   2967  C  C   . GLU A 1 375  ? 52.152  108.605 159.157 1.00 73.17  ? 375  GLU A C   1 
ATOM   2968  O  O   . GLU A 1 375  ? 52.176  107.818 158.203 1.00 72.82  ? 375  GLU A O   1 
ATOM   2969  C  CB  . GLU A 1 375  ? 50.412  110.416 159.229 1.00 75.85  ? 375  GLU A CB  1 
ATOM   2970  C  CG  . GLU A 1 375  ? 48.901  110.653 159.177 1.00 78.91  ? 375  GLU A CG  1 
ATOM   2971  C  CD  . GLU A 1 375  ? 48.218  109.870 158.054 1.00 81.00  ? 375  GLU A CD  1 
ATOM   2972  O  OE1 . GLU A 1 375  ? 47.300  109.066 158.368 1.00 82.61  ? 375  GLU A OE1 1 
ATOM   2973  O  OE2 . GLU A 1 375  ? 48.598  110.052 156.866 1.00 79.97  ? 375  GLU A OE2 1 
ATOM   2974  N  N   . GLN A 1 376  ? 53.257  109.137 159.669 1.00 71.74  ? 376  GLN A N   1 
ATOM   2975  C  CA  . GLN A 1 376  ? 54.574  108.685 159.245 1.00 69.81  ? 376  GLN A CA  1 
ATOM   2976  C  C   . GLN A 1 376  ? 55.572  108.718 160.394 1.00 68.64  ? 376  GLN A C   1 
ATOM   2977  O  O   . GLN A 1 376  ? 55.285  109.266 161.467 1.00 69.02  ? 376  GLN A O   1 
ATOM   2978  C  CB  . GLN A 1 376  ? 55.077  109.482 158.038 1.00 69.46  ? 376  GLN A CB  1 
ATOM   2979  C  CG  . GLN A 1 376  ? 55.601  110.879 158.337 1.00 70.78  ? 376  GLN A CG  1 
ATOM   2980  C  CD  . GLN A 1 376  ? 56.272  111.511 157.123 1.00 71.71  ? 376  GLN A CD  1 
ATOM   2981  O  OE1 . GLN A 1 376  ? 56.291  110.930 156.036 1.00 71.90  ? 376  GLN A OE1 1 
ATOM   2982  N  NE2 . GLN A 1 376  ? 56.827  112.706 157.305 1.00 72.31  ? 376  GLN A NE2 1 
ATOM   2983  N  N   . LEU A 1 377  ? 56.732  108.107 160.166 1.00 66.55  ? 377  LEU A N   1 
ATOM   2984  C  CA  . LEU A 1 377  ? 57.797  108.093 161.157 1.00 65.34  ? 377  LEU A CA  1 
ATOM   2985  C  C   . LEU A 1 377  ? 59.028  108.788 160.591 1.00 64.08  ? 377  LEU A C   1 
ATOM   2986  O  O   . LEU A 1 377  ? 59.655  108.303 159.640 1.00 63.16  ? 377  LEU A O   1 
ATOM   2987  C  CB  . LEU A 1 377  ? 58.119  106.659 161.606 1.00 64.99  ? 377  LEU A CB  1 
ATOM   2988  C  CG  . LEU A 1 377  ? 57.011  105.833 162.288 1.00 65.28  ? 377  LEU A CG  1 
ATOM   2989  C  CD1 . LEU A 1 377  ? 57.351  104.347 162.271 1.00 63.90  ? 377  LEU A CD1 1 
ATOM   2990  C  CD2 . LEU A 1 377  ? 56.711  106.301 163.714 1.00 64.37  ? 377  LEU A CD2 1 
ATOM   2991  N  N   . SER A 1 378  ? 59.354  109.942 161.168 1.00 63.65  ? 378  SER A N   1 
ATOM   2992  C  CA  . SER A 1 378  ? 60.500  110.717 160.718 1.00 62.55  ? 378  SER A CA  1 
ATOM   2993  C  C   . SER A 1 378  ? 61.728  110.394 161.538 1.00 61.26  ? 378  SER A C   1 
ATOM   2994  O  O   . SER A 1 378  ? 61.850  110.799 162.702 1.00 61.39  ? 378  SER A O   1 
ATOM   2995  C  CB  . SER A 1 378  ? 60.191  112.208 160.751 1.00 63.39  ? 378  SER A CB  1 
ATOM   2996  O  OG  . SER A 1 378  ? 59.259  112.511 159.733 1.00 65.04  ? 378  SER A OG  1 
ATOM   2997  N  N   . ILE A 1 379  ? 62.636  109.657 160.911 1.00 59.46  ? 379  ILE A N   1 
ATOM   2998  C  CA  . ILE A 1 379  ? 63.798  109.127 161.603 1.00 58.22  ? 379  ILE A CA  1 
ATOM   2999  C  C   . ILE A 1 379  ? 65.001  110.018 161.344 1.00 57.45  ? 379  ILE A C   1 
ATOM   3000  O  O   . ILE A 1 379  ? 65.568  110.023 160.257 1.00 56.51  ? 379  ILE A O   1 
ATOM   3001  C  CB  . ILE A 1 379  ? 64.044  107.650 161.228 1.00 57.44  ? 379  ILE A CB  1 
ATOM   3002  C  CG1 . ILE A 1 379  ? 62.792  106.833 161.571 1.00 57.99  ? 379  ILE A CG1 1 
ATOM   3003  C  CG2 . ILE A 1 379  ? 65.288  107.110 161.930 1.00 56.01  ? 379  ILE A CG2 1 
ATOM   3004  C  CD1 . ILE A 1 379  ? 62.756  105.425 161.000 1.00 58.68  ? 379  ILE A CD1 1 
ATOM   3005  N  N   . HIS A 1 380  ? 65.354  110.796 162.358 1.00 57.80  ? 380  HIS A N   1 
ATOM   3006  C  CA  . HIS A 1 380  ? 66.444  111.749 162.268 1.00 57.51  ? 380  HIS A CA  1 
ATOM   3007  C  C   . HIS A 1 380  ? 67.613  111.194 163.041 1.00 57.16  ? 380  HIS A C   1 
ATOM   3008  O  O   . HIS A 1 380  ? 67.434  110.604 164.106 1.00 57.80  ? 380  HIS A O   1 
ATOM   3009  C  CB  . HIS A 1 380  ? 66.039  113.092 162.886 1.00 58.39  ? 380  HIS A CB  1 
ATOM   3010  C  CG  . HIS A 1 380  ? 65.141  113.926 162.022 1.00 59.23  ? 380  HIS A CG  1 
ATOM   3011  N  ND1 . HIS A 1 380  ? 64.370  113.398 161.007 1.00 59.67  ? 380  HIS A ND1 1 
ATOM   3012  C  CD2 . HIS A 1 380  ? 64.877  115.254 162.039 1.00 60.30  ? 380  HIS A CD2 1 
ATOM   3013  C  CE1 . HIS A 1 380  ? 63.683  114.366 160.427 1.00 60.28  ? 380  HIS A CE1 1 
ATOM   3014  N  NE2 . HIS A 1 380  ? 63.971  115.502 161.036 1.00 60.76  ? 380  HIS A NE2 1 
ATOM   3015  N  N   . PHE A 1 381  ? 68.807  111.376 162.498 1.00 56.20  ? 381  PHE A N   1 
ATOM   3016  C  CA  . PHE A 1 381  ? 70.033  111.101 163.226 1.00 55.89  ? 381  PHE A CA  1 
ATOM   3017  C  C   . PHE A 1 381  ? 70.984  112.274 163.037 1.00 56.09  ? 381  PHE A C   1 
ATOM   3018  O  O   . PHE A 1 381  ? 71.235  112.711 161.906 1.00 55.65  ? 381  PHE A O   1 
ATOM   3019  C  CB  . PHE A 1 381  ? 70.692  109.799 162.753 1.00 54.99  ? 381  PHE A CB  1 
ATOM   3020  C  CG  . PHE A 1 381  ? 72.029  109.534 163.389 1.00 53.61  ? 381  PHE A CG  1 
ATOM   3021  C  CD1 . PHE A 1 381  ? 72.119  108.808 164.569 1.00 53.20  ? 381  PHE A CD1 1 
ATOM   3022  C  CD2 . PHE A 1 381  ? 73.196  110.025 162.817 1.00 51.35  ? 381  PHE A CD2 1 
ATOM   3023  C  CE1 . PHE A 1 381  ? 73.353  108.570 165.166 1.00 52.70  ? 381  PHE A CE1 1 
ATOM   3024  C  CE2 . PHE A 1 381  ? 74.429  109.794 163.409 1.00 51.25  ? 381  PHE A CE2 1 
ATOM   3025  C  CZ  . PHE A 1 381  ? 74.511  109.064 164.583 1.00 51.49  ? 381  PHE A CZ  1 
ATOM   3026  N  N   . ASN A 1 382  ? 71.521  112.761 164.149 1.00 56.65  ? 382  ASN A N   1 
ATOM   3027  C  CA  . ASN A 1 382  ? 72.404  113.907 164.143 1.00 56.90  ? 382  ASN A CA  1 
ATOM   3028  C  C   . ASN A 1 382  ? 73.629  113.637 165.003 1.00 57.43  ? 382  ASN A C   1 
ATOM   3029  O  O   . ASN A 1 382  ? 73.506  113.277 166.174 1.00 58.06  ? 382  ASN A O   1 
ATOM   3030  C  CB  . ASN A 1 382  ? 71.656  115.152 164.638 1.00 57.59  ? 382  ASN A CB  1 
ATOM   3031  C  CG  . ASN A 1 382  ? 70.625  115.660 163.634 1.00 57.40  ? 382  ASN A CG  1 
ATOM   3032  O  OD1 . ASN A 1 382  ? 70.959  116.383 162.689 1.00 58.05  ? 382  ASN A OD1 1 
ATOM   3033  N  ND2 . ASN A 1 382  ? 69.368  115.300 163.844 1.00 57.03  ? 382  ASN A ND2 1 
ATOM   3034  N  N   . ALA A 1 383  ? 74.811  113.790 164.414 1.00 57.42  ? 383  ALA A N   1 
ATOM   3035  C  CA  . ALA A 1 383  ? 76.055  113.665 165.163 1.00 58.25  ? 383  ALA A CA  1 
ATOM   3036  C  C   . ALA A 1 383  ? 76.702  115.032 165.356 1.00 59.32  ? 383  ALA A C   1 
ATOM   3037  O  O   . ALA A 1 383  ? 76.477  115.949 164.560 1.00 59.58  ? 383  ALA A O   1 
ATOM   3038  C  CB  . ALA A 1 383  ? 77.003  112.709 164.473 1.00 57.19  ? 383  ALA A CB  1 
ATOM   3039  N  N   . VAL A 1 384  ? 77.500  115.171 166.414 1.00 60.51  ? 384  VAL A N   1 
ATOM   3040  C  CA  . VAL A 1 384  ? 78.140  116.456 166.733 1.00 61.45  ? 384  VAL A CA  1 
ATOM   3041  C  C   . VAL A 1 384  ? 79.121  116.935 165.643 1.00 61.11  ? 384  VAL A C   1 
ATOM   3042  O  O   . VAL A 1 384  ? 79.424  118.130 165.558 1.00 61.81  ? 384  VAL A O   1 
ATOM   3043  C  CB  . VAL A 1 384  ? 78.786  116.469 168.157 1.00 62.19  ? 384  VAL A CB  1 
ATOM   3044  C  CG1 . VAL A 1 384  ? 77.756  116.069 169.206 1.00 62.89  ? 384  VAL A CG1 1 
ATOM   3045  C  CG2 . VAL A 1 384  ? 80.020  115.558 168.236 1.00 61.91  ? 384  VAL A CG2 1 
ATOM   3046  N  N   . ASP A 1 385  ? 79.583  116.013 164.797 1.00 60.22  ? 385  ASP A N   1 
ATOM   3047  C  CA  . ASP A 1 385  ? 80.465  116.363 163.681 1.00 59.63  ? 385  ASP A CA  1 
ATOM   3048  C  C   . ASP A 1 385  ? 79.747  117.102 162.542 1.00 59.25  ? 385  ASP A C   1 
ATOM   3049  O  O   . ASP A 1 385  ? 80.374  117.441 161.528 1.00 58.86  ? 385  ASP A O   1 
ATOM   3050  C  CB  . ASP A 1 385  ? 81.192  115.119 163.141 1.00 58.92  ? 385  ASP A CB  1 
ATOM   3051  C  CG  . ASP A 1 385  ? 80.235  114.023 162.671 1.00 58.89  ? 385  ASP A CG  1 
ATOM   3052  O  OD1 . ASP A 1 385  ? 79.010  114.268 162.601 1.00 58.56  ? 385  ASP A OD1 1 
ATOM   3053  O  OD2 . ASP A 1 385  ? 80.718  112.905 162.375 1.00 58.89  ? 385  ASP A OD2 1 
ATOM   3054  N  N   . GLY A 1 386  ? 78.442  117.333 162.708 1.00 59.33  ? 386  GLY A N   1 
ATOM   3055  C  CA  . GLY A 1 386  ? 77.622  118.018 161.699 1.00 58.91  ? 386  GLY A CA  1 
ATOM   3056  C  C   . GLY A 1 386  ? 76.840  117.090 160.781 1.00 58.14  ? 386  GLY A C   1 
ATOM   3057  O  O   . GLY A 1 386  ? 75.969  117.534 160.025 1.00 57.88  ? 386  GLY A O   1 
ATOM   3058  N  N   . PHE A 1 387  ? 77.164  115.798 160.849 1.00 57.59  ? 387  PHE A N   1 
ATOM   3059  C  CA  . PHE A 1 387  ? 76.502  114.756 160.067 1.00 56.71  ? 387  PHE A CA  1 
ATOM   3060  C  C   . PHE A 1 387  ? 75.038  114.628 160.448 1.00 57.34  ? 387  PHE A C   1 
ATOM   3061  O  O   . PHE A 1 387  ? 74.684  114.686 161.628 1.00 57.81  ? 387  PHE A O   1 
ATOM   3062  C  CB  . PHE A 1 387  ? 77.201  113.414 160.301 1.00 56.12  ? 387  PHE A CB  1 
ATOM   3063  C  CG  . PHE A 1 387  ? 76.620  112.268 159.511 1.00 54.65  ? 387  PHE A CG  1 
ATOM   3064  C  CD1 . PHE A 1 387  ? 77.132  111.939 158.263 1.00 52.21  ? 387  PHE A CD1 1 
ATOM   3065  C  CD2 . PHE A 1 387  ? 75.580  111.505 160.025 1.00 53.86  ? 387  PHE A CD2 1 
ATOM   3066  C  CE1 . PHE A 1 387  ? 76.612  110.883 157.533 1.00 50.42  ? 387  PHE A CE1 1 
ATOM   3067  C  CE2 . PHE A 1 387  ? 75.054  110.451 159.295 1.00 52.61  ? 387  PHE A CE2 1 
ATOM   3068  C  CZ  . PHE A 1 387  ? 75.579  110.143 158.043 1.00 51.39  ? 387  PHE A CZ  1 
ATOM   3069  N  N   . PHE A 1 388  ? 74.192  114.453 159.440 1.00 57.28  ? 388  PHE A N   1 
ATOM   3070  C  CA  . PHE A 1 388  ? 72.776  114.216 159.669 1.00 58.36  ? 388  PHE A CA  1 
ATOM   3071  C  C   . PHE A 1 388  ? 72.212  113.282 158.616 1.00 57.55  ? 388  PHE A C   1 
ATOM   3072  O  O   . PHE A 1 388  ? 72.602  113.343 157.455 1.00 56.95  ? 388  PHE A O   1 
ATOM   3073  C  CB  . PHE A 1 388  ? 71.983  115.532 159.729 1.00 59.45  ? 388  PHE A CB  1 
ATOM   3074  C  CG  . PHE A 1 388  ? 71.896  116.265 158.413 1.00 61.49  ? 388  PHE A CG  1 
ATOM   3075  C  CD1 . PHE A 1 388  ? 72.961  117.065 157.962 1.00 63.91  ? 388  PHE A CD1 1 
ATOM   3076  C  CD2 . PHE A 1 388  ? 70.750  116.174 157.628 1.00 63.35  ? 388  PHE A CD2 1 
ATOM   3077  C  CE1 . PHE A 1 388  ? 72.889  117.755 156.739 1.00 64.09  ? 388  PHE A CE1 1 
ATOM   3078  C  CE2 . PHE A 1 388  ? 70.665  116.860 156.401 1.00 65.15  ? 388  PHE A CE2 1 
ATOM   3079  C  CZ  . PHE A 1 388  ? 71.738  117.653 155.958 1.00 64.63  ? 388  PHE A CZ  1 
ATOM   3080  N  N   . PHE A 1 389  ? 71.309  112.405 159.043 1.00 57.64  ? 389  PHE A N   1 
ATOM   3081  C  CA  . PHE A 1 389  ? 70.606  111.498 158.142 1.00 57.09  ? 389  PHE A CA  1 
ATOM   3082  C  C   . PHE A 1 389  ? 69.127  111.472 158.513 1.00 58.00  ? 389  PHE A C   1 
ATOM   3083  O  O   . PHE A 1 389  ? 68.779  111.314 159.682 1.00 58.68  ? 389  PHE A O   1 
ATOM   3084  C  CB  . PHE A 1 389  ? 71.206  110.086 158.204 1.00 56.32  ? 389  PHE A CB  1 
ATOM   3085  C  CG  . PHE A 1 389  ? 70.347  109.026 157.556 1.00 55.34  ? 389  PHE A CG  1 
ATOM   3086  C  CD1 . PHE A 1 389  ? 70.547  108.668 156.225 1.00 53.45  ? 389  PHE A CD1 1 
ATOM   3087  C  CD2 . PHE A 1 389  ? 69.338  108.386 158.277 1.00 54.11  ? 389  PHE A CD2 1 
ATOM   3088  C  CE1 . PHE A 1 389  ? 69.754  107.697 155.628 1.00 52.16  ? 389  PHE A CE1 1 
ATOM   3089  C  CE2 . PHE A 1 389  ? 68.541  107.423 157.682 1.00 53.08  ? 389  PHE A CE2 1 
ATOM   3090  C  CZ  . PHE A 1 389  ? 68.751  107.076 156.356 1.00 52.27  ? 389  PHE A CZ  1 
ATOM   3091  N  N   . TYR A 1 390  ? 68.269  111.643 157.512 1.00 58.36  ? 390  TYR A N   1 
ATOM   3092  C  CA  . TYR A 1 390  ? 66.824  111.609 157.694 1.00 59.35  ? 390  TYR A CA  1 
ATOM   3093  C  C   . TYR A 1 390  ? 66.213  110.677 156.666 1.00 58.85  ? 390  TYR A C   1 
ATOM   3094  O  O   . TYR A 1 390  ? 66.576  110.721 155.484 1.00 58.40  ? 390  TYR A O   1 
ATOM   3095  C  CB  . TYR A 1 390  ? 66.198  113.002 157.529 1.00 60.50  ? 390  TYR A CB  1 
ATOM   3096  C  CG  . TYR A 1 390  ? 66.865  114.148 158.289 1.00 62.43  ? 390  TYR A CG  1 
ATOM   3097  C  CD1 . TYR A 1 390  ? 66.970  115.418 157.712 1.00 63.58  ? 390  TYR A CD1 1 
ATOM   3098  C  CD2 . TYR A 1 390  ? 67.379  113.972 159.584 1.00 63.87  ? 390  TYR A CD2 1 
ATOM   3099  C  CE1 . TYR A 1 390  ? 67.570  116.478 158.399 1.00 64.45  ? 390  TYR A CE1 1 
ATOM   3100  C  CE2 . TYR A 1 390  ? 67.988  115.023 160.277 1.00 64.64  ? 390  TYR A CE2 1 
ATOM   3101  C  CZ  . TYR A 1 390  ? 68.080  116.274 159.679 1.00 65.30  ? 390  TYR A CZ  1 
ATOM   3102  O  OH  . TYR A 1 390  ? 68.678  117.323 160.356 1.00 65.11  ? 390  TYR A OH  1 
ATOM   3103  N  N   . GLU A 1 391  ? 65.300  109.825 157.118 1.00 58.93  ? 391  GLU A N   1 
ATOM   3104  C  CA  . GLU A 1 391  ? 64.457  109.052 156.213 1.00 58.94  ? 391  GLU A CA  1 
ATOM   3105  C  C   . GLU A 1 391  ? 63.048  108.961 156.792 1.00 60.22  ? 391  GLU A C   1 
ATOM   3106  O  O   . GLU A 1 391  ? 62.863  108.732 157.990 1.00 60.90  ? 391  GLU A O   1 
ATOM   3107  C  CB  . GLU A 1 391  ? 65.047  107.660 155.928 1.00 58.12  ? 391  GLU A CB  1 
ATOM   3108  C  CG  . GLU A 1 391  ? 64.287  106.836 154.865 1.00 57.37  ? 391  GLU A CG  1 
ATOM   3109  C  CD  . GLU A 1 391  ? 65.067  105.614 154.356 1.00 56.79  ? 391  GLU A CD  1 
ATOM   3110  O  OE1 . GLU A 1 391  ? 66.244  105.765 153.953 1.00 55.45  ? 391  GLU A OE1 1 
ATOM   3111  O  OE2 . GLU A 1 391  ? 64.500  104.497 154.345 1.00 56.70  ? 391  GLU A OE2 1 
ATOM   3112  N  N   . ASP A 1 392  ? 62.055  109.165 155.938 1.00 60.83  ? 392  ASP A N   1 
ATOM   3113  C  CA  . ASP A 1 392  ? 60.672  109.015 156.346 1.00 61.96  ? 392  ASP A CA  1 
ATOM   3114  C  C   . ASP A 1 392  ? 60.172  107.609 156.044 1.00 62.10  ? 392  ASP A C   1 
ATOM   3115  O  O   . ASP A 1 392  ? 60.438  107.066 154.970 1.00 61.54  ? 392  ASP A O   1 
ATOM   3116  C  CB  . ASP A 1 392  ? 59.796  110.066 155.659 1.00 62.35  ? 392  ASP A CB  1 
ATOM   3117  C  CG  . ASP A 1 392  ? 59.924  111.443 156.296 1.00 63.00  ? 392  ASP A CG  1 
ATOM   3118  O  OD1 . ASP A 1 392  ? 60.227  111.528 157.510 1.00 62.56  ? 392  ASP A OD1 1 
ATOM   3119  O  OD2 . ASP A 1 392  ? 59.708  112.446 155.579 1.00 63.34  ? 392  ASP A OD2 1 
ATOM   3120  N  N   . VAL A 1 393  ? 59.466  107.022 157.008 1.00 62.91  ? 393  VAL A N   1 
ATOM   3121  C  CA  . VAL A 1 393  ? 58.755  105.769 156.791 1.00 63.45  ? 393  VAL A CA  1 
ATOM   3122  C  C   . VAL A 1 393  ? 57.254  106.055 156.714 1.00 64.84  ? 393  VAL A C   1 
ATOM   3123  O  O   . VAL A 1 393  ? 56.690  106.678 157.616 1.00 65.34  ? 393  VAL A O   1 
ATOM   3124  C  CB  . VAL A 1 393  ? 59.032  104.737 157.918 1.00 63.51  ? 393  VAL A CB  1 
ATOM   3125  C  CG1 . VAL A 1 393  ? 58.290  103.438 157.649 1.00 63.26  ? 393  VAL A CG1 1 
ATOM   3126  C  CG2 . VAL A 1 393  ? 60.524  104.465 158.053 1.00 62.42  ? 393  VAL A CG2 1 
ATOM   3127  N  N   . ASN A 1 394  ? 56.619  105.601 155.634 1.00 65.57  ? 394  ASN A N   1 
ATOM   3128  C  CA  . ASN A 1 394  ? 55.167  105.754 155.462 1.00 67.41  ? 394  ASN A CA  1 
ATOM   3129  C  C   . ASN A 1 394  ? 54.365  104.543 155.940 1.00 68.74  ? 394  ASN A C   1 
ATOM   3130  O  O   . ASN A 1 394  ? 54.911  103.453 156.131 1.00 68.37  ? 394  ASN A O   1 
ATOM   3131  C  CB  . ASN A 1 394  ? 54.817  106.061 153.999 1.00 67.25  ? 394  ASN A CB  1 
ATOM   3132  C  CG  . ASN A 1 394  ? 55.631  107.218 153.426 1.00 66.04  ? 394  ASN A CG  1 
ATOM   3133  O  OD1 . ASN A 1 394  ? 56.294  107.078 152.392 1.00 62.96  ? 394  ASN A OD1 1 
ATOM   3134  N  ND2 . ASN A 1 394  ? 55.588  108.365 154.104 1.00 66.00  ? 394  ASN A ND2 1 
ATOM   3135  N  N   . LYS A 1 395  ? 53.064  104.745 156.136 1.00 70.82  ? 395  LYS A N   1 
ATOM   3136  C  CA  . LYS A 1 395  ? 52.169  103.672 156.570 1.00 72.34  ? 395  LYS A CA  1 
ATOM   3137  C  C   . LYS A 1 395  ? 51.725  102.783 155.407 1.00 72.90  ? 395  LYS A C   1 
ATOM   3138  O  O   . LYS A 1 395  ? 51.730  103.211 154.249 1.00 72.85  ? 395  LYS A O   1 
ATOM   3139  C  CB  . LYS A 1 395  ? 50.959  104.246 157.313 1.00 73.49  ? 395  LYS A CB  1 
ATOM   3140  C  CG  . LYS A 1 395  ? 49.942  104.957 156.444 1.00 74.77  ? 395  LYS A CG  1 
ATOM   3141  C  CD  . LYS A 1 395  ? 48.757  105.426 157.280 1.00 77.29  ? 395  LYS A CD  1 
ATOM   3142  C  CE  . LYS A 1 395  ? 47.618  105.923 156.403 1.00 78.33  ? 395  LYS A CE  1 
ATOM   3143  N  NZ  . LYS A 1 395  ? 46.338  105.920 157.167 1.00 80.31  ? 395  LYS A NZ  1 
ATOM   3144  N  N   . VAL A 1 396  ? 51.353  101.544 155.722 1.00 73.98  ? 396  VAL A N   1 
ATOM   3145  C  CA  . VAL A 1 396  ? 50.899  100.589 154.708 1.00 74.75  ? 396  VAL A CA  1 
ATOM   3146  C  C   . VAL A 1 396  ? 49.624  101.056 153.993 1.00 76.14  ? 396  VAL A C   1 
ATOM   3147  O  O   . VAL A 1 396  ? 48.618  101.397 154.630 1.00 77.13  ? 396  VAL A O   1 
ATOM   3148  C  CB  . VAL A 1 396  ? 50.699  99.162  155.291 1.00 75.06  ? 396  VAL A CB  1 
ATOM   3149  C  CG1 . VAL A 1 396  ? 50.062  98.234  154.257 1.00 75.29  ? 396  VAL A CG1 1 
ATOM   3150  C  CG2 . VAL A 1 396  ? 52.026  98.587  155.766 1.00 73.93  ? 396  VAL A CG2 1 
ATOM   3151  N  N   . GLU A 1 397  ? 49.698  101.074 152.663 1.00 76.46  ? 397  GLU A N   1 
ATOM   3152  C  CA  . GLU A 1 397  ? 48.561  101.383 151.803 1.00 77.89  ? 397  GLU A CA  1 
ATOM   3153  C  C   . GLU A 1 397  ? 48.170  100.139 150.999 1.00 78.09  ? 397  GLU A C   1 
ATOM   3154  O  O   . GLU A 1 397  ? 48.936  99.670  150.146 1.00 77.50  ? 397  GLU A O   1 
ATOM   3155  C  CB  . GLU A 1 397  ? 48.900  102.555 150.874 1.00 77.55  ? 397  GLU A CB  1 
ATOM   3156  C  CG  . GLU A 1 397  ? 47.749  103.516 150.652 1.00 80.07  ? 397  GLU A CG  1 
ATOM   3157  C  CD  . GLU A 1 397  ? 47.321  104.234 151.926 1.00 81.88  ? 397  GLU A CD  1 
ATOM   3158  O  OE1 . GLU A 1 397  ? 47.974  105.232 152.306 1.00 81.92  ? 397  GLU A OE1 1 
ATOM   3159  O  OE2 . GLU A 1 397  ? 46.322  103.802 152.538 1.00 83.34  ? 397  GLU A OE2 1 
ATOM   3160  N  N   . THR A 1 398  ? 46.974  99.624  151.284 1.00 79.22  ? 398  THR A N   1 
ATOM   3161  C  CA  . THR A 1 398  ? 46.471  98.335  150.771 1.00 79.67  ? 398  THR A CA  1 
ATOM   3162  C  C   . THR A 1 398  ? 46.725  98.066  149.278 1.00 79.50  ? 398  THR A C   1 
ATOM   3163  O  O   . THR A 1 398  ? 47.047  96.937  148.893 1.00 79.37  ? 398  THR A O   1 
ATOM   3164  C  CB  . THR A 1 398  ? 44.956  98.177  151.101 1.00 81.05  ? 398  THR A CB  1 
ATOM   3165  O  OG1 . THR A 1 398  ? 44.771  98.231  152.522 1.00 80.87  ? 398  THR A OG1 1 
ATOM   3166  C  CG2 . THR A 1 398  ? 44.390  96.864  150.570 1.00 81.44  ? 398  THR A CG2 1 
ATOM   3167  N  N   . VAL A 1 399  ? 46.595  99.109  148.457 1.00 79.64  ? 399  VAL A N   1 
ATOM   3168  C  CA  . VAL A 1 399  ? 46.690  98.994  146.999 1.00 79.49  ? 399  VAL A CA  1 
ATOM   3169  C  C   . VAL A 1 399  ? 48.087  98.579  146.527 1.00 78.16  ? 399  VAL A C   1 
ATOM   3170  O  O   . VAL A 1 399  ? 48.219  97.829  145.554 1.00 78.00  ? 399  VAL A O   1 
ATOM   3171  C  CB  . VAL A 1 399  ? 46.270  100.320 146.283 1.00 79.96  ? 399  VAL A CB  1 
ATOM   3172  C  CG1 . VAL A 1 399  ? 46.049  100.093 144.785 1.00 80.05  ? 399  VAL A CG1 1 
ATOM   3173  C  CG2 . VAL A 1 399  ? 45.007  100.908 146.909 1.00 81.43  ? 399  VAL A CG2 1 
ATOM   3174  N  N   . THR A 1 400  ? 49.119  99.051  147.227 1.00 75.54  ? 400  THR A N   1 
ATOM   3175  C  CA  . THR A 1 400  ? 50.504  98.898  146.760 1.00 74.54  ? 400  THR A CA  1 
ATOM   3176  C  C   . THR A 1 400  ? 51.459  98.290  147.784 1.00 72.28  ? 400  THR A C   1 
ATOM   3177  O  O   . THR A 1 400  ? 52.502  97.741  147.417 1.00 71.01  ? 400  THR A O   1 
ATOM   3178  C  CB  . THR A 1 400  ? 51.093  100.263 146.322 1.00 76.77  ? 400  THR A CB  1 
ATOM   3179  O  OG1 . THR A 1 400  ? 50.805  101.250 147.324 1.00 77.87  ? 400  THR A OG1 1 
ATOM   3180  C  CG2 . THR A 1 400  ? 50.509  100.709 144.972 1.00 78.55  ? 400  THR A CG2 1 
ATOM   3181  N  N   . ASP A 1 401  ? 51.098  98.395  149.060 1.00 71.75  ? 401  ASP A N   1 
ATOM   3182  C  CA  . ASP A 1 401  ? 52.028  98.117  150.156 1.00 70.23  ? 401  ASP A CA  1 
ATOM   3183  C  C   . ASP A 1 401  ? 51.752  96.824  150.926 1.00 68.24  ? 401  ASP A C   1 
ATOM   3184  O  O   . ASP A 1 401  ? 52.629  96.321  151.627 1.00 67.02  ? 401  ASP A O   1 
ATOM   3185  C  CB  . ASP A 1 401  ? 52.049  99.297  151.134 1.00 71.53  ? 401  ASP A CB  1 
ATOM   3186  C  CG  . ASP A 1 401  ? 52.395  100.612 150.465 1.00 73.37  ? 401  ASP A CG  1 
ATOM   3187  O  OD1 . ASP A 1 401  ? 53.171  100.611 149.483 1.00 72.94  ? 401  ASP A OD1 1 
ATOM   3188  O  OD2 . ASP A 1 401  ? 51.896  101.654 150.937 1.00 74.80  ? 401  ASP A OD2 1 
ATOM   3189  N  N   . ALA A 1 402  ? 50.535  96.300  150.799 1.00 68.09  ? 402  ALA A N   1 
ATOM   3190  C  CA  . ALA A 1 402  ? 50.121  95.094  151.515 1.00 66.41  ? 402  ALA A CA  1 
ATOM   3191  C  C   . ALA A 1 402  ? 51.094  93.940  151.317 1.00 64.52  ? 402  ALA A C   1 
ATOM   3192  O  O   . ALA A 1 402  ? 51.598  93.727  150.213 1.00 64.73  ? 402  ALA A O   1 
ATOM   3193  C  CB  . ALA A 1 402  ? 48.723  94.684  151.095 1.00 66.82  ? 402  ALA A CB  1 
ATOM   3194  N  N   . TYR A 1 403  ? 51.378  93.226  152.404 1.00 63.14  ? 403  TYR A N   1 
ATOM   3195  C  CA  . TYR A 1 403  ? 52.173  91.998  152.362 1.00 61.12  ? 403  TYR A CA  1 
ATOM   3196  C  C   . TYR A 1 403  ? 51.563  90.922  153.270 1.00 60.56  ? 403  TYR A C   1 
ATOM   3197  O  O   . TYR A 1 403  ? 50.699  91.194  154.114 1.00 60.69  ? 403  TYR A O   1 
ATOM   3198  C  CB  . TYR A 1 403  ? 53.648  92.252  152.737 1.00 60.18  ? 403  TYR A CB  1 
ATOM   3199  C  CG  . TYR A 1 403  ? 53.862  92.789  154.146 1.00 60.66  ? 403  TYR A CG  1 
ATOM   3200  C  CD1 . TYR A 1 403  ? 54.111  94.145  154.361 1.00 61.34  ? 403  TYR A CD1 1 
ATOM   3201  C  CD2 . TYR A 1 403  ? 53.805  91.943  155.268 1.00 59.13  ? 403  TYR A CD2 1 
ATOM   3202  C  CE1 . TYR A 1 403  ? 54.295  94.651  155.649 1.00 61.69  ? 403  TYR A CE1 1 
ATOM   3203  C  CE2 . TYR A 1 403  ? 53.986  92.442  156.561 1.00 59.17  ? 403  TYR A CE2 1 
ATOM   3204  C  CZ  . TYR A 1 403  ? 54.233  93.799  156.741 1.00 61.15  ? 403  TYR A CZ  1 
ATOM   3205  O  OH  . TYR A 1 403  ? 54.420  94.320  158.004 1.00 62.32  ? 403  TYR A OH  1 
ATOM   3206  N  N   . ILE A 1 404  ? 52.030  89.698  153.058 1.00 59.69  ? 404  ILE A N   1 
ATOM   3207  C  CA  . ILE A 1 404  ? 51.743  88.562  153.901 1.00 59.07  ? 404  ILE A CA  1 
ATOM   3208  C  C   . ILE A 1 404  ? 53.088  87.877  154.156 1.00 58.62  ? 404  ILE A C   1 
ATOM   3209  O  O   . ILE A 1 404  ? 53.872  87.650  153.231 1.00 58.23  ? 404  ILE A O   1 
ATOM   3210  C  CB  . ILE A 1 404  ? 50.704  87.619  153.237 1.00 59.03  ? 404  ILE A CB  1 
ATOM   3211  C  CG1 . ILE A 1 404  ? 50.148  86.618  154.251 1.00 58.79  ? 404  ILE A CG1 1 
ATOM   3212  C  CG2 . ILE A 1 404  ? 51.282  86.920  152.017 1.00 58.03  ? 404  ILE A CG2 1 
ATOM   3213  C  CD1 . ILE A 1 404  ? 48.917  85.883  153.781 1.00 58.01  ? 404  ILE A CD1 1 
ATOM   3214  N  N   . LYS A 1 405  ? 53.384  87.595  155.417 1.00 59.19  ? 405  LYS A N   1 
ATOM   3215  C  CA  . LYS A 1 405  ? 54.635  86.925  155.746 1.00 59.24  ? 405  LYS A CA  1 
ATOM   3216  C  C   . LYS A 1 405  ? 54.407  85.622  156.502 1.00 59.23  ? 405  LYS A C   1 
ATOM   3217  O  O   . LYS A 1 405  ? 53.380  85.433  157.151 1.00 59.69  ? 405  LYS A O   1 
ATOM   3218  C  CB  . LYS A 1 405  ? 55.587  87.855  156.501 1.00 59.68  ? 405  LYS A CB  1 
ATOM   3219  C  CG  . LYS A 1 405  ? 55.001  88.487  157.762 1.00 62.70  ? 405  LYS A CG  1 
ATOM   3220  C  CD  . LYS A 1 405  ? 56.099  89.107  158.639 1.00 66.34  ? 405  LYS A CD  1 
ATOM   3221  C  CE  . LYS A 1 405  ? 56.660  88.113  159.661 1.00 66.38  ? 405  LYS A CE  1 
ATOM   3222  N  NZ  . LYS A 1 405  ? 58.001  88.553  160.137 1.00 67.61  ? 405  LYS A NZ  1 
ATOM   3223  N  N   . LEU A 1 406  ? 55.378  84.726  156.383 1.00 59.13  ? 406  LEU A N   1 
ATOM   3224  C  CA  . LEU A 1 406  ? 55.325  83.407  156.981 1.00 59.73  ? 406  LEU A CA  1 
ATOM   3225  C  C   . LEU A 1 406  ? 56.468  83.273  157.969 1.00 60.25  ? 406  LEU A C   1 
ATOM   3226  O  O   . LEU A 1 406  ? 57.587  83.713  157.708 1.00 60.06  ? 406  LEU A O   1 
ATOM   3227  C  CB  . LEU A 1 406  ? 55.447  82.348  155.891 1.00 59.25  ? 406  LEU A CB  1 
ATOM   3228  C  CG  . LEU A 1 406  ? 55.200  80.873  156.206 1.00 59.60  ? 406  LEU A CG  1 
ATOM   3229  C  CD1 . LEU A 1 406  ? 53.784  80.639  156.715 1.00 60.43  ? 406  LEU A CD1 1 
ATOM   3230  C  CD2 . LEU A 1 406  ? 55.460  80.058  154.942 1.00 59.22  ? 406  LEU A CD2 1 
ATOM   3231  N  N   . GLU A 1 407  ? 56.186  82.675  159.113 1.00 61.54  ? 407  GLU A N   1 
ATOM   3232  C  CA  . GLU A 1 407  ? 57.192  82.538  160.140 1.00 62.75  ? 407  GLU A CA  1 
ATOM   3233  C  C   . GLU A 1 407  ? 57.056  81.182  160.807 1.00 63.58  ? 407  GLU A C   1 
ATOM   3234  O  O   . GLU A 1 407  ? 56.013  80.856  161.374 1.00 64.45  ? 407  GLU A O   1 
ATOM   3235  C  CB  . GLU A 1 407  ? 57.075  83.674  161.157 1.00 63.66  ? 407  GLU A CB  1 
ATOM   3236  C  CG  . GLU A 1 407  ? 58.328  83.902  161.997 1.00 66.05  ? 407  GLU A CG  1 
ATOM   3237  C  CD  . GLU A 1 407  ? 58.166  85.042  162.997 1.00 69.90  ? 407  GLU A CD  1 
ATOM   3238  O  OE1 . GLU A 1 407  ? 57.523  86.059  162.636 1.00 70.71  ? 407  GLU A OE1 1 
ATOM   3239  O  OE2 . GLU A 1 407  ? 58.681  84.921  164.140 1.00 70.75  ? 407  GLU A OE2 1 
ATOM   3240  N  N   . LEU A 1 408  ? 58.118  80.391  160.711 1.00 63.92  ? 408  LEU A N   1 
ATOM   3241  C  CA  . LEU A 1 408  ? 58.179  79.085  161.333 1.00 65.17  ? 408  LEU A CA  1 
ATOM   3242  C  C   . LEU A 1 408  ? 58.202  79.235  162.855 1.00 66.56  ? 408  LEU A C   1 
ATOM   3243  O  O   . LEU A 1 408  ? 59.042  79.941  163.404 1.00 66.65  ? 408  LEU A O   1 
ATOM   3244  C  CB  . LEU A 1 408  ? 59.408  78.331  160.826 1.00 64.94  ? 408  LEU A CB  1 
ATOM   3245  C  CG  . LEU A 1 408  ? 59.575  76.889  161.313 1.00 67.15  ? 408  LEU A CG  1 
ATOM   3246  C  CD1 . LEU A 1 408  ? 58.416  75.995  160.854 1.00 67.64  ? 408  LEU A CD1 1 
ATOM   3247  C  CD2 . LEU A 1 408  ? 60.925  76.326  160.874 1.00 68.06  ? 408  LEU A CD2 1 
ATOM   3248  N  N   . LYS A 1 409  ? 57.261  78.580  163.526 1.00 67.97  ? 409  LYS A N   1 
ATOM   3249  C  CA  . LYS A 1 409  ? 57.083  78.747  164.966 1.00 69.82  ? 409  LYS A CA  1 
ATOM   3250  C  C   . LYS A 1 409  ? 57.599  77.578  165.803 1.00 71.75  ? 409  LYS A C   1 
ATOM   3251  O  O   . LYS A 1 409  ? 57.780  77.704  167.017 1.00 73.06  ? 409  LYS A O   1 
ATOM   3252  C  CB  . LYS A 1 409  ? 55.612  79.026  165.288 1.00 70.10  ? 409  LYS A CB  1 
ATOM   3253  C  CG  . LYS A 1 409  ? 55.221  80.478  165.166 1.00 68.96  ? 409  LYS A CG  1 
ATOM   3254  C  CD  . LYS A 1 409  ? 56.025  81.323  166.129 1.00 69.94  ? 409  LYS A CD  1 
ATOM   3255  C  CE  . LYS A 1 409  ? 55.869  82.799  165.847 1.00 70.13  ? 409  LYS A CE  1 
ATOM   3256  N  NZ  . LYS A 1 409  ? 56.909  83.575  166.578 1.00 71.37  ? 409  LYS A NZ  1 
ATOM   3257  N  N   . SER A 1 410  ? 57.836  76.447  165.144 1.00 72.43  ? 410  SER A N   1 
ATOM   3258  C  CA  . SER A 1 410  ? 58.311  75.229  165.793 1.00 74.73  ? 410  SER A CA  1 
ATOM   3259  C  C   . SER A 1 410  ? 59.240  74.500  164.827 1.00 74.24  ? 410  SER A C   1 
ATOM   3260  O  O   . SER A 1 410  ? 59.144  74.712  163.629 1.00 72.98  ? 410  SER A O   1 
ATOM   3261  C  CB  . SER A 1 410  ? 57.117  74.333  166.137 1.00 76.22  ? 410  SER A CB  1 
ATOM   3262  O  OG  . SER A 1 410  ? 56.468  73.902  164.947 1.00 76.59  ? 410  SER A OG  1 
ATOM   3263  N  N   . PRO A 1 411  ? 60.122  73.614  165.331 1.00 75.83  ? 411  PRO A N   1 
ATOM   3264  C  CA  . PRO A 1 411  ? 61.002  72.957  164.363 1.00 75.48  ? 411  PRO A CA  1 
ATOM   3265  C  C   . PRO A 1 411  ? 60.250  71.891  163.564 1.00 75.93  ? 411  PRO A C   1 
ATOM   3266  O  O   . PRO A 1 411  ? 59.129  71.524  163.919 1.00 77.00  ? 411  PRO A O   1 
ATOM   3267  C  CB  . PRO A 1 411  ? 62.105  72.330  165.236 1.00 77.00  ? 411  PRO A CB  1 
ATOM   3268  C  CG  . PRO A 1 411  ? 61.810  72.758  166.663 1.00 78.26  ? 411  PRO A CG  1 
ATOM   3269  C  CD  . PRO A 1 411  ? 60.366  73.135  166.703 1.00 77.92  ? 411  PRO A CD  1 
ATOM   3270  N  N   . ILE A 1 412  ? 60.869  71.407  162.495 1.00 75.47  ? 412  ILE A N   1 
ATOM   3271  C  CA  . ILE A 1 412  ? 60.197  70.545  161.532 1.00 75.94  ? 412  ILE A CA  1 
ATOM   3272  C  C   . ILE A 1 412  ? 60.705  69.101  161.614 1.00 77.92  ? 412  ILE A C   1 
ATOM   3273  O  O   . ILE A 1 412  ? 61.873  68.822  161.320 1.00 77.76  ? 412  ILE A O   1 
ATOM   3274  C  CB  . ILE A 1 412  ? 60.327  71.146  160.117 1.00 74.14  ? 412  ILE A CB  1 
ATOM   3275  C  CG1 . ILE A 1 412  ? 59.367  72.326  159.982 1.00 73.08  ? 412  ILE A CG1 1 
ATOM   3276  C  CG2 . ILE A 1 412  ? 60.048  70.121  159.034 1.00 74.67  ? 412  ILE A CG2 1 
ATOM   3277  C  CD1 . ILE A 1 412  ? 59.770  73.297  158.926 1.00 72.62  ? 412  ILE A CD1 1 
ATOM   3278  N  N   . LYS A 1 413  ? 59.816  68.196  162.027 1.00 79.98  ? 413  LYS A N   1 
ATOM   3279  C  CA  . LYS A 1 413  ? 60.172  66.795  162.247 1.00 82.34  ? 413  LYS A CA  1 
ATOM   3280  C  C   . LYS A 1 413  ? 59.230  65.816  161.545 1.00 83.83  ? 413  LYS A C   1 
ATOM   3281  O  O   . LYS A 1 413  ? 58.076  66.150  161.264 1.00 83.70  ? 413  LYS A O   1 
ATOM   3282  C  CB  . LYS A 1 413  ? 60.230  66.487  163.746 1.00 84.25  ? 413  LYS A CB  1 
ATOM   3283  C  CG  . LYS A 1 413  ? 61.382  67.149  164.480 1.00 84.18  ? 413  LYS A CG  1 
ATOM   3284  C  CD  . LYS A 1 413  ? 61.422  66.719  165.938 1.00 87.49  ? 413  LYS A CD  1 
ATOM   3285  C  CE  . LYS A 1 413  ? 62.475  67.495  166.723 1.00 87.75  ? 413  LYS A CE  1 
ATOM   3286  N  NZ  . LYS A 1 413  ? 62.578  67.013  168.131 1.00 90.63  ? 413  LYS A NZ  1 
ATOM   3287  N  N   . ARG A 1 414  ? 59.746  64.607  161.293 1.00 85.66  ? 414  ARG A N   1 
ATOM   3288  C  CA  . ARG A 1 414  ? 59.067  63.501  160.578 1.00 87.48  ? 414  ARG A CA  1 
ATOM   3289  C  C   . ARG A 1 414  ? 57.533  63.468  160.638 1.00 88.00  ? 414  ARG A C   1 
ATOM   3290  O  O   . ARG A 1 414  ? 56.865  63.825  159.665 1.00 87.58  ? 414  ARG A O   1 
ATOM   3291  C  CB  . ARG A 1 414  ? 59.635  62.135  161.017 1.00 90.37  ? 414  ARG A CB  1 
ATOM   3292  C  CG  . ARG A 1 414  ? 61.058  61.833  160.527 1.00 91.11  ? 414  ARG A CG  1 
ATOM   3293  C  CD  . ARG A 1 414  ? 61.092  61.278  159.101 1.00 92.94  ? 414  ARG A CD  1 
ATOM   3294  N  NE  . ARG A 1 414  ? 61.003  59.817  159.054 1.00 97.26  ? 414  ARG A NE  1 
ATOM   3295  C  CZ  . ARG A 1 414  ? 60.014  59.127  158.484 1.00 99.70  ? 414  ARG A CZ  1 
ATOM   3296  N  NH1 . ARG A 1 414  ? 59.000  59.745  157.885 1.00 98.82  ? 414  ARG A NH1 1 
ATOM   3297  N  NH2 . ARG A 1 414  ? 60.044  57.802  158.505 1.00 103.11 ? 414  ARG A NH2 1 
ATOM   3298  N  N   . ASN A 1 415  ? 56.975  63.019  161.755 1.00 89.06  ? 415  ASN A N   1 
ATOM   3299  C  CA  . ASN A 1 415  ? 55.525  62.887  161.857 1.00 89.59  ? 415  ASN A CA  1 
ATOM   3300  C  C   . ASN A 1 415  ? 54.947  63.792  162.938 1.00 88.38  ? 415  ASN A C   1 
ATOM   3301  O  O   . ASN A 1 415  ? 54.225  63.346  163.833 1.00 90.30  ? 415  ASN A O   1 
ATOM   3302  C  CB  . ASN A 1 415  ? 55.121  61.421  162.067 1.00 93.15  ? 415  ASN A CB  1 
ATOM   3303  C  CG  . ASN A 1 415  ? 55.212  60.596  160.786 1.00 94.07  ? 415  ASN A CG  1 
ATOM   3304  O  OD1 . ASN A 1 415  ? 56.195  60.672  160.038 1.00 92.43  ? 415  ASN A OD1 1 
ATOM   3305  N  ND2 . ASN A 1 415  ? 54.183  59.796  160.535 1.00 96.42  ? 415  ASN A ND2 1 
ATOM   3306  N  N   . LYS A 1 416  ? 55.284  65.073  162.829 1.00 84.92  ? 416  LYS A N   1 
ATOM   3307  C  CA  . LYS A 1 416  ? 54.884  66.085  163.797 1.00 83.18  ? 416  LYS A CA  1 
ATOM   3308  C  C   . LYS A 1 416  ? 54.166  67.236  163.110 1.00 80.25  ? 416  LYS A C   1 
ATOM   3309  O  O   . LYS A 1 416  ? 54.231  67.392  161.885 1.00 78.80  ? 416  LYS A O   1 
ATOM   3310  C  CB  . LYS A 1 416  ? 56.108  66.613  164.561 1.00 82.57  ? 416  LYS A CB  1 
ATOM   3311  C  CG  . LYS A 1 416  ? 56.861  65.544  165.341 1.00 85.31  ? 416  LYS A CG  1 
ATOM   3312  C  CD  . LYS A 1 416  ? 56.076  65.099  166.573 1.00 89.28  ? 416  LYS A CD  1 
ATOM   3313  C  CE  . LYS A 1 416  ? 55.969  63.585  166.660 1.00 92.82  ? 416  LYS A CE  1 
ATOM   3314  N  NZ  . LYS A 1 416  ? 57.252  62.911  166.315 1.00 93.92  ? 416  LYS A NZ  1 
ATOM   3315  N  N   . LEU A 1 417  ? 53.468  68.030  163.915 1.00 78.96  ? 417  LEU A N   1 
ATOM   3316  C  CA  . LEU A 1 417  ? 52.809  69.223  163.429 1.00 75.99  ? 417  LEU A CA  1 
ATOM   3317  C  C   . LEU A 1 417  ? 53.833  70.299  163.171 1.00 72.97  ? 417  LEU A C   1 
ATOM   3318  O  O   . LEU A 1 417  ? 54.747  70.515  163.972 1.00 73.00  ? 417  LEU A O   1 
ATOM   3319  C  CB  . LEU A 1 417  ? 51.773  69.732  164.432 1.00 76.71  ? 417  LEU A CB  1 
ATOM   3320  C  CG  . LEU A 1 417  ? 50.374  69.114  164.419 1.00 78.41  ? 417  LEU A CG  1 
ATOM   3321  C  CD1 . LEU A 1 417  ? 49.448  69.947  165.283 1.00 79.19  ? 417  LEU A CD1 1 
ATOM   3322  C  CD2 . LEU A 1 417  ? 49.804  68.992  163.015 1.00 77.97  ? 417  LEU A CD2 1 
ATOM   3323  N  N   . MET A 1 418  ? 53.680  70.951  162.030 1.00 70.23  ? 418  MET A N   1 
ATOM   3324  C  CA  . MET A 1 418  ? 54.443  72.135  161.703 1.00 67.26  ? 418  MET A CA  1 
ATOM   3325  C  C   . MET A 1 418  ? 53.576  73.335  162.045 1.00 65.98  ? 418  MET A C   1 
ATOM   3326  O  O   . MET A 1 418  ? 52.381  73.357  161.729 1.00 66.39  ? 418  MET A O   1 
ATOM   3327  C  CB  . MET A 1 418  ? 54.798  72.132  160.224 1.00 66.02  ? 418  MET A CB  1 
ATOM   3328  C  CG  . MET A 1 418  ? 55.894  71.149  159.867 1.00 66.40  ? 418  MET A CG  1 
ATOM   3329  S  SD  . MET A 1 418  ? 55.716  70.370  158.250 1.00 66.61  ? 418  MET A SD  1 
ATOM   3330  C  CE  . MET A 1 418  ? 55.124  71.727  157.238 1.00 64.52  ? 418  MET A CE  1 
ATOM   3331  N  N   . ARG A 1 419  ? 54.176  74.323  162.700 1.00 64.00  ? 419  ARG A N   1 
ATOM   3332  C  CA  . ARG A 1 419  ? 53.438  75.490  163.159 1.00 62.57  ? 419  ARG A CA  1 
ATOM   3333  C  C   . ARG A 1 419  ? 53.992  76.764  162.548 1.00 59.84  ? 419  ARG A C   1 
ATOM   3334  O  O   . ARG A 1 419  ? 55.194  77.015  162.607 1.00 59.09  ? 419  ARG A O   1 
ATOM   3335  C  CB  . ARG A 1 419  ? 53.454  75.570  164.687 1.00 64.01  ? 419  ARG A CB  1 
ATOM   3336  C  CG  . ARG A 1 419  ? 52.864  74.347  165.389 1.00 66.51  ? 419  ARG A CG  1 
ATOM   3337  C  CD  . ARG A 1 419  ? 53.058  74.398  166.907 1.00 69.48  ? 419  ARG A CD  1 
ATOM   3338  N  NE  . ARG A 1 419  ? 52.329  75.509  167.522 1.00 71.43  ? 419  ARG A NE  1 
ATOM   3339  C  CZ  . ARG A 1 419  ? 52.898  76.556  168.121 1.00 72.43  ? 419  ARG A CZ  1 
ATOM   3340  N  NH1 . ARG A 1 419  ? 54.218  76.650  168.227 1.00 72.46  ? 419  ARG A NH1 1 
ATOM   3341  N  NH2 . ARG A 1 419  ? 52.136  77.509  168.639 1.00 74.19  ? 419  ARG A NH2 1 
ATOM   3342  N  N   . PHE A 1 420  ? 53.102  77.555  161.952 1.00 58.22  ? 420  PHE A N   1 
ATOM   3343  C  CA  . PHE A 1 420  ? 53.466  78.815  161.303 1.00 55.95  ? 420  PHE A CA  1 
ATOM   3344  C  C   . PHE A 1 420  ? 52.563  79.944  161.767 1.00 55.60  ? 420  PHE A C   1 
ATOM   3345  O  O   . PHE A 1 420  ? 51.360  79.755  161.923 1.00 56.19  ? 420  PHE A O   1 
ATOM   3346  C  CB  . PHE A 1 420  ? 53.326  78.721  159.780 1.00 55.16  ? 420  PHE A CB  1 
ATOM   3347  C  CG  . PHE A 1 420  ? 53.941  77.499  159.179 1.00 54.91  ? 420  PHE A CG  1 
ATOM   3348  C  CD1 . PHE A 1 420  ? 53.194  76.323  159.047 1.00 56.59  ? 420  PHE A CD1 1 
ATOM   3349  C  CD2 . PHE A 1 420  ? 55.250  77.525  158.719 1.00 53.40  ? 420  PHE A CD2 1 
ATOM   3350  C  CE1 . PHE A 1 420  ? 53.759  75.183  158.485 1.00 57.32  ? 420  PHE A CE1 1 
ATOM   3351  C  CE2 . PHE A 1 420  ? 55.826  76.403  158.156 1.00 54.09  ? 420  PHE A CE2 1 
ATOM   3352  C  CZ  . PHE A 1 420  ? 55.083  75.224  158.039 1.00 56.54  ? 420  PHE A CZ  1 
ATOM   3353  N  N   . MET A 1 421  ? 53.145  81.119  161.976 1.00 54.34  ? 421  MET A N   1 
ATOM   3354  C  CA  . MET A 1 421  ? 52.352  82.316  162.158 1.00 53.98  ? 421  MET A CA  1 
ATOM   3355  C  C   . MET A 1 421  ? 52.307  83.051  160.832 1.00 52.80  ? 421  MET A C   1 
ATOM   3356  O  O   . MET A 1 421  ? 53.323  83.541  160.328 1.00 51.73  ? 421  MET A O   1 
ATOM   3357  C  CB  . MET A 1 421  ? 52.908  83.214  163.265 1.00 54.62  ? 421  MET A CB  1 
ATOM   3358  C  CG  . MET A 1 421  ? 51.998  84.390  163.615 1.00 55.55  ? 421  MET A CG  1 
ATOM   3359  S  SD  . MET A 1 421  ? 50.417  83.875  164.329 1.00 59.28  ? 421  MET A SD  1 
ATOM   3360  C  CE  . MET A 1 421  ? 50.896  83.565  166.035 1.00 58.09  ? 421  MET A CE  1 
ATOM   3361  N  N   . VAL A 1 422  ? 51.117  83.092  160.258 1.00 52.64  ? 422  VAL A N   1 
ATOM   3362  C  CA  . VAL A 1 422  ? 50.873  83.862  159.059 1.00 51.73  ? 422  VAL A CA  1 
ATOM   3363  C  C   . VAL A 1 422  ? 50.489  85.254  159.542 1.00 52.28  ? 422  VAL A C   1 
ATOM   3364  O  O   . VAL A 1 422  ? 49.541  85.399  160.323 1.00 53.45  ? 422  VAL A O   1 
ATOM   3365  C  CB  . VAL A 1 422  ? 49.729  83.238  158.231 1.00 51.97  ? 422  VAL A CB  1 
ATOM   3366  C  CG1 . VAL A 1 422  ? 49.445  84.061  157.009 1.00 51.38  ? 422  VAL A CG1 1 
ATOM   3367  C  CG2 . VAL A 1 422  ? 50.066  81.812  157.841 1.00 51.15  ? 422  VAL A CG2 1 
ATOM   3368  N  N   . THR A 1 423  ? 51.248  86.261  159.123 1.00 51.68  ? 423  THR A N   1 
ATOM   3369  C  CA  . THR A 1 423  ? 50.917  87.649  159.425 1.00 52.54  ? 423  THR A CA  1 
ATOM   3370  C  C   . THR A 1 423  ? 50.663  88.407  158.129 1.00 52.88  ? 423  THR A C   1 
ATOM   3371  O  O   . THR A 1 423  ? 51.453  88.338  157.183 1.00 52.02  ? 423  THR A O   1 
ATOM   3372  C  CB  . THR A 1 423  ? 52.028  88.353  160.225 1.00 52.64  ? 423  THR A CB  1 
ATOM   3373  O  OG1 . THR A 1 423  ? 52.167  87.732  161.509 1.00 53.88  ? 423  THR A OG1 1 
ATOM   3374  C  CG2 . THR A 1 423  ? 51.701  89.821  160.433 1.00 53.51  ? 423  THR A CG2 1 
ATOM   3375  N  N   . CYS A 1 424  ? 49.545  89.123  158.097 1.00 53.97  ? 424  CYS A N   1 
ATOM   3376  C  CA  . CYS A 1 424  ? 49.190  89.955  156.961 1.00 54.28  ? 424  CYS A CA  1 
ATOM   3377  C  C   . CYS A 1 424  ? 48.970  91.374  157.445 1.00 55.23  ? 424  CYS A C   1 
ATOM   3378  O  O   . CYS A 1 424  ? 48.704  91.596  158.626 1.00 56.03  ? 424  CYS A O   1 
ATOM   3379  C  CB  . CYS A 1 424  ? 47.916  89.424  156.312 1.00 54.86  ? 424  CYS A CB  1 
ATOM   3380  S  SG  . CYS A 1 424  ? 47.437  90.242  154.781 1.00 55.79  ? 424  CYS A SG  1 
ATOM   3381  N  N   . THR A 1 425  ? 49.086  92.331  156.536 1.00 55.65  ? 425  THR A N   1 
ATOM   3382  C  CA  . THR A 1 425  ? 48.841  93.729  156.865 1.00 57.05  ? 425  THR A CA  1 
ATOM   3383  C  C   . THR A 1 425  ? 47.350  93.927  156.961 1.00 58.33  ? 425  THR A C   1 
ATOM   3384  O  O   . THR A 1 425  ? 46.871  94.743  157.733 1.00 59.43  ? 425  THR A O   1 
ATOM   3385  C  CB  . THR A 1 425  ? 49.422  94.698  155.798 1.00 57.57  ? 425  THR A CB  1 
ATOM   3386  O  OG1 . THR A 1 425  ? 49.019  94.281  154.488 1.00 56.72  ? 425  THR A OG1 1 
ATOM   3387  C  CG2 . THR A 1 425  ? 50.930  94.712  155.854 1.00 56.35  ? 425  THR A CG2 1 
ATOM   3388  N  N   . GLU A 1 426  ? 46.631  93.148  156.165 1.00 58.72  ? 426  GLU A N   1 
ATOM   3389  C  CA  . GLU A 1 426  ? 45.184  93.214  156.067 1.00 60.69  ? 426  GLU A CA  1 
ATOM   3390  C  C   . GLU A 1 426  ? 44.557  92.190  157.001 1.00 60.71  ? 426  GLU A C   1 
ATOM   3391  O  O   . GLU A 1 426  ? 45.126  91.113  157.233 1.00 59.62  ? 426  GLU A O   1 
ATOM   3392  C  CB  . GLU A 1 426  ? 44.758  92.933  154.618 1.00 61.11  ? 426  GLU A CB  1 
ATOM   3393  C  CG  . GLU A 1 426  ? 44.536  94.161  153.712 1.00 63.80  ? 426  GLU A CG  1 
ATOM   3394  C  CD  . GLU A 1 426  ? 45.375  95.376  154.090 1.00 66.19  ? 426  GLU A CD  1 
ATOM   3395  O  OE1 . GLU A 1 426  ? 46.612  95.367  153.878 1.00 65.41  ? 426  GLU A OE1 1 
ATOM   3396  O  OE2 . GLU A 1 426  ? 44.781  96.353  154.597 1.00 69.24  ? 426  GLU A OE2 1 
ATOM   3397  N  N   . ARG A 1 427  ? 43.394  92.535  157.550 1.00 62.31  ? 427  ARG A N   1 
ATOM   3398  C  CA  . ARG A 1 427  ? 42.583  91.581  158.301 1.00 62.21  ? 427  ARG A CA  1 
ATOM   3399  C  C   . ARG A 1 427  ? 41.982  90.581  157.306 1.00 62.23  ? 427  ARG A C   1 
ATOM   3400  O  O   . ARG A 1 427  ? 41.081  90.918  156.524 1.00 63.61  ? 427  ARG A O   1 
ATOM   3401  C  CB  . ARG A 1 427  ? 41.511  92.310  159.107 1.00 63.71  ? 427  ARG A CB  1 
ATOM   3402  C  CG  . ARG A 1 427  ? 42.083  93.129  160.254 1.00 64.68  ? 427  ARG A CG  1 
ATOM   3403  C  CD  . ARG A 1 427  ? 40.999  93.685  161.168 1.00 67.25  ? 427  ARG A CD  1 
ATOM   3404  N  NE  . ARG A 1 427  ? 41.512  93.855  162.526 1.00 69.24  ? 427  ARG A NE  1 
ATOM   3405  C  CZ  . ARG A 1 427  ? 41.167  93.103  163.576 1.00 70.81  ? 427  ARG A CZ  1 
ATOM   3406  N  NH1 . ARG A 1 427  ? 40.271  92.123  163.460 1.00 71.19  ? 427  ARG A NH1 1 
ATOM   3407  N  NH2 . ARG A 1 427  ? 41.707  93.344  164.764 1.00 71.33  ? 427  ARG A NH2 1 
ATOM   3408  N  N   . MET A 1 428  ? 42.519  89.363  157.324 1.00 61.00  ? 428  MET A N   1 
ATOM   3409  C  CA  . MET A 1 428  ? 42.247  88.350  156.300 1.00 60.83  ? 428  MET A CA  1 
ATOM   3410  C  C   . MET A 1 428  ? 40.850  87.732  156.390 1.00 62.01  ? 428  MET A C   1 
ATOM   3411  O  O   . MET A 1 428  ? 40.386  87.400  157.486 1.00 62.56  ? 428  MET A O   1 
ATOM   3412  C  CB  . MET A 1 428  ? 43.286  87.229  156.395 1.00 59.33  ? 428  MET A CB  1 
ATOM   3413  C  CG  . MET A 1 428  ? 44.719  87.669  156.164 1.00 58.43  ? 428  MET A CG  1 
ATOM   3414  S  SD  . MET A 1 428  ? 45.921  86.339  156.377 1.00 57.08  ? 428  MET A SD  1 
ATOM   3415  C  CE  . MET A 1 428  ? 45.974  86.212  158.161 1.00 55.29  ? 428  MET A CE  1 
ATOM   3416  N  N   . THR A 1 429  ? 40.184  87.567  155.248 1.00 62.63  ? 429  THR A N   1 
ATOM   3417  C  CA  . THR A 1 429  ? 38.997  86.712  155.210 1.00 63.95  ? 429  THR A CA  1 
ATOM   3418  C  C   . THR A 1 429  ? 39.375  85.338  154.667 1.00 63.32  ? 429  THR A C   1 
ATOM   3419  O  O   . THR A 1 429  ? 38.640  84.358  154.844 1.00 64.74  ? 429  THR A O   1 
ATOM   3420  C  CB  . THR A 1 429  ? 37.806  87.300  154.414 1.00 65.70  ? 429  THR A CB  1 
ATOM   3421  O  OG1 . THR A 1 429  ? 37.859  88.729  154.413 1.00 66.59  ? 429  THR A OG1 1 
ATOM   3422  C  CG2 . THR A 1 429  ? 36.486  86.857  155.057 1.00 68.03  ? 429  THR A CG2 1 
ATOM   3423  N  N   . PHE A 1 430  ? 40.530  85.277  154.013 1.00 61.72  ? 430  PHE A N   1 
ATOM   3424  C  CA  . PHE A 1 430  ? 41.101  84.021  153.556 1.00 60.85  ? 430  PHE A CA  1 
ATOM   3425  C  C   . PHE A 1 430  ? 42.604  84.166  153.351 1.00 59.08  ? 430  PHE A C   1 
ATOM   3426  O  O   . PHE A 1 430  ? 43.131  85.281  153.363 1.00 58.60  ? 430  PHE A O   1 
ATOM   3427  C  CB  . PHE A 1 430  ? 40.433  83.565  152.248 1.00 62.14  ? 430  PHE A CB  1 
ATOM   3428  C  CG  . PHE A 1 430  ? 40.983  84.232  151.016 1.00 61.74  ? 430  PHE A CG  1 
ATOM   3429  C  CD1 . PHE A 1 430  ? 40.644  85.549  150.707 1.00 62.33  ? 430  PHE A CD1 1 
ATOM   3430  C  CD2 . PHE A 1 430  ? 41.847  83.543  150.167 1.00 60.90  ? 430  PHE A CD2 1 
ATOM   3431  C  CE1 . PHE A 1 430  ? 41.160  86.172  149.569 1.00 62.86  ? 430  PHE A CE1 1 
ATOM   3432  C  CE2 . PHE A 1 430  ? 42.372  84.157  149.025 1.00 61.53  ? 430  PHE A CE2 1 
ATOM   3433  C  CZ  . PHE A 1 430  ? 42.026  85.472  148.724 1.00 62.17  ? 430  PHE A CZ  1 
ATOM   3434  N  N   . PHE A 1 431  ? 43.274  83.024  153.194 1.00 58.30  ? 431  PHE A N   1 
ATOM   3435  C  CA  . PHE A 1 431  ? 44.577  82.907  152.522 1.00 56.96  ? 431  PHE A CA  1 
ATOM   3436  C  C   . PHE A 1 431  ? 44.769  81.436  152.172 1.00 57.40  ? 431  PHE A C   1 
ATOM   3437  O  O   . PHE A 1 431  ? 44.077  80.572  152.709 1.00 58.42  ? 431  PHE A O   1 
ATOM   3438  C  CB  . PHE A 1 431  ? 45.733  83.409  153.391 1.00 55.21  ? 431  PHE A CB  1 
ATOM   3439  C  CG  . PHE A 1 431  ? 46.108  82.472  154.504 1.00 53.99  ? 431  PHE A CG  1 
ATOM   3440  C  CD1 . PHE A 1 431  ? 45.424  82.500  155.712 1.00 53.13  ? 431  PHE A CD1 1 
ATOM   3441  C  CD2 . PHE A 1 431  ? 47.148  81.563  154.342 1.00 52.11  ? 431  PHE A CD2 1 
ATOM   3442  C  CE1 . PHE A 1 431  ? 45.770  81.647  156.738 1.00 52.50  ? 431  PHE A CE1 1 
ATOM   3443  C  CE2 . PHE A 1 431  ? 47.494  80.703  155.361 1.00 51.62  ? 431  PHE A CE2 1 
ATOM   3444  C  CZ  . PHE A 1 431  ? 46.800  80.743  156.565 1.00 51.80  ? 431  PHE A CZ  1 
ATOM   3445  N  N   . VAL A 1 432  ? 45.709  81.146  151.284 1.00 57.14  ? 432  VAL A N   1 
ATOM   3446  C  CA  . VAL A 1 432  ? 45.905  79.782  150.795 1.00 58.08  ? 432  VAL A CA  1 
ATOM   3447  C  C   . VAL A 1 432  ? 47.334  79.334  151.058 1.00 56.80  ? 432  VAL A C   1 
ATOM   3448  O  O   . VAL A 1 432  ? 48.253  80.149  151.060 1.00 55.84  ? 432  VAL A O   1 
ATOM   3449  C  CB  . VAL A 1 432  ? 45.566  79.673  149.273 1.00 59.21  ? 432  VAL A CB  1 
ATOM   3450  C  CG1 . VAL A 1 432  ? 45.847  78.273  148.730 1.00 60.47  ? 432  VAL A CG1 1 
ATOM   3451  C  CG2 . VAL A 1 432  ? 44.109  80.018  149.025 1.00 60.85  ? 432  VAL A CG2 1 
ATOM   3452  N  N   . TYR A 1 433  ? 47.519  78.045  151.305 1.00 57.43  ? 433  TYR A N   1 
ATOM   3453  C  CA  . TYR A 1 433  ? 48.863  77.492  151.370 1.00 56.79  ? 433  TYR A CA  1 
ATOM   3454  C  C   . TYR A 1 433  ? 49.018  76.410  150.319 1.00 58.22  ? 433  TYR A C   1 
ATOM   3455  O  O   . TYR A 1 433  ? 48.033  75.826  149.869 1.00 59.81  ? 433  TYR A O   1 
ATOM   3456  C  CB  . TYR A 1 433  ? 49.202  76.959  152.771 1.00 56.02  ? 433  TYR A CB  1 
ATOM   3457  C  CG  . TYR A 1 433  ? 48.513  75.669  153.144 1.00 57.19  ? 433  TYR A CG  1 
ATOM   3458  C  CD1 . TYR A 1 433  ? 47.316  75.678  153.867 1.00 57.70  ? 433  TYR A CD1 1 
ATOM   3459  C  CD2 . TYR A 1 433  ? 49.058  74.435  152.782 1.00 57.28  ? 433  TYR A CD2 1 
ATOM   3460  C  CE1 . TYR A 1 433  ? 46.677  74.493  154.221 1.00 58.79  ? 433  TYR A CE1 1 
ATOM   3461  C  CE2 . TYR A 1 433  ? 48.422  73.241  153.120 1.00 58.78  ? 433  TYR A CE2 1 
ATOM   3462  C  CZ  . TYR A 1 433  ? 47.228  73.278  153.835 1.00 59.99  ? 433  TYR A CZ  1 
ATOM   3463  O  OH  . TYR A 1 433  ? 46.603  72.097  154.179 1.00 61.70  ? 433  TYR A OH  1 
ATOM   3464  N  N   . TYR A 1 434  ? 50.261  76.174  149.920 1.00 58.16  ? 434  TYR A N   1 
ATOM   3465  C  CA  . TYR A 1 434  ? 50.612  75.078  149.036 1.00 59.83  ? 434  TYR A CA  1 
ATOM   3466  C  C   . TYR A 1 434  ? 51.901  74.506  149.559 1.00 59.72  ? 434  TYR A C   1 
ATOM   3467  O  O   . TYR A 1 434  ? 52.761  75.247  150.030 1.00 58.39  ? 434  TYR A O   1 
ATOM   3468  C  CB  . TYR A 1 434  ? 50.877  75.566  147.617 1.00 59.75  ? 434  TYR A CB  1 
ATOM   3469  C  CG  . TYR A 1 434  ? 49.901  76.563  147.045 1.00 60.21  ? 434  TYR A CG  1 
ATOM   3470  C  CD1 . TYR A 1 434  ? 50.040  77.926  147.302 1.00 59.06  ? 434  TYR A CD1 1 
ATOM   3471  C  CD2 . TYR A 1 434  ? 48.871  76.150  146.204 1.00 62.00  ? 434  TYR A CD2 1 
ATOM   3472  C  CE1 . TYR A 1 434  ? 49.161  78.847  146.765 1.00 60.34  ? 434  TYR A CE1 1 
ATOM   3473  C  CE2 . TYR A 1 434  ? 47.987  77.066  145.655 1.00 63.09  ? 434  TYR A CE2 1 
ATOM   3474  C  CZ  . TYR A 1 434  ? 48.139  78.412  145.940 1.00 62.19  ? 434  TYR A CZ  1 
ATOM   3475  O  OH  . TYR A 1 434  ? 47.264  79.326  145.410 1.00 63.58  ? 434  TYR A OH  1 
ATOM   3476  N  N   . VAL A 1 435  ? 52.052  73.192  149.475 1.00 61.87  ? 435  VAL A N   1 
ATOM   3477  C  CA  . VAL A 1 435  ? 53.342  72.576  149.783 1.00 62.50  ? 435  VAL A CA  1 
ATOM   3478  C  C   . VAL A 1 435  ? 53.789  71.657  148.640 1.00 64.34  ? 435  VAL A C   1 
ATOM   3479  O  O   . VAL A 1 435  ? 53.028  70.796  148.187 1.00 66.23  ? 435  VAL A O   1 
ATOM   3480  C  CB  . VAL A 1 435  ? 53.391  71.926  151.224 1.00 62.59  ? 435  VAL A CB  1 
ATOM   3481  C  CG1 . VAL A 1 435  ? 52.009  71.744  151.806 1.00 64.04  ? 435  VAL A CG1 1 
ATOM   3482  C  CG2 . VAL A 1 435  ? 54.178  70.627  151.256 1.00 63.25  ? 435  VAL A CG2 1 
ATOM   3483  N  N   . MET A 1 436  ? 55.009  71.884  148.153 1.00 64.32  ? 436  MET A N   1 
ATOM   3484  C  CA  . MET A 1 436  ? 55.572  71.080  147.069 1.00 66.38  ? 436  MET A CA  1 
ATOM   3485  C  C   . MET A 1 436  ? 56.895  70.423  147.409 1.00 66.28  ? 436  MET A C   1 
ATOM   3486  O  O   . MET A 1 436  ? 57.730  70.998  148.092 1.00 65.05  ? 436  MET A O   1 
ATOM   3487  C  CB  . MET A 1 436  ? 55.698  71.861  145.754 1.00 66.30  ? 436  MET A CB  1 
ATOM   3488  C  CG  . MET A 1 436  ? 56.100  73.309  145.878 1.00 65.99  ? 436  MET A CG  1 
ATOM   3489  S  SD  . MET A 1 436  ? 54.757  74.368  146.470 1.00 70.17  ? 436  MET A SD  1 
ATOM   3490  C  CE  . MET A 1 436  ? 53.322  73.654  145.699 1.00 69.73  ? 436  MET A CE  1 
ATOM   3491  N  N   . SER A 1 437  ? 57.053  69.202  146.915 1.00 68.53  ? 437  SER A N   1 
ATOM   3492  C  CA  . SER A 1 437  ? 58.257  68.409  147.090 1.00 69.00  ? 437  SER A CA  1 
ATOM   3493  C  C   . SER A 1 437  ? 58.504  67.637  145.798 1.00 70.81  ? 437  SER A C   1 
ATOM   3494  O  O   . SER A 1 437  ? 57.583  67.009  145.251 1.00 72.41  ? 437  SER A O   1 
ATOM   3495  C  CB  . SER A 1 437  ? 58.098  67.448  148.270 1.00 70.02  ? 437  SER A CB  1 
ATOM   3496  O  OG  . SER A 1 437  ? 59.283  66.709  148.497 1.00 70.27  ? 437  SER A OG  1 
ATOM   3497  N  N   . LYS A 1 438  ? 59.747  67.704  145.312 1.00 70.60  ? 438  LYS A N   1 
ATOM   3498  C  CA  . LYS A 1 438  ? 60.148  67.061  144.055 1.00 72.14  ? 438  LYS A CA  1 
ATOM   3499  C  C   . LYS A 1 438  ? 59.254  67.553  142.905 1.00 72.78  ? 438  LYS A C   1 
ATOM   3500  O  O   . LYS A 1 438  ? 58.653  66.749  142.168 1.00 75.01  ? 438  LYS A O   1 
ATOM   3501  C  CB  . LYS A 1 438  ? 60.094  65.527  144.173 1.00 74.53  ? 438  LYS A CB  1 
ATOM   3502  C  CG  . LYS A 1 438  ? 60.808  64.925  145.383 1.00 75.35  ? 438  LYS A CG  1 
ATOM   3503  C  CD  . LYS A 1 438  ? 60.436  63.445  145.532 1.00 80.58  ? 438  LYS A CD  1 
ATOM   3504  C  CE  . LYS A 1 438  ? 60.695  62.920  146.942 1.00 82.29  ? 438  LYS A CE  1 
ATOM   3505  N  NZ  . LYS A 1 438  ? 62.155  62.823  147.252 1.00 82.37  ? 438  LYS A NZ  1 
ATOM   3506  N  N   . GLY A 1 439  ? 59.152  68.879  142.790 1.00 70.87  ? 439  GLY A N   1 
ATOM   3507  C  CA  . GLY A 1 439  ? 58.344  69.536  141.759 1.00 71.14  ? 439  GLY A CA  1 
ATOM   3508  C  C   . GLY A 1 439  ? 56.897  69.089  141.572 1.00 72.86  ? 439  GLY A C   1 
ATOM   3509  O  O   . GLY A 1 439  ? 56.405  69.052  140.443 1.00 74.61  ? 439  GLY A O   1 
ATOM   3510  N  N   . ASN A 1 440  ? 56.215  68.738  142.663 1.00 72.63  ? 440  ASN A N   1 
ATOM   3511  C  CA  . ASN A 1 440  ? 54.757  68.550  142.634 1.00 73.79  ? 440  ASN A CA  1 
ATOM   3512  C  C   . ASN A 1 440  ? 54.099  69.086  143.905 1.00 72.06  ? 440  ASN A C   1 
ATOM   3513  O  O   . ASN A 1 440  ? 54.683  69.012  144.985 1.00 70.88  ? 440  ASN A O   1 
ATOM   3514  C  CB  . ASN A 1 440  ? 54.375  67.080  142.403 1.00 76.52  ? 440  ASN A CB  1 
ATOM   3515  C  CG  . ASN A 1 440  ? 52.847  66.865  142.304 1.00 79.97  ? 440  ASN A CG  1 
ATOM   3516  O  OD1 . ASN A 1 440  ? 52.110  67.706  141.772 1.00 81.02  ? 440  ASN A OD1 1 
ATOM   3517  N  ND2 . ASN A 1 440  ? 52.375  65.724  142.813 1.00 82.63  ? 440  ASN A ND2 1 
ATOM   3518  N  N   . ILE A 1 441  ? 52.890  69.631  143.757 1.00 71.79  ? 441  ILE A N   1 
ATOM   3519  C  CA  . ILE A 1 441  ? 52.070  70.089  144.885 1.00 70.08  ? 441  ILE A CA  1 
ATOM   3520  C  C   . ILE A 1 441  ? 51.495  68.899  145.650 1.00 71.40  ? 441  ILE A C   1 
ATOM   3521  O  O   . ILE A 1 441  ? 50.577  68.222  145.183 1.00 73.63  ? 441  ILE A O   1 
ATOM   3522  C  CB  . ILE A 1 441  ? 50.927  71.029  144.433 1.00 70.33  ? 441  ILE A CB  1 
ATOM   3523  C  CG1 . ILE A 1 441  ? 51.481  72.125  143.503 1.00 68.35  ? 441  ILE A CG1 1 
ATOM   3524  C  CG2 . ILE A 1 441  ? 50.182  71.578  145.653 1.00 68.89  ? 441  ILE A CG2 1 
ATOM   3525  C  CD1 . ILE A 1 441  ? 50.483  73.164  143.028 1.00 67.60  ? 441  ILE A CD1 1 
ATOM   3526  N  N   . ILE A 1 442  ? 52.056  68.666  146.831 1.00 70.02  ? 442  ILE A N   1 
ATOM   3527  C  CA  . ILE A 1 442  ? 51.713  67.537  147.691 1.00 71.20  ? 442  ILE A CA  1 
ATOM   3528  C  C   . ILE A 1 442  ? 50.440  67.790  148.502 1.00 71.37  ? 442  ILE A C   1 
ATOM   3529  O  O   . ILE A 1 442  ? 49.694  66.859  148.822 1.00 73.53  ? 442  ILE A O   1 
ATOM   3530  C  CB  . ILE A 1 442  ? 52.924  67.190  148.613 1.00 70.26  ? 442  ILE A CB  1 
ATOM   3531  C  CG1 . ILE A 1 442  ? 53.651  65.945  148.102 1.00 72.03  ? 442  ILE A CG1 1 
ATOM   3532  C  CG2 . ILE A 1 442  ? 52.529  67.020  150.069 1.00 70.87  ? 442  ILE A CG2 1 
ATOM   3533  C  CD1 . ILE A 1 442  ? 54.857  66.261  147.231 1.00 71.53  ? 442  ILE A CD1 1 
ATOM   3534  N  N   . ASP A 1 443  ? 50.194  69.059  148.810 1.00 69.10  ? 443  ASP A N   1 
ATOM   3535  C  CA  . ASP A 1 443  ? 49.139  69.447  149.726 1.00 68.85  ? 443  ASP A CA  1 
ATOM   3536  C  C   . ASP A 1 443  ? 48.873  70.939  149.590 1.00 66.78  ? 443  ASP A C   1 
ATOM   3537  O  O   . ASP A 1 443  ? 49.772  71.712  149.254 1.00 65.16  ? 443  ASP A O   1 
ATOM   3538  C  CB  . ASP A 1 443  ? 49.556  69.112  151.159 1.00 68.41  ? 443  ASP A CB  1 
ATOM   3539  C  CG  . ASP A 1 443  ? 48.399  69.128  152.122 1.00 70.40  ? 443  ASP A CG  1 
ATOM   3540  O  OD1 . ASP A 1 443  ? 48.515  69.814  153.156 1.00 70.82  ? 443  ASP A OD1 1 
ATOM   3541  O  OD2 . ASP A 1 443  ? 47.376  68.459  151.855 1.00 73.53  ? 443  ASP A OD2 1 
ATOM   3542  N  N   . ALA A 1 444  ? 47.630  71.335  149.844 1.00 66.99  ? 444  ALA A N   1 
ATOM   3543  C  CA  . ALA A 1 444  ? 47.217  72.731  149.787 1.00 65.31  ? 444  ALA A CA  1 
ATOM   3544  C  C   . ALA A 1 444  ? 45.983  72.896  150.661 1.00 65.87  ? 444  ALA A C   1 
ATOM   3545  O  O   . ALA A 1 444  ? 45.355  71.906  151.026 1.00 67.79  ? 444  ALA A O   1 
ATOM   3546  C  CB  . ALA A 1 444  ? 46.919  73.140  148.349 1.00 65.79  ? 444  ALA A CB  1 
ATOM   3547  N  N   . GLY A 1 445  ? 45.636  74.134  151.001 1.00 64.41  ? 445  GLY A N   1 
ATOM   3548  C  CA  . GLY A 1 445  ? 44.421  74.397  151.768 1.00 64.92  ? 445  GLY A CA  1 
ATOM   3549  C  C   . GLY A 1 445  ? 43.856  75.791  151.590 1.00 64.12  ? 445  GLY A C   1 
ATOM   3550  O  O   . GLY A 1 445  ? 44.588  76.731  151.298 1.00 62.90  ? 445  GLY A O   1 
ATOM   3551  N  N   . PHE A 1 446  ? 42.545  75.918  151.757 1.00 65.21  ? 446  PHE A N   1 
ATOM   3552  C  CA  . PHE A 1 446  ? 41.885  77.216  151.769 1.00 64.86  ? 446  PHE A CA  1 
ATOM   3553  C  C   . PHE A 1 446  ? 41.572  77.572  153.219 1.00 64.50  ? 446  PHE A C   1 
ATOM   3554  O  O   . PHE A 1 446  ? 40.745  76.931  153.863 1.00 65.90  ? 446  PHE A O   1 
ATOM   3555  C  CB  . PHE A 1 446  ? 40.603  77.179  150.933 1.00 66.87  ? 446  PHE A CB  1 
ATOM   3556  C  CG  . PHE A 1 446  ? 40.147  78.531  150.445 1.00 66.79  ? 446  PHE A CG  1 
ATOM   3557  C  CD1 . PHE A 1 446  ? 40.428  78.945  149.144 1.00 66.89  ? 446  PHE A CD1 1 
ATOM   3558  C  CD2 . PHE A 1 446  ? 39.424  79.384  151.275 1.00 66.73  ? 446  PHE A CD2 1 
ATOM   3559  C  CE1 . PHE A 1 446  ? 40.003  80.193  148.678 1.00 66.98  ? 446  PHE A CE1 1 
ATOM   3560  C  CE2 . PHE A 1 446  ? 38.997  80.635  150.822 1.00 66.73  ? 446  PHE A CE2 1 
ATOM   3561  C  CZ  . PHE A 1 446  ? 39.287  81.039  149.519 1.00 67.17  ? 446  PHE A CZ  1 
ATOM   3562  N  N   . MET A 1 447  ? 42.250  78.589  153.733 1.00 62.93  ? 447  MET A N   1 
ATOM   3563  C  CA  . MET A 1 447  ? 42.127  78.960  155.136 1.00 62.51  ? 447  MET A CA  1 
ATOM   3564  C  C   . MET A 1 447  ? 41.300  80.216  155.272 1.00 62.95  ? 447  MET A C   1 
ATOM   3565  O  O   . MET A 1 447  ? 41.390  81.119  154.445 1.00 62.72  ? 447  MET A O   1 
ATOM   3566  C  CB  . MET A 1 447  ? 43.504  79.150  155.758 1.00 60.79  ? 447  MET A CB  1 
ATOM   3567  C  CG  . MET A 1 447  ? 44.465  78.000  155.473 1.00 60.33  ? 447  MET A CG  1 
ATOM   3568  S  SD  . MET A 1 447  ? 43.759  76.388  155.886 1.00 62.66  ? 447  MET A SD  1 
ATOM   3569  C  CE  . MET A 1 447  ? 43.741  76.451  157.674 1.00 61.10  ? 447  MET A CE  1 
ATOM   3570  N  N   . ARG A 1 448  ? 40.474  80.258  156.310 1.00 64.11  ? 448  ARG A N   1 
ATOM   3571  C  CA  . ARG A 1 448  ? 39.534  81.356  156.489 1.00 64.91  ? 448  ARG A CA  1 
ATOM   3572  C  C   . ARG A 1 448  ? 39.698  81.996  157.852 1.00 64.06  ? 448  ARG A C   1 
ATOM   3573  O  O   . ARG A 1 448  ? 38.962  81.678  158.774 1.00 64.85  ? 448  ARG A O   1 
ATOM   3574  C  CB  . ARG A 1 448  ? 38.090  80.881  156.301 1.00 67.04  ? 448  ARG A CB  1 
ATOM   3575  C  CG  . ARG A 1 448  ? 37.782  80.296  154.935 1.00 69.21  ? 448  ARG A CG  1 
ATOM   3576  C  CD  . ARG A 1 448  ? 36.345  79.810  154.876 1.00 74.58  ? 448  ARG A CD  1 
ATOM   3577  N  NE  . ARG A 1 448  ? 35.406  80.926  154.776 1.00 77.59  ? 448  ARG A NE  1 
ATOM   3578  C  CZ  . ARG A 1 448  ? 34.110  80.862  155.073 1.00 80.18  ? 448  ARG A CZ  1 
ATOM   3579  N  NH1 . ARG A 1 448  ? 33.563  79.728  155.507 1.00 81.71  ? 448  ARG A NH1 1 
ATOM   3580  N  NH2 . ARG A 1 448  ? 33.358  81.945  154.940 1.00 81.38  ? 448  ARG A NH2 1 
ATOM   3581  N  N   . PRO A 1 449  ? 40.676  82.904  157.987 1.00 62.83  ? 449  PRO A N   1 
ATOM   3582  C  CA  . PRO A 1 449  ? 40.757  83.655  159.235 1.00 62.55  ? 449  PRO A CA  1 
ATOM   3583  C  C   . PRO A 1 449  ? 39.471  84.449  159.432 1.00 63.74  ? 449  PRO A C   1 
ATOM   3584  O  O   . PRO A 1 449  ? 38.829  84.860  158.453 1.00 64.14  ? 449  PRO A O   1 
ATOM   3585  C  CB  . PRO A 1 449  ? 41.940  84.601  159.001 1.00 61.25  ? 449  PRO A CB  1 
ATOM   3586  C  CG  . PRO A 1 449  ? 42.742  83.950  157.915 1.00 60.21  ? 449  PRO A CG  1 
ATOM   3587  C  CD  . PRO A 1 449  ? 41.735  83.293  157.037 1.00 61.28  ? 449  PRO A CD  1 
ATOM   3588  N  N   . ASN A 1 450  ? 39.088  84.646  160.685 1.00 64.24  ? 450  ASN A N   1 
ATOM   3589  C  CA  . ASN A 1 450  ? 37.884  85.402  160.980 1.00 65.35  ? 450  ASN A CA  1 
ATOM   3590  C  C   . ASN A 1 450  ? 38.179  86.897  161.078 1.00 64.82  ? 450  ASN A C   1 
ATOM   3591  O  O   . ASN A 1 450  ? 38.126  87.482  162.167 1.00 65.11  ? 450  ASN A O   1 
ATOM   3592  C  CB  . ASN A 1 450  ? 37.215  84.877  162.251 1.00 66.60  ? 450  ASN A CB  1 
ATOM   3593  C  CG  . ASN A 1 450  ? 35.748  85.259  162.334 1.00 68.94  ? 450  ASN A CG  1 
ATOM   3594  O  OD1 . ASN A 1 450  ? 35.130  85.641  161.336 1.00 69.82  ? 450  ASN A OD1 1 
ATOM   3595  N  ND2 . ASN A 1 450  ? 35.182  85.154  163.529 1.00 70.68  ? 450  ASN A ND2 1 
ATOM   3596  N  N   . LYS A 1 451  ? 38.502  87.500  159.930 1.00 64.03  ? 451  LYS A N   1 
ATOM   3597  C  CA  . LYS A 1 451  ? 38.825  88.931  159.847 1.00 63.84  ? 451  LYS A CA  1 
ATOM   3598  C  C   . LYS A 1 451  ? 40.018  89.238  160.766 1.00 62.27  ? 451  LYS A C   1 
ATOM   3599  O  O   . LYS A 1 451  ? 39.949  90.087  161.655 1.00 63.01  ? 451  LYS A O   1 
ATOM   3600  C  CB  . LYS A 1 451  ? 37.579  89.781  160.183 1.00 65.93  ? 451  LYS A CB  1 
ATOM   3601  C  CG  . LYS A 1 451  ? 37.790  91.288  160.160 1.00 67.93  ? 451  LYS A CG  1 
ATOM   3602  C  CD  . LYS A 1 451  ? 36.489  92.081  160.337 1.00 71.17  ? 451  LYS A CD  1 
ATOM   3603  C  CE  . LYS A 1 451  ? 36.738  93.595  160.125 1.00 72.89  ? 451  LYS A CE  1 
ATOM   3604  N  NZ  . LYS A 1 451  ? 37.617  93.931  158.929 1.00 70.23  ? 451  LYS A NZ  1 
ATOM   3605  N  N   . GLN A 1 452  ? 41.113  88.522  160.548 1.00 60.12  ? 452  GLN A N   1 
ATOM   3606  C  CA  . GLN A 1 452  ? 42.246  88.570  161.459 1.00 58.62  ? 452  GLN A CA  1 
ATOM   3607  C  C   . GLN A 1 452  ? 43.556  88.814  160.729 1.00 56.87  ? 452  GLN A C   1 
ATOM   3608  O  O   . GLN A 1 452  ? 43.772  88.258  159.653 1.00 56.27  ? 452  GLN A O   1 
ATOM   3609  C  CB  . GLN A 1 452  ? 42.319  87.268  162.268 1.00 58.72  ? 452  GLN A CB  1 
ATOM   3610  C  CG  . GLN A 1 452  ? 41.236  87.122  163.346 1.00 59.32  ? 452  GLN A CG  1 
ATOM   3611  C  CD  . GLN A 1 452  ? 41.412  88.095  164.502 1.00 59.57  ? 452  GLN A CD  1 
ATOM   3612  O  OE1 . GLN A 1 452  ? 42.529  88.362  164.942 1.00 59.78  ? 452  GLN A OE1 1 
ATOM   3613  N  NE2 . GLN A 1 452  ? 40.309  88.634  164.992 1.00 60.40  ? 452  GLN A NE2 1 
ATOM   3614  N  N   . PRO A 1 453  ? 44.429  89.664  161.300 1.00 56.23  ? 453  PRO A N   1 
ATOM   3615  C  CA  . PRO A 1 453  ? 45.749  89.917  160.716 1.00 54.92  ? 453  PRO A CA  1 
ATOM   3616  C  C   . PRO A 1 453  ? 46.760  88.777  160.913 1.00 53.68  ? 453  PRO A C   1 
ATOM   3617  O  O   . PRO A 1 453  ? 47.651  88.588  160.081 1.00 52.74  ? 453  PRO A O   1 
ATOM   3618  C  CB  . PRO A 1 453  ? 46.215  91.183  161.432 1.00 55.46  ? 453  PRO A CB  1 
ATOM   3619  C  CG  . PRO A 1 453  ? 45.497  91.197  162.713 1.00 56.44  ? 453  PRO A CG  1 
ATOM   3620  C  CD  . PRO A 1 453  ? 44.194  90.461  162.517 1.00 57.18  ? 453  PRO A CD  1 
ATOM   3621  N  N   . LYS A 1 454  ? 46.625  88.039  162.007 1.00 54.02  ? 454  LYS A N   1 
ATOM   3622  C  CA  . LYS A 1 454  ? 47.503  86.917  162.300 1.00 53.44  ? 454  LYS A CA  1 
ATOM   3623  C  C   . LYS A 1 454  ? 46.717  85.621  162.271 1.00 53.93  ? 454  LYS A C   1 
ATOM   3624  O  O   . LYS A 1 454  ? 45.523  85.607  162.569 1.00 55.17  ? 454  LYS A O   1 
ATOM   3625  C  CB  . LYS A 1 454  ? 48.149  87.083  163.675 1.00 53.90  ? 454  LYS A CB  1 
ATOM   3626  C  CG  . LYS A 1 454  ? 49.212  88.152  163.738 1.00 53.76  ? 454  LYS A CG  1 
ATOM   3627  C  CD  . LYS A 1 454  ? 50.183  87.908  164.884 1.00 55.06  ? 454  LYS A CD  1 
ATOM   3628  C  CE  . LYS A 1 454  ? 49.811  88.699  166.122 1.00 57.64  ? 454  LYS A CE  1 
ATOM   3629  N  NZ  . LYS A 1 454  ? 50.926  88.697  167.113 1.00 59.08  ? 454  LYS A NZ  1 
ATOM   3630  N  N   . TYR A 1 455  ? 47.394  84.531  161.925 1.00 53.44  ? 455  TYR A N   1 
ATOM   3631  C  CA  . TYR A 1 455  ? 46.777  83.207  161.915 1.00 54.01  ? 455  TYR A CA  1 
ATOM   3632  C  C   . TYR A 1 455  ? 47.804  82.105  162.152 1.00 53.98  ? 455  TYR A C   1 
ATOM   3633  O  O   . TYR A 1 455  ? 48.818  82.027  161.459 1.00 53.27  ? 455  TYR A O   1 
ATOM   3634  C  CB  . TYR A 1 455  ? 46.075  82.969  160.583 1.00 53.76  ? 455  TYR A CB  1 
ATOM   3635  C  CG  . TYR A 1 455  ? 45.236  81.720  160.529 1.00 53.73  ? 455  TYR A CG  1 
ATOM   3636  C  CD1 . TYR A 1 455  ? 43.874  81.769  160.806 1.00 54.12  ? 455  TYR A CD1 1 
ATOM   3637  C  CD2 . TYR A 1 455  ? 45.800  80.492  160.180 1.00 52.85  ? 455  TYR A CD2 1 
ATOM   3638  C  CE1 . TYR A 1 455  ? 43.095  80.625  160.744 1.00 55.89  ? 455  TYR A CE1 1 
ATOM   3639  C  CE2 . TYR A 1 455  ? 45.031  79.340  160.118 1.00 54.44  ? 455  TYR A CE2 1 
ATOM   3640  C  CZ  . TYR A 1 455  ? 43.677  79.412  160.401 1.00 55.79  ? 455  TYR A CZ  1 
ATOM   3641  O  OH  . TYR A 1 455  ? 42.902  78.275  160.347 1.00 57.73  ? 455  TYR A OH  1 
ATOM   3642  N  N   . LEU A 1 456  ? 47.529  81.244  163.121 1.00 55.30  ? 456  LEU A N   1 
ATOM   3643  C  CA  . LEU A 1 456  ? 48.394  80.109  163.370 1.00 55.62  ? 456  LEU A CA  1 
ATOM   3644  C  C   . LEU A 1 456  ? 48.045  78.937  162.445 1.00 55.94  ? 456  LEU A C   1 
ATOM   3645  O  O   . LEU A 1 456  ? 47.041  78.252  162.630 1.00 57.13  ? 456  LEU A O   1 
ATOM   3646  C  CB  . LEU A 1 456  ? 48.374  79.703  164.854 1.00 56.86  ? 456  LEU A CB  1 
ATOM   3647  C  CG  . LEU A 1 456  ? 49.615  78.924  165.316 1.00 57.03  ? 456  LEU A CG  1 
ATOM   3648  C  CD1 . LEU A 1 456  ? 50.884  79.744  165.184 1.00 56.87  ? 456  LEU A CD1 1 
ATOM   3649  C  CD2 . LEU A 1 456  ? 49.475  78.493  166.732 1.00 60.08  ? 456  LEU A CD2 1 
ATOM   3650  N  N   . LEU A 1 457  ? 48.883  78.735  161.434 1.00 55.30  ? 457  LEU A N   1 
ATOM   3651  C  CA  . LEU A 1 457  ? 48.753  77.606  160.527 1.00 55.75  ? 457  LEU A CA  1 
ATOM   3652  C  C   . LEU A 1 457  ? 49.439  76.364  161.097 1.00 56.72  ? 457  LEU A C   1 
ATOM   3653  O  O   . LEU A 1 457  ? 50.594  76.422  161.513 1.00 55.95  ? 457  LEU A O   1 
ATOM   3654  C  CB  . LEU A 1 457  ? 49.323  77.968  159.155 1.00 54.20  ? 457  LEU A CB  1 
ATOM   3655  C  CG  . LEU A 1 457  ? 49.163  76.976  157.998 1.00 54.58  ? 457  LEU A CG  1 
ATOM   3656  C  CD1 . LEU A 1 457  ? 47.701  76.553  157.770 1.00 55.36  ? 457  LEU A CD1 1 
ATOM   3657  C  CD2 . LEU A 1 457  ? 49.762  77.557  156.722 1.00 52.17  ? 457  LEU A CD2 1 
ATOM   3658  N  N   . GLN A 1 458  ? 48.711  75.252  161.124 1.00 58.89  ? 458  GLN A N   1 
ATOM   3659  C  CA  . GLN A 1 458  ? 49.240  73.979  161.609 1.00 61.09  ? 458  GLN A CA  1 
ATOM   3660  C  C   . GLN A 1 458  ? 49.062  72.900  160.552 1.00 62.29  ? 458  GLN A C   1 
ATOM   3661  O  O   . GLN A 1 458  ? 47.974  72.737  160.007 1.00 63.22  ? 458  GLN A O   1 
ATOM   3662  C  CB  . GLN A 1 458  ? 48.555  73.546  162.919 1.00 63.03  ? 458  GLN A CB  1 
ATOM   3663  C  CG  . GLN A 1 458  ? 49.125  74.184  164.191 1.00 63.50  ? 458  GLN A CG  1 
ATOM   3664  C  CD  . GLN A 1 458  ? 48.726  73.443  165.466 1.00 67.47  ? 458  GLN A CD  1 
ATOM   3665  O  OE1 . GLN A 1 458  ? 47.572  73.024  165.632 1.00 69.31  ? 458  GLN A OE1 1 
ATOM   3666  N  NE2 . GLN A 1 458  ? 49.686  73.279  166.379 1.00 68.45  ? 458  GLN A NE2 1 
ATOM   3667  N  N   . LEU A 1 459  ? 50.133  72.166  160.265 1.00 62.99  ? 459  LEU A N   1 
ATOM   3668  C  CA  . LEU A 1 459  ? 50.095  71.114  159.249 1.00 64.59  ? 459  LEU A CA  1 
ATOM   3669  C  C   . LEU A 1 459  ? 50.851  69.874  159.670 1.00 66.42  ? 459  LEU A C   1 
ATOM   3670  O  O   . LEU A 1 459  ? 51.972  69.969  160.173 1.00 66.02  ? 459  LEU A O   1 
ATOM   3671  C  CB  . LEU A 1 459  ? 50.702  71.616  157.940 1.00 62.99  ? 459  LEU A CB  1 
ATOM   3672  C  CG  . LEU A 1 459  ? 49.977  72.738  157.206 1.00 61.97  ? 459  LEU A CG  1 
ATOM   3673  C  CD1 . LEU A 1 459  ? 50.865  73.274  156.110 1.00 60.41  ? 459  LEU A CD1 1 
ATOM   3674  C  CD2 . LEU A 1 459  ? 48.657  72.232  156.657 1.00 63.12  ? 459  LEU A CD2 1 
ATOM   3675  N  N   . ASN A 1 460  ? 50.244  68.714  159.446 1.00 69.19  ? 460  ASN A N   1 
ATOM   3676  C  CA  . ASN A 1 460  ? 50.940  67.444  159.603 1.00 71.59  ? 460  ASN A CA  1 
ATOM   3677  C  C   . ASN A 1 460  ? 51.977  67.220  158.499 1.00 71.14  ? 460  ASN A C   1 
ATOM   3678  O  O   . ASN A 1 460  ? 51.655  67.283  157.305 1.00 70.81  ? 460  ASN A O   1 
ATOM   3679  C  CB  . ASN A 1 460  ? 49.940  66.286  159.636 1.00 74.42  ? 460  ASN A CB  1 
ATOM   3680  C  CG  . ASN A 1 460  ? 49.494  65.940  161.049 1.00 77.48  ? 460  ASN A CG  1 
ATOM   3681  O  OD1 . ASN A 1 460  ? 50.307  65.921  161.977 1.00 78.79  ? 460  ASN A OD1 1 
ATOM   3682  N  ND2 . ASN A 1 460  ? 48.200  65.649  161.218 1.00 79.48  ? 460  ASN A ND2 1 
ATOM   3683  N  N   . ALA A 1 461  ? 53.223  66.979  158.902 1.00 71.44  ? 461  ALA A N   1 
ATOM   3684  C  CA  . ALA A 1 461  ? 54.267  66.574  157.964 1.00 71.66  ? 461  ALA A CA  1 
ATOM   3685  C  C   . ALA A 1 461  ? 54.012  65.142  157.481 1.00 74.72  ? 461  ALA A C   1 
ATOM   3686  O  O   . ALA A 1 461  ? 53.859  64.212  158.283 1.00 76.69  ? 461  ALA A O   1 
ATOM   3687  C  CB  . ALA A 1 461  ? 55.637  66.689  158.604 1.00 70.60  ? 461  ALA A CB  1 
ATOM   3688  N  N   . THR A 1 462  ? 53.949  64.980  156.164 1.00 75.56  ? 462  THR A N   1 
ATOM   3689  C  CA  . THR A 1 462  ? 53.707  63.675  155.548 1.00 78.85  ? 462  THR A CA  1 
ATOM   3690  C  C   . THR A 1 462  ? 54.980  63.163  154.865 1.00 79.17  ? 462  THR A C   1 
ATOM   3691  O  O   . THR A 1 462  ? 55.883  63.946  154.562 1.00 76.86  ? 462  THR A O   1 
ATOM   3692  C  CB  . THR A 1 462  ? 52.546  63.740  154.536 1.00 79.53  ? 462  THR A CB  1 
ATOM   3693  O  OG1 . THR A 1 462  ? 52.792  64.792  153.595 1.00 77.57  ? 462  THR A OG1 1 
ATOM   3694  C  CG2 . THR A 1 462  ? 51.227  64.014  155.248 1.00 80.52  ? 462  THR A CG2 1 
ATOM   3695  N  N   . GLU A 1 463  ? 55.040  61.855  154.620 1.00 82.41  ? 463  GLU A N   1 
ATOM   3696  C  CA  . GLU A 1 463  ? 56.257  61.218  154.107 1.00 83.46  ? 463  GLU A CA  1 
ATOM   3697  C  C   . GLU A 1 463  ? 56.674  61.691  152.704 1.00 82.37  ? 463  GLU A C   1 
ATOM   3698  O  O   . GLU A 1 463  ? 57.868  61.724  152.388 1.00 81.34  ? 463  GLU A O   1 
ATOM   3699  C  CB  . GLU A 1 463  ? 56.139  59.695  154.168 1.00 86.85  ? 463  GLU A CB  1 
ATOM   3700  C  CG  . GLU A 1 463  ? 57.455  58.985  154.468 1.00 88.37  ? 463  GLU A CG  1 
ATOM   3701  C  CD  . GLU A 1 463  ? 57.251  57.545  154.920 1.00 94.17  ? 463  GLU A CD  1 
ATOM   3702  O  OE1 . GLU A 1 463  ? 56.641  57.324  155.993 1.00 95.96  ? 463  GLU A OE1 1 
ATOM   3703  O  OE2 . GLU A 1 463  ? 57.707  56.627  154.202 1.00 96.62  ? 463  GLU A OE2 1 
ATOM   3704  N  N   . LYS A 1 464  ? 55.702  62.072  151.876 1.00 82.91  ? 464  LYS A N   1 
ATOM   3705  C  CA  . LYS A 1 464  ? 56.007  62.654  150.559 1.00 82.19  ? 464  LYS A CA  1 
ATOM   3706  C  C   . LYS A 1 464  ? 56.632  64.054  150.627 1.00 79.26  ? 464  LYS A C   1 
ATOM   3707  O  O   . LYS A 1 464  ? 57.061  64.601  149.607 1.00 78.33  ? 464  LYS A O   1 
ATOM   3708  C  CB  . LYS A 1 464  ? 54.800  62.609  149.598 1.00 83.70  ? 464  LYS A CB  1 
ATOM   3709  C  CG  . LYS A 1 464  ? 53.448  62.219  150.211 1.00 86.78  ? 464  LYS A CG  1 
ATOM   3710  C  CD  . LYS A 1 464  ? 52.585  63.442  150.529 1.00 86.51  ? 464  LYS A CD  1 
ATOM   3711  C  CE  . LYS A 1 464  ? 51.223  63.056  151.111 1.00 88.90  ? 464  LYS A CE  1 
ATOM   3712  N  NZ  . LYS A 1 464  ? 50.333  62.379  150.123 1.00 91.91  ? 464  LYS A NZ  1 
ATOM   3713  N  N   . MET A 1 465  ? 56.700  64.616  151.832 1.00 78.32  ? 465  MET A N   1 
ATOM   3714  C  CA  . MET A 1 465  ? 57.341  65.908  152.061 1.00 75.87  ? 465  MET A CA  1 
ATOM   3715  C  C   . MET A 1 465  ? 58.806  65.724  152.430 1.00 75.35  ? 465  MET A C   1 
ATOM   3716  O  O   . MET A 1 465  ? 59.583  66.684  152.473 1.00 73.35  ? 465  MET A O   1 
ATOM   3717  C  CB  . MET A 1 465  ? 56.641  66.647  153.194 1.00 75.24  ? 465  MET A CB  1 
ATOM   3718  C  CG  . MET A 1 465  ? 55.240  67.112  152.879 1.00 75.63  ? 465  MET A CG  1 
ATOM   3719  S  SD  . MET A 1 465  ? 54.409  67.708  154.361 1.00 75.43  ? 465  MET A SD  1 
ATOM   3720  C  CE  . MET A 1 465  ? 55.471  69.064  154.826 1.00 72.60  ? 465  MET A CE  1 
ATOM   3721  N  N   . ILE A 1 466  ? 59.167  64.476  152.699 1.00 77.33  ? 466  ILE A N   1 
ATOM   3722  C  CA  . ILE A 1 466  ? 60.490  64.116  153.184 1.00 77.50  ? 466  ILE A CA  1 
ATOM   3723  C  C   . ILE A 1 466  ? 61.440  63.812  152.020 1.00 77.34  ? 466  ILE A C   1 
ATOM   3724  O  O   . ILE A 1 466  ? 61.021  63.203  151.032 1.00 78.79  ? 466  ILE A O   1 
ATOM   3725  C  CB  . ILE A 1 466  ? 60.346  62.934  154.168 1.00 79.95  ? 466  ILE A CB  1 
ATOM   3726  C  CG1 . ILE A 1 466  ? 60.188  63.482  155.588 1.00 79.73  ? 466  ILE A CG1 1 
ATOM   3727  C  CG2 . ILE A 1 466  ? 61.496  61.925  154.052 1.00 81.33  ? 466  ILE A CG2 1 
ATOM   3728  C  CD1 . ILE A 1 466  ? 59.116  62.787  156.401 1.00 83.11  ? 466  ILE A CD1 1 
ATOM   3729  N  N   . PRO A 1 467  ? 62.719  64.236  152.121 1.00 75.93  ? 467  PRO A N   1 
ATOM   3730  C  CA  . PRO A 1 467  ? 63.410  64.963  153.196 1.00 74.61  ? 467  PRO A CA  1 
ATOM   3731  C  C   . PRO A 1 467  ? 63.474  66.483  153.016 1.00 72.12  ? 467  PRO A C   1 
ATOM   3732  O  O   . PRO A 1 467  ? 63.953  67.196  153.901 1.00 71.15  ? 467  PRO A O   1 
ATOM   3733  C  CB  . PRO A 1 467  ? 64.829  64.387  153.134 1.00 74.92  ? 467  PRO A CB  1 
ATOM   3734  C  CG  . PRO A 1 467  ? 64.995  63.885  151.707 1.00 75.51  ? 467  PRO A CG  1 
ATOM   3735  C  CD  . PRO A 1 467  ? 63.648  63.918  151.024 1.00 75.94  ? 467  PRO A CD  1 
ATOM   3736  N  N   . ARG A 1 468  ? 63.007  66.971  151.876 1.00 71.31  ? 468  ARG A N   1 
ATOM   3737  C  CA  . ARG A 1 468  ? 63.008  68.392  151.621 1.00 69.40  ? 468  ARG A CA  1 
ATOM   3738  C  C   . ARG A 1 468  ? 61.762  68.802  150.863 1.00 68.58  ? 468  ARG A C   1 
ATOM   3739  O  O   . ARG A 1 468  ? 61.416  68.213  149.838 1.00 69.26  ? 468  ARG A O   1 
ATOM   3740  C  CB  . ARG A 1 468  ? 64.259  68.798  150.846 1.00 69.06  ? 468  ARG A CB  1 
ATOM   3741  C  CG  . ARG A 1 468  ? 64.672  70.233  151.090 1.00 70.04  ? 468  ARG A CG  1 
ATOM   3742  C  CD  . ARG A 1 468  ? 65.713  70.683  150.086 1.00 74.42  ? 468  ARG A CD  1 
ATOM   3743  N  NE  . ARG A 1 468  ? 66.205  72.021  150.412 1.00 76.61  ? 468  ARG A NE  1 
ATOM   3744  C  CZ  . ARG A 1 468  ? 65.664  73.152  149.957 1.00 78.31  ? 468  ARG A CZ  1 
ATOM   3745  N  NH1 . ARG A 1 468  ? 64.607  73.119  149.138 1.00 78.76  ? 468  ARG A NH1 1 
ATOM   3746  N  NH2 . ARG A 1 468  ? 66.186  74.322  150.321 1.00 78.38  ? 468  ARG A NH2 1 
ATOM   3747  N  N   . ALA A 1 469  ? 61.090  69.812  151.399 1.00 66.90  ? 469  ALA A N   1 
ATOM   3748  C  CA  . ALA A 1 469  ? 59.922  70.404  150.779 1.00 66.19  ? 469  ALA A CA  1 
ATOM   3749  C  C   . ALA A 1 469  ? 59.939  71.891  151.076 1.00 64.26  ? 469  ALA A C   1 
ATOM   3750  O  O   . ALA A 1 469  ? 60.742  72.358  151.881 1.00 63.45  ? 469  ALA A O   1 
ATOM   3751  C  CB  . ALA A 1 469  ? 58.660  69.771  151.325 1.00 67.78  ? 469  ALA A CB  1 
ATOM   3752  N  N   . LYS A 1 470  ? 59.068  72.635  150.407 1.00 63.51  ? 470  LYS A N   1 
ATOM   3753  C  CA  . LYS A 1 470  ? 58.862  74.039  150.726 1.00 62.03  ? 470  LYS A CA  1 
ATOM   3754  C  C   . LYS A 1 470  ? 57.378  74.362  150.764 1.00 62.10  ? 470  LYS A C   1 
ATOM   3755  O  O   . LYS A 1 470  ? 56.537  73.548  150.374 1.00 63.26  ? 470  LYS A O   1 
ATOM   3756  C  CB  . LYS A 1 470  ? 59.609  74.972  149.764 1.00 61.17  ? 470  LYS A CB  1 
ATOM   3757  C  CG  . LYS A 1 470  ? 59.586  74.561  148.304 1.00 62.82  ? 470  LYS A CG  1 
ATOM   3758  C  CD  . LYS A 1 470  ? 60.861  73.831  147.898 1.00 64.38  ? 470  LYS A CD  1 
ATOM   3759  C  CE  . LYS A 1 470  ? 61.986  74.813  147.554 1.00 64.09  ? 470  LYS A CE  1 
ATOM   3760  N  NZ  . LYS A 1 470  ? 62.528  75.517  148.752 1.00 63.72  ? 470  LYS A NZ  1 
ATOM   3761  N  N   . ILE A 1 471  ? 57.065  75.555  151.250 1.00 60.77  ? 471  ILE A N   1 
ATOM   3762  C  CA  . ILE A 1 471  ? 55.686  75.949  151.472 1.00 60.71  ? 471  ILE A CA  1 
ATOM   3763  C  C   . ILE A 1 471  ? 55.454  77.378  151.001 1.00 59.62  ? 471  ILE A C   1 
ATOM   3764  O  O   . ILE A 1 471  ? 56.213  78.286  151.327 1.00 58.81  ? 471  ILE A O   1 
ATOM   3765  C  CB  . ILE A 1 471  ? 55.281  75.768  152.961 1.00 61.03  ? 471  ILE A CB  1 
ATOM   3766  C  CG1 . ILE A 1 471  ? 53.825  76.195  153.188 1.00 61.54  ? 471  ILE A CG1 1 
ATOM   3767  C  CG2 . ILE A 1 471  ? 56.270  76.495  153.894 1.00 60.23  ? 471  ILE A CG2 1 
ATOM   3768  C  CD1 . ILE A 1 471  ? 53.275  75.830  154.553 1.00 62.01  ? 471  ILE A CD1 1 
ATOM   3769  N  N   . LEU A 1 472  ? 54.406  77.555  150.212 1.00 59.79  ? 472  LEU A N   1 
ATOM   3770  C  CA  . LEU A 1 472  ? 54.007  78.863  149.731 1.00 59.16  ? 472  LEU A CA  1 
ATOM   3771  C  C   . LEU A 1 472  ? 52.655  79.210  150.330 1.00 59.25  ? 472  LEU A C   1 
ATOM   3772  O  O   . LEU A 1 472  ? 51.755  78.379  150.365 1.00 60.09  ? 472  LEU A O   1 
ATOM   3773  C  CB  . LEU A 1 472  ? 53.911  78.863  148.200 1.00 59.74  ? 472  LEU A CB  1 
ATOM   3774  C  CG  . LEU A 1 472  ? 53.502  80.186  147.553 1.00 60.58  ? 472  LEU A CG  1 
ATOM   3775  C  CD1 . LEU A 1 472  ? 54.661  81.166  147.591 1.00 60.12  ? 472  LEU A CD1 1 
ATOM   3776  C  CD2 . LEU A 1 472  ? 53.037  79.992  146.120 1.00 62.75  ? 472  LEU A CD2 1 
ATOM   3777  N  N   . ILE A 1 473  ? 52.530  80.431  150.826 1.00 58.38  ? 473  ILE A N   1 
ATOM   3778  C  CA  . ILE A 1 473  ? 51.236  80.958  151.215 1.00 58.74  ? 473  ILE A CA  1 
ATOM   3779  C  C   . ILE A 1 473  ? 50.978  82.164  150.344 1.00 59.09  ? 473  ILE A C   1 
ATOM   3780  O  O   . ILE A 1 473  ? 51.915  82.796  149.858 1.00 58.36  ? 473  ILE A O   1 
ATOM   3781  C  CB  . ILE A 1 473  ? 51.155  81.349  152.713 1.00 58.47  ? 473  ILE A CB  1 
ATOM   3782  C  CG1 . ILE A 1 473  ? 52.138  82.475  153.046 1.00 57.26  ? 473  ILE A CG1 1 
ATOM   3783  C  CG2 . ILE A 1 473  ? 51.381  80.126  153.611 1.00 58.19  ? 473  ILE A CG2 1 
ATOM   3784  C  CD1 . ILE A 1 473  ? 51.735  83.301  154.242 1.00 57.05  ? 473  ILE A CD1 1 
ATOM   3785  N  N   . ALA A 1 474  ? 49.707  82.473  150.138 1.00 60.14  ? 474  ALA A N   1 
ATOM   3786  C  CA  . ALA A 1 474  ? 49.323  83.590  149.296 1.00 60.72  ? 474  ALA A CA  1 
ATOM   3787  C  C   . ALA A 1 474  ? 47.906  84.023  149.623 1.00 61.82  ? 474  ALA A C   1 
ATOM   3788  O  O   . ALA A 1 474  ? 47.070  83.197  149.986 1.00 62.46  ? 474  ALA A O   1 
ATOM   3789  C  CB  . ALA A 1 474  ? 49.435  83.205  147.825 1.00 61.18  ? 474  ALA A CB  1 
ATOM   3790  N  N   . THR A 1 475  ? 47.649  85.321  149.500 1.00 62.26  ? 475  THR A N   1 
ATOM   3791  C  CA  . THR A 1 475  ? 46.296  85.866  149.599 1.00 63.58  ? 475  THR A CA  1 
ATOM   3792  C  C   . THR A 1 475  ? 46.081  86.969  148.558 1.00 64.66  ? 475  THR A C   1 
ATOM   3793  O  O   . THR A 1 475  ? 47.005  87.326  147.821 1.00 64.26  ? 475  THR A O   1 
ATOM   3794  C  CB  . THR A 1 475  ? 45.985  86.401  151.021 1.00 63.26  ? 475  THR A CB  1 
ATOM   3795  O  OG1 . THR A 1 475  ? 44.583  86.677  151.131 1.00 65.34  ? 475  THR A OG1 1 
ATOM   3796  C  CG2 . THR A 1 475  ? 46.759  87.671  151.319 1.00 62.30  ? 475  THR A CG2 1 
ATOM   3797  N  N   . VAL A 1 476  ? 44.857  87.491  148.497 1.00 66.15  ? 476  VAL A N   1 
ATOM   3798  C  CA  . VAL A 1 476  ? 44.560  88.672  147.691 1.00 67.48  ? 476  VAL A CA  1 
ATOM   3799  C  C   . VAL A 1 476  ? 44.320  89.856  148.624 1.00 67.97  ? 476  VAL A C   1 
ATOM   3800  O  O   . VAL A 1 476  ? 43.489  89.787  149.529 1.00 68.33  ? 476  VAL A O   1 
ATOM   3801  C  CB  . VAL A 1 476  ? 43.352  88.440  146.739 1.00 69.29  ? 476  VAL A CB  1 
ATOM   3802  C  CG1 . VAL A 1 476  ? 42.833  89.754  146.168 1.00 70.55  ? 476  VAL A CG1 1 
ATOM   3803  C  CG2 . VAL A 1 476  ? 43.735  87.485  145.622 1.00 69.04  ? 476  VAL A CG2 1 
ATOM   3804  N  N   . ALA A 1 477  ? 45.080  90.924  148.413 1.00 68.39  ? 477  ALA A N   1 
ATOM   3805  C  CA  . ALA A 1 477  ? 44.906  92.163  149.160 1.00 69.39  ? 477  ALA A CA  1 
ATOM   3806  C  C   . ALA A 1 477  ? 44.727  93.330  148.193 1.00 71.47  ? 477  ALA A C   1 
ATOM   3807  O  O   . ALA A 1 477  ? 45.540  93.533  147.289 1.00 71.34  ? 477  ALA A O   1 
ATOM   3808  C  CB  . ALA A 1 477  ? 46.085  92.398  150.068 1.00 68.05  ? 477  ALA A CB  1 
ATOM   3809  N  N   . GLY A 1 478  ? 43.650  94.085  148.390 1.00 73.61  ? 478  GLY A N   1 
ATOM   3810  C  CA  . GLY A 1 478  ? 43.262  95.145  147.467 1.00 76.11  ? 478  GLY A CA  1 
ATOM   3811  C  C   . GLY A 1 478  ? 42.799  94.548  146.155 1.00 77.27  ? 478  GLY A C   1 
ATOM   3812  O  O   . GLY A 1 478  ? 41.624  94.223  145.990 1.00 78.62  ? 478  GLY A O   1 
ATOM   3813  N  N   . ARG A 1 479  ? 43.739  94.400  145.230 1.00 77.02  ? 479  ARG A N   1 
ATOM   3814  C  CA  . ARG A 1 479  ? 43.488  93.808  143.916 1.00 78.22  ? 479  ARG A CA  1 
ATOM   3815  C  C   . ARG A 1 479  ? 44.781  93.171  143.391 1.00 76.37  ? 479  ARG A C   1 
ATOM   3816  O  O   . ARG A 1 479  ? 44.928  92.939  142.193 1.00 77.36  ? 479  ARG A O   1 
ATOM   3817  C  CB  . ARG A 1 479  ? 42.931  94.854  142.927 1.00 81.09  ? 479  ARG A CB  1 
ATOM   3818  C  CG  . ARG A 1 479  ? 43.495  96.270  143.122 1.00 83.44  ? 479  ARG A CG  1 
ATOM   3819  C  CD  . ARG A 1 479  ? 43.862  96.971  141.797 1.00 88.18  ? 479  ARG A CD  1 
ATOM   3820  N  NE  . ARG A 1 479  ? 45.178  97.619  141.871 1.00 88.07  ? 479  ARG A NE  1 
ATOM   3821  C  CZ  . ARG A 1 479  ? 46.337  97.006  141.614 1.00 87.01  ? 479  ARG A CZ  1 
ATOM   3822  N  NH1 . ARG A 1 479  ? 46.353  95.726  141.252 1.00 85.87  ? 479  ARG A NH1 1 
ATOM   3823  N  NH2 . ARG A 1 479  ? 47.485  97.670  141.714 1.00 86.21  ? 479  ARG A NH2 1 
ATOM   3824  N  N   . THR A 1 480  ? 45.707  92.888  144.308 1.00 73.77  ? 480  THR A N   1 
ATOM   3825  C  CA  . THR A 1 480  ? 46.983  92.244  143.990 1.00 71.74  ? 480  THR A CA  1 
ATOM   3826  C  C   . THR A 1 480  ? 47.224  91.002  144.857 1.00 69.29  ? 480  THR A C   1 
ATOM   3827  O  O   . THR A 1 480  ? 46.743  90.929  145.981 1.00 68.76  ? 480  THR A O   1 
ATOM   3828  C  CB  . THR A 1 480  ? 48.186  93.224  144.113 1.00 71.38  ? 480  THR A CB  1 
ATOM   3829  O  OG1 . THR A 1 480  ? 49.380  92.484  144.404 1.00 70.03  ? 480  THR A OG1 1 
ATOM   3830  C  CG2 . THR A 1 480  ? 47.967  94.235  145.227 1.00 71.59  ? 480  THR A CG2 1 
ATOM   3831  N  N   . VAL A 1 481  ? 47.972  90.038  144.322 1.00 67.94  ? 481  VAL A N   1 
ATOM   3832  C  CA  . VAL A 1 481  ? 48.271  88.788  145.017 1.00 65.93  ? 481  VAL A CA  1 
ATOM   3833  C  C   . VAL A 1 481  ? 49.608  88.884  145.735 1.00 64.18  ? 481  VAL A C   1 
ATOM   3834  O  O   . VAL A 1 481  ? 50.664  88.979  145.102 1.00 63.57  ? 481  VAL A O   1 
ATOM   3835  C  CB  . VAL A 1 481  ? 48.308  87.569  144.052 1.00 66.19  ? 481  VAL A CB  1 
ATOM   3836  C  CG1 . VAL A 1 481  ? 48.783  86.307  144.776 1.00 63.92  ? 481  VAL A CG1 1 
ATOM   3837  C  CG2 . VAL A 1 481  ? 46.948  87.329  143.432 1.00 68.14  ? 481  VAL A CG2 1 
ATOM   3838  N  N   . VAL A 1 482  ? 49.552  88.847  147.062 1.00 63.25  ? 482  VAL A N   1 
ATOM   3839  C  CA  . VAL A 1 482  ? 50.758  88.843  147.881 1.00 61.67  ? 482  VAL A CA  1 
ATOM   3840  C  C   . VAL A 1 482  ? 51.042  87.451  148.446 1.00 60.52  ? 482  VAL A C   1 
ATOM   3841  O  O   . VAL A 1 482  ? 50.122  86.711  148.804 1.00 60.65  ? 482  VAL A O   1 
ATOM   3842  C  CB  . VAL A 1 482  ? 50.703  89.898  149.007 1.00 61.73  ? 482  VAL A CB  1 
ATOM   3843  C  CG1 . VAL A 1 482  ? 50.503  91.277  148.421 1.00 63.24  ? 482  VAL A CG1 1 
ATOM   3844  C  CG2 . VAL A 1 482  ? 49.604  89.584  150.011 1.00 61.97  ? 482  VAL A CG2 1 
ATOM   3845  N  N   . TYR A 1 483  ? 52.326  87.113  148.520 1.00 59.50  ? 483  TYR A N   1 
ATOM   3846  C  CA  . TYR A 1 483  ? 52.770  85.792  148.939 1.00 58.68  ? 483  TYR A CA  1 
ATOM   3847  C  C   . TYR A 1 483  ? 53.985  85.855  149.856 1.00 57.35  ? 483  TYR A C   1 
ATOM   3848  O  O   . TYR A 1 483  ? 54.574  86.910  150.055 1.00 57.26  ? 483  TYR A O   1 
ATOM   3849  C  CB  . TYR A 1 483  ? 53.108  84.947  147.707 1.00 59.08  ? 483  TYR A CB  1 
ATOM   3850  C  CG  . TYR A 1 483  ? 53.971  85.678  146.706 1.00 60.24  ? 483  TYR A CG  1 
ATOM   3851  C  CD1 . TYR A 1 483  ? 53.409  86.249  145.562 1.00 62.61  ? 483  TYR A CD1 1 
ATOM   3852  C  CD2 . TYR A 1 483  ? 55.345  85.820  146.908 1.00 59.47  ? 483  TYR A CD2 1 
ATOM   3853  C  CE1 . TYR A 1 483  ? 54.198  86.932  144.645 1.00 63.29  ? 483  TYR A CE1 1 
ATOM   3854  C  CE2 . TYR A 1 483  ? 56.136  86.504  146.001 1.00 60.04  ? 483  TYR A CE2 1 
ATOM   3855  C  CZ  . TYR A 1 483  ? 55.559  87.053  144.873 1.00 61.72  ? 483  TYR A CZ  1 
ATOM   3856  O  OH  . TYR A 1 483  ? 56.343  87.723  143.968 1.00 62.31  ? 483  TYR A OH  1 
ATOM   3857  N  N   . ASP A 1 484  ? 54.331  84.705  150.421 1.00 56.70  ? 484  ASP A N   1 
ATOM   3858  C  CA  . ASP A 1 484  ? 55.619  84.477  151.048 1.00 55.95  ? 484  ASP A CA  1 
ATOM   3859  C  C   . ASP A 1 484  ? 55.875  82.980  150.972 1.00 55.88  ? 484  ASP A C   1 
ATOM   3860  O  O   . ASP A 1 484  ? 54.953  82.206  150.699 1.00 56.06  ? 484  ASP A O   1 
ATOM   3861  C  CB  . ASP A 1 484  ? 55.641  84.969  152.504 1.00 56.03  ? 484  ASP A CB  1 
ATOM   3862  C  CG  . ASP A 1 484  ? 57.064  85.101  153.066 1.00 55.29  ? 484  ASP A CG  1 
ATOM   3863  O  OD1 . ASP A 1 484  ? 58.028  85.110  152.268 1.00 54.88  ? 484  ASP A OD1 1 
ATOM   3864  O  OD2 . ASP A 1 484  ? 57.222  85.203  154.304 1.00 54.56  ? 484  ASP A OD2 1 
ATOM   3865  N  N   . PHE A 1 485  ? 57.125  82.576  151.189 1.00 55.77  ? 485  PHE A N   1 
ATOM   3866  C  CA  . PHE A 1 485  ? 57.477  81.162  151.201 1.00 56.33  ? 485  PHE A CA  1 
ATOM   3867  C  C   . PHE A 1 485  ? 58.536  80.834  152.237 1.00 55.77  ? 485  PHE A C   1 
ATOM   3868  O  O   . PHE A 1 485  ? 59.157  81.719  152.808 1.00 55.49  ? 485  PHE A O   1 
ATOM   3869  C  CB  . PHE A 1 485  ? 57.929  80.699  149.811 1.00 56.90  ? 485  PHE A CB  1 
ATOM   3870  C  CG  . PHE A 1 485  ? 59.382  80.952  149.521 1.00 57.90  ? 485  PHE A CG  1 
ATOM   3871  C  CD1 . PHE A 1 485  ? 59.835  82.236  149.218 1.00 58.58  ? 485  PHE A CD1 1 
ATOM   3872  C  CD2 . PHE A 1 485  ? 60.302  79.898  149.546 1.00 59.02  ? 485  PHE A CD2 1 
ATOM   3873  C  CE1 . PHE A 1 485  ? 61.181  82.475  148.942 1.00 58.83  ? 485  PHE A CE1 1 
ATOM   3874  C  CE2 . PHE A 1 485  ? 61.656  80.122  149.277 1.00 59.46  ? 485  PHE A CE2 1 
ATOM   3875  C  CZ  . PHE A 1 485  ? 62.095  81.415  148.969 1.00 59.36  ? 485  PHE A CZ  1 
ATOM   3876  N  N   . ALA A 1 486  ? 58.731  79.545  152.465 1.00 56.15  ? 486  ALA A N   1 
ATOM   3877  C  CA  . ALA A 1 486  ? 59.706  79.065  153.425 1.00 56.49  ? 486  ALA A CA  1 
ATOM   3878  C  C   . ALA A 1 486  ? 60.133  77.665  153.024 1.00 57.21  ? 486  ALA A C   1 
ATOM   3879  O  O   . ALA A 1 486  ? 59.349  76.920  152.439 1.00 58.02  ? 486  ALA A O   1 
ATOM   3880  C  CB  . ALA A 1 486  ? 59.116  79.053  154.822 1.00 56.77  ? 486  ALA A CB  1 
ATOM   3881  N  N   . ASP A 1 487  ? 61.378  77.315  153.326 1.00 57.58  ? 487  ASP A N   1 
ATOM   3882  C  CA  . ASP A 1 487  ? 61.845  75.949  153.151 1.00 58.73  ? 487  ASP A CA  1 
ATOM   3883  C  C   . ASP A 1 487  ? 61.341  75.108  154.312 1.00 59.53  ? 487  ASP A C   1 
ATOM   3884  O  O   . ASP A 1 487  ? 61.165  75.608  155.425 1.00 59.20  ? 487  ASP A O   1 
ATOM   3885  C  CB  . ASP A 1 487  ? 63.376  75.887  153.098 1.00 58.76  ? 487  ASP A CB  1 
ATOM   3886  C  CG  . ASP A 1 487  ? 63.971  76.864  152.095 1.00 60.13  ? 487  ASP A CG  1 
ATOM   3887  O  OD1 . ASP A 1 487  ? 63.696  76.724  150.877 1.00 62.55  ? 487  ASP A OD1 1 
ATOM   3888  O  OD2 . ASP A 1 487  ? 64.724  77.773  152.528 1.00 61.82  ? 487  ASP A OD2 1 
ATOM   3889  N  N   . LEU A 1 488  ? 61.094  73.835  154.037 1.00 60.82  ? 488  LEU A N   1 
ATOM   3890  C  CA  . LEU A 1 488  ? 60.778  72.879  155.081 1.00 62.62  ? 488  LEU A CA  1 
ATOM   3891  C  C   . LEU A 1 488  ? 61.880  71.836  155.098 1.00 63.67  ? 488  LEU A C   1 
ATOM   3892  O  O   . LEU A 1 488  ? 61.767  70.780  154.480 1.00 64.61  ? 488  LEU A O   1 
ATOM   3893  C  CB  . LEU A 1 488  ? 59.394  72.248  154.868 1.00 63.51  ? 488  LEU A CB  1 
ATOM   3894  C  CG  . LEU A 1 488  ? 58.205  73.201  154.682 1.00 62.79  ? 488  LEU A CG  1 
ATOM   3895  C  CD1 . LEU A 1 488  ? 56.992  72.459  154.144 1.00 63.31  ? 488  LEU A CD1 1 
ATOM   3896  C  CD2 . LEU A 1 488  ? 57.861  73.945  155.966 1.00 61.60  ? 488  LEU A CD2 1 
ATOM   3897  N  N   . ALA A 1 489  ? 62.959  72.156  155.803 1.00 64.27  ? 489  ALA A N   1 
ATOM   3898  C  CA  . ALA A 1 489  ? 64.115  71.273  155.877 1.00 65.81  ? 489  ALA A CA  1 
ATOM   3899  C  C   . ALA A 1 489  ? 64.084  70.430  157.149 1.00 67.78  ? 489  ALA A C   1 
ATOM   3900  O  O   . ALA A 1 489  ? 64.242  70.942  158.258 1.00 68.00  ? 489  ALA A O   1 
ATOM   3901  C  CB  . ALA A 1 489  ? 65.430  72.078  155.762 1.00 64.83  ? 489  ALA A CB  1 
ATOM   3902  N  N   . PHE A 1 490  ? 63.859  69.133  156.969 1.00 69.87  ? 490  PHE A N   1 
ATOM   3903  C  CA  . PHE A 1 490  ? 63.862  68.176  158.067 1.00 72.58  ? 490  PHE A CA  1 
ATOM   3904  C  C   . PHE A 1 490  ? 65.311  67.886  158.456 1.00 73.74  ? 490  PHE A C   1 
ATOM   3905  O  O   . PHE A 1 490  ? 66.024  67.161  157.754 1.00 74.14  ? 490  PHE A O   1 
ATOM   3906  C  CB  . PHE A 1 490  ? 63.119  66.897  157.663 1.00 74.04  ? 490  PHE A CB  1 
ATOM   3907  C  CG  . PHE A 1 490  ? 61.700  67.133  157.194 1.00 73.80  ? 490  PHE A CG  1 
ATOM   3908  C  CD1 . PHE A 1 490  ? 61.444  67.720  155.951 1.00 72.15  ? 490  PHE A CD1 1 
ATOM   3909  C  CD2 . PHE A 1 490  ? 60.621  66.758  157.987 1.00 74.83  ? 490  PHE A CD2 1 
ATOM   3910  C  CE1 . PHE A 1 490  ? 60.137  67.940  155.515 1.00 72.20  ? 490  PHE A CE1 1 
ATOM   3911  C  CE2 . PHE A 1 490  ? 59.307  66.973  157.558 1.00 74.86  ? 490  PHE A CE2 1 
ATOM   3912  C  CZ  . PHE A 1 490  ? 59.065  67.564  156.321 1.00 73.44  ? 490  PHE A CZ  1 
ATOM   3913  N  N   . GLN A 1 491  ? 65.739  68.477  159.572 1.00 74.95  ? 491  GLN A N   1 
ATOM   3914  C  CA  . GLN A 1 491  ? 67.151  68.465  159.985 1.00 76.17  ? 491  GLN A CA  1 
ATOM   3915  C  C   . GLN A 1 491  ? 67.706  67.052  160.228 1.00 78.31  ? 491  GLN A C   1 
ATOM   3916  O  O   . GLN A 1 491  ? 68.877  66.781  159.938 1.00 78.69  ? 491  GLN A O   1 
ATOM   3917  C  CB  . GLN A 1 491  ? 67.392  69.391  161.203 1.00 76.53  ? 491  GLN A CB  1 
ATOM   3918  C  CG  . GLN A 1 491  ? 67.114  68.778  162.607 1.00 79.66  ? 491  GLN A CG  1 
ATOM   3919  C  CD  . GLN A 1 491  ? 65.719  69.101  163.178 1.00 81.24  ? 491  GLN A CD  1 
ATOM   3920  O  OE1 . GLN A 1 491  ? 64.955  69.886  162.606 1.00 80.52  ? 491  GLN A OE1 1 
ATOM   3921  N  NE2 . GLN A 1 491  ? 65.397  68.495  164.326 1.00 83.12  ? 491  GLN A NE2 1 
ATOM   3922  N  N   . GLU A 1 492  ? 66.859  66.160  160.733 1.00 80.02  ? 492  GLU A N   1 
ATOM   3923  C  CA  . GLU A 1 492  ? 67.256  64.782  161.010 1.00 82.52  ? 492  GLU A CA  1 
ATOM   3924  C  C   . GLU A 1 492  ? 67.577  63.977  159.742 1.00 82.32  ? 492  GLU A C   1 
ATOM   3925  O  O   . GLU A 1 492  ? 68.261  62.953  159.811 1.00 84.07  ? 492  GLU A O   1 
ATOM   3926  C  CB  . GLU A 1 492  ? 66.192  64.067  161.868 1.00 84.87  ? 492  GLU A CB  1 
ATOM   3927  C  CG  . GLU A 1 492  ? 64.866  63.725  161.146 1.00 86.19  ? 492  GLU A CG  1 
ATOM   3928  C  CD  . GLU A 1 492  ? 63.818  64.846  161.182 1.00 85.55  ? 492  GLU A CD  1 
ATOM   3929  O  OE1 . GLU A 1 492  ? 62.645  64.537  161.491 1.00 85.88  ? 492  GLU A OE1 1 
ATOM   3930  O  OE2 . GLU A 1 492  ? 64.154  66.023  160.896 1.00 84.54  ? 492  GLU A OE2 1 
ATOM   3931  N  N   . LEU A 1 493  ? 67.094  64.445  158.593 1.00 80.43  ? 493  LEU A N   1 
ATOM   3932  C  CA  . LEU A 1 493  ? 67.287  63.736  157.327 1.00 80.41  ? 493  LEU A CA  1 
ATOM   3933  C  C   . LEU A 1 493  ? 68.228  64.475  156.384 1.00 78.36  ? 493  LEU A C   1 
ATOM   3934  O  O   . LEU A 1 493  ? 68.370  64.109  155.215 1.00 78.34  ? 493  LEU A O   1 
ATOM   3935  C  CB  . LEU A 1 493  ? 65.939  63.487  156.647 1.00 80.68  ? 493  LEU A CB  1 
ATOM   3936  C  CG  . LEU A 1 493  ? 64.937  62.612  157.415 1.00 83.08  ? 493  LEU A CG  1 
ATOM   3937  C  CD1 . LEU A 1 493  ? 63.524  62.979  157.018 1.00 82.37  ? 493  LEU A CD1 1 
ATOM   3938  C  CD2 . LEU A 1 493  ? 65.195  61.114  157.220 1.00 85.41  ? 493  LEU A CD2 1 
ATOM   3939  N  N   . ARG A 1 494  ? 68.889  65.497  156.919 1.00 76.88  ? 494  ARG A N   1 
ATOM   3940  C  CA  . ARG A 1 494  ? 69.689  66.429  156.137 1.00 74.76  ? 494  ARG A CA  1 
ATOM   3941  C  C   . ARG A 1 494  ? 71.185  66.115  156.221 1.00 74.45  ? 494  ARG A C   1 
ATOM   3942  O  O   . ARG A 1 494  ? 71.632  65.437  157.145 1.00 75.90  ? 494  ARG A O   1 
ATOM   3943  C  CB  . ARG A 1 494  ? 69.427  67.846  156.658 1.00 73.71  ? 494  ARG A CB  1 
ATOM   3944  C  CG  . ARG A 1 494  ? 69.390  68.921  155.594 1.00 73.51  ? 494  ARG A CG  1 
ATOM   3945  C  CD  . ARG A 1 494  ? 68.010  69.055  154.947 1.00 76.15  ? 494  ARG A CD  1 
ATOM   3946  N  NE  . ARG A 1 494  ? 68.108  69.814  153.703 1.00 76.80  ? 494  ARG A NE  1 
ATOM   3947  C  CZ  . ARG A 1 494  ? 68.155  69.269  152.491 1.00 78.53  ? 494  ARG A CZ  1 
ATOM   3948  N  NH1 . ARG A 1 494  ? 68.082  67.950  152.343 1.00 80.55  ? 494  ARG A NH1 1 
ATOM   3949  N  NH2 . ARG A 1 494  ? 68.275  70.044  151.421 1.00 78.13  ? 494  ARG A NH2 1 
ATOM   3950  N  N   . ASN A 1 495  ? 71.953  66.594  155.243 1.00 72.52  ? 495  ASN A N   1 
ATOM   3951  C  CA  . ASN A 1 495  ? 73.414  66.608  155.347 1.00 71.90  ? 495  ASN A CA  1 
ATOM   3952  C  C   . ASN A 1 495  ? 73.834  67.959  155.917 1.00 70.20  ? 495  ASN A C   1 
ATOM   3953  O  O   . ASN A 1 495  ? 73.830  68.975  155.220 1.00 68.47  ? 495  ASN A O   1 
ATOM   3954  C  CB  . ASN A 1 495  ? 74.080  66.331  153.989 1.00 71.55  ? 495  ASN A CB  1 
ATOM   3955  C  CG  . ASN A 1 495  ? 75.611  66.206  154.079 1.00 71.83  ? 495  ASN A CG  1 
ATOM   3956  O  OD1 . ASN A 1 495  ? 76.203  66.234  155.165 1.00 72.50  ? 495  ASN A OD1 1 
ATOM   3957  N  ND2 . ASN A 1 495  ? 76.251  66.062  152.922 1.00 70.13  ? 495  ASN A ND2 1 
ATOM   3958  N  N   . ASN A 1 496  ? 74.173  67.954  157.201 1.00 70.68  ? 496  ASN A N   1 
ATOM   3959  C  CA  . ASN A 1 496  ? 74.440  69.174  157.954 1.00 69.67  ? 496  ASN A CA  1 
ATOM   3960  C  C   . ASN A 1 496  ? 75.897  69.618  157.845 1.00 69.05  ? 496  ASN A C   1 
ATOM   3961  O  O   . ASN A 1 496  ? 76.594  69.768  158.848 1.00 70.18  ? 496  ASN A O   1 
ATOM   3962  C  CB  . ASN A 1 496  ? 73.999  69.010  159.422 1.00 71.24  ? 496  ASN A CB  1 
ATOM   3963  C  CG  . ASN A 1 496  ? 74.465  67.677  160.057 1.00 74.03  ? 496  ASN A CG  1 
ATOM   3964  O  OD1 . ASN A 1 496  ? 74.714  66.679  159.369 1.00 74.38  ? 496  ASN A OD1 1 
ATOM   3965  N  ND2 . ASN A 1 496  ? 74.562  67.668  161.385 1.00 75.67  ? 496  ASN A ND2 1 
ATOM   3966  N  N   . PHE A 1 497  ? 76.343  69.842  156.612 1.00 67.36  ? 497  PHE A N   1 
ATOM   3967  C  CA  . PHE A 1 497  ? 77.752  70.105  156.335 1.00 66.76  ? 497  PHE A CA  1 
ATOM   3968  C  C   . PHE A 1 497  ? 78.178  71.535  156.642 1.00 66.03  ? 497  PHE A C   1 
ATOM   3969  O  O   . PHE A 1 497  ? 77.471  72.490  156.333 1.00 64.67  ? 497  PHE A O   1 
ATOM   3970  C  CB  . PHE A 1 497  ? 78.094  69.751  154.885 1.00 65.80  ? 497  PHE A CB  1 
ATOM   3971  C  CG  . PHE A 1 497  ? 79.522  70.052  154.506 1.00 64.66  ? 497  PHE A CG  1 
ATOM   3972  C  CD1 . PHE A 1 497  ? 80.563  69.262  154.982 1.00 64.66  ? 497  PHE A CD1 1 
ATOM   3973  C  CD2 . PHE A 1 497  ? 79.823  71.132  153.675 1.00 62.59  ? 497  PHE A CD2 1 
ATOM   3974  C  CE1 . PHE A 1 497  ? 81.878  69.537  154.638 1.00 64.40  ? 497  PHE A CE1 1 
ATOM   3975  C  CE2 . PHE A 1 497  ? 81.136  71.417  153.324 1.00 61.71  ? 497  PHE A CE2 1 
ATOM   3976  C  CZ  . PHE A 1 497  ? 82.167  70.618  153.806 1.00 63.27  ? 497  PHE A CZ  1 
ATOM   3977  N  N   . ASP A 1 498  ? 79.354  71.664  157.244 1.00 67.17  ? 498  ASP A N   1 
ATOM   3978  C  CA  . ASP A 1 498  ? 79.915  72.968  157.562 1.00 67.37  ? 498  ASP A CA  1 
ATOM   3979  C  C   . ASP A 1 498  ? 81.440  72.958  157.500 1.00 67.97  ? 498  ASP A C   1 
ATOM   3980  O  O   . ASP A 1 498  ? 82.072  71.995  157.918 1.00 69.11  ? 498  ASP A O   1 
ATOM   3981  C  CB  . ASP A 1 498  ? 79.441  73.442  158.939 1.00 68.54  ? 498  ASP A CB  1 
ATOM   3982  C  CG  . ASP A 1 498  ? 79.649  74.928  159.144 1.00 69.58  ? 498  ASP A CG  1 
ATOM   3983  O  OD1 . ASP A 1 498  ? 79.647  75.676  158.134 1.00 69.89  ? 498  ASP A OD1 1 
ATOM   3984  O  OD2 . ASP A 1 498  ? 79.816  75.348  160.310 1.00 71.96  ? 498  ASP A OD2 1 
ATOM   3985  N  N   . LEU A 1 499  ? 82.007  74.040  156.969 1.00 67.43  ? 499  LEU A N   1 
ATOM   3986  C  CA  . LEU A 1 499  ? 83.454  74.215  156.821 1.00 68.14  ? 499  LEU A CA  1 
ATOM   3987  C  C   . LEU A 1 499  ? 83.838  75.543  157.453 1.00 68.89  ? 499  LEU A C   1 
ATOM   3988  O  O   . LEU A 1 499  ? 83.169  76.558  157.249 1.00 67.78  ? 499  LEU A O   1 
ATOM   3989  C  CB  . LEU A 1 499  ? 83.831  74.240  155.338 1.00 66.92  ? 499  LEU A CB  1 
ATOM   3990  C  CG  . LEU A 1 499  ? 85.193  73.801  154.775 1.00 67.38  ? 499  LEU A CG  1 
ATOM   3991  C  CD1 . LEU A 1 499  ? 85.396  74.470  153.425 1.00 65.87  ? 499  LEU A CD1 1 
ATOM   3992  C  CD2 . LEU A 1 499  ? 86.387  74.095  155.671 1.00 68.87  ? 499  LEU A CD2 1 
ATOM   3993  N  N   . SER A 1 500  ? 84.914  75.540  158.225 1.00 71.09  ? 500  SER A N   1 
ATOM   3994  C  CA  . SER A 1 500  ? 85.342  76.756  158.893 1.00 72.89  ? 500  SER A CA  1 
ATOM   3995  C  C   . SER A 1 500  ? 86.856  76.878  158.938 1.00 75.03  ? 500  SER A C   1 
ATOM   3996  O  O   . SER A 1 500  ? 87.584  75.890  158.806 1.00 75.22  ? 500  SER A O   1 
ATOM   3997  C  CB  . SER A 1 500  ? 84.733  76.861  160.303 1.00 74.03  ? 500  SER A CB  1 
ATOM   3998  O  OG  . SER A 1 500  ? 85.448  76.078  161.242 1.00 75.88  ? 500  SER A OG  1 
ATOM   3999  N  N   . ILE A 1 501  ? 87.312  78.108  159.132 1.00 77.01  ? 501  ILE A N   1 
ATOM   4000  C  CA  . ILE A 1 501  ? 88.725  78.419  159.115 1.00 79.96  ? 501  ILE A CA  1 
ATOM   4001  C  C   . ILE A 1 501  ? 89.115  79.044  160.456 1.00 83.25  ? 501  ILE A C   1 
ATOM   4002  O  O   . ILE A 1 501  ? 88.320  79.774  161.065 1.00 83.18  ? 501  ILE A O   1 
ATOM   4003  C  CB  . ILE A 1 501  ? 89.074  79.316  157.876 1.00 78.97  ? 501  ILE A CB  1 
ATOM   4004  C  CG1 . ILE A 1 501  ? 90.331  78.809  157.175 1.00 79.38  ? 501  ILE A CG1 1 
ATOM   4005  C  CG2 . ILE A 1 501  ? 89.130  80.807  158.218 1.00 80.49  ? 501  ILE A CG2 1 
ATOM   4006  C  CD1 . ILE A 1 501  ? 90.070  77.640  156.255 1.00 77.53  ? 501  ILE A CD1 1 
ATOM   4007  N  N   . ASP A 1 502  ? 90.323  78.727  160.925 1.00 86.69  ? 502  ASP A N   1 
ATOM   4008  C  CA  . ASP A 1 502  ? 90.786  79.210  162.229 1.00 90.69  ? 502  ASP A CA  1 
ATOM   4009  C  C   . ASP A 1 502  ? 90.803  80.736  162.288 1.00 92.08  ? 502  ASP A C   1 
ATOM   4010  O  O   . ASP A 1 502  ? 91.255  81.412  161.350 1.00 91.53  ? 502  ASP A O   1 
ATOM   4011  C  CB  . ASP A 1 502  ? 92.141  78.603  162.627 1.00 93.04  ? 502  ASP A CB  1 
ATOM   4012  C  CG  . ASP A 1 502  ? 93.263  78.986  161.681 1.00 93.87  ? 502  ASP A CG  1 
ATOM   4013  O  OD1 . ASP A 1 502  ? 94.155  79.757  162.101 1.00 97.03  ? 502  ASP A OD1 1 
ATOM   4014  O  OD2 . ASP A 1 502  ? 93.254  78.519  160.522 1.00 92.47  ? 502  ASP A OD2 1 
ATOM   4015  N  N   . GLU A 1 503  ? 90.285  81.257  163.400 1.00 94.34  ? 503  GLU A N   1 
ATOM   4016  C  CA  . GLU A 1 503  ? 90.015  82.687  163.571 1.00 95.71  ? 503  GLU A CA  1 
ATOM   4017  C  C   . GLU A 1 503  ? 91.294  83.484  163.796 1.00 98.54  ? 503  GLU A C   1 
ATOM   4018  O  O   . GLU A 1 503  ? 91.555  83.993  164.896 1.00 101.47 ? 503  GLU A O   1 
ATOM   4019  C  CB  . GLU A 1 503  ? 89.005  82.909  164.703 1.00 96.53  ? 503  GLU A CB  1 
ATOM   4020  C  CG  . GLU A 1 503  ? 87.654  82.246  164.433 1.00 95.02  ? 503  GLU A CG  1 
ATOM   4021  C  CD  . GLU A 1 503  ? 86.559  82.698  165.383 1.00 96.47  ? 503  GLU A CD  1 
ATOM   4022  O  OE1 . GLU A 1 503  ? 86.872  83.319  166.428 1.00 99.62  ? 503  GLU A OE1 1 
ATOM   4023  O  OE2 . GLU A 1 503  ? 85.377  82.426  165.077 1.00 94.31  ? 503  GLU A OE2 1 
ATOM   4024  N  N   . GLN A 1 504  ? 92.078  83.581  162.727 1.00 98.03  ? 504  GLN A N   1 
ATOM   4025  C  CA  . GLN A 1 504  ? 93.375  84.240  162.738 1.00 100.56 ? 504  GLN A CA  1 
ATOM   4026  C  C   . GLN A 1 504  ? 93.696  84.808  161.361 1.00 99.08  ? 504  GLN A C   1 
ATOM   4027  O  O   . GLN A 1 504  ? 92.962  84.583  160.391 1.00 96.33  ? 504  GLN A O   1 
ATOM   4028  C  CB  . GLN A 1 504  ? 94.472  83.251  163.147 1.00 102.36 ? 504  GLN A CB  1 
ATOM   4029  C  CG  . GLN A 1 504  ? 94.750  83.186  164.644 1.00 105.86 ? 504  GLN A CG  1 
ATOM   4030  C  CD  . GLN A 1 504  ? 95.637  82.011  165.029 1.00 107.81 ? 504  GLN A CD  1 
ATOM   4031  O  OE1 . GLN A 1 504  ? 96.167  81.302  164.170 1.00 106.76 ? 504  GLN A OE1 1 
ATOM   4032  N  NE2 . GLN A 1 504  ? 95.800  81.801  166.331 1.00 110.94 ? 504  GLN A NE2 1 
ATOM   4033  N  N   . GLU A 1 505  ? 94.796  85.554  161.294 1.00 101.02 ? 505  GLU A N   1 
ATOM   4034  C  CA  . GLU A 1 505  ? 95.352  85.998  160.029 1.00 99.94  ? 505  GLU A CA  1 
ATOM   4035  C  C   . GLU A 1 505  ? 96.045  84.817  159.367 1.00 98.43  ? 505  GLU A C   1 
ATOM   4036  O  O   . GLU A 1 505  ? 96.961  84.214  159.935 1.00 100.19 ? 505  GLU A O   1 
ATOM   4037  C  CB  . GLU A 1 505  ? 96.357  87.130  160.240 1.00 103.28 ? 505  GLU A CB  1 
ATOM   4038  C  CG  . GLU A 1 505  ? 95.769  88.455  160.705 1.00 105.09 ? 505  GLU A CG  1 
ATOM   4039  C  CD  . GLU A 1 505  ? 96.841  89.516  160.892 1.00 109.59 ? 505  GLU A CD  1 
ATOM   4040  O  OE1 . GLU A 1 505  ? 96.637  90.440  161.711 1.00 112.24 ? 505  GLU A OE1 1 
ATOM   4041  O  OE2 . GLU A 1 505  ? 97.896  89.418  160.225 1.00 110.68 ? 505  GLU A OE2 1 
ATOM   4042  N  N   . ILE A 1 506  ? 95.588  84.480  158.170 1.00 95.02  ? 506  ILE A N   1 
ATOM   4043  C  CA  . ILE A 1 506  ? 96.190  83.413  157.395 1.00 93.30  ? 506  ILE A CA  1 
ATOM   4044  C  C   . ILE A 1 506  ? 97.438  83.994  156.744 1.00 94.34  ? 506  ILE A C   1 
ATOM   4045  O  O   . ILE A 1 506  ? 97.369  85.040  156.100 1.00 94.46  ? 506  ILE A O   1 
ATOM   4046  C  CB  . ILE A 1 506  ? 95.196  82.875  156.343 1.00 90.11  ? 506  ILE A CB  1 
ATOM   4047  C  CG1 . ILE A 1 506  ? 94.020  82.156  157.021 1.00 88.96  ? 506  ILE A CG1 1 
ATOM   4048  C  CG2 . ILE A 1 506  ? 95.881  81.928  155.385 1.00 89.37  ? 506  ILE A CG2 1 
ATOM   4049  C  CD1 . ILE A 1 506  ? 92.826  83.044  157.358 1.00 88.64  ? 506  ILE A CD1 1 
ATOM   4050  N  N   . LYS A 1 507  ? 98.577  83.332  156.923 1.00 95.15  ? 507  LYS A N   1 
ATOM   4051  C  CA  . LYS A 1 507  ? 99.849  83.895  156.468 1.00 96.53  ? 507  LYS A CA  1 
ATOM   4052  C  C   . LYS A 1 507  ? 100.624 83.004  155.489 1.00 95.38  ? 507  LYS A C   1 
ATOM   4053  O  O   . LYS A 1 507  ? 100.856 81.828  155.771 1.00 95.32  ? 507  LYS A O   1 
ATOM   4054  C  CB  . LYS A 1 507  ? 100.712 84.298  157.668 1.00 100.05 ? 507  LYS A CB  1 
ATOM   4055  C  CG  . LYS A 1 507  ? 100.157 85.506  158.415 1.00 101.46 ? 507  LYS A CG  1 
ATOM   4056  C  CD  . LYS A 1 507  ? 101.093 85.991  159.499 1.00 105.74 ? 507  LYS A CD  1 
ATOM   4057  C  CE  . LYS A 1 507  ? 100.655 87.347  160.038 1.00 107.24 ? 507  LYS A CE  1 
ATOM   4058  N  NZ  . LYS A 1 507  ? 101.708 87.955  160.907 1.00 111.13 ? 507  LYS A NZ  1 
ATOM   4059  N  N   . PRO A 1 508  ? 101.024 83.570  154.330 1.00 94.60  ? 508  PRO A N   1 
ATOM   4060  C  CA  . PRO A 1 508  ? 101.723 82.856  153.254 1.00 93.57  ? 508  PRO A CA  1 
ATOM   4061  C  C   . PRO A 1 508  ? 102.914 82.050  153.750 1.00 95.15  ? 508  PRO A C   1 
ATOM   4062  O  O   . PRO A 1 508  ? 103.708 82.558  154.539 1.00 98.03  ? 508  PRO A O   1 
ATOM   4063  C  CB  . PRO A 1 508  ? 102.203 83.985  152.329 1.00 94.30  ? 508  PRO A CB  1 
ATOM   4064  C  CG  . PRO A 1 508  ? 101.945 85.262  153.076 1.00 96.06  ? 508  PRO A CG  1 
ATOM   4065  C  CD  . PRO A 1 508  ? 100.809 84.982  153.977 1.00 95.06  ? 508  PRO A CD  1 
ATOM   4066  N  N   . GLY A 1 509  ? 103.022 80.802  153.300 1.00 93.48  ? 509  GLY A N   1 
ATOM   4067  C  CA  . GLY A 1 509  ? 104.111 79.915  153.711 1.00 94.88  ? 509  GLY A CA  1 
ATOM   4068  C  C   . GLY A 1 509  ? 103.837 79.120  154.977 1.00 95.34  ? 509  GLY A C   1 
ATOM   4069  O  O   . GLY A 1 509  ? 104.296 77.985  155.113 1.00 95.69  ? 509  GLY A O   1 
ATOM   4070  N  N   . ARG A 1 510  ? 103.102 79.720  155.912 1.00 95.43  ? 510  ARG A N   1 
ATOM   4071  C  CA  . ARG A 1 510  ? 102.692 79.037  157.134 1.00 95.97  ? 510  ARG A CA  1 
ATOM   4072  C  C   . ARG A 1 510  ? 101.527 78.098  156.833 1.00 92.93  ? 510  ARG A C   1 
ATOM   4073  O  O   . ARG A 1 510  ? 101.032 78.052  155.701 1.00 90.50  ? 510  ARG A O   1 
ATOM   4074  C  CB  . ARG A 1 510  ? 102.320 80.044  158.230 1.00 97.64  ? 510  ARG A CB  1 
ATOM   4075  C  CG  . ARG A 1 510  ? 103.510 80.825  158.785 1.00 102.05 ? 510  ARG A CG  1 
ATOM   4076  C  CD  . ARG A 1 510  ? 103.224 81.382  160.176 1.00 105.75 ? 510  ARG A CD  1 
ATOM   4077  N  NE  . ARG A 1 510  ? 104.427 81.948  160.792 1.00 110.76 ? 510  ARG A NE  1 
ATOM   4078  C  CZ  . ARG A 1 510  ? 104.571 83.218  161.174 1.00 113.07 ? 510  ARG A CZ  1 
ATOM   4079  N  NH1 . ARG A 1 510  ? 103.578 84.089  161.029 1.00 111.69 ? 510  ARG A NH1 1 
ATOM   4080  N  NH2 . ARG A 1 510  ? 105.714 83.617  161.721 1.00 116.57 ? 510  ARG A NH2 1 
ATOM   4081  N  N   . GLN A 1 511  ? 101.095 77.344  157.839 1.00 93.13  ? 511  GLN A N   1 
ATOM   4082  C  CA  . GLN A 1 511  ? 100.013 76.380  157.646 1.00 90.60  ? 511  GLN A CA  1 
ATOM   4083  C  C   . GLN A 1 511  ? 98.710  76.817  158.294 1.00 89.03  ? 511  GLN A C   1 
ATOM   4084  O  O   . GLN A 1 511  ? 98.705  77.575  159.268 1.00 90.59  ? 511  GLN A O   1 
ATOM   4085  C  CB  . GLN A 1 511  ? 100.416 74.978  158.129 1.00 92.03  ? 511  GLN A CB  1 
ATOM   4086  C  CG  . GLN A 1 511  ? 100.454 74.795  159.646 1.00 95.39  ? 511  GLN A CG  1 
ATOM   4087  C  CD  . GLN A 1 511  ? 101.350 73.643  160.086 1.00 98.61  ? 511  GLN A CD  1 
ATOM   4088  O  OE1 . GLN A 1 511  ? 101.911 72.913  159.257 1.00 97.94  ? 511  GLN A OE1 1 
ATOM   4089  N  NE2 . GLN A 1 511  ? 101.495 73.481  161.402 1.00 101.15 ? 511  GLN A NE2 1 
ATOM   4090  N  N   . ILE A 1 512  ? 97.607  76.339  157.728 1.00 85.96  ? 512  ILE A N   1 
ATOM   4091  C  CA  . ILE A 1 512  ? 96.292  76.561  158.313 1.00 84.40  ? 512  ILE A CA  1 
ATOM   4092  C  C   . ILE A 1 512  ? 95.490  75.278  158.470 1.00 82.92  ? 512  ILE A C   1 
ATOM   4093  O  O   . ILE A 1 512  ? 95.719  74.286  157.771 1.00 82.17  ? 512  ILE A O   1 
ATOM   4094  C  CB  . ILE A 1 512  ? 95.454  77.602  157.540 1.00 82.46  ? 512  ILE A CB  1 
ATOM   4095  C  CG1 . ILE A 1 512  ? 95.294  77.203  156.069 1.00 79.94  ? 512  ILE A CG1 1 
ATOM   4096  C  CG2 . ILE A 1 512  ? 96.047  79.006  157.726 1.00 84.55  ? 512  ILE A CG2 1 
ATOM   4097  C  CD1 . ILE A 1 512  ? 94.028  77.748  155.439 1.00 77.34  ? 512  ILE A CD1 1 
ATOM   4098  N  N   . GLU A 1 513  ? 94.541  75.334  159.398 1.00 82.38  ? 513  GLU A N   1 
ATOM   4099  C  CA  . GLU A 1 513  ? 93.739  74.197  159.793 1.00 81.34  ? 513  GLU A CA  1 
ATOM   4100  C  C   . GLU A 1 513  ? 92.319  74.417  159.311 1.00 78.05  ? 513  GLU A C   1 
ATOM   4101  O  O   . GLU A 1 513  ? 91.685  75.417  159.659 1.00 77.49  ? 513  GLU A O   1 
ATOM   4102  C  CB  . GLU A 1 513  ? 93.783  74.053  161.320 1.00 84.02  ? 513  GLU A CB  1 
ATOM   4103  C  CG  . GLU A 1 513  ? 92.967  72.906  161.910 1.00 85.01  ? 513  GLU A CG  1 
ATOM   4104  C  CD  . GLU A 1 513  ? 93.074  72.845  163.425 1.00 88.81  ? 513  GLU A CD  1 
ATOM   4105  O  OE1 . GLU A 1 513  ? 94.153  72.465  163.929 1.00 92.02  ? 513  GLU A OE1 1 
ATOM   4106  O  OE2 . GLU A 1 513  ? 92.083  73.174  164.112 1.00 88.75  ? 513  GLU A OE2 1 
ATOM   4107  N  N   . LEU A 1 514  ? 91.840  73.486  158.492 1.00 75.77  ? 514  LEU A N   1 
ATOM   4108  C  CA  . LEU A 1 514  ? 90.453  73.472  158.050 1.00 72.95  ? 514  LEU A CA  1 
ATOM   4109  C  C   . LEU A 1 514  ? 89.633  72.560  158.953 1.00 73.29  ? 514  LEU A C   1 
ATOM   4110  O  O   . LEU A 1 514  ? 89.971  71.388  159.124 1.00 74.31  ? 514  LEU A O   1 
ATOM   4111  C  CB  . LEU A 1 514  ? 90.354  72.993  156.603 1.00 71.00  ? 514  LEU A CB  1 
ATOM   4112  C  CG  . LEU A 1 514  ? 90.498  74.022  155.489 1.00 69.17  ? 514  LEU A CG  1 
ATOM   4113  C  CD1 . LEU A 1 514  ? 91.949  74.381  155.262 1.00 70.19  ? 514  LEU A CD1 1 
ATOM   4114  C  CD2 . LEU A 1 514  ? 89.894  73.472  154.215 1.00 67.37  ? 514  LEU A CD2 1 
ATOM   4115  N  N   . SER A 1 515  ? 88.569  73.106  159.536 1.00 72.40  ? 515  SER A N   1 
ATOM   4116  C  CA  . SER A 1 515  ? 87.656  72.326  160.370 1.00 72.92  ? 515  SER A CA  1 
ATOM   4117  C  C   . SER A 1 515  ? 86.344  72.115  159.640 1.00 70.60  ? 515  SER A C   1 
ATOM   4118  O  O   . SER A 1 515  ? 85.735  73.071  159.156 1.00 69.13  ? 515  SER A O   1 
ATOM   4119  C  CB  . SER A 1 515  ? 87.388  73.023  161.711 1.00 74.23  ? 515  SER A CB  1 
ATOM   4120  O  OG  . SER A 1 515  ? 88.574  73.139  162.472 1.00 77.28  ? 515  SER A OG  1 
ATOM   4121  N  N   . MET A 1 516  ? 85.910  70.863  159.553 1.00 70.60  ? 516  MET A N   1 
ATOM   4122  C  CA  . MET A 1 516  ? 84.626  70.568  158.932 1.00 68.83  ? 516  MET A CA  1 
ATOM   4123  C  C   . MET A 1 516  ? 83.840  69.468  159.641 1.00 69.71  ? 516  MET A C   1 
ATOM   4124  O  O   . MET A 1 516  ? 84.418  68.528  160.192 1.00 71.70  ? 516  MET A O   1 
ATOM   4125  C  CB  . MET A 1 516  ? 84.777  70.296  157.427 1.00 67.35  ? 516  MET A CB  1 
ATOM   4126  C  CG  . MET A 1 516  ? 85.577  69.070  157.038 1.00 69.00  ? 516  MET A CG  1 
ATOM   4127  S  SD  . MET A 1 516  ? 86.449  69.337  155.473 1.00 68.79  ? 516  MET A SD  1 
ATOM   4128  C  CE  . MET A 1 516  ? 88.061  69.807  156.097 1.00 69.36  ? 516  MET A CE  1 
ATOM   4129  N  N   . SER A 1 517  ? 82.519  69.611  159.627 1.00 68.21  ? 517  SER A N   1 
ATOM   4130  C  CA  . SER A 1 517  ? 81.624  68.638  160.230 1.00 68.82  ? 517  SER A CA  1 
ATOM   4131  C  C   . SER A 1 517  ? 80.450  68.321  159.305 1.00 67.08  ? 517  SER A C   1 
ATOM   4132  O  O   . SER A 1 517  ? 80.072  69.144  158.468 1.00 64.92  ? 517  SER A O   1 
ATOM   4133  C  CB  . SER A 1 517  ? 81.120  69.153  161.577 1.00 69.69  ? 517  SER A CB  1 
ATOM   4134  O  OG  . SER A 1 517  ? 80.533  70.432  161.435 1.00 67.93  ? 517  SER A OG  1 
ATOM   4135  N  N   . GLY A 1 518  ? 79.892  67.121  159.469 1.00 68.07  ? 518  GLY A N   1 
ATOM   4136  C  CA  . GLY A 1 518  ? 78.729  66.652  158.709 1.00 66.95  ? 518  GLY A CA  1 
ATOM   4137  C  C   . GLY A 1 518  ? 78.358  65.235  159.101 1.00 68.73  ? 518  GLY A C   1 
ATOM   4138  O  O   . GLY A 1 518  ? 78.390  64.883  160.285 1.00 70.73  ? 518  GLY A O   1 
ATOM   4139  N  N   . ARG A 1 519  ? 78.012  64.418  158.110 1.00 68.34  ? 519  ARG A N   1 
ATOM   4140  C  CA  . ARG A 1 519  ? 77.686  63.009  158.341 1.00 70.25  ? 519  ARG A CA  1 
ATOM   4141  C  C   . ARG A 1 519  ? 78.923  62.127  158.187 1.00 71.61  ? 519  ARG A C   1 
ATOM   4142  O  O   . ARG A 1 519  ? 79.696  62.306  157.247 1.00 70.68  ? 519  ARG A O   1 
ATOM   4143  C  CB  . ARG A 1 519  ? 76.604  62.531  157.369 1.00 69.86  ? 519  ARG A CB  1 
ATOM   4144  C  CG  . ARG A 1 519  ? 75.314  63.325  157.403 1.00 68.92  ? 519  ARG A CG  1 
ATOM   4145  C  CD  . ARG A 1 519  ? 74.488  62.985  158.615 1.00 70.49  ? 519  ARG A CD  1 
ATOM   4146  N  NE  . ARG A 1 519  ? 73.242  63.743  158.650 1.00 69.83  ? 519  ARG A NE  1 
ATOM   4147  C  CZ  . ARG A 1 519  ? 72.183  63.403  159.381 1.00 71.48  ? 519  ARG A CZ  1 
ATOM   4148  N  NH1 . ARG A 1 519  ? 72.208  62.308  160.131 1.00 73.45  ? 519  ARG A NH1 1 
ATOM   4149  N  NH2 . ARG A 1 519  ? 71.091  64.156  159.356 1.00 70.87  ? 519  ARG A NH2 1 
ATOM   4150  N  N   . PRO A 1 520  ? 79.100  61.158  159.096 1.00 73.91  ? 520  PRO A N   1 
ATOM   4151  C  CA  . PRO A 1 520  ? 80.273  60.290  159.117 1.00 75.84  ? 520  PRO A CA  1 
ATOM   4152  C  C   . PRO A 1 520  ? 80.749  59.797  157.747 1.00 75.30  ? 520  PRO A C   1 
ATOM   4153  O  O   . PRO A 1 520  ? 81.921  59.990  157.399 1.00 75.36  ? 520  PRO A O   1 
ATOM   4154  C  CB  . PRO A 1 520  ? 79.818  59.126  159.999 1.00 78.89  ? 520  PRO A CB  1 
ATOM   4155  C  CG  . PRO A 1 520  ? 78.900  59.774  160.980 1.00 78.40  ? 520  PRO A CG  1 
ATOM   4156  C  CD  . PRO A 1 520  ? 78.173  60.841  160.200 1.00 75.48  ? 520  PRO A CD  1 
ATOM   4157  N  N   . GLY A 1 521  ? 79.866  59.181  156.968 1.00 75.02  ? 521  GLY A N   1 
ATOM   4158  C  CA  . GLY A 1 521  ? 80.278  58.641  155.665 1.00 74.50  ? 521  GLY A CA  1 
ATOM   4159  C  C   . GLY A 1 521  ? 80.621  59.680  154.605 1.00 71.30  ? 521  GLY A C   1 
ATOM   4160  O  O   . GLY A 1 521  ? 81.446  59.436  153.728 1.00 71.06  ? 521  GLY A O   1 
ATOM   4161  N  N   . ALA A 1 522  ? 79.999  60.849  154.718 1.00 68.94  ? 522  ALA A N   1 
ATOM   4162  C  CA  . ALA A 1 522  ? 79.913  61.827  153.635 1.00 66.41  ? 522  ALA A CA  1 
ATOM   4163  C  C   . ALA A 1 522  ? 81.223  62.170  152.906 1.00 65.78  ? 522  ALA A C   1 
ATOM   4164  O  O   . ALA A 1 522  ? 82.282  62.331  153.521 1.00 66.27  ? 522  ALA A O   1 
ATOM   4165  C  CB  . ALA A 1 522  ? 79.217  63.089  154.125 1.00 64.58  ? 522  ALA A CB  1 
ATOM   4166  N  N   . TYR A 1 523  ? 81.116  62.269  151.582 1.00 64.54  ? 523  TYR A N   1 
ATOM   4167  C  CA  . TYR A 1 523  ? 82.187  62.740  150.721 1.00 63.49  ? 523  TYR A CA  1 
ATOM   4168  C  C   . TYR A 1 523  ? 82.249  64.256  150.820 1.00 61.60  ? 523  TYR A C   1 
ATOM   4169  O  O   . TYR A 1 523  ? 81.211  64.917  150.869 1.00 60.52  ? 523  TYR A O   1 
ATOM   4170  C  CB  . TYR A 1 523  ? 81.909  62.333  149.270 1.00 63.11  ? 523  TYR A CB  1 
ATOM   4171  C  CG  . TYR A 1 523  ? 82.752  63.065  148.241 1.00 61.62  ? 523  TYR A CG  1 
ATOM   4172  C  CD1 . TYR A 1 523  ? 83.918  62.490  147.736 1.00 62.66  ? 523  TYR A CD1 1 
ATOM   4173  C  CD2 . TYR A 1 523  ? 82.388  64.333  147.779 1.00 58.51  ? 523  TYR A CD2 1 
ATOM   4174  C  CE1 . TYR A 1 523  ? 84.700  63.156  146.797 1.00 61.21  ? 523  TYR A CE1 1 
ATOM   4175  C  CE2 . TYR A 1 523  ? 83.169  65.008  146.844 1.00 57.80  ? 523  TYR A CE2 1 
ATOM   4176  C  CZ  . TYR A 1 523  ? 84.320  64.410  146.356 1.00 59.09  ? 523  TYR A CZ  1 
ATOM   4177  O  OH  . TYR A 1 523  ? 85.098  65.057  145.423 1.00 58.91  ? 523  TYR A OH  1 
ATOM   4178  N  N   . VAL A 1 524  ? 83.464  64.799  150.836 1.00 61.37  ? 524  VAL A N   1 
ATOM   4179  C  CA  . VAL A 1 524  ? 83.671  66.244  150.875 1.00 59.76  ? 524  VAL A CA  1 
ATOM   4180  C  C   . VAL A 1 524  ? 84.575  66.647  149.724 1.00 59.30  ? 524  VAL A C   1 
ATOM   4181  O  O   . VAL A 1 524  ? 85.646  66.073  149.540 1.00 60.40  ? 524  VAL A O   1 
ATOM   4182  C  CB  . VAL A 1 524  ? 84.299  66.703  152.221 1.00 60.45  ? 524  VAL A CB  1 
ATOM   4183  C  CG1 . VAL A 1 524  ? 84.630  68.193  152.198 1.00 58.96  ? 524  VAL A CG1 1 
ATOM   4184  C  CG2 . VAL A 1 524  ? 83.375  66.386  153.385 1.00 60.77  ? 524  VAL A CG2 1 
ATOM   4185  N  N   . GLY A 1 525  ? 84.123  67.624  148.945 1.00 58.04  ? 525  GLY A N   1 
ATOM   4186  C  CA  . GLY A 1 525  ? 84.918  68.209  147.876 1.00 57.95  ? 525  GLY A CA  1 
ATOM   4187  C  C   . GLY A 1 525  ? 85.264  69.645  148.206 1.00 57.52  ? 525  GLY A C   1 
ATOM   4188  O  O   . GLY A 1 525  ? 84.378  70.457  148.473 1.00 56.53  ? 525  GLY A O   1 
ATOM   4189  N  N   . LEU A 1 526  ? 86.556  69.953  148.193 1.00 58.64  ? 526  LEU A N   1 
ATOM   4190  C  CA  . LEU A 1 526  ? 87.040  71.296  148.494 1.00 58.87  ? 526  LEU A CA  1 
ATOM   4191  C  C   . LEU A 1 526  ? 87.706  71.923  147.287 1.00 59.22  ? 526  LEU A C   1 
ATOM   4192  O  O   . LEU A 1 526  ? 88.247  71.224  146.437 1.00 59.63  ? 526  LEU A O   1 
ATOM   4193  C  CB  . LEU A 1 526  ? 88.032  71.257  149.654 1.00 59.99  ? 526  LEU A CB  1 
ATOM   4194  C  CG  . LEU A 1 526  ? 87.547  70.632  150.961 1.00 60.51  ? 526  LEU A CG  1 
ATOM   4195  C  CD1 . LEU A 1 526  ? 88.717  70.372  151.891 1.00 61.88  ? 526  LEU A CD1 1 
ATOM   4196  C  CD2 . LEU A 1 526  ? 86.496  71.504  151.632 1.00 59.26  ? 526  LEU A CD2 1 
ATOM   4197  N  N   . ALA A 1 527  ? 87.661  73.249  147.223 1.00 59.82  ? 527  ALA A N   1 
ATOM   4198  C  CA  . ALA A 1 527  ? 88.280  74.009  146.147 1.00 60.83  ? 527  ALA A CA  1 
ATOM   4199  C  C   . ALA A 1 527  ? 88.524  75.437  146.594 1.00 61.92  ? 527  ALA A C   1 
ATOM   4200  O  O   . ALA A 1 527  ? 87.686  76.028  147.265 1.00 61.56  ? 527  ALA A O   1 
ATOM   4201  C  CB  . ALA A 1 527  ? 87.396  73.992  144.911 1.00 59.82  ? 527  ALA A CB  1 
ATOM   4202  N  N   . ALA A 1 528  ? 89.673  75.991  146.224 1.00 64.23  ? 528  ALA A N   1 
ATOM   4203  C  CA  . ALA A 1 528  ? 89.949  77.398  146.472 1.00 66.23  ? 528  ALA A CA  1 
ATOM   4204  C  C   . ALA A 1 528  ? 90.343  78.092  145.181 1.00 67.75  ? 528  ALA A C   1 
ATOM   4205  O  O   . ALA A 1 528  ? 91.128  77.564  144.393 1.00 68.25  ? 528  ALA A O   1 
ATOM   4206  C  CB  . ALA A 1 528  ? 91.033  77.559  147.521 1.00 67.43  ? 528  ALA A CB  1 
ATOM   4207  N  N   . TYR A 1 529  ? 89.783  79.274  144.963 1.00 69.54  ? 529  TYR A N   1 
ATOM   4208  C  CA  . TYR A 1 529  ? 90.090  80.065  143.780 1.00 72.00  ? 529  TYR A CA  1 
ATOM   4209  C  C   . TYR A 1 529  ? 90.521  81.453  144.224 1.00 74.45  ? 529  TYR A C   1 
ATOM   4210  O  O   . TYR A 1 529  ? 89.902  82.030  145.118 1.00 74.20  ? 529  TYR A O   1 
ATOM   4211  C  CB  . TYR A 1 529  ? 88.858  80.196  142.876 1.00 71.13  ? 529  TYR A CB  1 
ATOM   4212  C  CG  . TYR A 1 529  ? 88.051  78.926  142.667 1.00 70.81  ? 529  TYR A CG  1 
ATOM   4213  C  CD1 . TYR A 1 529  ? 86.988  78.605  143.516 1.00 70.33  ? 529  TYR A CD1 1 
ATOM   4214  C  CD2 . TYR A 1 529  ? 88.331  78.059  141.606 1.00 71.50  ? 529  TYR A CD2 1 
ATOM   4215  C  CE1 . TYR A 1 529  ? 86.236  77.447  143.327 1.00 69.97  ? 529  TYR A CE1 1 
ATOM   4216  C  CE2 . TYR A 1 529  ? 87.581  76.896  141.405 1.00 71.14  ? 529  TYR A CE2 1 
ATOM   4217  C  CZ  . TYR A 1 529  ? 86.534  76.601  142.270 1.00 70.63  ? 529  TYR A CZ  1 
ATOM   4218  O  OH  . TYR A 1 529  ? 85.787  75.460  142.085 1.00 70.23  ? 529  TYR A OH  1 
ATOM   4219  N  N   . ASP A 1 530  ? 91.577  81.993  143.619 1.00 77.75  ? 530  ASP A N   1 
ATOM   4220  C  CA  . ASP A 1 530  ? 91.898  83.401  143.859 1.00 81.23  ? 530  ASP A CA  1 
ATOM   4221  C  C   . ASP A 1 530  ? 91.012  84.259  142.977 1.00 82.52  ? 530  ASP A C   1 
ATOM   4222  O  O   . ASP A 1 530  ? 90.766  83.921  141.818 1.00 82.21  ? 530  ASP A O   1 
ATOM   4223  C  CB  . ASP A 1 530  ? 93.394  83.734  143.705 1.00 82.89  ? 530  ASP A CB  1 
ATOM   4224  C  CG  . ASP A 1 530  ? 93.918  83.540  142.293 1.00 83.40  ? 530  ASP A CG  1 
ATOM   4225  O  OD1 . ASP A 1 530  ? 93.464  82.603  141.604 1.00 83.05  ? 530  ASP A OD1 1 
ATOM   4226  O  OD2 . ASP A 1 530  ? 94.815  84.314  141.883 1.00 84.43  ? 530  ASP A OD2 1 
ATOM   4227  N  N   . LYS A 1 531  ? 90.503  85.346  143.549 1.00 85.12  ? 531  LYS A N   1 
ATOM   4228  C  CA  . LYS A 1 531  ? 89.548  86.209  142.858 1.00 86.94  ? 531  LYS A CA  1 
ATOM   4229  C  C   . LYS A 1 531  ? 90.162  86.857  141.615 1.00 89.42  ? 531  LYS A C   1 
ATOM   4230  O  O   . LYS A 1 531  ? 89.438  87.238  140.697 1.00 89.46  ? 531  LYS A O   1 
ATOM   4231  C  CB  . LYS A 1 531  ? 88.963  87.260  143.809 1.00 87.51  ? 531  LYS A CB  1 
ATOM   4232  C  CG  . LYS A 1 531  ? 88.184  86.671  144.991 1.00 86.99  ? 531  LYS A CG  1 
ATOM   4233  C  CD  . LYS A 1 531  ? 87.162  87.657  145.564 1.00 88.32  ? 531  LYS A CD  1 
ATOM   4234  C  CE  . LYS A 1 531  ? 87.823  88.819  146.304 1.00 90.90  ? 531  LYS A CE  1 
ATOM   4235  N  NZ  . LYS A 1 531  ? 86.818  89.804  146.797 1.00 91.67  ? 531  LYS A NZ  1 
ATOM   4236  N  N   . ALA A 1 532  ? 91.490  86.958  141.588 1.00 92.37  ? 532  ALA A N   1 
ATOM   4237  C  CA  . ALA A 1 532  ? 92.224  87.388  140.398 1.00 95.50  ? 532  ALA A CA  1 
ATOM   4238  C  C   . ALA A 1 532  ? 91.887  86.523  139.178 1.00 95.84  ? 532  ALA A C   1 
ATOM   4239  O  O   . ALA A 1 532  ? 91.834  87.014  138.051 1.00 96.90  ? 532  ALA A O   1 
ATOM   4240  C  CB  . ALA A 1 532  ? 93.724  87.361  140.664 1.00 96.89  ? 532  ALA A CB  1 
ATOM   4241  N  N   . LEU A 1 533  ? 91.660  85.236  139.418 1.00 96.02  ? 533  LEU A N   1 
ATOM   4242  C  CA  . LEU A 1 533  ? 91.302  84.294  138.369 1.00 96.81  ? 533  LEU A CA  1 
ATOM   4243  C  C   . LEU A 1 533  ? 89.802  84.343  138.104 1.00 96.94  ? 533  LEU A C   1 
ATOM   4244  O  O   . LEU A 1 533  ? 89.354  84.107  136.983 1.00 97.08  ? 533  LEU A O   1 
ATOM   4245  C  CB  . LEU A 1 533  ? 91.713  82.882  138.784 1.00 95.95  ? 533  LEU A CB  1 
ATOM   4246  C  CG  . LEU A 1 533  ? 92.255  81.905  137.743 1.00 96.17  ? 533  LEU A CG  1 
ATOM   4247  C  CD1 . LEU A 1 533  ? 93.652  82.306  137.259 1.00 97.79  ? 533  LEU A CD1 1 
ATOM   4248  C  CD2 . LEU A 1 533  ? 92.284  80.520  138.356 1.00 95.55  ? 533  LEU A CD2 1 
ATOM   4249  N  N   . LEU A 1 534  ? 89.032  84.645  139.144 1.00 97.82  ? 534  LEU A N   1 
ATOM   4250  C  CA  . LEU A 1 534  ? 87.593  84.843  139.003 1.00 98.58  ? 534  LEU A CA  1 
ATOM   4251  C  C   . LEU A 1 534  ? 87.244  86.173  138.332 1.00 100.72 ? 534  LEU A C   1 
ATOM   4252  O  O   . LEU A 1 534  ? 86.222  86.268  137.650 1.00 100.69 ? 534  LEU A O   1 
ATOM   4253  C  CB  . LEU A 1 534  ? 86.886  84.737  140.359 1.00 97.68  ? 534  LEU A CB  1 
ATOM   4254  C  CG  . LEU A 1 534  ? 86.682  83.330  140.935 1.00 97.08  ? 534  LEU A CG  1 
ATOM   4255  C  CD1 . LEU A 1 534  ? 86.074  83.399  142.330 1.00 96.63  ? 534  LEU A CD1 1 
ATOM   4256  C  CD2 . LEU A 1 534  ? 85.820  82.458  140.015 1.00 96.97  ? 534  LEU A CD2 1 
ATOM   4257  N  N   . LEU A 1 535  ? 88.091  87.188  138.520 1.00 103.33 ? 535  LEU A N   1 
ATOM   4258  C  CA  . LEU A 1 535  ? 87.830  88.528  137.986 1.00 105.96 ? 535  LEU A CA  1 
ATOM   4259  C  C   . LEU A 1 535  ? 87.761  88.532  136.461 1.00 107.55 ? 535  LEU A C   1 
ATOM   4260  O  O   . LEU A 1 535  ? 86.724  88.878  135.888 1.00 107.78 ? 535  LEU A O   1 
ATOM   4261  C  CB  . LEU A 1 535  ? 88.875  89.544  138.475 1.00 107.68 ? 535  LEU A CB  1 
ATOM   4262  C  CG  . LEU A 1 535  ? 88.599  91.027  138.190 1.00 109.47 ? 535  LEU A CG  1 
ATOM   4263  C  CD1 . LEU A 1 535  ? 87.720  91.643  139.275 1.00 109.08 ? 535  LEU A CD1 1 
ATOM   4264  C  CD2 . LEU A 1 535  ? 89.897  91.813  138.040 1.00 111.66 ? 535  LEU A CD2 1 
ATOM   4265  N  N   . PHE A 1 536  ? 88.857  88.132  135.817 1.00 109.39 ? 536  PHE A N   1 
ATOM   4266  C  CA  . PHE A 1 536  ? 88.988  88.190  134.354 1.00 111.58 ? 536  PHE A CA  1 
ATOM   4267  C  C   . PHE A 1 536  ? 87.822  87.570  133.583 1.00 111.33 ? 536  PHE A C   1 
ATOM   4268  O  O   . PHE A 1 536  ? 87.462  88.050  132.504 1.00 112.73 ? 536  PHE A O   1 
ATOM   4269  C  CB  . PHE A 1 536  ? 90.318  87.581  133.895 1.00 112.17 ? 536  PHE A CB  1 
ATOM   4270  C  CG  . PHE A 1 536  ? 91.412  88.591  133.708 1.00 114.84 ? 536  PHE A CG  1 
ATOM   4271  C  CD1 . PHE A 1 536  ? 92.255  88.930  134.765 1.00 115.75 ? 536  PHE A CD1 1 
ATOM   4272  C  CD2 . PHE A 1 536  ? 91.601  89.210  132.472 1.00 117.24 ? 536  PHE A CD2 1 
ATOM   4273  C  CE1 . PHE A 1 536  ? 93.277  89.872  134.595 1.00 118.48 ? 536  PHE A CE1 1 
ATOM   4274  C  CE2 . PHE A 1 536  ? 92.619  90.154  132.287 1.00 119.85 ? 536  PHE A CE2 1 
ATOM   4275  C  CZ  . PHE A 1 536  ? 93.460  90.485  133.352 1.00 120.42 ? 536  PHE A CZ  1 
ATOM   4276  N  N   . ASN A 1 537  ? 87.241  86.507  134.135 1.00 110.17 ? 537  ASN A N   1 
ATOM   4277  C  CA  . ASN A 1 537  ? 86.101  85.848  133.503 1.00 110.11 ? 537  ASN A CA  1 
ATOM   4278  C  C   . ASN A 1 537  ? 85.069  85.292  134.489 1.00 108.75 ? 537  ASN A C   1 
ATOM   4279  O  O   . ASN A 1 537  ? 85.002  84.080  134.744 1.00 107.60 ? 537  ASN A O   1 
ATOM   4280  C  CB  . ASN A 1 537  ? 86.551  84.799  132.466 1.00 110.48 ? 537  ASN A CB  1 
ATOM   4281  C  CG  . ASN A 1 537  ? 87.823  84.059  132.873 1.00 110.53 ? 537  ASN A CG  1 
ATOM   4282  O  OD1 . ASN A 1 537  ? 88.849  84.667  133.198 1.00 111.02 ? 537  ASN A OD1 1 
ATOM   4283  N  ND2 . ASN A 1 537  ? 87.762  82.735  132.829 1.00 109.93 ? 537  ASN A ND2 1 
ATOM   4284  N  N   . LYS A 1 538  ? 84.277  86.209  135.043 1.00 109.18 ? 538  LYS A N   1 
ATOM   4285  C  CA  . LYS A 1 538  ? 83.122  85.870  135.876 1.00 108.23 ? 538  LYS A CA  1 
ATOM   4286  C  C   . LYS A 1 538  ? 81.811  85.977  135.086 1.00 108.69 ? 538  LYS A C   1 
ATOM   4287  O  O   . LYS A 1 538  ? 80.737  85.644  135.602 1.00 107.73 ? 538  LYS A O   1 
ATOM   4288  C  CB  . LYS A 1 538  ? 83.069  86.751  137.130 1.00 108.16 ? 538  LYS A CB  1 
ATOM   4289  C  CG  . LYS A 1 538  ? 83.204  88.258  136.885 1.00 109.81 ? 538  LYS A CG  1 
ATOM   4290  C  CD  . LYS A 1 538  ? 82.992  89.052  138.174 1.00 109.88 ? 538  LYS A CD  1 
ATOM   4291  C  CE  . LYS A 1 538  ? 84.078  88.756  139.210 1.00 109.77 ? 538  LYS A CE  1 
ATOM   4292  N  NZ  . LYS A 1 538  ? 83.719  89.235  140.574 1.00 109.30 ? 538  LYS A NZ  1 
ATOM   4293  N  N   . ASN A 1 539  ? 81.917  86.444  133.840 1.00 110.45 ? 539  ASN A N   1 
ATOM   4294  C  CA  . ASN A 1 539  ? 80.784  86.542  132.910 1.00 111.28 ? 539  ASN A CA  1 
ATOM   4295  C  C   . ASN A 1 539  ? 80.149  85.186  132.560 1.00 110.45 ? 539  ASN A C   1 
ATOM   4296  O  O   . ASN A 1 539  ? 78.948  85.110  132.276 1.00 110.57 ? 539  ASN A O   1 
ATOM   4297  C  CB  . ASN A 1 539  ? 81.197  87.288  131.629 1.00 113.44 ? 539  ASN A CB  1 
ATOM   4298  C  CG  . ASN A 1 539  ? 82.322  86.585  130.860 1.00 114.27 ? 539  ASN A CG  1 
ATOM   4299  O  OD1 . ASN A 1 539  ? 83.062  85.761  131.410 1.00 113.38 ? 539  ASN A OD1 1 
ATOM   4300  N  ND2 . ASN A 1 539  ? 82.454  86.919  129.580 1.00 116.15 ? 539  ASN A ND2 1 
ATOM   4301  N  N   . HIS A 1 540  ? 80.964  84.129  132.581 1.00 109.78 ? 540  HIS A N   1 
ATOM   4302  C  CA  . HIS A 1 540  ? 80.492  82.757  132.380 1.00 108.90 ? 540  HIS A CA  1 
ATOM   4303  C  C   . HIS A 1 540  ? 79.892  82.211  133.692 1.00 106.75 ? 540  HIS A C   1 
ATOM   4304  O  O   . HIS A 1 540  ? 79.825  82.930  134.697 1.00 106.16 ? 540  HIS A O   1 
ATOM   4305  C  CB  . HIS A 1 540  ? 81.640  81.867  131.870 1.00 109.50 ? 540  HIS A CB  1 
ATOM   4306  C  CG  . HIS A 1 540  ? 81.235  80.908  130.790 1.00 110.84 ? 540  HIS A CG  1 
ATOM   4307  N  ND1 . HIS A 1 540  ? 81.501  81.134  129.455 1.00 112.94 ? 540  HIS A ND1 1 
ATOM   4308  C  CD2 . HIS A 1 540  ? 80.583  79.721  130.846 1.00 110.89 ? 540  HIS A CD2 1 
ATOM   4309  C  CE1 . HIS A 1 540  ? 81.030  80.130  128.737 1.00 113.82 ? 540  HIS A CE1 1 
ATOM   4310  N  NE2 . HIS A 1 540  ? 80.469  79.258  129.557 1.00 112.79 ? 540  HIS A NE2 1 
ATOM   4311  N  N   . ASP A 1 541  ? 79.462  80.948  133.680 1.00 105.53 ? 541  ASP A N   1 
ATOM   4312  C  CA  . ASP A 1 541  ? 78.766  80.340  134.827 1.00 103.48 ? 541  ASP A CA  1 
ATOM   4313  C  C   . ASP A 1 541  ? 79.694  79.835  135.944 1.00 101.63 ? 541  ASP A C   1 
ATOM   4314  O  O   . ASP A 1 541  ? 80.471  78.895  135.744 1.00 101.71 ? 541  ASP A O   1 
ATOM   4315  C  CB  . ASP A 1 541  ? 77.832  79.213  134.350 1.00 103.93 ? 541  ASP A CB  1 
ATOM   4316  C  CG  . ASP A 1 541  ? 76.660  79.730  133.519 1.00 105.49 ? 541  ASP A CG  1 
ATOM   4317  O  OD1 . ASP A 1 541  ? 75.766  80.397  134.091 1.00 105.63 ? 541  ASP A OD1 1 
ATOM   4318  O  OD2 . ASP A 1 541  ? 76.629  79.464  132.294 1.00 107.37 ? 541  ASP A OD2 1 
ATOM   4319  N  N   . LEU A 1 542  ? 79.601  80.468  137.115 1.00 99.69  ? 542  LEU A N   1 
ATOM   4320  C  CA  . LEU A 1 542  ? 80.324  80.025  138.314 1.00 97.87  ? 542  LEU A CA  1 
ATOM   4321  C  C   . LEU A 1 542  ? 79.790  78.700  138.845 1.00 96.42  ? 542  LEU A C   1 
ATOM   4322  O  O   . LEU A 1 542  ? 78.597  78.405  138.726 1.00 96.18  ? 542  LEU A O   1 
ATOM   4323  C  CB  . LEU A 1 542  ? 80.253  81.082  139.419 1.00 97.46  ? 542  LEU A CB  1 
ATOM   4324  C  CG  . LEU A 1 542  ? 81.517  81.885  139.729 1.00 98.26  ? 542  LEU A CG  1 
ATOM   4325  C  CD1 . LEU A 1 542  ? 81.842  82.913  138.638 1.00 99.61  ? 542  LEU A CD1 1 
ATOM   4326  C  CD2 . LEU A 1 542  ? 81.371  82.561  141.088 1.00 98.12  ? 542  LEU A CD2 1 
ATOM   4327  N  N   . PHE A 1 543  ? 80.678  77.903  139.433 1.00 95.20  ? 543  PHE A N   1 
ATOM   4328  C  CA  . PHE A 1 543  ? 80.287  76.606  139.973 1.00 93.80  ? 543  PHE A CA  1 
ATOM   4329  C  C   . PHE A 1 543  ? 79.439  76.758  141.224 1.00 92.61  ? 543  PHE A C   1 
ATOM   4330  O  O   . PHE A 1 543  ? 78.458  76.036  141.410 1.00 92.25  ? 543  PHE A O   1 
ATOM   4331  C  CB  . PHE A 1 543  ? 81.513  75.746  140.282 1.00 94.00  ? 543  PHE A CB  1 
ATOM   4332  C  CG  . PHE A 1 543  ? 81.201  74.523  141.096 1.00 92.61  ? 543  PHE A CG  1 
ATOM   4333  C  CD1 . PHE A 1 543  ? 80.529  73.447  140.528 1.00 92.23  ? 543  PHE A CD1 1 
ATOM   4334  C  CD2 . PHE A 1 543  ? 81.575  74.451  142.431 1.00 91.52  ? 543  PHE A CD2 1 
ATOM   4335  C  CE1 . PHE A 1 543  ? 80.236  72.315  141.277 1.00 92.02  ? 543  PHE A CE1 1 
ATOM   4336  C  CE2 . PHE A 1 543  ? 81.288  73.322  143.190 1.00 91.16  ? 543  PHE A CE2 1 
ATOM   4337  C  CZ  . PHE A 1 543  ? 80.620  72.253  142.612 1.00 91.51  ? 543  PHE A CZ  1 
ATOM   4338  N  N   . TRP A 1 544  ? 79.825  77.702  142.075 1.00 91.71  ? 544  TRP A N   1 
ATOM   4339  C  CA  . TRP A 1 544  ? 79.173  77.871  143.356 1.00 90.66  ? 544  TRP A CA  1 
ATOM   4340  C  C   . TRP A 1 544  ? 77.729  78.340  143.240 1.00 90.05  ? 544  TRP A C   1 
ATOM   4341  O  O   . TRP A 1 544  ? 76.883  77.964  144.053 1.00 89.63  ? 544  TRP A O   1 
ATOM   4342  C  CB  . TRP A 1 544  ? 79.967  78.797  144.272 1.00 90.83  ? 544  TRP A CB  1 
ATOM   4343  C  CG  . TRP A 1 544  ? 79.564  78.584  145.675 1.00 90.57  ? 544  TRP A CG  1 
ATOM   4344  C  CD1 . TRP A 1 544  ? 78.884  79.452  146.476 1.00 90.47  ? 544  TRP A CD1 1 
ATOM   4345  C  CD2 . TRP A 1 544  ? 79.752  77.387  146.441 1.00 90.82  ? 544  TRP A CD2 1 
ATOM   4346  N  NE1 . TRP A 1 544  ? 78.659  78.880  147.708 1.00 90.57  ? 544  TRP A NE1 1 
ATOM   4347  C  CE2 . TRP A 1 544  ? 79.180  77.612  147.711 1.00 90.69  ? 544  TRP A CE2 1 
ATOM   4348  C  CE3 . TRP A 1 544  ? 80.363  76.150  146.180 1.00 91.05  ? 544  TRP A CE3 1 
ATOM   4349  C  CZ2 . TRP A 1 544  ? 79.200  76.646  148.722 1.00 91.11  ? 544  TRP A CZ2 1 
ATOM   4350  C  CZ3 . TRP A 1 544  ? 80.380  75.189  147.184 1.00 91.47  ? 544  TRP A CZ3 1 
ATOM   4351  C  CH2 . TRP A 1 544  ? 79.803  75.445  148.440 1.00 91.55  ? 544  TRP A CH2 1 
ATOM   4352  N  N   . GLU A 1 545  ? 77.451  79.158  142.231 1.00 90.02  ? 545  GLU A N   1 
ATOM   4353  C  CA  . GLU A 1 545  ? 76.083  79.577  141.949 1.00 89.74  ? 545  GLU A CA  1 
ATOM   4354  C  C   . GLU A 1 545  ? 75.253  78.401  141.441 1.00 89.43  ? 545  GLU A C   1 
ATOM   4355  O  O   . GLU A 1 545  ? 74.091  78.258  141.814 1.00 89.13  ? 545  GLU A O   1 
ATOM   4356  C  CB  . GLU A 1 545  ? 76.059  80.730  140.944 1.00 90.50  ? 545  GLU A CB  1 
ATOM   4357  C  CG  . GLU A 1 545  ? 76.494  82.076  141.521 1.00 91.25  ? 545  GLU A CG  1 
ATOM   4358  C  CD  . GLU A 1 545  ? 76.632  83.159  140.457 1.00 93.23  ? 545  GLU A CD  1 
ATOM   4359  O  OE1 . GLU A 1 545  ? 75.842  83.168  139.484 1.00 93.97  ? 545  GLU A OE1 1 
ATOM   4360  O  OE2 . GLU A 1 545  ? 77.536  84.009  140.598 1.00 94.09  ? 545  GLU A OE2 1 
ATOM   4361  N  N   . ASP A 1 546  ? 75.862  77.563  140.603 1.00 89.54  ? 546  ASP A N   1 
ATOM   4362  C  CA  . ASP A 1 546  ? 75.212  76.368  140.074 1.00 89.68  ? 546  ASP A CA  1 
ATOM   4363  C  C   . ASP A 1 546  ? 74.842  75.412  141.200 1.00 89.14  ? 546  ASP A C   1 
ATOM   4364  O  O   . ASP A 1 546  ? 73.708  74.951  141.283 1.00 89.24  ? 546  ASP A O   1 
ATOM   4365  C  CB  . ASP A 1 546  ? 76.129  75.639  139.080 1.00 90.61  ? 546  ASP A CB  1 
ATOM   4366  C  CG  . ASP A 1 546  ? 76.249  76.349  137.733 1.00 91.55  ? 546  ASP A CG  1 
ATOM   4367  O  OD1 . ASP A 1 546  ? 75.366  77.167  137.385 1.00 92.06  ? 546  ASP A OD1 1 
ATOM   4368  O  OD2 . ASP A 1 546  ? 77.235  76.069  137.011 1.00 91.68  ? 546  ASP A OD2 1 
ATOM   4369  N  N   . ILE A 1 547  ? 75.812  75.131  142.065 1.00 88.71  ? 547  ILE A N   1 
ATOM   4370  C  CA  . ILE A 1 547  ? 75.669  74.134  143.120 1.00 88.54  ? 547  ILE A CA  1 
ATOM   4371  C  C   . ILE A 1 547  ? 74.674  74.605  144.188 1.00 88.26  ? 547  ILE A C   1 
ATOM   4372  O  O   . ILE A 1 547  ? 73.893  73.812  144.709 1.00 88.39  ? 547  ILE A O   1 
ATOM   4373  C  CB  . ILE A 1 547  ? 77.070  73.768  143.728 1.00 88.48  ? 547  ILE A CB  1 
ATOM   4374  C  CG1 . ILE A 1 547  ? 77.270  72.250  143.913 1.00 88.95  ? 547  ILE A CG1 1 
ATOM   4375  C  CG2 . ILE A 1 547  ? 77.405  74.602  144.965 1.00 87.80  ? 547  ILE A CG2 1 
ATOM   4376  C  CD1 . ILE A 1 547  ? 76.114  71.471  144.476 1.00 88.59  ? 547  ILE A CD1 1 
ATOM   4377  N  N   . GLY A 1 548  ? 74.696  75.902  144.485 1.00 88.12  ? 548  GLY A N   1 
ATOM   4378  C  CA  . GLY A 1 548  ? 73.820  76.492  145.494 1.00 88.20  ? 548  GLY A CA  1 
ATOM   4379  C  C   . GLY A 1 548  ? 72.378  76.586  145.037 1.00 88.58  ? 548  GLY A C   1 
ATOM   4380  O  O   . GLY A 1 548  ? 71.453  76.446  145.842 1.00 88.53  ? 548  GLY A O   1 
ATOM   4381  N  N   . GLN A 1 549  ? 72.194  76.825  143.741 1.00 89.10  ? 549  GLN A N   1 
ATOM   4382  C  CA  . GLN A 1 549  ? 70.874  76.896  143.134 1.00 89.76  ? 549  GLN A CA  1 
ATOM   4383  C  C   . GLN A 1 549  ? 70.158  75.542  143.185 1.00 90.50  ? 549  GLN A C   1 
ATOM   4384  O  O   . GLN A 1 549  ? 68.982  75.477  143.548 1.00 90.62  ? 549  GLN A O   1 
ATOM   4385  C  CB  . GLN A 1 549  ? 70.990  77.389  141.691 1.00 90.31  ? 549  GLN A CB  1 
ATOM   4386  C  CG  . GLN A 1 549  ? 69.668  77.552  140.959 1.00 91.51  ? 549  GLN A CG  1 
ATOM   4387  C  CD  . GLN A 1 549  ? 69.823  77.480  139.448 1.00 93.43  ? 549  GLN A CD  1 
ATOM   4388  O  OE1 . GLN A 1 549  ? 69.155  76.681  138.784 1.00 94.03  ? 549  GLN A OE1 1 
ATOM   4389  N  NE2 . GLN A 1 549  ? 70.706  78.315  138.895 1.00 93.46  ? 549  GLN A NE2 1 
ATOM   4390  N  N   . VAL A 1 550  ? 70.872  74.472  142.829 1.00 91.23  ? 550  VAL A N   1 
ATOM   4391  C  CA  . VAL A 1 550  ? 70.306  73.116  142.791 1.00 92.40  ? 550  VAL A CA  1 
ATOM   4392  C  C   . VAL A 1 550  ? 69.874  72.651  144.189 1.00 92.57  ? 550  VAL A C   1 
ATOM   4393  O  O   . VAL A 1 550  ? 68.894  71.918  144.338 1.00 93.21  ? 550  VAL A O   1 
ATOM   4394  C  CB  . VAL A 1 550  ? 71.286  72.109  142.125 1.00 93.02  ? 550  VAL A CB  1 
ATOM   4395  C  CG1 . VAL A 1 550  ? 70.765  70.682  142.216 1.00 94.33  ? 550  VAL A CG1 1 
ATOM   4396  C  CG2 . VAL A 1 550  ? 71.511  72.479  140.666 1.00 93.44  ? 550  VAL A CG2 1 
ATOM   4397  N  N   . PHE A 1 551  ? 70.607  73.107  145.201 1.00 92.33  ? 551  PHE A N   1 
ATOM   4398  C  CA  . PHE A 1 551  ? 70.253  72.915  146.604 1.00 92.78  ? 551  PHE A CA  1 
ATOM   4399  C  C   . PHE A 1 551  ? 68.846  73.456  146.897 1.00 93.20  ? 551  PHE A C   1 
ATOM   4400  O  O   . PHE A 1 551  ? 68.123  72.897  147.726 1.00 93.81  ? 551  PHE A O   1 
ATOM   4401  C  CB  . PHE A 1 551  ? 71.295  73.615  147.482 1.00 92.05  ? 551  PHE A CB  1 
ATOM   4402  C  CG  . PHE A 1 551  ? 71.273  73.200  148.929 1.00 92.24  ? 551  PHE A CG  1 
ATOM   4403  C  CD1 . PHE A 1 551  ? 71.851  71.998  149.335 1.00 92.93  ? 551  PHE A CD1 1 
ATOM   4404  C  CD2 . PHE A 1 551  ? 70.709  74.030  149.896 1.00 91.68  ? 551  PHE A CD2 1 
ATOM   4405  C  CE1 . PHE A 1 551  ? 71.845  71.617  150.681 1.00 93.36  ? 551  PHE A CE1 1 
ATOM   4406  C  CE2 . PHE A 1 551  ? 70.700  73.660  151.245 1.00 92.00  ? 551  PHE A CE2 1 
ATOM   4407  C  CZ  . PHE A 1 551  ? 71.270  72.450  151.636 1.00 92.90  ? 551  PHE A CZ  1 
ATOM   4408  N  N   . ASP A 1 552  ? 68.465  74.529  146.197 1.00 93.35  ? 552  ASP A N   1 
ATOM   4409  C  CA  . ASP A 1 552  ? 67.154  75.175  146.353 1.00 93.69  ? 552  ASP A CA  1 
ATOM   4410  C  C   . ASP A 1 552  ? 66.178  74.812  145.208 1.00 94.89  ? 552  ASP A C   1 
ATOM   4411  O  O   . ASP A 1 552  ? 65.540  73.761  145.255 1.00 95.53  ? 552  ASP A O   1 
ATOM   4412  C  CB  . ASP A 1 552  ? 67.313  76.704  146.494 1.00 92.92  ? 552  ASP A CB  1 
ATOM   4413  C  CG  . ASP A 1 552  ? 68.407  77.106  147.496 1.00 92.47  ? 552  ASP A CG  1 
ATOM   4414  O  OD1 . ASP A 1 552  ? 68.849  76.249  148.291 1.00 93.01  ? 552  ASP A OD1 1 
ATOM   4415  O  OD2 . ASP A 1 552  ? 68.830  78.284  147.492 1.00 91.60  ? 552  ASP A OD2 1 
ATOM   4416  N  N   . GLY A 1 553  ? 66.077  75.671  144.189 1.00 95.50  ? 553  GLY A N   1 
ATOM   4417  C  CA  . GLY A 1 553  ? 65.119  75.485  143.092 1.00 97.18  ? 553  GLY A CA  1 
ATOM   4418  C  C   . GLY A 1 553  ? 65.636  75.776  141.688 1.00 98.29  ? 553  GLY A C   1 
ATOM   4419  O  O   . GLY A 1 553  ? 66.680  75.263  141.282 1.00 98.37  ? 553  GLY A O   1 
ATOM   4420  N  N   . PHE A 1 554  ? 64.892  76.596  140.946 1.00 99.41  ? 554  PHE A N   1 
ATOM   4421  C  CA  . PHE A 1 554  ? 65.170  76.880  139.527 1.00 100.99 ? 554  PHE A CA  1 
ATOM   4422  C  C   . PHE A 1 554  ? 65.450  78.372  139.291 1.00 100.98 ? 554  PHE A C   1 
ATOM   4423  O  O   . PHE A 1 554  ? 65.147  79.205  140.150 1.00 100.56 ? 554  PHE A O   1 
ATOM   4424  C  CB  . PHE A 1 554  ? 63.991  76.425  138.652 1.00 102.62 ? 554  PHE A CB  1 
ATOM   4425  C  CG  . PHE A 1 554  ? 63.674  74.955  138.761 1.00 103.87 ? 554  PHE A CG  1 
ATOM   4426  C  CD1 . PHE A 1 554  ? 62.942  74.461  139.840 1.00 103.56 ? 554  PHE A CD1 1 
ATOM   4427  C  CD2 . PHE A 1 554  ? 64.097  74.066  137.775 1.00 105.80 ? 554  PHE A CD2 1 
ATOM   4428  C  CE1 . PHE A 1 554  ? 62.649  73.105  139.943 1.00 104.80 ? 554  PHE A CE1 1 
ATOM   4429  C  CE2 . PHE A 1 554  ? 63.805  72.704  137.868 1.00 106.77 ? 554  PHE A CE2 1 
ATOM   4430  C  CZ  . PHE A 1 554  ? 63.079  72.225  138.955 1.00 106.34 ? 554  PHE A CZ  1 
ATOM   4431  N  N   . HIS A 1 555  ? 66.020  78.715  138.136 1.00 101.93 ? 555  HIS A N   1 
ATOM   4432  C  CA  . HIS A 1 555  ? 66.375  80.108  137.855 1.00 102.18 ? 555  HIS A CA  1 
ATOM   4433  C  C   . HIS A 1 555  ? 65.723  80.608  136.573 1.00 103.71 ? 555  HIS A C   1 
ATOM   4434  O  O   . HIS A 1 555  ? 65.890  80.014  135.509 1.00 104.90 ? 555  HIS A O   1 
ATOM   4435  C  CB  . HIS A 1 555  ? 67.898  80.269  137.785 1.00 101.92 ? 555  HIS A CB  1 
ATOM   4436  C  CG  . HIS A 1 555  ? 68.373  81.686  137.926 1.00 102.50 ? 555  HIS A CG  1 
ATOM   4437  N  ND1 . HIS A 1 555  ? 68.751  82.229  139.137 1.00 101.80 ? 555  HIS A ND1 1 
ATOM   4438  C  CD2 . HIS A 1 555  ? 68.552  82.664  137.004 1.00 103.79 ? 555  HIS A CD2 1 
ATOM   4439  C  CE1 . HIS A 1 555  ? 69.133  83.481  138.957 1.00 102.37 ? 555  HIS A CE1 1 
ATOM   4440  N  NE2 . HIS A 1 555  ? 69.021  83.771  137.672 1.00 103.69 ? 555  HIS A NE2 1 
ATOM   4441  N  N   . GLU A 1 559  ? 66.432  86.093  133.175 1.00 97.89  ? 559  GLU A N   1 
ATOM   4442  C  CA  . GLU A 1 559  ? 66.602  87.540  133.312 1.00 98.57  ? 559  GLU A CA  1 
ATOM   4443  C  C   . GLU A 1 559  ? 65.441  88.205  134.071 1.00 98.16  ? 559  GLU A C   1 
ATOM   4444  O  O   . GLU A 1 559  ? 64.685  87.531  134.786 1.00 97.09  ? 559  GLU A O   1 
ATOM   4445  C  CB  . GLU A 1 559  ? 66.843  88.207  131.939 1.00 101.02 ? 559  GLU A CB  1 
ATOM   4446  C  CG  . GLU A 1 559  ? 66.044  87.627  130.758 1.00 103.61 ? 559  GLU A CG  1 
ATOM   4447  C  CD  . GLU A 1 559  ? 64.631  88.201  130.623 1.00 106.16 ? 559  GLU A CD  1 
ATOM   4448  O  OE1 . GLU A 1 559  ? 63.758  87.879  131.463 1.00 105.31 ? 559  GLU A OE1 1 
ATOM   4449  O  OE2 . GLU A 1 559  ? 64.389  88.959  129.654 1.00 108.65 ? 559  GLU A OE2 1 
ATOM   4450  N  N   . ASN A 1 560  ? 65.333  89.528  133.918 1.00 98.97  ? 560  ASN A N   1 
ATOM   4451  C  CA  . ASN A 1 560  ? 64.265  90.353  134.507 1.00 98.73  ? 560  ASN A CA  1 
ATOM   4452  C  C   . ASN A 1 560  ? 64.286  90.400  136.045 1.00 96.31  ? 560  ASN A C   1 
ATOM   4453  O  O   . ASN A 1 560  ? 65.310  90.751  136.641 1.00 95.66  ? 560  ASN A O   1 
ATOM   4454  C  CB  . ASN A 1 560  ? 62.884  89.945  133.962 1.00 99.82  ? 560  ASN A CB  1 
ATOM   4455  C  CG  . ASN A 1 560  ? 61.958  91.135  133.760 1.00 101.73 ? 560  ASN A CG  1 
ATOM   4456  O  OD1 . ASN A 1 560  ? 62.321  92.120  133.107 1.00 103.03 ? 560  ASN A OD1 1 
ATOM   4457  N  ND2 . ASN A 1 560  ? 60.748  91.043  134.308 1.00 101.30 ? 560  ASN A ND2 1 
ATOM   4458  N  N   . GLU A 1 561  ? 63.162  90.053  136.673 1.00 94.88  ? 561  GLU A N   1 
ATOM   4459  C  CA  . GLU A 1 561  ? 63.050  90.054  138.138 1.00 92.48  ? 561  GLU A CA  1 
ATOM   4460  C  C   . GLU A 1 561  ? 62.592  88.709  138.711 1.00 90.27  ? 561  GLU A C   1 
ATOM   4461  O  O   . GLU A 1 561  ? 61.833  87.972  138.069 1.00 90.63  ? 561  GLU A O   1 
ATOM   4462  C  CB  . GLU A 1 561  ? 62.136  91.192  138.629 1.00 93.48  ? 561  GLU A CB  1 
ATOM   4463  C  CG  . GLU A 1 561  ? 60.683  91.133  138.136 1.00 94.53  ? 561  GLU A CG  1 
ATOM   4464  C  CD  . GLU A 1 561  ? 59.754  92.089  138.877 1.00 94.83  ? 561  GLU A CD  1 
ATOM   4465  O  OE1 . GLU A 1 561  ? 58.702  92.441  138.310 1.00 95.88  ? 561  GLU A OE1 1 
ATOM   4466  O  OE2 . GLU A 1 561  ? 60.061  92.482  140.024 1.00 94.01  ? 561  GLU A OE2 1 
ATOM   4467  N  N   . PHE A 1 562  ? 63.065  88.416  139.924 1.00 87.79  ? 562  PHE A N   1 
ATOM   4468  C  CA  . PHE A 1 562  ? 62.795  87.164  140.648 1.00 85.46  ? 562  PHE A CA  1 
ATOM   4469  C  C   . PHE A 1 562  ? 61.311  86.791  140.714 1.00 84.90  ? 562  PHE A C   1 
ATOM   4470  O  O   . PHE A 1 562  ? 60.508  87.487  141.332 1.00 84.92  ? 562  PHE A O   1 
ATOM   4471  C  CB  . PHE A 1 562  ? 63.402  87.237  142.063 1.00 84.37  ? 562  PHE A CB  1 
ATOM   4472  C  CG  . PHE A 1 562  ? 63.148  86.014  142.912 1.00 83.58  ? 562  PHE A CG  1 
ATOM   4473  C  CD1 . PHE A 1 562  ? 63.767  84.798  142.618 1.00 83.46  ? 562  PHE A CD1 1 
ATOM   4474  C  CD2 . PHE A 1 562  ? 62.301  86.084  144.019 1.00 83.52  ? 562  PHE A CD2 1 
ATOM   4475  C  CE1 . PHE A 1 562  ? 63.532  83.666  143.406 1.00 82.78  ? 562  PHE A CE1 1 
ATOM   4476  C  CE2 . PHE A 1 562  ? 62.059  84.960  144.810 1.00 82.57  ? 562  PHE A CE2 1 
ATOM   4477  C  CZ  . PHE A 1 562  ? 62.675  83.749  144.504 1.00 82.48  ? 562  PHE A CZ  1 
ATOM   4478  N  N   . ASP A 1 563  ? 60.966  85.689  140.056 1.00 84.12  ? 563  ASP A N   1 
ATOM   4479  C  CA  . ASP A 1 563  ? 59.613  85.153  140.086 1.00 83.79  ? 563  ASP A CA  1 
ATOM   4480  C  C   . ASP A 1 563  ? 59.595  83.964  141.044 1.00 82.04  ? 563  ASP A C   1 
ATOM   4481  O  O   . ASP A 1 563  ? 60.153  82.906  140.747 1.00 81.72  ? 563  ASP A O   1 
ATOM   4482  C  CB  . ASP A 1 563  ? 59.174  84.745  138.672 1.00 85.21  ? 563  ASP A CB  1 
ATOM   4483  C  CG  . ASP A 1 563  ? 57.742  84.214  138.614 1.00 86.47  ? 563  ASP A CG  1 
ATOM   4484  O  OD1 . ASP A 1 563  ? 57.246  83.638  139.607 1.00 86.49  ? 563  ASP A OD1 1 
ATOM   4485  O  OD2 . ASP A 1 563  ? 57.103  84.361  137.550 1.00 88.24  ? 563  ASP A OD2 1 
ATOM   4486  N  N   . ILE A 1 564  ? 58.955  84.141  142.195 1.00 80.72  ? 564  ILE A N   1 
ATOM   4487  C  CA  . ILE A 1 564  ? 58.910  83.085  143.204 1.00 79.20  ? 564  ILE A CA  1 
ATOM   4488  C  C   . ILE A 1 564  ? 58.349  81.780  142.638 1.00 79.36  ? 564  ILE A C   1 
ATOM   4489  O  O   . ILE A 1 564  ? 58.856  80.699  142.940 1.00 78.82  ? 564  ILE A O   1 
ATOM   4490  C  CB  . ILE A 1 564  ? 58.128  83.522  144.475 1.00 78.96  ? 564  ILE A CB  1 
ATOM   4491  C  CG1 . ILE A 1 564  ? 58.405  82.566  145.638 1.00 77.77  ? 564  ILE A CG1 1 
ATOM   4492  C  CG2 . ILE A 1 564  ? 56.623  83.651  144.197 1.00 80.21  ? 564  ILE A CG2 1 
ATOM   4493  C  CD1 . ILE A 1 564  ? 57.772  83.001  146.938 1.00 78.34  ? 564  ILE A CD1 1 
ATOM   4494  N  N   . PHE A 1 565  ? 57.320  81.896  141.802 1.00 80.07  ? 565  PHE A N   1 
ATOM   4495  C  CA  . PHE A 1 565  ? 56.654  80.739  141.220 1.00 80.43  ? 565  PHE A CA  1 
ATOM   4496  C  C   . PHE A 1 565  ? 57.583  80.041  140.240 1.00 80.25  ? 565  PHE A C   1 
ATOM   4497  O  O   . PHE A 1 565  ? 57.712  78.816  140.274 1.00 80.36  ? 565  PHE A O   1 
ATOM   4498  C  CB  . PHE A 1 565  ? 55.346  81.153  140.545 1.00 82.16  ? 565  PHE A CB  1 
ATOM   4499  C  CG  . PHE A 1 565  ? 54.407  81.901  141.454 1.00 81.96  ? 565  PHE A CG  1 
ATOM   4500  C  CD1 . PHE A 1 565  ? 54.385  83.292  141.461 1.00 82.16  ? 565  PHE A CD1 1 
ATOM   4501  C  CD2 . PHE A 1 565  ? 53.544  81.216  142.299 1.00 81.57  ? 565  PHE A CD2 1 
ATOM   4502  C  CE1 . PHE A 1 565  ? 53.524  83.983  142.302 1.00 81.51  ? 565  PHE A CE1 1 
ATOM   4503  C  CE2 . PHE A 1 565  ? 52.680  81.902  143.135 1.00 81.16  ? 565  PHE A CE2 1 
ATOM   4504  C  CZ  . PHE A 1 565  ? 52.674  83.287  143.138 1.00 80.92  ? 565  PHE A CZ  1 
ATOM   4505  N  N   . HIS A 1 566  ? 58.240  80.826  139.387 1.00 79.73  ? 566  HIS A N   1 
ATOM   4506  C  CA  . HIS A 1 566  ? 59.293  80.314  138.516 1.00 79.48  ? 566  HIS A CA  1 
ATOM   4507  C  C   . HIS A 1 566  ? 60.298  79.477  139.309 1.00 77.49  ? 566  HIS A C   1 
ATOM   4508  O  O   . HIS A 1 566  ? 60.597  78.339  138.934 1.00 77.98  ? 566  HIS A O   1 
ATOM   4509  C  CB  . HIS A 1 566  ? 60.026  81.464  137.816 1.00 79.94  ? 566  HIS A CB  1 
ATOM   4510  C  CG  . HIS A 1 566  ? 59.395  81.908  136.531 1.00 82.92  ? 566  HIS A CG  1 
ATOM   4511  N  ND1 . HIS A 1 566  ? 58.038  81.820  136.290 1.00 85.30  ? 566  HIS A ND1 1 
ATOM   4512  C  CD2 . HIS A 1 566  ? 59.936  82.471  135.425 1.00 84.28  ? 566  HIS A CD2 1 
ATOM   4513  C  CE1 . HIS A 1 566  ? 57.775  82.296  135.086 1.00 87.01  ? 566  HIS A CE1 1 
ATOM   4514  N  NE2 . HIS A 1 566  ? 58.909  82.700  134.542 1.00 86.70  ? 566  HIS A NE2 1 
ATOM   4515  N  N   . SER A 1 567  ? 60.794  80.039  140.412 1.00 75.10  ? 567  SER A N   1 
ATOM   4516  C  CA  . SER A 1 567  ? 61.857  79.407  141.186 1.00 73.15  ? 567  SER A CA  1 
ATOM   4517  C  C   . SER A 1 567  ? 61.372  78.220  142.011 1.00 72.35  ? 567  SER A C   1 
ATOM   4518  O  O   . SER A 1 567  ? 62.128  77.277  142.249 1.00 72.19  ? 567  SER A O   1 
ATOM   4519  C  CB  . SER A 1 567  ? 62.586  80.430  142.069 1.00 72.27  ? 567  SER A CB  1 
ATOM   4520  O  OG  . SER A 1 567  ? 61.810  80.817  143.192 1.00 72.17  ? 567  SER A OG  1 
ATOM   4521  N  N   . LEU A 1 568  ? 60.113  78.263  142.440 1.00 71.71  ? 568  LEU A N   1 
ATOM   4522  C  CA  . LEU A 1 568  ? 59.529  77.154  143.192 1.00 70.69  ? 568  LEU A CA  1 
ATOM   4523  C  C   . LEU A 1 568  ? 59.144  75.981  142.291 1.00 71.45  ? 568  LEU A C   1 
ATOM   4524  O  O   . LEU A 1 568  ? 58.788  74.910  142.787 1.00 72.28  ? 568  LEU A O   1 
ATOM   4525  C  CB  . LEU A 1 568  ? 58.313  77.621  143.993 1.00 70.73  ? 568  LEU A CB  1 
ATOM   4526  C  CG  . LEU A 1 568  ? 58.559  78.482  145.232 1.00 69.08  ? 568  LEU A CG  1 
ATOM   4527  C  CD1 . LEU A 1 568  ? 57.251  79.089  145.703 1.00 69.33  ? 568  LEU A CD1 1 
ATOM   4528  C  CD2 . LEU A 1 568  ? 59.207  77.678  146.343 1.00 68.37  ? 568  LEU A CD2 1 
ATOM   4529  N  N   . GLY A 1 569  ? 59.211  76.188  140.976 1.00 71.12  ? 569  GLY A N   1 
ATOM   4530  C  CA  . GLY A 1 569  ? 58.903  75.140  140.003 1.00 71.44  ? 569  GLY A CA  1 
ATOM   4531  C  C   . GLY A 1 569  ? 57.449  75.084  139.556 1.00 72.09  ? 569  GLY A C   1 
ATOM   4532  O  O   . GLY A 1 569  ? 56.957  74.028  139.147 1.00 73.61  ? 569  GLY A O   1 
ATOM   4533  N  N   . LEU A 1 570  ? 56.759  76.220  139.615 1.00 70.83  ? 570  LEU A N   1 
ATOM   4534  C  CA  . LEU A 1 570  ? 55.349  76.266  139.243 1.00 71.34  ? 570  LEU A CA  1 
ATOM   4535  C  C   . LEU A 1 570  ? 54.895  77.536  138.508 1.00 71.08  ? 570  LEU A C   1 
ATOM   4536  O  O   . LEU A 1 570  ? 55.685  78.441  138.249 1.00 70.29  ? 570  LEU A O   1 
ATOM   4537  C  CB  . LEU A 1 570  ? 54.467  75.981  140.468 1.00 71.38  ? 570  LEU A CB  1 
ATOM   4538  C  CG  . LEU A 1 570  ? 54.881  76.374  141.883 1.00 69.23  ? 570  LEU A CG  1 
ATOM   4539  C  CD1 . LEU A 1 570  ? 54.118  77.596  142.346 1.00 69.06  ? 570  LEU A CD1 1 
ATOM   4540  C  CD2 . LEU A 1 570  ? 54.589  75.197  142.784 1.00 68.84  ? 570  LEU A CD2 1 
ATOM   4541  N  N   . PHE A 1 571  ? 53.619  77.573  138.144 1.00 71.59  ? 571  PHE A N   1 
ATOM   4542  C  CA  . PHE A 1 571  ? 53.030  78.759  137.546 1.00 71.24  ? 571  PHE A CA  1 
ATOM   4543  C  C   . PHE A 1 571  ? 51.822  79.214  138.355 1.00 71.00  ? 571  PHE A C   1 
ATOM   4544  O  O   . PHE A 1 571  ? 51.156  78.413  139.019 1.00 70.93  ? 571  PHE A O   1 
ATOM   4545  C  CB  . PHE A 1 571  ? 52.608  78.486  136.101 1.00 73.43  ? 571  PHE A CB  1 
ATOM   4546  C  CG  . PHE A 1 571  ? 51.305  77.750  135.981 1.00 74.24  ? 571  PHE A CG  1 
ATOM   4547  C  CD1 . PHE A 1 571  ? 51.274  76.364  135.992 1.00 74.07  ? 571  PHE A CD1 1 
ATOM   4548  C  CD2 . PHE A 1 571  ? 50.107  78.448  135.870 1.00 74.30  ? 571  PHE A CD2 1 
ATOM   4549  C  CE1 . PHE A 1 571  ? 50.068  75.685  135.893 1.00 75.77  ? 571  PHE A CE1 1 
ATOM   4550  C  CE2 . PHE A 1 571  ? 48.904  77.779  135.772 1.00 75.88  ? 571  PHE A CE2 1 
ATOM   4551  C  CZ  . PHE A 1 571  ? 48.881  76.395  135.781 1.00 76.77  ? 571  PHE A CZ  1 
ATOM   4552  N  N   . ALA A 1 572  ? 51.547  80.509  138.282 1.00 70.54  ? 572  ALA A N   1 
ATOM   4553  C  CA  . ALA A 1 572  ? 50.330  81.068  138.826 1.00 70.55  ? 572  ALA A CA  1 
ATOM   4554  C  C   . ALA A 1 572  ? 49.605  81.825  137.723 1.00 72.62  ? 572  ALA A C   1 
ATOM   4555  O  O   . ALA A 1 572  ? 50.231  82.369  136.810 1.00 72.81  ? 572  ALA A O   1 
ATOM   4556  C  CB  . ALA A 1 572  ? 50.636  81.978  139.985 1.00 68.44  ? 572  ALA A CB  1 
ATOM   4557  N  N   . ARG A 1 573  ? 48.279  81.821  137.810 1.00 74.02  ? 573  ARG A N   1 
ATOM   4558  C  CA  . ARG A 1 573  ? 47.418  82.596  136.932 1.00 76.15  ? 573  ARG A CA  1 
ATOM   4559  C  C   . ARG A 1 573  ? 46.248  83.107  137.769 1.00 76.43  ? 573  ARG A C   1 
ATOM   4560  O  O   . ARG A 1 573  ? 45.814  82.437  138.717 1.00 75.92  ? 573  ARG A O   1 
ATOM   4561  C  CB  . ARG A 1 573  ? 46.899  81.736  135.774 1.00 78.67  ? 573  ARG A CB  1 
ATOM   4562  C  CG  . ARG A 1 573  ? 47.952  81.200  134.807 1.00 78.89  ? 573  ARG A CG  1 
ATOM   4563  C  CD  . ARG A 1 573  ? 48.505  82.276  133.873 1.00 79.76  ? 573  ARG A CD  1 
ATOM   4564  N  NE  . ARG A 1 573  ? 49.403  81.706  132.867 1.00 80.10  ? 573  ARG A NE  1 
ATOM   4565  C  CZ  . ARG A 1 573  ? 50.716  81.546  133.024 1.00 78.31  ? 573  ARG A CZ  1 
ATOM   4566  N  NH1 . ARG A 1 573  ? 51.313  81.920  134.146 1.00 75.62  ? 573  ARG A NH1 1 
ATOM   4567  N  NH2 . ARG A 1 573  ? 51.439  81.012  132.049 1.00 79.43  ? 573  ARG A NH2 1 
ATOM   4568  N  N   . THR A 1 574  ? 45.740  84.287  137.425 1.00 77.33  ? 574  THR A N   1 
ATOM   4569  C  CA  . THR A 1 574  ? 44.627  84.881  138.164 1.00 77.71  ? 574  THR A CA  1 
ATOM   4570  C  C   . THR A 1 574  ? 43.767  85.791  137.284 1.00 80.28  ? 574  THR A C   1 
ATOM   4571  O  O   . THR A 1 574  ? 44.007  85.892  136.079 1.00 81.88  ? 574  THR A O   1 
ATOM   4572  C  CB  . THR A 1 574  ? 45.119  85.634  139.425 1.00 75.35  ? 574  THR A CB  1 
ATOM   4573  O  OG1 . THR A 1 574  ? 43.996  86.003  140.235 1.00 76.02  ? 574  THR A OG1 1 
ATOM   4574  C  CG2 . THR A 1 574  ? 45.911  86.872  139.046 1.00 75.02  ? 574  THR A CG2 1 
ATOM   4575  N  N   . LEU A 1 575  ? 42.766  86.435  137.888 1.00 80.81  ? 575  LEU A N   1 
ATOM   4576  C  CA  . LEU A 1 575  ? 41.886  87.364  137.179 1.00 83.51  ? 575  LEU A CA  1 
ATOM   4577  C  C   . LEU A 1 575  ? 42.683  88.451  136.466 1.00 83.90  ? 575  LEU A C   1 
ATOM   4578  O  O   . LEU A 1 575  ? 43.686  88.941  136.991 1.00 82.23  ? 575  LEU A O   1 
ATOM   4579  C  CB  . LEU A 1 575  ? 40.879  88.006  138.139 1.00 83.73  ? 575  LEU A CB  1 
ATOM   4580  C  CG  . LEU A 1 575  ? 39.787  87.154  138.801 1.00 84.23  ? 575  LEU A CG  1 
ATOM   4581  C  CD1 . LEU A 1 575  ? 39.079  87.959  139.881 1.00 83.93  ? 575  LEU A CD1 1 
ATOM   4582  C  CD2 . LEU A 1 575  ? 38.781  86.617  137.787 1.00 87.56  ? 575  LEU A CD2 1 
ATOM   4583  N  N   . ASP A 1 576  ? 42.229  88.830  135.275 1.00 86.54  ? 576  ASP A N   1 
ATOM   4584  C  CA  . ASP A 1 576  ? 42.949  89.794  134.441 1.00 87.34  ? 576  ASP A CA  1 
ATOM   4585  C  C   . ASP A 1 576  ? 43.296  91.082  135.197 1.00 86.11  ? 576  ASP A C   1 
ATOM   4586  O  O   . ASP A 1 576  ? 44.339  91.691  134.933 1.00 85.71  ? 576  ASP A O   1 
ATOM   4587  C  CB  . ASP A 1 576  ? 42.165  90.142  133.161 1.00 91.03  ? 576  ASP A CB  1 
ATOM   4588  C  CG  . ASP A 1 576  ? 41.362  88.970  132.614 1.00 92.98  ? 576  ASP A CG  1 
ATOM   4589  O  OD1 . ASP A 1 576  ? 41.602  88.571  131.457 1.00 94.34  ? 576  ASP A OD1 1 
ATOM   4590  O  OD2 . ASP A 1 576  ? 40.478  88.455  133.337 1.00 94.20  ? 576  ASP A OD2 1 
ATOM   4591  N  N   . ASP A 1 577  ? 42.427  91.487  136.128 1.00 85.59  ? 577  ASP A N   1 
ATOM   4592  C  CA  . ASP A 1 577  ? 42.614  92.744  136.857 1.00 84.89  ? 577  ASP A CA  1 
ATOM   4593  C  C   . ASP A 1 577  ? 43.317  92.597  138.217 1.00 81.59  ? 577  ASP A C   1 
ATOM   4594  O  O   . ASP A 1 577  ? 43.486  93.576  138.952 1.00 81.15  ? 577  ASP A O   1 
ATOM   4595  C  CB  . ASP A 1 577  ? 41.289  93.509  136.987 1.00 87.18  ? 577  ASP A CB  1 
ATOM   4596  C  CG  . ASP A 1 577  ? 40.295  92.834  137.919 1.00 87.10  ? 577  ASP A CG  1 
ATOM   4597  O  OD1 . ASP A 1 577  ? 40.607  91.771  138.499 1.00 85.88  ? 577  ASP A OD1 1 
ATOM   4598  O  OD2 . ASP A 1 577  ? 39.184  93.385  138.075 1.00 89.38  ? 577  ASP A OD2 1 
ATOM   4599  N  N   . ILE A 1 578  ? 43.714  91.369  138.542 1.00 79.30  ? 578  ILE A N   1 
ATOM   4600  C  CA  . ILE A 1 578  ? 44.544  91.115  139.710 1.00 76.22  ? 578  ILE A CA  1 
ATOM   4601  C  C   . ILE A 1 578  ? 46.004  91.065  139.266 1.00 74.84  ? 578  ILE A C   1 
ATOM   4602  O  O   . ILE A 1 578  ? 46.320  90.422  138.266 1.00 75.23  ? 578  ILE A O   1 
ATOM   4603  C  CB  . ILE A 1 578  ? 44.171  89.779  140.428 1.00 74.91  ? 578  ILE A CB  1 
ATOM   4604  C  CG1 . ILE A 1 578  ? 42.713  89.775  140.913 1.00 75.98  ? 578  ILE A CG1 1 
ATOM   4605  C  CG2 . ILE A 1 578  ? 45.140  89.489  141.577 1.00 71.65  ? 578  ILE A CG2 1 
ATOM   4606  C  CD1 . ILE A 1 578  ? 42.473  90.402  142.281 1.00 74.93  ? 578  ILE A CD1 1 
ATOM   4607  N  N   . LEU A 1 579  ? 46.882  91.743  140.006 1.00 73.30  ? 579  LEU A N   1 
ATOM   4608  C  CA  . LEU A 1 579  ? 48.333  91.674  139.761 1.00 71.95  ? 579  LEU A CA  1 
ATOM   4609  C  C   . LEU A 1 579  ? 49.036  90.776  140.773 1.00 69.19  ? 579  LEU A C   1 
ATOM   4610  O  O   . LEU A 1 579  ? 48.519  90.509  141.854 1.00 68.08  ? 579  LEU A O   1 
ATOM   4611  C  CB  . LEU A 1 579  ? 48.982  93.063  139.823 1.00 72.33  ? 579  LEU A CB  1 
ATOM   4612  C  CG  . LEU A 1 579  ? 48.501  94.221  138.953 1.00 75.35  ? 579  LEU A CG  1 
ATOM   4613  C  CD1 . LEU A 1 579  ? 49.115  95.505  139.472 1.00 76.34  ? 579  LEU A CD1 1 
ATOM   4614  C  CD2 . LEU A 1 579  ? 48.832  94.023  137.478 1.00 76.88  ? 579  LEU A CD2 1 
ATOM   4615  N  N   . PHE A 1 580  ? 50.228  90.322  140.409 1.00 68.16  ? 580  PHE A N   1 
ATOM   4616  C  CA  . PHE A 1 580  ? 51.105  89.638  141.338 1.00 65.98  ? 580  PHE A CA  1 
ATOM   4617  C  C   . PHE A 1 580  ? 52.099  90.626  141.923 1.00 65.37  ? 580  PHE A C   1 
ATOM   4618  O  O   . PHE A 1 580  ? 52.631  91.473  141.214 1.00 66.60  ? 580  PHE A O   1 
ATOM   4619  C  CB  . PHE A 1 580  ? 51.821  88.481  140.642 1.00 65.25  ? 580  PHE A CB  1 
ATOM   4620  C  CG  . PHE A 1 580  ? 50.900  87.366  140.237 1.00 66.46  ? 580  PHE A CG  1 
ATOM   4621  C  CD1 . PHE A 1 580  ? 50.442  87.263  138.928 1.00 68.57  ? 580  PHE A CD1 1 
ATOM   4622  C  CD2 . PHE A 1 580  ? 50.468  86.426  141.175 1.00 65.98  ? 580  PHE A CD2 1 
ATOM   4623  C  CE1 . PHE A 1 580  ? 49.578  86.236  138.549 1.00 69.89  ? 580  PHE A CE1 1 
ATOM   4624  C  CE2 . PHE A 1 580  ? 49.599  85.395  140.811 1.00 67.10  ? 580  PHE A CE2 1 
ATOM   4625  C  CZ  . PHE A 1 580  ? 49.153  85.301  139.492 1.00 69.46  ? 580  PHE A CZ  1 
ATOM   4626  N  N   . ASP A 1 581  ? 52.326  90.530  143.227 1.00 64.36  ? 581  ASP A N   1 
ATOM   4627  C  CA  . ASP A 1 581  ? 53.359  91.314  143.908 1.00 64.07  ? 581  ASP A CA  1 
ATOM   4628  C  C   . ASP A 1 581  ? 54.730  90.718  143.588 1.00 63.24  ? 581  ASP A C   1 
ATOM   4629  O  O   . ASP A 1 581  ? 54.821  89.596  143.089 1.00 62.88  ? 581  ASP A O   1 
ATOM   4630  C  CB  . ASP A 1 581  ? 53.109  91.295  145.420 1.00 63.03  ? 581  ASP A CB  1 
ATOM   4631  C  CG  . ASP A 1 581  ? 53.746  92.469  146.150 1.00 63.19  ? 581  ASP A CG  1 
ATOM   4632  O  OD1 . ASP A 1 581  ? 54.062  93.499  145.514 1.00 63.25  ? 581  ASP A OD1 1 
ATOM   4633  O  OD2 . ASP A 1 581  ? 53.905  92.358  147.388 1.00 63.38  ? 581  ASP A OD2 1 
ATOM   4634  N  N   . SER A 1 582  ? 55.792  91.465  143.873 1.00 63.53  ? 582  SER A N   1 
ATOM   4635  C  CA  . SER A 1 582  ? 57.160  90.987  143.646 1.00 62.77  ? 582  SER A CA  1 
ATOM   4636  C  C   . SER A 1 582  ? 57.776  90.405  144.923 1.00 61.39  ? 582  SER A C   1 
ATOM   4637  O  O   . SER A 1 582  ? 58.927  89.951  144.925 1.00 60.97  ? 582  SER A O   1 
ATOM   4638  C  CB  . SER A 1 582  ? 58.024  92.120  143.095 1.00 63.77  ? 582  SER A CB  1 
ATOM   4639  O  OG  . SER A 1 582  ? 57.711  93.334  143.750 1.00 64.60  ? 582  SER A OG  1 
ATOM   4640  N  N   . GLN A 1 609  ? 99.864  80.690  141.047 1.00 84.95  ? 609  GLN A N   1 
ATOM   4641  C  CA  . GLN A 1 609  ? 98.932  80.410  139.955 1.00 83.71  ? 609  GLN A CA  1 
ATOM   4642  C  C   . GLN A 1 609  ? 98.644  78.907  139.761 1.00 82.48  ? 609  GLN A C   1 
ATOM   4643  O  O   . GLN A 1 609  ? 97.978  78.505  138.795 1.00 81.67  ? 609  GLN A O   1 
ATOM   4644  C  CB  . GLN A 1 609  ? 99.406  81.062  138.645 1.00 84.79  ? 609  GLN A CB  1 
ATOM   4645  C  CG  . GLN A 1 609  ? 100.918 81.083  138.438 1.00 87.60  ? 609  GLN A CG  1 
ATOM   4646  C  CD  . GLN A 1 609  ? 101.529 79.695  138.315 1.00 88.81  ? 609  GLN A CD  1 
ATOM   4647  O  OE1 . GLN A 1 609  ? 100.936 78.788  137.726 1.00 88.02  ? 609  GLN A OE1 1 
ATOM   4648  N  NE2 . GLN A 1 609  ? 102.730 79.527  138.866 1.00 90.81  ? 609  GLN A NE2 1 
ATOM   4649  N  N   . GLU A 1 610  ? 99.150  78.092  140.686 1.00 82.35  ? 610  GLU A N   1 
ATOM   4650  C  CA  . GLU A 1 610  ? 98.833  76.664  140.759 1.00 81.09  ? 610  GLU A CA  1 
ATOM   4651  C  C   . GLU A 1 610  ? 97.562  76.470  141.606 1.00 78.91  ? 610  GLU A C   1 
ATOM   4652  O  O   . GLU A 1 610  ? 97.259  77.307  142.465 1.00 79.05  ? 610  GLU A O   1 
ATOM   4653  C  CB  . GLU A 1 610  ? 100.015 75.921  141.387 1.00 82.68  ? 610  GLU A CB  1 
ATOM   4654  C  CG  . GLU A 1 610  ? 100.034 74.412  141.170 1.00 84.00  ? 610  GLU A CG  1 
ATOM   4655  C  CD  . GLU A 1 610  ? 101.211 73.736  141.868 1.00 87.27  ? 610  GLU A CD  1 
ATOM   4656  O  OE1 . GLU A 1 610  ? 101.474 74.058  143.052 1.00 88.25  ? 610  GLU A OE1 1 
ATOM   4657  O  OE2 . GLU A 1 610  ? 101.870 72.880  141.232 1.00 88.27  ? 610  GLU A OE2 1 
ATOM   4658  N  N   . SER A 1 611  ? 96.820  75.385  141.373 1.00 76.83  ? 611  SER A N   1 
ATOM   4659  C  CA  . SER A 1 611  ? 95.578  75.126  142.129 1.00 74.38  ? 611  SER A CA  1 
ATOM   4660  C  C   . SER A 1 611  ? 95.863  74.763  143.584 1.00 73.80  ? 611  SER A C   1 
ATOM   4661  O  O   . SER A 1 611  ? 96.719  73.928  143.866 1.00 74.89  ? 611  SER A O   1 
ATOM   4662  C  CB  . SER A 1 611  ? 94.726  74.033  141.466 1.00 73.73  ? 611  SER A CB  1 
ATOM   4663  O  OG  . SER A 1 611  ? 95.310  72.748  141.615 1.00 74.48  ? 611  SER A OG  1 
ATOM   4664  N  N   . TRP A 1 612  ? 95.143  75.395  144.501 1.00 71.74  ? 612  TRP A N   1 
ATOM   4665  C  CA  . TRP A 1 612  ? 95.351  75.150  145.919 1.00 71.05  ? 612  TRP A CA  1 
ATOM   4666  C  C   . TRP A 1 612  ? 94.071  74.671  146.603 1.00 69.60  ? 612  TRP A C   1 
ATOM   4667  O  O   . TRP A 1 612  ? 92.979  75.191  146.350 1.00 68.29  ? 612  TRP A O   1 
ATOM   4668  C  CB  . TRP A 1 612  ? 95.905  76.407  146.592 1.00 71.51  ? 612  TRP A CB  1 
ATOM   4669  C  CG  . TRP A 1 612  ? 96.097  76.283  148.067 1.00 71.73  ? 612  TRP A CG  1 
ATOM   4670  C  CD1 . TRP A 1 612  ? 96.809  75.324  148.727 1.00 72.50  ? 612  TRP A CD1 1 
ATOM   4671  C  CD2 . TRP A 1 612  ? 95.579  77.159  149.070 1.00 71.18  ? 612  TRP A CD2 1 
ATOM   4672  N  NE1 . TRP A 1 612  ? 96.762  75.545  150.080 1.00 72.89  ? 612  TRP A NE1 1 
ATOM   4673  C  CE2 . TRP A 1 612  ? 96.012  76.665  150.319 1.00 72.51  ? 612  TRP A CE2 1 
ATOM   4674  C  CE3 . TRP A 1 612  ? 94.790  78.316  149.034 1.00 70.28  ? 612  TRP A CE3 1 
ATOM   4675  C  CZ2 . TRP A 1 612  ? 95.681  77.286  151.524 1.00 73.62  ? 612  TRP A CZ2 1 
ATOM   4676  C  CZ3 . TRP A 1 612  ? 94.461  78.933  150.229 1.00 71.32  ? 612  TRP A CZ3 1 
ATOM   4677  C  CH2 . TRP A 1 612  ? 94.906  78.415  151.460 1.00 73.02  ? 612  TRP A CH2 1 
ATOM   4678  N  N   . LEU A 1 613  ? 94.220  73.670  147.466 1.00 69.57  ? 613  LEU A N   1 
ATOM   4679  C  CA  . LEU A 1 613  ? 93.101  73.064  148.182 1.00 68.31  ? 613  LEU A CA  1 
ATOM   4680  C  C   . LEU A 1 613  ? 92.082  72.387  147.265 1.00 66.74  ? 613  LEU A C   1 
ATOM   4681  O  O   . LEU A 1 613  ? 90.881  72.384  147.550 1.00 65.75  ? 613  LEU A O   1 
ATOM   4682  C  CB  . LEU A 1 613  ? 92.417  74.075  149.119 1.00 68.01  ? 613  LEU A CB  1 
ATOM   4683  C  CG  . LEU A 1 613  ? 93.087  74.374  150.463 1.00 69.14  ? 613  LEU A CG  1 
ATOM   4684  C  CD1 . LEU A 1 613  ? 92.346  75.484  151.191 1.00 68.21  ? 613  LEU A CD1 1 
ATOM   4685  C  CD2 . LEU A 1 613  ? 93.154  73.126  151.321 1.00 69.59  ? 613  LEU A CD2 1 
ATOM   4686  N  N   . TRP A 1 614  ? 92.566  71.817  146.165 1.00 66.52  ? 614  TRP A N   1 
ATOM   4687  C  CA  . TRP A 1 614  ? 91.762  70.894  145.376 1.00 65.65  ? 614  TRP A CA  1 
ATOM   4688  C  C   . TRP A 1 614  ? 91.890  69.521  146.027 1.00 67.11  ? 614  TRP A C   1 
ATOM   4689  O  O   . TRP A 1 614  ? 92.659  68.661  145.587 1.00 68.11  ? 614  TRP A O   1 
ATOM   4690  C  CB  . TRP A 1 614  ? 92.201  70.863  143.911 1.00 65.04  ? 614  TRP A CB  1 
ATOM   4691  C  CG  . TRP A 1 614  ? 91.338  69.979  143.055 1.00 63.66  ? 614  TRP A CG  1 
ATOM   4692  C  CD1 . TRP A 1 614  ? 91.585  68.679  142.710 1.00 63.98  ? 614  TRP A CD1 1 
ATOM   4693  C  CD2 . TRP A 1 614  ? 90.087  70.323  142.447 1.00 61.61  ? 614  TRP A CD2 1 
ATOM   4694  N  NE1 . TRP A 1 614  ? 90.568  68.194  141.924 1.00 63.59  ? 614  TRP A NE1 1 
ATOM   4695  C  CE2 . TRP A 1 614  ? 89.636  69.183  141.744 1.00 62.24  ? 614  TRP A CE2 1 
ATOM   4696  C  CE3 . TRP A 1 614  ? 89.303  71.483  142.429 1.00 60.31  ? 614  TRP A CE3 1 
ATOM   4697  C  CZ2 . TRP A 1 614  ? 88.436  69.168  141.027 1.00 61.84  ? 614  TRP A CZ2 1 
ATOM   4698  C  CZ3 . TRP A 1 614  ? 88.106  71.468  141.713 1.00 60.43  ? 614  TRP A CZ3 1 
ATOM   4699  C  CH2 . TRP A 1 614  ? 87.685  70.315  141.025 1.00 60.76  ? 614  TRP A CH2 1 
ATOM   4700  N  N   . LYS A 1 615  ? 91.142  69.343  147.107 1.00 67.62  ? 615  LYS A N   1 
ATOM   4701  C  CA  . LYS A 1 615  ? 91.196  68.127  147.890 1.00 69.41  ? 615  LYS A CA  1 
ATOM   4702  C  C   . LYS A 1 615  ? 89.803  67.547  148.021 1.00 69.17  ? 615  LYS A C   1 
ATOM   4703  O  O   . LYS A 1 615  ? 88.814  68.282  148.088 1.00 67.85  ? 615  LYS A O   1 
ATOM   4704  C  CB  . LYS A 1 615  ? 91.793  68.407  149.277 1.00 70.41  ? 615  LYS A CB  1 
ATOM   4705  C  CG  . LYS A 1 615  ? 93.260  68.837  149.254 1.00 72.08  ? 615  LYS A CG  1 
ATOM   4706  C  CD  . LYS A 1 615  ? 94.220  67.639  149.303 1.00 75.03  ? 615  LYS A CD  1 
ATOM   4707  C  CE  . LYS A 1 615  ? 95.337  67.735  148.246 1.00 75.26  ? 615  LYS A CE  1 
ATOM   4708  N  NZ  . LYS A 1 615  ? 96.145  68.988  148.312 1.00 75.08  ? 615  LYS A NZ  1 
ATOM   4709  N  N   . ASN A 1 616  ? 89.732  66.222  148.020 1.00 70.76  ? 616  ASN A N   1 
ATOM   4710  C  CA  . ASN A 1 616  ? 88.533  65.531  148.446 1.00 71.38  ? 616  ASN A CA  1 
ATOM   4711  C  C   . ASN A 1 616  ? 88.850  64.739  149.701 1.00 72.74  ? 616  ASN A C   1 
ATOM   4712  O  O   . ASN A 1 616  ? 89.942  64.192  149.844 1.00 74.20  ? 616  ASN A O   1 
ATOM   4713  C  CB  . ASN A 1 616  ? 87.951  64.643  147.339 1.00 72.06  ? 616  ASN A CB  1 
ATOM   4714  C  CG  . ASN A 1 616  ? 88.803  63.423  147.045 1.00 76.63  ? 616  ASN A CG  1 
ATOM   4715  O  OD1 . ASN A 1 616  ? 89.736  63.484  146.244 1.00 77.62  ? 616  ASN A OD1 1 
ATOM   4716  N  ND2 . ASN A 1 616  ? 88.476  62.303  147.692 1.00 83.05  ? 616  ASN A ND2 1 
ATOM   4717  N  N   . VAL A 1 617  ? 87.898  64.696  150.617 1.00 72.50  ? 617  VAL A N   1 
ATOM   4718  C  CA  . VAL A 1 617  ? 88.103  64.015  151.881 1.00 74.22  ? 617  VAL A CA  1 
ATOM   4719  C  C   . VAL A 1 617  ? 86.775  63.401  152.329 1.00 74.51  ? 617  VAL A C   1 
ATOM   4720  O  O   . VAL A 1 617  ? 85.744  63.630  151.692 1.00 73.12  ? 617  VAL A O   1 
ATOM   4721  C  CB  . VAL A 1 617  ? 88.718  64.988  152.936 1.00 74.21  ? 617  VAL A CB  1 
ATOM   4722  C  CG1 . VAL A 1 617  ? 87.661  65.907  153.546 1.00 72.68  ? 617  VAL A CG1 1 
ATOM   4723  C  CG2 . VAL A 1 617  ? 89.468  64.226  154.010 1.00 77.07  ? 617  VAL A CG2 1 
ATOM   4724  N  N   . SER A 1 618  ? 86.809  62.601  153.392 1.00 76.51  ? 618  SER A N   1 
ATOM   4725  C  CA  . SER A 1 618  ? 85.597  62.053  153.998 1.00 77.10  ? 618  SER A CA  1 
ATOM   4726  C  C   . SER A 1 618  ? 85.503  62.524  155.439 1.00 77.69  ? 618  SER A C   1 
ATOM   4727  O  O   . SER A 1 618  ? 86.518  62.808  156.061 1.00 78.46  ? 618  SER A O   1 
ATOM   4728  C  CB  . SER A 1 618  ? 85.614  60.530  153.948 1.00 79.40  ? 618  SER A CB  1 
ATOM   4729  O  OG  . SER A 1 618  ? 86.648  60.025  154.771 1.00 82.10  ? 618  SER A OG  1 
ATOM   4730  N  N   . ILE A 1 619  ? 84.285  62.585  155.969 1.00 77.59  ? 619  ILE A N   1 
ATOM   4731  C  CA  . ILE A 1 619  ? 84.041  63.162  157.292 1.00 78.04  ? 619  ILE A CA  1 
ATOM   4732  C  C   . ILE A 1 619  ? 84.431  62.258  158.466 1.00 81.16  ? 619  ILE A C   1 
ATOM   4733  O  O   . ILE A 1 619  ? 84.670  62.742  159.573 1.00 82.21  ? 619  ILE A O   1 
ATOM   4734  C  CB  . ILE A 1 619  ? 82.596  63.691  157.407 1.00 76.53  ? 619  ILE A CB  1 
ATOM   4735  C  CG1 . ILE A 1 619  ? 82.513  65.081  156.780 1.00 74.19  ? 619  ILE A CG1 1 
ATOM   4736  C  CG2 . ILE A 1 619  ? 82.148  63.777  158.846 1.00 77.41  ? 619  ILE A CG2 1 
ATOM   4737  C  CD1 . ILE A 1 619  ? 81.130  65.467  156.318 1.00 73.57  ? 619  ILE A CD1 1 
ATOM   4738  N  N   . GLY A 1 620  ? 84.503  60.953  158.226 1.00 83.02  ? 620  GLY A N   1 
ATOM   4739  C  CA  . GLY A 1 620  ? 85.029  60.021  159.226 1.00 86.35  ? 620  GLY A CA  1 
ATOM   4740  C  C   . GLY A 1 620  ? 84.212  59.842  160.496 1.00 87.98  ? 620  GLY A C   1 
ATOM   4741  O  O   . GLY A 1 620  ? 83.170  60.479  160.681 1.00 86.42  ? 620  GLY A O   1 
ATOM   4742  N  N   . ARG A 1 621  ? 84.726  58.984  161.377 1.00 91.31  ? 621  ARG A N   1 
ATOM   4743  C  CA  . ARG A 1 621  ? 84.027  58.485  162.572 1.00 93.73  ? 621  ARG A CA  1 
ATOM   4744  C  C   . ARG A 1 621  ? 83.186  59.480  163.374 1.00 92.55  ? 621  ARG A C   1 
ATOM   4745  O  O   . ARG A 1 621  ? 81.963  59.351  163.442 1.00 92.05  ? 621  ARG A O   1 
ATOM   4746  C  CB  . ARG A 1 621  ? 85.027  57.800  163.511 1.00 97.43  ? 621  ARG A CB  1 
ATOM   4747  C  CG  . ARG A 1 621  ? 85.331  56.351  163.164 1.00 100.67 ? 621  ARG A CG  1 
ATOM   4748  C  CD  . ARG A 1 621  ? 86.417  55.780  164.067 1.00 105.16 ? 621  ARG A CD  1 
ATOM   4749  N  NE  . ARG A 1 621  ? 87.761  56.108  163.584 1.00 106.09 ? 621  ARG A NE  1 
ATOM   4750  C  CZ  . ARG A 1 621  ? 88.891  55.601  164.079 1.00 109.22 ? 621  ARG A CZ  1 
ATOM   4751  N  NH1 . ARG A 1 621  ? 88.859  54.730  165.085 1.00 113.00 ? 621  ARG A NH1 1 
ATOM   4752  N  NH2 . ARG A 1 621  ? 90.060  55.965  163.564 1.00 108.35 ? 621  ARG A NH2 1 
ATOM   4753  N  N   . SER A 1 622  ? 83.852  60.465  163.971 1.00 92.34  ? 622  SER A N   1 
ATOM   4754  C  CA  . SER A 1 622  ? 83.246  61.356  164.971 1.00 92.12  ? 622  SER A CA  1 
ATOM   4755  C  C   . SER A 1 622  ? 82.234  62.359  164.417 1.00 88.87  ? 622  SER A C   1 
ATOM   4756  O  O   . SER A 1 622  ? 81.623  63.113  165.180 1.00 88.42  ? 622  SER A O   1 
ATOM   4757  C  CB  . SER A 1 622  ? 84.348  62.110  165.725 1.00 93.24  ? 622  SER A CB  1 
ATOM   4758  O  OG  . SER A 1 622  ? 85.159  62.857  164.828 1.00 91.67  ? 622  SER A OG  1 
ATOM   4759  N  N   . GLY A 1 623  ? 82.065  62.368  163.096 1.00 86.67  ? 623  GLY A N   1 
ATOM   4760  C  CA  . GLY A 1 623  ? 81.198  63.336  162.436 1.00 83.60  ? 623  GLY A CA  1 
ATOM   4761  C  C   . GLY A 1 623  ? 81.924  64.626  162.102 1.00 81.83  ? 623  GLY A C   1 
ATOM   4762  O  O   . GLY A 1 623  ? 81.290  65.654  161.861 1.00 79.64  ? 623  GLY A O   1 
ATOM   4763  N  N   . SER A 1 624  ? 83.257  64.566  162.077 1.00 82.94  ? 624  SER A N   1 
ATOM   4764  C  CA  . SER A 1 624  ? 84.092  65.734  161.787 1.00 81.98  ? 624  SER A CA  1 
ATOM   4765  C  C   . SER A 1 624  ? 85.480  65.362  161.267 1.00 82.99  ? 624  SER A C   1 
ATOM   4766  O  O   . SER A 1 624  ? 86.031  64.321  161.635 1.00 85.32  ? 624  SER A O   1 
ATOM   4767  C  CB  . SER A 1 624  ? 84.251  66.595  163.041 1.00 82.95  ? 624  SER A CB  1 
ATOM   4768  O  OG  . SER A 1 624  ? 85.104  65.961  163.973 1.00 85.63  ? 624  SER A OG  1 
ATOM   4769  N  N   . ARG A 1 625  ? 86.039  66.222  160.417 1.00 81.60  ? 625  ARG A N   1 
ATOM   4770  C  CA  . ARG A 1 625  ? 87.442  66.109  160.002 1.00 82.67  ? 625  ARG A CA  1 
ATOM   4771  C  C   . ARG A 1 625  ? 88.193  67.424  160.093 1.00 82.11  ? 625  ARG A C   1 
ATOM   4772  O  O   . ARG A 1 625  ? 87.619  68.499  159.910 1.00 80.25  ? 625  ARG A O   1 
ATOM   4773  C  CB  . ARG A 1 625  ? 87.581  65.556  158.583 1.00 81.66  ? 625  ARG A CB  1 
ATOM   4774  C  CG  . ARG A 1 625  ? 87.667  64.058  158.543 1.00 84.49  ? 625  ARG A CG  1 
ATOM   4775  C  CD  . ARG A 1 625  ? 88.918  63.566  157.830 1.00 86.80  ? 625  ARG A CD  1 
ATOM   4776  N  NE  . ARG A 1 625  ? 88.849  62.119  157.609 1.00 90.35  ? 625  ARG A NE  1 
ATOM   4777  C  CZ  . ARG A 1 625  ? 89.100  61.191  158.534 1.00 93.59  ? 625  ARG A CZ  1 
ATOM   4778  N  NH1 . ARG A 1 625  ? 89.451  61.538  159.768 1.00 95.06  ? 625  ARG A NH1 1 
ATOM   4779  N  NH2 . ARG A 1 625  ? 89.002  59.904  158.225 1.00 95.43  ? 625  ARG A NH2 1 
ATOM   4780  N  N   . LYS A 1 626  ? 89.487  67.315  160.362 1.00 83.97  ? 626  LYS A N   1 
ATOM   4781  C  CA  . LYS A 1 626  ? 90.372  68.467  160.381 1.00 84.21  ? 626  LYS A CA  1 
ATOM   4782  C  C   . LYS A 1 626  ? 91.494  68.252  159.381 1.00 84.04  ? 626  LYS A C   1 
ATOM   4783  O  O   . LYS A 1 626  ? 92.415  67.480  159.641 1.00 86.21  ? 626  LYS A O   1 
ATOM   4784  C  CB  . LYS A 1 626  ? 90.934  68.698  161.792 1.00 86.99  ? 626  LYS A CB  1 
ATOM   4785  C  CG  . LYS A 1 626  ? 89.924  69.290  162.768 1.00 87.73  ? 626  LYS A CG  1 
ATOM   4786  C  CD  . LYS A 1 626  ? 90.282  68.985  164.219 1.00 92.44  ? 626  LYS A CD  1 
ATOM   4787  C  CE  . LYS A 1 626  ? 89.114  69.341  165.147 1.00 93.74  ? 626  LYS A CE  1 
ATOM   4788  N  NZ  . LYS A 1 626  ? 89.340  68.912  166.563 1.00 97.62  ? 626  LYS A NZ  1 
ATOM   4789  N  N   . LEU A 1 627  ? 91.401  68.912  158.229 1.00 81.91  ? 627  LEU A N   1 
ATOM   4790  C  CA  . LEU A 1 627  ? 92.486  68.898  157.240 1.00 81.81  ? 627  LEU A CA  1 
ATOM   4791  C  C   . LEU A 1 627  ? 93.441  70.066  157.502 1.00 82.52  ? 627  LEU A C   1 
ATOM   4792  O  O   . LEU A 1 627  ? 93.008  71.180  157.816 1.00 81.82  ? 627  LEU A O   1 
ATOM   4793  C  CB  . LEU A 1 627  ? 91.939  68.937  155.807 1.00 79.34  ? 627  LEU A CB  1 
ATOM   4794  C  CG  . LEU A 1 627  ? 92.910  68.763  154.624 1.00 79.64  ? 627  LEU A CG  1 
ATOM   4795  C  CD1 . LEU A 1 627  ? 93.363  67.315  154.428 1.00 81.05  ? 627  LEU A CD1 1 
ATOM   4796  C  CD2 . LEU A 1 627  ? 92.300  69.300  153.335 1.00 77.29  ? 627  LEU A CD2 1 
ATOM   4797  N  N   . ILE A 1 628  ? 94.740  69.794  157.393 1.00 84.07  ? 628  ILE A N   1 
ATOM   4798  C  CA  . ILE A 1 628  ? 95.769  70.801  157.638 1.00 85.24  ? 628  ILE A CA  1 
ATOM   4799  C  C   . ILE A 1 628  ? 96.594  71.045  156.371 1.00 84.21  ? 628  ILE A C   1 
ATOM   4800  O  O   . ILE A 1 628  ? 97.117  70.103  155.766 1.00 84.73  ? 628  ILE A O   1 
ATOM   4801  C  CB  . ILE A 1 628  ? 96.658  70.410  158.852 1.00 88.50  ? 628  ILE A CB  1 
ATOM   4802  C  CG1 . ILE A 1 628  ? 97.224  71.659  159.534 1.00 90.26  ? 628  ILE A CG1 1 
ATOM   4803  C  CG2 . ILE A 1 628  ? 97.758  69.401  158.454 1.00 90.37  ? 628  ILE A CG2 1 
ATOM   4804  C  CD1 . ILE A 1 628  ? 97.506  71.471  161.029 1.00 93.69  ? 628  ILE A CD1 1 
ATOM   4805  N  N   . GLU A 1 629  ? 96.691  72.308  155.959 1.00 82.89  ? 629  GLU A N   1 
ATOM   4806  C  CA  . GLU A 1 629  ? 97.325  72.640  154.680 1.00 81.59  ? 629  GLU A CA  1 
ATOM   4807  C  C   . GLU A 1 629  ? 98.265  73.844  154.731 1.00 82.11  ? 629  GLU A C   1 
ATOM   4808  O  O   . GLU A 1 629  ? 98.085  74.756  155.541 1.00 82.61  ? 629  GLU A O   1 
ATOM   4809  C  CB  . GLU A 1 629  ? 96.261  72.842  153.597 1.00 79.15  ? 629  GLU A CB  1 
ATOM   4810  C  CG  . GLU A 1 629  ? 95.620  71.551  153.104 1.00 78.88  ? 629  GLU A CG  1 
ATOM   4811  C  CD  . GLU A 1 629  ? 96.489  70.805  152.114 1.00 80.70  ? 629  GLU A CD  1 
ATOM   4812  O  OE1 . GLU A 1 629  ? 97.468  71.400  151.604 1.00 81.59  ? 629  GLU A OE1 1 
ATOM   4813  O  OE2 . GLU A 1 629  ? 96.187  69.623  151.838 1.00 81.17  ? 629  GLU A OE2 1 
ATOM   4814  N  N   . VAL A 1 630  ? 99.263  73.830  153.849 1.00 81.71  ? 630  VAL A N   1 
ATOM   4815  C  CA  . VAL A 1 630  ? 100.225 74.922  153.720 1.00 82.16  ? 630  VAL A CA  1 
ATOM   4816  C  C   . VAL A 1 630  ? 99.676  75.992  152.773 1.00 79.84  ? 630  VAL A C   1 
ATOM   4817  O  O   . VAL A 1 630  ? 99.269  75.690  151.651 1.00 78.07  ? 630  VAL A O   1 
ATOM   4818  C  CB  . VAL A 1 630  ? 101.613 74.404  153.229 1.00 83.69  ? 630  VAL A CB  1 
ATOM   4819  C  CG1 . VAL A 1 630  ? 102.547 75.554  152.872 1.00 84.58  ? 630  VAL A CG1 1 
ATOM   4820  C  CG2 . VAL A 1 630  ? 102.260 73.513  154.285 1.00 85.93  ? 630  VAL A CG2 1 
ATOM   4821  N  N   . VAL A 1 631  ? 99.662  77.237  153.245 1.00 79.78  ? 631  VAL A N   1 
ATOM   4822  C  CA  . VAL A 1 631  ? 99.231  78.384  152.447 1.00 77.88  ? 631  VAL A CA  1 
ATOM   4823  C  C   . VAL A 1 631  ? 100.339 78.824  151.483 1.00 78.11  ? 631  VAL A C   1 
ATOM   4824  O  O   . VAL A 1 631  ? 101.479 79.021  151.906 1.00 80.39  ? 631  VAL A O   1 
ATOM   4825  C  CB  . VAL A 1 631  ? 98.818  79.556  153.359 1.00 78.79  ? 631  VAL A CB  1 
ATOM   4826  C  CG1 . VAL A 1 631  ? 98.603  80.829  152.557 1.00 78.54  ? 631  VAL A CG1 1 
ATOM   4827  C  CG2 . VAL A 1 631  ? 97.563  79.199  154.130 1.00 77.38  ? 631  VAL A CG2 1 
ATOM   4828  N  N   . PRO A 1 632  ? 100.008 78.972  150.184 1.00 75.93  ? 632  PRO A N   1 
ATOM   4829  C  CA  . PRO A 1 632  ? 101.009 79.296  149.156 1.00 76.27  ? 632  PRO A CA  1 
ATOM   4830  C  C   . PRO A 1 632  ? 101.683 80.654  149.342 1.00 77.80  ? 632  PRO A C   1 
ATOM   4831  O  O   . PRO A 1 632  ? 101.084 81.581  149.885 1.00 77.77  ? 632  PRO A O   1 
ATOM   4832  C  CB  . PRO A 1 632  ? 100.203 79.264  147.852 1.00 74.14  ? 632  PRO A CB  1 
ATOM   4833  C  CG  . PRO A 1 632  ? 98.805  79.423  148.249 1.00 72.39  ? 632  PRO A CG  1 
ATOM   4834  C  CD  . PRO A 1 632  ? 98.661  78.828  149.607 1.00 73.30  ? 632  PRO A CD  1 
ATOM   4835  N  N   . ASP A 1 633  ? 102.927 80.755  148.889 1.00 79.28  ? 633  ASP A N   1 
ATOM   4836  C  CA  . ASP A 1 633  ? 103.723 81.962  149.084 1.00 81.33  ? 633  ASP A CA  1 
ATOM   4837  C  C   . ASP A 1 633  ? 103.403 83.008  148.019 1.00 80.40  ? 633  ASP A C   1 
ATOM   4838  O  O   . ASP A 1 633  ? 104.131 83.169  147.041 1.00 81.00  ? 633  ASP A O   1 
ATOM   4839  C  CB  . ASP A 1 633  ? 105.218 81.629  149.107 1.00 83.69  ? 633  ASP A CB  1 
ATOM   4840  C  CG  . ASP A 1 633  ? 106.026 82.625  149.930 1.00 87.32  ? 633  ASP A CG  1 
ATOM   4841  O  OD1 . ASP A 1 633  ? 107.099 83.057  149.452 1.00 90.48  ? 633  ASP A OD1 1 
ATOM   4842  O  OD2 . ASP A 1 633  ? 105.590 82.979  151.050 1.00 87.89  ? 633  ASP A OD2 1 
ATOM   4843  N  N   . THR A 1 634  ? 102.305 83.722  148.236 1.00 79.02  ? 634  THR A N   1 
ATOM   4844  C  CA  . THR A 1 634  ? 101.756 84.632  147.245 1.00 78.01  ? 634  THR A CA  1 
ATOM   4845  C  C   . THR A 1 634  ? 100.906 85.691  147.940 1.00 77.83  ? 634  THR A C   1 
ATOM   4846  O  O   . THR A 1 634  ? 100.418 85.457  149.038 1.00 77.58  ? 634  THR A O   1 
ATOM   4847  C  CB  . THR A 1 634  ? 100.928 83.847  146.185 1.00 75.44  ? 634  THR A CB  1 
ATOM   4848  O  OG1 . THR A 1 634  ? 100.282 84.758  145.294 1.00 75.96  ? 634  THR A OG1 1 
ATOM   4849  C  CG2 . THR A 1 634  ? 99.875  82.959  146.838 1.00 73.41  ? 634  THR A CG2 1 
ATOM   4850  N  N   . THR A 1 635  ? 100.754 86.857  147.314 1.00 78.28  ? 635  THR A N   1 
ATOM   4851  C  CA  . THR A 1 635  ? 99.881  87.908  147.840 1.00 78.44  ? 635  THR A CA  1 
ATOM   4852  C  C   . THR A 1 635  ? 98.591  87.961  147.025 1.00 76.41  ? 635  THR A C   1 
ATOM   4853  O  O   . THR A 1 635  ? 98.584  88.427  145.888 1.00 76.40  ? 635  THR A O   1 
ATOM   4854  C  CB  . THR A 1 635  ? 100.568 89.291  147.851 1.00 81.30  ? 635  THR A CB  1 
ATOM   4855  O  OG1 . THR A 1 635  ? 101.745 89.239  148.666 1.00 83.74  ? 635  THR A OG1 1 
ATOM   4856  C  CG2 . THR A 1 635  ? 99.630  90.365  148.399 1.00 81.21  ? 635  THR A CG2 1 
ATOM   4857  N  N   . THR A 1 636  ? 97.501  87.472  147.611 1.00 74.83  ? 636  THR A N   1 
ATOM   4858  C  CA  . THR A 1 636  ? 96.237  87.328  146.889 1.00 73.05  ? 636  THR A CA  1 
ATOM   4859  C  C   . THR A 1 636  ? 95.058  87.135  147.841 1.00 71.86  ? 636  THR A C   1 
ATOM   4860  O  O   . THR A 1 636  ? 95.254  86.956  149.048 1.00 73.01  ? 636  THR A O   1 
ATOM   4861  C  CB  . THR A 1 636  ? 96.287  86.150  145.861 1.00 71.56  ? 636  THR A CB  1 
ATOM   4862  O  OG1 . THR A 1 636  ? 94.965  85.864  145.384 1.00 69.78  ? 636  THR A OG1 1 
ATOM   4863  C  CG2 . THR A 1 636  ? 96.873  84.890  146.485 1.00 71.34  ? 636  THR A CG2 1 
ATOM   4864  N  N   . SER A 1 637  ? 93.843  87.182  147.301 1.00 69.76  ? 637  SER A N   1 
ATOM   4865  C  CA  . SER A 1 637  ? 92.653  86.937  148.104 1.00 68.57  ? 637  SER A CA  1 
ATOM   4866  C  C   . SER A 1 637  ? 91.916  85.690  147.644 1.00 65.89  ? 637  SER A C   1 
ATOM   4867  O  O   . SER A 1 637  ? 91.676  85.493  146.452 1.00 64.73  ? 637  SER A O   1 
ATOM   4868  C  CB  . SER A 1 637  ? 91.726  88.159  148.142 1.00 69.09  ? 637  SER A CB  1 
ATOM   4869  O  OG  . SER A 1 637  ? 91.623  88.779  146.877 1.00 70.17  ? 637  SER A OG  1 
ATOM   4870  N  N   . TRP A 1 638  ? 91.566  84.849  148.610 1.00 64.93  ? 638  TRP A N   1 
ATOM   4871  C  CA  . TRP A 1 638  ? 91.053  83.524  148.316 1.00 63.04  ? 638  TRP A CA  1 
ATOM   4872  C  C   . TRP A 1 638  ? 89.556  83.395  148.511 1.00 62.01  ? 638  TRP A C   1 
ATOM   4873  O  O   . TRP A 1 638  ? 88.957  84.069  149.352 1.00 62.44  ? 638  TRP A O   1 
ATOM   4874  C  CB  . TRP A 1 638  ? 91.780  82.472  149.147 1.00 62.62  ? 638  TRP A CB  1 
ATOM   4875  C  CG  . TRP A 1 638  ? 93.215  82.348  148.799 1.00 63.25  ? 638  TRP A CG  1 
ATOM   4876  C  CD1 . TRP A 1 638  ? 94.268  82.917  149.452 1.00 64.18  ? 638  TRP A CD1 1 
ATOM   4877  C  CD2 . TRP A 1 638  ? 93.770  81.615  147.701 1.00 62.12  ? 638  TRP A CD2 1 
ATOM   4878  N  NE1 . TRP A 1 638  ? 95.445  82.579  148.833 1.00 65.02  ? 638  TRP A NE1 1 
ATOM   4879  C  CE2 . TRP A 1 638  ? 95.168  81.781  147.754 1.00 63.37  ? 638  TRP A CE2 1 
ATOM   4880  C  CE3 . TRP A 1 638  ? 93.221  80.834  146.675 1.00 60.03  ? 638  TRP A CE3 1 
ATOM   4881  C  CZ2 . TRP A 1 638  ? 96.025  81.201  146.820 1.00 63.73  ? 638  TRP A CZ2 1 
ATOM   4882  C  CZ3 . TRP A 1 638  ? 94.078  80.253  145.751 1.00 60.40  ? 638  TRP A CZ3 1 
ATOM   4883  C  CH2 . TRP A 1 638  ? 95.461  80.438  145.833 1.00 62.05  ? 638  TRP A CH2 1 
ATOM   4884  N  N   . TYR A 1 639  ? 88.980  82.505  147.713 1.00 61.34  ? 639  TYR A N   1 
ATOM   4885  C  CA  . TYR A 1 639  ? 87.576  82.142  147.762 1.00 60.73  ? 639  TYR A CA  1 
ATOM   4886  C  C   . TYR A 1 639  ? 87.531  80.625  147.994 1.00 59.59  ? 639  TYR A C   1 
ATOM   4887  O  O   . TYR A 1 639  ? 87.778  79.841  147.077 1.00 59.03  ? 639  TYR A O   1 
ATOM   4888  C  CB  . TYR A 1 639  ? 86.929  82.515  146.424 1.00 61.31  ? 639  TYR A CB  1 
ATOM   4889  C  CG  . TYR A 1 639  ? 85.585  83.180  146.521 1.00 62.67  ? 639  TYR A CG  1 
ATOM   4890  C  CD1 . TYR A 1 639  ? 85.461  84.483  147.019 1.00 66.31  ? 639  TYR A CD1 1 
ATOM   4891  C  CD2 . TYR A 1 639  ? 84.431  82.520  146.090 1.00 64.49  ? 639  TYR A CD2 1 
ATOM   4892  C  CE1 . TYR A 1 639  ? 84.210  85.111  147.108 1.00 67.28  ? 639  TYR A CE1 1 
ATOM   4893  C  CE2 . TYR A 1 639  ? 83.171  83.137  146.166 1.00 65.96  ? 639  TYR A CE2 1 
ATOM   4894  C  CZ  . TYR A 1 639  ? 83.069  84.433  146.685 1.00 67.56  ? 639  TYR A CZ  1 
ATOM   4895  O  OH  . TYR A 1 639  ? 81.832  85.051  146.771 1.00 66.87  ? 639  TYR A OH  1 
ATOM   4896  N  N   . LEU A 1 640  ? 87.259  80.213  149.228 1.00 59.42  ? 640  LEU A N   1 
ATOM   4897  C  CA  . LEU A 1 640  ? 87.261  78.790  149.569 1.00 58.96  ? 640  LEU A CA  1 
ATOM   4898  C  C   . LEU A 1 640  ? 85.853  78.212  149.616 1.00 57.56  ? 640  LEU A C   1 
ATOM   4899  O  O   . LEU A 1 640  ? 84.964  78.783  150.246 1.00 57.40  ? 640  LEU A O   1 
ATOM   4900  C  CB  . LEU A 1 640  ? 87.982  78.544  150.896 1.00 60.31  ? 640  LEU A CB  1 
ATOM   4901  C  CG  . LEU A 1 640  ? 87.970  77.115  151.455 1.00 60.21  ? 640  LEU A CG  1 
ATOM   4902  C  CD1 . LEU A 1 640  ? 88.687  76.143  150.520 1.00 60.05  ? 640  LEU A CD1 1 
ATOM   4903  C  CD2 . LEU A 1 640  ? 88.598  77.093  152.833 1.00 61.14  ? 640  LEU A CD2 1 
ATOM   4904  N  N   . THR A 1 641  ? 85.668  77.074  148.952 1.00 56.72  ? 641  THR A N   1 
ATOM   4905  C  CA  . THR A 1 641  ? 84.357  76.438  148.834 1.00 55.83  ? 641  THR A CA  1 
ATOM   4906  C  C   . THR A 1 641  ? 84.389  74.969  149.243 1.00 55.93  ? 641  THR A C   1 
ATOM   4907  O  O   . THR A 1 641  ? 85.400  74.285  149.079 1.00 56.69  ? 641  THR A O   1 
ATOM   4908  C  CB  . THR A 1 641  ? 83.805  76.506  147.388 1.00 55.12  ? 641  THR A CB  1 
ATOM   4909  O  OG1 . THR A 1 641  ? 84.621  75.704  146.524 1.00 55.94  ? 641  THR A OG1 1 
ATOM   4910  C  CG2 . THR A 1 641  ? 83.752  77.945  146.868 1.00 54.97  ? 641  THR A CG2 1 
ATOM   4911  N  N   . GLY A 1 642  ? 83.261  74.485  149.749 1.00 55.21  ? 642  GLY A N   1 
ATOM   4912  C  CA  . GLY A 1 642  ? 83.141  73.102  150.169 1.00 55.55  ? 642  GLY A CA  1 
ATOM   4913  C  C   . GLY A 1 642  ? 81.712  72.615  150.078 1.00 54.87  ? 642  GLY A C   1 
ATOM   4914  O  O   . GLY A 1 642  ? 80.784  73.307  150.490 1.00 54.23  ? 642  GLY A O   1 
ATOM   4915  N  N   . PHE A 1 643  ? 81.535  71.422  149.527 1.00 55.14  ? 643  PHE A N   1 
ATOM   4916  C  CA  . PHE A 1 643  ? 80.227  70.784  149.504 1.00 55.15  ? 643  PHE A CA  1 
ATOM   4917  C  C   . PHE A 1 643  ? 80.396  69.355  149.979 1.00 56.56  ? 643  PHE A C   1 
ATOM   4918  O  O   . PHE A 1 643  ? 81.512  68.836  150.029 1.00 57.48  ? 643  PHE A O   1 
ATOM   4919  C  CB  . PHE A 1 643  ? 79.613  70.808  148.096 1.00 54.41  ? 643  PHE A CB  1 
ATOM   4920  C  CG  . PHE A 1 643  ? 80.354  69.967  147.109 1.00 54.72  ? 643  PHE A CG  1 
ATOM   4921  C  CD1 . PHE A 1 643  ? 81.398  70.499  146.374 1.00 53.73  ? 643  PHE A CD1 1 
ATOM   4922  C  CD2 . PHE A 1 643  ? 80.028  68.630  146.934 1.00 56.01  ? 643  PHE A CD2 1 
ATOM   4923  C  CE1 . PHE A 1 643  ? 82.098  69.716  145.470 1.00 54.67  ? 643  PHE A CE1 1 
ATOM   4924  C  CE2 . PHE A 1 643  ? 80.729  67.840  146.033 1.00 56.31  ? 643  PHE A CE2 1 
ATOM   4925  C  CZ  . PHE A 1 643  ? 81.764  68.386  145.304 1.00 55.22  ? 643  PHE A CZ  1 
ATOM   4926  N  N   . SER A 1 644  ? 79.283  68.722  150.326 1.00 56.94  ? 644  SER A N   1 
ATOM   4927  C  CA  . SER A 1 644  ? 79.308  67.343  150.758 1.00 58.42  ? 644  SER A CA  1 
ATOM   4928  C  C   . SER A 1 644  ? 78.147  66.561  150.183 1.00 58.60  ? 644  SER A C   1 
ATOM   4929  O  O   . SER A 1 644  ? 77.053  67.095  150.008 1.00 57.50  ? 644  SER A O   1 
ATOM   4930  C  CB  . SER A 1 644  ? 79.294  67.261  152.274 1.00 59.27  ? 644  SER A CB  1 
ATOM   4931  O  OG  . SER A 1 644  ? 79.413  65.916  152.694 1.00 62.14  ? 644  SER A OG  1 
ATOM   4932  N  N   . ILE A 1 645  ? 78.413  65.297  149.868 1.00 60.04  ? 645  ILE A N   1 
ATOM   4933  C  CA  . ILE A 1 645  ? 77.393  64.369  149.406 1.00 61.02  ? 645  ILE A CA  1 
ATOM   4934  C  C   . ILE A 1 645  ? 77.498  63.098  150.234 1.00 63.34  ? 645  ILE A C   1 
ATOM   4935  O  O   . ILE A 1 645  ? 78.552  62.451  150.256 1.00 64.45  ? 645  ILE A O   1 
ATOM   4936  C  CB  . ILE A 1 645  ? 77.539  64.017  147.911 1.00 61.00  ? 645  ILE A CB  1 
ATOM   4937  C  CG1 . ILE A 1 645  ? 77.567  65.282  147.059 1.00 59.53  ? 645  ILE A CG1 1 
ATOM   4938  C  CG2 . ILE A 1 645  ? 76.389  63.116  147.461 1.00 62.18  ? 645  ILE A CG2 1 
ATOM   4939  C  CD1 . ILE A 1 645  ? 78.023  65.049  145.634 1.00 60.45  ? 645  ILE A CD1 1 
ATOM   4940  N  N   . ASP A 1 646  ? 76.409  62.762  150.925 1.00 64.10  ? 646  ASP A N   1 
ATOM   4941  C  CA  . ASP A 1 646  ? 76.324  61.517  151.669 1.00 66.62  ? 646  ASP A CA  1 
ATOM   4942  C  C   . ASP A 1 646  ? 75.475  60.520  150.887 1.00 67.83  ? 646  ASP A C   1 
ATOM   4943  O  O   . ASP A 1 646  ? 74.402  60.882  150.400 1.00 66.82  ? 646  ASP A O   1 
ATOM   4944  C  CB  . ASP A 1 646  ? 75.721  61.749  153.052 1.00 67.08  ? 646  ASP A CB  1 
ATOM   4945  C  CG  . ASP A 1 646  ? 75.637  60.476  153.862 1.00 70.80  ? 646  ASP A CG  1 
ATOM   4946  O  OD1 . ASP A 1 646  ? 76.673  60.057  154.431 1.00 73.89  ? 646  ASP A OD1 1 
ATOM   4947  O  OD2 . ASP A 1 646  ? 74.541  59.879  153.913 1.00 72.73  ? 646  ASP A OD2 1 
ATOM   4948  N  N   . PRO A 1 647  ? 75.956  59.262  150.754 1.00 70.07  ? 647  PRO A N   1 
ATOM   4949  C  CA  . PRO A 1 647  ? 75.236  58.235  149.989 1.00 71.87  ? 647  PRO A CA  1 
ATOM   4950  C  C   . PRO A 1 647  ? 73.765  58.091  150.376 1.00 72.36  ? 647  PRO A C   1 
ATOM   4951  O  O   . PRO A 1 647  ? 72.968  57.609  149.573 1.00 73.31  ? 647  PRO A O   1 
ATOM   4952  C  CB  . PRO A 1 647  ? 76.010  56.953  150.312 1.00 74.54  ? 647  PRO A CB  1 
ATOM   4953  C  CG  . PRO A 1 647  ? 77.398  57.421  150.567 1.00 73.54  ? 647  PRO A CG  1 
ATOM   4954  C  CD  . PRO A 1 647  ? 77.229  58.738  151.288 1.00 71.38  ? 647  PRO A CD  1 
ATOM   4955  N  N   . VAL A 1 648  ? 73.420  58.523  151.588 1.00 72.02  ? 648  VAL A N   1 
ATOM   4956  C  CA  . VAL A 1 648  ? 72.053  58.422  152.109 1.00 72.50  ? 648  VAL A CA  1 
ATOM   4957  C  C   . VAL A 1 648  ? 71.413  59.799  152.293 1.00 70.05  ? 648  VAL A C   1 
ATOM   4958  O  O   . VAL A 1 648  ? 70.326  60.045  151.779 1.00 69.80  ? 648  VAL A O   1 
ATOM   4959  C  CB  . VAL A 1 648  ? 71.999  57.595  153.435 1.00 74.70  ? 648  VAL A CB  1 
ATOM   4960  C  CG1 . VAL A 1 648  ? 70.650  57.741  154.138 1.00 74.30  ? 648  VAL A CG1 1 
ATOM   4961  C  CG2 . VAL A 1 648  ? 72.303  56.127  153.157 1.00 77.64  ? 648  VAL A CG2 1 
ATOM   4962  N  N   . TYR A 1 649  ? 72.088  60.693  153.009 1.00 68.72  ? 649  TYR A N   1 
ATOM   4963  C  CA  . TYR A 1 649  ? 71.512  61.996  153.342 1.00 66.93  ? 649  TYR A CA  1 
ATOM   4964  C  C   . TYR A 1 649  ? 71.680  63.035  152.245 1.00 64.92  ? 649  TYR A C   1 
ATOM   4965  O  O   . TYR A 1 649  ? 71.045  64.089  152.292 1.00 63.46  ? 649  TYR A O   1 
ATOM   4966  C  CB  . TYR A 1 649  ? 72.062  62.515  154.676 1.00 66.85  ? 649  TYR A CB  1 
ATOM   4967  C  CG  . TYR A 1 649  ? 71.830  61.554  155.810 1.00 69.12  ? 649  TYR A CG  1 
ATOM   4968  C  CD1 . TYR A 1 649  ? 72.866  60.760  156.291 1.00 70.97  ? 649  TYR A CD1 1 
ATOM   4969  C  CD2 . TYR A 1 649  ? 70.566  61.411  156.379 1.00 70.24  ? 649  TYR A CD2 1 
ATOM   4970  C  CE1 . TYR A 1 649  ? 72.663  59.860  157.325 1.00 73.68  ? 649  TYR A CE1 1 
ATOM   4971  C  CE2 . TYR A 1 649  ? 70.348  60.509  157.413 1.00 73.05  ? 649  TYR A CE2 1 
ATOM   4972  C  CZ  . TYR A 1 649  ? 71.406  59.739  157.880 1.00 74.62  ? 649  TYR A CZ  1 
ATOM   4973  O  OH  . TYR A 1 649  ? 71.208  58.843  158.899 1.00 77.44  ? 649  TYR A OH  1 
ATOM   4974  N  N   . GLY A 1 650  ? 72.543  62.741  151.272 1.00 65.26  ? 650  GLY A N   1 
ATOM   4975  C  CA  . GLY A 1 650  ? 72.666  63.558  150.063 1.00 63.81  ? 650  GLY A CA  1 
ATOM   4976  C  C   . GLY A 1 650  ? 73.518  64.807  150.179 1.00 62.22  ? 650  GLY A C   1 
ATOM   4977  O  O   . GLY A 1 650  ? 74.505  64.839  150.922 1.00 62.13  ? 650  GLY A O   1 
ATOM   4978  N  N   . LEU A 1 651  ? 73.107  65.838  149.442 1.00 61.00  ? 651  LEU A N   1 
ATOM   4979  C  CA  . LEU A 1 651  ? 73.895  67.053  149.238 1.00 59.85  ? 651  LEU A CA  1 
ATOM   4980  C  C   . LEU A 1 651  ? 73.863  68.054  150.396 1.00 59.86  ? 651  LEU A C   1 
ATOM   4981  O  O   . LEU A 1 651  ? 72.802  68.474  150.844 1.00 59.54  ? 651  LEU A O   1 
ATOM   4982  C  CB  . LEU A 1 651  ? 73.467  67.748  147.937 1.00 58.48  ? 651  LEU A CB  1 
ATOM   4983  C  CG  . LEU A 1 651  ? 74.065  69.128  147.641 1.00 55.84  ? 651  LEU A CG  1 
ATOM   4984  C  CD1 . LEU A 1 651  ? 75.557  69.030  147.368 1.00 54.63  ? 651  LEU A CD1 1 
ATOM   4985  C  CD2 . LEU A 1 651  ? 73.341  69.784  146.489 1.00 53.83  ? 651  LEU A CD2 1 
ATOM   4986  N  N   . GLY A 1 652  ? 75.048  68.448  150.848 1.00 60.75  ? 652  GLY A N   1 
ATOM   4987  C  CA  . GLY A 1 652  ? 75.198  69.456  151.888 1.00 61.55  ? 652  GLY A CA  1 
ATOM   4988  C  C   . GLY A 1 652  ? 76.170  70.527  151.435 1.00 61.70  ? 652  GLY A C   1 
ATOM   4989  O  O   . GLY A 1 652  ? 77.206  70.231  150.842 1.00 61.98  ? 652  GLY A O   1 
ATOM   4990  N  N   . ILE A 1 653  ? 75.838  71.775  151.733 1.00 61.87  ? 653  ILE A N   1 
ATOM   4991  C  CA  . ILE A 1 653  ? 76.582  72.916  151.229 1.00 62.15  ? 653  ILE A CA  1 
ATOM   4992  C  C   . ILE A 1 653  ? 76.812  73.943  152.328 1.00 62.97  ? 653  ILE A C   1 
ATOM   4993  O  O   . ILE A 1 653  ? 76.045  73.989  153.293 1.00 63.61  ? 653  ILE A O   1 
ATOM   4994  C  CB  . ILE A 1 653  ? 75.855  73.500  150.002 1.00 61.18  ? 653  ILE A CB  1 
ATOM   4995  C  CG1 . ILE A 1 653  ? 76.721  73.308  148.769 1.00 61.71  ? 653  ILE A CG1 1 
ATOM   4996  C  CG2 . ILE A 1 653  ? 75.482  74.967  150.178 1.00 60.46  ? 653  ILE A CG2 1 
ATOM   4997  C  CD1 . ILE A 1 653  ? 75.941  72.831  147.608 1.00 63.18  ? 653  ILE A CD1 1 
ATOM   4998  N  N   . ILE A 1 654  ? 77.879  74.734  152.200 1.00 63.85  ? 654  ILE A N   1 
ATOM   4999  C  CA  . ILE A 1 654  ? 78.129  75.837  153.128 1.00 65.12  ? 654  ILE A CA  1 
ATOM   5000  C  C   . ILE A 1 654  ? 77.399  77.096  152.666 1.00 65.09  ? 654  ILE A C   1 
ATOM   5001  O  O   . ILE A 1 654  ? 77.244  77.329  151.461 1.00 64.05  ? 654  ILE A O   1 
ATOM   5002  C  CB  . ILE A 1 654  ? 79.640  76.113  153.360 1.00 65.95  ? 654  ILE A CB  1 
ATOM   5003  C  CG1 . ILE A 1 654  ? 80.324  76.622  152.088 1.00 65.82  ? 654  ILE A CG1 1 
ATOM   5004  C  CG2 . ILE A 1 654  ? 80.341  74.862  153.885 1.00 67.34  ? 654  ILE A CG2 1 
ATOM   5005  C  CD1 . ILE A 1 654  ? 81.701  77.232  152.315 1.00 66.82  ? 654  ILE A CD1 1 
ATOM   5006  N  N   . LYS A 1 655  ? 76.944  77.887  153.643 1.00 66.53  ? 655  LYS A N   1 
ATOM   5007  C  CA  . LYS A 1 655  ? 76.123  79.086  153.411 1.00 67.08  ? 655  LYS A CA  1 
ATOM   5008  C  C   . LYS A 1 655  ? 76.720  79.988  152.322 1.00 66.76  ? 655  LYS A C   1 
ATOM   5009  O  O   . LYS A 1 655  ? 76.202  80.058  151.203 1.00 66.25  ? 655  LYS A O   1 
ATOM   5010  C  CB  . LYS A 1 655  ? 75.955  79.866  154.726 1.00 68.39  ? 655  LYS A CB  1 
ATOM   5011  C  CG  . LYS A 1 655  ? 74.769  80.849  154.754 1.00 70.23  ? 655  LYS A CG  1 
ATOM   5012  C  CD  . LYS A 1 655  ? 73.638  80.345  155.656 1.00 73.38  ? 655  LYS A CD  1 
ATOM   5013  C  CE  . LYS A 1 655  ? 72.331  81.115  155.423 1.00 74.90  ? 655  LYS A CE  1 
ATOM   5014  N  NZ  . LYS A 1 655  ? 71.645  80.697  154.153 1.00 75.07  ? 655  LYS A NZ  1 
ATOM   5015  N  N   . LYS A 1 656  ? 77.815  80.665  152.659 1.00 67.38  ? 656  LYS A N   1 
ATOM   5016  C  CA  . LYS A 1 656  ? 78.584  81.449  151.687 1.00 67.17  ? 656  LYS A CA  1 
ATOM   5017  C  C   . LYS A 1 656  ? 80.040  80.971  151.668 1.00 66.96  ? 656  LYS A C   1 
ATOM   5018  O  O   . LYS A 1 656  ? 80.513  80.397  152.659 1.00 67.62  ? 656  LYS A O   1 
ATOM   5019  C  CB  . LYS A 1 656  ? 78.504  82.956  152.006 1.00 68.13  ? 656  LYS A CB  1 
ATOM   5020  C  CG  . LYS A 1 656  ? 78.891  83.335  153.442 1.00 70.51  ? 656  LYS A CG  1 
ATOM   5021  C  CD  . LYS A 1 656  ? 78.851  84.855  153.688 1.00 73.53  ? 656  LYS A CD  1 
ATOM   5022  C  CE  . LYS A 1 656  ? 80.074  85.576  153.097 1.00 75.21  ? 656  LYS A CE  1 
ATOM   5023  N  NZ  . LYS A 1 656  ? 80.326  86.896  153.752 1.00 76.78  ? 656  LYS A NZ  1 
ATOM   5024  N  N   . PRO A 1 657  ? 80.751  81.196  150.544 1.00 66.00  ? 657  PRO A N   1 
ATOM   5025  C  CA  . PRO A 1 657  ? 82.181  80.867  150.465 1.00 65.96  ? 657  PRO A CA  1 
ATOM   5026  C  C   . PRO A 1 657  ? 83.029  81.591  151.508 1.00 66.32  ? 657  PRO A C   1 
ATOM   5027  O  O   . PRO A 1 657  ? 82.718  82.725  151.884 1.00 66.78  ? 657  PRO A O   1 
ATOM   5028  C  CB  . PRO A 1 657  ? 82.573  81.331  149.059 1.00 65.97  ? 657  PRO A CB  1 
ATOM   5029  C  CG  . PRO A 1 657  ? 81.294  81.313  148.287 1.00 65.37  ? 657  PRO A CG  1 
ATOM   5030  C  CD  . PRO A 1 657  ? 80.250  81.746  149.272 1.00 65.34  ? 657  PRO A CD  1 
ATOM   5031  N  N   . ILE A 1 658  ? 84.083  80.920  151.966 1.00 65.99  ? 658  ILE A N   1 
ATOM   5032  C  CA  . ILE A 1 658  ? 85.015  81.469  152.948 1.00 66.39  ? 658  ILE A CA  1 
ATOM   5033  C  C   . ILE A 1 658  ? 86.033  82.356  152.240 1.00 66.63  ? 658  ILE A C   1 
ATOM   5034  O  O   . ILE A 1 658  ? 86.635  81.950  151.243 1.00 66.19  ? 658  ILE A O   1 
ATOM   5035  C  CB  . ILE A 1 658  ? 85.740  80.346  153.727 1.00 67.09  ? 658  ILE A CB  1 
ATOM   5036  C  CG1 . ILE A 1 658  ? 84.747  79.598  154.614 1.00 66.29  ? 658  ILE A CG1 1 
ATOM   5037  C  CG2 . ILE A 1 658  ? 86.890  80.906  154.561 1.00 68.60  ? 658  ILE A CG2 1 
ATOM   5038  C  CD1 . ILE A 1 658  ? 85.278  78.307  155.184 1.00 67.01  ? 658  ILE A CD1 1 
ATOM   5039  N  N   . GLN A 1 659  ? 86.217  83.564  152.764 1.00 67.08  ? 659  GLN A N   1 
ATOM   5040  C  CA  . GLN A 1 659  ? 87.121  84.541  152.163 1.00 67.49  ? 659  GLN A CA  1 
ATOM   5041  C  C   . GLN A 1 659  ? 88.171  85.041  153.140 1.00 68.67  ? 659  GLN A C   1 
ATOM   5042  O  O   . GLN A 1 659  ? 87.887  85.296  154.311 1.00 69.45  ? 659  GLN A O   1 
ATOM   5043  C  CB  . GLN A 1 659  ? 86.342  85.725  151.588 1.00 67.55  ? 659  GLN A CB  1 
ATOM   5044  C  CG  . GLN A 1 659  ? 85.265  85.342  150.572 1.00 67.24  ? 659  GLN A CG  1 
ATOM   5045  C  CD  . GLN A 1 659  ? 84.702  86.548  149.838 1.00 69.87  ? 659  GLN A CD  1 
ATOM   5046  O  OE1 . GLN A 1 659  ? 85.376  87.156  148.994 1.00 72.04  ? 659  GLN A OE1 1 
ATOM   5047  N  NE2 . GLN A 1 659  ? 83.458  86.898  150.149 1.00 69.47  ? 659  GLN A NE2 1 
ATOM   5048  N  N   . PHE A 1 660  ? 89.389  85.179  152.633 1.00 68.67  ? 660  PHE A N   1 
ATOM   5049  C  CA  . PHE A 1 660  ? 90.518  85.693  153.395 1.00 69.74  ? 660  PHE A CA  1 
ATOM   5050  C  C   . PHE A 1 660  ? 91.578  86.136  152.404 1.00 70.28  ? 660  PHE A C   1 
ATOM   5051  O  O   . PHE A 1 660  ? 91.557  85.715  151.242 1.00 68.78  ? 660  PHE A O   1 
ATOM   5052  C  CB  . PHE A 1 660  ? 91.079  84.614  154.327 1.00 70.06  ? 660  PHE A CB  1 
ATOM   5053  C  CG  . PHE A 1 660  ? 91.543  83.372  153.615 1.00 67.93  ? 660  PHE A CG  1 
ATOM   5054  C  CD1 . PHE A 1 660  ? 90.630  82.424  153.168 1.00 64.76  ? 660  PHE A CD1 1 
ATOM   5055  C  CD2 . PHE A 1 660  ? 92.899  83.147  153.395 1.00 68.12  ? 660  PHE A CD2 1 
ATOM   5056  C  CE1 . PHE A 1 660  ? 91.059  81.279  152.514 1.00 63.55  ? 660  PHE A CE1 1 
ATOM   5057  C  CE2 . PHE A 1 660  ? 93.337  82.004  152.736 1.00 65.92  ? 660  PHE A CE2 1 
ATOM   5058  C  CZ  . PHE A 1 660  ? 92.419  81.070  152.299 1.00 64.32  ? 660  PHE A CZ  1 
ATOM   5059  N  N   . THR A 1 661  ? 92.500  86.982  152.854 1.00 58.68  ? 661  THR A N   1 
ATOM   5060  C  CA  . THR A 1 661  ? 93.623  87.379  152.015 1.00 57.89  ? 661  THR A CA  1 
ATOM   5061  C  C   . THR A 1 661  ? 94.928  86.900  152.624 1.00 57.52  ? 661  THR A C   1 
ATOM   5062  O  O   . THR A 1 661  ? 95.042  86.773  153.839 1.00 57.89  ? 661  THR A O   1 
ATOM   5063  C  CB  . THR A 1 661  ? 93.702  88.905  151.803 1.00 57.86  ? 661  THR A CB  1 
ATOM   5064  O  OG1 . THR A 1 661  ? 94.019  89.542  153.047 1.00 58.81  ? 661  THR A OG1 1 
ATOM   5065  C  CG2 . THR A 1 661  ? 92.385  89.460  151.244 1.00 57.67  ? 661  THR A CG2 1 
ATOM   5066  N  N   . THR A 1 662  ? 95.896  86.616  151.758 1.00 56.47  ? 662  THR A N   1 
ATOM   5067  C  CA  . THR A 1 662  ? 97.256  86.306  152.171 1.00 56.04  ? 662  THR A CA  1 
ATOM   5068  C  C   . THR A 1 662  ? 98.155  87.385  151.597 1.00 55.11  ? 662  THR A C   1 
ATOM   5069  O  O   . THR A 1 662  ? 98.126  87.645  150.396 1.00 54.50  ? 662  THR A O   1 
ATOM   5070  C  CB  . THR A 1 662  ? 97.715  84.938  151.663 1.00 56.12  ? 662  THR A CB  1 
ATOM   5071  O  OG1 . THR A 1 662  ? 97.698  84.924  150.230 1.00 55.43  ? 662  THR A OG1 1 
ATOM   5072  C  CG2 . THR A 1 662  ? 96.799  83.852  152.185 1.00 56.78  ? 662  THR A CG2 1 
ATOM   5073  N  N   . VAL A 1 663  ? 98.933  88.023  152.467 1.00 54.68  ? 663  VAL A N   1 
ATOM   5074  C  CA  . VAL A 1 663  ? 99.774  89.152  152.079 1.00 53.34  ? 663  VAL A CA  1 
ATOM   5075  C  C   . VAL A 1 663  ? 101.206 88.885  152.491 1.00 52.70  ? 663  VAL A C   1 
ATOM   5076  O  O   . VAL A 1 663  ? 101.510 88.837  153.682 1.00 53.23  ? 663  VAL A O   1 
ATOM   5077  C  CB  . VAL A 1 663  ? 99.285  90.478  152.718 1.00 53.62  ? 663  VAL A CB  1 
ATOM   5078  C  CG1 . VAL A 1 663  ? 100.224 91.635  152.356 1.00 54.01  ? 663  VAL A CG1 1 
ATOM   5079  C  CG2 . VAL A 1 663  ? 97.859  90.798  152.273 1.00 52.96  ? 663  VAL A CG2 1 
ATOM   5080  N  N   . GLN A 1 664  ? 102.077 88.702  151.502 1.00 51.33  ? 664  GLN A N   1 
ATOM   5081  C  CA  . GLN A 1 664  ? 103.509 88.539  151.756 1.00 50.76  ? 664  GLN A CA  1 
ATOM   5082  C  C   . GLN A 1 664  ? 104.091 89.816  152.349 1.00 50.12  ? 664  GLN A C   1 
ATOM   5083  O  O   . GLN A 1 664  ? 103.936 90.901  151.770 1.00 49.55  ? 664  GLN A O   1 
ATOM   5084  C  CB  . GLN A 1 664  ? 104.266 88.234  150.470 1.00 50.68  ? 664  GLN A CB  1 
ATOM   5085  C  CG  . GLN A 1 664  ? 103.961 86.921  149.817 1.00 50.67  ? 664  GLN A CG  1 
ATOM   5086  C  CD  . GLN A 1 664  ? 104.374 86.935  148.364 1.00 51.07  ? 664  GLN A CD  1 
ATOM   5087  O  OE1 . GLN A 1 664  ? 105.277 86.208  147.967 1.00 53.32  ? 664  GLN A OE1 1 
ATOM   5088  N  NE2 . GLN A 1 664  ? 103.728 87.780  147.564 1.00 49.09  ? 664  GLN A NE2 1 
ATOM   5089  N  N   . PRO A 1 665  ? 104.774 89.694  153.493 1.00 49.81  ? 665  PRO A N   1 
ATOM   5090  C  CA  . PRO A 1 665  ? 105.390 90.865  154.105 1.00 49.52  ? 665  PRO A CA  1 
ATOM   5091  C  C   . PRO A 1 665  ? 106.430 91.506  153.177 1.00 48.44  ? 665  PRO A C   1 
ATOM   5092  O  O   . PRO A 1 665  ? 106.510 92.735  153.088 1.00 48.28  ? 665  PRO A O   1 
ATOM   5093  C  CB  . PRO A 1 665  ? 106.070 90.300  155.363 1.00 50.36  ? 665  PRO A CB  1 
ATOM   5094  C  CG  . PRO A 1 665  ? 105.445 88.962  155.595 1.00 50.57  ? 665  PRO A CG  1 
ATOM   5095  C  CD  . PRO A 1 665  ? 105.032 88.459  154.258 1.00 50.55  ? 665  PRO A CD  1 
ATOM   5096  N  N   . PHE A 1 666  ? 107.186 90.673  152.467 1.00 47.37  ? 666  PHE A N   1 
ATOM   5097  C  CA  . PHE A 1 666  ? 108.324 91.147  151.695 1.00 46.59  ? 666  PHE A CA  1 
ATOM   5098  C  C   . PHE A 1 666  ? 108.730 90.153  150.612 1.00 45.43  ? 666  PHE A C   1 
ATOM   5099  O  O   . PHE A 1 666  ? 108.915 88.974  150.895 1.00 45.80  ? 666  PHE A O   1 
ATOM   5100  C  CB  . PHE A 1 666  ? 109.490 91.395  152.656 1.00 47.37  ? 666  PHE A CB  1 
ATOM   5101  C  CG  . PHE A 1 666  ? 110.791 91.691  151.983 1.00 47.93  ? 666  PHE A CG  1 
ATOM   5102  C  CD1 . PHE A 1 666  ? 111.069 92.968  151.504 1.00 48.02  ? 666  PHE A CD1 1 
ATOM   5103  C  CD2 . PHE A 1 666  ? 111.758 90.694  151.849 1.00 48.81  ? 666  PHE A CD2 1 
ATOM   5104  C  CE1 . PHE A 1 666  ? 112.286 93.246  150.889 1.00 48.12  ? 666  PHE A CE1 1 
ATOM   5105  C  CE2 . PHE A 1 666  ? 112.976 90.963  151.237 1.00 48.79  ? 666  PHE A CE2 1 
ATOM   5106  C  CZ  . PHE A 1 666  ? 113.239 92.245  150.759 1.00 48.72  ? 666  PHE A CZ  1 
ATOM   5107  N  N   . TYR A 1 667  ? 108.878 90.636  149.381 1.00 43.79  ? 667  TYR A N   1 
ATOM   5108  C  CA  . TYR A 1 667  ? 109.327 89.788  148.276 1.00 42.65  ? 667  TYR A CA  1 
ATOM   5109  C  C   . TYR A 1 667  ? 110.120 90.550  147.205 1.00 42.15  ? 667  TYR A C   1 
ATOM   5110  O  O   . TYR A 1 667  ? 110.065 91.783  147.128 1.00 42.06  ? 667  TYR A O   1 
ATOM   5111  C  CB  . TYR A 1 667  ? 108.153 89.025  147.640 1.00 41.88  ? 667  TYR A CB  1 
ATOM   5112  C  CG  . TYR A 1 667  ? 107.134 89.902  146.950 1.00 40.40  ? 667  TYR A CG  1 
ATOM   5113  C  CD1 . TYR A 1 667  ? 106.194 90.623  147.689 1.00 39.13  ? 667  TYR A CD1 1 
ATOM   5114  C  CD2 . TYR A 1 667  ? 107.100 90.003  145.556 1.00 38.99  ? 667  TYR A CD2 1 
ATOM   5115  C  CE1 . TYR A 1 667  ? 105.255 91.421  147.069 1.00 38.53  ? 667  TYR A CE1 1 
ATOM   5116  C  CE2 . TYR A 1 667  ? 106.161 90.797  144.922 1.00 38.33  ? 667  TYR A CE2 1 
ATOM   5117  C  CZ  . TYR A 1 667  ? 105.238 91.503  145.686 1.00 39.58  ? 667  TYR A CZ  1 
ATOM   5118  O  OH  . TYR A 1 667  ? 104.313 92.322  145.074 1.00 40.83  ? 667  TYR A OH  1 
ATOM   5119  N  N   . ILE A 1 668  ? 110.844 89.792  146.384 1.00 41.24  ? 668  ILE A N   1 
ATOM   5120  C  CA  . ILE A 1 668  ? 111.681 90.330  145.327 1.00 40.69  ? 668  ILE A CA  1 
ATOM   5121  C  C   . ILE A 1 668  ? 111.280 89.684  143.993 1.00 39.86  ? 668  ILE A C   1 
ATOM   5122  O  O   . ILE A 1 668  ? 111.020 88.493  143.941 1.00 40.14  ? 668  ILE A O   1 
ATOM   5123  C  CB  . ILE A 1 668  ? 113.181 90.101  145.649 1.00 41.29  ? 668  ILE A CB  1 
ATOM   5124  C  CG1 . ILE A 1 668  ? 114.073 90.841  144.645 1.00 41.60  ? 668  ILE A CG1 1 
ATOM   5125  C  CG2 . ILE A 1 668  ? 113.511 88.598  145.748 1.00 41.20  ? 668  ILE A CG2 1 
ATOM   5126  C  CD1 . ILE A 1 668  ? 115.572 90.785  144.955 1.00 41.99  ? 668  ILE A CD1 1 
ATOM   5127  N  N   . VAL A 1 669  ? 111.193 90.469  142.925 1.00 39.09  ? 669  VAL A N   1 
ATOM   5128  C  CA  . VAL A 1 669  ? 110.784 89.928  141.628 1.00 38.41  ? 669  VAL A CA  1 
ATOM   5129  C  C   . VAL A 1 669  ? 111.898 90.135  140.626 1.00 38.78  ? 669  VAL A C   1 
ATOM   5130  O  O   . VAL A 1 669  ? 112.439 91.233  140.523 1.00 39.39  ? 669  VAL A O   1 
ATOM   5131  C  CB  . VAL A 1 669  ? 109.497 90.598  141.102 1.00 37.68  ? 669  VAL A CB  1 
ATOM   5132  C  CG1 . VAL A 1 669  ? 109.026 89.935  139.826 1.00 35.73  ? 669  VAL A CG1 1 
ATOM   5133  C  CG2 . VAL A 1 669  ? 108.404 90.530  142.146 1.00 37.70  ? 669  VAL A CG2 1 
ATOM   5134  N  N   . GLU A 1 670  ? 112.256 89.082  139.901 1.00 38.86  ? 670  GLU A N   1 
ATOM   5135  C  CA  . GLU A 1 670  ? 113.305 89.192  138.893 1.00 39.61  ? 670  GLU A CA  1 
ATOM   5136  C  C   . GLU A 1 670  ? 112.779 89.672  137.541 1.00 39.02  ? 670  GLU A C   1 
ATOM   5137  O  O   . GLU A 1 670  ? 111.584 89.574  137.241 1.00 38.43  ? 670  GLU A O   1 
ATOM   5138  C  CB  . GLU A 1 670  ? 114.055 87.864  138.725 1.00 40.44  ? 670  GLU A CB  1 
ATOM   5139  C  CG  . GLU A 1 670  ? 113.430 86.890  137.728 1.00 40.60  ? 670  GLU A CG  1 
ATOM   5140  C  CD  . GLU A 1 670  ? 112.137 86.271  138.217 1.00 42.28  ? 670  GLU A CD  1 
ATOM   5141  O  OE1 . GLU A 1 670  ? 111.720 86.538  139.359 1.00 43.87  ? 670  GLU A OE1 1 
ATOM   5142  O  OE2 . GLU A 1 670  ? 111.526 85.500  137.454 1.00 44.86  ? 670  GLU A OE2 1 
ATOM   5143  N  N   . ASN A 1 671  ? 113.698 90.197  136.740 1.00 39.11  ? 671  ASN A N   1 
ATOM   5144  C  CA  . ASN A 1 671  ? 113.421 90.637  135.394 1.00 38.69  ? 671  ASN A CA  1 
ATOM   5145  C  C   . ASN A 1 671  ? 114.688 90.419  134.610 1.00 39.12  ? 671  ASN A C   1 
ATOM   5146  O  O   . ASN A 1 671  ? 115.553 91.290  134.558 1.00 40.11  ? 671  ASN A O   1 
ATOM   5147  C  CB  . ASN A 1 671  ? 113.039 92.106  135.404 1.00 38.72  ? 671  ASN A CB  1 
ATOM   5148  C  CG  . ASN A 1 671  ? 112.764 92.654  134.021 1.00 39.20  ? 671  ASN A CG  1 
ATOM   5149  O  OD1 . ASN A 1 671  ? 112.210 91.967  133.149 1.00 39.06  ? 671  ASN A OD1 1 
ATOM   5150  N  ND2 . ASN A 1 671  ? 113.147 93.913  133.813 1.00 39.51  ? 671  ASN A ND2 1 
ATOM   5151  N  N   . LEU A 1 672  ? 114.810 89.225  134.039 1.00 39.14  ? 672  LEU A N   1 
ATOM   5152  C  CA  . LEU A 1 672  ? 116.040 88.784  133.394 1.00 39.36  ? 672  LEU A CA  1 
ATOM   5153  C  C   . LEU A 1 672  ? 115.875 88.509  131.893 1.00 39.12  ? 672  LEU A C   1 
ATOM   5154  O  O   . LEU A 1 672  ? 114.779 88.154  131.433 1.00 38.31  ? 672  LEU A O   1 
ATOM   5155  C  CB  . LEU A 1 672  ? 116.547 87.519  134.075 1.00 39.44  ? 672  LEU A CB  1 
ATOM   5156  C  CG  . LEU A 1 672  ? 116.543 87.477  135.602 1.00 40.77  ? 672  LEU A CG  1 
ATOM   5157  C  CD1 . LEU A 1 672  ? 116.483 86.024  136.069 1.00 41.04  ? 672  LEU A CD1 1 
ATOM   5158  C  CD2 . LEU A 1 672  ? 117.752 88.207  136.229 1.00 41.50  ? 672  LEU A CD2 1 
ATOM   5159  N  N   . PRO A 1 673  ? 116.975 88.647  131.129 1.00 39.53  ? 673  PRO A N   1 
ATOM   5160  C  CA  . PRO A 1 673  ? 116.985 88.237  129.733 1.00 39.72  ? 673  PRO A CA  1 
ATOM   5161  C  C   . PRO A 1 673  ? 117.017 86.709  129.653 1.00 40.10  ? 673  PRO A C   1 
ATOM   5162  O  O   . PRO A 1 673  ? 117.540 86.053  130.568 1.00 40.51  ? 673  PRO A O   1 
ATOM   5163  C  CB  . PRO A 1 673  ? 118.300 88.819  129.222 1.00 40.12  ? 673  PRO A CB  1 
ATOM   5164  C  CG  . PRO A 1 673  ? 119.183 88.802  130.400 1.00 40.19  ? 673  PRO A CG  1 
ATOM   5165  C  CD  . PRO A 1 673  ? 118.289 89.166  131.545 1.00 40.14  ? 673  PRO A CD  1 
ATOM   5166  N  N   . TYR A 1 674  ? 116.451 86.145  128.590 1.00 39.99  ? 674  TYR A N   1 
ATOM   5167  C  CA  . TYR A 1 674  ? 116.445 84.687  128.426 1.00 40.56  ? 674  TYR A CA  1 
ATOM   5168  C  C   . TYR A 1 674  ? 117.878 84.159  128.302 1.00 41.30  ? 674  TYR A C   1 
ATOM   5169  O  O   . TYR A 1 674  ? 118.228 83.130  128.887 1.00 41.70  ? 674  TYR A O   1 
ATOM   5170  C  CB  . TYR A 1 674  ? 115.598 84.276  127.214 1.00 40.64  ? 674  TYR A CB  1 
ATOM   5171  C  CG  . TYR A 1 674  ? 115.605 82.789  126.911 1.00 41.72  ? 674  TYR A CG  1 
ATOM   5172  C  CD1 . TYR A 1 674  ? 114.642 81.936  127.457 1.00 42.47  ? 674  TYR A CD1 1 
ATOM   5173  C  CD2 . TYR A 1 674  ? 116.575 82.238  126.074 1.00 42.53  ? 674  TYR A CD2 1 
ATOM   5174  C  CE1 . TYR A 1 674  ? 114.652 80.575  127.179 1.00 42.69  ? 674  TYR A CE1 1 
ATOM   5175  C  CE2 . TYR A 1 674  ? 116.599 80.891  125.797 1.00 43.33  ? 674  TYR A CE2 1 
ATOM   5176  C  CZ  . TYR A 1 674  ? 115.639 80.062  126.347 1.00 44.35  ? 674  TYR A CZ  1 
ATOM   5177  O  OH  . TYR A 1 674  ? 115.679 78.708  126.048 1.00 45.72  ? 674  TYR A OH  1 
ATOM   5178  N  N   . SER A 1 675  ? 118.701 84.874  127.543 1.00 41.47  ? 675  SER A N   1 
ATOM   5179  C  CA  . SER A 1 675  ? 120.051 84.445  127.282 1.00 42.47  ? 675  SER A CA  1 
ATOM   5180  C  C   . SER A 1 675  ? 120.997 85.618  127.192 1.00 42.98  ? 675  SER A C   1 
ATOM   5181  O  O   . SER A 1 675  ? 120.582 86.749  126.933 1.00 42.78  ? 675  SER A O   1 
ATOM   5182  C  CB  . SER A 1 675  ? 120.115 83.647  125.976 1.00 42.70  ? 675  SER A CB  1 
ATOM   5183  O  OG  . SER A 1 675  ? 119.808 84.459  124.849 1.00 43.11  ? 675  SER A OG  1 
ATOM   5184  N  N   . ILE A 1 676  ? 122.272 85.322  127.412 1.00 43.93  ? 676  ILE A N   1 
ATOM   5185  C  CA  . ILE A 1 676  ? 123.379 86.236  127.155 1.00 44.62  ? 676  ILE A CA  1 
ATOM   5186  C  C   . ILE A 1 676  ? 124.560 85.434  126.608 1.00 45.54  ? 676  ILE A C   1 
ATOM   5187  O  O   . ILE A 1 676  ? 124.512 84.206  126.541 1.00 45.25  ? 676  ILE A O   1 
ATOM   5188  C  CB  . ILE A 1 676  ? 123.821 86.989  128.432 1.00 44.89  ? 676  ILE A CB  1 
ATOM   5189  C  CG1 . ILE A 1 676  ? 124.333 85.997  129.488 1.00 44.67  ? 676  ILE A CG1 1 
ATOM   5190  C  CG2 . ILE A 1 676  ? 122.678 87.878  128.958 1.00 44.53  ? 676  ILE A CG2 1 
ATOM   5191  C  CD1 . ILE A 1 676  ? 124.850 86.637  130.770 1.00 44.29  ? 676  ILE A CD1 1 
ATOM   5192  N  N   . LYS A 1 677  ? 125.622 86.129  126.227 1.00 46.70  ? 677  LYS A N   1 
ATOM   5193  C  CA  . LYS A 1 677  ? 126.822 85.465  125.750 1.00 48.51  ? 677  LYS A CA  1 
ATOM   5194  C  C   . LYS A 1 677  ? 128.035 85.819  126.616 1.00 49.45  ? 677  LYS A C   1 
ATOM   5195  O  O   . LYS A 1 677  ? 128.087 86.903  127.191 1.00 49.56  ? 677  LYS A O   1 
ATOM   5196  C  CB  . LYS A 1 677  ? 127.040 85.785  124.265 1.00 48.91  ? 677  LYS A CB  1 
ATOM   5197  C  CG  . LYS A 1 677  ? 126.041 85.045  123.351 1.00 49.71  ? 677  LYS A CG  1 
ATOM   5198  C  CD  . LYS A 1 677  ? 125.812 85.742  122.014 1.00 51.01  ? 677  LYS A CD  1 
ATOM   5199  C  CE  . LYS A 1 677  ? 124.484 85.296  121.394 1.00 51.34  ? 677  LYS A CE  1 
ATOM   5200  N  NZ  . LYS A 1 677  ? 123.926 86.321  120.454 1.00 52.24  ? 677  LYS A NZ  1 
ATOM   5201  N  N   . ARG A 1 678  ? 128.986 84.887  126.730 1.00 50.61  ? 678  ARG A N   1 
ATOM   5202  C  CA  . ARG A 1 678  ? 130.229 85.106  127.480 1.00 51.84  ? 678  ARG A CA  1 
ATOM   5203  C  C   . ARG A 1 678  ? 130.878 86.434  127.098 1.00 51.85  ? 678  ARG A C   1 
ATOM   5204  O  O   . ARG A 1 678  ? 130.943 86.789  125.916 1.00 52.09  ? 678  ARG A O   1 
ATOM   5205  C  CB  . ARG A 1 678  ? 131.229 83.980  127.206 1.00 53.13  ? 678  ARG A CB  1 
ATOM   5206  C  CG  . ARG A 1 678  ? 131.228 82.832  128.203 1.00 55.85  ? 678  ARG A CG  1 
ATOM   5207  C  CD  . ARG A 1 678  ? 132.316 81.800  127.876 1.00 60.95  ? 678  ARG A CD  1 
ATOM   5208  N  NE  . ARG A 1 678  ? 132.057 81.133  126.598 1.00 65.42  ? 678  ARG A NE  1 
ATOM   5209  C  CZ  . ARG A 1 678  ? 132.841 81.201  125.516 1.00 68.27  ? 678  ARG A CZ  1 
ATOM   5210  N  NH1 . ARG A 1 678  ? 133.979 81.894  125.536 1.00 70.00  ? 678  ARG A NH1 1 
ATOM   5211  N  NH2 . ARG A 1 678  ? 132.488 80.561  124.403 1.00 68.60  ? 678  ARG A NH2 1 
ATOM   5212  N  N   . GLY A 1 679  ? 131.354 87.170  128.095 1.00 51.85  ? 679  GLY A N   1 
ATOM   5213  C  CA  . GLY A 1 679  ? 132.065 88.414  127.835 1.00 51.54  ? 679  GLY A CA  1 
ATOM   5214  C  C   . GLY A 1 679  ? 131.170 89.636  127.809 1.00 50.54  ? 679  GLY A C   1 
ATOM   5215  O  O   . GLY A 1 679  ? 131.654 90.767  127.934 1.00 51.44  ? 679  GLY A O   1 
ATOM   5216  N  N   . GLU A 1 680  ? 129.865 89.421  127.642 1.00 48.72  ? 680  GLU A N   1 
ATOM   5217  C  CA  . GLU A 1 680  ? 128.905 90.518  127.652 1.00 46.77  ? 680  GLU A CA  1 
ATOM   5218  C  C   . GLU A 1 680  ? 128.656 90.987  129.077 1.00 46.17  ? 680  GLU A C   1 
ATOM   5219  O  O   . GLU A 1 680  ? 128.520 90.164  129.990 1.00 46.02  ? 680  GLU A O   1 
ATOM   5220  C  CB  . GLU A 1 680  ? 127.596 90.094  126.992 1.00 45.69  ? 680  GLU A CB  1 
ATOM   5221  C  CG  . GLU A 1 680  ? 127.727 89.772  125.511 1.00 45.53  ? 680  GLU A CG  1 
ATOM   5222  C  CD  . GLU A 1 680  ? 126.409 89.385  124.862 1.00 43.82  ? 680  GLU A CD  1 
ATOM   5223  O  OE1 . GLU A 1 680  ? 125.549 88.803  125.556 1.00 42.39  ? 680  GLU A OE1 1 
ATOM   5224  O  OE2 . GLU A 1 680  ? 126.245 89.651  123.650 1.00 42.94  ? 680  GLU A OE2 1 
ATOM   5225  N  N   . ALA A 1 681  ? 128.606 92.310  129.252 1.00 45.30  ? 681  ALA A N   1 
ATOM   5226  C  CA  . ALA A 1 681  ? 128.298 92.930  130.538 1.00 44.46  ? 681  ALA A CA  1 
ATOM   5227  C  C   . ALA A 1 681  ? 126.804 93.185  130.646 1.00 43.17  ? 681  ALA A C   1 
ATOM   5228  O  O   . ALA A 1 681  ? 126.256 93.989  129.897 1.00 43.14  ? 681  ALA A O   1 
ATOM   5229  C  CB  . ALA A 1 681  ? 129.053 94.209  130.687 1.00 44.79  ? 681  ALA A CB  1 
ATOM   5230  N  N   . VAL A 1 682  ? 126.153 92.500  131.583 1.00 42.06  ? 682  VAL A N   1 
ATOM   5231  C  CA  . VAL A 1 682  ? 124.698 92.514  131.707 1.00 40.35  ? 682  VAL A CA  1 
ATOM   5232  C  C   . VAL A 1 682  ? 124.266 93.074  133.044 1.00 39.95  ? 682  VAL A C   1 
ATOM   5233  O  O   . VAL A 1 682  ? 124.890 92.804  134.076 1.00 40.35  ? 682  VAL A O   1 
ATOM   5234  C  CB  . VAL A 1 682  ? 124.108 91.094  131.633 1.00 40.17  ? 682  VAL A CB  1 
ATOM   5235  C  CG1 . VAL A 1 682  ? 122.564 91.146  131.511 1.00 39.55  ? 682  VAL A CG1 1 
ATOM   5236  C  CG2 . VAL A 1 682  ? 124.726 90.320  130.478 1.00 40.52  ? 682  VAL A CG2 1 
ATOM   5237  N  N   . VAL A 1 683  ? 123.179 93.837  133.019 1.00 38.77  ? 683  VAL A N   1 
ATOM   5238  C  CA  . VAL A 1 683  ? 122.576 94.333  134.233 1.00 38.14  ? 683  VAL A CA  1 
ATOM   5239  C  C   . VAL A 1 683  ? 121.390 93.433  134.567 1.00 37.77  ? 683  VAL A C   1 
ATOM   5240  O  O   . VAL A 1 683  ? 120.440 93.309  133.780 1.00 36.98  ? 683  VAL A O   1 
ATOM   5241  C  CB  . VAL A 1 683  ? 122.157 95.821  134.115 1.00 37.71  ? 683  VAL A CB  1 
ATOM   5242  C  CG1 . VAL A 1 683  ? 121.440 96.265  135.368 1.00 36.72  ? 683  VAL A CG1 1 
ATOM   5243  C  CG2 . VAL A 1 683  ? 123.371 96.695  133.877 1.00 37.27  ? 683  VAL A CG2 1 
ATOM   5244  N  N   . LEU A 1 684  ? 121.467 92.781  135.725 1.00 37.78  ? 684  LEU A N   1 
ATOM   5245  C  CA  . LEU A 1 684  ? 120.368 91.961  136.188 1.00 37.07  ? 684  LEU A CA  1 
ATOM   5246  C  C   . LEU A 1 684  ? 119.537 92.818  137.102 1.00 36.80  ? 684  LEU A C   1 
ATOM   5247  O  O   . LEU A 1 684  ? 119.981 93.198  138.166 1.00 37.70  ? 684  LEU A O   1 
ATOM   5248  C  CB  . LEU A 1 684  ? 120.880 90.715  136.896 1.00 37.52  ? 684  LEU A CB  1 
ATOM   5249  C  CG  . LEU A 1 684  ? 121.810 89.826  136.066 1.00 37.70  ? 684  LEU A CG  1 
ATOM   5250  C  CD1 . LEU A 1 684  ? 122.079 88.524  136.813 1.00 37.18  ? 684  LEU A CD1 1 
ATOM   5251  C  CD2 . LEU A 1 684  ? 121.200 89.550  134.687 1.00 36.32  ? 684  LEU A CD2 1 
ATOM   5252  N  N   A GLN A 1 685  ? 118.318 93.123  136.674 0.50 36.35  ? 685  GLN A N   1 
ATOM   5253  N  N   B GLN A 1 685  ? 118.330 93.129  136.649 0.50 36.32  ? 685  GLN A N   1 
ATOM   5254  C  CA  A GLN A 1 685  ? 117.432 94.042  137.384 0.50 36.12  ? 685  GLN A CA  1 
ATOM   5255  C  CA  B GLN A 1 685  ? 117.405 93.985  137.370 0.50 36.03  ? 685  GLN A CA  1 
ATOM   5256  C  C   A GLN A 1 685  ? 116.336 93.289  138.146 0.50 35.83  ? 685  GLN A C   1 
ATOM   5257  C  C   B GLN A 1 685  ? 116.468 93.150  138.232 0.50 35.86  ? 685  GLN A C   1 
ATOM   5258  O  O   A GLN A 1 685  ? 115.712 92.369  137.612 0.50 35.65  ? 685  GLN A O   1 
ATOM   5259  O  O   B GLN A 1 685  ? 116.089 92.034  137.859 0.50 35.77  ? 685  GLN A O   1 
ATOM   5260  C  CB  A GLN A 1 685  ? 116.849 95.059  136.387 0.50 35.69  ? 685  GLN A CB  1 
ATOM   5261  C  CB  B GLN A 1 685  ? 116.602 94.829  136.375 0.50 35.49  ? 685  GLN A CB  1 
ATOM   5262  C  CG  A GLN A 1 685  ? 115.464 95.622  136.714 0.50 35.15  ? 685  GLN A CG  1 
ATOM   5263  C  CG  B GLN A 1 685  ? 117.350 96.054  135.855 0.50 35.48  ? 685  GLN A CG  1 
ATOM   5264  C  CD  A GLN A 1 685  ? 115.476 96.792  137.691 0.50 34.89  ? 685  GLN A CD  1 
ATOM   5265  C  CD  B GLN A 1 685  ? 117.032 96.399  134.410 0.50 34.86  ? 685  GLN A CD  1 
ATOM   5266  O  OE1 A GLN A 1 685  ? 116.402 97.617  137.712 0.50 33.86  ? 685  GLN A OE1 1 
ATOM   5267  O  OE1 B GLN A 1 685  ? 116.285 95.695  133.729 0.50 35.13  ? 685  GLN A OE1 1 
ATOM   5268  N  NE2 A GLN A 1 685  ? 114.416 96.884  138.486 0.50 33.58  ? 685  GLN A NE2 1 
ATOM   5269  N  NE2 B GLN A 1 685  ? 117.629 97.480  133.923 0.50 35.57  ? 685  GLN A NE2 1 
ATOM   5270  N  N   . PHE A 1 686  ? 116.124 93.685  139.400 1.00 35.93  ? 686  PHE A N   1 
ATOM   5271  C  CA  . PHE A 1 686  ? 115.124 93.075  140.279 1.00 35.40  ? 686  PHE A CA  1 
ATOM   5272  C  C   . PHE A 1 686  ? 114.312 94.221  140.859 1.00 35.47  ? 686  PHE A C   1 
ATOM   5273  O  O   . PHE A 1 686  ? 114.712 95.378  140.767 1.00 36.35  ? 686  PHE A O   1 
ATOM   5274  C  CB  . PHE A 1 686  ? 115.789 92.297  141.423 1.00 35.94  ? 686  PHE A CB  1 
ATOM   5275  C  CG  . PHE A 1 686  ? 116.808 91.283  140.972 1.00 35.17  ? 686  PHE A CG  1 
ATOM   5276  C  CD1 . PHE A 1 686  ? 118.119 91.659  140.715 1.00 33.83  ? 686  PHE A CD1 1 
ATOM   5277  C  CD2 . PHE A 1 686  ? 116.456 89.949  140.820 1.00 34.13  ? 686  PHE A CD2 1 
ATOM   5278  C  CE1 . PHE A 1 686  ? 119.050 90.721  140.300 1.00 34.33  ? 686  PHE A CE1 1 
ATOM   5279  C  CE2 . PHE A 1 686  ? 117.387 89.008  140.407 1.00 32.59  ? 686  PHE A CE2 1 
ATOM   5280  C  CZ  . PHE A 1 686  ? 118.680 89.392  140.149 1.00 32.54  ? 686  PHE A CZ  1 
ATOM   5281  N  N   . THR A 1 687  ? 113.176 93.909  141.464 1.00 35.05  ? 687  THR A N   1 
ATOM   5282  C  CA  . THR A 1 687  ? 112.340 94.928  142.074 1.00 34.83  ? 687  THR A CA  1 
ATOM   5283  C  C   . THR A 1 687  ? 111.880 94.400  143.412 1.00 35.35  ? 687  THR A C   1 
ATOM   5284  O  O   . THR A 1 687  ? 111.511 93.227  143.510 1.00 35.49  ? 687  THR A O   1 
ATOM   5285  C  CB  . THR A 1 687  ? 111.124 95.233  141.196 1.00 34.09  ? 687  THR A CB  1 
ATOM   5286  O  OG1 . THR A 1 687  ? 111.567 95.462  139.849 1.00 33.92  ? 687  THR A OG1 1 
ATOM   5287  C  CG2 . THR A 1 687  ? 110.366 96.455  141.717 1.00 33.01  ? 687  THR A CG2 1 
ATOM   5288  N  N   . LEU A 1 688  ? 111.910 95.260  144.433 1.00 35.65  ? 688  LEU A N   1 
ATOM   5289  C  CA  . LEU A 1 688  ? 111.579 94.862  145.806 1.00 35.80  ? 688  LEU A CA  1 
ATOM   5290  C  C   . LEU A 1 688  ? 110.221 95.398  146.241 1.00 35.78  ? 688  LEU A C   1 
ATOM   5291  O  O   . LEU A 1 688  ? 109.794 96.483  145.821 1.00 35.81  ? 688  LEU A O   1 
ATOM   5292  C  CB  . LEU A 1 688  ? 112.651 95.339  146.772 1.00 36.30  ? 688  LEU A CB  1 
ATOM   5293  C  CG  . LEU A 1 688  ? 114.017 94.663  146.702 1.00 36.94  ? 688  LEU A CG  1 
ATOM   5294  C  CD1 . LEU A 1 688  ? 115.087 95.684  146.954 1.00 37.78  ? 688  LEU A CD1 1 
ATOM   5295  C  CD2 . LEU A 1 688  ? 114.137 93.528  147.695 1.00 37.63  ? 688  LEU A CD2 1 
ATOM   5296  N  N   . PHE A 1 689  ? 109.536 94.621  147.073 1.00 35.89  ? 689  PHE A N   1 
ATOM   5297  C  CA  . PHE A 1 689  ? 108.223 94.993  147.566 1.00 35.58  ? 689  PHE A CA  1 
ATOM   5298  C  C   . PHE A 1 689  ? 108.151 94.752  149.060 1.00 36.71  ? 689  PHE A C   1 
ATOM   5299  O  O   . PHE A 1 689  ? 108.513 93.674  149.550 1.00 37.40  ? 689  PHE A O   1 
ATOM   5300  C  CB  . PHE A 1 689  ? 107.127 94.236  146.818 1.00 34.65  ? 689  PHE A CB  1 
ATOM   5301  C  CG  . PHE A 1 689  ? 106.996 94.640  145.373 1.00 33.45  ? 689  PHE A CG  1 
ATOM   5302  C  CD1 . PHE A 1 689  ? 107.712 93.974  144.385 1.00 31.35  ? 689  PHE A CD1 1 
ATOM   5303  C  CD2 . PHE A 1 689  ? 106.176 95.706  145.004 1.00 33.23  ? 689  PHE A CD2 1 
ATOM   5304  C  CE1 . PHE A 1 689  ? 107.607 94.347  143.052 1.00 30.91  ? 689  PHE A CE1 1 
ATOM   5305  C  CE2 . PHE A 1 689  ? 106.058 96.097  143.655 1.00 32.74  ? 689  PHE A CE2 1 
ATOM   5306  C  CZ  . PHE A 1 689  ? 106.780 95.413  142.680 1.00 31.23  ? 689  PHE A CZ  1 
ATOM   5307  N  N   . ASN A 1 690  ? 107.705 95.781  149.775 1.00 37.28  ? 690  ASN A N   1 
ATOM   5308  C  CA  . ASN A 1 690  ? 107.610 95.774  151.232 1.00 38.18  ? 690  ASN A CA  1 
ATOM   5309  C  C   . ASN A 1 690  ? 106.159 96.018  151.625 1.00 37.94  ? 690  ASN A C   1 
ATOM   5310  O  O   . ASN A 1 690  ? 105.607 97.073  151.329 1.00 37.69  ? 690  ASN A O   1 
ATOM   5311  C  CB  . ASN A 1 690  ? 108.538 96.856  151.795 1.00 38.92  ? 690  ASN A CB  1 
ATOM   5312  C  CG  . ASN A 1 690  ? 108.312 97.148  153.270 1.00 40.28  ? 690  ASN A CG  1 
ATOM   5313  O  OD1 . ASN A 1 690  ? 107.778 96.328  154.020 1.00 41.22  ? 690  ASN A OD1 1 
ATOM   5314  N  ND2 . ASN A 1 690  ? 108.745 98.332  153.698 1.00 41.35  ? 690  ASN A ND2 1 
ATOM   5315  N  N   . ASN A 1 691  ? 105.533 95.039  152.270 1.00 38.19  ? 691  ASN A N   1 
ATOM   5316  C  CA  . ASN A 1 691  ? 104.134 95.190  152.666 1.00 38.49  ? 691  ASN A CA  1 
ATOM   5317  C  C   . ASN A 1 691  ? 103.892 95.478  154.161 1.00 39.62  ? 691  ASN A C   1 
ATOM   5318  O  O   . ASN A 1 691  ? 102.742 95.582  154.599 1.00 40.01  ? 691  ASN A O   1 
ATOM   5319  C  CB  . ASN A 1 691  ? 103.293 94.006  152.176 1.00 37.92  ? 691  ASN A CB  1 
ATOM   5320  C  CG  . ASN A 1 691  ? 103.052 94.047  150.683 1.00 36.39  ? 691  ASN A CG  1 
ATOM   5321  O  OD1 . ASN A 1 691  ? 102.651 95.068  150.137 1.00 36.62  ? 691  ASN A OD1 1 
ATOM   5322  N  ND2 . ASN A 1 691  ? 103.298 92.934  150.017 1.00 35.24  ? 691  ASN A ND2 1 
ATOM   5323  N  N   . LEU A 1 692  ? 104.965 95.637  154.932 1.00 40.31  ? 692  LEU A N   1 
ATOM   5324  C  CA  . LEU A 1 692  ? 104.835 95.983  156.343 1.00 41.17  ? 692  LEU A CA  1 
ATOM   5325  C  C   . LEU A 1 692  ? 104.381 97.428  156.484 1.00 41.43  ? 692  LEU A C   1 
ATOM   5326  O  O   . LEU A 1 692  ? 104.133 98.100  155.477 1.00 40.88  ? 692  LEU A O   1 
ATOM   5327  C  CB  . LEU A 1 692  ? 106.137 95.718  157.095 1.00 41.60  ? 692  LEU A CB  1 
ATOM   5328  C  CG  . LEU A 1 692  ? 106.537 94.239  157.084 1.00 42.45  ? 692  LEU A CG  1 
ATOM   5329  C  CD1 . LEU A 1 692  ? 107.896 94.043  157.725 1.00 42.83  ? 692  LEU A CD1 1 
ATOM   5330  C  CD2 . LEU A 1 692  ? 105.485 93.366  157.770 1.00 42.60  ? 692  LEU A CD2 1 
ATOM   5331  N  N   . GLY A 1 693  ? 104.260 97.900  157.725 1.00 42.20  ? 693  GLY A N   1 
ATOM   5332  C  CA  . GLY A 1 693  ? 103.711 99.227  157.984 1.00 42.44  ? 693  GLY A CA  1 
ATOM   5333  C  C   . GLY A 1 693  ? 104.715 100.369 157.997 1.00 43.10  ? 693  GLY A C   1 
ATOM   5334  O  O   . GLY A 1 693  ? 104.351 101.510 158.305 1.00 43.47  ? 693  GLY A O   1 
ATOM   5335  N  N   . ALA A 1 694  ? 105.972 100.080 157.657 1.00 42.83  ? 694  ALA A N   1 
ATOM   5336  C  CA  . ALA A 1 694  ? 107.044 101.063 157.783 1.00 42.97  ? 694  ALA A CA  1 
ATOM   5337  C  C   . ALA A 1 694  ? 108.149 100.789 156.785 1.00 42.63  ? 694  ALA A C   1 
ATOM   5338  O  O   . ALA A 1 694  ? 108.299 99.665  156.316 1.00 42.76  ? 694  ALA A O   1 
ATOM   5339  C  CB  . ALA A 1 694  ? 107.604 101.053 159.207 1.00 43.56  ? 694  ALA A CB  1 
ATOM   5340  N  N   . GLU A 1 695  ? 108.930 101.821 156.486 1.00 42.60  ? 695  GLU A N   1 
ATOM   5341  C  CA  . GLU A 1 695  ? 110.044 101.743 155.554 1.00 42.47  ? 695  GLU A CA  1 
ATOM   5342  C  C   . GLU A 1 695  ? 111.231 100.997 156.158 1.00 43.00  ? 695  GLU A C   1 
ATOM   5343  O  O   . GLU A 1 695  ? 111.683 101.296 157.264 1.00 44.04  ? 695  GLU A O   1 
ATOM   5344  C  CB  . GLU A 1 695  ? 110.452 103.155 155.139 1.00 42.77  ? 695  GLU A CB  1 
ATOM   5345  C  CG  . GLU A 1 695  ? 111.533 103.233 154.078 1.00 44.41  ? 695  GLU A CG  1 
ATOM   5346  C  CD  . GLU A 1 695  ? 111.542 104.576 153.344 1.00 46.85  ? 695  GLU A CD  1 
ATOM   5347  O  OE1 . GLU A 1 695  ? 110.634 105.410 153.583 1.00 47.72  ? 695  GLU A OE1 1 
ATOM   5348  O  OE2 . GLU A 1 695  ? 112.448 104.791 152.511 1.00 46.95  ? 695  GLU A OE2 1 
ATOM   5349  N  N   . TYR A 1 696  ? 111.734 100.020 155.418 1.00 42.47  ? 696  TYR A N   1 
ATOM   5350  C  CA  . TYR A 1 696  ? 112.863 99.227  155.878 1.00 42.87  ? 696  TYR A CA  1 
ATOM   5351  C  C   . TYR A 1 696  ? 113.957 99.118  154.829 1.00 42.17  ? 696  TYR A C   1 
ATOM   5352  O  O   . TYR A 1 696  ? 113.681 98.989  153.635 1.00 41.09  ? 696  TYR A O   1 
ATOM   5353  C  CB  . TYR A 1 696  ? 112.393 97.837  156.311 1.00 43.40  ? 696  TYR A CB  1 
ATOM   5354  C  CG  . TYR A 1 696  ? 111.530 97.868  157.546 1.00 44.72  ? 696  TYR A CG  1 
ATOM   5355  C  CD1 . TYR A 1 696  ? 110.186 97.510  157.491 1.00 45.89  ? 696  TYR A CD1 1 
ATOM   5356  C  CD2 . TYR A 1 696  ? 112.048 98.284  158.762 1.00 47.24  ? 696  TYR A CD2 1 
ATOM   5357  C  CE1 . TYR A 1 696  ? 109.379 97.546  158.626 1.00 46.52  ? 696  TYR A CE1 1 
ATOM   5358  C  CE2 . TYR A 1 696  ? 111.258 98.322  159.909 1.00 49.37  ? 696  TYR A CE2 1 
ATOM   5359  C  CZ  . TYR A 1 696  ? 109.921 97.950  159.832 1.00 49.04  ? 696  TYR A CZ  1 
ATOM   5360  O  OH  . TYR A 1 696  ? 109.137 97.999  160.968 1.00 49.23  ? 696  TYR A OH  1 
ATOM   5361  N  N   . ILE A 1 697  ? 115.201 99.189  155.288 1.00 42.31  ? 697  ILE A N   1 
ATOM   5362  C  CA  . ILE A 1 697  ? 116.344 98.908  154.434 1.00 41.90  ? 697  ILE A CA  1 
ATOM   5363  C  C   . ILE A 1 697  ? 116.408 97.414  154.109 1.00 41.53  ? 697  ILE A C   1 
ATOM   5364  O  O   . ILE A 1 697  ? 116.435 96.571  155.007 1.00 42.33  ? 697  ILE A O   1 
ATOM   5365  C  CB  . ILE A 1 697  ? 117.662 99.374  155.079 1.00 42.68  ? 697  ILE A CB  1 
ATOM   5366  C  CG1 . ILE A 1 697  ? 117.629 100.899 155.280 1.00 42.77  ? 697  ILE A CG1 1 
ATOM   5367  C  CG2 . ILE A 1 697  ? 118.831 98.961  154.205 1.00 43.28  ? 697  ILE A CG2 1 
ATOM   5368  C  CD1 . ILE A 1 697  ? 118.846 101.515 155.959 1.00 41.43  ? 697  ILE A CD1 1 
ATOM   5369  N  N   . ALA A 1 698  ? 116.424 97.099  152.820 1.00 40.58  ? 698  ALA A N   1 
ATOM   5370  C  CA  . ALA A 1 698  ? 116.552 95.728  152.346 1.00 40.07  ? 698  ALA A CA  1 
ATOM   5371  C  C   . ALA A 1 698  ? 117.995 95.410  151.971 1.00 40.67  ? 698  ALA A C   1 
ATOM   5372  O  O   . ALA A 1 698  ? 118.710 96.275  151.469 1.00 41.01  ? 698  ALA A O   1 
ATOM   5373  C  CB  . ALA A 1 698  ? 115.657 95.524  151.150 1.00 39.15  ? 698  ALA A CB  1 
ATOM   5374  N  N   . ASP A 1 699  ? 118.422 94.172  152.201 1.00 40.97  ? 699  ASP A N   1 
ATOM   5375  C  CA  . ASP A 1 699  ? 119.766 93.739  151.808 1.00 41.79  ? 699  ASP A CA  1 
ATOM   5376  C  C   . ASP A 1 699  ? 119.664 92.625  150.775 1.00 41.67  ? 699  ASP A C   1 
ATOM   5377  O  O   . ASP A 1 699  ? 119.084 91.564  151.038 1.00 42.04  ? 699  ASP A O   1 
ATOM   5378  C  CB  . ASP A 1 699  ? 120.569 93.277  153.016 1.00 42.37  ? 699  ASP A CB  1 
ATOM   5379  C  CG  . ASP A 1 699  ? 120.724 94.364  154.067 1.00 44.30  ? 699  ASP A CG  1 
ATOM   5380  O  OD1 . ASP A 1 699  ? 120.658 95.570  153.726 1.00 43.93  ? 699  ASP A OD1 1 
ATOM   5381  O  OD2 . ASP A 1 699  ? 120.915 94.011  155.252 1.00 47.00  ? 699  ASP A OD2 1 
ATOM   5382  N  N   . VAL A 1 700  ? 120.206 92.876  149.590 1.00 41.39  ? 700  VAL A N   1 
ATOM   5383  C  CA  . VAL A 1 700  ? 120.047 91.953  148.486 1.00 40.62  ? 700  VAL A CA  1 
ATOM   5384  C  C   . VAL A 1 700  ? 121.403 91.369  148.151 1.00 41.43  ? 700  VAL A C   1 
ATOM   5385  O  O   . VAL A 1 700  ? 122.368 92.106  147.955 1.00 41.70  ? 700  VAL A O   1 
ATOM   5386  C  CB  . VAL A 1 700  ? 119.411 92.639  147.269 1.00 39.94  ? 700  VAL A CB  1 
ATOM   5387  C  CG1 . VAL A 1 700  ? 119.188 91.639  146.135 1.00 39.05  ? 700  VAL A CG1 1 
ATOM   5388  C  CG2 . VAL A 1 700  ? 118.094 93.293  147.665 1.00 38.68  ? 700  VAL A CG2 1 
ATOM   5389  N  N   . THR A 1 701  ? 121.467 90.039  148.123 1.00 41.78  ? 701  THR A N   1 
ATOM   5390  C  CA  . THR A 1 701  ? 122.710 89.324  147.882 1.00 42.93  ? 701  THR A CA  1 
ATOM   5391  C  C   . THR A 1 701  ? 122.572 88.497  146.619 1.00 42.81  ? 701  THR A C   1 
ATOM   5392  O  O   . THR A 1 701  ? 121.625 87.729  146.485 1.00 42.79  ? 701  THR A O   1 
ATOM   5393  C  CB  . THR A 1 701  ? 123.078 88.413  149.070 1.00 43.74  ? 701  THR A CB  1 
ATOM   5394  O  OG1 . THR A 1 701  ? 123.035 89.167  150.289 1.00 44.12  ? 701  THR A OG1 1 
ATOM   5395  C  CG2 . THR A 1 701  ? 124.472 87.841  148.896 1.00 44.63  ? 701  THR A CG2 1 
ATOM   5396  N  N   . LEU A 1 702  ? 123.491 88.691  145.678 1.00 43.43  ? 702  LEU A N   1 
ATOM   5397  C  CA  . LEU A 1 702  ? 123.539 87.879  144.471 1.00 43.43  ? 702  LEU A CA  1 
ATOM   5398  C  C   . LEU A 1 702  ? 124.739 86.949  144.600 1.00 44.90  ? 702  LEU A C   1 
ATOM   5399  O  O   . LEU A 1 702  ? 125.840 87.402  144.918 1.00 45.86  ? 702  LEU A O   1 
ATOM   5400  C  CB  . LEU A 1 702  ? 123.655 88.766  143.225 1.00 42.81  ? 702  LEU A CB  1 
ATOM   5401  C  CG  . LEU A 1 702  ? 123.817 88.074  141.861 1.00 42.18  ? 702  LEU A CG  1 
ATOM   5402  C  CD1 . LEU A 1 702  ? 122.610 87.223  141.534 1.00 41.06  ? 702  LEU A CD1 1 
ATOM   5403  C  CD2 . LEU A 1 702  ? 124.083 89.064  140.738 1.00 40.37  ? 702  LEU A CD2 1 
ATOM   5404  N  N   . TYR A 1 703  ? 124.528 85.652  144.381 1.00 45.45  ? 703  TYR A N   1 
ATOM   5405  C  CA  . TYR A 1 703  ? 125.600 84.672  144.586 1.00 46.90  ? 703  TYR A CA  1 
ATOM   5406  C  C   . TYR A 1 703  ? 126.314 84.288  143.310 1.00 47.35  ? 703  TYR A C   1 
ATOM   5407  O  O   . TYR A 1 703  ? 125.735 84.290  142.228 1.00 46.82  ? 703  TYR A O   1 
ATOM   5408  C  CB  . TYR A 1 703  ? 125.087 83.421  145.305 1.00 47.16  ? 703  TYR A CB  1 
ATOM   5409  C  CG  . TYR A 1 703  ? 124.637 83.700  146.720 1.00 47.84  ? 703  TYR A CG  1 
ATOM   5410  C  CD1 . TYR A 1 703  ? 123.319 84.094  146.987 1.00 47.16  ? 703  TYR A CD1 1 
ATOM   5411  C  CD2 . TYR A 1 703  ? 125.529 83.604  147.789 1.00 48.40  ? 703  TYR A CD2 1 
ATOM   5412  C  CE1 . TYR A 1 703  ? 122.902 84.372  148.275 1.00 47.03  ? 703  TYR A CE1 1 
ATOM   5413  C  CE2 . TYR A 1 703  ? 125.120 83.886  149.082 1.00 48.42  ? 703  TYR A CE2 1 
ATOM   5414  C  CZ  . TYR A 1 703  ? 123.804 84.263  149.312 1.00 48.88  ? 703  TYR A CZ  1 
ATOM   5415  O  OH  . TYR A 1 703  ? 123.378 84.538  150.589 1.00 51.11  ? 703  TYR A OH  1 
ATOM   5416  N  N   . ASN A 1 704  ? 127.594 83.983  143.456 1.00 49.10  ? 704  ASN A N   1 
ATOM   5417  C  CA  . ASN A 1 704  ? 128.402 83.461  142.378 1.00 50.09  ? 704  ASN A CA  1 
ATOM   5418  C  C   . ASN A 1 704  ? 128.415 81.954  142.528 1.00 50.97  ? 704  ASN A C   1 
ATOM   5419  O  O   . ASN A 1 704  ? 129.235 81.391  143.245 1.00 51.92  ? 704  ASN A O   1 
ATOM   5420  C  CB  . ASN A 1 704  ? 129.818 84.047  142.435 1.00 50.99  ? 704  ASN A CB  1 
ATOM   5421  C  CG  . ASN A 1 704  ? 130.757 83.411  141.429 1.00 51.19  ? 704  ASN A CG  1 
ATOM   5422  O  OD1 . ASN A 1 704  ? 130.328 82.898  140.393 1.00 51.02  ? 704  ASN A OD1 1 
ATOM   5423  N  ND2 . ASN A 1 704  ? 132.047 83.445  141.727 1.00 50.98  ? 704  ASN A ND2 1 
ATOM   5424  N  N   . VAL A 1 705  ? 127.468 81.312  141.861 1.00 51.34  ? 705  VAL A N   1 
ATOM   5425  C  CA  . VAL A 1 705  ? 127.288 79.871  141.954 1.00 52.28  ? 705  VAL A CA  1 
ATOM   5426  C  C   . VAL A 1 705  ? 128.276 79.140  141.036 1.00 53.40  ? 705  VAL A C   1 
ATOM   5427  O  O   . VAL A 1 705  ? 128.334 79.394  139.826 1.00 52.71  ? 705  VAL A O   1 
ATOM   5428  C  CB  . VAL A 1 705  ? 125.835 79.485  141.629 1.00 51.30  ? 705  VAL A CB  1 
ATOM   5429  C  CG1 . VAL A 1 705  ? 125.618 77.989  141.831 1.00 52.05  ? 705  VAL A CG1 1 
ATOM   5430  C  CG2 . VAL A 1 705  ? 124.878 80.282  142.497 1.00 50.37  ? 705  VAL A CG2 1 
ATOM   5431  N  N   . ALA A 1 706  ? 129.067 78.252  141.641 1.00 55.13  ? 706  ALA A N   1 
ATOM   5432  C  CA  . ALA A 1 706  ? 130.067 77.436  140.938 1.00 56.31  ? 706  ALA A CA  1 
ATOM   5433  C  C   . ALA A 1 706  ? 130.860 78.195  139.865 1.00 56.83  ? 706  ALA A C   1 
ATOM   5434  O  O   . ALA A 1 706  ? 130.968 77.739  138.727 1.00 56.63  ? 706  ALA A O   1 
ATOM   5435  C  CB  . ALA A 1 706  ? 129.416 76.186  140.357 1.00 55.80  ? 706  ALA A CB  1 
ATOM   5436  N  N   . ASN A 1 707  ? 131.404 79.352  140.245 1.00 57.85  ? 707  ASN A N   1 
ATOM   5437  C  CA  . ASN A 1 707  ? 132.260 80.178  139.373 1.00 58.61  ? 707  ASN A CA  1 
ATOM   5438  C  C   . ASN A 1 707  ? 131.598 80.685  138.074 1.00 57.48  ? 707  ASN A C   1 
ATOM   5439  O  O   . ASN A 1 707  ? 132.273 80.936  137.075 1.00 57.71  ? 707  ASN A O   1 
ATOM   5440  C  CB  . ASN A 1 707  ? 133.568 79.446  139.060 1.00 59.91  ? 707  ASN A CB  1 
ATOM   5441  C  CG  . ASN A 1 707  ? 134.683 80.395  138.667 1.00 62.88  ? 707  ASN A CG  1 
ATOM   5442  O  OD1 . ASN A 1 707  ? 134.994 80.561  137.475 1.00 64.55  ? 707  ASN A OD1 1 
ATOM   5443  N  ND2 . ASN A 1 707  ? 135.294 81.036  139.668 1.00 65.25  ? 707  ASN A ND2 1 
ATOM   5444  N  N   . GLN A 1 708  ? 130.278 80.849  138.095 1.00 56.30  ? 708  GLN A N   1 
ATOM   5445  C  CA  . GLN A 1 708  ? 129.547 81.282  136.906 1.00 54.91  ? 708  GLN A CA  1 
ATOM   5446  C  C   . GLN A 1 708  ? 129.552 82.786  136.719 1.00 54.24  ? 708  GLN A C   1 
ATOM   5447  O  O   . GLN A 1 708  ? 129.512 83.272  135.590 1.00 54.08  ? 708  GLN A O   1 
ATOM   5448  C  CB  . GLN A 1 708  ? 128.100 80.806  136.959 1.00 54.07  ? 708  GLN A CB  1 
ATOM   5449  C  CG  . GLN A 1 708  ? 127.927 79.316  136.814 1.00 54.66  ? 708  GLN A CG  1 
ATOM   5450  C  CD  . GLN A 1 708  ? 126.532 78.859  137.184 1.00 55.82  ? 708  GLN A CD  1 
ATOM   5451  O  OE1 . GLN A 1 708  ? 125.656 79.663  137.532 1.00 55.75  ? 708  GLN A OE1 1 
ATOM   5452  N  NE2 . GLN A 1 708  ? 126.315 77.556  137.115 1.00 56.96  ? 708  GLN A NE2 1 
ATOM   5453  N  N   . THR A 1 709  ? 129.593 83.520  137.825 1.00 54.01  ? 709  THR A N   1 
ATOM   5454  C  CA  . THR A 1 709  ? 129.338 84.953  137.793 1.00 53.06  ? 709  THR A CA  1 
ATOM   5455  C  C   . THR A 1 709  ? 130.551 85.781  138.172 1.00 53.71  ? 709  THR A C   1 
ATOM   5456  O  O   . THR A 1 709  ? 131.085 85.650  139.272 1.00 54.52  ? 709  THR A O   1 
ATOM   5457  C  CB  . THR A 1 709  ? 128.171 85.344  138.731 1.00 52.44  ? 709  THR A CB  1 
ATOM   5458  O  OG1 . THR A 1 709  ? 127.068 84.453  138.538 1.00 51.62  ? 709  THR A OG1 1 
ATOM   5459  C  CG2 . THR A 1 709  ? 127.723 86.754  138.453 1.00 51.32  ? 709  THR A CG2 1 
ATOM   5460  N  N   . GLU A 1 710  ? 130.976 86.636  137.248 1.00 53.23  ? 710  GLU A N   1 
ATOM   5461  C  CA  . GLU A 1 710  ? 131.860 87.743  137.582 1.00 53.37  ? 710  GLU A CA  1 
ATOM   5462  C  C   . GLU A 1 710  ? 130.987 88.960  137.887 1.00 52.34  ? 710  GLU A C   1 
ATOM   5463  O  O   . GLU A 1 710  ? 130.070 89.285  137.121 1.00 51.53  ? 710  GLU A O   1 
ATOM   5464  C  CB  . GLU A 1 710  ? 132.799 88.051  136.419 1.00 53.65  ? 710  GLU A CB  1 
ATOM   5465  C  CG  . GLU A 1 710  ? 133.684 89.269  136.628 1.00 54.56  ? 710  GLU A CG  1 
ATOM   5466  C  CD  . GLU A 1 710  ? 134.470 89.652  135.381 1.00 55.63  ? 710  GLU A CD  1 
ATOM   5467  O  OE1 . GLU A 1 710  ? 134.368 88.942  134.358 1.00 55.53  ? 710  GLU A OE1 1 
ATOM   5468  O  OE2 . GLU A 1 710  ? 135.191 90.670  135.424 1.00 56.13  ? 710  GLU A OE2 1 
ATOM   5469  N  N   . PHE A 1 711  ? 131.259 89.603  139.018 1.00 52.15  ? 711  PHE A N   1 
ATOM   5470  C  CA  . PHE A 1 711  ? 130.689 90.900  139.334 1.00 51.02  ? 711  PHE A CA  1 
ATOM   5471  C  C   . PHE A 1 711  ? 131.657 91.935  138.813 1.00 51.84  ? 711  PHE A C   1 
ATOM   5472  O  O   . PHE A 1 711  ? 132.767 92.074  139.339 1.00 52.67  ? 711  PHE A O   1 
ATOM   5473  C  CB  . PHE A 1 711  ? 130.539 91.093  140.845 1.00 50.96  ? 711  PHE A CB  1 
ATOM   5474  C  CG  . PHE A 1 711  ? 129.922 89.937  141.551 1.00 49.01  ? 711  PHE A CG  1 
ATOM   5475  C  CD1 . PHE A 1 711  ? 130.710 89.060  142.281 1.00 48.65  ? 711  PHE A CD1 1 
ATOM   5476  C  CD2 . PHE A 1 711  ? 128.556 89.722  141.493 1.00 46.71  ? 711  PHE A CD2 1 
ATOM   5477  C  CE1 . PHE A 1 711  ? 130.147 87.982  142.951 1.00 48.34  ? 711  PHE A CE1 1 
ATOM   5478  C  CE2 . PHE A 1 711  ? 127.981 88.647  142.155 1.00 46.93  ? 711  PHE A CE2 1 
ATOM   5479  C  CZ  . PHE A 1 711  ? 128.781 87.774  142.892 1.00 47.24  ? 711  PHE A CZ  1 
ATOM   5480  N  N   . VAL A 1 712  ? 131.247 92.666  137.785 1.00 51.66  ? 712  VAL A N   1 
ATOM   5481  C  CA  . VAL A 1 712  ? 132.114 93.682  137.206 1.00 52.90  ? 712  VAL A CA  1 
ATOM   5482  C  C   . VAL A 1 712  ? 132.646 94.608  138.299 1.00 54.49  ? 712  VAL A C   1 
ATOM   5483  O  O   . VAL A 1 712  ? 131.874 95.219  139.040 1.00 53.96  ? 712  VAL A O   1 
ATOM   5484  C  CB  . VAL A 1 712  ? 131.402 94.494  136.113 1.00 51.98  ? 712  VAL A CB  1 
ATOM   5485  C  CG1 . VAL A 1 712  ? 132.320 95.556  135.550 1.00 52.02  ? 712  VAL A CG1 1 
ATOM   5486  C  CG2 . VAL A 1 712  ? 130.928 93.578  135.000 1.00 51.56  ? 712  VAL A CG2 1 
ATOM   5487  N  N   . GLY A 1 713  ? 133.971 94.662  138.411 1.00 56.56  ? 713  GLY A N   1 
ATOM   5488  C  CA  . GLY A 1 713  ? 134.631 95.605  139.295 1.00 58.90  ? 713  GLY A CA  1 
ATOM   5489  C  C   . GLY A 1 713  ? 135.074 95.012  140.614 1.00 60.76  ? 713  GLY A C   1 
ATOM   5490  O  O   . GLY A 1 713  ? 135.569 95.728  141.482 1.00 61.84  ? 713  GLY A O   1 
ATOM   5491  N  N   . ARG A 1 714  ? 134.878 93.708  140.778 1.00 61.59  ? 714  ARG A N   1 
ATOM   5492  C  CA  . ARG A 1 714  ? 135.431 92.986  141.928 1.00 63.47  ? 714  ARG A CA  1 
ATOM   5493  C  C   . ARG A 1 714  ? 135.953 91.593  141.550 1.00 63.96  ? 714  ARG A C   1 
ATOM   5494  O  O   . ARG A 1 714  ? 135.444 90.975  140.604 1.00 63.05  ? 714  ARG A O   1 
ATOM   5495  C  CB  . ARG A 1 714  ? 134.450 92.942  143.109 1.00 63.33  ? 714  ARG A CB  1 
ATOM   5496  C  CG  . ARG A 1 714  ? 132.993 92.996  142.751 1.00 63.95  ? 714  ARG A CG  1 
ATOM   5497  C  CD  . ARG A 1 714  ? 132.155 93.162  144.007 1.00 67.50  ? 714  ARG A CD  1 
ATOM   5498  N  NE  . ARG A 1 714  ? 131.946 94.566  144.353 1.00 70.35  ? 714  ARG A NE  1 
ATOM   5499  C  CZ  . ARG A 1 714  ? 131.698 95.012  145.586 1.00 73.10  ? 714  ARG A CZ  1 
ATOM   5500  N  NH1 . ARG A 1 714  ? 131.634 94.172  146.623 1.00 73.21  ? 714  ARG A NH1 1 
ATOM   5501  N  NH2 . ARG A 1 714  ? 131.515 96.312  145.787 1.00 74.75  ? 714  ARG A NH2 1 
ATOM   5502  N  N   . PRO A 1 715  ? 136.981 91.105  142.282 1.00 65.47  ? 715  PRO A N   1 
ATOM   5503  C  CA  . PRO A 1 715  ? 137.716 89.863  141.976 1.00 66.29  ? 715  PRO A CA  1 
ATOM   5504  C  C   . PRO A 1 715  ? 136.844 88.641  141.661 1.00 65.71  ? 715  PRO A C   1 
ATOM   5505  O  O   . PRO A 1 715  ? 135.736 88.511  142.188 1.00 64.99  ? 715  PRO A O   1 
ATOM   5506  C  CB  . PRO A 1 715  ? 138.537 89.614  143.252 1.00 67.54  ? 715  PRO A CB  1 
ATOM   5507  C  CG  . PRO A 1 715  ? 137.997 90.582  144.286 1.00 67.23  ? 715  PRO A CG  1 
ATOM   5508  C  CD  . PRO A 1 715  ? 137.509 91.743  143.501 1.00 66.40  ? 715  PRO A CD  1 
ATOM   5509  N  N   . ASN A 1 716  ? 137.362 87.759  140.807 1.00 66.31  ? 716  ASN A N   1 
ATOM   5510  C  CA  . ASN A 1 716  ? 136.679 86.514  140.428 1.00 66.20  ? 716  ASN A CA  1 
ATOM   5511  C  C   . ASN A 1 716  ? 136.493 85.563  141.603 1.00 66.25  ? 716  ASN A C   1 
ATOM   5512  O  O   . ASN A 1 716  ? 135.700 84.628  141.536 1.00 65.66  ? 716  ASN A O   1 
ATOM   5513  C  CB  . ASN A 1 716  ? 137.466 85.771  139.345 1.00 67.05  ? 716  ASN A CB  1 
ATOM   5514  C  CG  . ASN A 1 716  ? 137.775 86.641  138.140 1.00 68.45  ? 716  ASN A CG  1 
ATOM   5515  O  OD1 . ASN A 1 716  ? 138.609 87.556  138.213 1.00 69.72  ? 716  ASN A OD1 1 
ATOM   5516  N  ND2 . ASN A 1 716  ? 137.114 86.348  137.014 1.00 68.75  ? 716  ASN A ND2 1 
ATOM   5517  N  N   . THR A 1 717  ? 137.247 85.802  142.671 1.00 66.98  ? 717  THR A N   1 
ATOM   5518  C  CA  . THR A 1 717  ? 137.222 84.935  143.840 1.00 67.00  ? 717  THR A CA  1 
ATOM   5519  C  C   . THR A 1 717  ? 135.977 85.149  144.690 1.00 65.71  ? 717  THR A C   1 
ATOM   5520  O  O   . THR A 1 717  ? 135.547 84.230  145.389 1.00 66.03  ? 717  THR A O   1 
ATOM   5521  C  CB  . THR A 1 717  ? 138.503 85.085  144.702 1.00 68.62  ? 717  THR A CB  1 
ATOM   5522  O  OG1 . THR A 1 717  ? 138.865 86.470  144.801 1.00 69.13  ? 717  THR A OG1 1 
ATOM   5523  C  CG2 . THR A 1 717  ? 139.655 84.312  144.076 1.00 69.28  ? 717  THR A CG2 1 
ATOM   5524  N  N   . ASP A 1 718  ? 135.404 86.353  144.620 1.00 64.15  ? 718  ASP A N   1 
ATOM   5525  C  CA  . ASP A 1 718  ? 134.202 86.696  145.384 1.00 62.55  ? 718  ASP A CA  1 
ATOM   5526  C  C   . ASP A 1 718  ? 133.055 85.743  145.073 1.00 60.64  ? 718  ASP A C   1 
ATOM   5527  O  O   . ASP A 1 718  ? 132.808 85.414  143.909 1.00 59.86  ? 718  ASP A O   1 
ATOM   5528  C  CB  . ASP A 1 718  ? 133.770 88.140  145.109 1.00 62.24  ? 718  ASP A CB  1 
ATOM   5529  C  CG  . ASP A 1 718  ? 134.639 89.170  145.825 1.00 64.03  ? 718  ASP A CG  1 
ATOM   5530  O  OD1 . ASP A 1 718  ? 135.816 88.885  146.143 1.00 66.39  ? 718  ASP A OD1 1 
ATOM   5531  O  OD2 . ASP A 1 718  ? 134.140 90.288  146.058 1.00 64.67  ? 718  ASP A OD2 1 
ATOM   5532  N  N   . LEU A 1 719  ? 132.364 85.307  146.121 1.00 59.46  ? 719  LEU A N   1 
ATOM   5533  C  CA  . LEU A 1 719  ? 131.273 84.344  145.993 1.00 57.78  ? 719  LEU A CA  1 
ATOM   5534  C  C   . LEU A 1 719  ? 129.896 85.006  146.027 1.00 55.97  ? 719  LEU A C   1 
ATOM   5535  O  O   . LEU A 1 719  ? 128.890 84.379  145.686 1.00 55.03  ? 719  LEU A O   1 
ATOM   5536  C  CB  . LEU A 1 719  ? 131.357 83.288  147.101 1.00 58.70  ? 719  LEU A CB  1 
ATOM   5537  C  CG  . LEU A 1 719  ? 132.685 82.562  147.362 1.00 60.49  ? 719  LEU A CG  1 
ATOM   5538  C  CD1 . LEU A 1 719  ? 132.606 81.797  148.686 1.00 61.18  ? 719  LEU A CD1 1 
ATOM   5539  C  CD2 . LEU A 1 719  ? 133.082 81.635  146.203 1.00 60.12  ? 719  LEU A CD2 1 
ATOM   5540  N  N   . SER A 1 720  ? 129.855 86.265  146.455 1.00 55.00  ? 720  SER A N   1 
ATOM   5541  C  CA  . SER A 1 720  ? 128.611 87.026  146.529 1.00 52.87  ? 720  SER A CA  1 
ATOM   5542  C  C   . SER A 1 720  ? 128.881 88.529  146.486 1.00 52.37  ? 720  SER A C   1 
ATOM   5543  O  O   . SER A 1 720  ? 130.021 88.980  146.637 1.00 53.32  ? 720  SER A O   1 
ATOM   5544  C  CB  . SER A 1 720  ? 127.829 86.662  147.796 1.00 52.86  ? 720  SER A CB  1 
ATOM   5545  O  OG  . SER A 1 720  ? 128.484 87.142  148.963 1.00 53.57  ? 720  SER A OG  1 
ATOM   5546  N  N   . TYR A 1 721  ? 127.813 89.291  146.283 1.00 50.65  ? 721  TYR A N   1 
ATOM   5547  C  CA  . TYR A 1 721  ? 127.840 90.742  146.245 1.00 49.56  ? 721  TYR A CA  1 
ATOM   5548  C  C   . TYR A 1 721  ? 126.537 91.221  146.869 1.00 48.06  ? 721  TYR A C   1 
ATOM   5549  O  O   . TYR A 1 721  ? 125.448 90.761  146.511 1.00 47.00  ? 721  TYR A O   1 
ATOM   5550  C  CB  . TYR A 1 721  ? 127.959 91.205  144.795 1.00 49.61  ? 721  TYR A CB  1 
ATOM   5551  C  CG  . TYR A 1 721  ? 128.078 92.697  144.548 1.00 50.65  ? 721  TYR A CG  1 
ATOM   5552  C  CD1 . TYR A 1 721  ? 128.489 93.581  145.546 1.00 52.55  ? 721  TYR A CD1 1 
ATOM   5553  C  CD2 . TYR A 1 721  ? 127.827 93.217  143.282 1.00 51.43  ? 721  TYR A CD2 1 
ATOM   5554  C  CE1 . TYR A 1 721  ? 128.610 94.950  145.293 1.00 53.59  ? 721  TYR A CE1 1 
ATOM   5555  C  CE2 . TYR A 1 721  ? 127.953 94.576  143.017 1.00 52.36  ? 721  TYR A CE2 1 
ATOM   5556  C  CZ  . TYR A 1 721  ? 128.345 95.438  144.022 1.00 53.47  ? 721  TYR A CZ  1 
ATOM   5557  O  OH  . TYR A 1 721  ? 128.466 96.783  143.745 1.00 53.50  ? 721  TYR A OH  1 
ATOM   5558  N  N   . THR A 1 722  ? 126.649 92.134  147.819 1.00 47.63  ? 722  THR A N   1 
ATOM   5559  C  CA  . THR A 1 722  ? 125.492 92.593  148.552 1.00 46.23  ? 722  THR A CA  1 
ATOM   5560  C  C   . THR A 1 722  ? 125.358 94.087  148.441 1.00 45.64  ? 722  THR A C   1 
ATOM   5561  O  O   . THR A 1 722  ? 126.316 94.825  148.641 1.00 46.29  ? 722  THR A O   1 
ATOM   5562  C  CB  . THR A 1 722  ? 125.550 92.144  150.021 1.00 46.94  ? 722  THR A CB  1 
ATOM   5563  O  OG1 . THR A 1 722  ? 125.495 90.717  150.053 1.00 47.28  ? 722  THR A OG1 1 
ATOM   5564  C  CG2 . THR A 1 722  ? 124.370 92.691  150.826 1.00 46.16  ? 722  THR A CG2 1 
ATOM   5565  N  N   . LYS A 1 723  ? 124.155 94.514  148.084 1.00 44.15  ? 723  LYS A N   1 
ATOM   5566  C  CA  . LYS A 1 723  ? 123.812 95.916  148.043 1.00 43.63  ? 723  LYS A CA  1 
ATOM   5567  C  C   . LYS A 1 723  ? 122.629 96.125  148.953 1.00 43.22  ? 723  LYS A C   1 
ATOM   5568  O  O   . LYS A 1 723  ? 121.836 95.212  149.170 1.00 43.48  ? 723  LYS A O   1 
ATOM   5569  C  CB  . LYS A 1 723  ? 123.415 96.313  146.630 1.00 42.92  ? 723  LYS A CB  1 
ATOM   5570  C  CG  . LYS A 1 723  ? 124.520 96.278  145.606 1.00 43.04  ? 723  LYS A CG  1 
ATOM   5571  C  CD  . LYS A 1 723  ? 123.979 96.748  144.275 1.00 43.30  ? 723  LYS A CD  1 
ATOM   5572  C  CE  . LYS A 1 723  ? 125.078 96.939  143.254 1.00 44.21  ? 723  LYS A CE  1 
ATOM   5573  N  NZ  . LYS A 1 723  ? 124.555 97.759  142.131 1.00 45.46  ? 723  LYS A NZ  1 
ATOM   5574  N  N   . SER A 1 724  ? 122.494 97.330  149.478 1.00 43.19  ? 724  SER A N   1 
ATOM   5575  C  CA  . SER A 1 724  ? 121.344 97.671  150.290 1.00 42.19  ? 724  SER A CA  1 
ATOM   5576  C  C   . SER A 1 724  ? 120.563 98.796  149.624 1.00 41.77  ? 724  SER A C   1 
ATOM   5577  O  O   . SER A 1 724  ? 121.125 99.563  148.839 1.00 42.37  ? 724  SER A O   1 
ATOM   5578  C  CB  . SER A 1 724  ? 121.806 98.083  151.684 1.00 43.16  ? 724  SER A CB  1 
ATOM   5579  O  OG  . SER A 1 724  ? 122.437 97.002  152.355 1.00 42.22  ? 724  SER A OG  1 
ATOM   5580  N  N   . VAL A 1 725  ? 119.270 98.882  149.920 1.00 40.98  ? 725  VAL A N   1 
ATOM   5581  C  CA  . VAL A 1 725  ? 118.412 99.977  149.454 1.00 40.51  ? 725  VAL A CA  1 
ATOM   5582  C  C   . VAL A 1 725  ? 117.230 100.105 150.411 1.00 40.27  ? 725  VAL A C   1 
ATOM   5583  O  O   . VAL A 1 725  ? 116.773 99.111  150.970 1.00 40.07  ? 725  VAL A O   1 
ATOM   5584  C  CB  . VAL A 1 725  ? 117.916 99.753  147.979 1.00 39.61  ? 725  VAL A CB  1 
ATOM   5585  C  CG1 . VAL A 1 725  ? 116.678 100.513 147.689 1.00 38.61  ? 725  VAL A CG1 1 
ATOM   5586  C  CG2 . VAL A 1 725  ? 118.947 100.231 147.009 1.00 41.25  ? 725  VAL A CG2 1 
ATOM   5587  N  N   . SER A 1 726  ? 116.747 101.327 150.605 1.00 40.26  ? 726  SER A N   1 
ATOM   5588  C  CA  . SER A 1 726  ? 115.560 101.550 151.407 1.00 40.36  ? 726  SER A CA  1 
ATOM   5589  C  C   . SER A 1 726  ? 114.279 101.223 150.623 1.00 39.29  ? 726  SER A C   1 
ATOM   5590  O  O   . SER A 1 726  ? 114.171 101.513 149.432 1.00 38.64  ? 726  SER A O   1 
ATOM   5591  C  CB  . SER A 1 726  ? 115.531 102.982 151.926 1.00 40.82  ? 726  SER A CB  1 
ATOM   5592  O  OG  . SER A 1 726  ? 114.519 103.129 152.911 1.00 42.38  ? 726  SER A OG  1 
ATOM   5593  N  N   . VAL A 1 727  ? 113.310 100.609 151.292 1.00 39.19  ? 727  VAL A N   1 
ATOM   5594  C  CA  . VAL A 1 727  ? 112.075 100.205 150.621 1.00 38.38  ? 727  VAL A CA  1 
ATOM   5595  C  C   . VAL A 1 727  ? 110.886 100.659 151.456 1.00 38.71  ? 727  VAL A C   1 
ATOM   5596  O  O   . VAL A 1 727  ? 110.568 100.046 152.481 1.00 38.85  ? 727  VAL A O   1 
ATOM   5597  C  CB  . VAL A 1 727  ? 112.007 98.657  150.353 1.00 38.15  ? 727  VAL A CB  1 
ATOM   5598  C  CG1 . VAL A 1 727  ? 110.780 98.286  149.515 1.00 36.75  ? 727  VAL A CG1 1 
ATOM   5599  C  CG2 . VAL A 1 727  ? 113.266 98.152  149.673 1.00 37.54  ? 727  VAL A CG2 1 
ATOM   5600  N  N   . PRO A 1 728  ? 110.225 101.747 151.025 1.00 38.90  ? 728  PRO A N   1 
ATOM   5601  C  CA  . PRO A 1 728  ? 108.993 102.197 151.682 1.00 39.02  ? 728  PRO A CA  1 
ATOM   5602  C  C   . PRO A 1 728  ? 107.840 101.194 151.456 1.00 38.54  ? 728  PRO A C   1 
ATOM   5603  O  O   . PRO A 1 728  ? 107.923 100.358 150.557 1.00 37.78  ? 728  PRO A O   1 
ATOM   5604  C  CB  . PRO A 1 728  ? 108.712 103.552 151.019 1.00 38.77  ? 728  PRO A CB  1 
ATOM   5605  C  CG  . PRO A 1 728  ? 109.434 103.526 149.737 1.00 38.39  ? 728  PRO A CG  1 
ATOM   5606  C  CD  . PRO A 1 728  ? 110.601 102.606 149.887 1.00 38.62  ? 728  PRO A CD  1 
ATOM   5607  N  N   . PRO A 1 729  ? 106.793 101.237 152.298 1.00 39.01  ? 729  PRO A N   1 
ATOM   5608  C  CA  . PRO A 1 729  ? 105.661 100.319 152.098 1.00 38.67  ? 729  PRO A CA  1 
ATOM   5609  C  C   . PRO A 1 729  ? 104.978 100.516 150.759 1.00 38.09  ? 729  PRO A C   1 
ATOM   5610  O  O   . PRO A 1 729  ? 104.764 101.657 150.344 1.00 37.85  ? 729  PRO A O   1 
ATOM   5611  C  CB  . PRO A 1 729  ? 104.689 100.707 153.215 1.00 38.52  ? 729  PRO A CB  1 
ATOM   5612  C  CG  . PRO A 1 729  ? 105.557 101.324 154.251 1.00 39.90  ? 729  PRO A CG  1 
ATOM   5613  C  CD  . PRO A 1 729  ? 106.597 102.084 153.485 1.00 39.32  ? 729  PRO A CD  1 
ATOM   5614  N  N   . LYS A 1 730  ? 104.667 99.406  150.092 1.00 38.16  ? 730  LYS A N   1 
ATOM   5615  C  CA  . LYS A 1 730  ? 103.794 99.405  148.922 1.00 38.50  ? 730  LYS A CA  1 
ATOM   5616  C  C   . LYS A 1 730  ? 104.358 100.219 147.759 1.00 38.12  ? 730  LYS A C   1 
ATOM   5617  O  O   . LYS A 1 730  ? 103.599 100.841 146.998 1.00 38.36  ? 730  LYS A O   1 
ATOM   5618  C  CB  . LYS A 1 730  ? 102.405 99.952  149.301 1.00 39.10  ? 730  LYS A CB  1 
ATOM   5619  C  CG  . LYS A 1 730  ? 101.369 98.927  149.770 1.00 41.02  ? 730  LYS A CG  1 
ATOM   5620  C  CD  . LYS A 1 730  ? 101.626 98.392  151.143 1.00 45.98  ? 730  LYS A CD  1 
ATOM   5621  C  CE  . LYS A 1 730  ? 100.499 97.430  151.555 1.00 50.06  ? 730  LYS A CE  1 
ATOM   5622  N  NZ  . LYS A 1 730  ? 99.310  98.134  152.144 1.00 50.84  ? 730  LYS A NZ  1 
ATOM   5623  N  N   . VAL A 1 731  ? 105.685 100.244 147.636 1.00 37.47  ? 731  VAL A N   1 
ATOM   5624  C  CA  . VAL A 1 731  ? 106.335 100.956 146.546 1.00 36.12  ? 731  VAL A CA  1 
ATOM   5625  C  C   . VAL A 1 731  ? 107.434 100.068 146.046 1.00 35.84  ? 731  VAL A C   1 
ATOM   5626  O  O   . VAL A 1 731  ? 108.337 99.727  146.805 1.00 36.15  ? 731  VAL A O   1 
ATOM   5627  C  CB  . VAL A 1 731  ? 106.984 102.308 146.994 1.00 36.77  ? 731  VAL A CB  1 
ATOM   5628  C  CG1 . VAL A 1 731  ? 107.742 102.969 145.814 1.00 35.24  ? 731  VAL A CG1 1 
ATOM   5629  C  CG2 . VAL A 1 731  ? 105.948 103.257 147.551 1.00 35.80  ? 731  VAL A CG2 1 
ATOM   5630  N  N   . GLY A 1 732  ? 107.363 99.688  144.775 1.00 34.86  ? 732  GLY A N   1 
ATOM   5631  C  CA  . GLY A 1 732  ? 108.445 98.926  144.166 1.00 34.58  ? 732  GLY A CA  1 
ATOM   5632  C  C   . GLY A 1 732  ? 109.709 99.773  144.086 1.00 34.90  ? 732  GLY A C   1 
ATOM   5633  O  O   . GLY A 1 732  ? 109.668 100.923 143.608 1.00 34.98  ? 732  GLY A O   1 
ATOM   5634  N  N   . VAL A 1 733  ? 110.821 99.235  144.588 1.00 34.28  ? 733  VAL A N   1 
ATOM   5635  C  CA  . VAL A 1 733  ? 112.107 99.888  144.384 1.00 34.14  ? 733  VAL A CA  1 
ATOM   5636  C  C   . VAL A 1 733  ? 113.075 98.935  143.672 1.00 33.88  ? 733  VAL A C   1 
ATOM   5637  O  O   . VAL A 1 733  ? 113.153 97.744  144.011 1.00 34.04  ? 733  VAL A O   1 
ATOM   5638  C  CB  . VAL A 1 733  ? 112.694 100.549 145.693 1.00 34.99  ? 733  VAL A CB  1 
ATOM   5639  C  CG1 . VAL A 1 733  ? 111.664 100.588 146.790 1.00 34.70  ? 733  VAL A CG1 1 
ATOM   5640  C  CG2 . VAL A 1 733  ? 113.928 99.866  146.167 1.00 34.79  ? 733  VAL A CG2 1 
ATOM   5641  N  N   . PRO A 1 734  ? 113.784 99.446  142.655 1.00 33.35  ? 734  PRO A N   1 
ATOM   5642  C  CA  . PRO A 1 734  ? 114.637 98.593  141.826 1.00 33.06  ? 734  PRO A CA  1 
ATOM   5643  C  C   . PRO A 1 734  ? 115.969 98.300  142.510 1.00 33.98  ? 734  PRO A C   1 
ATOM   5644  O  O   . PRO A 1 734  ? 116.378 99.023  143.421 1.00 34.66  ? 734  PRO A O   1 
ATOM   5645  C  CB  . PRO A 1 734  ? 114.865 99.445  140.584 1.00 32.48  ? 734  PRO A CB  1 
ATOM   5646  C  CG  . PRO A 1 734  ? 114.802 100.847 141.080 1.00 32.95  ? 734  PRO A CG  1 
ATOM   5647  C  CD  . PRO A 1 734  ? 113.832 100.858 142.232 1.00 33.18  ? 734  PRO A CD  1 
ATOM   5648  N  N   . ILE A 1 735  ? 116.628 97.234  142.081 1.00 33.91  ? 735  ILE A N   1 
ATOM   5649  C  CA  . ILE A 1 735  ? 117.982 96.925  142.538 1.00 34.89  ? 735  ILE A CA  1 
ATOM   5650  C  C   . ILE A 1 735  ? 118.595 96.115  141.423 1.00 34.82  ? 735  ILE A C   1 
ATOM   5651  O  O   . ILE A 1 735  ? 117.885 95.340  140.762 1.00 34.70  ? 735  ILE A O   1 
ATOM   5652  C  CB  . ILE A 1 735  ? 118.019 96.157  143.912 1.00 35.44  ? 735  ILE A CB  1 
ATOM   5653  C  CG1 . ILE A 1 735  ? 119.436 96.043  144.442 1.00 36.26  ? 735  ILE A CG1 1 
ATOM   5654  C  CG2 . ILE A 1 735  ? 117.434 94.762  143.826 1.00 34.93  ? 735  ILE A CG2 1 
ATOM   5655  C  CD1 . ILE A 1 735  ? 119.895 97.262  145.153 1.00 37.62  ? 735  ILE A CD1 1 
ATOM   5656  N  N   . SER A 1 736  ? 119.883 96.304  141.173 1.00 35.02  ? 736  SER A N   1 
ATOM   5657  C  CA  . SER A 1 736  ? 120.488 95.625  140.042 1.00 35.18  ? 736  SER A CA  1 
ATOM   5658  C  C   . SER A 1 736  ? 121.969 95.351  140.195 1.00 36.20  ? 736  SER A C   1 
ATOM   5659  O  O   . SER A 1 736  ? 122.655 96.018  140.982 1.00 36.85  ? 736  SER A O   1 
ATOM   5660  C  CB  . SER A 1 736  ? 120.216 96.390  138.754 1.00 34.64  ? 736  SER A CB  1 
ATOM   5661  O  OG  . SER A 1 736  ? 120.584 97.737  138.884 1.00 35.90  ? 736  SER A OG  1 
ATOM   5662  N  N   . PHE A 1 737  ? 122.444 94.361  139.439 1.00 36.18  ? 737  PHE A N   1 
ATOM   5663  C  CA  . PHE A 1 737  ? 123.837 93.938  139.488 1.00 37.52  ? 737  PHE A CA  1 
ATOM   5664  C  C   . PHE A 1 737  ? 124.418 93.851  138.093 1.00 38.16  ? 737  PHE A C   1 
ATOM   5665  O  O   . PHE A 1 737  ? 123.772 93.350  137.173 1.00 38.19  ? 737  PHE A O   1 
ATOM   5666  C  CB  . PHE A 1 737  ? 123.972 92.593  140.203 1.00 37.42  ? 737  PHE A CB  1 
ATOM   5667  C  CG  . PHE A 1 737  ? 123.484 92.609  141.633 1.00 37.14  ? 737  PHE A CG  1 
ATOM   5668  C  CD1 . PHE A 1 737  ? 122.151 92.333  141.936 1.00 35.47  ? 737  PHE A CD1 1 
ATOM   5669  C  CD2 . PHE A 1 737  ? 124.351 92.909  142.674 1.00 37.67  ? 737  PHE A CD2 1 
ATOM   5670  C  CE1 . PHE A 1 737  ? 121.689 92.357  143.253 1.00 34.06  ? 737  PHE A CE1 1 
ATOM   5671  C  CE2 . PHE A 1 737  ? 123.892 92.921  144.001 1.00 37.71  ? 737  PHE A CE2 1 
ATOM   5672  C  CZ  . PHE A 1 737  ? 122.555 92.637  144.279 1.00 35.29  ? 737  PHE A CZ  1 
ATOM   5673  N  N   . LEU A 1 738  ? 125.631 94.367  137.938 1.00 39.73  ? 738  LEU A N   1 
ATOM   5674  C  CA  . LEU A 1 738  ? 126.319 94.362  136.667 1.00 40.65  ? 738  LEU A CA  1 
ATOM   5675  C  C   . LEU A 1 738  ? 127.225 93.156  136.658 1.00 42.14  ? 738  LEU A C   1 
ATOM   5676  O  O   . LEU A 1 738  ? 128.200 93.090  137.430 1.00 43.24  ? 738  LEU A O   1 
ATOM   5677  C  CB  . LEU A 1 738  ? 127.156 95.629  136.506 1.00 41.28  ? 738  LEU A CB  1 
ATOM   5678  C  CG  . LEU A 1 738  ? 127.387 96.234  135.110 1.00 41.88  ? 738  LEU A CG  1 
ATOM   5679  C  CD1 . LEU A 1 738  ? 128.792 96.811  134.992 1.00 40.98  ? 738  LEU A CD1 1 
ATOM   5680  C  CD2 . LEU A 1 738  ? 127.123 95.261  133.964 1.00 41.82  ? 738  LEU A CD2 1 
ATOM   5681  N  N   . ILE A 1 739  ? 126.919 92.195  135.790 1.00 42.61  ? 739  ILE A N   1 
ATOM   5682  C  CA  . ILE A 1 739  ? 127.689 90.954  135.778 1.00 43.99  ? 739  ILE A CA  1 
ATOM   5683  C  C   . ILE A 1 739  ? 128.203 90.538  134.399 1.00 44.90  ? 739  ILE A C   1 
ATOM   5684  O  O   . ILE A 1 739  ? 127.797 91.093  133.371 1.00 44.49  ? 739  ILE A O   1 
ATOM   5685  C  CB  . ILE A 1 739  ? 126.891 89.794  136.416 1.00 43.66  ? 739  ILE A CB  1 
ATOM   5686  C  CG1 . ILE A 1 739  ? 125.618 89.508  135.618 1.00 42.32  ? 739  ILE A CG1 1 
ATOM   5687  C  CG2 . ILE A 1 739  ? 126.559 90.106  137.868 1.00 43.43  ? 739  ILE A CG2 1 
ATOM   5688  C  CD1 . ILE A 1 739  ? 125.439 88.064  135.300 1.00 41.32  ? 739  ILE A CD1 1 
ATOM   5689  N  N   . LYS A 1 740  ? 129.117 89.568  134.399 1.00 46.64  ? 740  LYS A N   1 
ATOM   5690  C  CA  . LYS A 1 740  ? 129.534 88.856  133.180 1.00 47.38  ? 740  LYS A CA  1 
ATOM   5691  C  C   . LYS A 1 740  ? 129.449 87.368  133.446 1.00 48.17  ? 740  LYS A C   1 
ATOM   5692  O  O   . LYS A 1 740  ? 129.695 86.919  134.570 1.00 48.99  ? 740  LYS A O   1 
ATOM   5693  C  CB  . LYS A 1 740  ? 130.966 89.201  132.794 1.00 47.99  ? 740  LYS A CB  1 
ATOM   5694  C  CG  . LYS A 1 740  ? 131.136 90.567  132.176 1.00 48.42  ? 740  LYS A CG  1 
ATOM   5695  C  CD  . LYS A 1 740  ? 132.596 90.831  131.849 1.00 50.41  ? 740  LYS A CD  1 
ATOM   5696  C  CE  . LYS A 1 740  ? 132.836 92.311  131.596 1.00 51.72  ? 740  LYS A CE  1 
ATOM   5697  N  NZ  . LYS A 1 740  ? 134.221 92.600  131.138 1.00 53.04  ? 740  LYS A NZ  1 
ATOM   5698  N  N   . ALA A 1 741  ? 129.090 86.604  132.421 1.00 48.70  ? 741  ALA A N   1 
ATOM   5699  C  CA  . ALA A 1 741  ? 129.031 85.161  132.545 1.00 49.80  ? 741  ALA A CA  1 
ATOM   5700  C  C   . ALA A 1 741  ? 130.378 84.560  132.172 1.00 51.82  ? 741  ALA A C   1 
ATOM   5701  O  O   . ALA A 1 741  ? 131.003 84.986  131.194 1.00 51.93  ? 741  ALA A O   1 
ATOM   5702  C  CB  . ALA A 1 741  ? 127.946 84.610  131.678 1.00 48.68  ? 741  ALA A CB  1 
ATOM   5703  N  N   . ARG A 1 742  ? 130.814 83.581  132.967 1.00 53.89  ? 742  ARG A N   1 
ATOM   5704  C  CA  . ARG A 1 742  ? 132.100 82.894  132.782 1.00 56.35  ? 742  ARG A CA  1 
ATOM   5705  C  C   . ARG A 1 742  ? 131.967 81.604  131.969 1.00 56.71  ? 742  ARG A C   1 
ATOM   5706  O  O   . ARG A 1 742  ? 132.852 81.269  131.186 1.00 57.40  ? 742  ARG A O   1 
ATOM   5707  C  CB  . ARG A 1 742  ? 132.720 82.537  134.138 1.00 57.51  ? 742  ARG A CB  1 
ATOM   5708  C  CG  . ARG A 1 742  ? 132.694 83.647  135.184 1.00 59.82  ? 742  ARG A CG  1 
ATOM   5709  C  CD  . ARG A 1 742  ? 133.973 84.457  135.202 1.00 64.49  ? 742  ARG A CD  1 
ATOM   5710  N  NE  . ARG A 1 742  ? 135.067 83.763  135.874 1.00 68.83  ? 742  ARG A NE  1 
ATOM   5711  C  CZ  . ARG A 1 742  ? 135.287 83.789  137.189 1.00 72.10  ? 742  ARG A CZ  1 
ATOM   5712  N  NH1 . ARG A 1 742  ? 134.472 84.470  138.002 1.00 71.44  ? 742  ARG A NH1 1 
ATOM   5713  N  NH2 . ARG A 1 742  ? 136.332 83.125  137.696 1.00 73.62  ? 742  ARG A NH2 1 
ATOM   5714  N  N   . LYS A 1 743  ? 130.860 80.889  132.168 1.00 56.60  ? 743  LYS A N   1 
ATOM   5715  C  CA  . LYS A 1 743  ? 130.679 79.546  131.623 1.00 56.95  ? 743  LYS A CA  1 
ATOM   5716  C  C   . LYS A 1 743  ? 129.461 79.413  130.716 1.00 56.06  ? 743  LYS A C   1 
ATOM   5717  O  O   . LYS A 1 743  ? 128.379 79.937  131.011 1.00 55.32  ? 743  LYS A O   1 
ATOM   5718  C  CB  . LYS A 1 743  ? 130.536 78.536  132.763 1.00 57.53  ? 743  LYS A CB  1 
ATOM   5719  C  CG  . LYS A 1 743  ? 131.801 78.297  133.570 1.00 60.47  ? 743  LYS A CG  1 
ATOM   5720  C  CD  . LYS A 1 743  ? 131.801 76.888  134.148 1.00 64.03  ? 743  LYS A CD  1 
ATOM   5721  C  CE  . LYS A 1 743  ? 131.138 76.823  135.520 1.00 65.34  ? 743  LYS A CE  1 
ATOM   5722  N  NZ  . LYS A 1 743  ? 132.168 76.944  136.598 1.00 67.63  ? 743  LYS A NZ  1 
ATOM   5723  N  N   . LEU A 1 744  ? 129.636 78.678  129.622 1.00 56.27  ? 744  LEU A N   1 
ATOM   5724  C  CA  . LEU A 1 744  ? 128.516 78.304  128.777 1.00 55.53  ? 744  LEU A CA  1 
ATOM   5725  C  C   . LEU A 1 744  ? 127.576 77.389  129.553 1.00 55.36  ? 744  LEU A C   1 
ATOM   5726  O  O   . LEU A 1 744  ? 128.006 76.635  130.434 1.00 55.77  ? 744  LEU A O   1 
ATOM   5727  C  CB  . LEU A 1 744  ? 129.004 77.590  127.520 1.00 55.98  ? 744  LEU A CB  1 
ATOM   5728  C  CG  . LEU A 1 744  ? 129.878 78.315  126.491 1.00 56.94  ? 744  LEU A CG  1 
ATOM   5729  C  CD1 . LEU A 1 744  ? 130.194 77.367  125.357 1.00 57.17  ? 744  LEU A CD1 1 
ATOM   5730  C  CD2 . LEU A 1 744  ? 129.204 79.557  125.939 1.00 57.10  ? 744  LEU A CD2 1 
ATOM   5731  N  N   . GLY A 1 745  ? 126.293 77.463  129.229 1.00 54.51  ? 745  GLY A N   1 
ATOM   5732  C  CA  . GLY A 1 745  ? 125.319 76.579  129.826 1.00 54.57  ? 745  GLY A CA  1 
ATOM   5733  C  C   . GLY A 1 745  ? 124.303 77.384  130.590 1.00 54.46  ? 745  GLY A C   1 
ATOM   5734  O  O   . GLY A 1 745  ? 124.029 78.534  130.242 1.00 54.37  ? 745  GLY A O   1 
ATOM   5735  N  N   . GLU A 1 746  ? 123.734 76.770  131.624 1.00 54.52  ? 746  GLU A N   1 
ATOM   5736  C  CA  . GLU A 1 746  ? 122.770 77.435  132.476 1.00 53.87  ? 746  GLU A CA  1 
ATOM   5737  C  C   . GLU A 1 746  ? 123.524 78.185  133.539 1.00 53.65  ? 746  GLU A C   1 
ATOM   5738  O  O   . GLU A 1 746  ? 124.353 77.598  134.238 1.00 54.71  ? 746  GLU A O   1 
ATOM   5739  C  CB  . GLU A 1 746  ? 121.846 76.426  133.150 1.00 54.15  ? 746  GLU A CB  1 
ATOM   5740  C  CG  . GLU A 1 746  ? 120.881 75.727  132.211 1.00 55.81  ? 746  GLU A CG  1 
ATOM   5741  C  CD  . GLU A 1 746  ? 119.546 75.409  132.867 1.00 59.40  ? 746  GLU A CD  1 
ATOM   5742  O  OE1 . GLU A 1 746  ? 119.477 75.259  134.123 1.00 59.60  ? 746  GLU A OE1 1 
ATOM   5743  O  OE2 . GLU A 1 746  ? 118.552 75.313  132.105 1.00 61.52  ? 746  GLU A OE2 1 
ATOM   5744  N  N   . MET A 1 747  ? 123.252 79.483  133.651 1.00 52.33  ? 747  MET A N   1 
ATOM   5745  C  CA  . MET A 1 747  ? 123.730 80.265  134.781 1.00 51.64  ? 747  MET A CA  1 
ATOM   5746  C  C   . MET A 1 747  ? 122.640 80.327  135.834 1.00 50.59  ? 747  MET A C   1 
ATOM   5747  O  O   . MET A 1 747  ? 121.515 80.735  135.555 1.00 49.81  ? 747  MET A O   1 
ATOM   5748  C  CB  . MET A 1 747  ? 124.133 81.674  134.355 1.00 51.60  ? 747  MET A CB  1 
ATOM   5749  C  CG  . MET A 1 747  ? 124.167 82.663  135.507 1.00 51.53  ? 747  MET A CG  1 
ATOM   5750  S  SD  . MET A 1 747  ? 124.514 84.336  134.978 1.00 50.66  ? 747  MET A SD  1 
ATOM   5751  C  CE  . MET A 1 747  ? 126.294 84.353  135.157 1.00 52.71  ? 747  MET A CE  1 
ATOM   5752  N  N   . ALA A 1 748  ? 122.980 79.908  137.045 1.00 50.55  ? 748  ALA A N   1 
ATOM   5753  C  CA  . ALA A 1 748  ? 122.065 80.008  138.163 1.00 49.68  ? 748  ALA A CA  1 
ATOM   5754  C  C   . ALA A 1 748  ? 122.026 81.459  138.607 1.00 49.06  ? 748  ALA A C   1 
ATOM   5755  O  O   . ALA A 1 748  ? 123.065 82.067  138.863 1.00 49.55  ? 748  ALA A O   1 
ATOM   5756  C  CB  . ALA A 1 748  ? 122.522 79.117  139.294 1.00 50.25  ? 748  ALA A CB  1 
ATOM   5757  N  N   . VAL A 1 749  ? 120.833 82.030  138.664 1.00 47.98  ? 749  VAL A N   1 
ATOM   5758  C  CA  . VAL A 1 749  ? 120.688 83.355  139.255 1.00 47.40  ? 749  VAL A CA  1 
ATOM   5759  C  C   . VAL A 1 749  ? 120.081 83.197  140.646 1.00 47.58  ? 749  VAL A C   1 
ATOM   5760  O  O   . VAL A 1 749  ? 118.875 83.011  140.793 1.00 46.70  ? 749  VAL A O   1 
ATOM   5761  C  CB  . VAL A 1 749  ? 119.925 84.339  138.349 1.00 46.13  ? 749  VAL A CB  1 
ATOM   5762  C  CG1 . VAL A 1 749  ? 119.799 85.686  139.027 1.00 45.92  ? 749  VAL A CG1 1 
ATOM   5763  C  CG2 . VAL A 1 749  ? 120.681 84.516  137.057 1.00 45.40  ? 749  VAL A CG2 1 
ATOM   5764  N  N   . ARG A 1 750  ? 120.960 83.239  141.646 1.00 48.55  ? 750  ARG A N   1 
ATOM   5765  C  CA  . ARG A 1 750  ? 120.628 82.933  143.035 1.00 49.42  ? 750  ARG A CA  1 
ATOM   5766  C  C   . ARG A 1 750  ? 120.670 84.205  143.885 1.00 49.59  ? 750  ARG A C   1 
ATOM   5767  O  O   . ARG A 1 750  ? 121.746 84.786  144.121 1.00 50.14  ? 750  ARG A O   1 
ATOM   5768  C  CB  . ARG A 1 750  ? 121.604 81.875  143.570 1.00 50.44  ? 750  ARG A CB  1 
ATOM   5769  C  CG  . ARG A 1 750  ? 121.323 81.352  144.976 1.00 52.19  ? 750  ARG A CG  1 
ATOM   5770  C  CD  . ARG A 1 750  ? 122.162 80.103  145.269 1.00 55.53  ? 750  ARG A CD  1 
ATOM   5771  N  NE  . ARG A 1 750  ? 121.812 78.983  144.383 1.00 58.14  ? 750  ARG A NE  1 
ATOM   5772  C  CZ  . ARG A 1 750  ? 122.578 77.912  144.156 1.00 59.32  ? 750  ARG A CZ  1 
ATOM   5773  N  NH1 . ARG A 1 750  ? 123.764 77.782  144.744 1.00 60.80  ? 750  ARG A NH1 1 
ATOM   5774  N  NH2 . ARG A 1 750  ? 122.156 76.964  143.329 1.00 58.28  ? 750  ARG A NH2 1 
ATOM   5775  N  N   . VAL A 1 751  ? 119.495 84.628  144.343 1.00 49.05  ? 751  VAL A N   1 
ATOM   5776  C  CA  . VAL A 1 751  ? 119.357 85.889  145.067 1.00 49.40  ? 751  VAL A CA  1 
ATOM   5777  C  C   . VAL A 1 751  ? 118.670 85.685  146.406 1.00 49.87  ? 751  VAL A C   1 
ATOM   5778  O  O   . VAL A 1 751  ? 117.694 84.948  146.493 1.00 49.53  ? 751  VAL A O   1 
ATOM   5779  C  CB  . VAL A 1 751  ? 118.541 86.923  144.256 1.00 48.51  ? 751  VAL A CB  1 
ATOM   5780  C  CG1 . VAL A 1 751  ? 118.512 88.257  144.968 1.00 48.36  ? 751  VAL A CG1 1 
ATOM   5781  C  CG2 . VAL A 1 751  ? 119.117 87.093  142.867 1.00 48.47  ? 751  VAL A CG2 1 
ATOM   5782  N  N   . LYS A 1 752  ? 119.187 86.334  147.444 1.00 50.88  ? 752  LYS A N   1 
ATOM   5783  C  CA  . LYS A 1 752  ? 118.495 86.404  148.731 1.00 51.78  ? 752  LYS A CA  1 
ATOM   5784  C  C   . LYS A 1 752  ? 118.311 87.854  149.135 1.00 51.33  ? 752  LYS A C   1 
ATOM   5785  O  O   . LYS A 1 752  ? 119.229 88.659  148.981 1.00 51.81  ? 752  LYS A O   1 
ATOM   5786  C  CB  . LYS A 1 752  ? 119.267 85.661  149.820 1.00 53.27  ? 752  LYS A CB  1 
ATOM   5787  C  CG  . LYS A 1 752  ? 119.410 84.170  149.567 1.00 56.23  ? 752  LYS A CG  1 
ATOM   5788  C  CD  . LYS A 1 752  ? 119.759 83.393  150.850 1.00 61.25  ? 752  LYS A CD  1 
ATOM   5789  C  CE  . LYS A 1 752  ? 119.597 81.871  150.644 1.00 63.25  ? 752  LYS A CE  1 
ATOM   5790  N  NZ  . LYS A 1 752  ? 118.304 81.478  149.961 1.00 61.94  ? 752  LYS A NZ  1 
ATOM   5791  N  N   . ALA A 1 753  ? 117.123 88.177  149.637 1.00 50.59  ? 753  ALA A N   1 
ATOM   5792  C  CA  . ALA A 1 753  ? 116.801 89.516  150.125 1.00 50.41  ? 753  ALA A CA  1 
ATOM   5793  C  C   . ALA A 1 753  ? 116.194 89.426  151.529 1.00 50.96  ? 753  ALA A C   1 
ATOM   5794  O  O   . ALA A 1 753  ? 115.492 88.462  151.834 1.00 50.68  ? 753  ALA A O   1 
ATOM   5795  C  CB  . ALA A 1 753  ? 115.849 90.196  149.176 1.00 48.93  ? 753  ALA A CB  1 
ATOM   5796  N  N   . SER A 1 754  ? 116.480 90.414  152.381 1.00 51.81  ? 754  SER A N   1 
ATOM   5797  C  CA  . SER A 1 754  ? 115.870 90.506  153.717 1.00 52.54  ? 754  SER A CA  1 
ATOM   5798  C  C   . SER A 1 754  ? 115.814 91.955  154.209 1.00 53.37  ? 754  SER A C   1 
ATOM   5799  O  O   . SER A 1 754  ? 116.513 92.799  153.651 1.00 53.80  ? 754  SER A O   1 
ATOM   5800  C  CB  . SER A 1 754  ? 116.625 89.630  154.713 1.00 53.32  ? 754  SER A CB  1 
ATOM   5801  O  OG  . SER A 1 754  ? 117.893 90.163  155.003 1.00 53.29  ? 754  SER A OG  1 
ATOM   5802  N  N   . ILE A 1 755  ? 115.012 92.242  155.247 1.00 54.11  ? 755  ILE A N   1 
ATOM   5803  C  CA  . ILE A 1 755  ? 114.810 93.631  155.714 1.00 54.86  ? 755  ILE A CA  1 
ATOM   5804  C  C   . ILE A 1 755  ? 115.096 93.984  157.180 1.00 56.74  ? 755  ILE A C   1 
ATOM   5805  O  O   . ILE A 1 755  ? 115.714 95.030  157.465 1.00 58.02  ? 755  ILE A O   1 
ATOM   5806  C  CB  . ILE A 1 755  ? 113.416 94.191  155.368 1.00 53.85  ? 755  ILE A CB  1 
ATOM   5807  C  CG1 . ILE A 1 755  ? 112.326 93.158  155.635 1.00 53.38  ? 755  ILE A CG1 1 
ATOM   5808  C  CG2 . ILE A 1 755  ? 113.380 94.682  153.928 1.00 53.41  ? 755  ILE A CG2 1 
ATOM   5809  C  CD1 . ILE A 1 755  ? 110.948 93.585  155.178 1.00 52.14  ? 755  ILE A CD1 1 
ATOM   5810  N  N   . MET A 1 756  ? 114.638 93.168  158.118 1.00 57.35  ? 756  MET A N   1 
ATOM   5811  C  CA  . MET A 1 756  ? 114.835 93.533  159.520 1.00 58.33  ? 756  MET A CA  1 
ATOM   5812  C  C   . MET A 1 756  ? 115.770 92.546  160.180 1.00 59.43  ? 756  MET A C   1 
ATOM   5813  O  O   . MET A 1 756  ? 115.351 91.700  160.973 1.00 59.68  ? 756  MET A O   1 
ATOM   5814  C  CB  . MET A 1 756  ? 113.507 93.615  160.263 1.00 58.14  ? 756  MET A CB  1 
ATOM   5815  C  CG  . MET A 1 756  ? 112.602 94.739  159.805 1.00 58.33  ? 756  MET A CG  1 
ATOM   5816  S  SD  . MET A 1 756  ? 110.922 94.591  160.463 1.00 59.24  ? 756  MET A SD  1 
ATOM   5817  C  CE  . MET A 1 756  ? 110.479 92.960  159.880 1.00 59.15  ? 756  MET A CE  1 
ATOM   5818  N  N   . LEU A 1 757  ? 117.050 92.652  159.840 1.00 60.28  ? 757  LEU A N   1 
ATOM   5819  C  CA  . LEU A 1 757  ? 118.055 91.700  160.311 1.00 61.51  ? 757  LEU A CA  1 
ATOM   5820  C  C   . LEU A 1 757  ? 117.636 90.256  160.019 1.00 61.32  ? 757  LEU A C   1 
ATOM   5821  O  O   . LEU A 1 757  ? 117.964 89.342  160.778 1.00 62.63  ? 757  LEU A O   1 
ATOM   5822  C  CB  . LEU A 1 757  ? 118.336 91.882  161.813 1.00 62.50  ? 757  LEU A CB  1 
ATOM   5823  C  CG  . LEU A 1 757  ? 118.964 93.192  162.291 1.00 63.49  ? 757  LEU A CG  1 
ATOM   5824  C  CD1 . LEU A 1 757  ? 119.031 93.237  163.823 1.00 64.85  ? 757  LEU A CD1 1 
ATOM   5825  C  CD2 . LEU A 1 757  ? 120.351 93.399  161.673 1.00 63.79  ? 757  LEU A CD2 1 
ATOM   5826  N  N   . GLY A 1 758  ? 116.899 90.059  158.929 1.00 60.18  ? 758  GLY A N   1 
ATOM   5827  C  CA  . GLY A 1 758  ? 116.518 88.722  158.503 1.00 59.79  ? 758  GLY A CA  1 
ATOM   5828  C  C   . GLY A 1 758  ? 115.230 88.201  159.106 1.00 59.67  ? 758  GLY A C   1 
ATOM   5829  O  O   . GLY A 1 758  ? 114.909 87.020  158.950 1.00 59.46  ? 758  GLY A O   1 
ATOM   5830  N  N   . HIS A 1 759  ? 114.488 89.071  159.789 1.00 59.89  ? 759  HIS A N   1 
ATOM   5831  C  CA  . HIS A 1 759  ? 113.174 88.709  160.318 1.00 59.97  ? 759  HIS A CA  1 
ATOM   5832  C  C   . HIS A 1 759  ? 112.156 88.503  159.197 1.00 58.61  ? 759  HIS A C   1 
ATOM   5833  O  O   . HIS A 1 759  ? 111.042 88.028  159.426 1.00 58.60  ? 759  HIS A O   1 
ATOM   5834  C  CB  . HIS A 1 759  ? 112.678 89.746  161.326 1.00 60.39  ? 759  HIS A CB  1 
ATOM   5835  C  CG  . HIS A 1 759  ? 113.323 89.626  162.678 1.00 64.39  ? 759  HIS A CG  1 
ATOM   5836  N  ND1 . HIS A 1 759  ? 113.949 90.685  163.307 1.00 66.96  ? 759  HIS A ND1 1 
ATOM   5837  C  CD2 . HIS A 1 759  ? 113.443 88.568  163.518 1.00 66.45  ? 759  HIS A CD2 1 
ATOM   5838  C  CE1 . HIS A 1 759  ? 114.424 90.284  164.474 1.00 68.56  ? 759  HIS A CE1 1 
ATOM   5839  N  NE2 . HIS A 1 759  ? 114.128 89.004  164.628 1.00 68.28  ? 759  HIS A NE2 1 
ATOM   5840  N  N   . GLU A 1 760  ? 112.560 88.838  157.978 1.00 57.63  ? 760  GLU A N   1 
ATOM   5841  C  CA  . GLU A 1 760  ? 111.677 88.807  156.830 1.00 56.14  ? 760  GLU A CA  1 
ATOM   5842  C  C   . GLU A 1 760  ? 112.545 88.658  155.597 1.00 55.43  ? 760  GLU A C   1 
ATOM   5843  O  O   . GLU A 1 760  ? 113.376 89.513  155.312 1.00 55.69  ? 760  GLU A O   1 
ATOM   5844  C  CB  . GLU A 1 760  ? 110.883 90.108  156.776 1.00 55.67  ? 760  GLU A CB  1 
ATOM   5845  C  CG  . GLU A 1 760  ? 109.435 89.942  156.409 1.00 55.96  ? 760  GLU A CG  1 
ATOM   5846  C  CD  . GLU A 1 760  ? 108.692 88.988  157.330 1.00 57.29  ? 760  GLU A CD  1 
ATOM   5847  O  OE1 . GLU A 1 760  ? 108.577 89.273  158.545 1.00 57.69  ? 760  GLU A OE1 1 
ATOM   5848  O  OE2 . GLU A 1 760  ? 108.217 87.949  156.822 1.00 57.92  ? 760  GLU A OE2 1 
ATOM   5849  N  N   . THR A 1 761  ? 112.385 87.551  154.884 1.00 54.48  ? 761  THR A N   1 
ATOM   5850  C  CA  . THR A 1 761  ? 113.278 87.247  153.781 1.00 53.94  ? 761  THR A CA  1 
ATOM   5851  C  C   . THR A 1 761  ? 112.533 86.772  152.558 1.00 52.77  ? 761  THR A C   1 
ATOM   5852  O  O   . THR A 1 761  ? 111.394 86.316  152.644 1.00 52.75  ? 761  THR A O   1 
ATOM   5853  C  CB  . THR A 1 761  ? 114.295 86.140  154.148 1.00 54.98  ? 761  THR A CB  1 
ATOM   5854  O  OG1 . THR A 1 761  ? 113.607 84.896  154.312 1.00 55.97  ? 761  THR A OG1 1 
ATOM   5855  C  CG2 . THR A 1 761  ? 115.075 86.469  155.423 1.00 55.10  ? 761  THR A CG2 1 
ATOM   5856  N  N   . ASP A 1 762  ? 113.188 86.877  151.411 1.00 52.09  ? 762  ASP A N   1 
ATOM   5857  C  CA  . ASP A 1 762  ? 112.726 86.215  150.197 1.00 50.86  ? 762  ASP A CA  1 
ATOM   5858  C  C   . ASP A 1 762  ? 113.946 85.741  149.424 1.00 50.67  ? 762  ASP A C   1 
ATOM   5859  O  O   . ASP A 1 762  ? 115.038 86.284  149.572 1.00 51.19  ? 762  ASP A O   1 
ATOM   5860  C  CB  . ASP A 1 762  ? 111.844 87.131  149.345 1.00 50.14  ? 762  ASP A CB  1 
ATOM   5861  C  CG  . ASP A 1 762  ? 111.075 86.369  148.274 1.00 50.11  ? 762  ASP A CG  1 
ATOM   5862  O  OD1 . ASP A 1 762  ? 110.997 85.134  148.379 1.00 52.54  ? 762  ASP A OD1 1 
ATOM   5863  O  OD2 . ASP A 1 762  ? 110.553 86.986  147.323 1.00 49.35  ? 762  ASP A OD2 1 
ATOM   5864  N  N   . ALA A 1 763  ? 113.767 84.703  148.626 1.00 49.98  ? 763  ALA A N   1 
ATOM   5865  C  CA  . ALA A 1 763  ? 114.862 84.132  147.871 1.00 50.00  ? 763  ALA A CA  1 
ATOM   5866  C  C   . ALA A 1 763  ? 114.340 83.733  146.516 1.00 49.27  ? 763  ALA A C   1 
ATOM   5867  O  O   . ALA A 1 763  ? 113.160 83.418  146.383 1.00 48.95  ? 763  ALA A O   1 
ATOM   5868  C  CB  . ALA A 1 763  ? 115.406 82.922  148.583 1.00 50.57  ? 763  ALA A CB  1 
ATOM   5869  N  N   . LEU A 1 764  ? 115.202 83.756  145.508 1.00 49.24  ? 764  LEU A N   1 
ATOM   5870  C  CA  . LEU A 1 764  ? 114.840 83.157  144.235 1.00 49.17  ? 764  LEU A CA  1 
ATOM   5871  C  C   . LEU A 1 764  ? 115.980 82.450  143.501 1.00 49.46  ? 764  LEU A C   1 
ATOM   5872  O  O   . LEU A 1 764  ? 117.144 82.801  143.639 1.00 50.10  ? 764  LEU A O   1 
ATOM   5873  C  CB  . LEU A 1 764  ? 114.044 84.119  143.340 1.00 48.73  ? 764  LEU A CB  1 
ATOM   5874  C  CG  . LEU A 1 764  ? 114.540 85.519  143.036 1.00 49.31  ? 764  LEU A CG  1 
ATOM   5875  C  CD1 . LEU A 1 764  ? 115.613 85.441  141.957 1.00 51.01  ? 764  LEU A CD1 1 
ATOM   5876  C  CD2 . LEU A 1 764  ? 113.353 86.347  142.583 1.00 47.77  ? 764  LEU A CD2 1 
ATOM   5877  N  N   . GLU A 1 765  ? 115.610 81.426  142.750 1.00 49.55  ? 765  GLU A N   1 
ATOM   5878  C  CA  . GLU A 1 765  ? 116.552 80.584  142.051 1.00 50.35  ? 765  GLU A CA  1 
ATOM   5879  C  C   . GLU A 1 765  ? 116.064 80.554  140.615 1.00 49.55  ? 765  GLU A C   1 
ATOM   5880  O  O   . GLU A 1 765  ? 115.058 79.923  140.301 1.00 49.33  ? 765  GLU A O   1 
ATOM   5881  C  CB  . GLU A 1 765  ? 116.568 79.179  142.678 1.00 51.02  ? 765  GLU A CB  1 
ATOM   5882  C  CG  . GLU A 1 765  ? 117.655 78.229  142.156 1.00 53.30  ? 765  GLU A CG  1 
ATOM   5883  C  CD  . GLU A 1 765  ? 119.051 78.497  142.734 1.00 57.01  ? 765  GLU A CD  1 
ATOM   5884  O  OE1 . GLU A 1 765  ? 119.169 78.990  143.885 1.00 58.10  ? 765  GLU A OE1 1 
ATOM   5885  O  OE2 . GLU A 1 765  ? 120.042 78.195  142.029 1.00 58.10  ? 765  GLU A OE2 1 
ATOM   5886  N  N   . LYS A 1 766  ? 116.760 81.280  139.751 1.00 49.48  ? 766  LYS A N   1 
ATOM   5887  C  CA  . LYS A 1 766  ? 116.334 81.426  138.369 1.00 48.78  ? 766  LYS A CA  1 
ATOM   5888  C  C   . LYS A 1 766  ? 117.448 81.066  137.410 1.00 49.23  ? 766  LYS A C   1 
ATOM   5889  O  O   . LYS A 1 766  ? 118.513 80.594  137.822 1.00 50.45  ? 766  LYS A O   1 
ATOM   5890  C  CB  . LYS A 1 766  ? 115.831 82.845  138.105 1.00 48.25  ? 766  LYS A CB  1 
ATOM   5891  C  CG  . LYS A 1 766  ? 114.632 83.274  138.938 1.00 47.97  ? 766  LYS A CG  1 
ATOM   5892  C  CD  . LYS A 1 766  ? 113.419 82.379  138.719 1.00 47.21  ? 766  LYS A CD  1 
ATOM   5893  C  CE  . LYS A 1 766  ? 112.199 82.947  139.423 1.00 46.89  ? 766  LYS A CE  1 
ATOM   5894  N  NZ  . LYS A 1 766  ? 111.059 82.007  139.406 1.00 47.59  ? 766  LYS A NZ  1 
ATOM   5895  N  N   . VAL A 1 767  ? 117.207 81.304  136.127 1.00 49.03  ? 767  VAL A N   1 
ATOM   5896  C  CA  . VAL A 1 767  ? 118.077 80.788  135.079 1.00 49.32  ? 767  VAL A CA  1 
ATOM   5897  C  C   . VAL A 1 767  ? 118.257 81.795  133.959 1.00 49.02  ? 767  VAL A C   1 
ATOM   5898  O  O   . VAL A 1 767  ? 117.293 82.421  133.511 1.00 48.54  ? 767  VAL A O   1 
ATOM   5899  C  CB  . VAL A 1 767  ? 117.503 79.458  134.501 1.00 49.04  ? 767  VAL A CB  1 
ATOM   5900  C  CG1 . VAL A 1 767  ? 118.138 79.112  133.186 1.00 49.27  ? 767  VAL A CG1 1 
ATOM   5901  C  CG2 . VAL A 1 767  ? 117.710 78.317  135.486 1.00 49.54  ? 767  VAL A CG2 1 
ATOM   5902  N  N   . ILE A 1 768  ? 119.505 81.957  133.531 1.00 49.43  ? 768  ILE A N   1 
ATOM   5903  C  CA  . ILE A 1 768  ? 119.819 82.617  132.268 1.00 49.32  ? 768  ILE A CA  1 
ATOM   5904  C  C   . ILE A 1 768  ? 120.656 81.644  131.434 1.00 50.37  ? 768  ILE A C   1 
ATOM   5905  O  O   . ILE A 1 768  ? 121.569 81.004  131.956 1.00 51.26  ? 768  ILE A O   1 
ATOM   5906  C  CB  . ILE A 1 768  ? 120.569 83.959  132.483 1.00 49.08  ? 768  ILE A CB  1 
ATOM   5907  C  CG1 . ILE A 1 768  ? 119.665 84.973  133.180 1.00 48.01  ? 768  ILE A CG1 1 
ATOM   5908  C  CG2 . ILE A 1 768  ? 121.033 84.537  131.166 1.00 48.75  ? 768  ILE A CG2 1 
ATOM   5909  C  CD1 . ILE A 1 768  ? 120.379 86.199  133.665 1.00 47.53  ? 768  ILE A CD1 1 
ATOM   5910  N  N   . ARG A 1 769  ? 120.337 81.513  130.151 1.00 50.66  ? 769  ARG A N   1 
ATOM   5911  C  CA  . ARG A 1 769  ? 121.127 80.662  129.267 1.00 51.92  ? 769  ARG A CA  1 
ATOM   5912  C  C   . ARG A 1 769  ? 122.315 81.407  128.679 1.00 52.49  ? 769  ARG A C   1 
ATOM   5913  O  O   . ARG A 1 769  ? 122.152 82.420  128.008 1.00 52.05  ? 769  ARG A O   1 
ATOM   5914  C  CB  . ARG A 1 769  ? 120.255 80.048  128.164 1.00 51.62  ? 769  ARG A CB  1 
ATOM   5915  C  CG  . ARG A 1 769  ? 119.536 78.798  128.624 1.00 52.75  ? 769  ARG A CG  1 
ATOM   5916  C  CD  . ARG A 1 769  ? 118.218 78.623  127.919 1.00 55.16  ? 769  ARG A CD  1 
ATOM   5917  N  NE  . ARG A 1 769  ? 117.203 77.978  128.762 1.00 58.17  ? 769  ARG A NE  1 
ATOM   5918  C  CZ  . ARG A 1 769  ? 116.440 78.607  129.664 1.00 59.04  ? 769  ARG A CZ  1 
ATOM   5919  N  NH1 . ARG A 1 769  ? 116.566 79.922  129.876 1.00 59.20  ? 769  ARG A NH1 1 
ATOM   5920  N  NH2 . ARG A 1 769  ? 115.548 77.916  130.368 1.00 58.47  ? 769  ARG A NH2 1 
ATOM   5921  N  N   . VAL A 1 770  ? 123.513 80.904  128.946 1.00 53.86  ? 770  VAL A N   1 
ATOM   5922  C  CA  . VAL A 1 770  ? 124.721 81.489  128.385 1.00 55.33  ? 770  VAL A CA  1 
ATOM   5923  C  C   . VAL A 1 770  ? 125.080 80.734  127.118 1.00 56.51  ? 770  VAL A C   1 
ATOM   5924  O  O   . VAL A 1 770  ? 125.183 79.507  127.127 1.00 57.09  ? 770  VAL A O   1 
ATOM   5925  C  CB  . VAL A 1 770  ? 125.891 81.475  129.387 1.00 55.98  ? 770  VAL A CB  1 
ATOM   5926  C  CG1 . VAL A 1 770  ? 127.130 82.140  128.784 1.00 56.28  ? 770  VAL A CG1 1 
ATOM   5927  C  CG2 . VAL A 1 770  ? 125.486 82.176  130.668 1.00 55.39  ? 770  VAL A CG2 1 
ATOM   5928  N  N   . MET A 1 771  ? 125.266 81.478  126.033 1.00 57.57  ? 771  MET A N   1 
ATOM   5929  C  CA  . MET A 1 771  ? 125.412 80.889  124.702 1.00 58.93  ? 771  MET A CA  1 
ATOM   5930  C  C   . MET A 1 771  ? 126.734 81.258  124.025 1.00 60.11  ? 771  MET A C   1 
ATOM   5931  O  O   . MET A 1 771  ? 127.400 82.213  124.435 1.00 60.58  ? 771  MET A O   1 
ATOM   5932  C  CB  . MET A 1 771  ? 124.219 81.276  123.821 1.00 58.09  ? 771  MET A CB  1 
ATOM   5933  C  CG  . MET A 1 771  ? 122.894 81.087  124.528 1.00 59.49  ? 771  MET A CG  1 
ATOM   5934  S  SD  . MET A 1 771  ? 121.511 80.561  123.510 1.00 64.40  ? 771  MET A SD  1 
ATOM   5935  C  CE  . MET A 1 771  ? 121.450 81.860  122.258 1.00 63.24  ? 771  MET A CE  1 
ATOM   5936  N  N   . PRO A 1 772  ? 127.136 80.482  123.005 1.00 92.23  ? 772  PRO A N   1 
ATOM   5937  C  CA  . PRO A 1 772  ? 128.300 80.851  122.206 1.00 94.56  ? 772  PRO A CA  1 
ATOM   5938  C  C   . PRO A 1 772  ? 127.931 81.840  121.100 1.00 95.35  ? 772  PRO A C   1 
ATOM   5939  O  O   . PRO A 1 772  ? 126.743 82.039  120.828 1.00 93.44  ? 772  PRO A O   1 
ATOM   5940  C  CB  . PRO A 1 772  ? 128.716 79.517  121.589 1.00 92.09  ? 772  PRO A CB  1 
ATOM   5941  C  CG  . PRO A 1 772  ? 127.432 78.764  121.448 1.00 87.96  ? 772  PRO A CG  1 
ATOM   5942  C  CD  . PRO A 1 772  ? 126.541 79.203  122.564 1.00 88.36  ? 772  PRO A CD  1 
ATOM   5943  N  N   . GLU A 1 773  ? 128.944 82.444  120.474 1.00 98.58  ? 773  GLU A N   1 
ATOM   5944  C  CA  . GLU A 1 773  ? 128.768 83.276  119.274 1.00 99.70  ? 773  GLU A CA  1 
ATOM   5945  C  C   . GLU A 1 773  ? 127.955 82.572  118.180 1.00 96.35  ? 773  GLU A C   1 
ATOM   5946  O  O   . GLU A 1 773  ? 126.885 83.045  117.781 1.00 95.25  ? 773  GLU A O   1 
ATOM   5947  C  CB  . GLU A 1 773  ? 130.133 83.664  118.705 1.00 102.69 ? 773  GLU A CB  1 
ATOM   5948  C  CG  . GLU A 1 773  ? 130.793 84.861  119.375 1.00 107.91 ? 773  GLU A CG  1 
ATOM   5949  C  CD  . GLU A 1 773  ? 130.814 86.118  118.508 1.00 110.64 ? 773  GLU A CD  1 
ATOM   5950  O  OE1 . GLU A 1 773  ? 130.078 86.180  117.494 1.00 108.94 ? 773  GLU A OE1 1 
ATOM   5951  O  OE2 . GLU A 1 773  ? 131.579 87.050  118.848 1.00 114.62 ? 773  GLU A OE2 1 
ATOM   5952  N  N   . SER A 1 774  ? 128.476 81.440  117.707 1.00 95.12  ? 774  SER A N   1 
ATOM   5953  C  CA  . SER A 1 774  ? 127.871 80.692  116.611 1.00 92.30  ? 774  SER A CA  1 
ATOM   5954  C  C   . SER A 1 774  ? 127.026 79.544  117.131 1.00 89.33  ? 774  SER A C   1 
ATOM   5955  O  O   . SER A 1 774  ? 127.442 78.847  118.058 1.00 89.58  ? 774  SER A O   1 
ATOM   5956  C  CB  . SER A 1 774  ? 128.966 80.135  115.697 1.00 92.59  ? 774  SER A CB  1 
ATOM   5957  O  OG  . SER A 1 774  ? 128.573 78.898  115.114 1.00 89.47  ? 774  SER A OG  1 
ATOM   5958  N  N   . LEU A 1 775  ? 125.853 79.333  116.531 1.00 87.00  ? 775  LEU A N   1 
ATOM   5959  C  CA  . LEU A 1 775  ? 125.077 78.135  116.838 1.00 84.36  ? 775  LEU A CA  1 
ATOM   5960  C  C   . LEU A 1 775  ? 125.986 76.944  116.569 1.00 83.60  ? 775  LEU A C   1 
ATOM   5961  O  O   . LEU A 1 775  ? 126.235 76.580  115.407 1.00 82.75  ? 775  LEU A O   1 
ATOM   5962  C  CB  . LEU A 1 775  ? 123.790 78.033  116.006 1.00 81.98  ? 775  LEU A CB  1 
ATOM   5963  C  CG  . LEU A 1 775  ? 123.025 76.690  116.038 1.00 79.53  ? 775  LEU A CG  1 
ATOM   5964  C  CD1 . LEU A 1 775  ? 122.189 76.494  117.317 1.00 79.54  ? 775  LEU A CD1 1 
ATOM   5965  C  CD2 . LEU A 1 775  ? 122.155 76.513  114.791 1.00 77.93  ? 775  LEU A CD2 1 
ATOM   5966  N  N   . VAL A 1 776  ? 126.512 76.381  117.658 1.00 84.23  ? 776  VAL A N   1 
ATOM   5967  C  CA  . VAL A 1 776  ? 127.392 75.211  117.602 1.00 83.34  ? 776  VAL A CA  1 
ATOM   5968  C  C   . VAL A 1 776  ? 126.655 74.053  116.938 1.00 79.38  ? 776  VAL A C   1 
ATOM   5969  O  O   . VAL A 1 776  ? 125.489 73.785  117.252 1.00 77.57  ? 776  VAL A O   1 
ATOM   5970  C  CB  . VAL A 1 776  ? 127.932 74.802  119.014 1.00 85.07  ? 776  VAL A CB  1 
ATOM   5971  C  CG1 . VAL A 1 776  ? 128.796 75.922  119.615 1.00 88.32  ? 776  VAL A CG1 1 
ATOM   5972  C  CG2 . VAL A 1 776  ? 126.792 74.408  119.971 1.00 83.82  ? 776  VAL A CG2 1 
ATOM   5973  N  N   . GLN A 1 777  ? 127.326 73.404  115.993 1.00 78.02  ? 777  GLN A N   1 
ATOM   5974  C  CA  . GLN A 1 777  ? 126.746 72.273  115.278 1.00 74.35  ? 777  GLN A CA  1 
ATOM   5975  C  C   . GLN A 1 777  ? 127.491 70.996  115.662 1.00 73.08  ? 777  GLN A C   1 
ATOM   5976  O  O   . GLN A 1 777  ? 128.537 70.686  115.077 1.00 73.96  ? 777  GLN A O   1 
ATOM   5977  C  CB  . GLN A 1 777  ? 126.804 72.498  113.765 1.00 74.16  ? 777  GLN A CB  1 
ATOM   5978  C  CG  . GLN A 1 777  ? 126.105 73.770  113.277 1.00 75.89  ? 777  GLN A CG  1 
ATOM   5979  C  CD  . GLN A 1 777  ? 125.592 73.641  111.840 1.00 76.34  ? 777  GLN A CD  1 
ATOM   5980  O  OE1 . GLN A 1 777  ? 125.943 74.449  110.966 1.00 77.55  ? 777  GLN A OE1 1 
ATOM   5981  N  NE2 . GLN A 1 777  ? 124.761 72.616  111.589 1.00 73.40  ? 777  GLN A NE2 1 
ATOM   5982  N  N   . PRO A 1 778  ? 126.965 70.258  116.659 1.00 71.01  ? 778  PRO A N   1 
ATOM   5983  C  CA  . PRO A 1 778  ? 127.653 69.075  117.164 1.00 70.28  ? 778  PRO A CA  1 
ATOM   5984  C  C   . PRO A 1 778  ? 127.737 67.956  116.126 1.00 67.61  ? 778  PRO A C   1 
ATOM   5985  O  O   . PRO A 1 778  ? 126.780 67.711  115.385 1.00 65.40  ? 778  PRO A O   1 
ATOM   5986  C  CB  . PRO A 1 778  ? 126.788 68.646  118.352 1.00 69.68  ? 778  PRO A CB  1 
ATOM   5987  C  CG  . PRO A 1 778  ? 125.439 69.191  118.055 1.00 68.32  ? 778  PRO A CG  1 
ATOM   5988  C  CD  . PRO A 1 778  ? 125.690 70.491  117.363 1.00 69.95  ? 778  PRO A CD  1 
ATOM   5989  N  N   . ARG A 1 779  ? 128.895 67.312  116.064 1.00 67.57  ? 779  ARG A N   1 
ATOM   5990  C  CA  . ARG A 1 779  ? 129.078 66.140  115.236 1.00 65.26  ? 779  ARG A CA  1 
ATOM   5991  C  C   . ARG A 1 779  ? 129.229 64.936  116.147 1.00 63.89  ? 779  ARG A C   1 
ATOM   5992  O  O   . ARG A 1 779  ? 129.950 64.994  117.139 1.00 65.77  ? 779  ARG A O   1 
ATOM   5993  C  CB  . ARG A 1 779  ? 130.311 66.289  114.337 1.00 67.25  ? 779  ARG A CB  1 
ATOM   5994  C  CG  . ARG A 1 779  ? 130.439 65.177  113.269 1.00 68.30  ? 779  ARG A CG  1 
ATOM   5995  C  CD  . ARG A 1 779  ? 131.353 65.578  112.109 1.00 72.54  ? 779  ARG A CD  1 
ATOM   5996  N  NE  . ARG A 1 779  ? 132.742 65.782  112.532 1.00 77.52  ? 779  ARG A NE  1 
ATOM   5997  C  CZ  . ARG A 1 779  ? 133.722 64.899  112.350 1.00 79.93  ? 779  ARG A CZ  1 
ATOM   5998  N  NH1 . ARG A 1 779  ? 133.478 63.738  111.746 1.00 78.82  ? 779  ARG A NH1 1 
ATOM   5999  N  NH2 . ARG A 1 779  ? 134.954 65.178  112.767 1.00 82.91  ? 779  ARG A NH2 1 
ATOM   6000  N  N   . MET A 1 780  ? 128.534 63.852  115.826 1.00 60.28  ? 780  MET A N   1 
ATOM   6001  C  CA  . MET A 1 780  ? 128.763 62.609  116.540 1.00 59.07  ? 780  MET A CA  1 
ATOM   6002  C  C   . MET A 1 780  ? 129.283 61.528  115.615 1.00 57.83  ? 780  MET A C   1 
ATOM   6003  O  O   . MET A 1 780  ? 128.674 61.212  114.599 1.00 55.59  ? 780  MET A O   1 
ATOM   6004  C  CB  . MET A 1 780  ? 127.521 62.142  117.293 1.00 57.56  ? 780  MET A CB  1 
ATOM   6005  C  CG  . MET A 1 780  ? 127.782 60.924  118.163 1.00 57.34  ? 780  MET A CG  1 
ATOM   6006  S  SD  . MET A 1 780  ? 126.359 60.387  119.126 1.00 55.32  ? 780  MET A SD  1 
ATOM   6007  C  CE  . MET A 1 780  ? 125.160 59.980  117.869 1.00 51.48  ? 780  MET A CE  1 
ATOM   6008  N  N   . ASP A 1 781  ? 130.440 60.988  115.968 1.00 59.03  ? 781  ASP A N   1 
ATOM   6009  C  CA  . ASP A 1 781  ? 130.979 59.820  115.300 1.00 58.30  ? 781  ASP A CA  1 
ATOM   6010  C  C   . ASP A 1 781  ? 130.592 58.603  116.120 1.00 57.64  ? 781  ASP A C   1 
ATOM   6011  O  O   . ASP A 1 781  ? 130.862 58.549  117.321 1.00 59.36  ? 781  ASP A O   1 
ATOM   6012  C  CB  . ASP A 1 781  ? 132.498 59.915  115.213 1.00 60.90  ? 781  ASP A CB  1 
ATOM   6013  C  CG  . ASP A 1 781  ? 132.968 60.981  114.247 1.00 61.61  ? 781  ASP A CG  1 
ATOM   6014  O  OD1 . ASP A 1 781  ? 132.169 61.464  113.417 1.00 59.10  ? 781  ASP A OD1 1 
ATOM   6015  O  OD2 . ASP A 1 781  ? 134.164 61.331  114.319 1.00 65.81  ? 781  ASP A OD2 1 
ATOM   6016  N  N   . THR A 1 782  ? 129.947 57.630  115.494 1.00 55.27  ? 782  THR A N   1 
ATOM   6017  C  CA  . THR A 1 782  ? 129.633 56.402  116.215 1.00 54.95  ? 782  THR A CA  1 
ATOM   6018  C  C   . THR A 1 782  ? 129.999 55.124  115.481 1.00 55.18  ? 782  THR A C   1 
ATOM   6019  O  O   . THR A 1 782  ? 129.897 55.028  114.259 1.00 54.11  ? 782  THR A O   1 
ATOM   6020  C  CB  . THR A 1 782  ? 128.182 56.381  116.788 1.00 53.19  ? 782  THR A CB  1 
ATOM   6021  O  OG1 . THR A 1 782  ? 127.554 55.122  116.519 1.00 50.99  ? 782  THR A OG1 1 
ATOM   6022  C  CG2 . THR A 1 782  ? 127.360 57.482  116.209 1.00 50.71  ? 782  THR A CG2 1 
ATOM   6023  N  N   . ARG A 1 783  ? 130.466 54.158  116.261 1.00 57.00  ? 783  ARG A N   1 
ATOM   6024  C  CA  . ARG A 1 783  ? 130.762 52.822  115.780 1.00 57.97  ? 783  ARG A CA  1 
ATOM   6025  C  C   . ARG A 1 783  ? 130.070 51.833  116.698 1.00 57.94  ? 783  ARG A C   1 
ATOM   6026  O  O   . ARG A 1 783  ? 130.091 51.998  117.910 1.00 59.55  ? 783  ARG A O   1 
ATOM   6027  C  CB  . ARG A 1 783  ? 132.282 52.575  115.737 1.00 60.65  ? 783  ARG A CB  1 
ATOM   6028  C  CG  . ARG A 1 783  ? 133.000 53.382  114.632 1.00 62.80  ? 783  ARG A CG  1 
ATOM   6029  C  CD  . ARG A 1 783  ? 133.988 52.535  113.818 1.00 67.38  ? 783  ARG A CD  1 
ATOM   6030  N  NE  . ARG A 1 783  ? 135.362 52.643  114.324 1.00 73.19  ? 783  ARG A NE  1 
ATOM   6031  C  CZ  . ARG A 1 783  ? 136.328 51.743  114.115 1.00 76.03  ? 783  ARG A CZ  1 
ATOM   6032  N  NH1 . ARG A 1 783  ? 136.087 50.638  113.414 1.00 75.19  ? 783  ARG A NH1 1 
ATOM   6033  N  NH2 . ARG A 1 783  ? 137.543 51.942  114.625 1.00 79.77  ? 783  ARG A NH2 1 
ATOM   6034  N  N   . PHE A 1 784  ? 129.428 50.824  116.128 1.00 56.95  ? 784  PHE A N   1 
ATOM   6035  C  CA  . PHE A 1 784  ? 128.813 49.789  116.949 1.00 57.78  ? 784  PHE A CA  1 
ATOM   6036  C  C   . PHE A 1 784  ? 129.567 48.456  116.866 1.00 60.00  ? 784  PHE A C   1 
ATOM   6037  O  O   . PHE A 1 784  ? 130.311 48.204  115.923 1.00 60.12  ? 784  PHE A O   1 
ATOM   6038  C  CB  . PHE A 1 784  ? 127.321 49.621  116.621 1.00 55.27  ? 784  PHE A CB  1 
ATOM   6039  C  CG  . PHE A 1 784  ? 127.035 48.649  115.510 1.00 54.72  ? 784  PHE A CG  1 
ATOM   6040  C  CD1 . PHE A 1 784  ? 126.904 49.090  114.192 1.00 52.74  ? 784  PHE A CD1 1 
ATOM   6041  C  CD2 . PHE A 1 784  ? 126.869 47.285  115.777 1.00 56.18  ? 784  PHE A CD2 1 
ATOM   6042  C  CE1 . PHE A 1 784  ? 126.621 48.186  113.151 1.00 50.97  ? 784  PHE A CE1 1 
ATOM   6043  C  CE2 . PHE A 1 784  ? 126.590 46.376  114.741 1.00 54.89  ? 784  PHE A CE2 1 
ATOM   6044  C  CZ  . PHE A 1 784  ? 126.463 46.835  113.428 1.00 51.89  ? 784  PHE A CZ  1 
ATOM   6045  N  N   . PHE A 1 785  ? 129.376 47.620  117.880 1.00 61.99  ? 785  PHE A N   1 
ATOM   6046  C  CA  . PHE A 1 785  ? 129.873 46.257  117.857 1.00 64.30  ? 785  PHE A CA  1 
ATOM   6047  C  C   . PHE A 1 785  ? 128.747 45.317  118.236 1.00 64.68  ? 785  PHE A C   1 
ATOM   6048  O  O   . PHE A 1 785  ? 127.865 45.670  119.019 1.00 64.22  ? 785  PHE A O   1 
ATOM   6049  C  CB  . PHE A 1 785  ? 131.083 46.081  118.785 1.00 67.41  ? 785  PHE A CB  1 
ATOM   6050  C  CG  . PHE A 1 785  ? 130.825 46.462  120.219 1.00 68.49  ? 785  PHE A CG  1 
ATOM   6051  C  CD1 . PHE A 1 785  ? 130.962 47.783  120.639 1.00 67.94  ? 785  PHE A CD1 1 
ATOM   6052  C  CD2 . PHE A 1 785  ? 130.465 45.498  121.153 1.00 70.35  ? 785  PHE A CD2 1 
ATOM   6053  C  CE1 . PHE A 1 785  ? 130.728 48.137  121.956 1.00 69.52  ? 785  PHE A CE1 1 
ATOM   6054  C  CE2 . PHE A 1 785  ? 130.231 45.839  122.477 1.00 71.88  ? 785  PHE A CE2 1 
ATOM   6055  C  CZ  . PHE A 1 785  ? 130.365 47.161  122.881 1.00 71.68  ? 785  PHE A CZ  1 
ATOM   6056  N  N   . CYS A 1 786  ? 128.772 44.128  117.653 1.00 66.06  ? 786  CYS A N   1 
ATOM   6057  C  CA  . CYS A 1 786  ? 127.798 43.097  117.960 1.00 67.31  ? 786  CYS A CA  1 
ATOM   6058  C  C   . CYS A 1 786  ? 128.528 41.754  118.004 1.00 70.91  ? 786  CYS A C   1 
ATOM   6059  O  O   . CYS A 1 786  ? 128.818 41.152  116.961 1.00 70.86  ? 786  CYS A O   1 
ATOM   6060  C  CB  . CYS A 1 786  ? 126.682 43.098  116.915 1.00 64.69  ? 786  CYS A CB  1 
ATOM   6061  S  SG  . CYS A 1 786  ? 125.311 42.012  117.306 1.00 64.13  ? 786  CYS A SG  1 
ATOM   6062  N  N   . PHE A 1 787  ? 128.843 41.311  119.221 1.00 74.49  ? 787  PHE A N   1 
ATOM   6063  C  CA  . PHE A 1 787  ? 129.648 40.111  119.440 1.00 78.52  ? 787  PHE A CA  1 
ATOM   6064  C  C   . PHE A 1 787  ? 128.794 38.926  119.871 1.00 81.04  ? 787  PHE A C   1 
ATOM   6065  O  O   . PHE A 1 787  ? 128.199 38.949  120.950 1.00 81.98  ? 787  PHE A O   1 
ATOM   6066  C  CB  . PHE A 1 787  ? 130.726 40.360  120.505 1.00 80.76  ? 787  PHE A CB  1 
ATOM   6067  C  CG  . PHE A 1 787  ? 131.819 41.315  120.083 1.00 79.56  ? 787  PHE A CG  1 
ATOM   6068  C  CD1 . PHE A 1 787  ? 132.715 41.812  121.036 1.00 80.61  ? 787  PHE A CD1 1 
ATOM   6069  C  CD2 . PHE A 1 787  ? 131.959 41.722  118.752 1.00 75.90  ? 787  PHE A CD2 1 
ATOM   6070  C  CE1 . PHE A 1 787  ? 133.737 42.690  120.671 1.00 79.89  ? 787  PHE A CE1 1 
ATOM   6071  C  CE2 . PHE A 1 787  ? 132.973 42.604  118.374 1.00 75.09  ? 787  PHE A CE2 1 
ATOM   6072  C  CZ  . PHE A 1 787  ? 133.863 43.091  119.335 1.00 77.88  ? 787  PHE A CZ  1 
ATOM   6073  N  N   . ASP A 1 788  ? 128.747 37.893  119.031 1.00 83.01  ? 788  ASP A N   1 
ATOM   6074  C  CA  . ASP A 1 788  ? 128.051 36.644  119.355 1.00 86.38  ? 788  ASP A CA  1 
ATOM   6075  C  C   . ASP A 1 788  ? 128.889 35.724  120.237 1.00 91.07  ? 788  ASP A C   1 
ATOM   6076  O  O   . ASP A 1 788  ? 128.455 35.340  121.321 1.00 93.16  ? 788  ASP A O   1 
ATOM   6077  C  CB  . ASP A 1 788  ? 127.622 35.914  118.082 1.00 85.80  ? 788  ASP A CB  1 
ATOM   6078  C  CG  . ASP A 1 788  ? 126.317 36.436  117.531 1.00 83.92  ? 788  ASP A CG  1 
ATOM   6079  O  OD1 . ASP A 1 788  ? 125.325 36.470  118.294 1.00 85.66  ? 788  ASP A OD1 1 
ATOM   6080  O  OD2 . ASP A 1 788  ? 126.280 36.812  116.339 1.00 82.59  ? 788  ASP A OD2 1 
ATOM   6081  N  N   . ASP A 1 789  ? 130.079 35.367  119.761 1.00 93.48  ? 789  ASP A N   1 
ATOM   6082  C  CA  . ASP A 1 789  ? 131.039 34.604  120.555 1.00 98.41  ? 789  ASP A CA  1 
ATOM   6083  C  C   . ASP A 1 789  ? 131.939 35.584  121.298 1.00 99.56  ? 789  ASP A C   1 
ATOM   6084  O  O   . ASP A 1 789  ? 131.996 36.764  120.936 1.00 97.07  ? 789  ASP A O   1 
ATOM   6085  C  CB  . ASP A 1 789  ? 131.881 33.704  119.651 1.00 99.99  ? 789  ASP A CB  1 
ATOM   6086  C  CG  . ASP A 1 789  ? 131.055 32.643  118.944 1.00 100.52 ? 789  ASP A CG  1 
ATOM   6087  O  OD1 . ASP A 1 789  ? 130.040 32.988  118.299 1.00 97.60  ? 789  ASP A OD1 1 
ATOM   6088  O  OD2 . ASP A 1 789  ? 131.434 31.456  119.026 1.00 104.75 ? 789  ASP A OD2 1 
ATOM   6089  N  N   . HIS A 1 790  ? 132.631 35.105  122.333 1.00 103.98 ? 790  HIS A N   1 
ATOM   6090  C  CA  . HIS A 1 790  ? 133.566 35.947  123.087 1.00 105.78 ? 790  HIS A CA  1 
ATOM   6091  C  C   . HIS A 1 790  ? 134.602 36.570  122.151 1.00 105.12 ? 790  HIS A C   1 
ATOM   6092  O  O   . HIS A 1 790  ? 135.373 35.854  121.501 1.00 106.73 ? 790  HIS A O   1 
ATOM   6093  C  CB  . HIS A 1 790  ? 134.246 35.157  124.212 1.00 110.38 ? 790  HIS A CB  1 
ATOM   6094  C  CG  . HIS A 1 790  ? 133.759 35.513  125.585 1.00 112.05 ? 790  HIS A CG  1 
ATOM   6095  N  ND1 . HIS A 1 790  ? 132.762 34.812  126.229 1.00 113.56 ? 790  HIS A ND1 1 
ATOM   6096  C  CD2 . HIS A 1 790  ? 134.140 36.494  126.439 1.00 112.84 ? 790  HIS A CD2 1 
ATOM   6097  C  CE1 . HIS A 1 790  ? 132.546 35.348  127.418 1.00 114.83 ? 790  HIS A CE1 1 
ATOM   6098  N  NE2 . HIS A 1 790  ? 133.369 36.370  127.570 1.00 114.25 ? 790  HIS A NE2 1 
ATOM   6099  N  N   . LYS A 1 791  ? 134.592 37.900  122.064 1.00 103.08 ? 791  LYS A N   1 
ATOM   6100  C  CA  . LYS A 1 791  ? 135.500 38.618  121.168 1.00 102.53 ? 791  LYS A CA  1 
ATOM   6101  C  C   . LYS A 1 791  ? 136.268 39.740  121.853 1.00 103.56 ? 791  LYS A C   1 
ATOM   6102  O  O   . LYS A 1 791  ? 135.765 40.388  122.773 1.00 103.05 ? 791  LYS A O   1 
ATOM   6103  C  CB  . LYS A 1 791  ? 134.754 39.171  119.949 1.00 98.58  ? 791  LYS A CB  1 
ATOM   6104  C  CG  . LYS A 1 791  ? 134.360 38.124  118.917 1.00 98.49  ? 791  LYS A CG  1 
ATOM   6105  C  CD  . LYS A 1 791  ? 134.045 38.744  117.563 1.00 95.19  ? 791  LYS A CD  1 
ATOM   6106  C  CE  . LYS A 1 791  ? 133.573 37.675  116.588 1.00 95.71  ? 791  LYS A CE  1 
ATOM   6107  N  NZ  . LYS A 1 791  ? 133.508 38.152  115.179 1.00 93.20  ? 791  LYS A NZ  1 
ATOM   6108  N  N   . ASN A 1 792  ? 137.503 39.933  121.395 1.00 105.45 ? 792  ASN A N   1 
ATOM   6109  C  CA  . ASN A 1 792  ? 138.333 41.081  121.749 1.00 106.49 ? 792  ASN A CA  1 
ATOM   6110  C  C   . ASN A 1 792  ? 138.526 41.935  120.498 1.00 104.15 ? 792  ASN A C   1 
ATOM   6111  O  O   . ASN A 1 792  ? 138.869 41.410  119.432 1.00 104.03 ? 792  ASN A O   1 
ATOM   6112  C  CB  . ASN A 1 792  ? 139.704 40.632  122.280 1.00 110.68 ? 792  ASN A CB  1 
ATOM   6113  C  CG  . ASN A 1 792  ? 139.653 40.106  123.710 1.00 114.09 ? 792  ASN A CG  1 
ATOM   6114  O  OD1 . ASN A 1 792  ? 138.871 40.579  124.536 1.00 113.21 ? 792  ASN A OD1 1 
ATOM   6115  N  ND2 . ASN A 1 792  ? 140.516 39.130  124.014 1.00 118.28 ? 792  ASN A ND2 1 
ATOM   6116  N  N   . GLN A 1 793  ? 138.289 43.239  120.615 1.00 102.55 ? 793  GLN A N   1 
ATOM   6117  C  CA  . GLN A 1 793  ? 138.520 44.153  119.496 1.00 100.76 ? 793  GLN A CA  1 
ATOM   6118  C  C   . GLN A 1 793  ? 138.986 45.525  119.963 1.00 101.29 ? 793  GLN A C   1 
ATOM   6119  O  O   . GLN A 1 793  ? 138.555 46.022  121.007 1.00 101.17 ? 793  GLN A O   1 
ATOM   6120  C  CB  . GLN A 1 793  ? 137.279 44.279  118.602 1.00 96.82  ? 793  GLN A CB  1 
ATOM   6121  C  CG  . GLN A 1 793  ? 137.631 44.387  117.122 1.00 95.43  ? 793  GLN A CG  1 
ATOM   6122  C  CD  . GLN A 1 793  ? 136.509 44.939  116.256 1.00 90.81  ? 793  GLN A CD  1 
ATOM   6123  O  OE1 . GLN A 1 793  ? 135.350 44.539  116.372 1.00 88.73  ? 793  GLN A OE1 1 
ATOM   6124  N  NE2 . GLN A 1 793  ? 136.861 45.853  115.365 1.00 89.25  ? 793  GLN A NE2 1 
ATOM   6125  N  N   . THR A 1 794  ? 139.870 46.125  119.171 1.00 102.18 ? 794  THR A N   1 
ATOM   6126  C  CA  . THR A 1 794  ? 140.455 47.422  119.495 1.00 103.53 ? 794  THR A CA  1 
ATOM   6127  C  C   . THR A 1 794  ? 140.141 48.472  118.418 1.00 101.14 ? 794  THR A C   1 
ATOM   6128  O  O   . THR A 1 794  ? 140.623 48.392  117.287 1.00 101.03 ? 794  THR A O   1 
ATOM   6129  C  CB  . THR A 1 794  ? 141.988 47.307  119.814 1.00 107.64 ? 794  THR A CB  1 
ATOM   6130  O  OG1 . THR A 1 794  ? 142.571 48.612  119.931 1.00 108.26 ? 794  THR A OG1 1 
ATOM   6131  C  CG2 . THR A 1 794  ? 142.736 46.493  118.751 1.00 109.08 ? 794  THR A CG2 1 
ATOM   6132  N  N   . PHE A 1 795  ? 139.308 49.443  118.792 1.00 99.68  ? 795  PHE A N   1 
ATOM   6133  C  CA  . PHE A 1 795  ? 138.885 50.523  117.903 1.00 97.58  ? 795  PHE A CA  1 
ATOM   6134  C  C   . PHE A 1 795  ? 139.739 51.771  118.139 1.00 99.89  ? 795  PHE A C   1 
ATOM   6135  O  O   . PHE A 1 795  ? 139.673 52.374  119.218 1.00 100.80 ? 795  PHE A O   1 
ATOM   6136  C  CB  . PHE A 1 795  ? 137.412 50.876  118.142 1.00 94.31  ? 795  PHE A CB  1 
ATOM   6137  C  CG  . PHE A 1 795  ? 136.463 49.717  117.984 1.00 92.26  ? 795  PHE A CG  1 
ATOM   6138  C  CD1 . PHE A 1 795  ? 135.717 49.571  116.823 1.00 88.68  ? 795  PHE A CD1 1 
ATOM   6139  C  CD2 . PHE A 1 795  ? 136.297 48.785  119.005 1.00 93.48  ? 795  PHE A CD2 1 
ATOM   6140  C  CE1 . PHE A 1 795  ? 134.830 48.511  116.671 1.00 87.10  ? 795  PHE A CE1 1 
ATOM   6141  C  CE2 . PHE A 1 795  ? 135.414 47.718  118.858 1.00 92.08  ? 795  PHE A CE2 1 
ATOM   6142  C  CZ  . PHE A 1 795  ? 134.677 47.585  117.689 1.00 88.64  ? 795  PHE A CZ  1 
ATOM   6143  N  N   . PRO A 1 796  ? 140.554 52.157  117.140 1.00 101.22 ? 796  PRO A N   1 
ATOM   6144  C  CA  . PRO A 1 796  ? 141.283 53.417  117.233 1.00 103.28 ? 796  PRO A CA  1 
ATOM   6145  C  C   . PRO A 1 796  ? 140.467 54.560  116.633 1.00 101.14 ? 796  PRO A C   1 
ATOM   6146  O  O   . PRO A 1 796  ? 139.705 54.349  115.683 1.00 98.47  ? 796  PRO A O   1 
ATOM   6147  C  CB  . PRO A 1 796  ? 142.540 53.155  116.402 1.00 105.54 ? 796  PRO A CB  1 
ATOM   6148  C  CG  . PRO A 1 796  ? 142.155 52.057  115.431 1.00 103.80 ? 796  PRO A CG  1 
ATOM   6149  C  CD  . PRO A 1 796  ? 140.846 51.447  115.881 1.00 100.95 ? 796  PRO A CD  1 
ATOM   6150  N  N   . ILE A 1 797  ? 140.619 55.754  117.195 1.00 102.79 ? 797  ILE A N   1 
ATOM   6151  C  CA  . ILE A 1 797  ? 139.879 56.920  116.732 1.00 101.45 ? 797  ILE A CA  1 
ATOM   6152  C  C   . ILE A 1 797  ? 140.780 58.141  116.631 1.00 104.46 ? 797  ILE A C   1 
ATOM   6153  O  O   . ILE A 1 797  ? 141.486 58.493  117.581 1.00 107.26 ? 797  ILE A O   1 
ATOM   6154  C  CB  . ILE A 1 797  ? 138.639 57.204  117.625 1.00 99.44  ? 797  ILE A CB  1 
ATOM   6155  C  CG1 . ILE A 1 797  ? 137.515 56.219  117.288 1.00 96.49  ? 797  ILE A CG1 1 
ATOM   6156  C  CG2 . ILE A 1 797  ? 138.131 58.632  117.432 1.00 98.21  ? 797  ILE A CG2 1 
ATOM   6157  C  CD1 . ILE A 1 797  ? 136.640 55.841  118.456 1.00 95.64  ? 797  ILE A CD1 1 
ATOM   6158  N  N   . ASN A 1 798  ? 140.759 58.766  115.458 1.00 104.54 ? 798  ASN A N   1 
ATOM   6159  C  CA  . ASN A 1 798  ? 141.444 60.031  115.239 1.00 107.55 ? 798  ASN A CA  1 
ATOM   6160  C  C   . ASN A 1 798  ? 140.464 61.187  115.384 1.00 106.23 ? 798  ASN A C   1 
ATOM   6161  O  O   . ASN A 1 798  ? 139.342 61.127  114.872 1.00 103.09 ? 798  ASN A O   1 
ATOM   6162  C  CB  . ASN A 1 798  ? 142.108 60.062  113.859 1.00 108.35 ? 798  ASN A CB  1 
ATOM   6163  C  CG  . ASN A 1 798  ? 142.891 61.346  113.613 1.00 111.28 ? 798  ASN A CG  1 
ATOM   6164  O  OD1 . ASN A 1 798  ? 142.635 62.066  112.645 1.00 111.03 ? 798  ASN A OD1 1 
ATOM   6165  N  ND2 . ASN A 1 798  ? 143.841 61.643  114.495 1.00 114.76 ? 798  ASN A ND2 1 
ATOM   6166  N  N   . LEU A 1 799  ? 140.899 62.237  116.072 1.00 109.15 ? 799  LEU A N   1 
ATOM   6167  C  CA  . LEU A 1 799  ? 140.020 63.349  116.416 1.00 108.73 ? 799  LEU A CA  1 
ATOM   6168  C  C   . LEU A 1 799  ? 140.233 64.593  115.556 1.00 110.18 ? 799  LEU A C   1 
ATOM   6169  O  O   . LEU A 1 799  ? 139.280 65.330  115.280 1.00 108.34 ? 799  LEU A O   1 
ATOM   6170  C  CB  . LEU A 1 799  ? 140.187 63.713  117.894 1.00 110.54 ? 799  LEU A CB  1 
ATOM   6171  C  CG  . LEU A 1 799  ? 140.085 62.583  118.924 1.00 110.48 ? 799  LEU A CG  1 
ATOM   6172  C  CD1 . LEU A 1 799  ? 140.649 63.033  120.268 1.00 113.15 ? 799  LEU A CD1 1 
ATOM   6173  C  CD2 . LEU A 1 799  ? 138.651 62.076  119.064 1.00 106.58 ? 799  LEU A CD2 1 
ATOM   6174  N  N   . ASP A 1 800  ? 141.472 64.798  115.110 1.00 114.03 ? 800  ASP A N   1 
ATOM   6175  C  CA  . ASP A 1 800  ? 141.928 66.092  114.574 1.00 116.78 ? 800  ASP A CA  1 
ATOM   6176  C  C   . ASP A 1 800  ? 141.285 66.654  113.288 1.00 115.41 ? 800  ASP A C   1 
ATOM   6177  O  O   . ASP A 1 800  ? 141.690 67.720  112.814 1.00 117.38 ? 800  ASP A O   1 
ATOM   6178  C  CB  . ASP A 1 800  ? 143.459 66.126  114.485 1.00 120.92 ? 800  ASP A CB  1 
ATOM   6179  C  CG  . ASP A 1 800  ? 144.109 66.482  115.813 1.00 124.07 ? 800  ASP A CG  1 
ATOM   6180  O  OD1 . ASP A 1 800  ? 143.397 66.982  116.715 1.00 122.80 ? 800  ASP A OD1 1 
ATOM   6181  O  OD2 . ASP A 1 800  ? 145.333 66.268  115.954 1.00 127.45 ? 800  ASP A OD2 1 
ATOM   6182  N  N   . ILE A 1 801  ? 140.289 65.956  112.741 1.00 112.56 ? 801  ILE A N   1 
ATOM   6183  C  CA  . ILE A 1 801  ? 139.420 66.534  111.704 1.00 111.14 ? 801  ILE A CA  1 
ATOM   6184  C  C   . ILE A 1 801  ? 138.392 67.473  112.367 1.00 110.21 ? 801  ILE A C   1 
ATOM   6185  O  O   . ILE A 1 801  ? 137.187 67.185  112.395 1.00 107.12 ? 801  ILE A O   1 
ATOM   6186  C  CB  . ILE A 1 801  ? 138.721 65.447  110.806 1.00 108.17 ? 801  ILE A CB  1 
ATOM   6187  C  CG1 . ILE A 1 801  ? 138.152 64.275  111.641 1.00 106.57 ? 801  ILE A CG1 1 
ATOM   6188  C  CG2 . ILE A 1 801  ? 139.659 64.982  109.670 1.00 109.70 ? 801  ILE A CG2 1 
ATOM   6189  C  CD1 . ILE A 1 801  ? 139.110 63.090  111.884 1.00 108.77 ? 801  ILE A CD1 1 
ATOM   6190  N  N   . ASN A 1 802  ? 138.884 68.602  112.889 1.00 113.28 ? 802  ASN A N   1 
ATOM   6191  C  CA  . ASN A 1 802  ? 138.118 69.418  113.847 1.00 113.14 ? 802  ASN A CA  1 
ATOM   6192  C  C   . ASN A 1 802  ? 138.505 70.905  114.031 1.00 116.18 ? 802  ASN A C   1 
ATOM   6193  O  O   . ASN A 1 802  ? 138.256 71.479  115.102 1.00 117.08 ? 802  ASN A O   1 
ATOM   6194  C  CB  . ASN A 1 802  ? 138.119 68.721  115.224 1.00 113.33 ? 802  ASN A CB  1 
ATOM   6195  C  CG  . ASN A 1 802  ? 139.527 68.553  115.818 1.00 116.99 ? 802  ASN A CG  1 
ATOM   6196  O  OD1 . ASN A 1 802  ? 139.699 67.861  116.821 1.00 117.51 ? 802  ASN A OD1 1 
ATOM   6197  N  ND2 . ASN A 1 802  ? 140.527 69.183  115.206 1.00 119.87 ? 802  ASN A ND2 1 
ATOM   6198  N  N   . LYS A 1 803  ? 139.101 71.532  113.017 1.00 117.97 ? 803  LYS A N   1 
ATOM   6199  C  CA  . LYS A 1 803  ? 139.510 72.939  113.157 1.00 121.11 ? 803  LYS A CA  1 
ATOM   6200  C  C   . LYS A 1 803  ? 139.577 73.739  111.852 1.00 121.90 ? 803  LYS A C   1 
ATOM   6201  O  O   . LYS A 1 803  ? 139.875 73.197  110.782 1.00 121.48 ? 803  LYS A O   1 
ATOM   6202  C  CB  . LYS A 1 803  ? 140.853 73.049  113.894 1.00 125.23 ? 803  LYS A CB  1 
ATOM   6203  C  CG  . LYS A 1 803  ? 140.900 74.211  114.872 1.00 127.77 ? 803  LYS A CG  1 
ATOM   6204  C  CD  . LYS A 1 803  ? 142.262 74.876  114.928 1.00 132.48 ? 803  LYS A CD  1 
ATOM   6205  C  CE  . LYS A 1 803  ? 142.178 76.150  115.753 1.00 134.83 ? 803  LYS A CE  1 
ATOM   6206  N  NZ  . LYS A 1 803  ? 143.394 76.990  115.612 1.00 140.01 ? 803  LYS A NZ  1 
ATOM   6207  N  N   . LYS A 1 804  ? 139.298 75.038  111.970 1.00 123.19 ? 804  LYS A N   1 
ATOM   6208  C  CA  . LYS A 1 804  ? 139.476 75.998  110.881 1.00 124.73 ? 804  LYS A CA  1 
ATOM   6209  C  C   . LYS A 1 804  ? 140.406 77.127  111.345 1.00 129.19 ? 804  LYS A C   1 
ATOM   6210  O  O   . LYS A 1 804  ? 141.452 76.855  111.945 1.00 131.74 ? 804  LYS A O   1 
ATOM   6211  C  CB  . LYS A 1 804  ? 138.118 76.526  110.397 1.00 122.15 ? 804  LYS A CB  1 
ATOM   6212  C  CG  . LYS A 1 804  ? 137.343 75.511  109.564 1.00 118.39 ? 804  LYS A CG  1 
ATOM   6213  C  CD  . LYS A 1 804  ? 135.903 75.940  109.318 1.00 116.12 ? 804  LYS A CD  1 
ATOM   6214  C  CE  . LYS A 1 804  ? 135.138 74.835  108.599 1.00 112.58 ? 804  LYS A CE  1 
ATOM   6215  N  NZ  . LYS A 1 804  ? 133.654 74.995  108.719 1.00 109.86 ? 804  LYS A NZ  1 
ATOM   6216  N  N   . ALA A 1 805  ? 140.039 78.380  111.070 1.00 130.20 ? 805  ALA A N   1 
ATOM   6217  C  CA  . ALA A 1 805  ? 140.828 79.533  111.520 1.00 134.48 ? 805  ALA A CA  1 
ATOM   6218  C  C   . ALA A 1 805  ? 140.735 79.683  113.040 1.00 134.71 ? 805  ALA A C   1 
ATOM   6219  O  O   . ALA A 1 805  ? 141.750 79.619  113.741 1.00 137.79 ? 805  ALA A O   1 
ATOM   6220  C  CB  . ALA A 1 805  ? 140.377 80.814  110.813 1.00 135.89 ? 805  ALA A CB  1 
ATOM   6221  N  N   . ASP A 1 806  ? 139.511 79.877  113.533 1.00 131.41 ? 806  ASP A N   1 
ATOM   6222  C  CA  . ASP A 1 806  ? 139.218 79.879  114.965 1.00 130.65 ? 806  ASP A CA  1 
ATOM   6223  C  C   . ASP A 1 806  ? 138.230 78.764  115.310 1.00 125.42 ? 806  ASP A C   1 
ATOM   6224  O  O   . ASP A 1 806  ? 137.258 78.531  114.583 1.00 122.08 ? 806  ASP A O   1 
ATOM   6225  C  CB  . ASP A 1 806  ? 138.662 81.238  115.417 1.00 132.44 ? 806  ASP A CB  1 
ATOM   6226  C  CG  . ASP A 1 806  ? 139.752 82.197  115.901 1.00 137.90 ? 806  ASP A CG  1 
ATOM   6227  O  OD1 . ASP A 1 806  ? 140.779 82.358  115.205 1.00 140.82 ? 806  ASP A OD1 1 
ATOM   6228  O  OD2 . ASP A 1 806  ? 139.572 82.801  116.982 1.00 139.37 ? 806  ASP A OD2 1 
ATOM   6229  N  N   . SER A 1 807  ? 138.506 78.071  116.412 1.00 124.67 ? 807  SER A N   1 
ATOM   6230  C  CA  . SER A 1 807  ? 137.595 77.067  116.971 1.00 120.01 ? 807  SER A CA  1 
ATOM   6231  C  C   . SER A 1 807  ? 137.574 77.166  118.498 1.00 120.50 ? 807  SER A C   1 
ATOM   6232  O  O   . SER A 1 807  ? 136.948 76.343  119.177 1.00 118.12 ? 807  SER A O   1 
ATOM   6233  C  CB  . SER A 1 807  ? 137.993 75.655  116.523 1.00 118.31 ? 807  SER A CB  1 
ATOM   6234  O  OG  . SER A 1 807  ? 137.819 75.487  115.124 1.00 116.90 ? 807  SER A OG  1 
ATOM   6235  N  N   . GLY A 1 808  ? 138.257 78.188  119.018 1.00 123.54 ? 808  GLY A N   1 
ATOM   6236  C  CA  . GLY A 1 808  ? 138.409 78.414  120.459 1.00 124.38 ? 808  GLY A CA  1 
ATOM   6237  C  C   . GLY A 1 808  ? 139.118 77.251  121.129 1.00 123.68 ? 808  GLY A C   1 
ATOM   6238  O  O   . GLY A 1 808  ? 140.318 77.320  121.432 1.00 127.37 ? 808  GLY A O   1 
ATOM   6239  N  N   . SER A 1 809  ? 138.336 76.201  121.377 1.00 118.65 ? 809  SER A N   1 
ATOM   6240  C  CA  . SER A 1 809  ? 138.798 74.873  121.761 1.00 116.58 ? 809  SER A CA  1 
ATOM   6241  C  C   . SER A 1 809  ? 137.543 74.018  121.764 1.00 110.96 ? 809  SER A C   1 
ATOM   6242  O  O   . SER A 1 809  ? 136.707 74.125  122.668 1.00 110.21 ? 809  SER A O   1 
ATOM   6243  C  CB  . SER A 1 809  ? 139.480 74.860  123.138 1.00 120.15 ? 809  SER A CB  1 
ATOM   6244  O  OG  . SER A 1 809  ? 138.618 75.338  124.158 1.00 120.33 ? 809  SER A OG  1 
ATOM   6245  N  N   . THR A 1 810  ? 137.392 73.207  120.722 1.00 106.39 ? 810  THR A N   1 
ATOM   6246  C  CA  . THR A 1 810  ? 136.239 72.333  120.594 1.00 100.52 ? 810  THR A CA  1 
ATOM   6247  C  C   . THR A 1 810  ? 136.255 71.327  121.743 1.00 99.18  ? 810  THR A C   1 
ATOM   6248  O  O   . THR A 1 810  ? 137.301 70.750  122.052 1.00 101.10 ? 810  THR A O   1 
ATOM   6249  C  CB  . THR A 1 810  ? 136.226 71.611  119.226 1.00 98.31  ? 810  THR A CB  1 
ATOM   6250  O  OG1 . THR A 1 810  ? 137.138 70.506  119.247 1.00 98.98  ? 810  THR A OG1 1 
ATOM   6251  C  CG2 . THR A 1 810  ? 136.629 72.571  118.111 1.00 99.43  ? 810  THR A CG2 1 
ATOM   6252  N  N   . LYS A 1 811  ? 135.108 71.148  122.395 1.00 95.33  ? 811  LYS A N   1 
ATOM   6253  C  CA  . LYS A 1 811  ? 135.009 70.241  123.536 1.00 93.65  ? 811  LYS A CA  1 
ATOM   6254  C  C   . LYS A 1 811  ? 134.420 68.910  123.098 1.00 88.69  ? 811  LYS A C   1 
ATOM   6255  O  O   . LYS A 1 811  ? 133.451 68.874  122.340 1.00 85.63  ? 811  LYS A O   1 
ATOM   6256  C  CB  . LYS A 1 811  ? 134.192 70.862  124.673 1.00 94.41  ? 811  LYS A CB  1 
ATOM   6257  C  CG  . LYS A 1 811  ? 134.392 70.161  126.012 1.00 96.64  ? 811  LYS A CG  1 
ATOM   6258  C  CD  . LYS A 1 811  ? 134.245 71.118  127.191 1.00 100.00 ? 811  LYS A CD  1 
ATOM   6259  C  CE  . LYS A 1 811  ? 134.825 70.502  128.465 1.00 102.95 ? 811  LYS A CE  1 
ATOM   6260  N  NZ  . LYS A 1 811  ? 135.021 71.503  129.551 1.00 106.41 ? 811  LYS A NZ  1 
ATOM   6261  N  N   . ILE A 1 812  ? 135.017 67.820  123.573 1.00 87.39  ? 812  ILE A N   1 
ATOM   6262  C  CA  . ILE A 1 812  ? 134.670 66.491  123.086 1.00 82.89  ? 812  ILE A CA  1 
ATOM   6263  C  C   . ILE A 1 812  ? 134.458 65.460  124.194 1.00 81.67  ? 812  ILE A C   1 
ATOM   6264  O  O   . ILE A 1 812  ? 135.158 65.462  125.192 1.00 84.31  ? 812  ILE A O   1 
ATOM   6265  C  CB  . ILE A 1 812  ? 135.677 65.993  122.010 1.00 83.38  ? 812  ILE A CB  1 
ATOM   6266  C  CG1 . ILE A 1 812  ? 136.885 65.307  122.627 1.00 86.56  ? 812  ILE A CG1 1 
ATOM   6267  C  CG2 . ILE A 1 812  ? 136.147 67.147  121.118 1.00 84.54  ? 812  ILE A CG2 1 
ATOM   6268  C  CD1 . ILE A 1 812  ? 137.760 64.633  121.596 1.00 87.22  ? 812  ILE A CD1 1 
ATOM   6269  N  N   . GLU A 1 813  ? 133.468 64.592  124.011 1.00 77.37  ? 813  GLU A N   1 
ATOM   6270  C  CA  . GLU A 1 813  ? 133.142 63.576  125.006 1.00 76.25  ? 813  GLU A CA  1 
ATOM   6271  C  C   . GLU A 1 813  ? 132.929 62.187  124.392 1.00 73.41  ? 813  GLU A C   1 
ATOM   6272  O  O   . GLU A 1 813  ? 132.347 62.055  123.311 1.00 70.42  ? 813  GLU A O   1 
ATOM   6273  C  CB  . GLU A 1 813  ? 131.935 64.010  125.856 1.00 75.43  ? 813  GLU A CB  1 
ATOM   6274  C  CG  . GLU A 1 813  ? 130.603 63.364  125.505 1.00 72.47  ? 813  GLU A CG  1 
ATOM   6275  C  CD  . GLU A 1 813  ? 129.434 63.906  126.318 1.00 72.89  ? 813  GLU A CD  1 
ATOM   6276  O  OE1 . GLU A 1 813  ? 129.642 64.327  127.479 1.00 75.71  ? 813  GLU A OE1 1 
ATOM   6277  O  OE2 . GLU A 1 813  ? 128.296 63.909  125.793 1.00 70.28  ? 813  GLU A OE2 1 
ATOM   6278  N  N   . PHE A 1 814  ? 133.427 61.160  125.082 1.00 73.79  ? 814  PHE A N   1 
ATOM   6279  C  CA  . PHE A 1 814  ? 133.186 59.770  124.698 1.00 71.26  ? 814  PHE A CA  1 
ATOM   6280  C  C   . PHE A 1 814  ? 131.978 59.231  125.439 1.00 69.59  ? 814  PHE A C   1 
ATOM   6281  O  O   . PHE A 1 814  ? 131.787 59.522  126.617 1.00 71.24  ? 814  PHE A O   1 
ATOM   6282  C  CB  . PHE A 1 814  ? 134.410 58.882  124.986 1.00 73.83  ? 814  PHE A CB  1 
ATOM   6283  C  CG  . PHE A 1 814  ? 134.084 57.411  125.061 1.00 72.31  ? 814  PHE A CG  1 
ATOM   6284  C  CD1 . PHE A 1 814  ? 134.028 56.638  123.911 1.00 69.54  ? 814  PHE A CD1 1 
ATOM   6285  C  CD2 . PHE A 1 814  ? 133.800 56.808  126.282 1.00 73.08  ? 814  PHE A CD2 1 
ATOM   6286  C  CE1 . PHE A 1 814  ? 133.705 55.292  123.975 1.00 68.83  ? 814  PHE A CE1 1 
ATOM   6287  C  CE2 . PHE A 1 814  ? 133.478 55.461  126.351 1.00 72.62  ? 814  PHE A CE2 1 
ATOM   6288  C  CZ  . PHE A 1 814  ? 133.431 54.702  125.194 1.00 70.56  ? 814  PHE A CZ  1 
ATOM   6289  N  N   . ARG A 1 815  ? 131.174 58.431  124.752 1.00 66.45  ? 815  ARG A N   1 
ATOM   6290  C  CA  . ARG A 1 815  ? 130.000 57.821  125.363 1.00 65.12  ? 815  ARG A CA  1 
ATOM   6291  C  C   . ARG A 1 815  ? 129.894 56.354  124.987 1.00 64.31  ? 815  ARG A C   1 
ATOM   6292  O  O   . ARG A 1 815  ? 130.066 55.992  123.820 1.00 62.86  ? 815  ARG A O   1 
ATOM   6293  C  CB  . ARG A 1 815  ? 128.714 58.533  124.928 1.00 62.38  ? 815  ARG A CB  1 
ATOM   6294  C  CG  . ARG A 1 815  ? 128.759 60.049  124.974 1.00 62.29  ? 815  ARG A CG  1 
ATOM   6295  C  CD  . ARG A 1 815  ? 127.367 60.649  124.978 1.00 60.51  ? 815  ARG A CD  1 
ATOM   6296  N  NE  . ARG A 1 815  ? 126.591 60.238  123.815 1.00 58.01  ? 815  ARG A NE  1 
ATOM   6297  C  CZ  . ARG A 1 815  ? 125.562 60.917  123.322 1.00 55.63  ? 815  ARG A CZ  1 
ATOM   6298  N  NH1 . ARG A 1 815  ? 125.186 62.053  123.887 1.00 56.62  ? 815  ARG A NH1 1 
ATOM   6299  N  NH2 . ARG A 1 815  ? 124.919 60.469  122.253 1.00 52.22  ? 815  ARG A NH2 1 
ATOM   6300  N  N   . LEU A 1 816  ? 129.606 55.522  125.984 1.00 65.28  ? 816  LEU A N   1 
ATOM   6301  C  CA  . LEU A 1 816  ? 129.260 54.128  125.762 1.00 64.49  ? 816  LEU A CA  1 
ATOM   6302  C  C   . LEU A 1 816  ? 127.783 53.903  126.048 1.00 63.08  ? 816  LEU A C   1 
ATOM   6303  O  O   . LEU A 1 816  ? 127.290 54.216  127.136 1.00 64.48  ? 816  LEU A O   1 
ATOM   6304  C  CB  . LEU A 1 816  ? 130.116 53.207  126.625 1.00 67.52  ? 816  LEU A CB  1 
ATOM   6305  C  CG  . LEU A 1 816  ? 129.715 51.735  126.741 1.00 67.57  ? 816  LEU A CG  1 
ATOM   6306  C  CD1 . LEU A 1 816  ? 129.720 51.017  125.398 1.00 65.98  ? 816  LEU A CD1 1 
ATOM   6307  C  CD2 . LEU A 1 816  ? 130.650 51.045  127.701 1.00 71.46  ? 816  LEU A CD2 1 
ATOM   6308  N  N   . ASN A 1 817  ? 127.086 53.360  125.057 1.00 60.68  ? 817  ASN A N   1 
ATOM   6309  C  CA  . ASN A 1 817  ? 125.655 53.105  125.148 1.00 59.20  ? 817  ASN A CA  1 
ATOM   6310  C  C   . ASN A 1 817  ? 125.298 51.679  124.754 1.00 58.88  ? 817  ASN A C   1 
ATOM   6311  O  O   . ASN A 1 817  ? 125.694 51.209  123.688 1.00 57.79  ? 817  ASN A O   1 
ATOM   6312  C  CB  . ASN A 1 817  ? 124.874 54.095  124.285 1.00 56.60  ? 817  ASN A CB  1 
ATOM   6313  C  CG  . ASN A 1 817  ? 124.682 55.434  124.969 1.00 56.90  ? 817  ASN A CG  1 
ATOM   6314  O  OD1 . ASN A 1 817  ? 124.258 55.494  126.120 1.00 57.76  ? 817  ASN A OD1 1 
ATOM   6315  N  ND2 . ASN A 1 817  ? 124.990 56.517  124.259 1.00 55.96  ? 817  ASN A ND2 1 
ATOM   6316  N  N   . PRO A 1 818  ? 124.536 50.991  125.616 1.00 59.74  ? 818  PRO A N   1 
ATOM   6317  C  CA  . PRO A 1 818  ? 124.199 49.593  125.410 1.00 59.88  ? 818  PRO A CA  1 
ATOM   6318  C  C   . PRO A 1 818  ? 123.105 49.404  124.376 1.00 56.94  ? 818  PRO A C   1 
ATOM   6319  O  O   . PRO A 1 818  ? 122.892 48.290  123.900 1.00 57.18  ? 818  PRO A O   1 
ATOM   6320  C  CB  . PRO A 1 818  ? 123.669 49.179  126.774 1.00 62.16  ? 818  PRO A CB  1 
ATOM   6321  C  CG  . PRO A 1 818  ? 123.040 50.402  127.294 1.00 61.81  ? 818  PRO A CG  1 
ATOM   6322  C  CD  . PRO A 1 818  ? 123.940 51.515  126.856 1.00 60.90  ? 818  PRO A CD  1 
ATOM   6323  N  N   . ASN A 1 819  ? 122.417 50.484  124.035 1.00 54.45  ? 819  ASN A N   1 
ATOM   6324  C  CA  . ASN A 1 819  ? 121.238 50.386  123.212 1.00 52.23  ? 819  ASN A CA  1 
ATOM   6325  C  C   . ASN A 1 819  ? 121.045 51.633  122.352 1.00 49.76  ? 819  ASN A C   1 
ATOM   6326  O  O   . ASN A 1 819  ? 121.428 52.735  122.751 1.00 50.01  ? 819  ASN A O   1 
ATOM   6327  C  CB  . ASN A 1 819  ? 120.014 50.138  124.101 1.00 53.07  ? 819  ASN A CB  1 
ATOM   6328  C  CG  . ASN A 1 819  ? 118.825 49.628  123.327 1.00 51.91  ? 819  ASN A CG  1 
ATOM   6329  O  OD1 . ASN A 1 819  ? 118.111 50.403  122.692 1.00 50.83  ? 819  ASN A OD1 1 
ATOM   6330  N  ND2 . ASN A 1 819  ? 118.608 48.316  123.365 1.00 52.41  ? 819  ASN A ND2 1 
ATOM   6331  N  N   . LEU A 1 820  ? 120.457 51.445  121.172 1.00 47.29  ? 820  LEU A N   1 
ATOM   6332  C  CA  . LEU A 1 820  ? 120.151 52.542  120.273 1.00 44.96  ? 820  LEU A CA  1 
ATOM   6333  C  C   . LEU A 1 820  ? 119.169 53.533  120.881 1.00 44.61  ? 820  LEU A C   1 
ATOM   6334  O  O   . LEU A 1 820  ? 119.134 54.707  120.502 1.00 43.58  ? 820  LEU A O   1 
ATOM   6335  C  CB  . LEU A 1 820  ? 119.554 52.007  118.975 1.00 43.24  ? 820  LEU A CB  1 
ATOM   6336  C  CG  . LEU A 1 820  ? 120.474 51.264  118.022 1.00 42.84  ? 820  LEU A CG  1 
ATOM   6337  C  CD1 . LEU A 1 820  ? 119.623 50.456  117.083 1.00 41.58  ? 820  LEU A CD1 1 
ATOM   6338  C  CD2 . LEU A 1 820  ? 121.360 52.239  117.273 1.00 41.28  ? 820  LEU A CD2 1 
ATOM   6339  N  N   . LEU A 1 821  ? 118.361 53.062  121.815 1.00 45.47  ? 821  LEU A N   1 
ATOM   6340  C  CA  . LEU A 1 821  ? 117.320 53.901  122.357 1.00 45.25  ? 821  LEU A CA  1 
ATOM   6341  C  C   . LEU A 1 821  ? 117.681 54.598  123.666 1.00 47.36  ? 821  LEU A C   1 
ATOM   6342  O  O   . LEU A 1 821  ? 116.901 55.426  124.141 1.00 47.74  ? 821  LEU A O   1 
ATOM   6343  C  CB  . LEU A 1 821  ? 116.019 53.113  122.499 1.00 45.15  ? 821  LEU A CB  1 
ATOM   6344  C  CG  . LEU A 1 821  ? 115.452 52.523  121.208 1.00 43.63  ? 821  LEU A CG  1 
ATOM   6345  C  CD1 . LEU A 1 821  ? 114.100 51.885  121.483 1.00 43.65  ? 821  LEU A CD1 1 
ATOM   6346  C  CD2 . LEU A 1 821  ? 115.333 53.582  120.121 1.00 40.38  ? 821  LEU A CD2 1 
ATOM   6347  N  N   . THR A 1 822  ? 118.840 54.303  124.257 1.00 49.01  ? 822  THR A N   1 
ATOM   6348  C  CA  . THR A 1 822  ? 119.107 54.909  125.566 1.00 51.11  ? 822  THR A CA  1 
ATOM   6349  C  C   . THR A 1 822  ? 119.117 56.434  125.490 1.00 50.02  ? 822  THR A C   1 
ATOM   6350  O  O   . THR A 1 822  ? 118.320 57.068  126.165 1.00 50.89  ? 822  THR A O   1 
ATOM   6351  C  CB  . THR A 1 822  ? 120.322 54.301  126.377 1.00 53.78  ? 822  THR A CB  1 
ATOM   6352  O  OG1 . THR A 1 822  ? 121.300 55.305  126.675 1.00 54.77  ? 822  THR A OG1 1 
ATOM   6353  C  CG2 . THR A 1 822  ? 120.953 53.119  125.682 1.00 53.54  ? 822  THR A CG2 1 
ATOM   6354  N  N   . THR A 1 823  ? 119.956 57.027  124.644 1.00 48.61  ? 823  THR A N   1 
ATOM   6355  C  CA  . THR A 1 823  ? 119.948 58.492  124.509 1.00 47.85  ? 823  THR A CA  1 
ATOM   6356  C  C   . THR A 1 823  ? 118.632 59.017  123.919 1.00 45.91  ? 823  THR A C   1 
ATOM   6357  O  O   . THR A 1 823  ? 118.181 60.111  124.266 1.00 45.88  ? 823  THR A O   1 
ATOM   6358  C  CB  . THR A 1 823  ? 121.148 59.052  123.710 1.00 47.16  ? 823  THR A CB  1 
ATOM   6359  O  OG1 . THR A 1 823  ? 121.065 58.617  122.350 1.00 46.19  ? 823  THR A OG1 1 
ATOM   6360  C  CG2 . THR A 1 823  ? 122.462 58.596  124.312 1.00 48.61  ? 823  THR A CG2 1 
ATOM   6361  N  N   . VAL A 1 824  ? 118.007 58.230  123.050 1.00 44.44  ? 824  VAL A N   1 
ATOM   6362  C  CA  . VAL A 1 824  ? 116.735 58.641  122.462 1.00 43.17  ? 824  VAL A CA  1 
ATOM   6363  C  C   . VAL A 1 824  ? 115.659 58.780  123.543 1.00 44.73  ? 824  VAL A C   1 
ATOM   6364  O  O   . VAL A 1 824  ? 115.035 59.831  123.679 1.00 44.59  ? 824  VAL A O   1 
ATOM   6365  C  CB  . VAL A 1 824  ? 116.258 57.683  121.359 1.00 41.51  ? 824  VAL A CB  1 
ATOM   6366  C  CG1 . VAL A 1 824  ? 114.907 58.149  120.809 1.00 39.78  ? 824  VAL A CG1 1 
ATOM   6367  C  CG2 . VAL A 1 824  ? 117.284 57.611  120.234 1.00 40.19  ? 824  VAL A CG2 1 
ATOM   6368  N  N   . ILE A 1 825  ? 115.468 57.716  124.317 1.00 46.56  ? 825  ILE A N   1 
ATOM   6369  C  CA  . ILE A 1 825  ? 114.504 57.708  125.407 1.00 48.08  ? 825  ILE A CA  1 
ATOM   6370  C  C   . ILE A 1 825  ? 114.813 58.833  126.372 1.00 49.91  ? 825  ILE A C   1 
ATOM   6371  O  O   . ILE A 1 825  ? 113.908 59.537  126.821 1.00 50.68  ? 825  ILE A O   1 
ATOM   6372  C  CB  . ILE A 1 825  ? 114.488 56.347  126.132 1.00 49.88  ? 825  ILE A CB  1 
ATOM   6373  C  CG1 . ILE A 1 825  ? 113.926 55.267  125.193 1.00 48.60  ? 825  ILE A CG1 1 
ATOM   6374  C  CG2 . ILE A 1 825  ? 113.692 56.428  127.441 1.00 51.17  ? 825  ILE A CG2 1 
ATOM   6375  C  CD1 . ILE A 1 825  ? 114.076 53.847  125.723 1.00 50.89  ? 825  ILE A CD1 1 
ATOM   6376  N  N   . LYS A 1 826  ? 116.095 59.026  126.662 1.00 51.06  ? 826  LYS A N   1 
ATOM   6377  C  CA  . LYS A 1 826  ? 116.516 60.112  127.540 1.00 52.87  ? 826  LYS A CA  1 
ATOM   6378  C  C   . LYS A 1 826  ? 116.086 61.462  126.979 1.00 51.63  ? 826  LYS A C   1 
ATOM   6379  O  O   . LYS A 1 826  ? 115.755 62.364  127.725 1.00 52.70  ? 826  LYS A O   1 
ATOM   6380  C  CB  . LYS A 1 826  ? 118.034 60.076  127.750 1.00 54.14  ? 826  LYS A CB  1 
ATOM   6381  C  CG  . LYS A 1 826  ? 118.572 61.211  128.593 1.00 57.14  ? 826  LYS A CG  1 
ATOM   6382  C  CD  . LYS A 1 826  ? 119.901 60.862  129.228 1.00 62.76  ? 826  LYS A CD  1 
ATOM   6383  C  CE  . LYS A 1 826  ? 120.190 61.776  130.422 1.00 67.11  ? 826  LYS A CE  1 
ATOM   6384  N  NZ  . LYS A 1 826  ? 121.207 61.167  131.338 1.00 71.20  ? 826  LYS A NZ  1 
ATOM   6385  N  N   . ASN A 1 827  ? 116.079 61.585  125.657 1.00 49.85  ? 827  ASN A N   1 
ATOM   6386  C  CA  . ASN A 1 827  ? 115.835 62.864  125.015 1.00 49.03  ? 827  ASN A CA  1 
ATOM   6387  C  C   . ASN A 1 827  ? 114.488 62.940  124.320 1.00 47.96  ? 827  ASN A C   1 
ATOM   6388  O  O   . ASN A 1 827  ? 114.298 63.757  123.418 1.00 46.78  ? 827  ASN A O   1 
ATOM   6389  C  CB  . ASN A 1 827  ? 116.962 63.160  124.022 1.00 48.02  ? 827  ASN A CB  1 
ATOM   6390  C  CG  . ASN A 1 827  ? 118.270 63.479  124.709 1.00 49.06  ? 827  ASN A CG  1 
ATOM   6391  O  OD1 . ASN A 1 827  ? 118.400 64.501  125.370 1.00 50.15  ? 827  ASN A OD1 1 
ATOM   6392  N  ND2 . ASN A 1 827  ? 119.244 62.605  124.558 1.00 49.50  ? 827  ASN A ND2 1 
ATOM   6393  N  N   . LEU A 1 828  ? 113.543 62.110  124.754 1.00 48.98  ? 828  LEU A N   1 
ATOM   6394  C  CA  . LEU A 1 828  ? 112.292 61.916  124.001 1.00 48.37  ? 828  LEU A CA  1 
ATOM   6395  C  C   . LEU A 1 828  ? 111.460 63.163  123.728 1.00 48.41  ? 828  LEU A C   1 
ATOM   6396  O  O   . LEU A 1 828  ? 110.701 63.185  122.763 1.00 47.80  ? 828  LEU A O   1 
ATOM   6397  C  CB  . LEU A 1 828  ? 111.406 60.861  124.655 1.00 49.30  ? 828  LEU A CB  1 
ATOM   6398  C  CG  . LEU A 1 828  ? 111.347 59.480  124.013 1.00 48.38  ? 828  LEU A CG  1 
ATOM   6399  C  CD1 . LEU A 1 828  ? 110.368 58.617  124.788 1.00 49.14  ? 828  LEU A CD1 1 
ATOM   6400  C  CD2 . LEU A 1 828  ? 110.951 59.561  122.542 1.00 45.08  ? 828  LEU A CD2 1 
ATOM   6401  N  N   . ASP A 1 829  ? 111.596 64.185  124.564 1.00 49.97  ? 829  ASP A N   1 
ATOM   6402  C  CA  . ASP A 1 829  ? 110.828 65.419  124.401 1.00 50.54  ? 829  ASP A CA  1 
ATOM   6403  C  C   . ASP A 1 829  ? 111.548 66.492  123.583 1.00 49.41  ? 829  ASP A C   1 
ATOM   6404  O  O   . ASP A 1 829  ? 110.934 67.490  123.171 1.00 49.45  ? 829  ASP A O   1 
ATOM   6405  C  CB  . ASP A 1 829  ? 110.403 65.996  125.768 1.00 53.54  ? 829  ASP A CB  1 
ATOM   6406  C  CG  . ASP A 1 829  ? 111.549 66.024  126.796 1.00 57.86  ? 829  ASP A CG  1 
ATOM   6407  O  OD1 . ASP A 1 829  ? 111.751 67.098  127.413 1.00 61.74  ? 829  ASP A OD1 1 
ATOM   6408  O  OD2 . ASP A 1 829  ? 112.235 64.981  127.006 1.00 60.46  ? 829  ASP A OD2 1 
ATOM   6409  N  N   A HIS A 1 830  ? 112.840 66.275  123.340 0.50 48.77  ? 830  HIS A N   1 
ATOM   6410  N  N   B HIS A 1 830  ? 112.844 66.300  123.360 0.50 48.89  ? 830  HIS A N   1 
ATOM   6411  C  CA  A HIS A 1 830  ? 113.694 67.262  122.686 0.50 48.06  ? 830  HIS A CA  1 
ATOM   6412  C  CA  B HIS A 1 830  ? 113.638 67.273  122.631 0.50 48.13  ? 830  HIS A CA  1 
ATOM   6413  C  C   A HIS A 1 830  ? 114.756 66.587  121.816 0.50 46.50  ? 830  HIS A C   1 
ATOM   6414  C  C   B HIS A 1 830  ? 114.727 66.541  121.862 0.50 46.60  ? 830  HIS A C   1 
ATOM   6415  O  O   A HIS A 1 830  ? 115.955 66.773  122.022 0.50 47.47  ? 830  HIS A O   1 
ATOM   6416  O  O   B HIS A 1 830  ? 115.908 66.620  122.200 0.50 47.65  ? 830  HIS A O   1 
ATOM   6417  C  CB  A HIS A 1 830  ? 114.345 68.175  123.735 0.50 50.44  ? 830  HIS A CB  1 
ATOM   6418  C  CB  B HIS A 1 830  ? 114.240 68.302  123.594 0.50 50.49  ? 830  HIS A CB  1 
ATOM   6419  C  CG  A HIS A 1 830  ? 115.001 67.434  124.863 0.50 52.41  ? 830  HIS A CG  1 
ATOM   6420  C  CG  B HIS A 1 830  ? 114.247 69.704  123.066 0.50 51.67  ? 830  HIS A CG  1 
ATOM   6421  N  ND1 A HIS A 1 830  ? 114.431 67.324  126.113 0.50 54.26  ? 830  HIS A ND1 1 
ATOM   6422  N  ND1 B HIS A 1 830  ? 114.280 69.997  121.718 0.50 50.66  ? 830  HIS A ND1 1 
ATOM   6423  C  CD2 A HIS A 1 830  ? 116.176 66.761  124.926 0.50 52.73  ? 830  HIS A CD2 1 
ATOM   6424  C  CD2 B HIS A 1 830  ? 114.250 70.896  123.711 0.50 53.89  ? 830  HIS A CD2 1 
ATOM   6425  C  CE1 A HIS A 1 830  ? 115.225 66.617  126.897 0.50 55.71  ? 830  HIS A CE1 1 
ATOM   6426  C  CE1 B HIS A 1 830  ? 114.289 71.309  121.556 0.50 52.36  ? 830  HIS A CE1 1 
ATOM   6427  N  NE2 A HIS A 1 830  ? 116.291 66.263  126.200 0.50 55.01  ? 830  HIS A NE2 1 
ATOM   6428  N  NE2 B HIS A 1 830  ? 114.271 71.877  122.750 0.50 54.36  ? 830  HIS A NE2 1 
ATOM   6429  N  N   . LEU A 1 831  ? 114.304 65.820  120.829 1.00 44.38  ? 831  LEU A N   1 
ATOM   6430  C  CA  . LEU A 1 831  ? 115.197 65.030  119.981 1.00 42.67  ? 831  LEU A CA  1 
ATOM   6431  C  C   . LEU A 1 831  ? 116.005 65.818  118.940 1.00 41.85  ? 831  LEU A C   1 
ATOM   6432  O  O   . LEU A 1 831  ? 117.146 65.453  118.653 1.00 42.27  ? 831  LEU A O   1 
ATOM   6433  C  CB  . LEU A 1 831  ? 114.412 63.912  119.291 1.00 40.98  ? 831  LEU A CB  1 
ATOM   6434  C  CG  . LEU A 1 831  ? 113.971 62.725  120.149 1.00 41.09  ? 831  LEU A CG  1 
ATOM   6435  C  CD1 . LEU A 1 831  ? 112.982 61.864  119.392 1.00 39.68  ? 831  LEU A CD1 1 
ATOM   6436  C  CD2 . LEU A 1 831  ? 115.162 61.897  120.578 1.00 41.33  ? 831  LEU A CD2 1 
ATOM   6437  N  N   . LEU A 1 832  ? 115.430 66.876  118.369 1.00 40.65  ? 832  LEU A N   1 
ATOM   6438  C  CA  . LEU A 1 832  ? 116.121 67.620  117.308 1.00 39.69  ? 832  LEU A CA  1 
ATOM   6439  C  C   . LEU A 1 832  ? 116.630 68.993  117.734 1.00 41.06  ? 832  LEU A C   1 
ATOM   6440  O  O   . LEU A 1 832  ? 116.124 69.584  118.687 1.00 42.30  ? 832  LEU A O   1 
ATOM   6441  C  CB  . LEU A 1 832  ? 115.231 67.765  116.078 1.00 38.28  ? 832  LEU A CB  1 
ATOM   6442  C  CG  . LEU A 1 832  ? 114.491 66.527  115.570 1.00 36.25  ? 832  LEU A CG  1 
ATOM   6443  C  CD1 . LEU A 1 832  ? 113.721 66.884  114.314 1.00 34.48  ? 832  LEU A CD1 1 
ATOM   6444  C  CD2 . LEU A 1 832  ? 115.441 65.365  115.318 1.00 35.35  ? 832  LEU A CD2 1 
ATOM   6445  N  N   . GLY A 1 833  ? 117.644 69.481  117.019 1.00 41.07  ? 833  GLY A N   1 
ATOM   6446  C  CA  . GLY A 1 833  ? 118.216 70.807  117.237 1.00 42.27  ? 833  GLY A CA  1 
ATOM   6447  C  C   . GLY A 1 833  ? 117.711 71.785  116.192 1.00 41.91  ? 833  GLY A C   1 
ATOM   6448  O  O   . GLY A 1 833  ? 118.341 72.813  115.912 1.00 43.66  ? 833  GLY A O   1 
ATOM   6449  N  N   . VAL A 1 834  ? 116.548 71.462  115.634 1.00 39.65  ? 834  VAL A N   1 
ATOM   6450  C  CA  . VAL A 1 834  ? 115.951 72.201  114.544 1.00 38.44  ? 834  VAL A CA  1 
ATOM   6451  C  C   . VAL A 1 834  ? 114.454 72.400  114.902 1.00 37.86  ? 834  VAL A C   1 
ATOM   6452  O  O   . VAL A 1 834  ? 113.846 71.518  115.510 1.00 37.17  ? 834  VAL A O   1 
ATOM   6453  C  CB  . VAL A 1 834  ? 116.234 71.418  113.216 1.00 36.80  ? 834  VAL A CB  1 
ATOM   6454  C  CG1 . VAL A 1 834  ? 115.050 70.586  112.752 1.00 34.28  ? 834  VAL A CG1 1 
ATOM   6455  C  CG2 . VAL A 1 834  ? 116.726 72.338  112.132 1.00 37.64  ? 834  VAL A CG2 1 
ATOM   6456  N  N   . PRO A 1 835  ? 113.864 73.570  114.584 1.00 38.34  ? 835  PRO A N   1 
ATOM   6457  C  CA  . PRO A 1 835  ? 112.441 73.756  114.902 1.00 38.04  ? 835  PRO A CA  1 
ATOM   6458  C  C   . PRO A 1 835  ? 111.553 72.703  114.233 1.00 36.31  ? 835  PRO A C   1 
ATOM   6459  O  O   . PRO A 1 835  ? 111.947 72.108  113.219 1.00 35.12  ? 835  PRO A O   1 
ATOM   6460  C  CB  . PRO A 1 835  ? 112.132 75.148  114.332 1.00 39.01  ? 835  PRO A CB  1 
ATOM   6461  C  CG  . PRO A 1 835  ? 113.414 75.840  114.309 1.00 40.14  ? 835  PRO A CG  1 
ATOM   6462  C  CD  . PRO A 1 835  ? 114.426 74.773  113.951 1.00 39.88  ? 835  PRO A CD  1 
ATOM   6463  N  N   . THR A 1 836  ? 110.370 72.468  114.790 1.00 36.26  ? 836  THR A N   1 
ATOM   6464  C  CA  . THR A 1 836  ? 109.476 71.446  114.236 1.00 35.17  ? 836  THR A CA  1 
ATOM   6465  C  C   . THR A 1 836  ? 108.019 71.876  114.265 1.00 35.99  ? 836  THR A C   1 
ATOM   6466  O  O   . THR A 1 836  ? 107.158 71.099  114.665 1.00 35.62  ? 836  THR A O   1 
ATOM   6467  C  CB  . THR A 1 836  ? 109.562 70.114  115.015 1.00 34.56  ? 836  THR A CB  1 
ATOM   6468  O  OG1 . THR A 1 836  ? 109.316 70.357  116.407 1.00 35.07  ? 836  THR A OG1 1 
ATOM   6469  C  CG2 . THR A 1 836  ? 110.910 69.445  114.835 1.00 33.58  ? 836  THR A CG2 1 
ATOM   6470  N  N   . GLY A 1 837  ? 107.739 73.102  113.835 1.00 37.26  ? 837  GLY A N   1 
ATOM   6471  C  CA  . GLY A 1 837  ? 106.397 73.635  113.934 1.00 38.86  ? 837  GLY A CA  1 
ATOM   6472  C  C   . GLY A 1 837  ? 105.444 73.378  112.783 1.00 39.23  ? 837  GLY A C   1 
ATOM   6473  O  O   . GLY A 1 837  ? 104.437 74.073  112.676 1.00 40.85  ? 837  GLY A O   1 
ATOM   6474  N  N   . CYS A 1 838  ? 105.746 72.410  111.917 1.00 38.22  ? 838  CYS A N   1 
ATOM   6475  C  CA  . CYS A 1 838  ? 104.883 72.090  110.789 1.00 38.62  ? 838  CYS A CA  1 
ATOM   6476  C  C   . CYS A 1 838  ? 104.288 70.695  110.957 1.00 37.84  ? 838  CYS A C   1 
ATOM   6477  O  O   . CYS A 1 838  ? 104.861 69.850  111.651 1.00 37.66  ? 838  CYS A O   1 
ATOM   6478  C  CB  . CYS A 1 838  ? 105.672 72.128  109.478 1.00 38.15  ? 838  CYS A CB  1 
ATOM   6479  S  SG  . CYS A 1 838  ? 106.603 70.564  109.155 1.00 39.35  ? 838  CYS A SG  1 
ATOM   6480  N  N   . GLY A 1 839  ? 103.173 70.441  110.272 1.00 37.86  ? 839  GLY A N   1 
ATOM   6481  C  CA  . GLY A 1 839  ? 102.471 69.166  110.359 1.00 37.40  ? 839  GLY A CA  1 
ATOM   6482  C  C   . GLY A 1 839  ? 103.347 67.926  110.306 1.00 36.54  ? 839  GLY A C   1 
ATOM   6483  O  O   . GLY A 1 839  ? 103.179 67.021  111.116 1.00 36.61  ? 839  GLY A O   1 
ATOM   6484  N  N   . GLU A 1 840  ? 104.279 67.873  109.355 1.00 35.92  ? 840  GLU A N   1 
ATOM   6485  C  CA  . GLU A 1 840  ? 105.152 66.715  109.227 1.00 35.01  ? 840  GLU A CA  1 
ATOM   6486  C  C   . GLU A 1 840  ? 106.135 66.679  110.383 1.00 35.51  ? 840  GLU A C   1 
ATOM   6487  O  O   . GLU A 1 840  ? 106.324 65.636  111.014 1.00 35.56  ? 840  GLU A O   1 
ATOM   6488  C  CB  . GLU A 1 840  ? 105.915 66.733  107.903 1.00 34.15  ? 840  GLU A CB  1 
ATOM   6489  C  CG  . GLU A 1 840  ? 106.738 65.467  107.648 1.00 33.16  ? 840  GLU A CG  1 
ATOM   6490  C  CD  . GLU A 1 840  ? 108.138 65.490  108.291 1.00 34.14  ? 840  GLU A CD  1 
ATOM   6491  O  OE1 . GLU A 1 840  ? 108.791 66.558  108.313 1.00 33.54  ? 840  GLU A OE1 1 
ATOM   6492  O  OE2 . GLU A 1 840  ? 108.598 64.424  108.754 1.00 34.13  ? 840  GLU A OE2 1 
ATOM   6493  N  N   . GLN A 1 841  ? 106.769 67.820  110.647 1.00 36.09  ? 841  GLN A N   1 
ATOM   6494  C  CA  . GLN A 1 841  ? 107.830 67.870  111.636 1.00 36.00  ? 841  GLN A CA  1 
ATOM   6495  C  C   . GLN A 1 841  ? 107.274 67.502  113.000 1.00 36.43  ? 841  GLN A C   1 
ATOM   6496  O  O   . GLN A 1 841  ? 107.941 66.880  113.822 1.00 36.14  ? 841  GLN A O   1 
ATOM   6497  C  CB  . GLN A 1 841  ? 108.451 69.262  111.697 1.00 36.99  ? 841  GLN A CB  1 
ATOM   6498  C  CG  . GLN A 1 841  ? 108.910 69.821  110.377 1.00 36.50  ? 841  GLN A CG  1 
ATOM   6499  C  CD  . GLN A 1 841  ? 108.095 71.024  109.947 1.00 37.43  ? 841  GLN A CD  1 
ATOM   6500  O  OE1 . GLN A 1 841  ? 108.117 72.102  110.548 1.00 34.85  ? 841  GLN A OE1 1 
ATOM   6501  N  N   . ASN A 1 842  ? 106.027 67.876  113.221 1.00 37.00  ? 842  ASN A N   1 
ATOM   6502  C  CA  . ASN A 1 842  ? 105.423 67.704  114.518 1.00 37.94  ? 842  ASN A CA  1 
ATOM   6503  C  C   . ASN A 1 842  ? 105.279 66.258  114.951 1.00 37.48  ? 842  ASN A C   1 
ATOM   6504  O  O   . ASN A 1 842  ? 105.021 65.969  116.115 1.00 38.29  ? 842  ASN A O   1 
ATOM   6505  C  CB  . ASN A 1 842  ? 104.089 68.409  114.563 1.00 38.90  ? 842  ASN A CB  1 
ATOM   6506  C  CG  . ASN A 1 842  ? 103.938 69.196  115.802 1.00 40.93  ? 842  ASN A CG  1 
ATOM   6507  O  OD1 . ASN A 1 842  ? 104.170 68.679  116.889 1.00 41.72  ? 842  ASN A OD1 1 
ATOM   6508  N  ND2 . ASN A 1 842  ? 103.601 70.478  115.663 1.00 42.81  ? 842  ASN A ND2 1 
ATOM   6509  N  N   . MET A 1 843  ? 105.472 65.347  114.012 1.00 36.16  ? 843  MET A N   1 
ATOM   6510  C  CA  . MET A 1 843  ? 105.450 63.943  114.334 1.00 36.07  ? 843  MET A CA  1 
ATOM   6511  C  C   . MET A 1 843  ? 106.647 63.442  115.162 1.00 36.43  ? 843  MET A C   1 
ATOM   6512  O  O   . MET A 1 843  ? 106.618 62.287  115.596 1.00 36.79  ? 843  MET A O   1 
ATOM   6513  C  CB  . MET A 1 843  ? 105.254 63.127  113.071 1.00 35.01  ? 843  MET A CB  1 
ATOM   6514  C  CG  . MET A 1 843  ? 103.871 63.327  112.458 1.00 36.20  ? 843  MET A CG  1 
ATOM   6515  S  SD  . MET A 1 843  ? 102.530 62.584  113.420 1.00 38.84  ? 843  MET A SD  1 
ATOM   6516  C  CE  . MET A 1 843  ? 102.630 60.886  112.866 1.00 36.43  ? 843  MET A CE  1 
ATOM   6517  N  N   . VAL A 1 844  ? 107.670 64.284  115.402 1.00 36.60  ? 844  VAL A N   1 
ATOM   6518  C  CA  . VAL A 1 844  ? 108.763 63.921  116.346 1.00 37.70  ? 844  VAL A CA  1 
ATOM   6519  C  C   . VAL A 1 844  ? 108.248 63.712  117.752 1.00 39.00  ? 844  VAL A C   1 
ATOM   6520  O  O   . VAL A 1 844  ? 108.915 63.106  118.578 1.00 39.91  ? 844  VAL A O   1 
ATOM   6521  C  CB  . VAL A 1 844  ? 109.895 64.981  116.519 1.00 37.97  ? 844  VAL A CB  1 
ATOM   6522  C  CG1 . VAL A 1 844  ? 111.023 64.723  115.574 1.00 38.06  ? 844  VAL A CG1 1 
ATOM   6523  C  CG2 . VAL A 1 844  ? 109.373 66.403  116.438 1.00 38.18  ? 844  VAL A CG2 1 
ATOM   6524  N  N   . LYS A 1 845  ? 107.077 64.262  118.019 1.00 39.64  ? 845  LYS A N   1 
ATOM   6525  C  CA  . LYS A 1 845  ? 106.479 64.200  119.327 1.00 41.49  ? 845  LYS A CA  1 
ATOM   6526  C  C   . LYS A 1 845  ? 105.511 63.033  119.434 1.00 41.44  ? 845  LYS A C   1 
ATOM   6527  O  O   . LYS A 1 845  ? 104.821 62.893  120.446 1.00 42.72  ? 845  LYS A O   1 
ATOM   6528  C  CB  . LYS A 1 845  ? 105.795 65.531  119.624 1.00 42.63  ? 845  LYS A CB  1 
ATOM   6529  C  CG  . LYS A 1 845  ? 106.716 66.484  120.384 1.00 46.37  ? 845  LYS A CG  1 
ATOM   6530  C  CD  . LYS A 1 845  ? 106.738 67.887  119.787 1.00 50.55  ? 845  LYS A CD  1 
ATOM   6531  C  CE  . LYS A 1 845  ? 107.654 68.822  120.600 1.00 53.89  ? 845  LYS A CE  1 
ATOM   6532  N  NZ  . LYS A 1 845  ? 109.063 68.323  120.726 1.00 54.67  ? 845  LYS A NZ  1 
ATOM   6533  N  N   . PHE A 1 846  ? 105.499 62.189  118.396 1.00 39.74  ? 846  PHE A N   1 
ATOM   6534  C  CA  . PHE A 1 846  ? 104.540 61.100  118.264 1.00 39.77  ? 846  PHE A CA  1 
ATOM   6535  C  C   . PHE A 1 846  ? 105.243 59.797  117.853 1.00 39.48  ? 846  PHE A C   1 
ATOM   6536  O  O   . PHE A 1 846  ? 105.314 58.840  118.632 1.00 40.33  ? 846  PHE A O   1 
ATOM   6537  C  CB  . PHE A 1 846  ? 103.470 61.490  117.239 1.00 39.08  ? 846  PHE A CB  1 
ATOM   6538  C  CG  . PHE A 1 846  ? 102.249 60.618  117.261 1.00 39.53  ? 846  PHE A CG  1 
ATOM   6539  C  CD1 . PHE A 1 846  ? 101.291 60.768  118.233 1.00 42.28  ? 846  PHE A CD1 1 
ATOM   6540  C  CD2 . PHE A 1 846  ? 102.052 59.656  116.294 1.00 40.57  ? 846  PHE A CD2 1 
ATOM   6541  C  CE1 . PHE A 1 846  ? 100.157 59.956  118.254 1.00 43.95  ? 846  PHE A CE1 1 
ATOM   6542  C  CE2 . PHE A 1 846  ? 100.921 58.842  116.305 1.00 41.38  ? 846  PHE A CE2 1 
ATOM   6543  C  CZ  . PHE A 1 846  ? 99.976  58.997  117.286 1.00 42.44  ? 846  PHE A CZ  1 
ATOM   6544  N  N   . VAL A 1 847  ? 105.790 59.778  116.639 1.00 37.88  ? 847  VAL A N   1 
ATOM   6545  C  CA  . VAL A 1 847  ? 106.390 58.573  116.078 1.00 37.36  ? 847  VAL A CA  1 
ATOM   6546  C  C   . VAL A 1 847  ? 107.508 57.954  116.922 1.00 38.58  ? 847  VAL A C   1 
ATOM   6547  O  O   . VAL A 1 847  ? 107.478 56.749  117.168 1.00 39.42  ? 847  VAL A O   1 
ATOM   6548  C  CB  . VAL A 1 847  ? 106.844 58.787  114.618 1.00 35.61  ? 847  VAL A CB  1 
ATOM   6549  C  CG1 . VAL A 1 847  ? 107.556 57.561  114.080 1.00 33.25  ? 847  VAL A CG1 1 
ATOM   6550  C  CG2 . VAL A 1 847  ? 105.639 59.100  113.767 1.00 35.51  ? 847  VAL A CG2 1 
ATOM   6551  N  N   . PRO A 1 848  ? 108.503 58.754  117.351 1.00 39.06  ? 848  PRO A N   1 
ATOM   6552  C  CA  . PRO A 1 848  ? 109.578 58.176  118.149 1.00 40.31  ? 848  PRO A CA  1 
ATOM   6553  C  C   . PRO A 1 848  ? 109.074 57.421  119.371 1.00 42.45  ? 848  PRO A C   1 
ATOM   6554  O  O   . PRO A 1 848  ? 109.694 56.448  119.775 1.00 43.36  ? 848  PRO A O   1 
ATOM   6555  C  CB  . PRO A 1 848  ? 110.384 59.404  118.576 1.00 40.58  ? 848  PRO A CB  1 
ATOM   6556  C  CG  . PRO A 1 848  ? 110.178 60.355  117.464 1.00 39.13  ? 848  PRO A CG  1 
ATOM   6557  C  CD  . PRO A 1 848  ? 108.732 60.191  117.125 1.00 38.64  ? 848  PRO A CD  1 
ATOM   6558  N  N   . ASN A 1 849  ? 107.954 57.857  119.938 1.00 43.83  ? 849  ASN A N   1 
ATOM   6559  C  CA  . ASN A 1 849  ? 107.374 57.198  121.099 1.00 46.32  ? 849  ASN A CA  1 
ATOM   6560  C  C   . ASN A 1 849  ? 106.827 55.826  120.734 1.00 47.77  ? 849  ASN A C   1 
ATOM   6561  O  O   . ASN A 1 849  ? 106.917 54.882  121.525 1.00 49.63  ? 849  ASN A O   1 
ATOM   6562  C  CB  . ASN A 1 849  ? 106.278 58.066  121.699 1.00 46.85  ? 849  ASN A CB  1 
ATOM   6563  C  CG  . ASN A 1 849  ? 106.789 59.422  122.121 1.00 46.48  ? 849  ASN A CG  1 
ATOM   6564  O  OD1 . ASN A 1 849  ? 107.556 59.526  123.070 1.00 48.42  ? 849  ASN A OD1 1 
ATOM   6565  N  ND2 . ASN A 1 849  ? 106.387 60.466  121.408 1.00 44.23  ? 849  ASN A ND2 1 
ATOM   6566  N  N   . ILE A 1 850  ? 106.263 55.724  119.532 1.00 47.41  ? 850  ILE A N   1 
ATOM   6567  C  CA  . ILE A 1 850  ? 105.775 54.456  119.009 1.00 48.90  ? 850  ILE A CA  1 
ATOM   6568  C  C   . ILE A 1 850  ? 106.946 53.496  118.782 1.00 49.44  ? 850  ILE A C   1 
ATOM   6569  O  O   . ILE A 1 850  ? 106.891 52.345  119.207 1.00 50.80  ? 850  ILE A O   1 
ATOM   6570  C  CB  . ILE A 1 850  ? 104.982 54.650  117.687 1.00 47.93  ? 850  ILE A CB  1 
ATOM   6571  C  CG1 . ILE A 1 850  ? 103.729 55.493  117.924 1.00 48.28  ? 850  ILE A CG1 1 
ATOM   6572  C  CG2 . ILE A 1 850  ? 104.619 53.296  117.047 1.00 48.00  ? 850  ILE A CG2 1 
ATOM   6573  C  CD1 . ILE A 1 850  ? 103.165 56.076  116.640 1.00 48.03  ? 850  ILE A CD1 1 
ATOM   6574  N  N   . LEU A 1 851  ? 107.993 53.975  118.106 1.00 48.85  ? 851  LEU A N   1 
ATOM   6575  C  CA  . LEU A 1 851  ? 109.197 53.179  117.869 1.00 49.79  ? 851  LEU A CA  1 
ATOM   6576  C  C   . LEU A 1 851  ? 109.692 52.620  119.201 1.00 52.59  ? 851  LEU A C   1 
ATOM   6577  O  O   . LEU A 1 851  ? 109.801 51.405  119.375 1.00 54.00  ? 851  LEU A O   1 
ATOM   6578  C  CB  . LEU A 1 851  ? 110.279 54.020  117.177 1.00 48.06  ? 851  LEU A CB  1 
ATOM   6579  C  CG  . LEU A 1 851  ? 110.439 54.067  115.633 1.00 46.70  ? 851  LEU A CG  1 
ATOM   6580  C  CD1 . LEU A 1 851  ? 109.211 53.615  114.808 1.00 45.83  ? 851  LEU A CD1 1 
ATOM   6581  C  CD2 . LEU A 1 851  ? 110.931 55.437  115.152 1.00 43.71  ? 851  LEU A CD2 1 
ATOM   6582  N  N   . VAL A 1 852  ? 109.934 53.505  120.161 1.00 54.04  ? 852  VAL A N   1 
ATOM   6583  C  CA  . VAL A 1 852  ? 110.369 53.082  121.477 1.00 57.02  ? 852  VAL A CA  1 
ATOM   6584  C  C   . VAL A 1 852  ? 109.464 51.966  121.991 1.00 59.90  ? 852  VAL A C   1 
ATOM   6585  O  O   . VAL A 1 852  ? 109.941 50.853  122.227 1.00 61.45  ? 852  VAL A O   1 
ATOM   6586  C  CB  . VAL A 1 852  ? 110.454 54.272  122.460 1.00 57.41  ? 852  VAL A CB  1 
ATOM   6587  C  CG1 . VAL A 1 852  ? 110.612 53.797  123.891 1.00 59.53  ? 852  VAL A CG1 1 
ATOM   6588  C  CG2 . VAL A 1 852  ? 111.612 55.172  122.079 1.00 56.26  ? 852  VAL A CG2 1 
ATOM   6589  N  N   . LEU A 1 853  ? 108.165 52.247  122.113 1.00 61.39  ? 853  LEU A N   1 
ATOM   6590  C  CA  . LEU A 1 853  ? 107.219 51.309  122.734 1.00 64.64  ? 853  LEU A CA  1 
ATOM   6591  C  C   . LEU A 1 853  ? 107.166 49.966  122.021 1.00 65.88  ? 853  LEU A C   1 
ATOM   6592  O  O   . LEU A 1 853  ? 107.238 48.914  122.662 1.00 68.29  ? 853  LEU A O   1 
ATOM   6593  C  CB  . LEU A 1 853  ? 105.810 51.906  122.823 1.00 64.69  ? 853  LEU A CB  1 
ATOM   6594  C  CG  . LEU A 1 853  ? 105.568 53.052  123.810 1.00 64.95  ? 853  LEU A CG  1 
ATOM   6595  C  CD1 . LEU A 1 853  ? 104.250 53.761  123.533 1.00 63.74  ? 853  LEU A CD1 1 
ATOM   6596  C  CD2 . LEU A 1 853  ? 105.623 52.584  125.238 1.00 66.69  ? 853  LEU A CD2 1 
ATOM   6597  N  N   . ASP A 1 854  ? 107.063 49.997  120.698 1.00 65.03  ? 854  ASP A N   1 
ATOM   6598  C  CA  . ASP A 1 854  ? 106.921 48.757  119.952 1.00 66.62  ? 854  ASP A CA  1 
ATOM   6599  C  C   . ASP A 1 854  ? 108.245 47.993  119.778 1.00 67.35  ? 854  ASP A C   1 
ATOM   6600  O  O   . ASP A 1 854  ? 108.243 46.813  119.394 1.00 68.72  ? 854  ASP A O   1 
ATOM   6601  C  CB  . ASP A 1 854  ? 106.141 48.962  118.638 1.00 64.98  ? 854  ASP A CB  1 
ATOM   6602  C  CG  . ASP A 1 854  ? 106.966 49.596  117.559 1.00 63.75  ? 854  ASP A CG  1 
ATOM   6603  O  OD1 . ASP A 1 854  ? 108.208 49.604  117.695 1.00 64.98  ? 854  ASP A OD1 1 
ATOM   6604  O  OD2 . ASP A 1 854  ? 106.372 50.075  116.566 1.00 63.13  ? 854  ASP A OD2 1 
ATOM   6605  N  N   . TYR A 1 855  ? 109.364 48.658  120.072 1.00 67.33  ? 855  TYR A N   1 
ATOM   6606  C  CA  . TYR A 1 855  ? 110.651 47.961  120.212 1.00 68.46  ? 855  TYR A CA  1 
ATOM   6607  C  C   . TYR A 1 855  ? 110.771 47.287  121.576 1.00 71.59  ? 855  TYR A C   1 
ATOM   6608  O  O   . TYR A 1 855  ? 111.121 46.108  121.658 1.00 73.51  ? 855  TYR A O   1 
ATOM   6609  C  CB  . TYR A 1 855  ? 111.860 48.881  119.992 1.00 66.75  ? 855  TYR A CB  1 
ATOM   6610  C  CG  . TYR A 1 855  ? 113.137 48.322  120.607 1.00 68.38  ? 855  TYR A CG  1 
ATOM   6611  C  CD1 . TYR A 1 855  ? 114.026 47.550  119.849 1.00 68.34  ? 855  TYR A CD1 1 
ATOM   6612  C  CD2 . TYR A 1 855  ? 113.438 48.537  121.959 1.00 69.14  ? 855  TYR A CD2 1 
ATOM   6613  C  CE1 . TYR A 1 855  ? 115.188 47.020  120.422 1.00 69.56  ? 855  TYR A CE1 1 
ATOM   6614  C  CE2 . TYR A 1 855  ? 114.583 48.019  122.534 1.00 70.76  ? 855  TYR A CE2 1 
ATOM   6615  C  CZ  . TYR A 1 855  ? 115.457 47.264  121.768 1.00 71.21  ? 855  TYR A CZ  1 
ATOM   6616  O  OH  . TYR A 1 855  ? 116.597 46.762  122.354 1.00 72.50  ? 855  TYR A OH  1 
ATOM   6617  N  N   . LEU A 1 856  ? 110.513 48.029  122.648 1.00 72.71  ? 856  LEU A N   1 
ATOM   6618  C  CA  . LEU A 1 856  ? 110.670 47.447  123.976 1.00 76.11  ? 856  LEU A CA  1 
ATOM   6619  C  C   . LEU A 1 856  ? 109.550 46.465  124.300 1.00 78.47  ? 856  LEU A C   1 
ATOM   6620  O  O   . LEU A 1 856  ? 109.585 45.800  125.332 1.00 81.39  ? 856  LEU A O   1 
ATOM   6621  C  CB  . LEU A 1 856  ? 110.839 48.517  125.064 1.00 76.72  ? 856  LEU A CB  1 
ATOM   6622  C  CG  . LEU A 1 856  ? 109.860 49.686  125.153 1.00 76.19  ? 856  LEU A CG  1 
ATOM   6623  C  CD1 . LEU A 1 856  ? 108.494 49.219  125.636 1.00 78.90  ? 856  LEU A CD1 1 
ATOM   6624  C  CD2 . LEU A 1 856  ? 110.422 50.752  126.072 1.00 76.76  ? 856  LEU A CD2 1 
ATOM   6625  N  N   . HIS A 1 857  ? 108.562 46.371  123.413 1.00 77.90  ? 857  HIS A N   1 
ATOM   6626  C  CA  . HIS A 1 857  ? 107.582 45.292  123.503 1.00 80.41  ? 857  HIS A CA  1 
ATOM   6627  C  C   . HIS A 1 857  ? 108.120 44.028  122.832 1.00 81.01  ? 857  HIS A C   1 
ATOM   6628  O  O   . HIS A 1 857  ? 108.035 42.936  123.398 1.00 83.56  ? 857  HIS A O   1 
ATOM   6629  C  CB  . HIS A 1 857  ? 106.233 45.688  122.900 1.00 79.64  ? 857  HIS A CB  1 
ATOM   6630  C  CG  . HIS A 1 857  ? 105.082 44.915  123.467 1.00 82.97  ? 857  HIS A CG  1 
ATOM   6631  N  ND1 . HIS A 1 857  ? 104.508 43.844  122.815 1.00 83.89  ? 857  HIS A ND1 1 
ATOM   6632  C  CD2 . HIS A 1 857  ? 104.417 45.043  124.642 1.00 85.38  ? 857  HIS A CD2 1 
ATOM   6633  C  CE1 . HIS A 1 857  ? 103.528 43.356  123.556 1.00 87.18  ? 857  HIS A CE1 1 
ATOM   6634  N  NE2 . HIS A 1 857  ? 103.453 44.064  124.670 1.00 88.00  ? 857  HIS A NE2 1 
ATOM   6635  N  N   . ALA A 1 858  ? 108.683 44.197  121.635 1.00 78.73  ? 858  ALA A N   1 
ATOM   6636  C  CA  . ALA A 1 858  ? 109.305 43.104  120.884 1.00 79.32  ? 858  ALA A CA  1 
ATOM   6637  C  C   . ALA A 1 858  ? 110.447 42.426  121.649 1.00 81.44  ? 858  ALA A C   1 
ATOM   6638  O  O   . ALA A 1 858  ? 110.661 41.218  121.495 1.00 83.38  ? 858  ALA A O   1 
ATOM   6639  C  CB  . ALA A 1 858  ? 109.785 43.587  119.520 1.00 76.44  ? 858  ALA A CB  1 
ATOM   6640  N  N   . ILE A 1 859  ? 111.178 43.193  122.462 1.00 81.23  ? 859  ILE A N   1 
ATOM   6641  C  CA  . ILE A 1 859  ? 112.184 42.600  123.354 1.00 83.37  ? 859  ILE A CA  1 
ATOM   6642  C  C   . ILE A 1 859  ? 111.599 42.271  124.726 1.00 86.31  ? 859  ILE A C   1 
ATOM   6643  O  O   . ILE A 1 859  ? 112.299 41.746  125.586 1.00 88.83  ? 859  ILE A O   1 
ATOM   6644  C  CB  . ILE A 1 859  ? 113.498 43.446  123.480 1.00 82.03  ? 859  ILE A CB  1 
ATOM   6645  C  CG1 . ILE A 1 859  ? 113.283 44.705  124.333 1.00 81.83  ? 859  ILE A CG1 1 
ATOM   6646  C  CG2 . ILE A 1 859  ? 114.083 43.757  122.092 1.00 79.02  ? 859  ILE A CG2 1 
ATOM   6647  C  CD1 . ILE A 1 859  ? 114.553 45.243  124.994 1.00 81.80  ? 859  ILE A CD1 1 
ATOM   6648  N  N   . GLY A 1 860  ? 110.317 42.582  124.916 1.00 86.44  ? 860  GLY A N   1 
ATOM   6649  C  CA  . GLY A 1 860  ? 109.601 42.285  126.158 1.00 89.51  ? 860  GLY A CA  1 
ATOM   6650  C  C   . GLY A 1 860  ? 110.212 42.900  127.399 1.00 90.74  ? 860  GLY A C   1 
ATOM   6651  O  O   . GLY A 1 860  ? 110.222 42.276  128.457 1.00 93.88  ? 860  GLY A O   1 
ATOM   6652  N  N   . SER A 1 861  ? 110.718 44.125  127.266 1.00 88.58  ? 861  SER A N   1 
ATOM   6653  C  CA  . SER A 1 861  ? 111.364 44.839  128.369 1.00 89.82  ? 861  SER A CA  1 
ATOM   6654  C  C   . SER A 1 861  ? 110.416 45.071  129.537 1.00 92.31  ? 861  SER A C   1 
ATOM   6655  O  O   . SER A 1 861  ? 109.216 45.261  129.346 1.00 92.02  ? 861  SER A O   1 
ATOM   6656  C  CB  . SER A 1 861  ? 111.940 46.178  127.895 1.00 86.83  ? 861  SER A CB  1 
ATOM   6657  O  OG  . SER A 1 861  ? 112.452 46.935  128.986 1.00 87.84  ? 861  SER A OG  1 
ATOM   6658  N  N   . LYS A 1 862  ? 110.976 45.056  130.742 1.00 95.10  ? 862  LYS A N   1 
ATOM   6659  C  CA  . LYS A 1 862  ? 110.203 45.223  131.968 1.00 98.17  ? 862  LYS A CA  1 
ATOM   6660  C  C   . LYS A 1 862  ? 110.551 46.541  132.671 1.00 97.60  ? 862  LYS A C   1 
ATOM   6661  O  O   . LYS A 1 862  ? 110.098 46.794  133.792 1.00 100.19 ? 862  LYS A O   1 
ATOM   6662  C  CB  . LYS A 1 862  ? 110.441 44.030  132.908 1.00 102.47 ? 862  LYS A CB  1 
ATOM   6663  C  CG  . LYS A 1 862  ? 109.202 43.566  133.703 1.00 106.77 ? 862  LYS A CG  1 
ATOM   6664  C  CD  . LYS A 1 862  ? 108.461 42.391  133.022 1.00 108.91 ? 862  LYS A CD  1 
ATOM   6665  C  CE  . LYS A 1 862  ? 107.651 42.815  131.780 1.00 105.93 ? 862  LYS A CE  1 
ATOM   6666  N  NZ  . LYS A 1 862  ? 106.955 41.660  131.135 1.00 106.97 ? 862  LYS A NZ  1 
ATOM   6667  N  N   . GLU A 1 863  ? 111.355 47.374  132.006 1.00 94.53  ? 863  GLU A N   1 
ATOM   6668  C  CA  . GLU A 1 863  ? 111.780 48.665  132.556 1.00 93.67  ? 863  GLU A CA  1 
ATOM   6669  C  C   . GLU A 1 863  ? 110.610 49.637  132.516 1.00 92.41  ? 863  GLU A C   1 
ATOM   6670  O  O   . GLU A 1 863  ? 110.469 50.422  131.574 1.00 89.34  ? 863  GLU A O   1 
ATOM   6671  C  CB  . GLU A 1 863  ? 112.984 49.219  131.785 1.00 91.05  ? 863  GLU A CB  1 
ATOM   6672  C  CG  . GLU A 1 863  ? 114.182 48.275  131.753 1.00 91.88  ? 863  GLU A CG  1 
ATOM   6673  C  CD  . GLU A 1 863  ? 115.425 48.897  131.148 1.00 89.01  ? 863  GLU A CD  1 
ATOM   6674  O  OE1 . GLU A 1 863  ? 115.888 49.942  131.659 1.00 88.51  ? 863  GLU A OE1 1 
ATOM   6675  O  OE2 . GLU A 1 863  ? 115.948 48.323  130.170 1.00 87.21  ? 863  GLU A OE2 1 
ATOM   6676  N  N   . GLN A 1 864  ? 109.772 49.569  133.547 1.00 94.85  ? 864  GLN A N   1 
ATOM   6677  C  CA  . GLN A 1 864  ? 108.482 50.251  133.548 1.00 94.32  ? 864  GLN A CA  1 
ATOM   6678  C  C   . GLN A 1 864  ? 108.600 51.749  133.315 1.00 91.95  ? 864  GLN A C   1 
ATOM   6679  O  O   . GLN A 1 864  ? 107.844 52.309  132.517 1.00 89.92  ? 864  GLN A O   1 
ATOM   6680  C  CB  . GLN A 1 864  ? 107.700 49.956  134.834 1.00 98.30  ? 864  GLN A CB  1 
ATOM   6681  C  CG  . GLN A 1 864  ? 106.206 50.324  134.784 1.00 98.70  ? 864  GLN A CG  1 
ATOM   6682  C  CD  . GLN A 1 864  ? 105.465 49.728  133.584 1.00 97.26  ? 864  GLN A CD  1 
ATOM   6683  O  OE1 . GLN A 1 864  ? 105.737 48.606  133.151 1.00 97.44  ? 864  GLN A OE1 1 
ATOM   6684  N  NE2 . GLN A 1 864  ? 104.519 50.486  133.050 1.00 95.98  ? 864  GLN A NE2 1 
ATOM   6685  N  N   . HIS A 1 865  ? 109.556 52.388  133.989 1.00 92.34  ? 865  HIS A N   1 
ATOM   6686  C  CA  . HIS A 1 865  ? 109.753 53.832  133.853 1.00 90.49  ? 865  HIS A CA  1 
ATOM   6687  C  C   . HIS A 1 865  ? 109.794 54.271  132.385 1.00 86.04  ? 865  HIS A C   1 
ATOM   6688  O  O   . HIS A 1 865  ? 109.176 55.267  132.010 1.00 84.62  ? 865  HIS A O   1 
ATOM   6689  C  CB  . HIS A 1 865  ? 111.018 54.300  134.589 1.00 92.00  ? 865  HIS A CB  1 
ATOM   6690  C  CG  . HIS A 1 865  ? 111.323 55.755  134.390 1.00 91.82  ? 865  HIS A CG  1 
ATOM   6691  N  ND1 . HIS A 1 865  ? 110.786 56.745  135.188 1.00 94.31  ? 865  HIS A ND1 1 
ATOM   6692  C  CD2 . HIS A 1 865  ? 112.090 56.389  133.468 1.00 90.08  ? 865  HIS A CD2 1 
ATOM   6693  C  CE1 . HIS A 1 865  ? 111.215 57.924  134.770 1.00 93.34  ? 865  HIS A CE1 1 
ATOM   6694  N  NE2 . HIS A 1 865  ? 112.006 57.736  133.727 1.00 90.48  ? 865  HIS A NE2 1 
ATOM   6695  N  N   . LEU A 1 866  ? 110.511 53.509  131.564 1.00 83.89  ? 866  LEU A N   1 
ATOM   6696  C  CA  . LEU A 1 866  ? 110.693 53.847  130.158 1.00 79.76  ? 866  LEU A CA  1 
ATOM   6697  C  C   . LEU A 1 866  ? 109.396 53.773  129.364 1.00 77.98  ? 866  LEU A C   1 
ATOM   6698  O  O   . LEU A 1 866  ? 109.077 54.692  128.617 1.00 76.19  ? 866  LEU A O   1 
ATOM   6699  C  CB  . LEU A 1 866  ? 111.765 52.964  129.522 1.00 78.86  ? 866  LEU A CB  1 
ATOM   6700  C  CG  . LEU A 1 866  ? 113.122 52.903  130.228 1.00 80.25  ? 866  LEU A CG  1 
ATOM   6701  C  CD1 . LEU A 1 866  ? 114.081 52.006  129.462 1.00 79.21  ? 866  LEU A CD1 1 
ATOM   6702  C  CD2 . LEU A 1 866  ? 113.713 54.288  130.403 1.00 79.48  ? 866  LEU A CD2 1 
ATOM   6703  N  N   . ILE A 1 867  ? 108.652 52.683  129.532 1.00 78.82  ? 867  ILE A N   1 
ATOM   6704  C  CA  . ILE A 1 867  ? 107.377 52.493  128.831 1.00 77.12  ? 867  ILE A CA  1 
ATOM   6705  C  C   . ILE A 1 867  ? 106.390 53.602  129.209 1.00 76.52  ? 867  ILE A C   1 
ATOM   6706  O  O   . ILE A 1 867  ? 105.748 54.184  128.332 1.00 74.61  ? 867  ILE A O   1 
ATOM   6707  C  CB  . ILE A 1 867  ? 106.765 51.089  129.101 1.00 79.58  ? 867  ILE A CB  1 
ATOM   6708  C  CG1 . ILE A 1 867  ? 107.778 49.989  128.776 1.00 79.53  ? 867  ILE A CG1 1 
ATOM   6709  C  CG2 . ILE A 1 867  ? 105.487 50.876  128.287 1.00 78.88  ? 867  ILE A CG2 1 
ATOM   6710  C  CD1 . ILE A 1 867  ? 107.414 48.621  129.323 1.00 82.53  ? 867  ILE A CD1 1 
ATOM   6711  N  N   . ASP A 1 868  ? 106.299 53.904  130.504 1.00 77.77  ? 868  ASP A N   1 
ATOM   6712  C  CA  . ASP A 1 868  ? 105.441 54.984  130.996 1.00 77.46  ? 868  ASP A CA  1 
ATOM   6713  C  C   . ASP A 1 868  ? 105.748 56.311  130.309 1.00 74.08  ? 868  ASP A C   1 
ATOM   6714  O  O   . ASP A 1 868  ? 104.836 57.026  129.894 1.00 73.32  ? 868  ASP A O   1 
ATOM   6715  C  CB  . ASP A 1 868  ? 105.578 55.148  132.518 1.00 80.63  ? 868  ASP A CB  1 
ATOM   6716  C  CG  . ASP A 1 868  ? 104.831 54.072  133.304 1.00 84.19  ? 868  ASP A CG  1 
ATOM   6717  O  OD1 . ASP A 1 868  ? 104.319 53.112  132.687 1.00 83.75  ? 868  ASP A OD1 1 
ATOM   6718  O  OD2 . ASP A 1 868  ? 104.756 54.189  134.550 1.00 87.58  ? 868  ASP A OD2 1 
ATOM   6719  N  N   . LYS A 1 869  ? 107.035 56.625  130.186 1.00 71.93  ? 869  LYS A N   1 
ATOM   6720  C  CA  . LYS A 1 869  ? 107.478 57.900  129.639 1.00 68.92  ? 869  LYS A CA  1 
ATOM   6721  C  C   . LYS A 1 869  ? 107.017 58.061  128.196 1.00 65.78  ? 869  LYS A C   1 
ATOM   6722  O  O   . LYS A 1 869  ? 106.355 59.041  127.852 1.00 64.77  ? 869  LYS A O   1 
ATOM   6723  C  CB  . LYS A 1 869  ? 109.000 58.013  129.725 1.00 68.48  ? 869  LYS A CB  1 
ATOM   6724  C  CG  . LYS A 1 869  ? 109.507 59.431  129.627 1.00 66.93  ? 869  LYS A CG  1 
ATOM   6725  C  CD  . LYS A 1 869  ? 110.968 59.471  129.259 1.00 64.85  ? 869  LYS A CD  1 
ATOM   6726  C  CE  . LYS A 1 869  ? 111.444 60.899  129.165 1.00 63.78  ? 869  LYS A CE  1 
ATOM   6727  N  NZ  . LYS A 1 869  ? 112.841 60.972  128.695 1.00 62.82  ? 869  LYS A NZ  1 
ATOM   6728  N  N   . ALA A 1 870  ? 107.360 57.082  127.363 1.00 64.12  ? 870  ALA A N   1 
ATOM   6729  C  CA  . ALA A 1 870  ? 106.958 57.069  125.960 1.00 61.42  ? 870  ALA A CA  1 
ATOM   6730  C  C   . ALA A 1 870  ? 105.436 57.075  125.802 1.00 61.56  ? 870  ALA A C   1 
ATOM   6731  O  O   . ALA A 1 870  ? 104.911 57.724  124.903 1.00 60.02  ? 870  ALA A O   1 
ATOM   6732  C  CB  . ALA A 1 870  ? 107.576 55.879  125.239 1.00 60.58  ? 870  ALA A CB  1 
ATOM   6733  N  N   . THR A 1 871  ? 104.741 56.367  126.691 1.00 63.70  ? 871  THR A N   1 
ATOM   6734  C  CA  . THR A 1 871  ? 103.274 56.332  126.712 1.00 64.24  ? 871  THR A CA  1 
ATOM   6735  C  C   . THR A 1 871  ? 102.672 57.714  126.962 1.00 63.75  ? 871  THR A C   1 
ATOM   6736  O  O   . THR A 1 871  ? 101.813 58.168  126.212 1.00 62.91  ? 871  THR A O   1 
ATOM   6737  C  CB  . THR A 1 871  ? 102.743 55.320  127.762 1.00 67.32  ? 871  THR A CB  1 
ATOM   6738  O  OG1 . THR A 1 871  ? 103.188 53.998  127.421 1.00 67.51  ? 871  THR A OG1 1 
ATOM   6739  C  CG2 . THR A 1 871  ? 101.218 55.334  127.820 1.00 68.46  ? 871  THR A CG2 1 
ATOM   6740  N  N   . ASN A 1 872  ? 103.144 58.381  128.004 1.00 64.46  ? 872  ASN A N   1 
ATOM   6741  C  CA  . ASN A 1 872  ? 102.615 59.685  128.378 1.00 64.60  ? 872  ASN A CA  1 
ATOM   6742  C  C   . ASN A 1 872  ? 102.813 60.725  127.289 1.00 61.46  ? 872  ASN A C   1 
ATOM   6743  O  O   . ASN A 1 872  ? 101.896 61.480  126.976 1.00 61.32  ? 872  ASN A O   1 
ATOM   6744  C  CB  . ASN A 1 872  ? 103.258 60.159  129.679 1.00 66.83  ? 872  ASN A CB  1 
ATOM   6745  C  CG  . ASN A 1 872  ? 102.490 61.286  130.331 1.00 69.53  ? 872  ASN A CG  1 
ATOM   6746  O  OD1 . ASN A 1 872  ? 102.265 62.339  129.728 1.00 70.04  ? 872  ASN A OD1 1 
ATOM   6747  N  ND2 . ASN A 1 872  ? 102.089 61.075  131.580 1.00 72.97  ? 872  ASN A ND2 1 
ATOM   6748  N  N   . LEU A 1 873  ? 104.009 60.747  126.708 1.00 58.92  ? 873  LEU A N   1 
ATOM   6749  C  CA  . LEU A 1 873  ? 104.352 61.727  125.691 1.00 56.00  ? 873  LEU A CA  1 
ATOM   6750  C  C   . LEU A 1 873  ? 103.603 61.461  124.401 1.00 54.40  ? 873  LEU A C   1 
ATOM   6751  O  O   . LEU A 1 873  ? 103.276 62.394  123.667 1.00 53.34  ? 873  LEU A O   1 
ATOM   6752  C  CB  . LEU A 1 873  ? 105.859 61.743  125.441 1.00 54.61  ? 873  LEU A CB  1 
ATOM   6753  C  CG  . LEU A 1 873  ? 106.737 62.364  126.530 1.00 55.13  ? 873  LEU A CG  1 
ATOM   6754  C  CD1 . LEU A 1 873  ? 108.199 62.030  126.285 1.00 53.14  ? 873  LEU A CD1 1 
ATOM   6755  C  CD2 . LEU A 1 873  ? 106.537 63.876  126.631 1.00 53.36  ? 873  LEU A CD2 1 
ATOM   6756  N  N   . LEU A 1 874  ? 103.335 60.185  124.128 1.00 54.42  ? 874  LEU A N   1 
ATOM   6757  C  CA  . LEU A 1 874  ? 102.523 59.795  122.981 1.00 53.31  ? 874  LEU A CA  1 
ATOM   6758  C  C   . LEU A 1 874  ? 101.135 60.403  123.106 1.00 54.47  ? 874  LEU A C   1 
ATOM   6759  O  O   . LEU A 1 874  ? 100.609 60.965  122.153 1.00 53.57  ? 874  LEU A O   1 
ATOM   6760  C  CB  . LEU A 1 874  ? 102.431 58.277  122.878 1.00 53.65  ? 874  LEU A CB  1 
ATOM   6761  C  CG  . LEU A 1 874  ? 101.880 57.649  121.596 1.00 52.58  ? 874  LEU A CG  1 
ATOM   6762  C  CD1 . LEU A 1 874  ? 102.698 58.042  120.393 1.00 50.61  ? 874  LEU A CD1 1 
ATOM   6763  C  CD2 . LEU A 1 874  ? 101.848 56.132  121.719 1.00 54.02  ? 874  LEU A CD2 1 
ATOM   6764  N  N   . ARG A 1 875  ? 100.562 60.312  124.299 1.00 56.82  ? 875  ARG A N   1 
ATOM   6765  C  CA  . ARG A 1 875  ? 99.289  60.950  124.586 1.00 58.43  ? 875  ARG A CA  1 
ATOM   6766  C  C   . ARG A 1 875  ? 99.345  62.458  124.293 1.00 57.14  ? 875  ARG A C   1 
ATOM   6767  O  O   . ARG A 1 875  ? 98.551  62.952  123.496 1.00 57.02  ? 875  ARG A O   1 
ATOM   6768  C  CB  . ARG A 1 875  ? 98.874  60.666  126.028 1.00 61.60  ? 875  ARG A CB  1 
ATOM   6769  C  CG  . ARG A 1 875  ? 97.383  60.762  126.277 1.00 65.68  ? 875  ARG A CG  1 
ATOM   6770  C  CD  . ARG A 1 875  ? 97.027  60.318  127.698 1.00 71.98  ? 875  ARG A CD  1 
ATOM   6771  N  NE  . ARG A 1 875  ? 97.210  58.875  127.883 1.00 75.28  ? 875  ARG A NE  1 
ATOM   6772  C  CZ  . ARG A 1 875  ? 98.103  58.318  128.703 1.00 77.68  ? 875  ARG A CZ  1 
ATOM   6773  N  NH1 . ARG A 1 875  ? 98.908  59.080  129.443 1.00 78.53  ? 875  ARG A NH1 1 
ATOM   6774  N  NH2 . ARG A 1 875  ? 98.186  56.991  128.797 1.00 78.38  ? 875  ARG A NH2 1 
ATOM   6775  N  N   . GLN A 1 876  ? 100.297 63.169  124.903 1.00 56.19  ? 876  GLN A N   1 
ATOM   6776  C  CA  . GLN A 1 876  ? 100.521 64.594  124.631 1.00 54.69  ? 876  GLN A CA  1 
ATOM   6777  C  C   . GLN A 1 876  ? 100.714 64.907  123.152 1.00 51.74  ? 876  GLN A C   1 
ATOM   6778  O  O   . GLN A 1 876  ? 100.294 65.964  122.676 1.00 51.42  ? 876  GLN A O   1 
ATOM   6779  C  CB  . GLN A 1 876  ? 101.751 65.085  125.380 1.00 55.19  ? 876  GLN A CB  1 
ATOM   6780  C  CG  . GLN A 1 876  ? 101.504 65.493  126.823 1.00 59.58  ? 876  GLN A CG  1 
ATOM   6781  C  CD  . GLN A 1 876  ? 102.748 66.092  127.481 1.00 61.39  ? 876  GLN A CD  1 
ATOM   6782  O  OE1 . GLN A 1 876  ? 103.651 66.595  126.797 1.00 59.50  ? 876  GLN A OE1 1 
ATOM   6783  N  NE2 . GLN A 1 876  ? 102.796 66.042  128.817 1.00 63.24  ? 876  GLN A NE2 1 
ATOM   6784  N  N   . GLY A 1 877  ? 101.375 63.993  122.439 1.00 49.23  ? 877  GLY A N   1 
ATOM   6785  C  CA  . GLY A 1 877  ? 101.612 64.126  121.004 1.00 46.07  ? 877  GLY A CA  1 
ATOM   6786  C  C   . GLY A 1 877  ? 100.363 63.979  120.149 1.00 45.16  ? 877  GLY A C   1 
ATOM   6787  O  O   . GLY A 1 877  ? 100.245 64.618  119.108 1.00 44.20  ? 877  GLY A O   1 
ATOM   6788  N  N   . TYR A 1 878  ? 99.427  63.140  120.583 1.00 45.64  ? 878  TYR A N   1 
ATOM   6789  C  CA  . TYR A 1 878  ? 98.143  63.021  119.903 1.00 45.28  ? 878  TYR A CA  1 
ATOM   6790  C  C   . TYR A 1 878  ? 97.404  64.351  119.923 1.00 45.46  ? 878  TYR A C   1 
ATOM   6791  O  O   . TYR A 1 878  ? 97.028  64.893  118.883 1.00 44.48  ? 878  TYR A O   1 
ATOM   6792  C  CB  . TYR A 1 878  ? 97.282  61.942  120.548 1.00 47.11  ? 878  TYR A CB  1 
ATOM   6793  C  CG  . TYR A 1 878  ? 95.903  61.815  119.938 1.00 47.86  ? 878  TYR A CG  1 
ATOM   6794  C  CD1 . TYR A 1 878  ? 95.720  61.286  118.656 1.00 46.01  ? 878  TYR A CD1 1 
ATOM   6795  C  CD2 . TYR A 1 878  ? 94.777  62.205  120.649 1.00 50.42  ? 878  TYR A CD2 1 
ATOM   6796  C  CE1 . TYR A 1 878  ? 94.443  61.163  118.101 1.00 47.28  ? 878  TYR A CE1 1 
ATOM   6797  C  CE2 . TYR A 1 878  ? 93.499  62.080  120.105 1.00 51.22  ? 878  TYR A CE2 1 
ATOM   6798  C  CZ  . TYR A 1 878  ? 93.339  61.563  118.840 1.00 49.88  ? 878  TYR A CZ  1 
ATOM   6799  O  OH  . TYR A 1 878  ? 92.067  61.463  118.329 1.00 52.48  ? 878  TYR A OH  1 
ATOM   6800  N  N   . GLN A 1 879  ? 97.206  64.873  121.123 1.00 46.68  ? 879  GLN A N   1 
ATOM   6801  C  CA  . GLN A 1 879  ? 96.582  66.175  121.314 1.00 47.32  ? 879  GLN A CA  1 
ATOM   6802  C  C   . GLN A 1 879  ? 97.225  67.176  120.363 1.00 45.64  ? 879  GLN A C   1 
ATOM   6803  O  O   . GLN A 1 879  ? 96.552  67.956  119.687 1.00 45.05  ? 879  GLN A O   1 
ATOM   6804  C  CB  . GLN A 1 879  ? 96.772  66.609  122.760 1.00 48.74  ? 879  GLN A CB  1 
ATOM   6805  C  CG  . GLN A 1 879  ? 96.027  67.843  123.162 1.00 49.82  ? 879  GLN A CG  1 
ATOM   6806  C  CD  . GLN A 1 879  ? 96.259  68.182  124.612 1.00 51.28  ? 879  GLN A CD  1 
ATOM   6807  O  OE1 . GLN A 1 879  ? 96.437  69.344  124.955 1.00 53.26  ? 879  GLN A OE1 1 
ATOM   6808  N  NE2 . GLN A 1 879  ? 96.258  67.168  125.476 1.00 50.95  ? 879  GLN A NE2 1 
ATOM   6809  N  N   . ASN A 1 880  ? 98.544  67.106  120.290 1.00 44.61  ? 880  ASN A N   1 
ATOM   6810  C  CA  . ASN A 1 880  ? 99.302  68.067  119.533 1.00 43.87  ? 880  ASN A CA  1 
ATOM   6811  C  C   . ASN A 1 880  ? 99.147  67.917  118.037 1.00 42.05  ? 880  ASN A C   1 
ATOM   6812  O  O   . ASN A 1 880  ? 99.072  68.905  117.318 1.00 42.03  ? 880  ASN A O   1 
ATOM   6813  C  CB  . ASN A 1 880  ? 100.774 67.984  119.899 1.00 43.63  ? 880  ASN A CB  1 
ATOM   6814  C  CG  . ASN A 1 880  ? 101.505 69.242  119.551 1.00 44.49  ? 880  ASN A CG  1 
ATOM   6815  O  OD1 . ASN A 1 880  ? 102.155 69.313  118.519 1.00 44.98  ? 880  ASN A OD1 1 
ATOM   6816  N  ND2 . ASN A 1 880  ? 101.371 70.266  120.392 1.00 46.74  ? 880  ASN A ND2 1 
ATOM   6817  N  N   . GLN A 1 881  ? 99.102  66.679  117.570 1.00 41.06  ? 881  GLN A N   1 
ATOM   6818  C  CA  . GLN A 1 881  ? 99.038  66.426  116.143 1.00 39.74  ? 881  GLN A CA  1 
ATOM   6819  C  C   . GLN A 1 881  ? 97.707  66.893  115.585 1.00 40.53  ? 881  GLN A C   1 
ATOM   6820  O  O   . GLN A 1 881  ? 97.631  67.363  114.456 1.00 40.19  ? 881  GLN A O   1 
ATOM   6821  C  CB  . GLN A 1 881  ? 99.268  64.943  115.849 1.00 39.06  ? 881  GLN A CB  1 
ATOM   6822  C  CG  . GLN A 1 881  ? 99.688  64.650  114.418 1.00 38.47  ? 881  GLN A CG  1 
ATOM   6823  C  CD  . GLN A 1 881  ? 100.866 65.500  113.966 1.00 38.83  ? 881  GLN A CD  1 
ATOM   6824  O  OE1 . GLN A 1 881  ? 100.898 65.979  112.836 1.00 37.60  ? 881  GLN A OE1 1 
ATOM   6825  N  NE2 . GLN A 1 881  ? 101.832 65.703  114.857 1.00 40.42  ? 881  GLN A NE2 1 
ATOM   6826  N  N   . MET A 1 882  ? 96.668  66.792  116.405 1.00 42.25  ? 882  MET A N   1 
ATOM   6827  C  CA  . MET A 1 882  ? 95.316  67.143  115.994 1.00 43.35  ? 882  MET A CA  1 
ATOM   6828  C  C   . MET A 1 882  ? 95.221  68.558  115.446 1.00 43.72  ? 882  MET A C   1 
ATOM   6829  O  O   . MET A 1 882  ? 94.318  68.854  114.665 1.00 44.47  ? 882  MET A O   1 
ATOM   6830  C  CB  . MET A 1 882  ? 94.302  66.911  117.131 1.00 45.20  ? 882  MET A CB  1 
ATOM   6831  C  CG  . MET A 1 882  ? 94.082  65.440  117.504 1.00 44.84  ? 882  MET A CG  1 
ATOM   6832  S  SD  . MET A 1 882  ? 93.915  64.336  116.073 1.00 44.92  ? 882  MET A SD  1 
ATOM   6833  C  CE  . MET A 1 882  ? 92.323  64.875  115.455 1.00 44.72  ? 882  MET A CE  1 
ATOM   6834  N  N   . ARG A 1 883  ? 96.166  69.417  115.830 1.00 43.56  ? 883  ARG A N   1 
ATOM   6835  C  CA  . ARG A 1 883  ? 96.228  70.784  115.303 1.00 44.45  ? 883  ARG A CA  1 
ATOM   6836  C  C   . ARG A 1 883  ? 96.150  70.788  113.784 1.00 42.77  ? 883  ARG A C   1 
ATOM   6837  O  O   . ARG A 1 883  ? 95.568  71.699  113.199 1.00 43.89  ? 883  ARG A O   1 
ATOM   6838  C  CB  . ARG A 1 883  ? 97.510  71.489  115.760 1.00 44.62  ? 883  ARG A CB  1 
ATOM   6839  C  CG  . ARG A 1 883  ? 97.705  72.970  115.275 1.00 48.92  ? 883  ARG A CG  1 
ATOM   6840  C  CD  . ARG A 1 883  ? 98.540  73.832  116.303 1.00 55.50  ? 883  ARG A CD  1 
ATOM   6841  N  NE  . ARG A 1 883  ? 99.847  73.213  116.586 1.00 57.26  ? 883  ARG A NE  1 
ATOM   6842  C  CZ  . ARG A 1 883  ? 100.094 72.363  117.587 1.00 58.06  ? 883  ARG A CZ  1 
ATOM   6843  N  NH1 . ARG A 1 883  ? 99.133  72.031  118.450 1.00 59.41  ? 883  ARG A NH1 1 
ATOM   6844  N  NH2 . ARG A 1 883  ? 101.308 71.842  117.726 1.00 56.26  ? 883  ARG A NH2 1 
ATOM   6845  N  N   . TYR A 1 884  ? 96.709  69.752  113.159 1.00 40.28  ? 884  TYR A N   1 
ATOM   6846  C  CA  . TYR A 1 884  ? 96.891  69.738  111.716 1.00 38.57  ? 884  TYR A CA  1 
ATOM   6847  C  C   . TYR A 1 884  ? 95.774  69.038  110.960 1.00 38.85  ? 884  TYR A C   1 
ATOM   6848  O  O   . TYR A 1 884  ? 95.779  69.008  109.724 1.00 38.14  ? 884  TYR A O   1 
ATOM   6849  C  CB  . TYR A 1 884  ? 98.277  69.208  111.354 1.00 36.63  ? 884  TYR A CB  1 
ATOM   6850  C  CG  . TYR A 1 884  ? 99.370  70.037  111.998 1.00 36.55  ? 884  TYR A CG  1 
ATOM   6851  C  CD1 . TYR A 1 884  ? 99.915  69.664  113.221 1.00 36.37  ? 884  TYR A CD1 1 
ATOM   6852  C  CD2 . TYR A 1 884  ? 99.824  71.225  111.409 1.00 36.79  ? 884  TYR A CD2 1 
ATOM   6853  C  CE1 . TYR A 1 884  ? 100.891 70.426  113.836 1.00 36.84  ? 884  TYR A CE1 1 
ATOM   6854  C  CE2 . TYR A 1 884  ? 100.811 72.001  112.015 1.00 36.48  ? 884  TYR A CE2 1 
ATOM   6855  C  CZ  . TYR A 1 884  ? 101.339 71.588  113.234 1.00 37.86  ? 884  TYR A CZ  1 
ATOM   6856  O  OH  . TYR A 1 884  ? 102.319 72.318  113.863 1.00 38.82  ? 884  TYR A OH  1 
ATOM   6857  N  N   . ARG A 1 885  ? 94.804  68.496  111.698 1.00 39.74  ? 885  ARG A N   1 
ATOM   6858  C  CA  . ARG A 1 885  ? 93.612  67.939  111.072 1.00 40.43  ? 885  ARG A CA  1 
ATOM   6859  C  C   . ARG A 1 885  ? 92.838  69.066  110.408 1.00 41.61  ? 885  ARG A C   1 
ATOM   6860  O  O   . ARG A 1 885  ? 92.729  70.163  110.951 1.00 42.29  ? 885  ARG A O   1 
ATOM   6861  C  CB  . ARG A 1 885  ? 92.733  67.209  112.084 1.00 41.72  ? 885  ARG A CB  1 
ATOM   6862  C  CG  . ARG A 1 885  ? 91.693  66.308  111.447 1.00 43.13  ? 885  ARG A CG  1 
ATOM   6863  C  CD  . ARG A 1 885  ? 90.703  65.776  112.472 1.00 47.72  ? 885  ARG A CD  1 
ATOM   6864  N  NE  . ARG A 1 885  ? 89.574  65.079  111.849 1.00 50.87  ? 885  ARG A NE  1 
ATOM   6865  C  CZ  . ARG A 1 885  ? 88.479  65.677  111.369 1.00 53.18  ? 885  ARG A CZ  1 
ATOM   6866  N  NH1 . ARG A 1 885  ? 88.343  66.996  111.425 1.00 53.02  ? 885  ARG A NH1 1 
ATOM   6867  N  NH2 . ARG A 1 885  ? 87.513  64.952  110.819 1.00 55.43  ? 885  ARG A NH2 1 
ATOM   6868  N  N   . GLN A 1 886  ? 92.327  68.795  109.216 1.00 41.85  ? 886  GLN A N   1 
ATOM   6869  C  CA  . GLN A 1 886  ? 91.561  69.776  108.474 1.00 43.54  ? 886  GLN A CA  1 
ATOM   6870  C  C   . GLN A 1 886  ? 90.078  69.409  108.496 1.00 46.23  ? 886  GLN A C   1 
ATOM   6871  O  O   . GLN A 1 886  ? 89.709  68.303  108.884 1.00 46.65  ? 886  GLN A O   1 
ATOM   6872  C  CB  . GLN A 1 886  ? 92.069  69.845  107.029 1.00 42.70  ? 886  GLN A CB  1 
ATOM   6873  C  CG  . GLN A 1 886  ? 93.557  70.176  106.884 1.00 39.39  ? 886  GLN A CG  1 
ATOM   6874  C  CD  . GLN A 1 886  ? 93.925  71.502  107.517 1.00 38.84  ? 886  GLN A CD  1 
ATOM   6875  O  OE1 . GLN A 1 886  ? 94.867  71.585  108.299 1.00 38.71  ? 886  GLN A OE1 1 
ATOM   6876  N  NE2 . GLN A 1 886  ? 93.181  72.542  107.189 1.00 39.45  ? 886  GLN A NE2 1 
ATOM   6877  N  N   . THR A 1 887  ? 89.232  70.342  108.078 1.00 48.53  ? 887  THR A N   1 
ATOM   6878  C  CA  . THR A 1 887  ? 87.806  70.091  107.906 1.00 51.26  ? 887  THR A CA  1 
ATOM   6879  C  C   . THR A 1 887  ? 87.558  68.849  107.044 1.00 51.37  ? 887  THR A C   1 
ATOM   6880  O  O   . THR A 1 887  ? 86.686  68.041  107.354 1.00 52.93  ? 887  THR A O   1 
ATOM   6881  C  CB  . THR A 1 887  ? 87.148  71.331  107.311 1.00 53.01  ? 887  THR A CB  1 
ATOM   6882  O  OG1 . THR A 1 887  ? 87.006  72.304  108.354 1.00 54.60  ? 887  THR A OG1 1 
ATOM   6883  C  CG2 . THR A 1 887  ? 85.776  71.014  106.698 1.00 56.20  ? 887  THR A CG2 1 
ATOM   6884  N  N   . ASP A 1 888  ? 88.337  68.726  105.967 1.00 50.33  ? 888  ASP A N   1 
ATOM   6885  C  CA  . ASP A 1 888  ? 88.473  67.522  105.138 1.00 49.65  ? 888  ASP A CA  1 
ATOM   6886  C  C   . ASP A 1 888  ? 88.324  66.211  105.897 1.00 49.21  ? 888  ASP A C   1 
ATOM   6887  O  O   . ASP A 1 888  ? 87.675  65.278  105.424 1.00 50.09  ? 888  ASP A O   1 
ATOM   6888  C  CB  . ASP A 1 888  ? 89.896  67.485  104.560 1.00 47.42  ? 888  ASP A CB  1 
ATOM   6889  C  CG  . ASP A 1 888  ? 90.026  68.219  103.264 1.00 48.86  ? 888  ASP A CG  1 
ATOM   6890  O  OD1 . ASP A 1 888  ? 91.168  68.614  102.919 1.00 49.06  ? 888  ASP A OD1 1 
ATOM   6891  O  OD2 . ASP A 1 888  ? 88.994  68.402  102.587 1.00 52.09  ? 888  ASP A OD2 1 
ATOM   6892  N  N   . GLY A 1 889  ? 88.971  66.156  107.059 1.00 47.56  ? 889  GLY A N   1 
ATOM   6893  C  CA  . GLY A 1 889  ? 89.287  64.906  107.721 1.00 46.54  ? 889  GLY A CA  1 
ATOM   6894  C  C   . GLY A 1 889  ? 90.734  64.545  107.427 1.00 43.78  ? 889  GLY A C   1 
ATOM   6895  O  O   . GLY A 1 889  ? 91.251  63.543  107.927 1.00 43.11  ? 889  GLY A O   1 
ATOM   6896  N  N   . SER A 1 890  ? 91.392  65.377  106.621 1.00 42.09  ? 890  SER A N   1 
ATOM   6897  C  CA  . SER A 1 890  ? 92.764  65.139  106.221 1.00 39.46  ? 890  SER A CA  1 
ATOM   6898  C  C   . SER A 1 890  ? 93.725  65.869  107.135 1.00 38.31  ? 890  SER A C   1 
ATOM   6899  O  O   . SER A 1 890  ? 93.296  66.572  108.052 1.00 39.16  ? 890  SER A O   1 
ATOM   6900  C  CB  . SER A 1 890  ? 92.979  65.592  104.778 1.00 39.37  ? 890  SER A CB  1 
ATOM   6901  O  OG  . SER A 1 890  ? 93.049  67.004  104.688 1.00 39.96  ? 890  SER A OG  1 
ATOM   6902  N  N   . PHE A 1 891  ? 95.024  65.691  106.876 1.00 36.47  ? 891  PHE A N   1 
ATOM   6903  C  CA  . PHE A 1 891  ? 96.087  66.389  107.608 1.00 35.38  ? 891  PHE A CA  1 
ATOM   6904  C  C   . PHE A 1 891  ? 96.916  67.257  106.675 1.00 35.02  ? 891  PHE A C   1 
ATOM   6905  O  O   . PHE A 1 891  ? 97.271  66.838  105.561 1.00 34.78  ? 891  PHE A O   1 
ATOM   6906  C  CB  . PHE A 1 891  ? 96.962  65.402  108.381 1.00 33.80  ? 891  PHE A CB  1 
ATOM   6907  C  CG  . PHE A 1 891  ? 96.281  64.837  109.583 1.00 34.89  ? 891  PHE A CG  1 
ATOM   6908  C  CD1 . PHE A 1 891  ? 95.435  63.732  109.468 1.00 35.04  ? 891  PHE A CD1 1 
ATOM   6909  C  CD2 . PHE A 1 891  ? 96.432  65.437  110.831 1.00 34.75  ? 891  PHE A CD2 1 
ATOM   6910  C  CE1 . PHE A 1 891  ? 94.771  63.231  110.579 1.00 34.35  ? 891  PHE A CE1 1 
ATOM   6911  C  CE2 . PHE A 1 891  ? 95.770  64.937  111.945 1.00 34.42  ? 891  PHE A CE2 1 
ATOM   6912  C  CZ  . PHE A 1 891  ? 94.937  63.836  111.816 1.00 34.73  ? 891  PHE A CZ  1 
ATOM   6913  N  N   . GLY A 1 892  ? 97.193  68.478  107.127 1.00 35.25  ? 892  GLY A N   1 
ATOM   6914  C  CA  . GLY A 1 892  ? 97.944  69.445  106.346 1.00 35.19  ? 892  GLY A CA  1 
ATOM   6915  C  C   . GLY A 1 892  ? 99.240  69.848  107.023 1.00 34.85  ? 892  GLY A C   1 
ATOM   6916  O  O   . GLY A 1 892  ? 99.458  69.566  108.197 1.00 35.21  ? 892  GLY A O   1 
ATOM   6917  N  N   . LEU A 1 893  ? 100.102 70.511  106.268 1.00 34.57  ? 893  LEU A N   1 
ATOM   6918  C  CA  . LEU A 1 893  ? 101.332 71.075  106.781 1.00 33.98  ? 893  LEU A CA  1 
ATOM   6919  C  C   . LEU A 1 893  ? 101.117 72.149  107.846 1.00 35.39  ? 893  LEU A C   1 
ATOM   6920  O  O   . LEU A 1 893  ? 101.960 72.311  108.723 1.00 35.75  ? 893  LEU A O   1 
ATOM   6921  C  CB  . LEU A 1 893  ? 102.126 71.672  105.617 1.00 34.02  ? 893  LEU A CB  1 
ATOM   6922  C  CG  . LEU A 1 893  ? 103.615 71.946  105.796 1.00 32.38  ? 893  LEU A CG  1 
ATOM   6923  C  CD1 . LEU A 1 893  ? 104.371 70.670  106.125 1.00 29.24  ? 893  LEU A CD1 1 
ATOM   6924  C  CD2 . LEU A 1 893  ? 104.120 72.559  104.534 1.00 31.00  ? 893  LEU A CD2 1 
ATOM   6925  N  N   . TRP A 1 894  ? 100.017 72.896  107.759 1.00 36.82  ? 894  TRP A N   1 
ATOM   6926  C  CA  . TRP A 1 894  ? 99.718  73.980  108.727 1.00 38.38  ? 894  TRP A CA  1 
ATOM   6927  C  C   . TRP A 1 894  ? 98.371  73.754  109.387 1.00 39.76  ? 894  TRP A C   1 
ATOM   6928  O  O   . TRP A 1 894  ? 97.557  72.958  108.901 1.00 39.59  ? 894  TRP A O   1 
ATOM   6929  C  CB  . TRP A 1 894  ? 99.762  75.371  108.065 1.00 39.27  ? 894  TRP A CB  1 
ATOM   6930  C  CG  . TRP A 1 894  ? 100.897 75.493  107.109 1.00 38.71  ? 894  TRP A CG  1 
ATOM   6931  C  CD1 . TRP A 1 894  ? 100.818 75.582  105.748 1.00 37.65  ? 894  TRP A CD1 1 
ATOM   6932  C  CD2 . TRP A 1 894  ? 102.292 75.457  107.431 1.00 37.87  ? 894  TRP A CD2 1 
ATOM   6933  N  NE1 . TRP A 1 894  ? 102.074 75.625  105.205 1.00 36.31  ? 894  TRP A NE1 1 
ATOM   6934  C  CE2 . TRP A 1 894  ? 103.001 75.542  106.211 1.00 37.03  ? 894  TRP A CE2 1 
ATOM   6935  C  CE3 . TRP A 1 894  ? 103.013 75.362  108.633 1.00 36.69  ? 894  TRP A CE3 1 
ATOM   6936  C  CZ2 . TRP A 1 894  ? 104.397 75.542  106.154 1.00 36.56  ? 894  TRP A CZ2 1 
ATOM   6937  C  CZ3 . TRP A 1 894  ? 104.395 75.366  108.580 1.00 36.55  ? 894  TRP A CZ3 1 
ATOM   6938  C  CH2 . TRP A 1 894  ? 105.075 75.456  107.346 1.00 36.83  ? 894  TRP A CH2 1 
ATOM   6939  N  N   . GLU A 1 895  ? 98.149  74.442  110.503 1.00 41.52  ? 895  GLU A N   1 
ATOM   6940  C  CA  . GLU A 1 895  ? 96.882  74.376  111.232 1.00 43.82  ? 895  GLU A CA  1 
ATOM   6941  C  C   . GLU A 1 895  ? 95.671  74.462  110.290 1.00 44.44  ? 895  GLU A C   1 
ATOM   6942  O  O   . GLU A 1 895  ? 94.742  73.657  110.399 1.00 44.91  ? 895  GLU A O   1 
ATOM   6943  C  CB  . GLU A 1 895  ? 96.860  75.453  112.316 1.00 45.94  ? 895  GLU A CB  1 
ATOM   6944  C  CG  . GLU A 1 895  ? 95.511  75.780  112.967 1.00 51.38  ? 895  GLU A CG  1 
ATOM   6945  C  CD  . GLU A 1 895  ? 95.669  76.800  114.114 1.00 57.56  ? 895  GLU A CD  1 
ATOM   6946  O  OE1 . GLU A 1 895  ? 96.830  77.097  114.497 1.00 59.91  ? 895  GLU A OE1 1 
ATOM   6947  O  OE2 . GLU A 1 895  ? 94.649  77.297  114.643 1.00 60.35  ? 895  GLU A OE2 1 
ATOM   6948  N  N   . THR A 1 896  ? 95.709  75.398  109.344 1.00 44.63  ? 896  THR A N   1 
ATOM   6949  C  CA  . THR A 1 896  ? 94.678  75.501  108.322 1.00 45.32  ? 896  THR A CA  1 
ATOM   6950  C  C   . THR A 1 896  ? 95.290  75.608  106.922 1.00 44.85  ? 896  THR A C   1 
ATOM   6951  O  O   . THR A 1 896  ? 95.877  76.627  106.566 1.00 45.71  ? 896  THR A O   1 
ATOM   6952  C  CB  . THR A 1 896  ? 93.738  76.699  108.586 1.00 47.63  ? 896  THR A CB  1 
ATOM   6953  O  OG1 . THR A 1 896  ? 93.248  76.625  109.927 1.00 48.85  ? 896  THR A OG1 1 
ATOM   6954  C  CG2 . THR A 1 896  ? 92.559  76.699  107.621 1.00 47.47  ? 896  THR A CG2 1 
ATOM   6955  N  N   . THR A 1 897  ? 95.124  74.554  106.134 1.00 43.71  ? 897  THR A N   1 
ATOM   6956  C  CA  . THR A 1 897  ? 95.601  74.505  104.756 1.00 43.45  ? 897  THR A CA  1 
ATOM   6957  C  C   . THR A 1 897  ? 95.045  73.242  104.079 1.00 42.91  ? 897  THR A C   1 
ATOM   6958  O  O   . THR A 1 897  ? 94.509  72.360  104.756 1.00 42.83  ? 897  THR A O   1 
ATOM   6959  C  CB  . THR A 1 897  ? 97.159  74.484  104.694 1.00 42.29  ? 897  THR A CB  1 
ATOM   6960  O  OG1 . THR A 1 897  ? 97.592  74.605  103.334 1.00 42.16  ? 897  THR A OG1 1 
ATOM   6961  C  CG2 . THR A 1 897  ? 97.729  73.189  105.313 1.00 39.04  ? 897  THR A CG2 1 
ATOM   6962  N  N   . ASN A 1 898  ? 95.176  73.152  102.756 1.00 42.56  ? 898  ASN A N   1 
ATOM   6963  C  CA  . ASN A 1 898  ? 94.760  71.957  102.035 1.00 41.93  ? 898  ASN A CA  1 
ATOM   6964  C  C   . ASN A 1 898  ? 95.515  70.728  102.540 1.00 39.79  ? 898  ASN A C   1 
ATOM   6965  O  O   . ASN A 1 898  ? 96.726  70.775  102.749 1.00 38.50  ? 898  ASN A O   1 
ATOM   6966  C  CB  . ASN A 1 898  ? 94.983  72.125  100.525 1.00 42.57  ? 898  ASN A CB  1 
ATOM   6967  C  CG  . ASN A 1 898  ? 94.089  73.182  99.906  1.00 45.72  ? 898  ASN A CG  1 
ATOM   6968  O  OD1 . ASN A 1 898  ? 94.526  73.955  99.057  1.00 48.23  ? 898  ASN A OD1 1 
ATOM   6969  N  ND2 . ASN A 1 898  ? 92.830  73.222  100.325 1.00 48.87  ? 898  ASN A ND2 1 
ATOM   6970  N  N   . GLY A 1 899  ? 94.798  69.629  102.741 1.00 39.68  ? 899  GLY A N   1 
ATOM   6971  C  CA  . GLY A 1 899  ? 95.423  68.377  103.148 1.00 38.11  ? 899  GLY A CA  1 
ATOM   6972  C  C   . GLY A 1 899  ? 96.458  67.807  102.192 1.00 37.13  ? 899  GLY A C   1 
ATOM   6973  O  O   . GLY A 1 899  ? 96.438  68.078  100.987 1.00 37.11  ? 899  GLY A O   1 
ATOM   6974  N  N   . SER A 1 900  ? 97.357  66.999  102.751 1.00 36.01  ? 900  SER A N   1 
ATOM   6975  C  CA  . SER A 1 900  ? 98.463  66.396  102.018 1.00 35.29  ? 900  SER A CA  1 
ATOM   6976  C  C   . SER A 1 900  ? 98.268  64.880  101.998 1.00 35.36  ? 900  SER A C   1 
ATOM   6977  O  O   . SER A 1 900  ? 97.919  64.297  103.030 1.00 35.35  ? 900  SER A O   1 
ATOM   6978  C  CB  . SER A 1 900  ? 99.781  66.772  102.714 1.00 34.07  ? 900  SER A CB  1 
ATOM   6979  O  OG  . SER A 1 900  ? 100.807 65.803  102.524 1.00 32.96  ? 900  SER A OG  1 
ATOM   6980  N  N   . VAL A 1 901  ? 98.482  64.224  100.853 1.00 35.61  ? 901  VAL A N   1 
ATOM   6981  C  CA  . VAL A 1 901  ? 98.294  62.769  100.858 1.00 36.12  ? 901  VAL A CA  1 
ATOM   6982  C  C   . VAL A 1 901  ? 99.424  62.103  101.636 1.00 35.29  ? 901  VAL A C   1 
ATOM   6983  O  O   . VAL A 1 901  ? 99.193  61.158  102.380 1.00 35.77  ? 901  VAL A O   1 
ATOM   6984  C  CB  . VAL A 1 901  ? 98.038  62.091  99.458  1.00 36.87  ? 901  VAL A CB  1 
ATOM   6985  C  CG1 . VAL A 1 901  ? 97.443  63.052  98.425  1.00 37.09  ? 901  VAL A CG1 1 
ATOM   6986  C  CG2 . VAL A 1 901  ? 99.265  61.399  98.937  1.00 35.88  ? 901  VAL A CG2 1 
ATOM   6987  N  N   . PHE A 1 902  ? 100.631 62.635  101.503 1.00 35.01  ? 902  PHE A N   1 
ATOM   6988  C  CA  . PHE A 1 902  ? 101.762 62.175  102.293 1.00 34.45  ? 902  PHE A CA  1 
ATOM   6989  C  C   . PHE A 1 902  ? 101.441 62.298  103.778 1.00 34.68  ? 902  PHE A C   1 
ATOM   6990  O  O   . PHE A 1 902  ? 101.505 61.302  104.517 1.00 34.44  ? 902  PHE A O   1 
ATOM   6991  C  CB  . PHE A 1 902  ? 103.018 62.963  101.918 1.00 34.32  ? 902  PHE A CB  1 
ATOM   6992  C  CG  . PHE A 1 902  ? 104.259 62.576  102.681 1.00 35.70  ? 902  PHE A CG  1 
ATOM   6993  C  CD1 . PHE A 1 902  ? 104.525 61.247  103.017 1.00 37.56  ? 902  PHE A CD1 1 
ATOM   6994  C  CD2 . PHE A 1 902  ? 105.196 63.544  103.019 1.00 37.28  ? 902  PHE A CD2 1 
ATOM   6995  C  CE1 . PHE A 1 902  ? 105.686 60.905  103.714 1.00 37.18  ? 902  PHE A CE1 1 
ATOM   6996  C  CE2 . PHE A 1 902  ? 106.363 63.203  103.714 1.00 37.68  ? 902  PHE A CE2 1 
ATOM   6997  C  CZ  . PHE A 1 902  ? 106.601 61.889  104.068 1.00 36.62  ? 902  PHE A CZ  1 
ATOM   6998  N  N   . LEU A 1 903  ? 101.059 63.497  104.218 1.00 35.10  ? 903  LEU A N   1 
ATOM   6999  C  CA  . LEU A 1 903  ? 100.844 63.699  105.641 1.00 35.23  ? 903  LEU A CA  1 
ATOM   7000  C  C   . LEU A 1 903  ? 99.679  62.862  106.148 1.00 35.79  ? 903  LEU A C   1 
ATOM   7001  O  O   . LEU A 1 903  ? 99.769  62.260  107.216 1.00 35.63  ? 903  LEU A O   1 
ATOM   7002  C  CB  . LEU A 1 903  ? 100.651 65.174  105.992 1.00 36.28  ? 903  LEU A CB  1 
ATOM   7003  C  CG  . LEU A 1 903  ? 100.907 65.443  107.486 1.00 37.98  ? 903  LEU A CG  1 
ATOM   7004  C  CD1 . LEU A 1 903  ? 102.293 64.951  107.899 1.00 37.91  ? 903  LEU A CD1 1 
ATOM   7005  C  CD2 . LEU A 1 903  ? 100.738 66.897  107.867 1.00 38.71  ? 903  LEU A CD2 1 
ATOM   7006  N  N   . THR A 1 904  ? 98.605  62.797  105.361 1.00 36.07  ? 904  THR A N   1 
ATOM   7007  C  CA  . THR A 1 904  ? 97.430  62.029  105.738 1.00 36.54  ? 904  THR A CA  1 
ATOM   7008  C  C   . THR A 1 904  ? 97.731  60.527  105.816 1.00 36.23  ? 904  THR A C   1 
ATOM   7009  O  O   . THR A 1 904  ? 97.279  59.861  106.741 1.00 36.73  ? 904  THR A O   1 
ATOM   7010  C  CB  . THR A 1 904  ? 96.248  62.355  104.820 1.00 37.91  ? 904  THR A CB  1 
ATOM   7011  O  OG1 . THR A 1 904  ? 96.037  63.776  104.824 1.00 38.02  ? 904  THR A OG1 1 
ATOM   7012  C  CG2 . THR A 1 904  ? 94.981  61.656  105.283 1.00 38.54  ? 904  THR A CG2 1 
ATOM   7013  N  N   . ALA A 1 905  ? 98.521  60.003  104.882 1.00 35.25  ? 905  ALA A N   1 
ATOM   7014  C  CA  . ALA A 1 905  ? 98.993  58.614  104.980 1.00 35.24  ? 905  ALA A CA  1 
ATOM   7015  C  C   . ALA A 1 905  ? 99.904  58.412  106.195 1.00 34.84  ? 905  ALA A C   1 
ATOM   7016  O  O   . ALA A 1 905  ? 99.775  57.432  106.934 1.00 35.57  ? 905  ALA A O   1 
ATOM   7017  C  CB  . ALA A 1 905  ? 99.720  58.205  103.719 1.00 34.24  ? 905  ALA A CB  1 
ATOM   7018  N  N   . PHE A 1 906  ? 100.829 59.346  106.387 1.00 34.20  ? 906  PHE A N   1 
ATOM   7019  C  CA  . PHE A 1 906  ? 101.793 59.286  107.476 1.00 33.74  ? 906  PHE A CA  1 
ATOM   7020  C  C   . PHE A 1 906  ? 101.081 59.289  108.825 1.00 35.33  ? 906  PHE A C   1 
ATOM   7021  O  O   . PHE A 1 906  ? 101.234 58.354  109.604 1.00 36.26  ? 906  PHE A O   1 
ATOM   7022  C  CB  . PHE A 1 906  ? 102.773 60.461  107.352 1.00 32.64  ? 906  PHE A CB  1 
ATOM   7023  C  CG  . PHE A 1 906  ? 103.825 60.511  108.424 1.00 30.78  ? 906  PHE A CG  1 
ATOM   7024  C  CD1 . PHE A 1 906  ? 104.237 59.357  109.091 1.00 29.41  ? 906  PHE A CD1 1 
ATOM   7025  C  CD2 . PHE A 1 906  ? 104.438 61.715  108.731 1.00 29.39  ? 906  PHE A CD2 1 
ATOM   7026  C  CE1 . PHE A 1 906  ? 105.206 59.410  110.081 1.00 29.07  ? 906  PHE A CE1 1 
ATOM   7027  C  CE2 . PHE A 1 906  ? 105.423 61.783  109.708 1.00 29.44  ? 906  PHE A CE2 1 
ATOM   7028  C  CZ  . PHE A 1 906  ? 105.805 60.625  110.392 1.00 29.62  ? 906  PHE A CZ  1 
ATOM   7029  N  N   . VAL A 1 907  ? 100.291 60.331  109.082 1.00 36.52  ? 907  VAL A N   1 
ATOM   7030  C  CA  . VAL A 1 907  ? 99.595  60.506  110.357 1.00 37.82  ? 907  VAL A CA  1 
ATOM   7031  C  C   . VAL A 1 907  ? 98.568  59.408  110.585 1.00 39.73  ? 907  VAL A C   1 
ATOM   7032  O  O   . VAL A 1 907  ? 98.629  58.707  111.590 1.00 40.66  ? 907  VAL A O   1 
ATOM   7033  C  CB  . VAL A 1 907  ? 98.914  61.888  110.452 1.00 38.22  ? 907  VAL A CB  1 
ATOM   7034  C  CG1 . VAL A 1 907  ? 98.211  62.056  111.792 1.00 39.61  ? 907  VAL A CG1 1 
ATOM   7035  C  CG2 . VAL A 1 907  ? 99.931  63.001  110.234 1.00 36.93  ? 907  VAL A CG2 1 
ATOM   7036  N  N   . GLY A 1 908  ? 97.646  59.248  109.639 1.00 40.86  ? 908  GLY A N   1 
ATOM   7037  C  CA  . GLY A 1 908  ? 96.579  58.263  109.754 1.00 43.19  ? 908  GLY A CA  1 
ATOM   7038  C  C   . GLY A 1 908  ? 97.052  56.882  110.169 1.00 44.11  ? 908  GLY A C   1 
ATOM   7039  O  O   . GLY A 1 908  ? 96.498  56.278  111.086 1.00 45.57  ? 908  GLY A O   1 
ATOM   7040  N  N   . THR A 1 909  ? 98.085  56.378  109.509 1.00 43.57  ? 909  THR A N   1 
ATOM   7041  C  CA  . THR A 1 909  ? 98.534  55.015  109.783 1.00 45.10  ? 909  THR A CA  1 
ATOM   7042  C  C   . THR A 1 909  ? 99.263  54.977  111.105 1.00 45.38  ? 909  THR A C   1 
ATOM   7043  O  O   . THR A 1 909  ? 99.117  54.039  111.887 1.00 46.92  ? 909  THR A O   1 
ATOM   7044  C  CB  . THR A 1 909  ? 99.441  54.466  108.674 1.00 44.05  ? 909  THR A CB  1 
ATOM   7045  O  OG1 . THR A 1 909  ? 100.609 55.296  108.552 1.00 43.17  ? 909  THR A OG1 1 
ATOM   7046  C  CG2 . THR A 1 909  ? 98.680  54.435  107.354 1.00 44.38  ? 909  THR A CG2 1 
ATOM   7047  N  N   . SER A 1 910  ? 100.029 56.026  111.356 1.00 44.71  ? 910  SER A N   1 
ATOM   7048  C  CA  . SER A 1 910  ? 100.773 56.152  112.587 1.00 45.54  ? 910  SER A CA  1 
ATOM   7049  C  C   . SER A 1 910  ? 99.854  56.170  113.829 1.00 47.60  ? 910  SER A C   1 
ATOM   7050  O  O   . SER A 1 910  ? 100.184 55.573  114.863 1.00 48.58  ? 910  SER A O   1 
ATOM   7051  C  CB  . SER A 1 910  ? 101.645 57.392  112.502 1.00 44.11  ? 910  SER A CB  1 
ATOM   7052  O  OG  . SER A 1 910  ? 102.491 57.468  113.621 1.00 47.20  ? 910  SER A OG  1 
ATOM   7053  N  N   . MET A 1 911  ? 98.693  56.818  113.712 1.00 48.60  ? 911  MET A N   1 
ATOM   7054  C  CA  . MET A 1 911  ? 97.715  56.854  114.799 1.00 50.97  ? 911  MET A CA  1 
ATOM   7055  C  C   . MET A 1 911  ? 97.098  55.494  115.033 1.00 52.63  ? 911  MET A C   1 
ATOM   7056  O  O   . MET A 1 911  ? 96.855  55.101  116.171 1.00 54.28  ? 911  MET A O   1 
ATOM   7057  C  CB  . MET A 1 911  ? 96.595  57.844  114.510 1.00 51.69  ? 911  MET A CB  1 
ATOM   7058  C  CG  . MET A 1 911  ? 97.048  59.148  113.941 1.00 51.95  ? 911  MET A CG  1 
ATOM   7059  S  SD  . MET A 1 911  ? 96.232  60.544  114.722 1.00 56.22  ? 911  MET A SD  1 
ATOM   7060  C  CE  . MET A 1 911  ? 97.546  61.078  115.816 1.00 55.67  ? 911  MET A CE  1 
ATOM   7061  N  N   . GLN A 1 912  ? 96.826  54.798  113.936 1.00 52.78  ? 912  GLN A N   1 
ATOM   7062  C  CA  . GLN A 1 912  ? 96.244  53.469  113.962 1.00 54.72  ? 912  GLN A CA  1 
ATOM   7063  C  C   . GLN A 1 912  ? 97.161  52.537  114.748 1.00 54.93  ? 912  GLN A C   1 
ATOM   7064  O  O   . GLN A 1 912  ? 96.705  51.841  115.657 1.00 56.91  ? 912  GLN A O   1 
ATOM   7065  C  CB  . GLN A 1 912  ? 96.017  52.976  112.528 1.00 54.47  ? 912  GLN A CB  1 
ATOM   7066  C  CG  . GLN A 1 912  ? 95.201  51.698  112.392 1.00 58.45  ? 912  GLN A CG  1 
ATOM   7067  C  CD  . GLN A 1 912  ? 93.904  51.719  113.194 1.00 63.25  ? 912  GLN A CD  1 
ATOM   7068  O  OE1 . GLN A 1 912  ? 92.945  52.404  112.832 1.00 65.03  ? 912  GLN A OE1 1 
ATOM   7069  N  NE2 . GLN A 1 912  ? 93.869  50.950  114.283 1.00 64.97  ? 912  GLN A NE2 1 
ATOM   7070  N  N   . THR A 1 913  ? 98.452  52.559  114.411 1.00 52.97  ? 913  THR A N   1 
ATOM   7071  C  CA  . THR A 1 913  ? 99.492  51.853  115.171 1.00 53.24  ? 913  THR A CA  1 
ATOM   7072  C  C   . THR A 1 913  ? 99.419  52.197  116.665 1.00 54.63  ? 913  THR A C   1 
ATOM   7073  O  O   . THR A 1 913  ? 99.529  51.317  117.520 1.00 56.40  ? 913  THR A O   1 
ATOM   7074  C  CB  . THR A 1 913  ? 100.913 52.188  114.628 1.00 50.91  ? 913  THR A CB  1 
ATOM   7075  O  OG1 . THR A 1 913  ? 100.976 51.919  113.225 1.00 50.60  ? 913  THR A OG1 1 
ATOM   7076  C  CG2 . THR A 1 913  ? 101.988 51.372  115.315 1.00 50.81  ? 913  THR A CG2 1 
ATOM   7077  N  N   . ALA A 1 914  ? 99.210  53.477  116.967 1.00 54.33  ? 914  ALA A N   1 
ATOM   7078  C  CA  . ALA A 1 914  ? 99.216  53.973  118.347 1.00 55.68  ? 914  ALA A CA  1 
ATOM   7079  C  C   . ALA A 1 914  ? 98.053  53.489  119.199 1.00 58.52  ? 914  ALA A C   1 
ATOM   7080  O  O   . ALA A 1 914  ? 98.106  53.601  120.424 1.00 60.14  ? 914  ALA A O   1 
ATOM   7081  C  CB  . ALA A 1 914  ? 99.293  55.503  118.372 1.00 54.48  ? 914  ALA A CB  1 
ATOM   7082  N  N   . VAL A 1 915  ? 97.012  52.947  118.566 1.00 59.67  ? 915  VAL A N   1 
ATOM   7083  C  CA  . VAL A 1 915  ? 95.855  52.410  119.307 1.00 62.81  ? 915  VAL A CA  1 
ATOM   7084  C  C   . VAL A 1 915  ? 96.271  51.250  120.241 1.00 65.01  ? 915  VAL A C   1 
ATOM   7085  O  O   . VAL A 1 915  ? 95.620  50.996  121.262 1.00 67.30  ? 915  VAL A O   1 
ATOM   7086  C  CB  . VAL A 1 915  ? 94.680  52.019  118.352 1.00 63.48  ? 915  VAL A CB  1 
ATOM   7087  C  CG1 . VAL A 1 915  ? 93.555  51.340  119.107 1.00 66.85  ? 915  VAL A CG1 1 
ATOM   7088  C  CG2 . VAL A 1 915  ? 94.137  53.247  117.648 1.00 61.62  ? 915  VAL A CG2 1 
ATOM   7089  N  N   . LYS A 1 916  ? 97.371  50.577  119.893 1.00 64.26  ? 916  LYS A N   1 
ATOM   7090  C  CA  . LYS A 1 916  ? 97.977  49.548  120.745 1.00 66.36  ? 916  LYS A CA  1 
ATOM   7091  C  C   . LYS A 1 916  ? 98.314  50.046  122.146 1.00 67.47  ? 916  LYS A C   1 
ATOM   7092  O  O   . LYS A 1 916  ? 98.200  49.295  123.107 1.00 70.45  ? 916  LYS A O   1 
ATOM   7093  C  CB  . LYS A 1 916  ? 99.277  49.029  120.132 1.00 64.74  ? 916  LYS A CB  1 
ATOM   7094  C  CG  . LYS A 1 916  ? 99.143  48.144  118.918 1.00 65.58  ? 916  LYS A CG  1 
ATOM   7095  C  CD  . LYS A 1 916  ? 100.506 48.005  118.259 1.00 65.86  ? 916  LYS A CD  1 
ATOM   7096  C  CE  . LYS A 1 916  ? 100.515 46.975  117.143 1.00 67.52  ? 916  LYS A CE  1 
ATOM   7097  N  NZ  . LYS A 1 916  ? 101.909 46.769  116.635 1.00 67.07  ? 916  LYS A NZ  1 
ATOM   7098  N  N   . TYR A 1 917  ? 98.743  51.302  122.263 1.00 65.67  ? 917  TYR A N   1 
ATOM   7099  C  CA  . TYR A 1 917  ? 99.346  51.786  123.510 1.00 66.15  ? 917  TYR A CA  1 
ATOM   7100  C  C   . TYR A 1 917  ? 98.522  52.785  124.314 1.00 67.31  ? 917  TYR A C   1 
ATOM   7101  O  O   . TYR A 1 917  ? 98.649  52.841  125.541 1.00 69.49  ? 917  TYR A O   1 
ATOM   7102  C  CB  . TYR A 1 917  ? 100.732 52.361  123.235 1.00 63.69  ? 917  TYR A CB  1 
ATOM   7103  C  CG  . TYR A 1 917  ? 101.640 51.427  122.472 1.00 62.28  ? 917  TYR A CG  1 
ATOM   7104  C  CD1 . TYR A 1 917  ? 102.215 50.321  123.093 1.00 63.62  ? 917  TYR A CD1 1 
ATOM   7105  C  CD2 . TYR A 1 917  ? 101.929 51.654  121.130 1.00 59.95  ? 917  TYR A CD2 1 
ATOM   7106  C  CE1 . TYR A 1 917  ? 103.050 49.465  122.402 1.00 62.31  ? 917  TYR A CE1 1 
ATOM   7107  C  CE2 . TYR A 1 917  ? 102.767 50.802  120.427 1.00 59.32  ? 917  TYR A CE2 1 
ATOM   7108  C  CZ  . TYR A 1 917  ? 103.324 49.712  121.080 1.00 60.39  ? 917  TYR A CZ  1 
ATOM   7109  O  OH  . TYR A 1 917  ? 104.149 48.868  120.399 1.00 60.06  ? 917  TYR A OH  1 
ATOM   7110  N  N   . ILE A 1 918  ? 97.710  53.586  123.631 1.00 66.17  ? 918  ILE A N   1 
ATOM   7111  C  CA  . ILE A 1 918  ? 96.790  54.510  124.300 1.00 67.52  ? 918  ILE A CA  1 
ATOM   7112  C  C   . ILE A 1 918  ? 95.369  54.323  123.775 1.00 68.81  ? 918  ILE A C   1 
ATOM   7113  O  O   . ILE A 1 918  ? 95.172  53.972  122.614 1.00 68.35  ? 918  ILE A O   1 
ATOM   7114  C  CB  . ILE A 1 918  ? 97.230  55.997  124.168 1.00 65.57  ? 918  ILE A CB  1 
ATOM   7115  C  CG1 . ILE A 1 918  ? 97.401  56.407  122.704 1.00 62.50  ? 918  ILE A CG1 1 
ATOM   7116  C  CG2 . ILE A 1 918  ? 98.519  56.248  124.949 1.00 65.20  ? 918  ILE A CG2 1 
ATOM   7117  C  CD1 . ILE A 1 918  ? 97.549  57.904  122.500 1.00 61.14  ? 918  ILE A CD1 1 
ATOM   7118  N  N   . SER A 1 919  ? 94.382  54.548  124.627 1.00 71.22  ? 919  SER A N   1 
ATOM   7119  C  CA  . SER A 1 919  ? 92.990  54.350  124.242 1.00 72.80  ? 919  SER A CA  1 
ATOM   7120  C  C   . SER A 1 919  ? 92.338  55.638  123.741 1.00 71.81  ? 919  SER A C   1 
ATOM   7121  O  O   . SER A 1 919  ? 91.186  55.639  123.309 1.00 73.17  ? 919  SER A O   1 
ATOM   7122  C  CB  . SER A 1 919  ? 92.209  53.802  125.430 1.00 76.50  ? 919  SER A CB  1 
ATOM   7123  O  OG  . SER A 1 919  ? 92.539  54.528  126.597 1.00 77.48  ? 919  SER A OG  1 
ATOM   7124  N  N   . ASP A 1 920  ? 93.090  56.730  123.784 1.00 69.72  ? 920  ASP A N   1 
ATOM   7125  C  CA  . ASP A 1 920  ? 92.526  58.060  123.572 1.00 69.12  ? 920  ASP A CA  1 
ATOM   7126  C  C   . ASP A 1 920  ? 92.357  58.424  122.090 1.00 66.39  ? 920  ASP A C   1 
ATOM   7127  O  O   . ASP A 1 920  ? 91.754  59.448  121.760 1.00 66.50  ? 920  ASP A O   1 
ATOM   7128  C  CB  . ASP A 1 920  ? 93.370  59.112  124.314 1.00 68.66  ? 920  ASP A CB  1 
ATOM   7129  C  CG  . ASP A 1 920  ? 93.610  58.747  125.779 1.00 71.62  ? 920  ASP A CG  1 
ATOM   7130  O  OD1 . ASP A 1 920  ? 92.632  58.665  126.559 1.00 75.09  ? 920  ASP A OD1 1 
ATOM   7131  O  OD2 . ASP A 1 920  ? 94.785  58.540  126.153 1.00 71.74  ? 920  ASP A OD2 1 
ATOM   7132  N  N   . ILE A 1 921  ? 92.866  57.577  121.204 1.00 63.93  ? 921  ILE A N   1 
ATOM   7133  C  CA  . ILE A 1 921  ? 92.774  57.838  119.771 1.00 61.36  ? 921  ILE A CA  1 
ATOM   7134  C  C   . ILE A 1 921  ? 91.366  57.591  119.229 1.00 62.90  ? 921  ILE A C   1 
ATOM   7135  O  O   . ILE A 1 921  ? 90.775  56.535  119.462 1.00 64.98  ? 921  ILE A O   1 
ATOM   7136  C  CB  . ILE A 1 921  ? 93.853  57.063  118.980 1.00 59.04  ? 921  ILE A CB  1 
ATOM   7137  C  CG1 . ILE A 1 921  ? 95.206  57.746  119.182 1.00 56.19  ? 921  ILE A CG1 1 
ATOM   7138  C  CG2 . ILE A 1 921  ? 93.516  57.016  117.504 1.00 57.42  ? 921  ILE A CG2 1 
ATOM   7139  C  CD1 . ILE A 1 921  ? 96.363  56.839  119.087 1.00 54.19  ? 921  ILE A CD1 1 
ATOM   7140  N  N   . ASP A 1 922  ? 90.847  58.590  118.517 1.00 61.94  ? 922  ASP A N   1 
ATOM   7141  C  CA  . ASP A 1 922  ? 89.515  58.555  117.920 1.00 63.08  ? 922  ASP A CA  1 
ATOM   7142  C  C   . ASP A 1 922  ? 89.522  57.735  116.620 1.00 61.71  ? 922  ASP A C   1 
ATOM   7143  O  O   . ASP A 1 922  ? 89.987  58.205  115.578 1.00 59.59  ? 922  ASP A O   1 
ATOM   7144  C  CB  . ASP A 1 922  ? 89.042  59.992  117.661 1.00 63.02  ? 922  ASP A CB  1 
ATOM   7145  C  CG  . ASP A 1 922  ? 87.576  60.074  117.274 1.00 66.14  ? 922  ASP A CG  1 
ATOM   7146  O  OD1 . ASP A 1 922  ? 87.119  59.276  116.427 1.00 67.83  ? 922  ASP A OD1 1 
ATOM   7147  O  OD2 . ASP A 1 922  ? 86.872  60.954  117.811 1.00 68.72  ? 922  ASP A OD2 1 
ATOM   7148  N  N   . ALA A 1 923  ? 88.993  56.514  116.694 1.00 62.89  ? 923  ALA A N   1 
ATOM   7149  C  CA  . ALA A 1 923  ? 88.994  55.569  115.568 1.00 61.73  ? 923  ALA A CA  1 
ATOM   7150  C  C   . ALA A 1 923  ? 88.261  56.097  114.340 1.00 61.09  ? 923  ALA A C   1 
ATOM   7151  O  O   . ALA A 1 923  ? 88.723  55.920  113.210 1.00 59.05  ? 923  ALA A O   1 
ATOM   7152  C  CB  . ALA A 1 923  ? 88.398  54.233  116.000 1.00 64.47  ? 923  ALA A CB  1 
ATOM   7153  N  N   . ALA A 1 924  ? 87.113  56.730  114.576 1.00 62.61  ? 924  ALA A N   1 
ATOM   7154  C  CA  . ALA A 1 924  ? 86.293  57.304  113.512 1.00 62.53  ? 924  ALA A CA  1 
ATOM   7155  C  C   . ALA A 1 924  ? 87.084  58.360  112.754 1.00 59.40  ? 924  ALA A C   1 
ATOM   7156  O  O   . ALA A 1 924  ? 87.025  58.427  111.523 1.00 58.59  ? 924  ALA A O   1 
ATOM   7157  C  CB  . ALA A 1 924  ? 85.016  57.904  114.083 1.00 65.12  ? 924  ALA A CB  1 
ATOM   7158  N  N   . MET A 1 925  ? 87.831  59.164  113.510 1.00 57.55  ? 925  MET A N   1 
ATOM   7159  C  CA  . MET A 1 925  ? 88.648  60.237  112.969 1.00 54.64  ? 925  MET A CA  1 
ATOM   7160  C  C   . MET A 1 925  ? 89.725  59.664  112.060 1.00 52.28  ? 925  MET A C   1 
ATOM   7161  O  O   . MET A 1 925  ? 90.007  60.217  110.996 1.00 51.34  ? 925  MET A O   1 
ATOM   7162  C  CB  . MET A 1 925  ? 89.258  61.048  114.116 1.00 53.92  ? 925  MET A CB  1 
ATOM   7163  C  CG  . MET A 1 925  ? 90.049  62.260  113.704 1.00 51.13  ? 925  MET A CG  1 
ATOM   7164  S  SD  . MET A 1 925  ? 91.706  61.830  113.161 1.00 48.46  ? 925  MET A SD  1 
ATOM   7165  C  CE  . MET A 1 925  ? 92.387  61.129  114.659 1.00 49.21  ? 925  MET A CE  1 
ATOM   7166  N  N   . VAL A 1 926  ? 90.319  58.552  112.485 1.00 51.91  ? 926  VAL A N   1 
ATOM   7167  C  CA  . VAL A 1 926  ? 91.318  57.841  111.687 1.00 49.93  ? 926  VAL A CA  1 
ATOM   7168  C  C   . VAL A 1 926  ? 90.700  57.319  110.382 1.00 50.58  ? 926  VAL A C   1 
ATOM   7169  O  O   . VAL A 1 926  ? 91.239  57.575  109.302 1.00 49.23  ? 926  VAL A O   1 
ATOM   7170  C  CB  . VAL A 1 926  ? 91.978  56.699  112.501 1.00 50.12  ? 926  VAL A CB  1 
ATOM   7171  C  CG1 . VAL A 1 926  ? 92.916  55.861  111.635 1.00 48.05  ? 926  VAL A CG1 1 
ATOM   7172  C  CG2 . VAL A 1 926  ? 92.724  57.276  113.706 1.00 49.37  ? 926  VAL A CG2 1 
ATOM   7173  N  N   . GLU A 1 927  ? 89.566  56.621  110.493 1.00 52.77  ? 927  GLU A N   1 
ATOM   7174  C  CA  . GLU A 1 927  ? 88.814  56.132  109.337 1.00 53.83  ? 927  GLU A CA  1 
ATOM   7175  C  C   . GLU A 1 927  ? 88.541  57.238  108.333 1.00 52.54  ? 927  GLU A C   1 
ATOM   7176  O  O   . GLU A 1 927  ? 88.735  57.045  107.129 1.00 52.04  ? 927  GLU A O   1 
ATOM   7177  C  CB  . GLU A 1 927  ? 87.479  55.509  109.755 1.00 57.76  ? 927  GLU A CB  1 
ATOM   7178  C  CG  . GLU A 1 927  ? 87.564  54.216  110.573 1.00 61.90  ? 927  GLU A CG  1 
ATOM   7179  C  CD  . GLU A 1 927  ? 86.183  53.596  110.829 1.00 69.32  ? 927  GLU A CD  1 
ATOM   7180  O  OE1 . GLU A 1 927  ? 85.547  53.130  109.845 1.00 72.19  ? 927  GLU A OE1 1 
ATOM   7181  O  OE2 . GLU A 1 927  ? 85.741  53.568  112.009 1.00 70.99  ? 927  GLU A OE2 1 
ATOM   7182  N  N   . LYS A 1 928  ? 88.098  58.392  108.822 1.00 52.21  ? 928  LYS A N   1 
ATOM   7183  C  CA  . LYS A 1 928  ? 87.829  59.534  107.951 1.00 51.67  ? 928  LYS A CA  1 
ATOM   7184  C  C   . LYS A 1 928  ? 89.078  59.972  107.175 1.00 48.65  ? 928  LYS A C   1 
ATOM   7185  O  O   . LYS A 1 928  ? 88.996  60.283  105.980 1.00 48.38  ? 928  LYS A O   1 
ATOM   7186  C  CB  . LYS A 1 928  ? 87.250  60.707  108.741 1.00 52.68  ? 928  LYS A CB  1 
ATOM   7187  C  CG  . LYS A 1 928  ? 86.624  61.802  107.874 1.00 54.22  ? 928  LYS A CG  1 
ATOM   7188  C  CD  . LYS A 1 928  ? 85.907  62.822  108.739 1.00 58.64  ? 928  LYS A CD  1 
ATOM   7189  C  CE  . LYS A 1 928  ? 84.898  63.647  107.951 1.00 61.98  ? 928  LYS A CE  1 
ATOM   7190  N  NZ  . LYS A 1 928  ? 85.369  65.037  107.725 1.00 61.86  ? 928  LYS A NZ  1 
ATOM   7191  N  N   . ALA A 1 929  ? 90.224  59.982  107.853 1.00 46.16  ? 929  ALA A N   1 
ATOM   7192  C  CA  . ALA A 1 929  ? 91.468  60.391  107.228 1.00 43.53  ? 929  ALA A CA  1 
ATOM   7193  C  C   . ALA A 1 929  ? 91.859  59.406  106.146 1.00 42.86  ? 929  ALA A C   1 
ATOM   7194  O  O   . ALA A 1 929  ? 92.237  59.798  105.048 1.00 42.04  ? 929  ALA A O   1 
ATOM   7195  C  CB  . ALA A 1 929  ? 92.568  60.517  108.264 1.00 42.06  ? 929  ALA A CB  1 
ATOM   7196  N  N   . LEU A 1 930  ? 91.745  58.119  106.444 1.00 43.63  ? 930  LEU A N   1 
ATOM   7197  C  CA  . LEU A 1 930  ? 92.154  57.101  105.481 1.00 43.21  ? 930  LEU A CA  1 
ATOM   7198  C  C   . LEU A 1 930  ? 91.188  57.015  104.292 1.00 44.39  ? 930  LEU A C   1 
ATOM   7199  O  O   . LEU A 1 930  ? 91.621  56.768  103.168 1.00 43.45  ? 930  LEU A O   1 
ATOM   7200  C  CB  . LEU A 1 930  ? 92.365  55.744  106.164 1.00 43.82  ? 930  LEU A CB  1 
ATOM   7201  C  CG  . LEU A 1 930  ? 93.487  55.676  107.211 1.00 42.84  ? 930  LEU A CG  1 
ATOM   7202  C  CD1 . LEU A 1 930  ? 93.786  54.237  107.563 1.00 42.35  ? 930  LEU A CD1 1 
ATOM   7203  C  CD2 . LEU A 1 930  ? 94.775  56.390  106.748 1.00 40.39  ? 930  LEU A CD2 1 
ATOM   7204  N  N   . ASP A 1 931  ? 89.897  57.249  104.540 1.00 46.11  ? 931  ASP A N   1 
ATOM   7205  C  CA  . ASP A 1 931  ? 88.917  57.347  103.456 1.00 47.58  ? 931  ASP A CA  1 
ATOM   7206  C  C   . ASP A 1 931  ? 89.249  58.500  102.507 1.00 46.39  ? 931  ASP A C   1 
ATOM   7207  O  O   . ASP A 1 931  ? 89.214  58.339  101.283 1.00 46.87  ? 931  ASP A O   1 
ATOM   7208  C  CB  . ASP A 1 931  ? 87.490  57.464  104.004 1.00 50.26  ? 931  ASP A CB  1 
ATOM   7209  C  CG  . ASP A 1 931  ? 86.971  56.138  104.584 1.00 52.84  ? 931  ASP A CG  1 
ATOM   7210  O  OD1 . ASP A 1 931  ? 87.517  55.070  104.218 1.00 54.19  ? 931  ASP A OD1 1 
ATOM   7211  O  OD2 . ASP A 1 931  ? 86.026  56.157  105.403 1.00 53.44  ? 931  ASP A OD2 1 
ATOM   7212  N  N   . TRP A 1 932  ? 89.605  59.650  103.077 1.00 45.05  ? 932  TRP A N   1 
ATOM   7213  C  CA  . TRP A 1 932  ? 90.005  60.810  102.298 1.00 43.82  ? 932  TRP A CA  1 
ATOM   7214  C  C   . TRP A 1 932  ? 91.191  60.451  101.430 1.00 42.34  ? 932  TRP A C   1 
ATOM   7215  O  O   . TRP A 1 932  ? 91.185  60.699  100.226 1.00 42.57  ? 932  TRP A O   1 
ATOM   7216  C  CB  . TRP A 1 932  ? 90.352  61.969  103.222 1.00 42.74  ? 932  TRP A CB  1 
ATOM   7217  C  CG  . TRP A 1 932  ? 90.801  63.216  102.521 1.00 41.83  ? 932  TRP A CG  1 
ATOM   7218  C  CD1 . TRP A 1 932  ? 90.023  64.271  102.155 1.00 42.92  ? 932  TRP A CD1 1 
ATOM   7219  C  CD2 . TRP A 1 932  ? 92.141  63.545  102.117 1.00 39.72  ? 932  TRP A CD2 1 
ATOM   7220  N  NE1 . TRP A 1 932  ? 90.790  65.243  101.556 1.00 42.59  ? 932  TRP A NE1 1 
ATOM   7221  C  CE2 . TRP A 1 932  ? 92.093  64.819  101.515 1.00 41.09  ? 932  TRP A CE2 1 
ATOM   7222  C  CE3 . TRP A 1 932  ? 93.375  62.889  102.209 1.00 36.58  ? 932  TRP A CE3 1 
ATOM   7223  C  CZ2 . TRP A 1 932  ? 93.238  65.451  101.007 1.00 39.70  ? 932  TRP A CZ2 1 
ATOM   7224  C  CZ3 . TRP A 1 932  ? 94.502  63.509  101.707 1.00 35.81  ? 932  TRP A CZ3 1 
ATOM   7225  C  CH2 . TRP A 1 932  ? 94.429  64.775  101.111 1.00 37.17  ? 932  TRP A CH2 1 
ATOM   7226  N  N   . LEU A 1 933  ? 92.203  59.858  102.055 1.00 41.11  ? 933  LEU A N   1 
ATOM   7227  C  CA  . LEU A 1 933  ? 93.370  59.351  101.350 1.00 39.95  ? 933  LEU A CA  1 
ATOM   7228  C  C   . LEU A 1 933  ? 93.003  58.381  100.222 1.00 41.30  ? 933  LEU A C   1 
ATOM   7229  O  O   . LEU A 1 933  ? 93.472  58.537  99.088  1.00 41.35  ? 933  LEU A O   1 
ATOM   7230  C  CB  . LEU A 1 933  ? 94.299  58.660  102.333 1.00 38.62  ? 933  LEU A CB  1 
ATOM   7231  C  CG  . LEU A 1 933  ? 95.533  57.970  101.766 1.00 37.88  ? 933  LEU A CG  1 
ATOM   7232  C  CD1 . LEU A 1 933  ? 96.509  58.980  101.159 1.00 36.33  ? 933  LEU A CD1 1 
ATOM   7233  C  CD2 . LEU A 1 933  ? 96.183  57.168  102.876 1.00 38.12  ? 933  LEU A CD2 1 
ATOM   7234  N  N   . ALA A 1 934  ? 92.164  57.394  100.528 1.00 42.61  ? 934  ALA A N   1 
ATOM   7235  C  CA  . ALA A 1 934  ? 91.789  56.389  99.538  1.00 43.98  ? 934  ALA A CA  1 
ATOM   7236  C  C   . ALA A 1 934  ? 91.080  57.002  98.332  1.00 45.60  ? 934  ALA A C   1 
ATOM   7237  O  O   . ALA A 1 934  ? 91.238  56.530  97.206  1.00 46.11  ? 934  ALA A O   1 
ATOM   7238  C  CB  . ALA A 1 934  ? 90.928  55.316  100.168 1.00 45.64  ? 934  ALA A CB  1 
ATOM   7239  N  N   . SER A 1 935  ? 90.297  58.054  98.564  1.00 46.79  ? 935  SER A N   1 
ATOM   7240  C  CA  . SER A 1 935  ? 89.549  58.678  97.476  1.00 48.61  ? 935  SER A CA  1 
ATOM   7241  C  C   . SER A 1 935  ? 90.469  59.470  96.552  1.00 47.44  ? 935  SER A C   1 
ATOM   7242  O  O   . SER A 1 935  ? 90.099  59.783  95.427  1.00 49.00  ? 935  SER A O   1 
ATOM   7243  C  CB  . SER A 1 935  ? 88.399  59.539  98.005  1.00 50.00  ? 935  SER A CB  1 
ATOM   7244  O  OG  . SER A 1 935  ? 88.876  60.744  98.568  1.00 49.51  ? 935  SER A OG  1 
ATOM   7245  N  N   . LYS A 1 936  ? 91.675  59.766  97.023  1.00 45.57  ? 936  LYS A N   1 
ATOM   7246  C  CA  . LYS A 1 936  ? 92.652  60.511  96.230  1.00 44.82  ? 936  LYS A CA  1 
ATOM   7247  C  C   . LYS A 1 936  ? 93.366  59.651  95.211  1.00 44.43  ? 936  LYS A C   1 
ATOM   7248  O  O   . LYS A 1 936  ? 93.971  60.180  94.286  1.00 44.80  ? 936  LYS A O   1 
ATOM   7249  C  CB  . LYS A 1 936  ? 93.683  61.198  97.127  1.00 43.10  ? 936  LYS A CB  1 
ATOM   7250  C  CG  . LYS A 1 936  ? 93.145  62.389  97.889  1.00 44.34  ? 936  LYS A CG  1 
ATOM   7251  C  CD  . LYS A 1 936  ? 92.941  63.590  96.985  1.00 47.61  ? 936  LYS A CD  1 
ATOM   7252  C  CE  . LYS A 1 936  ? 92.149  64.673  97.703  1.00 51.24  ? 936  LYS A CE  1 
ATOM   7253  N  NZ  . LYS A 1 936  ? 92.577  66.042  97.262  1.00 53.75  ? 936  LYS A NZ  1 
ATOM   7254  N  N   . GLN A 1 937  ? 93.294  58.332  95.368  1.00 44.51  ? 937  GLN A N   1 
ATOM   7255  C  CA  . GLN A 1 937  ? 93.964  57.422  94.452  1.00 44.10  ? 937  GLN A CA  1 
ATOM   7256  C  C   . GLN A 1 937  ? 93.373  57.490  93.061  1.00 46.39  ? 937  GLN A C   1 
ATOM   7257  O  O   . GLN A 1 937  ? 92.163  57.654  92.890  1.00 48.36  ? 937  GLN A O   1 
ATOM   7258  C  CB  . GLN A 1 937  ? 93.903  55.987  94.952  1.00 44.06  ? 937  GLN A CB  1 
ATOM   7259  C  CG  . GLN A 1 937  ? 94.948  55.084  94.306  1.00 42.68  ? 937  GLN A CG  1 
ATOM   7260  C  CD  . GLN A 1 937  ? 94.906  53.676  94.853  1.00 42.25  ? 937  GLN A CD  1 
ATOM   7261  O  OE1 . GLN A 1 937  ? 93.848  53.198  95.277  1.00 44.09  ? 937  GLN A OE1 1 
ATOM   7262  N  NE2 . GLN A 1 937  ? 96.051  52.994  94.833  1.00 38.14  ? 937  GLN A NE2 1 
ATOM   7263  N  N   . HIS A 1 938  ? 94.245  57.333  92.074  1.00 46.27  ? 938  HIS A N   1 
ATOM   7264  C  CA  . HIS A 1 938  ? 93.862  57.352  90.683  1.00 48.13  ? 938  HIS A CA  1 
ATOM   7265  C  C   . HIS A 1 938  ? 93.432  55.972  90.234  1.00 49.99  ? 938  HIS A C   1 
ATOM   7266  O  O   . HIS A 1 938  ? 93.790  54.969  90.851  1.00 49.75  ? 938  HIS A O   1 
ATOM   7267  C  CB  . HIS A 1 938  ? 95.048  57.812  89.847  1.00 47.27  ? 938  HIS A CB  1 
ATOM   7268  C  CG  . HIS A 1 938  ? 95.353  59.269  89.983  1.00 46.89  ? 938  HIS A CG  1 
ATOM   7269  N  ND1 . HIS A 1 938  ? 95.597  60.080  88.898  1.00 48.51  ? 938  HIS A ND1 1 
ATOM   7270  C  CD2 . HIS A 1 938  ? 95.432  60.066  91.073  1.00 46.00  ? 938  HIS A CD2 1 
ATOM   7271  C  CE1 . HIS A 1 938  ? 95.829  61.310  89.315  1.00 47.61  ? 938  HIS A CE1 1 
ATOM   7272  N  NE2 . HIS A 1 938  ? 95.732  61.329  90.630  1.00 45.97  ? 938  HIS A NE2 1 
ATOM   7273  N  N   . PHE A 1 939  ? 92.678  55.929  89.140  1.00 52.38  ? 939  PHE A N   1 
ATOM   7274  C  CA  . PHE A 1 939  ? 92.278  54.687  88.518  1.00 54.28  ? 939  PHE A CA  1 
ATOM   7275  C  C   . PHE A 1 939  ? 93.469  53.760  88.345  1.00 52.70  ? 939  PHE A C   1 
ATOM   7276  O  O   . PHE A 1 939  ? 93.357  52.559  88.551  1.00 53.41  ? 939  PHE A O   1 
ATOM   7277  C  CB  . PHE A 1 939  ? 91.632  54.961  87.159  1.00 57.15  ? 939  PHE A CB  1 
ATOM   7278  C  CG  . PHE A 1 939  ? 90.291  55.631  87.243  1.00 61.34  ? 939  PHE A CG  1 
ATOM   7279  C  CD1 . PHE A 1 939  ? 89.172  54.935  87.695  1.00 65.44  ? 939  PHE A CD1 1 
ATOM   7280  C  CD2 . PHE A 1 939  ? 90.135  56.959  86.853  1.00 63.80  ? 939  PHE A CD2 1 
ATOM   7281  C  CE1 . PHE A 1 939  ? 87.916  55.561  87.769  1.00 68.54  ? 939  PHE A CE1 1 
ATOM   7282  C  CE2 . PHE A 1 939  ? 88.888  57.594  86.920  1.00 65.72  ? 939  PHE A CE2 1 
ATOM   7283  C  CZ  . PHE A 1 939  ? 87.778  56.893  87.378  1.00 68.25  ? 939  PHE A CZ  1 
ATOM   7284  N  N   . SER A 1 940  ? 94.612  54.324  87.976  1.00 50.85  ? 940  SER A N   1 
ATOM   7285  C  CA  . SER A 1 940  ? 95.792  53.523  87.691  1.00 49.85  ? 940  SER A CA  1 
ATOM   7286  C  C   . SER A 1 940  ? 96.432  52.957  88.950  1.00 48.10  ? 940  SER A C   1 
ATOM   7287  O  O   . SER A 1 940  ? 97.231  52.031  88.860  1.00 48.19  ? 940  SER A O   1 
ATOM   7288  C  CB  . SER A 1 940  ? 96.816  54.344  86.927  1.00 48.82  ? 940  SER A CB  1 
ATOM   7289  O  OG  . SER A 1 940  ? 97.164  55.488  87.678  1.00 47.17  ? 940  SER A OG  1 
ATOM   7290  N  N   . GLY A 1 941  ? 96.083  53.511  90.111  1.00 46.83  ? 941  GLY A N   1 
ATOM   7291  C  CA  . GLY A 1 941  ? 96.652  53.080  91.383  1.00 45.16  ? 941  GLY A CA  1 
ATOM   7292  C  C   . GLY A 1 941  ? 97.639  54.085  91.952  1.00 43.31  ? 941  GLY A C   1 
ATOM   7293  O  O   . GLY A 1 941  ? 98.206  53.884  93.026  1.00 41.81  ? 941  GLY A O   1 
ATOM   7294  N  N   . ARG A 1 942  ? 97.816  55.186  91.230  1.00 43.38  ? 942  ARG A N   1 
ATOM   7295  C  CA  . ARG A 1 942  ? 98.861  56.159  91.487  1.00 41.59  ? 942  ARG A CA  1 
ATOM   7296  C  C   . ARG A 1 942  ? 98.399  57.272  92.417  1.00 40.74  ? 942  ARG A C   1 
ATOM   7297  O  O   . ARG A 1 942  ? 97.249  57.702  92.346  1.00 42.03  ? 942  ARG A O   1 
ATOM   7298  C  CB  . ARG A 1 942  ? 99.257  56.770  90.154  1.00 42.64  ? 942  ARG A CB  1 
ATOM   7299  C  CG  . ARG A 1 942  ? 100.426 57.708  90.208  1.00 42.64  ? 942  ARG A CG  1 
ATOM   7300  C  CD  . ARG A 1 942  ? 100.106 58.909  89.399  1.00 45.89  ? 942  ARG A CD  1 
ATOM   7301  N  NE  . ARG A 1 942  ? 101.266 59.377  88.674  1.00 50.24  ? 942  ARG A NE  1 
ATOM   7302  C  CZ  . ARG A 1 942  ? 101.228 60.379  87.802  1.00 56.46  ? 942  ARG A CZ  1 
ATOM   7303  N  NH1 . ARG A 1 942  ? 100.068 61.017  87.568  1.00 58.82  ? 942  ARG A NH1 1 
ATOM   7304  N  NH2 . ARG A 1 942  ? 102.345 60.747  87.163  1.00 57.30  ? 942  ARG A NH2 1 
ATOM   7305  N  N   . PHE A 1 943  ? 99.302  57.743  93.274  1.00 38.68  ? 943  PHE A N   1 
ATOM   7306  C  CA  . PHE A 1 943  ? 99.032  58.901  94.113  1.00 37.99  ? 943  PHE A CA  1 
ATOM   7307  C  C   . PHE A 1 943  ? 99.810  60.140  93.652  1.00 37.99  ? 943  PHE A C   1 
ATOM   7308  O  O   . PHE A 1 943  ? 101.020 60.074  93.397  1.00 37.60  ? 943  PHE A O   1 
ATOM   7309  C  CB  . PHE A 1 943  ? 99.351  58.595  95.571  1.00 36.28  ? 943  PHE A CB  1 
ATOM   7310  C  CG  . PHE A 1 943  ? 98.304  57.762  96.267  1.00 36.80  ? 943  PHE A CG  1 
ATOM   7311  C  CD1 . PHE A 1 943  ? 98.412  56.369  96.309  1.00 36.15  ? 943  PHE A CD1 1 
ATOM   7312  C  CD2 . PHE A 1 943  ? 97.218  58.366  96.897  1.00 36.25  ? 943  PHE A CD2 1 
ATOM   7313  C  CE1 . PHE A 1 943  ? 97.448  55.603  96.951  1.00 35.27  ? 943  PHE A CE1 1 
ATOM   7314  C  CE2 . PHE A 1 943  ? 96.251  57.600  97.543  1.00 35.68  ? 943  PHE A CE2 1 
ATOM   7315  C  CZ  . PHE A 1 943  ? 96.369  56.220  97.567  1.00 35.47  ? 943  PHE A CZ  1 
ATOM   7316  N  N   . ASP A 1 944  ? 99.104  61.263  93.543  1.00 38.81  ? 944  ASP A N   1 
ATOM   7317  C  CA  . ASP A 1 944  ? 99.726  62.555  93.294  1.00 38.85  ? 944  ASP A CA  1 
ATOM   7318  C  C   . ASP A 1 944  ? 99.673  63.408  94.538  1.00 38.13  ? 944  ASP A C   1 
ATOM   7319  O  O   . ASP A 1 944  ? 98.828  63.188  95.402  1.00 38.91  ? 944  ASP A O   1 
ATOM   7320  C  CB  . ASP A 1 944  ? 99.000  63.285  92.183  1.00 40.68  ? 944  ASP A CB  1 
ATOM   7321  C  CG  . ASP A 1 944  ? 99.325  62.739  90.827  1.00 43.02  ? 944  ASP A CG  1 
ATOM   7322  O  OD1 . ASP A 1 944  ? 100.336 61.994  90.688  1.00 42.95  ? 944  ASP A OD1 1 
ATOM   7323  O  OD2 . ASP A 1 944  ? 98.558  63.062  89.893  1.00 46.45  ? 944  ASP A OD2 1 
ATOM   7324  N  N   . LYS A 1 945  ? 100.553 64.403  94.621  1.00 37.54  ? 945  LYS A N   1 
ATOM   7325  C  CA  . LYS A 1 945  ? 100.574 65.316  95.764  1.00 36.50  ? 945  LYS A CA  1 
ATOM   7326  C  C   . LYS A 1 945  ? 99.291  66.154  95.882  1.00 37.75  ? 945  LYS A C   1 
ATOM   7327  O  O   . LYS A 1 945  ? 98.500  66.242  94.943  1.00 39.43  ? 945  LYS A O   1 
ATOM   7328  C  CB  . LYS A 1 945  ? 101.828 66.195  95.739  1.00 36.14  ? 945  LYS A CB  1 
ATOM   7329  C  CG  . LYS A 1 945  ? 101.927 67.155  94.582  1.00 37.28  ? 945  LYS A CG  1 
ATOM   7330  C  CD  . LYS A 1 945  ? 101.897 68.576  95.077  1.00 41.76  ? 945  LYS A CD  1 
ATOM   7331  C  CE  . LYS A 1 945  ? 101.897 69.586  93.934  1.00 46.01  ? 945  LYS A CE  1 
ATOM   7332  N  NZ  . LYS A 1 945  ? 102.921 69.206  92.916  1.00 47.49  ? 945  LYS A NZ  1 
ATOM   7333  N  N   . ALA A 1 946  ? 99.079  66.732  97.058  1.00 36.96  ? 946  ALA A N   1 
ATOM   7334  C  CA  . ALA A 1 946  ? 97.967  67.629  97.299  1.00 38.00  ? 946  ALA A CA  1 
ATOM   7335  C  C   . ALA A 1 946  ? 98.446  68.669  98.299  1.00 37.90  ? 946  ALA A C   1 
ATOM   7336  O  O   . ALA A 1 946  ? 99.200  68.349  99.215  1.00 37.27  ? 946  ALA A O   1 
ATOM   7337  C  CB  . ALA A 1 946  ? 96.780  66.867  97.845  1.00 37.90  ? 946  ALA A CB  1 
ATOM   7338  N  N   . GLY A 1 947  ? 98.011  69.909  98.134  1.00 39.19  ? 947  GLY A N   1 
ATOM   7339  C  CA  . GLY A 1 947  ? 98.505  70.986  98.965  1.00 39.43  ? 947  GLY A CA  1 
ATOM   7340  C  C   . GLY A 1 947  ? 99.886  71.415  98.517  1.00 39.21  ? 947  GLY A C   1 
ATOM   7341  O  O   . GLY A 1 947  ? 100.319 71.100  97.407  1.00 39.30  ? 947  GLY A O   1 
ATOM   7342  N  N   . ALA A 1 948  ? 100.588 72.129  99.388  1.00 39.08  ? 948  ALA A N   1 
ATOM   7343  C  CA  . ALA A 1 948  ? 101.890 72.682  99.038  1.00 39.11  ? 948  ALA A CA  1 
ATOM   7344  C  C   . ALA A 1 948  ? 102.947 71.590  98.909  1.00 37.64  ? 948  ALA A C   1 
ATOM   7345  O  O   . ALA A 1 948  ? 102.861 70.536  99.573  1.00 36.20  ? 948  ALA A O   1 
ATOM   7346  C  CB  . ALA A 1 948  ? 102.312 73.688  100.069 1.00 39.45  ? 948  ALA A CB  1 
ATOM   7347  N  N   . GLU A 1 949  ? 103.943 71.854  98.061  1.00 37.76  ? 949  GLU A N   1 
ATOM   7348  C  CA  . GLU A 1 949  ? 105.103 70.975  97.932  1.00 36.38  ? 949  GLU A CA  1 
ATOM   7349  C  C   . GLU A 1 949  ? 106.219 71.389  98.899  1.00 36.10  ? 949  GLU A C   1 
ATOM   7350  O  O   . GLU A 1 949  ? 106.996 72.300  98.629  1.00 37.36  ? 949  GLU A O   1 
ATOM   7351  C  CB  . GLU A 1 949  ? 105.609 70.937  96.490  1.00 36.59  ? 949  GLU A CB  1 
ATOM   7352  C  CG  . GLU A 1 949  ? 106.524 69.748  96.221  1.00 35.29  ? 949  GLU A CG  1 
ATOM   7353  C  CD  . GLU A 1 949  ? 106.902 69.600  94.770  1.00 34.54  ? 949  GLU A CD  1 
ATOM   7354  O  OE1 . GLU A 1 949  ? 106.431 70.381  93.937  1.00 36.84  ? 949  GLU A OE1 1 
ATOM   7355  O  OE2 . GLU A 1 949  ? 107.672 68.695  94.450  1.00 34.42  ? 949  GLU A OE2 1 
ATOM   7356  N  N   . TYR A 1 950  ? 106.280 70.711  100.032 1.00 34.98  ? 950  TYR A N   1 
ATOM   7357  C  CA  . TYR A 1 950  ? 107.280 70.986  101.060 1.00 34.87  ? 950  TYR A CA  1 
ATOM   7358  C  C   . TYR A 1 950  ? 108.423 69.971  101.034 1.00 34.00  ? 950  TYR A C   1 
ATOM   7359  O  O   . TYR A 1 950  ? 109.469 70.196  101.618 1.00 34.24  ? 950  TYR A O   1 
ATOM   7360  C  CB  . TYR A 1 950  ? 106.623 71.008  102.452 1.00 34.16  ? 950  TYR A CB  1 
ATOM   7361  C  CG  . TYR A 1 950  ? 105.785 69.793  102.769 1.00 32.20  ? 950  TYR A CG  1 
ATOM   7362  C  CD1 . TYR A 1 950  ? 104.476 69.681  102.292 1.00 33.55  ? 950  TYR A CD1 1 
ATOM   7363  C  CD2 . TYR A 1 950  ? 106.286 68.764  103.552 1.00 31.11  ? 950  TYR A CD2 1 
ATOM   7364  C  CE1 . TYR A 1 950  ? 103.683 68.564  102.582 1.00 33.44  ? 950  TYR A CE1 1 
ATOM   7365  C  CE2 . TYR A 1 950  ? 105.507 67.634  103.851 1.00 31.95  ? 950  TYR A CE2 1 
ATOM   7366  C  CZ  . TYR A 1 950  ? 104.205 67.543  103.357 1.00 32.92  ? 950  TYR A CZ  1 
ATOM   7367  O  OH  . TYR A 1 950  ? 103.429 66.436  103.633 1.00 32.31  ? 950  TYR A OH  1 
ATOM   7368  N  N   . HIS A 1 951  ? 108.205 68.845  100.370 1.00 33.72  ? 951  HIS A N   1 
ATOM   7369  C  CA  . HIS A 1 951  ? 109.204 67.797  100.272 1.00 33.37  ? 951  HIS A CA  1 
ATOM   7370  C  C   . HIS A 1 951  ? 109.251 67.273  98.825  1.00 33.21  ? 951  HIS A C   1 
ATOM   7371  O  O   . HIS A 1 951  ? 108.584 66.288  98.484  1.00 32.25  ? 951  HIS A O   1 
ATOM   7372  C  CB  . HIS A 1 951  ? 108.873 66.683  101.262 1.00 32.50  ? 951  HIS A CB  1 
ATOM   7373  C  CG  . HIS A 1 951  ? 109.936 65.636  101.378 1.00 34.51  ? 951  HIS A CG  1 
ATOM   7374  N  ND1 . HIS A 1 951  ? 110.454 65.235  102.591 1.00 37.70  ? 951  HIS A ND1 1 
ATOM   7375  C  CD2 . HIS A 1 951  ? 110.585 64.913  100.437 1.00 35.76  ? 951  HIS A CD2 1 
ATOM   7376  C  CE1 . HIS A 1 951  ? 111.368 64.301  102.392 1.00 37.19  ? 951  HIS A CE1 1 
ATOM   7377  N  NE2 . HIS A 1 951  ? 111.473 64.095  101.092 1.00 37.01  ? 951  HIS A NE2 1 
ATOM   7378  N  N   . LYS A 1 952  ? 110.037 67.956  97.987  1.00 34.04  ? 952  LYS A N   1 
ATOM   7379  C  CA  . LYS A 1 952  ? 110.120 67.678  96.547  1.00 34.58  ? 952  LYS A CA  1 
ATOM   7380  C  C   . LYS A 1 952  ? 110.299 66.204  96.182  1.00 34.41  ? 952  LYS A C   1 
ATOM   7381  O  O   . LYS A 1 952  ? 109.639 65.710  95.256  1.00 34.40  ? 952  LYS A O   1 
ATOM   7382  C  CB  . LYS A 1 952  ? 111.249 68.470  95.898  1.00 35.10  ? 952  LYS A CB  1 
ATOM   7383  C  CG  . LYS A 1 952  ? 110.925 69.909  95.650  1.00 36.17  ? 952  LYS A CG  1 
ATOM   7384  C  CD  . LYS A 1 952  ? 112.114 70.645  95.075  1.00 36.49  ? 952  LYS A CD  1 
ATOM   7385  C  CE  . LYS A 1 952  ? 113.287 70.669  96.047  1.00 35.10  ? 952  LYS A CE  1 
ATOM   7386  N  NZ  . LYS A 1 952  ? 114.447 71.343  95.408  1.00 38.33  ? 952  LYS A NZ  1 
ATOM   7387  N  N   . GLU A 1 953  ? 111.195 65.517  96.892  1.00 34.03  ? 953  GLU A N   1 
ATOM   7388  C  CA  . GLU A 1 953  ? 111.559 64.160  96.522  1.00 34.17  ? 953  GLU A CA  1 
ATOM   7389  C  C   . GLU A 1 953  ? 110.422 63.192  96.762  1.00 33.84  ? 953  GLU A C   1 
ATOM   7390  O  O   . GLU A 1 953  ? 110.302 62.191  96.051  1.00 35.01  ? 953  GLU A O   1 
ATOM   7391  C  CB  . GLU A 1 953  ? 112.838 63.703  97.229  1.00 33.75  ? 953  GLU A CB  1 
ATOM   7392  C  CG  . GLU A 1 953  ? 114.126 64.309  96.649  1.00 35.85  ? 953  GLU A CG  1 
ATOM   7393  C  CD  . GLU A 1 953  ? 114.217 64.211  95.128  1.00 39.64  ? 953  GLU A CD  1 
ATOM   7394  O  OE1 . GLU A 1 953  ? 114.065 63.100  94.566  1.00 41.55  ? 953  GLU A OE1 1 
ATOM   7395  O  OE2 . GLU A 1 953  ? 114.453 65.252  94.481  1.00 42.13  ? 953  GLU A OE2 1 
ATOM   7396  N  N   . MET A 1 954  ? 109.574 63.497  97.735  1.00 33.56  ? 954  MET A N   1 
ATOM   7397  C  CA  . MET A 1 954  ? 108.431 62.646  98.060  1.00 33.57  ? 954  MET A CA  1 
ATOM   7398  C  C   . MET A 1 954  ? 107.231 62.995  97.210  1.00 34.28  ? 954  MET A C   1 
ATOM   7399  O  O   . MET A 1 954  ? 106.571 62.115  96.650  1.00 35.13  ? 954  MET A O   1 
ATOM   7400  C  CB  . MET A 1 954  ? 108.004 62.863  99.492  1.00 32.98  ? 954  MET A CB  1 
ATOM   7401  C  CG  . MET A 1 954  ? 108.026 61.653  100.349 1.00 33.90  ? 954  MET A CG  1 
ATOM   7402  S  SD  . MET A 1 954  ? 107.181 60.160  99.853  1.00 35.73  ? 954  MET A SD  1 
ATOM   7403  C  CE  . MET A 1 954  ? 108.024 59.145  101.038 1.00 33.19  ? 954  MET A CE  1 
ATOM   7404  N  N   . GLN A 1 955  ? 106.937 64.289  97.136  1.00 34.52  ? 955  GLN A N   1 
ATOM   7405  C  CA  . GLN A 1 955  ? 105.676 64.750  96.570  1.00 34.72  ? 955  GLN A CA  1 
ATOM   7406  C  C   . GLN A 1 955  ? 105.782 64.988  95.076  1.00 35.59  ? 955  GLN A C   1 
ATOM   7407  O  O   . GLN A 1 955  ? 104.772 65.057  94.375  1.00 36.68  ? 955  GLN A O   1 
ATOM   7408  C  CB  . GLN A 1 955  ? 105.249 66.034  97.260  1.00 34.64  ? 955  GLN A CB  1 
ATOM   7409  C  CG  . GLN A 1 955  ? 105.061 65.920  98.746  1.00 32.54  ? 955  GLN A CG  1 
ATOM   7410  C  CD  . GLN A 1 955  ? 104.594 67.242  99.335  1.00 32.97  ? 955  GLN A CD  1 
ATOM   7411  O  OE1 . GLN A 1 955  ? 103.405 67.440  99.573  1.00 33.32  ? 955  GLN A OE1 1 
ATOM   7412  N  NE2 . GLN A 1 955  ? 105.522 68.167  99.524  1.00 31.91  ? 955  GLN A NE2 1 
ATOM   7413  N  N   . GLY A 1 956  ? 107.011 65.131  94.595  1.00 35.41  ? 956  GLY A N   1 
ATOM   7414  C  CA  . GLY A 1 956  ? 107.252 65.511  93.215  1.00 36.08  ? 956  GLY A CA  1 
ATOM   7415  C  C   . GLY A 1 956  ? 106.640 64.520  92.258  1.00 36.12  ? 956  GLY A C   1 
ATOM   7416  O  O   . GLY A 1 956  ? 106.604 63.325  92.532  1.00 35.59  ? 956  GLY A O   1 
ATOM   7417  N  N   . GLY A 1 957  ? 106.139 65.022  91.143  1.00 37.53  ? 957  GLY A N   1 
ATOM   7418  C  CA  . GLY A 1 957  ? 105.596 64.166  90.106  1.00 38.39  ? 957  GLY A CA  1 
ATOM   7419  C  C   . GLY A 1 957  ? 106.462 64.134  88.861  1.00 39.60  ? 957  GLY A C   1 
ATOM   7420  O  O   . GLY A 1 957  ? 105.936 64.081  87.755  1.00 40.95  ? 957  GLY A O   1 
ATOM   7421  N  N   . LEU A 1 958  ? 107.784 64.157  89.044  1.00 39.18  ? 958  LEU A N   1 
ATOM   7422  C  CA  . LEU A 1 958  ? 108.729 64.137  87.918  1.00 40.49  ? 958  LEU A CA  1 
ATOM   7423  C  C   . LEU A 1 958  ? 109.174 62.726  87.542  1.00 39.85  ? 958  LEU A C   1 
ATOM   7424  O  O   . LEU A 1 958  ? 109.762 62.529  86.487  1.00 41.30  ? 958  LEU A O   1 
ATOM   7425  C  CB  . LEU A 1 958  ? 109.967 64.993  88.225  1.00 41.00  ? 958  LEU A CB  1 
ATOM   7426  C  CG  . LEU A 1 958  ? 109.804 66.463  88.648  1.00 41.93  ? 958  LEU A CG  1 
ATOM   7427  C  CD1 . LEU A 1 958  ? 111.116 66.992  89.194  1.00 40.90  ? 958  LEU A CD1 1 
ATOM   7428  C  CD2 . LEU A 1 958  ? 109.342 67.310  87.472  1.00 44.09  ? 958  LEU A CD2 1 
ATOM   7429  N  N   . ARG A 1 959  ? 108.913 61.755  88.415  1.00 37.89  ? 959  ARG A N   1 
ATOM   7430  C  CA  . ARG A 1 959  ? 109.276 60.355  88.165  1.00 37.35  ? 959  ARG A CA  1 
ATOM   7431  C  C   . ARG A 1 959  ? 108.048 59.439  88.328  1.00 37.56  ? 959  ARG A C   1 
ATOM   7432  O  O   . ARG A 1 959  ? 108.091 58.442  89.063  1.00 36.63  ? 959  ARG A O   1 
ATOM   7433  C  CB  . ARG A 1 959  ? 110.425 59.910  89.089  1.00 35.42  ? 959  ARG A CB  1 
ATOM   7434  C  CG  . ARG A 1 959  ? 111.631 60.817  89.036  1.00 34.80  ? 959  ARG A CG  1 
ATOM   7435  C  CD  . ARG A 1 959  ? 112.799 60.366  89.868  1.00 31.94  ? 959  ARG A CD  1 
ATOM   7436  N  NE  . ARG A 1 959  ? 112.491 60.273  91.296  1.00 33.22  ? 959  ARG A NE  1 
ATOM   7437  C  CZ  . ARG A 1 959  ? 112.721 61.225  92.204  1.00 32.99  ? 959  ARG A CZ  1 
ATOM   7438  N  NH1 . ARG A 1 959  ? 113.247 62.393  91.858  1.00 31.47  ? 959  ARG A NH1 1 
ATOM   7439  N  NH2 . ARG A 1 959  ? 112.409 61.004  93.478  1.00 32.45  ? 959  ARG A NH2 1 
ATOM   7440  N  N   . ASN A 1 960  ? 106.950 59.807  87.659  1.00 38.83  ? 960  ASN A N   1 
ATOM   7441  C  CA  . ASN A 1 960  ? 105.707 59.024  87.652  1.00 39.29  ? 960  ASN A CA  1 
ATOM   7442  C  C   . ASN A 1 960  ? 105.060 58.767  89.013  1.00 38.30  ? 960  ASN A C   1 
ATOM   7443  O  O   . ASN A 1 960  ? 104.294 57.810  89.169  1.00 38.72  ? 960  ASN A O   1 
ATOM   7444  C  CB  . ASN A 1 960  ? 105.923 57.686  86.935  1.00 39.94  ? 960  ASN A CB  1 
ATOM   7445  C  CG  . ASN A 1 960  ? 106.453 57.860  85.538  1.00 41.55  ? 960  ASN A CG  1 
ATOM   7446  O  OD1 . ASN A 1 960  ? 105.789 58.446  84.677  1.00 42.31  ? 960  ASN A OD1 1 
ATOM   7447  N  ND2 . ASN A 1 960  ? 107.654 57.347  85.297  1.00 41.00  ? 960  ASN A ND2 1 
ATOM   7448  N  N   . GLY A 1 961  ? 105.380 59.590  90.005  1.00 37.12  ? 961  GLY A N   1 
ATOM   7449  C  CA  . GLY A 1 961  ? 104.709 59.500  91.295  1.00 36.20  ? 961  GLY A CA  1 
ATOM   7450  C  C   . GLY A 1 961  ? 105.004 58.234  92.065  1.00 35.57  ? 961  GLY A C   1 
ATOM   7451  O  O   . GLY A 1 961  ? 104.221 57.824  92.912  1.00 35.66  ? 961  GLY A O   1 
ATOM   7452  N  N   . VAL A 1 962  ? 106.156 57.632  91.796  1.00 35.60  ? 962  VAL A N   1 
ATOM   7453  C  CA  . VAL A 1 962  ? 106.522 56.368  92.411  1.00 34.73  ? 962  VAL A CA  1 
ATOM   7454  C  C   . VAL A 1 962  ? 106.801 56.499  93.908  1.00 33.65  ? 962  VAL A C   1 
ATOM   7455  O  O   . VAL A 1 962  ? 106.393 55.638  94.701  1.00 33.69  ? 962  VAL A O   1 
ATOM   7456  C  CB  . VAL A 1 962  ? 107.721 55.722  91.691  1.00 34.90  ? 962  VAL A CB  1 
ATOM   7457  C  CG1 . VAL A 1 962  ? 108.188 54.485  92.430  1.00 34.24  ? 962  VAL A CG1 1 
ATOM   7458  C  CG2 . VAL A 1 962  ? 107.333 55.355  90.270  1.00 36.26  ? 962  VAL A CG2 1 
ATOM   7459  N  N   . ALA A 1 963  ? 107.501 57.557  94.304  1.00 33.02  ? 963  ALA A N   1 
ATOM   7460  C  CA  . ALA A 1 963  ? 107.864 57.703  95.710  1.00 31.86  ? 963  ALA A CA  1 
ATOM   7461  C  C   . ALA A 1 963  ? 106.590 57.720  96.549  1.00 31.81  ? 963  ALA A C   1 
ATOM   7462  O  O   . ALA A 1 963  ? 106.411 56.884  97.448  1.00 31.70  ? 963  ALA A O   1 
ATOM   7463  C  CB  . ALA A 1 963  ? 108.689 58.965  95.940  1.00 31.72  ? 963  ALA A CB  1 
ATOM   7464  N  N   . LEU A 1 964  ? 105.686 58.638  96.206  1.00 31.81  ? 964  LEU A N   1 
ATOM   7465  C  CA  . LEU A 1 964  ? 104.492 58.870  97.007  1.00 31.43  ? 964  LEU A CA  1 
ATOM   7466  C  C   . LEU A 1 964  ? 103.563 57.661  96.991  1.00 31.90  ? 964  LEU A C   1 
ATOM   7467  O  O   . LEU A 1 964  ? 103.022 57.270  98.030  1.00 31.89  ? 964  LEU A O   1 
ATOM   7468  C  CB  . LEU A 1 964  ? 103.775 60.149  96.546  1.00 31.89  ? 964  LEU A CB  1 
ATOM   7469  C  CG  . LEU A 1 964  ? 102.540 60.598  97.322  1.00 31.74  ? 964  LEU A CG  1 
ATOM   7470  C  CD1 . LEU A 1 964  ? 102.859 60.825  98.793  1.00 30.60  ? 964  LEU A CD1 1 
ATOM   7471  C  CD2 . LEU A 1 964  ? 101.972 61.844  96.697  1.00 32.67  ? 964  LEU A CD2 1 
ATOM   7472  N  N   . THR A 1 965  ? 103.389 57.065  95.815  1.00 32.32  ? 965  THR A N   1 
ATOM   7473  C  CA  . THR A 1 965  ? 102.574 55.871  95.695  1.00 32.96  ? 965  THR A CA  1 
ATOM   7474  C  C   . THR A 1 965  ? 103.179 54.784  96.584  1.00 32.79  ? 965  THR A C   1 
ATOM   7475  O  O   . THR A 1 965  ? 102.472 54.157  97.381  1.00 32.98  ? 965  THR A O   1 
ATOM   7476  C  CB  . THR A 1 965  ? 102.448 55.423  94.222  1.00 33.84  ? 965  THR A CB  1 
ATOM   7477  O  OG1 . THR A 1 965  ? 101.904 56.502  93.460  1.00 34.95  ? 965  THR A OG1 1 
ATOM   7478  C  CG2 . THR A 1 965  ? 101.539 54.206  94.073  1.00 33.68  ? 965  THR A CG2 1 
ATOM   7479  N  N   . SER A 1 966  ? 104.492 54.599  96.487  1.00 32.21  ? 966  SER A N   1 
ATOM   7480  C  CA  . SER A 1 966  ? 105.155 53.597  97.302  1.00 32.66  ? 966  SER A CA  1 
ATOM   7481  C  C   . SER A 1 966  ? 105.000 53.869  98.794  1.00 32.12  ? 966  SER A C   1 
ATOM   7482  O  O   . SER A 1 966  ? 104.777 52.939  99.567  1.00 32.58  ? 966  SER A O   1 
ATOM   7483  C  CB  . SER A 1 966  ? 106.624 53.470  96.926  1.00 32.42  ? 966  SER A CB  1 
ATOM   7484  O  OG  . SER A 1 966  ? 106.753 53.080  95.566  1.00 34.46  ? 966  SER A OG  1 
ATOM   7485  N  N   . TYR A 1 967  ? 105.099 55.135  99.191  1.00 31.40  ? 967  TYR A N   1 
ATOM   7486  C  CA  . TYR A 1 967  ? 104.963 55.489  100.598 1.00 31.64  ? 967  TYR A CA  1 
ATOM   7487  C  C   . TYR A 1 967  ? 103.568 55.189  101.151 1.00 32.80  ? 967  TYR A C   1 
ATOM   7488  O  O   . TYR A 1 967  ? 103.440 54.531  102.188 1.00 32.82  ? 967  TYR A O   1 
ATOM   7489  C  CB  . TYR A 1 967  ? 105.317 56.955  100.844 1.00 31.32  ? 967  TYR A CB  1 
ATOM   7490  C  CG  . TYR A 1 967  ? 105.230 57.325  102.299 1.00 31.72  ? 967  TYR A CG  1 
ATOM   7491  C  CD1 . TYR A 1 967  ? 106.356 57.264  103.124 1.00 32.48  ? 967  TYR A CD1 1 
ATOM   7492  C  CD2 . TYR A 1 967  ? 104.020 57.712  102.866 1.00 32.41  ? 967  TYR A CD2 1 
ATOM   7493  C  CE1 . TYR A 1 967  ? 106.278 57.593  104.478 1.00 31.09  ? 967  TYR A CE1 1 
ATOM   7494  C  CE2 . TYR A 1 967  ? 103.933 58.029  104.220 1.00 32.98  ? 967  TYR A CE2 1 
ATOM   7495  C  CZ  . TYR A 1 967  ? 105.066 57.966  105.014 1.00 31.18  ? 967  TYR A CZ  1 
ATOM   7496  O  OH  . TYR A 1 967  ? 104.978 58.287  106.344 1.00 32.01  ? 967  TYR A OH  1 
ATOM   7497  N  N   . VAL A 1 968  ? 102.531 55.664  100.460 1.00 33.79  ? 968  VAL A N   1 
ATOM   7498  C  CA  . VAL A 1 968  ? 101.155 55.402  100.875 1.00 35.26  ? 968  VAL A CA  1 
ATOM   7499  C  C   . VAL A 1 968  ? 100.901 53.913  101.029 1.00 36.82  ? 968  VAL A C   1 
ATOM   7500  O  O   . VAL A 1 968  ? 100.337 53.476  102.035 1.00 38.16  ? 968  VAL A O   1 
ATOM   7501  C  CB  . VAL A 1 968  ? 100.124 55.991  99.907  1.00 36.11  ? 968  VAL A CB  1 
ATOM   7502  C  CG1 . VAL A 1 968  ? 98.721  55.614  100.345 1.00 37.26  ? 968  VAL A CG1 1 
ATOM   7503  C  CG2 . VAL A 1 968  ? 100.261 57.511  99.841  1.00 35.44  ? 968  VAL A CG2 1 
ATOM   7504  N  N   . LEU A 1 969  ? 101.336 53.127  100.053 1.00 37.28  ? 969  LEU A N   1 
ATOM   7505  C  CA  . LEU A 1 969  ? 101.165 51.682  100.146 1.00 38.82  ? 969  LEU A CA  1 
ATOM   7506  C  C   . LEU A 1 969  ? 101.923 51.132  101.344 1.00 38.68  ? 969  LEU A C   1 
ATOM   7507  O  O   . LEU A 1 969  ? 101.363 50.400  102.157 1.00 40.04  ? 969  LEU A O   1 
ATOM   7508  C  CB  . LEU A 1 969  ? 101.596 50.996  98.855  1.00 39.22  ? 969  LEU A CB  1 
ATOM   7509  C  CG  . LEU A 1 969  ? 100.749 51.434  97.655  1.00 40.42  ? 969  LEU A CG  1 
ATOM   7510  C  CD1 . LEU A 1 969  ? 101.484 51.182  96.347  1.00 41.86  ? 969  LEU A CD1 1 
ATOM   7511  C  CD2 . LEU A 1 969  ? 99.422  50.745  97.672  1.00 42.42  ? 969  LEU A CD2 1 
ATOM   7512  N  N   . MET A 1 970  ? 103.189 51.515  101.458 1.00 37.51  ? 970  MET A N   1 
ATOM   7513  C  CA  . MET A 1 970  ? 104.030 51.134  102.586 1.00 37.05  ? 970  MET A CA  1 
ATOM   7514  C  C   . MET A 1 970  ? 103.344 51.439  103.933 1.00 37.68  ? 970  MET A C   1 
ATOM   7515  O  O   . MET A 1 970  ? 103.243 50.565  104.794 1.00 38.34  ? 970  MET A O   1 
ATOM   7516  C  CB  . MET A 1 970  ? 105.372 51.854  102.444 1.00 35.64  ? 970  MET A CB  1 
ATOM   7517  C  CG  . MET A 1 970  ? 106.423 51.536  103.467 1.00 35.03  ? 970  MET A CG  1 
ATOM   7518  S  SD  . MET A 1 970  ? 106.308 52.564  104.928 1.00 37.03  ? 970  MET A SD  1 
ATOM   7519  C  CE  . MET A 1 970  ? 106.712 54.201  104.340 1.00 31.18  ? 970  MET A CE  1 
ATOM   7520  N  N   . ALA A 1 971  ? 102.856 52.668  104.101 1.00 37.28  ? 971  ALA A N   1 
ATOM   7521  C  CA  . ALA A 1 971  ? 102.215 53.069  105.346 1.00 37.76  ? 971  ALA A CA  1 
ATOM   7522  C  C   . ALA A 1 971  ? 100.980 52.221  105.663 1.00 39.79  ? 971  ALA A C   1 
ATOM   7523  O  O   . ALA A 1 971  ? 100.768 51.832  106.808 1.00 40.70  ? 971  ALA A O   1 
ATOM   7524  C  CB  . ALA A 1 971  ? 101.861 54.542  105.316 1.00 36.87  ? 971  ALA A CB  1 
ATOM   7525  N  N   . LEU A 1 972  ? 100.166 51.936  104.655 1.00 40.94  ? 972  LEU A N   1 
ATOM   7526  C  CA  . LEU A 1 972  ? 99.013  51.073  104.848 1.00 43.31  ? 972  LEU A CA  1 
ATOM   7527  C  C   . LEU A 1 972  ? 99.437  49.647  105.163 1.00 44.85  ? 972  LEU A C   1 
ATOM   7528  O  O   . LEU A 1 972  ? 98.838  48.984  106.016 1.00 46.86  ? 972  LEU A O   1 
ATOM   7529  C  CB  . LEU A 1 972  ? 98.108  51.091  103.622 1.00 43.79  ? 972  LEU A CB  1 
ATOM   7530  C  CG  . LEU A 1 972  ? 97.328  52.389  103.410 1.00 43.90  ? 972  LEU A CG  1 
ATOM   7531  C  CD1 . LEU A 1 972  ? 96.730  52.402  102.021 1.00 44.77  ? 972  LEU A CD1 1 
ATOM   7532  C  CD2 . LEU A 1 972  ? 96.245  52.598  104.465 1.00 43.89  ? 972  LEU A CD2 1 
ATOM   7533  N  N   . LEU A 1 973  ? 100.477 49.183  104.483 1.00 44.71  ? 973  LEU A N   1 
ATOM   7534  C  CA  . LEU A 1 973  ? 100.969 47.826  104.674 1.00 46.43  ? 973  LEU A CA  1 
ATOM   7535  C  C   . LEU A 1 973  ? 101.488 47.556  106.086 1.00 47.35  ? 973  LEU A C   1 
ATOM   7536  O  O   . LEU A 1 973  ? 101.324 46.452  106.598 1.00 48.92  ? 973  LEU A O   1 
ATOM   7537  C  CB  . LEU A 1 973  ? 102.012 47.468  103.613 1.00 45.19  ? 973  LEU A CB  1 
ATOM   7538  C  CG  . LEU A 1 973  ? 101.390 47.140  102.248 1.00 46.07  ? 973  LEU A CG  1 
ATOM   7539  C  CD1 . LEU A 1 973  ? 102.410 47.317  101.128 1.00 44.75  ? 973  LEU A CD1 1 
ATOM   7540  C  CD2 . LEU A 1 973  ? 100.752 45.744  102.202 1.00 45.56  ? 973  LEU A CD2 1 
ATOM   7541  N  N   . GLU A 1 974  ? 102.084 48.565  106.715 1.00 47.10  ? 974  GLU A N   1 
ATOM   7542  C  CA  . GLU A 1 974  ? 102.641 48.406  108.057 1.00 48.93  ? 974  GLU A CA  1 
ATOM   7543  C  C   . GLU A 1 974  ? 101.623 48.141  109.160 1.00 51.61  ? 974  GLU A C   1 
ATOM   7544  O  O   . GLU A 1 974  ? 101.984 47.618  110.209 1.00 52.75  ? 974  GLU A O   1 
ATOM   7545  C  CB  . GLU A 1 974  ? 103.576 49.559  108.428 1.00 47.01  ? 974  GLU A CB  1 
ATOM   7546  C  CG  . GLU A 1 974  ? 105.034 49.168  108.247 1.00 47.36  ? 974  GLU A CG  1 
ATOM   7547  C  CD  . GLU A 1 974  ? 105.989 50.334  108.137 1.00 47.88  ? 974  GLU A CD  1 
ATOM   7548  O  OE1 . GLU A 1 974  ? 105.548 51.505  108.068 1.00 49.58  ? 974  GLU A OE1 1 
ATOM   7549  O  OE2 . GLU A 1 974  ? 107.207 50.073  108.122 1.00 48.17  ? 974  GLU A OE2 1 
ATOM   7550  N  N   . ASN A 1 975  ? 100.356 48.463  108.915 1.00 53.64  ? 975  ASN A N   1 
ATOM   7551  C  CA  . ASN A 1 975  ? 99.313  48.217  109.906 1.00 56.80  ? 975  ASN A CA  1 
ATOM   7552  C  C   . ASN A 1 975  ? 98.213  47.277  109.422 1.00 59.20  ? 975  ASN A C   1 
ATOM   7553  O  O   . ASN A 1 975  ? 97.479  47.590  108.492 1.00 59.31  ? 975  ASN A O   1 
ATOM   7554  C  CB  . ASN A 1 975  ? 98.718  49.536  110.424 1.00 56.59  ? 975  ASN A CB  1 
ATOM   7555  C  CG  . ASN A 1 975  ? 97.877  49.335  111.676 1.00 61.03  ? 975  ASN A CG  1 
ATOM   7556  O  OD1 . ASN A 1 975  ? 98.357  49.538  112.796 1.00 64.00  ? 975  ASN A OD1 1 
ATOM   7557  N  ND2 . ASN A 1 975  ? 96.625  48.897  111.499 1.00 64.56  ? 975  ASN A ND2 1 
ATOM   7558  N  N   . ASP A 1 976  ? 98.103  46.132  110.087 1.00 61.93  ? 976  ASP A N   1 
ATOM   7559  C  CA  . ASP A 1 976  ? 97.145  45.081  109.736 1.00 65.19  ? 976  ASP A CA  1 
ATOM   7560  C  C   . ASP A 1 976  ? 95.698  45.555  109.552 1.00 66.52  ? 976  ASP A C   1 
ATOM   7561  O  O   . ASP A 1 976  ? 95.026  45.151  108.597 1.00 67.79  ? 976  ASP A O   1 
ATOM   7562  C  CB  . ASP A 1 976  ? 97.213  43.933  110.761 1.00 67.82  ? 976  ASP A CB  1 
ATOM   7563  C  CG  . ASP A 1 976  ? 98.544  43.162  110.706 1.00 68.52  ? 976  ASP A CG  1 
ATOM   7564  O  OD1 . ASP A 1 976  ? 99.347  43.393  109.764 1.00 67.51  ? 976  ASP A OD1 1 
ATOM   7565  O  OD2 . ASP A 1 976  ? 98.782  42.320  111.606 1.00 70.64  ? 976  ASP A OD2 1 
ATOM   7566  N  N   . ILE A 1 977  ? 95.227  46.403  110.463 1.00 66.63  ? 977  ILE A N   1 
ATOM   7567  C  CA  . ILE A 1 977  ? 93.862  46.917  110.402 1.00 67.92  ? 977  ILE A CA  1 
ATOM   7568  C  C   . ILE A 1 977  ? 93.654  47.792  109.160 1.00 66.33  ? 977  ILE A C   1 
ATOM   7569  O  O   . ILE A 1 977  ? 92.646  47.667  108.465 1.00 67.73  ? 977  ILE A O   1 
ATOM   7570  C  CB  . ILE A 1 977  ? 93.468  47.638  111.715 1.00 68.50  ? 977  ILE A CB  1 
ATOM   7571  C  CG1 . ILE A 1 977  ? 93.343  46.606  112.851 1.00 71.18  ? 977  ILE A CG1 1 
ATOM   7572  C  CG2 . ILE A 1 977  ? 92.158  48.411  111.547 1.00 69.70  ? 977  ILE A CG2 1 
ATOM   7573  C  CD1 . ILE A 1 977  ? 93.247  47.188  114.263 1.00 71.11  ? 977  ILE A CD1 1 
ATOM   7574  N  N   . ALA A 1 978  ? 94.622  48.650  108.866 1.00 63.74  ? 978  ALA A N   1 
ATOM   7575  C  CA  . ALA A 1 978  ? 94.563  49.487  107.667 1.00 62.46  ? 978  ALA A CA  1 
ATOM   7576  C  C   . ALA A 1 978  ? 94.709  48.642  106.399 1.00 62.92  ? 978  ALA A C   1 
ATOM   7577  O  O   . ALA A 1 978  ? 94.023  48.890  105.403 1.00 63.52  ? 978  ALA A O   1 
ATOM   7578  C  CB  . ALA A 1 978  ? 95.623  50.575  107.718 1.00 59.63  ? 978  ALA A CB  1 
ATOM   7579  N  N   . LYS A 1 979  ? 95.593  47.641  106.454 1.00 63.02  ? 979  LYS A N   1 
ATOM   7580  C  CA  . LYS A 1 979  ? 95.773  46.671  105.367 1.00 63.50  ? 979  LYS A CA  1 
ATOM   7581  C  C   . LYS A 1 979  ? 94.442  46.029  105.013 1.00 65.89  ? 979  LYS A C   1 
ATOM   7582  O  O   . LYS A 1 979  ? 94.043  46.037  103.853 1.00 66.55  ? 979  LYS A O   1 
ATOM   7583  C  CB  . LYS A 1 979  ? 96.811  45.597  105.743 1.00 63.74  ? 979  LYS A CB  1 
ATOM   7584  C  CG  . LYS A 1 979  ? 97.067  44.535  104.655 1.00 65.39  ? 979  LYS A CG  1 
ATOM   7585  C  CD  . LYS A 1 979  ? 98.412  43.810  104.814 1.00 65.73  ? 979  LYS A CD  1 
ATOM   7586  C  CE  . LYS A 1 979  ? 98.328  42.589  105.722 1.00 69.18  ? 979  LYS A CE  1 
ATOM   7587  N  NZ  . LYS A 1 979  ? 97.605  41.430  105.085 1.00 72.84  ? 979  LYS A NZ  1 
ATOM   7588  N  N   . ALA A 1 980  ? 93.753  45.504  106.022 1.00 67.67  ? 980  ALA A N   1 
ATOM   7589  C  CA  . ALA A 1 980  ? 92.478  44.817  105.828 1.00 70.57  ? 980  ALA A CA  1 
ATOM   7590  C  C   . ALA A 1 980  ? 91.387  45.738  105.287 1.00 70.84  ? 980  ALA A C   1 
ATOM   7591  O  O   . ALA A 1 980  ? 90.605  45.341  104.417 1.00 72.59  ? 980  ALA A O   1 
ATOM   7592  C  CB  . ALA A 1 980  ? 92.026  44.154  107.132 1.00 72.87  ? 980  ALA A CB  1 
ATOM   7593  N  N   . LYS A 1 981  ? 91.350  46.969  105.793 1.00 69.22  ? 981  LYS A N   1 
ATOM   7594  C  CA  . LYS A 1 981  ? 90.275  47.907  105.462 1.00 69.84  ? 981  LYS A CA  1 
ATOM   7595  C  C   . LYS A 1 981  ? 90.523  48.725  104.191 1.00 67.53  ? 981  LYS A C   1 
ATOM   7596  O  O   . LYS A 1 981  ? 89.648  49.471  103.750 1.00 68.31  ? 981  LYS A O   1 
ATOM   7597  C  CB  . LYS A 1 981  ? 89.958  48.816  106.656 1.00 69.91  ? 981  LYS A CB  1 
ATOM   7598  C  CG  . LYS A 1 981  ? 89.161  48.116  107.768 1.00 74.37  ? 981  LYS A CG  1 
ATOM   7599  C  CD  . LYS A 1 981  ? 89.271  48.844  109.117 1.00 76.45  ? 981  LYS A CD  1 
ATOM   7600  C  CE  . LYS A 1 981  ? 88.412  50.115  109.177 1.00 78.01  ? 981  LYS A CE  1 
ATOM   7601  N  NZ  . LYS A 1 981  ? 88.596  50.878  110.455 1.00 78.54  ? 981  LYS A NZ  1 
ATOM   7602  N  N   . HIS A 1 982  ? 91.704  48.585  103.601 1.00 64.76  ? 982  HIS A N   1 
ATOM   7603  C  CA  . HIS A 1 982  ? 91.986  49.233  102.324 1.00 63.12  ? 982  HIS A CA  1 
ATOM   7604  C  C   . HIS A 1 982  ? 92.760  48.308  101.367 1.00 62.58  ? 982  HIS A C   1 
ATOM   7605  O  O   . HIS A 1 982  ? 93.801  48.681  100.807 1.00 60.48  ? 982  HIS A O   1 
ATOM   7606  C  CB  . HIS A 1 982  ? 92.681  50.587  102.537 1.00 60.69  ? 982  HIS A CB  1 
ATOM   7607  C  CG  . HIS A 1 982  ? 91.814  51.605  103.220 1.00 61.58  ? 982  HIS A CG  1 
ATOM   7608  N  ND1 . HIS A 1 982  ? 91.918  51.891  104.566 1.00 60.93  ? 982  HIS A ND1 1 
ATOM   7609  C  CD2 . HIS A 1 982  ? 90.807  52.380  102.748 1.00 62.48  ? 982  HIS A CD2 1 
ATOM   7610  C  CE1 . HIS A 1 982  ? 91.022  52.807  104.890 1.00 61.80  ? 982  HIS A CE1 1 
ATOM   7611  N  NE2 . HIS A 1 982  ? 90.338  53.123  103.805 1.00 62.65  ? 982  HIS A NE2 1 
ATOM   7612  N  N   . ALA A 1 983  ? 92.223  47.101  101.185 1.00 64.31  ? 983  ALA A N   1 
ATOM   7613  C  CA  . ALA A 1 983  ? 92.795  46.110  100.286 1.00 64.08  ? 983  ALA A CA  1 
ATOM   7614  C  C   . ALA A 1 983  ? 92.773  46.597  98.839  1.00 63.28  ? 983  ALA A C   1 
ATOM   7615  O  O   . ALA A 1 983  ? 93.722  46.381  98.093  1.00 62.27  ? 983  ALA A O   1 
ATOM   7616  C  CB  . ALA A 1 983  ? 92.054  44.792  100.418 1.00 67.17  ? 983  ALA A CB  1 
ATOM   7617  N  N   . GLU A 1 984  ? 91.688  47.267  98.464  1.00 63.81  ? 984  GLU A N   1 
ATOM   7618  C  CA  . GLU A 1 984  ? 91.513  47.838  97.134  1.00 63.45  ? 984  GLU A CA  1 
ATOM   7619  C  C   . GLU A 1 984  ? 92.659  48.788  96.760  1.00 59.46  ? 984  GLU A C   1 
ATOM   7620  O  O   . GLU A 1 984  ? 93.245  48.668  95.680  1.00 59.18  ? 984  GLU A O   1 
ATOM   7621  C  CB  . GLU A 1 984  ? 90.167  48.570  97.070  1.00 65.65  ? 984  GLU A CB  1 
ATOM   7622  C  CG  . GLU A 1 984  ? 89.622  48.827  95.670  1.00 69.69  ? 984  GLU A CG  1 
ATOM   7623  C  CD  . GLU A 1 984  ? 88.473  49.845  95.661  1.00 75.04  ? 984  GLU A CD  1 
ATOM   7624  O  OE1 . GLU A 1 984  ? 87.391  49.553  96.237  1.00 78.56  ? 984  GLU A OE1 1 
ATOM   7625  O  OE2 . GLU A 1 984  ? 88.652  50.940  95.071  1.00 75.12  ? 984  GLU A OE2 1 
ATOM   7626  N  N   . VAL A 1 985  ? 92.981  49.714  97.662  1.00 56.21  ? 985  VAL A N   1 
ATOM   7627  C  CA  . VAL A 1 985  ? 94.064  50.677  97.451  1.00 52.31  ? 985  VAL A CA  1 
ATOM   7628  C  C   . VAL A 1 985  ? 95.425  49.998  97.246  1.00 50.47  ? 985  VAL A C   1 
ATOM   7629  O  O   . VAL A 1 985  ? 96.174  50.361  96.339  1.00 49.05  ? 985  VAL A O   1 
ATOM   7630  C  CB  . VAL A 1 985  ? 94.126  51.721  98.597  1.00 50.92  ? 985  VAL A CB  1 
ATOM   7631  C  CG1 . VAL A 1 985  ? 95.322  52.663  98.434  1.00 47.78  ? 985  VAL A CG1 1 
ATOM   7632  C  CG2 . VAL A 1 985  ? 92.827  52.514  98.655  1.00 51.52  ? 985  VAL A CG2 1 
ATOM   7633  N  N   . ILE A 1 986  ? 95.726  49.005  98.075  1.00 50.23  ? 986  ILE A N   1 
ATOM   7634  C  CA  . ILE A 1 986  ? 96.965  48.247  97.949  1.00 49.15  ? 986  ILE A CA  1 
ATOM   7635  C  C   . ILE A 1 986  ? 97.030  47.498  96.606  1.00 50.59  ? 986  ILE A C   1 
ATOM   7636  O  O   . ILE A 1 986  ? 98.025  47.598  95.881  1.00 49.85  ? 986  ILE A O   1 
ATOM   7637  C  CB  . ILE A 1 986  ? 97.178  47.303  99.157  1.00 49.49  ? 986  ILE A CB  1 
ATOM   7638  C  CG1 . ILE A 1 986  ? 97.451  48.132  100.419 1.00 47.83  ? 986  ILE A CG1 1 
ATOM   7639  C  CG2 . ILE A 1 986  ? 98.357  46.370  98.917  1.00 48.64  ? 986  ILE A CG2 1 
ATOM   7640  C  CD1 . ILE A 1 986  ? 96.889  47.540  101.696 1.00 49.35  ? 986  ILE A CD1 1 
ATOM   7641  N  N   . GLN A 1 987  ? 95.966  46.779  96.266  1.00 52.59  ? 987  GLN A N   1 
ATOM   7642  C  CA  . GLN A 1 987  ? 95.889  46.076  94.995  1.00 54.32  ? 987  GLN A CA  1 
ATOM   7643  C  C   . GLN A 1 987  ? 96.187  47.017  93.823  1.00 53.07  ? 987  GLN A C   1 
ATOM   7644  O  O   . GLN A 1 987  ? 97.133  46.786  93.067  1.00 52.65  ? 987  GLN A O   1 
ATOM   7645  C  CB  . GLN A 1 987  ? 94.514  45.431  94.828  1.00 57.56  ? 987  GLN A CB  1 
ATOM   7646  C  CG  . GLN A 1 987  ? 94.276  44.801  93.471  1.00 61.33  ? 987  GLN A CG  1 
ATOM   7647  C  CD  . GLN A 1 987  ? 94.282  43.286  93.519  1.00 66.39  ? 987  GLN A CD  1 
ATOM   7648  O  OE1 . GLN A 1 987  ? 93.866  42.687  94.517  1.00 68.90  ? 987  GLN A OE1 1 
ATOM   7649  N  NE2 . GLN A 1 987  ? 94.738  42.652  92.432  1.00 67.20  ? 987  GLN A NE2 1 
ATOM   7650  N  N   . LYS A 1 988  ? 95.393  48.082  93.688  1.00 52.55  ? 988  LYS A N   1 
ATOM   7651  C  CA  . LYS A 1 988  ? 95.581  49.043  92.603  1.00 51.43  ? 988  LYS A CA  1 
ATOM   7652  C  C   . LYS A 1 988  ? 96.982  49.638  92.671  1.00 48.47  ? 988  LYS A C   1 
ATOM   7653  O  O   . LYS A 1 988  ? 97.637  49.825  91.648  1.00 48.08  ? 988  LYS A O   1 
ATOM   7654  C  CB  . LYS A 1 988  ? 94.527  50.153  92.636  1.00 52.07  ? 988  LYS A CB  1 
ATOM   7655  C  CG  . LYS A 1 988  ? 93.090  49.691  92.402  1.00 55.65  ? 988  LYS A CG  1 
ATOM   7656  C  CD  . LYS A 1 988  ? 92.195  50.818  91.873  1.00 58.01  ? 988  LYS A CD  1 
ATOM   7657  C  CE  . LYS A 1 988  ? 91.838  51.857  92.940  1.00 59.13  ? 988  LYS A CE  1 
ATOM   7658  N  NZ  . LYS A 1 988  ? 91.168  53.091  92.380  1.00 60.21  ? 988  LYS A NZ  1 
ATOM   7659  N  N   . GLY A 1 989  ? 97.441  49.915  93.887  1.00 46.45  ? 989  GLY A N   1 
ATOM   7660  C  CA  . GLY A 1 989  ? 98.760  50.498  94.100  1.00 43.65  ? 989  GLY A CA  1 
ATOM   7661  C  C   . GLY A 1 989  ? 99.866  49.586  93.616  1.00 43.34  ? 989  GLY A C   1 
ATOM   7662  O  O   . GLY A 1 989  ? 100.759 50.026  92.885  1.00 42.18  ? 989  GLY A O   1 
ATOM   7663  N  N   . MET A 1 990  ? 99.792  48.309  94.007  1.00 44.19  ? 990  MET A N   1 
ATOM   7664  C  CA  . MET A 1 990  ? 100.811 47.325  93.632  1.00 44.17  ? 990  MET A CA  1 
ATOM   7665  C  C   . MET A 1 990  ? 100.818 47.063  92.126  1.00 44.98  ? 990  MET A C   1 
ATOM   7666  O  O   . MET A 1 990  ? 101.873 46.839  91.560  1.00 44.77  ? 990  MET A O   1 
ATOM   7667  C  CB  . MET A 1 990  ? 100.668 46.004  94.400  1.00 45.43  ? 990  MET A CB  1 
ATOM   7668  C  CG  . MET A 1 990  ? 100.967 46.031  95.904  1.00 45.89  ? 990  MET A CG  1 
ATOM   7669  S  SD  . MET A 1 990  ? 102.355 47.030  96.527  1.00 47.42  ? 990  MET A SD  1 
ATOM   7670  C  CE  . MET A 1 990  ? 103.750 46.189  95.794  1.00 47.26  ? 990  MET A CE  1 
ATOM   7671  N  N   . THR A 1 991  ? 99.653  47.098  91.478  1.00 46.33  ? 991  THR A N   1 
ATOM   7672  C  CA  . THR A 1 991  ? 99.607  47.036  90.009  1.00 47.36  ? 991  THR A CA  1 
ATOM   7673  C  C   . THR A 1 991  ? 100.395 48.190  89.372  1.00 45.84  ? 991  THR A C   1 
ATOM   7674  O  O   . THR A 1 991  ? 101.136 47.991  88.407  1.00 45.93  ? 991  THR A O   1 
ATOM   7675  C  CB  . THR A 1 991  ? 98.171  47.067  89.452  1.00 49.27  ? 991  THR A CB  1 
ATOM   7676  O  OG1 . THR A 1 991  ? 97.391  46.039  90.061  1.00 51.02  ? 991  THR A OG1 1 
ATOM   7677  C  CG2 . THR A 1 991  ? 98.186  46.840  87.954  1.00 50.41  ? 991  THR A CG2 1 
ATOM   7678  N  N   . TYR A 1 992  ? 100.226 49.390  89.920  1.00 44.26  ? 992  TYR A N   1 
ATOM   7679  C  CA  . TYR A 1 992  ? 100.892 50.555  89.387  1.00 43.47  ? 992  TYR A CA  1 
ATOM   7680  C  C   . TYR A 1 992  ? 102.405 50.391  89.417  1.00 42.58  ? 992  TYR A C   1 
ATOM   7681  O  O   . TYR A 1 992  ? 103.078 50.622  88.406  1.00 42.65  ? 992  TYR A O   1 
ATOM   7682  C  CB  . TYR A 1 992  ? 100.480 51.822  90.140  1.00 42.32  ? 992  TYR A CB  1 
ATOM   7683  C  CG  . TYR A 1 992  ? 101.079 53.072  89.539  1.00 41.53  ? 992  TYR A CG  1 
ATOM   7684  C  CD1 . TYR A 1 992  ? 100.655 53.536  88.296  1.00 42.35  ? 992  TYR A CD1 1 
ATOM   7685  C  CD2 . TYR A 1 992  ? 102.088 53.778  90.201  1.00 40.31  ? 992  TYR A CD2 1 
ATOM   7686  C  CE1 . TYR A 1 992  ? 101.201 54.671  87.726  1.00 42.82  ? 992  TYR A CE1 1 
ATOM   7687  C  CE2 . TYR A 1 992  ? 102.648 54.924  89.636  1.00 39.75  ? 992  TYR A CE2 1 
ATOM   7688  C  CZ  . TYR A 1 992  ? 102.194 55.362  88.397  1.00 41.53  ? 992  TYR A CZ  1 
ATOM   7689  O  OH  . TYR A 1 992  ? 102.723 56.490  87.820  1.00 42.02  ? 992  TYR A OH  1 
ATOM   7690  N  N   . LEU A 1 993  ? 102.924 49.996  90.580  1.00 41.72  ? 993  LEU A N   1 
ATOM   7691  C  CA  . LEU A 1 993  ? 104.356 49.817  90.777  1.00 40.91  ? 993  LEU A CA  1 
ATOM   7692  C  C   . LEU A 1 993  ? 104.878 48.763  89.827  1.00 42.98  ? 993  LEU A C   1 
ATOM   7693  O  O   . LEU A 1 993  ? 105.912 48.942  89.189  1.00 43.26  ? 993  LEU A O   1 
ATOM   7694  C  CB  . LEU A 1 993  ? 104.669 49.423  92.225  1.00 39.35  ? 993  LEU A CB  1 
ATOM   7695  C  CG  . LEU A 1 993  ? 104.374 50.430  93.351  1.00 36.87  ? 993  LEU A CG  1 
ATOM   7696  C  CD1 . LEU A 1 993  ? 104.851 49.869  94.664  1.00 35.10  ? 993  LEU A CD1 1 
ATOM   7697  C  CD2 . LEU A 1 993  ? 104.981 51.808  93.116  1.00 33.03  ? 993  LEU A CD2 1 
ATOM   7698  N  N   . SER A 1 994  ? 104.133 47.673  89.724  1.00 45.28  ? 994  SER A N   1 
ATOM   7699  C  CA  . SER A 1 994  ? 104.447 46.596  88.821  1.00 47.62  ? 994  SER A CA  1 
ATOM   7700  C  C   . SER A 1 994  ? 104.608 47.124  87.395  1.00 48.81  ? 994  SER A C   1 
ATOM   7701  O  O   . SER A 1 994  ? 105.531 46.731  86.693  1.00 49.88  ? 994  SER A O   1 
ATOM   7702  C  CB  . SER A 1 994  ? 103.348 45.548  88.896  1.00 49.52  ? 994  SER A CB  1 
ATOM   7703  O  OG  . SER A 1 994  ? 103.756 44.349  88.265  1.00 54.10  ? 994  SER A OG  1 
ATOM   7704  N  N   . ASN A 1 995  ? 103.725 48.029  86.979  1.00 49.34  ? 995  ASN A N   1 
ATOM   7705  C  CA  . ASN A 1 995  ? 103.825 48.659  85.666  1.00 50.48  ? 995  ASN A CA  1 
ATOM   7706  C  C   . ASN A 1 995  ? 105.002 49.620  85.525  1.00 49.21  ? 995  ASN A C   1 
ATOM   7707  O  O   . ASN A 1 995  ? 105.608 49.714  84.461  1.00 50.50  ? 995  ASN A O   1 
ATOM   7708  C  CB  . ASN A 1 995  ? 102.534 49.404  85.324  1.00 51.55  ? 995  ASN A CB  1 
ATOM   7709  C  CG  . ASN A 1 995  ? 101.350 48.480  85.143  1.00 54.11  ? 995  ASN A CG  1 
ATOM   7710  O  OD1 . ASN A 1 995  ? 101.468 47.368  84.621  1.00 56.21  ? 995  ASN A OD1 1 
ATOM   7711  N  ND2 . ASN A 1 995  ? 100.189 48.946  85.567  1.00 55.81  ? 995  ASN A ND2 1 
ATOM   7712  N  N   . GLN A 1 996  ? 105.317 50.336  86.596  1.00 47.16  ? 996  GLN A N   1 
ATOM   7713  C  CA  . GLN A 1 996  ? 106.352 51.361  86.547  1.00 46.14  ? 996  GLN A CA  1 
ATOM   7714  C  C   . GLN A 1 996  ? 107.759 50.818  86.795  1.00 45.52  ? 996  GLN A C   1 
ATOM   7715  O  O   . GLN A 1 996  ? 108.745 51.519  86.568  1.00 45.30  ? 996  GLN A O   1 
ATOM   7716  C  CB  . GLN A 1 996  ? 106.039 52.488  87.542  1.00 44.40  ? 996  GLN A CB  1 
ATOM   7717  C  CG  . GLN A 1 996  ? 104.735 53.239  87.247  1.00 45.29  ? 996  GLN A CG  1 
ATOM   7718  C  CD  . GLN A 1 996  ? 104.697 53.880  85.855  1.00 46.85  ? 996  GLN A CD  1 
ATOM   7719  O  OE1 . GLN A 1 996  ? 105.692 54.434  85.383  1.00 47.33  ? 996  GLN A OE1 1 
ATOM   7720  N  NE2 . GLN A 1 996  ? 103.540 53.820  85.207  1.00 47.40  ? 996  GLN A NE2 1 
ATOM   7721  N  N   . PHE A 1 997  ? 107.849 49.568  87.233  1.00 45.63  ? 997  PHE A N   1 
ATOM   7722  C  CA  . PHE A 1 997  ? 109.101 49.039  87.763  1.00 45.07  ? 997  PHE A CA  1 
ATOM   7723  C  C   . PHE A 1 997  ? 110.313 49.218  86.862  1.00 46.16  ? 997  PHE A C   1 
ATOM   7724  O  O   . PHE A 1 997  ? 111.386 49.589  87.344  1.00 45.24  ? 997  PHE A O   1 
ATOM   7725  C  CB  . PHE A 1 997  ? 108.978 47.566  88.146  1.00 45.73  ? 997  PHE A CB  1 
ATOM   7726  C  CG  . PHE A 1 997  ? 110.251 46.993  88.685  1.00 44.26  ? 997  PHE A CG  1 
ATOM   7727  C  CD1 . PHE A 1 997  ? 110.580 47.148  90.024  1.00 41.86  ? 997  PHE A CD1 1 
ATOM   7728  C  CD2 . PHE A 1 997  ? 111.134 46.320  87.852  1.00 44.67  ? 997  PHE A CD2 1 
ATOM   7729  C  CE1 . PHE A 1 997  ? 111.771 46.633  90.524  1.00 41.09  ? 997  PHE A CE1 1 
ATOM   7730  C  CE2 . PHE A 1 997  ? 112.328 45.798  88.346  1.00 44.43  ? 997  PHE A CE2 1 
ATOM   7731  C  CZ  . PHE A 1 997  ? 112.648 45.960  89.684  1.00 42.06  ? 997  PHE A CZ  1 
ATOM   7732  N  N   . GLY A 1 998  ? 110.146 48.931  85.571  1.00 48.42  ? 998  GLY A N   1 
ATOM   7733  C  CA  . GLY A 1 998  ? 111.233 49.025  84.600  1.00 49.75  ? 998  GLY A CA  1 
ATOM   7734  C  C   . GLY A 1 998  ? 111.795 50.424  84.418  1.00 49.74  ? 998  GLY A C   1 
ATOM   7735  O  O   . GLY A 1 998  ? 112.890 50.579  83.897  1.00 50.87  ? 998  GLY A O   1 
ATOM   7736  N  N   . SER A 1 999  ? 111.051 51.443  84.846  1.00 49.10  ? 999  SER A N   1 
ATOM   7737  C  CA  . SER A 1 999  ? 111.495 52.836  84.742  1.00 49.08  ? 999  SER A CA  1 
ATOM   7738  C  C   . SER A 1 999  ? 111.944 53.456  86.067  1.00 47.12  ? 999  SER A C   1 
ATOM   7739  O  O   . SER A 1 999  ? 112.426 54.590  86.073  1.00 47.29  ? 999  SER A O   1 
ATOM   7740  C  CB  . SER A 1 999  ? 110.388 53.717  84.170  1.00 49.65  ? 999  SER A CB  1 
ATOM   7741  O  OG  . SER A 1 999  ? 109.803 53.127  83.038  1.00 53.09  ? 999  SER A OG  1 
ATOM   7742  N  N   . ILE A 1 1000 ? 111.762 52.751  87.182  1.00 45.53  ? 1000 ILE A N   1 
ATOM   7743  C  CA  . ILE A 1 1000 ? 112.199 53.273  88.479  1.00 43.69  ? 1000 ILE A CA  1 
ATOM   7744  C  C   . ILE A 1 1000 ? 113.722 53.286  88.518  1.00 44.24  ? 1000 ILE A C   1 
ATOM   7745  O  O   . ILE A 1 1000 ? 114.361 52.244  88.688  1.00 44.93  ? 1000 ILE A O   1 
ATOM   7746  C  CB  . ILE A 1 1000 ? 111.628 52.470  89.656  1.00 42.46  ? 1000 ILE A CB  1 
ATOM   7747  C  CG1 . ILE A 1 1000 ? 110.103 52.372  89.535  1.00 41.84  ? 1000 ILE A CG1 1 
ATOM   7748  C  CG2 . ILE A 1 1000 ? 112.021 53.124  90.984  1.00 41.36  ? 1000 ILE A CG2 1 
ATOM   7749  C  CD1 . ILE A 1 1000 ? 109.461 51.520  90.579  1.00 40.10  ? 1000 ILE A CD1 1 
ATOM   7750  N  N   . ASN A 1 1001 ? 114.300 54.466  88.317  1.00 44.43  ? 1001 ASN A N   1 
ATOM   7751  C  CA  . ASN A 1 1001 ? 115.750 54.595  88.184  1.00 44.86  ? 1001 ASN A CA  1 
ATOM   7752  C  C   . ASN A 1 1001 ? 116.384 55.322  89.340  1.00 43.17  ? 1001 ASN A C   1 
ATOM   7753  O  O   . ASN A 1 1001 ? 117.601 55.465  89.402  1.00 44.08  ? 1001 ASN A O   1 
ATOM   7754  C  CB  . ASN A 1 1001 ? 116.081 55.314  86.896  1.00 46.79  ? 1001 ASN A CB  1 
ATOM   7755  C  CG  . ASN A 1 1001 ? 115.745 54.486  85.688  1.00 50.81  ? 1001 ASN A CG  1 
ATOM   7756  O  OD1 . ASN A 1 1001 ? 116.034 53.283  85.654  1.00 53.77  ? 1001 ASN A OD1 1 
ATOM   7757  N  ND2 . ASN A 1 1001 ? 115.122 55.113  84.683  1.00 53.00  ? 1001 ASN A ND2 1 
ATOM   7758  N  N   . ASN A 1 1002 ? 115.540 55.779  90.254  1.00 40.86  ? 1002 ASN A N   1 
ATOM   7759  C  CA  . ASN A 1 1002 ? 115.949 56.637  91.325  1.00 38.65  ? 1002 ASN A CA  1 
ATOM   7760  C  C   . ASN A 1 1002 ? 115.892 55.841  92.608  1.00 37.22  ? 1002 ASN A C   1 
ATOM   7761  O  O   . ASN A 1 1002 ? 114.833 55.324  92.987  1.00 36.14  ? 1002 ASN A O   1 
ATOM   7762  C  CB  . ASN A 1 1002 ? 115.028 57.844  91.370  1.00 38.20  ? 1002 ASN A CB  1 
ATOM   7763  C  CG  . ASN A 1 1002 ? 115.304 58.750  92.536  1.00 37.57  ? 1002 ASN A CG  1 
ATOM   7764  O  OD1 . ASN A 1 1002 ? 114.963 58.436  93.679  1.00 37.06  ? 1002 ASN A OD1 1 
ATOM   7765  N  ND2 . ASN A 1 1002 ? 115.893 59.898  92.257  1.00 37.82  ? 1002 ASN A ND2 1 
ATOM   7766  N  N   . ALA A 1 1003 ? 117.050 55.755  93.265  1.00 36.65  ? 1003 ALA A N   1 
ATOM   7767  C  CA  . ALA A 1 1003 ? 117.242 54.957  94.467  1.00 35.09  ? 1003 ALA A CA  1 
ATOM   7768  C  C   . ALA A 1 1003 ? 116.268 55.311  95.572  1.00 33.47  ? 1003 ALA A C   1 
ATOM   7769  O  O   . ALA A 1 1003 ? 115.872 54.451  96.343  1.00 33.05  ? 1003 ALA A O   1 
ATOM   7770  C  CB  . ALA A 1 1003 ? 118.672 55.091  94.961  1.00 35.51  ? 1003 ALA A CB  1 
ATOM   7771  N  N   . TYR A 1 1004 ? 115.889 56.579  95.666  1.00 32.97  ? 1004 TYR A N   1 
ATOM   7772  C  CA  . TYR A 1 1004 ? 114.948 56.983  96.705  1.00 31.65  ? 1004 TYR A CA  1 
ATOM   7773  C  C   . TYR A 1 1004 ? 113.637 56.247  96.466  1.00 31.18  ? 1004 TYR A C   1 
ATOM   7774  O  O   . TYR A 1 1004 ? 113.231 55.440  97.298  1.00 30.61  ? 1004 TYR A O   1 
ATOM   7775  C  CB  . TYR A 1 1004 ? 114.752 58.501  96.719  1.00 31.52  ? 1004 TYR A CB  1 
ATOM   7776  C  CG  . TYR A 1 1004 ? 113.807 59.035  97.792  1.00 30.83  ? 1004 TYR A CG  1 
ATOM   7777  C  CD1 . TYR A 1 1004 ? 114.096 58.884  99.145  1.00 30.26  ? 1004 TYR A CD1 1 
ATOM   7778  C  CD2 . TYR A 1 1004 ? 112.642 59.710  97.446  1.00 30.52  ? 1004 TYR A CD2 1 
ATOM   7779  C  CE1 . TYR A 1 1004 ? 113.251 59.376  100.112 1.00 29.36  ? 1004 TYR A CE1 1 
ATOM   7780  C  CE2 . TYR A 1 1004 ? 111.788 60.205  98.416  1.00 29.90  ? 1004 TYR A CE2 1 
ATOM   7781  C  CZ  . TYR A 1 1004 ? 112.105 60.040  99.743  1.00 28.99  ? 1004 TYR A CZ  1 
ATOM   7782  O  OH  . TYR A 1 1004 ? 111.272 60.535  100.712 1.00 29.25  ? 1004 TYR A OH  1 
ATOM   7783  N  N   . ASP A 1 1005 ? 113.020 56.501  95.307  1.00 31.45  ? 1005 ASP A N   1 
ATOM   7784  C  CA  . ASP A 1 1005 ? 111.779 55.840  94.894  1.00 31.47  ? 1005 ASP A CA  1 
ATOM   7785  C  C   . ASP A 1 1005 ? 111.867 54.318  95.026  1.00 31.94  ? 1005 ASP A C   1 
ATOM   7786  O  O   . ASP A 1 1005 ? 110.992 53.676  95.631  1.00 31.75  ? 1005 ASP A O   1 
ATOM   7787  C  CB  . ASP A 1 1005 ? 111.422 56.226  93.457  1.00 32.30  ? 1005 ASP A CB  1 
ATOM   7788  C  CG  . ASP A 1 1005 ? 111.301 57.730  93.266  1.00 32.48  ? 1005 ASP A CG  1 
ATOM   7789  O  OD1 . ASP A 1 1005 ? 111.023 58.183  92.147  1.00 32.23  ? 1005 ASP A OD1 1 
ATOM   7790  O  OD2 . ASP A 1 1005 ? 111.489 58.475  94.237  1.00 33.60  ? 1005 ASP A OD2 1 
ATOM   7791  N  N   . LEU A 1 1006 ? 112.939 53.746  94.487  1.00 32.47  ? 1006 LEU A N   1 
ATOM   7792  C  CA  . LEU A 1 1006 ? 113.108 52.299  94.496  1.00 33.07  ? 1006 LEU A CA  1 
ATOM   7793  C  C   . LEU A 1 1006 ? 113.177 51.725  95.901  1.00 32.60  ? 1006 LEU A C   1 
ATOM   7794  O  O   . LEU A 1 1006 ? 112.632 50.645  96.150  1.00 33.57  ? 1006 LEU A O   1 
ATOM   7795  C  CB  . LEU A 1 1006 ? 114.334 51.872  93.677  1.00 33.83  ? 1006 LEU A CB  1 
ATOM   7796  C  CG  . LEU A 1 1006 ? 114.548 50.378  93.447  1.00 33.57  ? 1006 LEU A CG  1 
ATOM   7797  C  CD1 . LEU A 1 1006 ? 113.338 49.747  92.801  1.00 32.30  ? 1006 LEU A CD1 1 
ATOM   7798  C  CD2 . LEU A 1 1006 ? 115.794 50.157  92.601  1.00 35.67  ? 1006 LEU A CD2 1 
ATOM   7799  N  N   . SER A 1 1007 ? 113.826 52.439  96.815  1.00 31.79  ? 1007 SER A N   1 
ATOM   7800  C  CA  . SER A 1 1007 ? 113.963 51.958  98.191  1.00 31.39  ? 1007 SER A CA  1 
ATOM   7801  C  C   . SER A 1 1007 ? 112.609 51.868  98.855  1.00 30.94  ? 1007 SER A C   1 
ATOM   7802  O  O   . SER A 1 1007 ? 112.334 50.902  99.560  1.00 31.50  ? 1007 SER A O   1 
ATOM   7803  C  CB  . SER A 1 1007 ? 114.894 52.841  99.013  1.00 30.85  ? 1007 SER A CB  1 
ATOM   7804  O  OG  . SER A 1 1007 ? 114.298 54.099  99.274  1.00 31.62  ? 1007 SER A OG  1 
ATOM   7805  N  N   . ILE A 1 1008 ? 111.752 52.858  98.614  1.00 30.65  ? 1008 ILE A N   1 
ATOM   7806  C  CA  . ILE A 1 1008 ? 110.401 52.814  99.161  1.00 30.72  ? 1008 ILE A CA  1 
ATOM   7807  C  C   . ILE A 1 1008 ? 109.577 51.737  98.473  1.00 31.92  ? 1008 ILE A C   1 
ATOM   7808  O  O   . ILE A 1 1008 ? 108.923 50.946  99.144  1.00 32.61  ? 1008 ILE A O   1 
ATOM   7809  C  CB  . ILE A 1 1008 ? 109.659 54.154  99.062  1.00 30.37  ? 1008 ILE A CB  1 
ATOM   7810  C  CG1 . ILE A 1 1008 ? 110.606 55.325  99.360  1.00 29.85  ? 1008 ILE A CG1 1 
ATOM   7811  C  CG2 . ILE A 1 1008 ? 108.440 54.142  99.995  1.00 29.81  ? 1008 ILE A CG2 1 
ATOM   7812  C  CD1 . ILE A 1 1008 ? 109.967 56.703  99.235  1.00 28.12  ? 1008 ILE A CD1 1 
ATOM   7813  N  N   . ALA A 1 1009 ? 109.629 51.696  97.143  1.00 32.83  ? 1009 ALA A N   1 
ATOM   7814  C  CA  . ALA A 1 1009 ? 108.848 50.721  96.372  1.00 34.20  ? 1009 ALA A CA  1 
ATOM   7815  C  C   . ALA A 1 1009 ? 109.223 49.307  96.780  1.00 35.21  ? 1009 ALA A C   1 
ATOM   7816  O  O   . ALA A 1 1009 ? 108.339 48.481  97.028  1.00 36.21  ? 1009 ALA A O   1 
ATOM   7817  C  CB  . ALA A 1 1009 ? 109.035 50.925  94.870  1.00 34.67  ? 1009 ALA A CB  1 
ATOM   7818  N  N   . THR A 1 1010 ? 110.529 49.044  96.871  1.00 35.20  ? 1010 THR A N   1 
ATOM   7819  C  CA  . THR A 1 1010 ? 111.030 47.756  97.344  1.00 36.38  ? 1010 THR A CA  1 
ATOM   7820  C  C   . THR A 1 1010 ? 110.450 47.380  98.713  1.00 36.61  ? 1010 THR A C   1 
ATOM   7821  O  O   . THR A 1 1010 ? 109.961 46.257  98.896  1.00 37.82  ? 1010 THR A O   1 
ATOM   7822  C  CB  . THR A 1 1010 ? 112.570 47.729  97.418  1.00 36.26  ? 1010 THR A CB  1 
ATOM   7823  O  OG1 . THR A 1 1010 ? 113.106 47.913  96.109  1.00 36.60  ? 1010 THR A OG1 1 
ATOM   7824  C  CG2 . THR A 1 1010 ? 113.075 46.393  97.983  1.00 36.84  ? 1010 THR A CG2 1 
ATOM   7825  N  N   . TYR A 1 1011 ? 110.508 48.310  99.663  1.00 35.48  ? 1011 TYR A N   1 
ATOM   7826  C  CA  . TYR A 1 1011 ? 110.044 48.020  101.016 1.00 36.21  ? 1011 TYR A CA  1 
ATOM   7827  C  C   . TYR A 1 1011 ? 108.534 47.727  101.037 1.00 37.12  ? 1011 TYR A C   1 
ATOM   7828  O  O   . TYR A 1 1011 ? 108.070 46.810  101.740 1.00 38.15  ? 1011 TYR A O   1 
ATOM   7829  C  CB  . TYR A 1 1011 ? 110.420 49.153  101.978 1.00 35.13  ? 1011 TYR A CB  1 
ATOM   7830  C  CG  . TYR A 1 1011 ? 109.964 48.945  103.407 1.00 35.57  ? 1011 TYR A CG  1 
ATOM   7831  C  CD1 . TYR A 1 1011 ? 110.077 47.701  104.029 1.00 37.45  ? 1011 TYR A CD1 1 
ATOM   7832  C  CD2 . TYR A 1 1011 ? 109.453 50.004  104.155 1.00 35.66  ? 1011 TYR A CD2 1 
ATOM   7833  C  CE1 . TYR A 1 1011 ? 109.664 47.510  105.341 1.00 37.51  ? 1011 TYR A CE1 1 
ATOM   7834  C  CE2 . TYR A 1 1011 ? 109.041 49.826  105.474 1.00 35.33  ? 1011 TYR A CE2 1 
ATOM   7835  C  CZ  . TYR A 1 1011 ? 109.151 48.582  106.055 1.00 36.94  ? 1011 TYR A CZ  1 
ATOM   7836  O  OH  . TYR A 1 1011 ? 108.746 48.402  107.352 1.00 38.08  ? 1011 TYR A OH  1 
ATOM   7837  N  N   . ALA A 1 1012 ? 107.774 48.487  100.252 1.00 36.53  ? 1012 ALA A N   1 
ATOM   7838  C  CA  . ALA A 1 1012 ? 106.359 48.213  100.104 1.00 37.06  ? 1012 ALA A CA  1 
ATOM   7839  C  C   . ALA A 1 1012 ? 106.189 46.787  99.582  1.00 38.93  ? 1012 ALA A C   1 
ATOM   7840  O  O   . ALA A 1 1012 ? 105.429 45.999  100.158 1.00 40.41  ? 1012 ALA A O   1 
ATOM   7841  C  CB  . ALA A 1 1012 ? 105.732 49.202  99.179  1.00 36.61  ? 1012 ALA A CB  1 
ATOM   7842  N  N   . MET A 1 1013 ? 106.926 46.445  98.523  1.00 38.75  ? 1013 MET A N   1 
ATOM   7843  C  CA  . MET A 1 1013 ? 106.856 45.108  97.925  1.00 40.23  ? 1013 MET A CA  1 
ATOM   7844  C  C   . MET A 1 1013 ? 107.190 44.002  98.926  1.00 41.22  ? 1013 MET A C   1 
ATOM   7845  O  O   . MET A 1 1013 ? 106.530 42.960  98.951  1.00 43.06  ? 1013 MET A O   1 
ATOM   7846  C  CB  . MET A 1 1013 ? 107.767 45.003  96.696  1.00 40.11  ? 1013 MET A CB  1 
ATOM   7847  C  CG  . MET A 1 1013 ? 107.220 45.693  95.466  1.00 39.93  ? 1013 MET A CG  1 
ATOM   7848  S  SD  . MET A 1 1013 ? 108.236 45.492  93.995  1.00 39.84  ? 1013 MET A SD  1 
ATOM   7849  C  CE  . MET A 1 1013 ? 107.120 46.100  92.747  1.00 40.79  ? 1013 MET A CE  1 
ATOM   7850  N  N   . MET A 1 1014 ? 108.215 44.232  99.744  1.00 40.20  ? 1014 MET A N   1 
ATOM   7851  C  CA  . MET A 1 1014 ? 108.601 43.273  100.768 1.00 41.18  ? 1014 MET A CA  1 
ATOM   7852  C  C   . MET A 1 1014 ? 107.439 43.072  101.742 1.00 42.04  ? 1014 MET A C   1 
ATOM   7853  O  O   . MET A 1 1014 ? 107.026 41.935  101.992 1.00 44.09  ? 1014 MET A O   1 
ATOM   7854  C  CB  . MET A 1 1014 ? 109.880 43.707  101.503 1.00 40.03  ? 1014 MET A CB  1 
ATOM   7855  C  CG  . MET A 1 1014 ? 111.165 43.641  100.665 1.00 39.83  ? 1014 MET A CG  1 
ATOM   7856  S  SD  . MET A 1 1014 ? 111.676 41.975  100.117 1.00 42.35  ? 1014 MET A SD  1 
ATOM   7857  C  CE  . MET A 1 1014 ? 111.911 41.179  101.702 1.00 44.59  ? 1014 MET A CE  1 
ATOM   7858  N  N   . LEU A 1 1015 ? 106.890 44.172  102.260 1.00 40.52  ? 1015 LEU A N   1 
ATOM   7859  C  CA  . LEU A 1 1015 ? 105.735 44.093  103.156 1.00 41.00  ? 1015 LEU A CA  1 
ATOM   7860  C  C   . LEU A 1 1015 ? 104.556 43.327  102.539 1.00 42.72  ? 1015 LEU A C   1 
ATOM   7861  O  O   . LEU A 1 1015 ? 103.834 42.616  103.228 1.00 44.76  ? 1015 LEU A O   1 
ATOM   7862  C  CB  . LEU A 1 1015 ? 105.290 45.488  103.571 1.00 39.20  ? 1015 LEU A CB  1 
ATOM   7863  C  CG  . LEU A 1 1015 ? 106.219 46.226  104.547 1.00 38.43  ? 1015 LEU A CG  1 
ATOM   7864  C  CD1 . LEU A 1 1015 ? 105.959 47.744  104.525 1.00 35.12  ? 1015 LEU A CD1 1 
ATOM   7865  C  CD2 . LEU A 1 1015 ? 106.107 45.658  105.966 1.00 37.87  ? 1015 LEU A CD2 1 
ATOM   7866  N  N   . ASN A 1 1016 ? 104.389 43.459  101.233 1.00 42.21  ? 1016 ASN A N   1 
ATOM   7867  C  CA  . ASN A 1 1016 ? 103.217 42.965  100.549 1.00 43.37  ? 1016 ASN A CA  1 
ATOM   7868  C  C   . ASN A 1 1016 ? 103.428 41.531  100.077 1.00 45.48  ? 1016 ASN A C   1 
ATOM   7869  O  O   . ASN A 1 1016 ? 102.470 40.813  99.766  1.00 47.29  ? 1016 ASN A O   1 
ATOM   7870  C  CB  . ASN A 1 1016 ? 102.937 43.899  99.372  1.00 42.51  ? 1016 ASN A CB  1 
ATOM   7871  C  CG  . ASN A 1 1016 ? 101.814 43.420  98.488  1.00 44.12  ? 1016 ASN A CG  1 
ATOM   7872  O  OD1 . ASN A 1 1016 ? 100.653 43.393  98.892  1.00 45.63  ? 1016 ASN A OD1 1 
ATOM   7873  N  ND2 . ASN A 1 1016 ? 102.152 43.055  97.263  1.00 44.72  ? 1016 ASN A ND2 1 
ATOM   7874  N  N   . GLY A 1 1017 ? 104.693 41.113  100.033 1.00 45.05  ? 1017 GLY A N   1 
ATOM   7875  C  CA  . GLY A 1 1017 ? 105.063 39.822  99.455  1.00 46.54  ? 1017 GLY A CA  1 
ATOM   7876  C  C   . GLY A 1 1017 ? 104.776 39.782  97.966  1.00 46.97  ? 1017 GLY A C   1 
ATOM   7877  O  O   . GLY A 1 1017 ? 104.311 38.779  97.447  1.00 49.19  ? 1017 GLY A O   1 
ATOM   7878  N  N   . HIS A 1 1018 ? 105.045 40.886  97.284  1.00 45.12  ? 1018 HIS A N   1 
ATOM   7879  C  CA  . HIS A 1 1018 ? 104.797 41.004  95.855  1.00 45.91  ? 1018 HIS A CA  1 
ATOM   7880  C  C   . HIS A 1 1018 ? 105.796 40.141  95.089  1.00 47.00  ? 1018 HIS A C   1 
ATOM   7881  O  O   . HIS A 1 1018 ? 106.962 40.087  95.470  1.00 46.13  ? 1018 HIS A O   1 
ATOM   7882  C  CB  . HIS A 1 1018 ? 104.970 42.468  95.469  1.00 43.77  ? 1018 HIS A CB  1 
ATOM   7883  C  CG  . HIS A 1 1018 ? 104.467 42.802  94.106  1.00 44.64  ? 1018 HIS A CG  1 
ATOM   7884  N  ND1 . HIS A 1 1018 ? 105.130 42.426  92.958  1.00 46.18  ? 1018 HIS A ND1 1 
ATOM   7885  C  CD2 . HIS A 1 1018 ? 103.374 43.491  93.704  1.00 45.45  ? 1018 HIS A CD2 1 
ATOM   7886  C  CE1 . HIS A 1 1018 ? 104.459 42.862  91.906  1.00 48.15  ? 1018 HIS A CE1 1 
ATOM   7887  N  NE2 . HIS A 1 1018 ? 103.392 43.516  92.331  1.00 47.29  ? 1018 HIS A NE2 1 
ATOM   7888  N  N   . THR A 1 1019 ? 105.361 39.469  94.019  1.00 49.10  ? 1019 THR A N   1 
ATOM   7889  C  CA  . THR A 1 1019 ? 106.276 38.595  93.259  1.00 50.88  ? 1019 THR A CA  1 
ATOM   7890  C  C   . THR A 1 1019 ? 107.581 39.284  92.860  1.00 49.10  ? 1019 THR A C   1 
ATOM   7891  O  O   . THR A 1 1019 ? 108.606 38.628  92.708  1.00 49.79  ? 1019 THR A O   1 
ATOM   7892  C  CB  . THR A 1 1019 ? 105.649 37.986  91.971  1.00 53.28  ? 1019 THR A CB  1 
ATOM   7893  O  OG1 . THR A 1 1019 ? 104.816 38.952  91.323  1.00 53.20  ? 1019 THR A OG1 1 
ATOM   7894  C  CG2 . THR A 1 1019 ? 104.837 36.736  92.286  1.00 57.11  ? 1019 THR A CG2 1 
ATOM   7895  N  N   . MET A 1 1020 ? 107.539 40.602  92.703  1.00 47.17  ? 1020 MET A N   1 
ATOM   7896  C  CA  . MET A 1 1020 ? 108.694 41.357  92.234  1.00 46.20  ? 1020 MET A CA  1 
ATOM   7897  C  C   . MET A 1 1020 ? 109.668 41.806  93.327  1.00 44.56  ? 1020 MET A C   1 
ATOM   7898  O  O   . MET A 1 1020 ? 110.656 42.489  93.033  1.00 43.45  ? 1020 MET A O   1 
ATOM   7899  C  CB  . MET A 1 1020 ? 108.237 42.567  91.421  1.00 45.51  ? 1020 MET A CB  1 
ATOM   7900  C  CG  . MET A 1 1020 ? 107.961 42.258  89.963  1.00 48.33  ? 1020 MET A CG  1 
ATOM   7901  S  SD  . MET A 1 1020 ? 107.285 43.723  89.186  1.00 50.66  ? 1020 MET A SD  1 
ATOM   7902  C  CE  . MET A 1 1020 ? 107.087 43.164  87.485  1.00 53.93  ? 1020 MET A CE  1 
ATOM   7903  N  N   . LYS A 1 1021 ? 109.406 41.423  94.574  1.00 44.43  ? 1021 LYS A N   1 
ATOM   7904  C  CA  . LYS A 1 1021 ? 110.213 41.913  95.689  1.00 43.27  ? 1021 LYS A CA  1 
ATOM   7905  C  C   . LYS A 1 1021 ? 111.702 41.564  95.556  1.00 43.80  ? 1021 LYS A C   1 
ATOM   7906  O  O   . LYS A 1 1021 ? 112.551 42.443  95.650  1.00 42.37  ? 1021 LYS A O   1 
ATOM   7907  C  CB  . LYS A 1 1021 ? 109.640 41.456  97.038  1.00 43.58  ? 1021 LYS A CB  1 
ATOM   7908  C  CG  . LYS A 1 1021 ? 109.523 39.964  97.199  1.00 45.10  ? 1021 LYS A CG  1 
ATOM   7909  C  CD  . LYS A 1 1021 ? 109.062 39.588  98.574  1.00 45.29  ? 1021 LYS A CD  1 
ATOM   7910  C  CE  . LYS A 1 1021 ? 109.117 38.088  98.750  1.00 47.73  ? 1021 LYS A CE  1 
ATOM   7911  N  NZ  . LYS A 1 1021 ? 109.350 37.737  100.163 1.00 49.06  ? 1021 LYS A NZ  1 
ATOM   7912  N  N   . GLU A 1 1022 ? 112.008 40.293  95.314  1.00 46.31  ? 1022 GLU A N   1 
ATOM   7913  C  CA  . GLU A 1 1022 ? 113.391 39.842  95.134  1.00 47.51  ? 1022 GLU A CA  1 
ATOM   7914  C  C   . GLU A 1 1022 ? 114.064 40.641  94.017  1.00 46.67  ? 1022 GLU A C   1 
ATOM   7915  O  O   . GLU A 1 1022 ? 115.220 41.052  94.135  1.00 45.94  ? 1022 GLU A O   1 
ATOM   7916  C  CB  . GLU A 1 1022 ? 113.453 38.327  94.838  1.00 50.19  ? 1022 GLU A CB  1 
ATOM   7917  C  CG  . GLU A 1 1022 ? 114.864 37.726  94.980  1.00 52.74  ? 1022 GLU A CG  1 
ATOM   7918  C  CD  . GLU A 1 1022 ? 114.998 36.301  94.427  1.00 59.43  ? 1022 GLU A CD  1 
ATOM   7919  O  OE1 . GLU A 1 1022 ? 114.755 36.071  93.209  1.00 60.72  ? 1022 GLU A OE1 1 
ATOM   7920  O  OE2 . GLU A 1 1022 ? 115.376 35.402  95.218  1.00 61.94  ? 1022 GLU A OE2 1 
ATOM   7921  N  N   . GLU A 1 1023 ? 113.317 40.869  92.945  1.00 47.02  ? 1023 GLU A N   1 
ATOM   7922  C  CA  . GLU A 1 1023 ? 113.818 41.600  91.793  1.00 47.05  ? 1023 GLU A CA  1 
ATOM   7923  C  C   . GLU A 1 1023 ? 114.085 43.059  92.147  1.00 44.38  ? 1023 GLU A C   1 
ATOM   7924  O  O   . GLU A 1 1023 ? 115.120 43.608  91.763  1.00 44.71  ? 1023 GLU A O   1 
ATOM   7925  C  CB  . GLU A 1 1023 ? 112.816 41.507  90.656  1.00 48.32  ? 1023 GLU A CB  1 
ATOM   7926  C  CG  . GLU A 1 1023 ? 113.319 41.944  89.309  1.00 51.48  ? 1023 GLU A CG  1 
ATOM   7927  C  CD  . GLU A 1 1023 ? 112.269 41.726  88.229  1.00 57.02  ? 1023 GLU A CD  1 
ATOM   7928  O  OE1 . GLU A 1 1023 ? 111.171 41.209  88.560  1.00 59.20  ? 1023 GLU A OE1 1 
ATOM   7929  O  OE2 . GLU A 1 1023 ? 112.537 42.067  87.054  1.00 58.98  ? 1023 GLU A OE2 1 
ATOM   7930  N  N   . ALA A 1 1024 ? 113.163 43.668  92.888  1.00 42.01  ? 1024 ALA A N   1 
ATOM   7931  C  CA  . ALA A 1 1024 ? 113.266 45.073  93.264  1.00 39.13  ? 1024 ALA A CA  1 
ATOM   7932  C  C   . ALA A 1 1024 ? 114.478 45.320  94.148  1.00 38.01  ? 1024 ALA A C   1 
ATOM   7933  O  O   . ALA A 1 1024 ? 115.207 46.300  93.958  1.00 37.51  ? 1024 ALA A O   1 
ATOM   7934  C  CB  . ALA A 1 1024 ? 111.998 45.526  93.967  1.00 37.94  ? 1024 ALA A CB  1 
ATOM   7935  N  N   . LEU A 1 1025 ? 114.686 44.428  95.113  1.00 37.32  ? 1025 LEU A N   1 
ATOM   7936  C  CA  . LEU A 1 1025 ? 115.773 44.564  96.052  1.00 35.98  ? 1025 LEU A CA  1 
ATOM   7937  C  C   . LEU A 1 1025 ? 117.134 44.373  95.383  1.00 37.02  ? 1025 LEU A C   1 
ATOM   7938  O  O   . LEU A 1 1025 ? 118.097 45.060  95.744  1.00 37.10  ? 1025 LEU A O   1 
ATOM   7939  C  CB  . LEU A 1 1025 ? 115.597 43.599  97.221  1.00 36.15  ? 1025 LEU A CB  1 
ATOM   7940  C  CG  . LEU A 1 1025 ? 116.638 43.632  98.344  1.00 34.89  ? 1025 LEU A CG  1 
ATOM   7941  C  CD1 . LEU A 1 1025 ? 116.802 45.025  98.939  1.00 31.34  ? 1025 LEU A CD1 1 
ATOM   7942  C  CD2 . LEU A 1 1025 ? 116.248 42.633  99.422  1.00 35.75  ? 1025 LEU A CD2 1 
ATOM   7943  N  N   . ASN A 1 1026 ? 117.217 43.451  94.426  1.00 37.84  ? 1026 ASN A N   1 
ATOM   7944  C  CA  . ASN A 1 1026 ? 118.446 43.256  93.683  1.00 38.93  ? 1026 ASN A CA  1 
ATOM   7945  C  C   . ASN A 1 1026 ? 118.803 44.529  92.920  1.00 38.44  ? 1026 ASN A C   1 
ATOM   7946  O  O   . ASN A 1 1026 ? 119.958 44.968  92.917  1.00 39.03  ? 1026 ASN A O   1 
ATOM   7947  C  CB  . ASN A 1 1026 ? 118.343 42.060  92.716  1.00 40.75  ? 1026 ASN A CB  1 
ATOM   7948  C  CG  . ASN A 1 1026 ? 118.731 40.741  93.364  1.00 41.19  ? 1026 ASN A CG  1 
ATOM   7949  O  OD1 . ASN A 1 1026 ? 119.647 40.671  94.181  1.00 40.14  ? 1026 ASN A OD1 1 
ATOM   7950  N  ND2 . ASN A 1 1026 ? 118.033 39.686  92.995  1.00 43.15  ? 1026 ASN A ND2 1 
ATOM   7951  N  N   . LYS A 1 1027 ? 117.804 45.124  92.286  1.00 37.54  ? 1027 LYS A N   1 
ATOM   7952  C  CA  . LYS A 1 1027 ? 117.997 46.376  91.594  1.00 37.28  ? 1027 LYS A CA  1 
ATOM   7953  C  C   . LYS A 1 1027 ? 118.516 47.438  92.568  1.00 36.07  ? 1027 LYS A C   1 
ATOM   7954  O  O   . LYS A 1 1027 ? 119.486 48.152  92.272  1.00 36.27  ? 1027 LYS A O   1 
ATOM   7955  C  CB  . LYS A 1 1027 ? 116.686 46.832  90.962  1.00 36.78  ? 1027 LYS A CB  1 
ATOM   7956  C  CG  . LYS A 1 1027 ? 116.869 47.745  89.773  1.00 37.35  ? 1027 LYS A CG  1 
ATOM   7957  C  CD  . LYS A 1 1027 ? 115.543 48.344  89.322  1.00 37.24  ? 1027 LYS A CD  1 
ATOM   7958  C  CE  . LYS A 1 1027 ? 115.738 49.230  88.121  1.00 37.45  ? 1027 LYS A CE  1 
ATOM   7959  N  NZ  . LYS A 1 1027 ? 114.441 49.562  87.519  1.00 39.21  ? 1027 LYS A NZ  1 
ATOM   7960  N  N   . LEU A 1 1028 ? 117.880 47.528  93.733  1.00 34.88  ? 1028 LEU A N   1 
ATOM   7961  C  CA  . LEU A 1 1028 ? 118.252 48.546  94.713  1.00 33.68  ? 1028 LEU A CA  1 
ATOM   7962  C  C   . LEU A 1 1028 ? 119.695 48.329  95.139  1.00 34.51  ? 1028 LEU A C   1 
ATOM   7963  O  O   . LEU A 1 1028 ? 120.468 49.291  95.232  1.00 34.72  ? 1028 LEU A O   1 
ATOM   7964  C  CB  . LEU A 1 1028 ? 117.307 48.534  95.911  1.00 32.17  ? 1028 LEU A CB  1 
ATOM   7965  C  CG  . LEU A 1 1028 ? 117.555 49.507  97.066  1.00 31.03  ? 1028 LEU A CG  1 
ATOM   7966  C  CD1 . LEU A 1 1028 ? 117.416 50.989  96.681  1.00 28.86  ? 1028 LEU A CD1 1 
ATOM   7967  C  CD2 . LEU A 1 1028 ? 116.592 49.157  98.178  1.00 29.86  ? 1028 LEU A CD2 1 
ATOM   7968  N  N   . ILE A 1 1029 ? 120.061 47.065  95.354  1.00 35.12  ? 1029 ILE A N   1 
ATOM   7969  C  CA  . ILE A 1 1029 ? 121.414 46.729  95.771  1.00 35.93  ? 1029 ILE A CA  1 
ATOM   7970  C  C   . ILE A 1 1029 ? 122.412 47.219  94.731  1.00 37.03  ? 1029 ILE A C   1 
ATOM   7971  O  O   . ILE A 1 1029 ? 123.423 47.826  95.089  1.00 37.26  ? 1029 ILE A O   1 
ATOM   7972  C  CB  . ILE A 1 1029 ? 121.585 45.203  96.067  1.00 37.21  ? 1029 ILE A CB  1 
ATOM   7973  C  CG1 . ILE A 1 1029 ? 120.934 44.860  97.417  1.00 36.62  ? 1029 ILE A CG1 1 
ATOM   7974  C  CG2 . ILE A 1 1029 ? 123.063 44.799  96.060  1.00 37.01  ? 1029 ILE A CG2 1 
ATOM   7975  C  CD1 . ILE A 1 1029 ? 120.795 43.367  97.688  1.00 37.93  ? 1029 ILE A CD1 1 
ATOM   7976  N  N   . ASP A 1 1030 ? 122.099 46.980  93.454  1.00 37.68  ? 1030 ASP A N   1 
ATOM   7977  C  CA  . ASP A 1 1030 ? 122.969 47.351  92.338  1.00 38.86  ? 1030 ASP A CA  1 
ATOM   7978  C  C   . ASP A 1 1030 ? 123.297 48.835  92.344  1.00 38.37  ? 1030 ASP A C   1 
ATOM   7979  O  O   . ASP A 1 1030 ? 124.333 49.237  91.840  1.00 39.53  ? 1030 ASP A O   1 
ATOM   7980  C  CB  . ASP A 1 1030 ? 122.345 46.960  90.992  1.00 39.63  ? 1030 ASP A CB  1 
ATOM   7981  C  CG  . ASP A 1 1030 ? 122.177 45.447  90.828  1.00 41.03  ? 1030 ASP A CG  1 
ATOM   7982  O  OD1 . ASP A 1 1030 ? 122.703 44.674  91.654  1.00 41.26  ? 1030 ASP A OD1 1 
ATOM   7983  O  OD2 . ASP A 1 1030 ? 121.500 45.025  89.867  1.00 42.52  ? 1030 ASP A OD2 1 
ATOM   7984  N  N   . MET A 1 1031 ? 122.428 49.647  92.934  1.00 37.15  ? 1031 MET A N   1 
ATOM   7985  C  CA  . MET A 1 1031 ? 122.668 51.081  92.970  1.00 37.42  ? 1031 MET A CA  1 
ATOM   7986  C  C   . MET A 1 1031 ? 123.466 51.526  94.196  1.00 37.43  ? 1031 MET A C   1 
ATOM   7987  O  O   . MET A 1 1031 ? 123.732 52.720  94.338  1.00 37.83  ? 1031 MET A O   1 
ATOM   7988  C  CB  . MET A 1 1031 ? 121.356 51.860  92.931  1.00 35.89  ? 1031 MET A CB  1 
ATOM   7989  C  CG  . MET A 1 1031 ? 120.329 51.325  91.989  1.00 37.86  ? 1031 MET A CG  1 
ATOM   7990  S  SD  . MET A 1 1031 ? 118.898 52.410  91.917  1.00 40.89  ? 1031 MET A SD  1 
ATOM   7991  C  CE  . MET A 1 1031 ? 119.576 53.701  90.873  1.00 44.92  ? 1031 MET A CE  1 
ATOM   7992  N  N   . SER A 1 1032 ? 123.835 50.594  95.078  1.00 37.49  ? 1032 SER A N   1 
ATOM   7993  C  CA  . SER A 1 1032 ? 124.447 50.963  96.354  1.00 37.44  ? 1032 SER A CA  1 
ATOM   7994  C  C   . SER A 1 1032 ? 125.902 51.398  96.209  1.00 39.64  ? 1032 SER A C   1 
ATOM   7995  O  O   . SER A 1 1032 ? 126.561 51.079  95.226  1.00 41.04  ? 1032 SER A O   1 
ATOM   7996  C  CB  . SER A 1 1032 ? 124.317 49.836  97.385  1.00 37.15  ? 1032 SER A CB  1 
ATOM   7997  O  OG  . SER A 1 1032 ? 125.028 48.679  96.994  1.00 37.75  ? 1032 SER A OG  1 
ATOM   7998  N  N   . PHE A 1 1033 ? 126.385 52.146  97.195  1.00 40.41  ? 1033 PHE A N   1 
ATOM   7999  C  CA  . PHE A 1 1033 ? 127.779 52.579  97.238  1.00 42.95  ? 1033 PHE A CA  1 
ATOM   8000  C  C   . PHE A 1 1033 ? 128.479 51.928  98.410  1.00 43.82  ? 1033 PHE A C   1 
ATOM   8001  O  O   . PHE A 1 1033 ? 127.841 51.367  99.286  1.00 42.86  ? 1033 PHE A O   1 
ATOM   8002  C  CB  . PHE A 1 1033 ? 127.890 54.110  97.316  1.00 42.79  ? 1033 PHE A CB  1 
ATOM   8003  C  CG  . PHE A 1 1033 ? 127.351 54.816  96.102  1.00 43.93  ? 1033 PHE A CG  1 
ATOM   8004  C  CD1 . PHE A 1 1033 ? 125.973 55.033  95.949  1.00 43.46  ? 1033 PHE A CD1 1 
ATOM   8005  C  CD2 . PHE A 1 1033 ? 128.211 55.259  95.102  1.00 46.82  ? 1033 PHE A CD2 1 
ATOM   8006  C  CE1 . PHE A 1 1033 ? 125.474 55.683  94.816  1.00 43.80  ? 1033 PHE A CE1 1 
ATOM   8007  C  CE2 . PHE A 1 1033 ? 127.718 55.906  93.963  1.00 46.84  ? 1033 PHE A CE2 1 
ATOM   8008  C  CZ  . PHE A 1 1033 ? 126.351 56.120  93.823  1.00 45.23  ? 1033 PHE A CZ  1 
ATOM   8009  N  N   . ILE A 1 1034 ? 129.802 52.018  98.411  1.00 46.58  ? 1034 ILE A N   1 
ATOM   8010  C  CA  . ILE A 1 1034 ? 130.646 51.353  99.385  1.00 48.36  ? 1034 ILE A CA  1 
ATOM   8011  C  C   . ILE A 1 1034 ? 131.710 52.337  99.855  1.00 50.06  ? 1034 ILE A C   1 
ATOM   8012  O  O   . ILE A 1 1034 ? 132.175 53.162  99.071  1.00 51.03  ? 1034 ILE A O   1 
ATOM   8013  C  CB  . ILE A 1 1034 ? 131.258 50.042  98.752  1.00 50.31  ? 1034 ILE A CB  1 
ATOM   8014  C  CG1 . ILE A 1 1034 ? 130.631 48.783  99.373  1.00 50.77  ? 1034 ILE A CG1 1 
ATOM   8015  C  CG2 . ILE A 1 1034 ? 132.797 49.991  98.801  1.00 52.02  ? 1034 ILE A CG2 1 
ATOM   8016  C  CD1 . ILE A 1 1034 ? 131.095 48.456  100.839 1.00 54.58  ? 1034 ILE A CD1 1 
ATOM   8017  N  N   . ASP A 1 1035 ? 132.038 52.292  101.144 1.00 50.88  ? 1035 ASP A N   1 
ATOM   8018  C  CA  . ASP A 1 1035 ? 133.289 52.854  101.656 1.00 53.22  ? 1035 ASP A CA  1 
ATOM   8019  C  C   . ASP A 1 1035 ? 134.022 51.685  102.301 1.00 55.03  ? 1035 ASP A C   1 
ATOM   8020  O  O   . ASP A 1 1035 ? 133.690 51.260  103.414 1.00 54.52  ? 1035 ASP A O   1 
ATOM   8021  C  CB  . ASP A 1 1035 ? 133.054 53.995  102.657 1.00 52.63  ? 1035 ASP A CB  1 
ATOM   8022  C  CG  . ASP A 1 1035 ? 134.356 54.695  103.084 1.00 55.75  ? 1035 ASP A CG  1 
ATOM   8023  O  OD1 . ASP A 1 1035 ? 135.388 54.016  103.290 1.00 59.14  ? 1035 ASP A OD1 1 
ATOM   8024  O  OD2 . ASP A 1 1035 ? 134.352 55.932  103.236 1.00 56.69  ? 1035 ASP A OD2 1 
ATOM   8025  N  N   . ALA A 1 1036 ? 135.007 51.161  101.578 1.00 57.64  ? 1036 ALA A N   1 
ATOM   8026  C  CA  . ALA A 1 1036 ? 135.688 49.926  101.955 1.00 59.94  ? 1036 ALA A CA  1 
ATOM   8027  C  C   . ALA A 1 1036 ? 136.527 50.130  103.198 1.00 61.97  ? 1036 ALA A C   1 
ATOM   8028  O  O   . ALA A 1 1036 ? 136.632 49.229  104.033 1.00 62.80  ? 1036 ALA A O   1 
ATOM   8029  C  CB  . ALA A 1 1036 ? 136.547 49.416  100.811 1.00 61.81  ? 1036 ALA A CB  1 
ATOM   8030  N  N   . ASP A 1 1037 ? 137.111 51.324  103.316 1.00 63.27  ? 1037 ASP A N   1 
ATOM   8031  C  CA  . ASP A 1 1037 ? 137.930 51.686  104.473 1.00 65.19  ? 1037 ASP A CA  1 
ATOM   8032  C  C   . ASP A 1 1037 ? 137.116 51.726  105.759 1.00 63.22  ? 1037 ASP A C   1 
ATOM   8033  O  O   . ASP A 1 1037 ? 137.663 51.561  106.840 1.00 65.12  ? 1037 ASP A O   1 
ATOM   8034  C  CB  . ASP A 1 1037 ? 138.621 53.037  104.257 1.00 66.77  ? 1037 ASP A CB  1 
ATOM   8035  C  CG  . ASP A 1 1037 ? 139.728 52.979  103.205 1.00 71.01  ? 1037 ASP A CG  1 
ATOM   8036  O  OD1 . ASP A 1 1037 ? 140.387 51.917  103.049 1.00 73.24  ? 1037 ASP A OD1 1 
ATOM   8037  O  OD2 . ASP A 1 1037 ? 139.945 54.016  102.533 1.00 73.22  ? 1037 ASP A OD2 1 
ATOM   8038  N  N   . LYS A 1 1038 ? 135.812 51.933  105.645 1.00 60.02  ? 1038 LYS A N   1 
ATOM   8039  C  CA  . LYS A 1 1038 ? 134.964 52.054  106.828 1.00 58.29  ? 1038 LYS A CA  1 
ATOM   8040  C  C   . LYS A 1 1038 ? 133.959 50.917  106.975 1.00 56.13  ? 1038 LYS A C   1 
ATOM   8041  O  O   . LYS A 1 1038 ? 133.214 50.883  107.953 1.00 54.91  ? 1038 LYS A O   1 
ATOM   8042  C  CB  . LYS A 1 1038 ? 134.240 53.404  106.827 1.00 56.87  ? 1038 LYS A CB  1 
ATOM   8043  C  CG  . LYS A 1 1038 ? 135.180 54.599  106.877 1.00 60.28  ? 1038 LYS A CG  1 
ATOM   8044  C  CD  . LYS A 1 1038 ? 134.449 55.892  106.579 1.00 61.98  ? 1038 LYS A CD  1 
ATOM   8045  C  CE  . LYS A 1 1038 ? 135.389 57.090  106.685 1.00 66.00  ? 1038 LYS A CE  1 
ATOM   8046  N  NZ  . LYS A 1 1038 ? 134.725 58.357  106.253 1.00 66.11  ? 1038 LYS A NZ  1 
ATOM   8047  N  N   . ASN A 1 1039 ? 133.952 49.986  106.015 1.00 55.48  ? 1039 ASN A N   1 
ATOM   8048  C  CA  . ASN A 1 1039 ? 132.979 48.891  105.987 1.00 53.70  ? 1039 ASN A CA  1 
ATOM   8049  C  C   . ASN A 1 1039 ? 131.550 49.426  105.985 1.00 50.67  ? 1039 ASN A C   1 
ATOM   8050  O  O   . ASN A 1 1039 ? 130.702 48.995  106.780 1.00 49.59  ? 1039 ASN A O   1 
ATOM   8051  C  CB  . ASN A 1 1039 ? 133.190 47.932  107.160 1.00 55.09  ? 1039 ASN A CB  1 
ATOM   8052  C  CG  . ASN A 1 1039 ? 134.564 47.295  107.154 1.00 58.86  ? 1039 ASN A CG  1 
ATOM   8053  O  OD1 . ASN A 1 1039 ? 135.106 46.952  106.102 1.00 61.00  ? 1039 ASN A OD1 1 
ATOM   8054  N  ND2 . ASN A 1 1039 ? 135.137 47.132  108.333 1.00 61.47  ? 1039 ASN A ND2 1 
ATOM   8055  N  N   . GLU A 1 1040 ? 131.302 50.379  105.087 1.00 48.94  ? 1040 GLU A N   1 
ATOM   8056  C  CA  . GLU A 1 1040 ? 130.022 51.068  105.008 1.00 45.95  ? 1040 GLU A CA  1 
ATOM   8057  C  C   . GLU A 1 1040 ? 129.335 50.792  103.678 1.00 44.51  ? 1040 GLU A C   1 
ATOM   8058  O  O   . GLU A 1 1040 ? 129.979 50.761  102.628 1.00 45.57  ? 1040 GLU A O   1 
ATOM   8059  C  CB  . GLU A 1 1040 ? 130.218 52.578  105.192 1.00 45.62  ? 1040 GLU A CB  1 
ATOM   8060  C  CG  . GLU A 1 1040 ? 130.556 53.014  106.609 1.00 46.73  ? 1040 GLU A CG  1 
ATOM   8061  C  CD  . GLU A 1 1040 ? 130.720 54.530  106.753 1.00 48.72  ? 1040 GLU A CD  1 
ATOM   8062  O  OE1 . GLU A 1 1040 ? 131.063 55.216  105.762 1.00 50.00  ? 1040 GLU A OE1 1 
ATOM   8063  O  OE2 . GLU A 1 1040 ? 130.503 55.054  107.868 1.00 49.16  ? 1040 GLU A OE2 1 
ATOM   8064  N  N   . ARG A 1 1041 ? 128.030 50.573  103.723 1.00 42.35  ? 1041 ARG A N   1 
ATOM   8065  C  CA  . ARG A 1 1041 ? 127.235 50.534  102.497 1.00 41.12  ? 1041 ARG A CA  1 
ATOM   8066  C  C   . ARG A 1 1041 ? 126.107 51.524  102.653 1.00 39.35  ? 1041 ARG A C   1 
ATOM   8067  O  O   . ARG A 1 1041 ? 125.501 51.606  103.728 1.00 38.87  ? 1041 ARG A O   1 
ATOM   8068  C  CB  . ARG A 1 1041 ? 126.697 49.124  102.197 1.00 40.77  ? 1041 ARG A CB  1 
ATOM   8069  C  CG  . ARG A 1 1041 ? 125.842 49.036  100.931 1.00 38.49  ? 1041 ARG A CG  1 
ATOM   8070  C  CD  . ARG A 1 1041 ? 125.481 47.594  100.557 1.00 36.78  ? 1041 ARG A CD  1 
ATOM   8071  N  NE  . ARG A 1 1041 ? 126.690 46.796  100.414 1.00 36.76  ? 1041 ARG A NE  1 
ATOM   8072  C  CZ  . ARG A 1 1041 ? 127.388 46.678  99.291  1.00 36.71  ? 1041 ARG A CZ  1 
ATOM   8073  N  NH1 . ARG A 1 1041 ? 126.986 47.275  98.174  1.00 34.62  ? 1041 ARG A NH1 1 
ATOM   8074  N  NH2 . ARG A 1 1041 ? 128.490 45.945  99.284  1.00 38.99  ? 1041 ARG A NH2 1 
ATOM   8075  N  N   . PHE A 1 1042 ? 125.837 52.276  101.589 1.00 38.94  ? 1042 PHE A N   1 
ATOM   8076  C  CA  . PHE A 1 1042 ? 124.808 53.325  101.605 1.00 37.75  ? 1042 PHE A CA  1 
ATOM   8077  C  C   . PHE A 1 1042 ? 124.392 53.693  100.195 1.00 37.54  ? 1042 PHE A C   1 
ATOM   8078  O  O   . PHE A 1 1042 ? 125.006 53.253  99.221  1.00 38.34  ? 1042 PHE A O   1 
ATOM   8079  C  CB  . PHE A 1 1042 ? 125.309 54.586  102.340 1.00 37.87  ? 1042 PHE A CB  1 
ATOM   8080  C  CG  . PHE A 1 1042 ? 126.462 55.269  101.658 1.00 39.01  ? 1042 PHE A CG  1 
ATOM   8081  C  CD1 . PHE A 1 1042 ? 127.764 54.792  101.811 1.00 40.98  ? 1042 PHE A CD1 1 
ATOM   8082  C  CD2 . PHE A 1 1042 ? 126.249 56.388  100.862 1.00 39.08  ? 1042 PHE A CD2 1 
ATOM   8083  C  CE1 . PHE A 1 1042 ? 128.841 55.424  101.169 1.00 42.83  ? 1042 PHE A CE1 1 
ATOM   8084  C  CE2 . PHE A 1 1042 ? 127.319 57.033  100.215 1.00 40.98  ? 1042 PHE A CE2 1 
ATOM   8085  C  CZ  . PHE A 1 1042 ? 128.613 56.551  100.369 1.00 42.34  ? 1042 PHE A CZ  1 
ATOM   8086  N  N   . TRP A 1 1043 ? 123.361 54.523  100.103 1.00 36.71  ? 1043 TRP A N   1 
ATOM   8087  C  CA  . TRP A 1 1043 ? 122.833 54.967  98.826  1.00 37.27  ? 1043 TRP A CA  1 
ATOM   8088  C  C   . TRP A 1 1043 ? 123.035 56.477  98.685  1.00 38.51  ? 1043 TRP A C   1 
ATOM   8089  O  O   . TRP A 1 1043 ? 122.675 57.215  99.581  1.00 38.66  ? 1043 TRP A O   1 
ATOM   8090  C  CB  . TRP A 1 1043 ? 121.359 54.563  98.721  1.00 35.06  ? 1043 TRP A CB  1 
ATOM   8091  C  CG  . TRP A 1 1043 ? 121.202 53.117  98.387  1.00 34.35  ? 1043 TRP A CG  1 
ATOM   8092  C  CD1 . TRP A 1 1043 ? 120.879 52.587  97.165  1.00 34.33  ? 1043 TRP A CD1 1 
ATOM   8093  C  CD2 . TRP A 1 1043 ? 121.408 52.000  99.262  1.00 33.77  ? 1043 TRP A CD2 1 
ATOM   8094  N  NE1 . TRP A 1 1043 ? 120.856 51.216  97.233  1.00 34.18  ? 1043 TRP A NE1 1 
ATOM   8095  C  CE2 . TRP A 1 1043 ? 121.179 50.830  98.507  1.00 33.81  ? 1043 TRP A CE2 1 
ATOM   8096  C  CE3 . TRP A 1 1043 ? 121.757 51.873  100.612 1.00 33.28  ? 1043 TRP A CE3 1 
ATOM   8097  C  CZ2 . TRP A 1 1043 ? 121.291 49.556  99.058  1.00 35.38  ? 1043 TRP A CZ2 1 
ATOM   8098  C  CZ3 . TRP A 1 1043 ? 121.873 50.607  101.155 1.00 34.21  ? 1043 TRP A CZ3 1 
ATOM   8099  C  CH2 . TRP A 1 1043 ? 121.640 49.464  100.381 1.00 35.19  ? 1043 TRP A CH2 1 
ATOM   8100  N  N   . ASN A 1 1044 ? 123.645 56.936  97.594  1.00 41.05  ? 1044 ASN A N   1 
ATOM   8101  C  CA  . ASN A 1 1044 ? 123.895 58.376  97.411  1.00 43.18  ? 1044 ASN A CA  1 
ATOM   8102  C  C   . ASN A 1 1044 ? 122.780 59.136  96.675  1.00 42.98  ? 1044 ASN A C   1 
ATOM   8103  O  O   . ASN A 1 1044 ? 122.948 59.493  95.520  1.00 44.59  ? 1044 ASN A O   1 
ATOM   8104  C  CB  . ASN A 1 1044 ? 125.249 58.643  96.712  1.00 45.59  ? 1044 ASN A CB  1 
ATOM   8105  C  CG  . ASN A 1 1044 ? 125.835 60.024  97.066  1.00 48.34  ? 1044 ASN A CG  1 
ATOM   8106  O  OD1 . ASN A 1 1044 ? 125.673 60.491  98.193  1.00 51.34  ? 1044 ASN A OD1 1 
ATOM   8107  N  ND2 . ASN A 1 1044 ? 126.521 60.668  96.116  1.00 50.16  ? 1044 ASN A ND2 1 
ATOM   8108  N  N   . THR A 1 1045 ? 121.648 59.375  97.330  1.00 41.84  ? 1045 THR A N   1 
ATOM   8109  C  CA  . THR A 1 1045 ? 120.635 60.286  96.783  1.00 41.90  ? 1045 THR A CA  1 
ATOM   8110  C  C   . THR A 1 1045 ? 120.711 61.620  97.524  1.00 42.46  ? 1045 THR A C   1 
ATOM   8111  O  O   . THR A 1 1045 ? 121.468 61.744  98.488  1.00 42.69  ? 1045 THR A O   1 
ATOM   8112  C  CB  . THR A 1 1045 ? 119.242 59.753  96.985  1.00 40.37  ? 1045 THR A CB  1 
ATOM   8113  O  OG1 . THR A 1 1045 ? 119.053 59.524  98.383  1.00 39.83  ? 1045 THR A OG1 1 
ATOM   8114  C  CG2 . THR A 1 1045 ? 119.044 58.463  96.207  1.00 39.86  ? 1045 THR A CG2 1 
ATOM   8115  N  N   . THR A 1 1046 ? 119.929 62.612  97.102  1.00 42.84  ? 1046 THR A N   1 
ATOM   8116  C  CA  . THR A 1 1046 ? 119.916 63.872  97.857  1.00 44.14  ? 1046 THR A CA  1 
ATOM   8117  C  C   . THR A 1 1046 ? 119.355 63.718  99.287  1.00 42.64  ? 1046 THR A C   1 
ATOM   8118  O  O   . THR A 1 1046 ? 119.587 64.583  100.116 1.00 43.74  ? 1046 THR A O   1 
ATOM   8119  C  CB  . THR A 1 1046 ? 119.246 65.090  97.112  1.00 44.95  ? 1046 THR A CB  1 
ATOM   8120  O  OG1 . THR A 1 1046 ? 117.825 65.010  97.224  1.00 45.11  ? 1046 THR A OG1 1 
ATOM   8121  C  CG2 . THR A 1 1046 ? 119.653 65.169  95.647  1.00 46.22  ? 1046 THR A CG2 1 
ATOM   8122  N  N   . ASN A 1 1047 ? 118.648 62.618  99.564  1.00 41.31  ? 1047 ASN A N   1 
ATOM   8123  C  CA  . ASN A 1 1047 ? 118.246 62.231  100.928 1.00 40.34  ? 1047 ASN A CA  1 
ATOM   8124  C  C   . ASN A 1 1047 ? 118.814 60.854  101.317 1.00 39.40  ? 1047 ASN A C   1 
ATOM   8125  O  O   . ASN A 1 1047 ? 118.060 59.888  101.475 1.00 38.45  ? 1047 ASN A O   1 
ATOM   8126  C  CB  . ASN A 1 1047 ? 116.718 62.198  101.090 1.00 39.77  ? 1047 ASN A CB  1 
ATOM   8127  C  CG  . ASN A 1 1047 ? 116.030 63.393  100.455 1.00 43.25  ? 1047 ASN A CG  1 
ATOM   8128  O  OD1 . ASN A 1 1047 ? 115.572 64.314  101.144 1.00 44.78  ? 1047 ASN A OD1 1 
ATOM   8129  N  ND2 . ASN A 1 1047 ? 115.949 63.384  99.123  1.00 47.52  ? 1047 ASN A ND2 1 
ATOM   8130  N  N   . PRO A 1 1048 ? 120.143 60.761  101.505 1.00 39.60  ? 1048 PRO A N   1 
ATOM   8131  C  CA  . PRO A 1 1048 ? 120.729 59.424  101.644 1.00 38.95  ? 1048 PRO A CA  1 
ATOM   8132  C  C   . PRO A 1 1048 ? 120.298 58.678  102.911 1.00 38.18  ? 1048 PRO A C   1 
ATOM   8133  O  O   . PRO A 1 1048 ? 120.291 57.446  102.919 1.00 38.11  ? 1048 PRO A O   1 
ATOM   8134  C  CB  . PRO A 1 1048 ? 122.231 59.698  101.677 1.00 40.36  ? 1048 PRO A CB  1 
ATOM   8135  C  CG  . PRO A 1 1048 ? 122.369 61.127  102.105 1.00 40.78  ? 1048 PRO A CG  1 
ATOM   8136  C  CD  . PRO A 1 1048 ? 121.146 61.838  101.627 1.00 40.42  ? 1048 PRO A CD  1 
ATOM   8137  N  N   . ILE A 1 1049 ? 119.957 59.399  103.981 1.00 37.51  ? 1049 ILE A N   1 
ATOM   8138  C  CA  . ILE A 1 1049 ? 119.588 58.717  105.229 1.00 36.40  ? 1049 ILE A CA  1 
ATOM   8139  C  C   . ILE A 1 1049 ? 118.284 57.953  105.022 1.00 35.09  ? 1049 ILE A C   1 
ATOM   8140  O  O   . ILE A 1 1049 ? 118.230 56.745  105.288 1.00 35.26  ? 1049 ILE A O   1 
ATOM   8141  C  CB  . ILE A 1 1049 ? 119.525 59.658  106.470 1.00 36.39  ? 1049 ILE A CB  1 
ATOM   8142  C  CG1 . ILE A 1 1049 ? 120.893 60.288  106.734 1.00 37.63  ? 1049 ILE A CG1 1 
ATOM   8143  C  CG2 . ILE A 1 1049 ? 119.108 58.884  107.696 1.00 35.63  ? 1049 ILE A CG2 1 
ATOM   8144  C  CD1 . ILE A 1 1049 ? 120.892 61.446  107.723 1.00 36.39  ? 1049 ILE A CD1 1 
ATOM   8145  N  N   . GLU A 1 1050 ? 117.260 58.641  104.511 1.00 33.67  ? 1050 GLU A N   1 
ATOM   8146  C  CA  . GLU A 1 1050 ? 115.972 57.999  104.237 1.00 32.38  ? 1050 GLU A CA  1 
ATOM   8147  C  C   . GLU A 1 1050 ? 116.125 56.763  103.357 1.00 31.84  ? 1050 GLU A C   1 
ATOM   8148  O  O   . GLU A 1 1050 ? 115.699 55.667  103.734 1.00 31.41  ? 1050 GLU A O   1 
ATOM   8149  C  CB  . GLU A 1 1050 ? 115.013 58.965  103.566 1.00 32.19  ? 1050 GLU A CB  1 
ATOM   8150  C  CG  . GLU A 1 1050 ? 114.263 59.876  104.494 1.00 33.48  ? 1050 GLU A CG  1 
ATOM   8151  C  CD  . GLU A 1 1050 ? 113.340 60.798  103.721 1.00 36.91  ? 1050 GLU A CD  1 
ATOM   8152  O  OE1 . GLU A 1 1050 ? 112.259 60.328  103.271 1.00 36.07  ? 1050 GLU A OE1 1 
ATOM   8153  O  OE2 . GLU A 1 1050 ? 113.710 61.992  103.555 1.00 39.34  ? 1050 GLU A OE2 1 
ATOM   8154  N  N   . THR A 1 1051 ? 116.751 56.932  102.194 1.00 31.49  ? 1051 THR A N   1 
ATOM   8155  C  CA  . THR A 1 1051 ? 116.794 55.842  101.239 1.00 31.19  ? 1051 THR A CA  1 
ATOM   8156  C  C   . THR A 1 1051 ? 117.595 54.670  101.756 1.00 31.37  ? 1051 THR A C   1 
ATOM   8157  O  O   . THR A 1 1051 ? 117.170 53.528  101.601 1.00 31.52  ? 1051 THR A O   1 
ATOM   8158  C  CB  . THR A 1 1051 ? 117.159 56.270  99.771  1.00 32.26  ? 1051 THR A CB  1 
ATOM   8159  O  OG1 . THR A 1 1051 ? 118.026 55.293  99.165  1.00 34.05  ? 1051 THR A OG1 1 
ATOM   8160  C  CG2 . THR A 1 1051 ? 117.789 57.620  99.715  1.00 31.10  ? 1051 THR A CG2 1 
ATOM   8161  N  N   . THR A 1 1052 ? 118.713 54.948  102.421 1.00 31.56  ? 1052 THR A N   1 
ATOM   8162  C  CA  . THR A 1 1052 ? 119.522 53.892  103.036 1.00 31.86  ? 1052 THR A CA  1 
ATOM   8163  C  C   . THR A 1 1052 ? 118.736 53.183  104.139 1.00 31.90  ? 1052 THR A C   1 
ATOM   8164  O  O   . THR A 1 1052 ? 118.835 51.954  104.290 1.00 32.51  ? 1052 THR A O   1 
ATOM   8165  C  CB  . THR A 1 1052 ? 120.861 54.439  103.588 1.00 32.69  ? 1052 THR A CB  1 
ATOM   8166  O  OG1 . THR A 1 1052 ? 121.616 55.029  102.526 1.00 32.74  ? 1052 THR A OG1 1 
ATOM   8167  C  CG2 . THR A 1 1052 ? 121.694 53.343  104.218 1.00 32.88  ? 1052 THR A CG2 1 
ATOM   8168  N  N   . ALA A 1 1053 ? 117.948 53.950  104.898 1.00 31.37  ? 1053 ALA A N   1 
ATOM   8169  C  CA  . ALA A 1 1053 ? 117.119 53.369  105.960 1.00 31.07  ? 1053 ALA A CA  1 
ATOM   8170  C  C   . ALA A 1 1053 ? 116.042 52.467  105.364 1.00 31.17  ? 1053 ALA A C   1 
ATOM   8171  O  O   . ALA A 1 1053 ? 115.818 51.341  105.846 1.00 32.14  ? 1053 ALA A O   1 
ATOM   8172  C  CB  . ALA A 1 1053 ? 116.511 54.434  106.794 1.00 30.09  ? 1053 ALA A CB  1 
ATOM   8173  N  N   . TYR A 1 1054 ? 115.384 52.938  104.306 1.00 30.21  ? 1054 TYR A N   1 
ATOM   8174  C  CA  . TYR A 1 1054 ? 114.382 52.110  103.656 1.00 30.38  ? 1054 TYR A CA  1 
ATOM   8175  C  C   . TYR A 1 1054 ? 115.005 50.807  103.121 1.00 31.17  ? 1054 TYR A C   1 
ATOM   8176  O  O   . TYR A 1 1054 ? 114.439 49.724  103.293 1.00 31.99  ? 1054 TYR A O   1 
ATOM   8177  C  CB  . TYR A 1 1054 ? 113.664 52.865  102.546 1.00 30.02  ? 1054 TYR A CB  1 
ATOM   8178  C  CG  . TYR A 1 1054 ? 112.545 53.780  103.003 1.00 29.62  ? 1054 TYR A CG  1 
ATOM   8179  C  CD1 . TYR A 1 1054 ? 112.626 55.160  102.797 1.00 29.10  ? 1054 TYR A CD1 1 
ATOM   8180  C  CD2 . TYR A 1 1054 ? 111.394 53.270  103.611 1.00 29.49  ? 1054 TYR A CD2 1 
ATOM   8181  C  CE1 . TYR A 1 1054 ? 111.594 56.012  103.188 1.00 28.82  ? 1054 TYR A CE1 1 
ATOM   8182  C  CE2 . TYR A 1 1054 ? 110.358 54.117  104.020 1.00 28.89  ? 1054 TYR A CE2 1 
ATOM   8183  C  CZ  . TYR A 1 1054 ? 110.464 55.484  103.801 1.00 29.46  ? 1054 TYR A CZ  1 
ATOM   8184  O  OH  . TYR A 1 1054 ? 109.442 56.334  104.184 1.00 30.11  ? 1054 TYR A OH  1 
ATOM   8185  N  N   . ALA A 1 1055 ? 116.176 50.914  102.496 1.00 30.85  ? 1055 ALA A N   1 
ATOM   8186  C  CA  . ALA A 1 1055 ? 116.905 49.743  102.033 1.00 31.31  ? 1055 ALA A CA  1 
ATOM   8187  C  C   . ALA A 1 1055 ? 117.199 48.775  103.190 1.00 32.17  ? 1055 ALA A C   1 
ATOM   8188  O  O   . ALA A 1 1055 ? 117.025 47.558  103.050 1.00 32.71  ? 1055 ALA A O   1 
ATOM   8189  C  CB  . ALA A 1 1055 ? 118.191 50.164  101.331 1.00 31.30  ? 1055 ALA A CB  1 
ATOM   8190  N  N   . LEU A 1 1056 ? 117.619 49.311  104.335 1.00 32.11  ? 1056 LEU A N   1 
ATOM   8191  C  CA  . LEU A 1 1056 ? 117.922 48.466  105.485 1.00 33.53  ? 1056 LEU A CA  1 
ATOM   8192  C  C   . LEU A 1 1056 ? 116.699 47.697  105.964 1.00 34.43  ? 1056 LEU A C   1 
ATOM   8193  O  O   . LEU A 1 1056 ? 116.813 46.523  106.331 1.00 35.97  ? 1056 LEU A O   1 
ATOM   8194  C  CB  . LEU A 1 1056 ? 118.524 49.264  106.643 1.00 33.58  ? 1056 LEU A CB  1 
ATOM   8195  C  CG  . LEU A 1 1056 ? 119.011 48.454  107.862 1.00 34.75  ? 1056 LEU A CG  1 
ATOM   8196  C  CD1 . LEU A 1 1056 ? 119.999 47.393  107.441 1.00 34.60  ? 1056 LEU A CD1 1 
ATOM   8197  C  CD2 . LEU A 1 1056 ? 119.634 49.351  108.928 1.00 34.03  ? 1056 LEU A CD2 1 
ATOM   8198  N  N   . LEU A 1 1057 ? 115.532 48.340  105.955 1.00 33.84  ? 1057 LEU A N   1 
ATOM   8199  C  CA  . LEU A 1 1057 ? 114.302 47.638  106.318 1.00 34.66  ? 1057 LEU A CA  1 
ATOM   8200  C  C   . LEU A 1 1057 ? 114.100 46.440  105.411 1.00 36.07  ? 1057 LEU A C   1 
ATOM   8201  O  O   . LEU A 1 1057 ? 113.839 45.327  105.894 1.00 38.21  ? 1057 LEU A O   1 
ATOM   8202  C  CB  . LEU A 1 1057 ? 113.090 48.572  106.297 1.00 33.78  ? 1057 LEU A CB  1 
ATOM   8203  C  CG  . LEU A 1 1057 ? 113.059 49.562  107.477 1.00 32.80  ? 1057 LEU A CG  1 
ATOM   8204  C  CD1 . LEU A 1 1057 ? 112.252 50.813  107.159 1.00 31.40  ? 1057 LEU A CD1 1 
ATOM   8205  C  CD2 . LEU A 1 1057 ? 112.562 48.906  108.744 1.00 31.40  ? 1057 LEU A CD2 1 
ATOM   8206  N  N   . SER A 1 1058 ? 114.277 46.639  104.106 1.00 35.74  ? 1058 SER A N   1 
ATOM   8207  C  CA  . SER A 1 1058 ? 114.155 45.527  103.164 1.00 36.91  ? 1058 SER A CA  1 
ATOM   8208  C  C   . SER A 1 1058 ? 115.192 44.437  103.400 1.00 38.41  ? 1058 SER A C   1 
ATOM   8209  O  O   . SER A 1 1058 ? 114.850 43.260  103.372 1.00 40.63  ? 1058 SER A O   1 
ATOM   8210  C  CB  . SER A 1 1058 ? 114.160 45.998  101.722 1.00 36.18  ? 1058 SER A CB  1 
ATOM   8211  O  OG  . SER A 1 1058 ? 112.954 46.684  101.439 1.00 36.26  ? 1058 SER A OG  1 
ATOM   8212  N  N   . PHE A 1 1059 ? 116.444 44.818  103.656 1.00 37.89  ? 1059 PHE A N   1 
ATOM   8213  C  CA  . PHE A 1 1059 ? 117.470 43.850  104.032 1.00 38.60  ? 1059 PHE A CA  1 
ATOM   8214  C  C   . PHE A 1 1059 ? 116.946 43.000  105.191 1.00 40.12  ? 1059 PHE A C   1 
ATOM   8215  O  O   . PHE A 1 1059 ? 117.005 41.766  105.145 1.00 41.56  ? 1059 PHE A O   1 
ATOM   8216  C  CB  . PHE A 1 1059 ? 118.753 44.569  104.458 1.00 37.98  ? 1059 PHE A CB  1 
ATOM   8217  C  CG  . PHE A 1 1059 ? 119.732 44.821  103.340 1.00 36.94  ? 1059 PHE A CG  1 
ATOM   8218  C  CD1 . PHE A 1 1059 ? 119.336 45.450  102.152 1.00 35.07  ? 1059 PHE A CD1 1 
ATOM   8219  C  CD2 . PHE A 1 1059 ? 121.070 44.457  103.487 1.00 37.01  ? 1059 PHE A CD2 1 
ATOM   8220  C  CE1 . PHE A 1 1059 ? 120.248 45.684  101.130 1.00 33.26  ? 1059 PHE A CE1 1 
ATOM   8221  C  CE2 . PHE A 1 1059 ? 121.992 44.696  102.468 1.00 35.54  ? 1059 PHE A CE2 1 
ATOM   8222  C  CZ  . PHE A 1 1059 ? 121.574 45.312  101.291 1.00 34.84  ? 1059 PHE A CZ  1 
ATOM   8223  N  N   . VAL A 1 1060 ? 116.422 43.670  106.221 1.00 39.61  ? 1060 VAL A N   1 
ATOM   8224  C  CA  . VAL A 1 1060 ? 115.922 42.992  107.420 1.00 41.37  ? 1060 VAL A CA  1 
ATOM   8225  C  C   . VAL A 1 1060 ? 114.790 42.052  107.038 1.00 42.68  ? 1060 VAL A C   1 
ATOM   8226  O  O   . VAL A 1 1060 ? 114.766 40.897  107.438 1.00 44.75  ? 1060 VAL A O   1 
ATOM   8227  C  CB  . VAL A 1 1060 ? 115.396 43.987  108.503 1.00 40.39  ? 1060 VAL A CB  1 
ATOM   8228  C  CG1 . VAL A 1 1060 ? 114.803 43.234  109.688 1.00 41.74  ? 1060 VAL A CG1 1 
ATOM   8229  C  CG2 . VAL A 1 1060 ? 116.492 44.905  108.977 1.00 39.29  ? 1060 VAL A CG2 1 
ATOM   8230  N  N   . MET A 1 1061 ? 113.858 42.563  106.247 1.00 41.92  ? 1061 MET A N   1 
ATOM   8231  C  CA  . MET A 1 1061 ? 112.704 41.793  105.852 1.00 43.30  ? 1061 MET A CA  1 
ATOM   8232  C  C   . MET A 1 1061 ? 113.112 40.557  105.041 1.00 44.88  ? 1061 MET A C   1 
ATOM   8233  O  O   . MET A 1 1061 ? 112.403 39.548  105.036 1.00 46.61  ? 1061 MET A O   1 
ATOM   8234  C  CB  . MET A 1 1061 ? 111.780 42.681  105.034 1.00 42.29  ? 1061 MET A CB  1 
ATOM   8235  C  CG  . MET A 1 1061 ? 110.355 42.184  104.961 1.00 45.06  ? 1061 MET A CG  1 
ATOM   8236  S  SD  . MET A 1 1061 ? 109.270 43.227  105.921 1.00 45.67  ? 1061 MET A SD  1 
ATOM   8237  C  CE  . MET A 1 1061 ? 109.747 42.813  107.604 1.00 48.51  ? 1061 MET A CE  1 
ATOM   8238  N  N   . ALA A 1 1062 ? 114.251 40.651  104.351 1.00 44.44  ? 1062 ALA A N   1 
ATOM   8239  C  CA  . ALA A 1 1062 ? 114.768 39.558  103.524 1.00 45.80  ? 1062 ALA A CA  1 
ATOM   8240  C  C   . ALA A 1 1062 ? 115.816 38.752  104.271 1.00 47.24  ? 1062 ALA A C   1 
ATOM   8241  O  O   . ALA A 1 1062 ? 116.478 37.895  103.685 1.00 48.50  ? 1062 ALA A O   1 
ATOM   8242  C  CB  . ALA A 1 1062 ? 115.346 40.096  102.239 1.00 44.56  ? 1062 ALA A CB  1 
ATOM   8243  N  N   . GLU A 1 1063 ? 115.968 39.050  105.562 1.00 46.95  ? 1063 GLU A N   1 
ATOM   8244  C  CA  . GLU A 1 1063 ? 116.897 38.341  106.451 1.00 48.67  ? 1063 GLU A CA  1 
ATOM   8245  C  C   . GLU A 1 1063 ? 118.370 38.424  106.028 1.00 48.16  ? 1063 GLU A C   1 
ATOM   8246  O  O   . GLU A 1 1063 ? 119.172 37.539  106.341 1.00 50.15  ? 1063 GLU A O   1 
ATOM   8247  C  CB  . GLU A 1 1063 ? 116.449 36.881  106.657 1.00 51.52  ? 1063 GLU A CB  1 
ATOM   8248  C  CG  . GLU A 1 1063 ? 115.113 36.765  107.382 1.00 53.32  ? 1063 GLU A CG  1 
ATOM   8249  C  CD  . GLU A 1 1063 ? 114.552 35.356  107.397 1.00 58.21  ? 1063 GLU A CD  1 
ATOM   8250  O  OE1 . GLU A 1 1063 ? 113.324 35.216  107.196 1.00 58.98  ? 1063 GLU A OE1 1 
ATOM   8251  O  OE2 . GLU A 1 1063 ? 115.327 34.393  107.611 1.00 61.20  ? 1063 GLU A OE2 1 
ATOM   8252  N  N   . LYS A 1 1064 ? 118.725 39.501  105.335 1.00 45.68  ? 1064 LYS A N   1 
ATOM   8253  C  CA  . LYS A 1 1064 ? 120.095 39.678  104.861 1.00 45.31  ? 1064 LYS A CA  1 
ATOM   8254  C  C   . LYS A 1 1064 ? 120.929 40.372  105.934 1.00 44.80  ? 1064 LYS A C   1 
ATOM   8255  O  O   . LYS A 1 1064 ? 121.418 41.486  105.750 1.00 43.18  ? 1064 LYS A O   1 
ATOM   8256  C  CB  . LYS A 1 1064 ? 120.117 40.415  103.519 1.00 43.55  ? 1064 LYS A CB  1 
ATOM   8257  C  CG  . LYS A 1 1064 ? 119.564 39.571  102.383 1.00 43.50  ? 1064 LYS A CG  1 
ATOM   8258  C  CD  . LYS A 1 1064 ? 118.746 40.410  101.382 1.00 41.27  ? 1064 LYS A CD  1 
ATOM   8259  C  CE  . LYS A 1 1064 ? 119.404 40.539  100.023 1.00 39.36  ? 1064 LYS A CE  1 
ATOM   8260  N  NZ  . LYS A 1 1064 ? 119.684 39.204  99.407  1.00 39.44  ? 1064 LYS A NZ  1 
ATOM   8261  N  N   . TYR A 1 1065 ? 121.085 39.678  107.057 1.00 46.25  ? 1065 TYR A N   1 
ATOM   8262  C  CA  . TYR A 1 1065 ? 121.708 40.245  108.247 1.00 46.55  ? 1065 TYR A CA  1 
ATOM   8263  C  C   . TYR A 1 1065 ? 123.191 40.533  108.074 1.00 46.99  ? 1065 TYR A C   1 
ATOM   8264  O  O   . TYR A 1 1065 ? 123.668 41.571  108.509 1.00 46.67  ? 1065 TYR A O   1 
ATOM   8265  C  CB  . TYR A 1 1065 ? 121.444 39.368  109.485 1.00 48.32  ? 1065 TYR A CB  1 
ATOM   8266  C  CG  . TYR A 1 1065 ? 119.970 39.089  109.690 1.00 48.27  ? 1065 TYR A CG  1 
ATOM   8267  C  CD1 . TYR A 1 1065 ? 119.489 37.781  109.808 1.00 49.62  ? 1065 TYR A CD1 1 
ATOM   8268  C  CD2 . TYR A 1 1065 ? 119.047 40.137  109.726 1.00 46.59  ? 1065 TYR A CD2 1 
ATOM   8269  C  CE1 . TYR A 1 1065 ? 118.127 37.522  109.970 1.00 49.63  ? 1065 TYR A CE1 1 
ATOM   8270  C  CE2 . TYR A 1 1065 ? 117.683 39.893  109.886 1.00 47.14  ? 1065 TYR A CE2 1 
ATOM   8271  C  CZ  . TYR A 1 1065 ? 117.232 38.584  110.008 1.00 49.38  ? 1065 TYR A CZ  1 
ATOM   8272  O  OH  . TYR A 1 1065 ? 115.885 38.361  110.171 1.00 50.28  ? 1065 TYR A OH  1 
ATOM   8273  N  N   . THR A 1 1066 ? 123.918 39.642  107.420 1.00 48.49  ? 1066 THR A N   1 
ATOM   8274  C  CA  . THR A 1 1066 ? 125.352 39.833  107.308 1.00 49.49  ? 1066 THR A CA  1 
ATOM   8275  C  C   . THR A 1 1066 ? 125.717 40.995  106.371 1.00 47.81  ? 1066 THR A C   1 
ATOM   8276  O  O   . THR A 1 1066 ? 126.567 41.806  106.715 1.00 47.90  ? 1066 THR A O   1 
ATOM   8277  C  CB  . THR A 1 1066 ? 126.133 38.497  107.061 1.00 52.21  ? 1066 THR A CB  1 
ATOM   8278  O  OG1 . THR A 1 1066 ? 127.467 38.786  106.634 1.00 53.22  ? 1066 THR A OG1 1 
ATOM   8279  C  CG2 . THR A 1 1066 ? 125.463 37.636  106.023 1.00 53.37  ? 1066 THR A CG2 1 
ATOM   8280  N  N   . ASP A 1 1067 ? 125.041 41.108  105.229 1.00 46.91  ? 1067 ASP A N   1 
ATOM   8281  C  CA  . ASP A 1 1067 ? 125.251 42.234  104.310 1.00 45.65  ? 1067 ASP A CA  1 
ATOM   8282  C  C   . ASP A 1 1067 ? 124.629 43.527  104.830 1.00 44.07  ? 1067 ASP A C   1 
ATOM   8283  O  O   . ASP A 1 1067 ? 124.904 44.620  104.312 1.00 43.13  ? 1067 ASP A O   1 
ATOM   8284  C  CB  . ASP A 1 1067 ? 124.702 41.925  102.913 1.00 45.15  ? 1067 ASP A CB  1 
ATOM   8285  C  CG  . ASP A 1 1067 ? 125.636 41.048  102.089 1.00 47.46  ? 1067 ASP A CG  1 
ATOM   8286  O  OD1 . ASP A 1 1067 ? 126.872 41.194  102.219 1.00 48.99  ? 1067 ASP A OD1 1 
ATOM   8287  O  OD2 . ASP A 1 1067 ? 125.132 40.205  101.305 1.00 48.94  ? 1067 ASP A OD2 1 
ATOM   8288  N  N   . GLY A 1 1068 ? 123.787 43.395  105.851 1.00 44.07  ? 1068 GLY A N   1 
ATOM   8289  C  CA  . GLY A 1 1068 ? 123.153 44.533  106.486 1.00 42.31  ? 1068 GLY A CA  1 
ATOM   8290  C  C   . GLY A 1 1068 ? 124.091 45.285  107.411 1.00 43.20  ? 1068 GLY A C   1 
ATOM   8291  O  O   . GLY A 1 1068 ? 123.927 46.503  107.587 1.00 41.73  ? 1068 GLY A O   1 
ATOM   8292  N  N   . ILE A 1 1069 ? 125.075 44.602  108.016 1.00 45.13  ? 1069 ILE A N   1 
ATOM   8293  C  CA  . ILE A 1 1069 ? 125.934 45.330  108.971 1.00 46.28  ? 1069 ILE A CA  1 
ATOM   8294  C  C   . ILE A 1 1069 ? 126.710 46.491  108.340 1.00 45.72  ? 1069 ILE A C   1 
ATOM   8295  O  O   . ILE A 1 1069 ? 126.770 47.557  108.939 1.00 45.63  ? 1069 ILE A O   1 
ATOM   8296  C  CB  . ILE A 1 1069 ? 126.796 44.446  109.959 1.00 48.59  ? 1069 ILE A CB  1 
ATOM   8297  C  CG1 . ILE A 1 1069 ? 128.200 44.176  109.421 1.00 51.41  ? 1069 ILE A CG1 1 
ATOM   8298  C  CG2 . ILE A 1 1069 ? 126.039 43.193  110.396 1.00 49.64  ? 1069 ILE A CG2 1 
ATOM   8299  C  CD1 . ILE A 1 1069 ? 129.089 43.278  110.323 1.00 56.95  ? 1069 ILE A CD1 1 
ATOM   8300  N  N   . PRO A 1 1070 ? 127.266 46.322  107.123 1.00 46.10  ? 1070 PRO A N   1 
ATOM   8301  C  CA  . PRO A 1 1070 ? 127.851 47.526  106.530 1.00 45.57  ? 1070 PRO A CA  1 
ATOM   8302  C  C   . PRO A 1 1070 ? 126.870 48.691  106.373 1.00 43.61  ? 1070 PRO A C   1 
ATOM   8303  O  O   . PRO A 1 1070 ? 127.272 49.847  106.492 1.00 43.71  ? 1070 PRO A O   1 
ATOM   8304  C  CB  . PRO A 1 1070 ? 128.343 47.035  105.169 1.00 46.24  ? 1070 PRO A CB  1 
ATOM   8305  C  CG  . PRO A 1 1070 ? 128.601 45.570  105.382 1.00 47.45  ? 1070 PRO A CG  1 
ATOM   8306  C  CD  . PRO A 1 1070 ? 127.470 45.143  106.257 1.00 47.03  ? 1070 PRO A CD  1 
ATOM   8307  N  N   . VAL A 1 1071 ? 125.597 48.395  106.128 1.00 42.30  ? 1071 VAL A N   1 
ATOM   8308  C  CA  . VAL A 1 1071 ? 124.572 49.439  105.988 1.00 40.24  ? 1071 VAL A CA  1 
ATOM   8309  C  C   . VAL A 1 1071 ? 124.344 50.102  107.345 1.00 40.38  ? 1071 VAL A C   1 
ATOM   8310  O  O   . VAL A 1 1071 ? 124.307 51.337  107.468 1.00 39.98  ? 1071 VAL A O   1 
ATOM   8311  C  CB  . VAL A 1 1071 ? 123.256 48.860  105.407 1.00 39.19  ? 1071 VAL A CB  1 
ATOM   8312  C  CG1 . VAL A 1 1071 ? 122.198 49.916  105.258 1.00 36.57  ? 1071 VAL A CG1 1 
ATOM   8313  C  CG2 . VAL A 1 1071 ? 123.527 48.179  104.055 1.00 39.62  ? 1071 VAL A CG2 1 
ATOM   8314  N  N   . MET A 1 1072 ? 124.223 49.274  108.373 1.00 41.27  ? 1072 MET A N   1 
ATOM   8315  C  CA  . MET A 1 1072 ? 124.069 49.778  109.721 1.00 41.38  ? 1072 MET A CA  1 
ATOM   8316  C  C   . MET A 1 1072 ? 125.292 50.601  110.138 1.00 42.14  ? 1072 MET A C   1 
ATOM   8317  O  O   . MET A 1 1072 ? 125.134 51.701  110.670 1.00 42.33  ? 1072 MET A O   1 
ATOM   8318  C  CB  . MET A 1 1072 ? 123.785 48.642  110.697 1.00 42.55  ? 1072 MET A CB  1 
ATOM   8319  C  CG  . MET A 1 1072 ? 123.276 49.140  112.017 1.00 43.58  ? 1072 MET A CG  1 
ATOM   8320  S  SD  . MET A 1 1072 ? 122.709 47.834  113.107 1.00 48.46  ? 1072 MET A SD  1 
ATOM   8321  C  CE  . MET A 1 1072 ? 122.987 48.600  114.706 1.00 46.63  ? 1072 MET A CE  1 
ATOM   8322  N  N   . ASN A 1 1073 ? 126.496 50.092  109.870 1.00 43.12  ? 1073 ASN A N   1 
ATOM   8323  C  CA  . ASN A 1 1073 ? 127.732 50.858  110.079 1.00 43.76  ? 1073 ASN A CA  1 
ATOM   8324  C  C   . ASN A 1 1073 ? 127.628 52.308  109.610 1.00 42.57  ? 1073 ASN A C   1 
ATOM   8325  O  O   . ASN A 1 1073 ? 128.020 53.217  110.336 1.00 43.42  ? 1073 ASN A O   1 
ATOM   8326  C  CB  . ASN A 1 1073 ? 128.916 50.195  109.380 1.00 45.23  ? 1073 ASN A CB  1 
ATOM   8327  C  CG  . ASN A 1 1073 ? 129.472 49.015  110.150 1.00 47.00  ? 1073 ASN A CG  1 
ATOM   8328  O  OD1 . ASN A 1 1073 ? 129.085 48.752  111.289 1.00 47.79  ? 1073 ASN A OD1 1 
ATOM   8329  N  ND2 . ASN A 1 1073 ? 130.395 48.299  109.528 1.00 47.54  ? 1073 ASN A ND2 1 
ATOM   8330  N  N   . TRP A 1 1074 ? 127.098 52.513  108.403 1.00 40.75  ? 1074 TRP A N   1 
ATOM   8331  C  CA  . TRP A 1 1074 ? 126.909 53.851  107.853 1.00 39.31  ? 1074 TRP A CA  1 
ATOM   8332  C  C   . TRP A 1 1074 ? 125.828 54.630  108.606 1.00 38.63  ? 1074 TRP A C   1 
ATOM   8333  O  O   . TRP A 1 1074 ? 126.100 55.727  109.093 1.00 39.35  ? 1074 TRP A O   1 
ATOM   8334  C  CB  . TRP A 1 1074 ? 126.567 53.786  106.367 1.00 37.53  ? 1074 TRP A CB  1 
ATOM   8335  C  CG  . TRP A 1 1074 ? 126.527 55.130  105.708 1.00 35.84  ? 1074 TRP A CG  1 
ATOM   8336  C  CD1 . TRP A 1 1074 ? 127.590 55.816  105.198 1.00 36.49  ? 1074 TRP A CD1 1 
ATOM   8337  C  CD2 . TRP A 1 1074 ? 125.371 55.951  105.481 1.00 33.53  ? 1074 TRP A CD2 1 
ATOM   8338  N  NE1 . TRP A 1 1074 ? 127.176 57.016  104.678 1.00 36.14  ? 1074 TRP A NE1 1 
ATOM   8339  C  CE2 . TRP A 1 1074 ? 125.820 57.131  104.840 1.00 33.79  ? 1074 TRP A CE2 1 
ATOM   8340  C  CE3 . TRP A 1 1074 ? 124.001 55.812  105.772 1.00 31.46  ? 1074 TRP A CE3 1 
ATOM   8341  C  CZ2 . TRP A 1 1074 ? 124.951 58.164  104.468 1.00 32.18  ? 1074 TRP A CZ2 1 
ATOM   8342  C  CZ3 . TRP A 1 1074 ? 123.133 56.832  105.402 1.00 31.31  ? 1074 TRP A CZ3 1 
ATOM   8343  C  CH2 . TRP A 1 1074 ? 123.615 58.002  104.754 1.00 32.19  ? 1074 TRP A CH2 1 
ATOM   8344  N  N   . LEU A 1 1075 ? 124.618 54.072  108.701 1.00 37.46  ? 1075 LEU A N   1 
ATOM   8345  C  CA  . LEU A 1 1075 ? 123.496 54.763  109.355 1.00 36.81  ? 1075 LEU A CA  1 
ATOM   8346  C  C   . LEU A 1 1075 ? 123.807 55.195  110.784 1.00 37.69  ? 1075 LEU A C   1 
ATOM   8347  O  O   . LEU A 1 1075 ? 123.687 56.368  111.152 1.00 37.90  ? 1075 LEU A O   1 
ATOM   8348  C  CB  . LEU A 1 1075 ? 122.245 53.889  109.377 1.00 35.85  ? 1075 LEU A CB  1 
ATOM   8349  C  CG  . LEU A 1 1075 ? 121.474 53.806  108.069 1.00 35.89  ? 1075 LEU A CG  1 
ATOM   8350  C  CD1 . LEU A 1 1075 ? 120.538 52.617  108.137 1.00 37.04  ? 1075 LEU A CD1 1 
ATOM   8351  C  CD2 . LEU A 1 1075 ? 120.709 55.090  107.781 1.00 33.69  ? 1075 LEU A CD2 1 
ATOM   8352  N  N   . VAL A 1 1076 ? 124.197 54.228  111.593 1.00 38.52  ? 1076 VAL A N   1 
ATOM   8353  C  CA  . VAL A 1 1076 ? 124.614 54.499  112.952 1.00 39.17  ? 1076 VAL A CA  1 
ATOM   8354  C  C   . VAL A 1 1076 ? 125.515 55.746  113.025 1.00 39.82  ? 1076 VAL A C   1 
ATOM   8355  O  O   . VAL A 1 1076 ? 125.412 56.530  113.957 1.00 40.26  ? 1076 VAL A O   1 
ATOM   8356  C  CB  . VAL A 1 1076 ? 125.245 53.222  113.535 1.00 40.50  ? 1076 VAL A CB  1 
ATOM   8357  C  CG1 . VAL A 1 1076 ? 126.642 53.449  114.091 1.00 42.11  ? 1076 VAL A CG1 1 
ATOM   8358  C  CG2 . VAL A 1 1076 ? 124.297 52.601  114.526 1.00 40.42  ? 1076 VAL A CG2 1 
ATOM   8359  N  N   . ASN A 1 1077 ? 126.335 55.961  111.999 1.00 40.09  ? 1077 ASN A N   1 
ATOM   8360  C  CA  . ASN A 1 1077 ? 127.325 57.038  112.008 1.00 41.19  ? 1077 ASN A CA  1 
ATOM   8361  C  C   . ASN A 1 1077 ? 126.829 58.386  111.462 1.00 40.05  ? 1077 ASN A C   1 
ATOM   8362  O  O   . ASN A 1 1077 ? 127.575 59.371  111.470 1.00 41.13  ? 1077 ASN A O   1 
ATOM   8363  C  CB  . ASN A 1 1077 ? 128.596 56.595  111.279 1.00 42.43  ? 1077 ASN A CB  1 
ATOM   8364  C  CG  . ASN A 1 1077 ? 129.774 57.491  111.572 1.00 45.16  ? 1077 ASN A CG  1 
ATOM   8365  O  OD1 . ASN A 1 1077 ? 130.006 57.872  112.719 1.00 49.06  ? 1077 ASN A OD1 1 
ATOM   8366  N  ND2 . ASN A 1 1077 ? 130.526 57.841  110.537 1.00 45.52  ? 1077 ASN A ND2 1 
ATOM   8367  N  N   . GLN A 1 1078 ? 125.581 58.428  110.997 1.00 37.94  ? 1078 GLN A N   1 
ATOM   8368  C  CA  . GLN A 1 1078 ? 124.959 59.687  110.552 1.00 37.11  ? 1078 GLN A CA  1 
ATOM   8369  C  C   . GLN A 1 1078 ? 124.037 60.285  111.624 1.00 36.27  ? 1078 GLN A C   1 
ATOM   8370  O  O   . GLN A 1 1078 ? 123.353 61.277  111.385 1.00 35.64  ? 1078 GLN A O   1 
ATOM   8371  C  CB  . GLN A 1 1078 ? 124.170 59.482  109.254 1.00 35.75  ? 1078 GLN A CB  1 
ATOM   8372  C  CG  . GLN A 1 1078 ? 124.860 58.642  108.199 1.00 37.17  ? 1078 GLN A CG  1 
ATOM   8373  C  CD  . GLN A 1 1078 ? 126.245 59.150  107.850 1.00 40.34  ? 1078 GLN A CD  1 
ATOM   8374  O  OE1 . GLN A 1 1078 ? 126.441 60.346  107.635 1.00 42.28  ? 1078 GLN A OE1 1 
ATOM   8375  N  NE2 . GLN A 1 1078 ? 127.215 58.242  107.792 1.00 41.11  ? 1078 GLN A NE2 1 
ATOM   8376  N  N   . ARG A 1 1079 ? 124.034 59.671  112.801 1.00 36.45  ? 1079 ARG A N   1 
ATOM   8377  C  CA  . ARG A 1 1079 ? 123.133 60.025  113.891 1.00 35.97  ? 1079 ARG A CA  1 
ATOM   8378  C  C   . ARG A 1 1079 ? 123.431 61.380  114.529 1.00 37.13  ? 1079 ARG A C   1 
ATOM   8379  O  O   . ARG A 1 1079 ? 124.587 61.813  114.637 1.00 38.33  ? 1079 ARG A O   1 
ATOM   8380  C  CB  . ARG A 1 1079 ? 123.163 58.930  114.959 1.00 36.64  ? 1079 ARG A CB  1 
ATOM   8381  C  CG  . ARG A 1 1079 ? 122.156 57.824  114.720 1.00 35.21  ? 1079 ARG A CG  1 
ATOM   8382  C  CD  . ARG A 1 1079 ? 122.618 56.506  115.317 1.00 36.71  ? 1079 ARG A CD  1 
ATOM   8383  N  NE  . ARG A 1 1079 ? 122.424 56.409  116.756 1.00 37.77  ? 1079 ARG A NE  1 
ATOM   8384  C  CZ  . ARG A 1 1079 ? 123.403 56.348  117.646 1.00 40.38  ? 1079 ARG A CZ  1 
ATOM   8385  N  NH1 . ARG A 1 1079 ? 124.675 56.371  117.277 1.00 41.09  ? 1079 ARG A NH1 1 
ATOM   8386  N  NH2 . ARG A 1 1079 ? 123.099 56.271  118.923 1.00 43.38  ? 1079 ARG A NH2 1 
ATOM   8387  N  N   . TYR A 1 1080 ? 122.363 62.049  114.941 1.00 36.51  ? 1080 TYR A N   1 
ATOM   8388  C  CA  . TYR A 1 1080 ? 122.472 63.310  115.661 1.00 37.72  ? 1080 TYR A CA  1 
ATOM   8389  C  C   . TYR A 1 1080 ? 122.809 63.015  117.119 1.00 39.33  ? 1080 TYR A C   1 
ATOM   8390  O  O   . TYR A 1 1080 ? 122.524 61.931  117.627 1.00 39.42  ? 1080 TYR A O   1 
ATOM   8391  C  CB  . TYR A 1 1080 ? 121.151 64.077  115.538 1.00 36.55  ? 1080 TYR A CB  1 
ATOM   8392  C  CG  . TYR A 1 1080 ? 121.100 65.418  116.238 1.00 37.10  ? 1080 TYR A CG  1 
ATOM   8393  C  CD1 . TYR A 1 1080 ? 121.800 66.514  115.739 1.00 37.05  ? 1080 TYR A CD1 1 
ATOM   8394  C  CD2 . TYR A 1 1080 ? 120.312 65.599  117.371 1.00 35.69  ? 1080 TYR A CD2 1 
ATOM   8395  C  CE1 . TYR A 1 1080 ? 121.736 67.739  116.360 1.00 37.14  ? 1080 TYR A CE1 1 
ATOM   8396  C  CE2 . TYR A 1 1080 ? 120.232 66.816  117.986 1.00 36.44  ? 1080 TYR A CE2 1 
ATOM   8397  C  CZ  . TYR A 1 1080 ? 120.955 67.882  117.487 1.00 38.15  ? 1080 TYR A CZ  1 
ATOM   8398  O  OH  . TYR A 1 1080 ? 120.889 69.106  118.118 1.00 40.87  ? 1080 TYR A OH  1 
ATOM   8399  N  N   . VAL A 1 1081 ? 123.415 63.983  117.791 1.00 41.13  ? 1081 VAL A N   1 
ATOM   8400  C  CA  . VAL A 1 1081 ? 123.846 63.814  119.185 1.00 43.12  ? 1081 VAL A CA  1 
ATOM   8401  C  C   . VAL A 1 1081 ? 122.818 63.173  120.147 1.00 43.15  ? 1081 VAL A C   1 
ATOM   8402  O  O   . VAL A 1 1081 ? 123.207 62.521  121.110 1.00 44.94  ? 1081 VAL A O   1 
ATOM   8403  C  CB  . VAL A 1 1081 ? 124.380 65.154  119.761 1.00 44.74  ? 1081 VAL A CB  1 
ATOM   8404  C  CG1 . VAL A 1 1081 ? 123.249 66.156  119.977 1.00 43.28  ? 1081 VAL A CG1 1 
ATOM   8405  C  CG2 . VAL A 1 1081 ? 125.150 64.918  121.040 1.00 47.68  ? 1081 VAL A CG2 1 
ATOM   8406  N  N   . THR A 1 1082 ? 121.524 63.345  119.886 1.00 42.10  ? 1082 THR A N   1 
ATOM   8407  C  CA  . THR A 1 1082 ? 120.474 62.817  120.770 1.00 42.35  ? 1082 THR A CA  1 
ATOM   8408  C  C   . THR A 1 1082 ? 120.156 61.337  120.558 1.00 41.99  ? 1082 THR A C   1 
ATOM   8409  O  O   . THR A 1 1082 ? 119.402 60.752  121.343 1.00 42.58  ? 1082 THR A O   1 
ATOM   8410  C  CB  . THR A 1 1082 ? 119.142 63.562  120.590 1.00 41.44  ? 1082 THR A CB  1 
ATOM   8411  O  OG1 . THR A 1 1082 ? 118.711 63.448  119.218 1.00 39.69  ? 1082 THR A OG1 1 
ATOM   8412  C  CG2 . THR A 1 1082 ? 119.268 65.015  121.013 1.00 41.56  ? 1082 THR A CG2 1 
ATOM   8413  N  N   . GLY A 1 1083 ? 120.705 60.743  119.501 1.00 41.14  ? 1083 GLY A N   1 
ATOM   8414  C  CA  . GLY A 1 1083 ? 120.355 59.379  119.124 1.00 40.62  ? 1083 GLY A CA  1 
ATOM   8415  C  C   . GLY A 1 1083 ? 119.437 59.340  117.913 1.00 38.98  ? 1083 GLY A C   1 
ATOM   8416  O  O   . GLY A 1 1083 ? 119.324 58.317  117.235 1.00 38.28  ? 1083 GLY A O   1 
ATOM   8417  N  N   . SER A 1 1084 ? 118.766 60.455  117.633 1.00 38.39  ? 1084 SER A N   1 
ATOM   8418  C  CA  . SER A 1 1084 ? 117.947 60.561  116.423 1.00 36.46  ? 1084 SER A CA  1 
ATOM   8419  C  C   . SER A 1 1084 ? 118.850 60.853  115.244 1.00 35.67  ? 1084 SER A C   1 
ATOM   8420  O  O   . SER A 1 1084 ? 120.077 60.825  115.367 1.00 36.84  ? 1084 SER A O   1 
ATOM   8421  C  CB  . SER A 1 1084 ? 116.911 61.685  116.560 1.00 36.28  ? 1084 SER A CB  1 
ATOM   8422  O  OG  . SER A 1 1084 ? 117.528 62.971  116.556 1.00 37.57  ? 1084 SER A OG  1 
ATOM   8423  N  N   . PHE A 1 1085 ? 118.242 61.128  114.101 1.00 33.89  ? 1085 PHE A N   1 
ATOM   8424  C  CA  . PHE A 1 1085 ? 118.973 61.692  112.990 1.00 33.56  ? 1085 PHE A CA  1 
ATOM   8425  C  C   . PHE A 1 1085 ? 118.643 63.183  112.957 1.00 33.68  ? 1085 PHE A C   1 
ATOM   8426  O  O   . PHE A 1 1085 ? 117.648 63.600  113.561 1.00 33.46  ? 1085 PHE A O   1 
ATOM   8427  C  CB  . PHE A 1 1085 ? 118.603 60.976  111.697 1.00 32.62  ? 1085 PHE A CB  1 
ATOM   8428  C  CG  . PHE A 1 1085 ? 119.175 59.584  111.585 1.00 32.98  ? 1085 PHE A CG  1 
ATOM   8429  C  CD1 . PHE A 1 1085 ? 118.494 58.485  112.106 1.00 32.93  ? 1085 PHE A CD1 1 
ATOM   8430  C  CD2 . PHE A 1 1085 ? 120.400 59.370  110.957 1.00 34.32  ? 1085 PHE A CD2 1 
ATOM   8431  C  CE1 . PHE A 1 1085 ? 119.014 57.194  111.995 1.00 31.45  ? 1085 PHE A CE1 1 
ATOM   8432  C  CE2 . PHE A 1 1085 ? 120.931 58.080  110.841 1.00 34.10  ? 1085 PHE A CE2 1 
ATOM   8433  C  CZ  . PHE A 1 1085 ? 120.229 56.996  111.361 1.00 32.98  ? 1085 PHE A CZ  1 
ATOM   8434  N  N   . PRO A 1 1086 ? 119.493 64.004  112.303 1.00 34.25  ? 1086 PRO A N   1 
ATOM   8435  C  CA  . PRO A 1 1086 ? 119.340 65.470  112.397 1.00 34.89  ? 1086 PRO A CA  1 
ATOM   8436  C  C   . PRO A 1 1086 ? 117.984 66.047  111.970 1.00 34.39  ? 1086 PRO A C   1 
ATOM   8437  O  O   . PRO A 1 1086 ? 117.674 67.187  112.312 1.00 35.47  ? 1086 PRO A O   1 
ATOM   8438  C  CB  . PRO A 1 1086 ? 120.461 66.004  111.499 1.00 34.94  ? 1086 PRO A CB  1 
ATOM   8439  C  CG  . PRO A 1 1086 ? 121.443 64.942  111.467 1.00 35.37  ? 1086 PRO A CG  1 
ATOM   8440  C  CD  . PRO A 1 1086 ? 120.677 63.648  111.503 1.00 34.29  ? 1086 PRO A CD  1 
ATOM   8441  N  N   . SER A 1 1087 ? 117.184 65.277  111.247 1.00 33.54  ? 1087 SER A N   1 
ATOM   8442  C  CA  . SER A 1 1087 ? 115.944 65.798  110.683 1.00 33.74  ? 1087 SER A CA  1 
ATOM   8443  C  C   . SER A 1 1087 ? 114.768 64.853  110.945 1.00 33.70  ? 1087 SER A C   1 
ATOM   8444  O  O   . SER A 1 1087 ? 114.925 63.826  111.622 1.00 34.11  ? 1087 SER A O   1 
ATOM   8445  C  CB  . SER A 1 1087 ? 116.121 66.027  109.182 1.00 33.37  ? 1087 SER A CB  1 
ATOM   8446  O  OG  . SER A 1 1087 ? 115.044 66.769  108.658 1.00 33.19  ? 1087 SER A OG  1 
ATOM   8447  N  N   . THR A 1 1088 ? 113.603 65.179  110.391 1.00 33.64  ? 1088 THR A N   1 
ATOM   8448  C  CA  . THR A 1 1088 ? 112.370 64.490  110.761 1.00 33.83  ? 1088 THR A CA  1 
ATOM   8449  C  C   . THR A 1 1088 ? 112.185 63.114  110.117 1.00 33.89  ? 1088 THR A C   1 
ATOM   8450  O  O   . THR A 1 1088 ? 112.209 62.095  110.820 1.00 34.43  ? 1088 THR A O   1 
ATOM   8451  C  CB  . THR A 1 1088 ? 111.161 65.377  110.514 1.00 33.72  ? 1088 THR A CB  1 
ATOM   8452  O  OG1 . THR A 1 1088 ? 111.244 65.899  109.191 1.00 33.79  ? 1088 THR A OG1 1 
ATOM   8453  C  CG2 . THR A 1 1088 ? 111.146 66.542  111.502 1.00 34.47  ? 1088 THR A CG2 1 
ATOM   8454  N  N   . GLN A 1 1089 ? 111.999 63.068  108.796 1.00 34.06  ? 1089 GLN A N   1 
ATOM   8455  C  CA  . GLN A 1 1089 ? 111.822 61.784  108.109 1.00 33.90  ? 1089 GLN A CA  1 
ATOM   8456  C  C   . GLN A 1 1089 ? 113.062 60.914  108.251 1.00 34.21  ? 1089 GLN A C   1 
ATOM   8457  O  O   . GLN A 1 1089 ? 112.956 59.700  108.392 1.00 34.51  ? 1089 GLN A O   1 
ATOM   8458  C  CB  . GLN A 1 1089 ? 111.464 61.971  106.634 1.00 33.69  ? 1089 GLN A CB  1 
ATOM   8459  C  CG  . GLN A 1 1089 ? 110.066 62.527  106.394 1.00 34.62  ? 1089 GLN A CG  1 
ATOM   8460  C  CD  . GLN A 1 1089 ? 108.971 61.543  106.761 1.00 35.36  ? 1089 GLN A CD  1 
ATOM   8461  O  OE1 . GLN A 1 1089 ? 108.981 60.393  106.317 1.00 35.37  ? 1089 GLN A OE1 1 
ATOM   8462  N  NE2 . GLN A 1 1089 ? 108.024 61.990  107.584 1.00 35.66  ? 1089 GLN A NE2 1 
ATOM   8463  N  N   . ASP A 1 1090 ? 114.238 61.536  108.226 1.00 34.78  ? 1090 ASP A N   1 
ATOM   8464  C  CA  . ASP A 1 1090 ? 115.472 60.823  108.510 1.00 35.46  ? 1090 ASP A CA  1 
ATOM   8465  C  C   . ASP A 1 1090 ? 115.306 60.034  109.812 1.00 35.24  ? 1090 ASP A C   1 
ATOM   8466  O  O   . ASP A 1 1090 ? 115.693 58.870  109.884 1.00 35.18  ? 1090 ASP A O   1 
ATOM   8467  C  CB  . ASP A 1 1090 ? 116.635 61.806  108.659 1.00 37.01  ? 1090 ASP A CB  1 
ATOM   8468  C  CG  . ASP A 1 1090 ? 117.005 62.481  107.356 1.00 40.43  ? 1090 ASP A CG  1 
ATOM   8469  O  OD1 . ASP A 1 1090 ? 116.593 61.982  106.270 1.00 44.05  ? 1090 ASP A OD1 1 
ATOM   8470  O  OD2 . ASP A 1 1090 ? 117.717 63.513  107.415 1.00 42.99  ? 1090 ASP A OD2 1 
ATOM   8471  N  N   . THR A 1 1091 ? 114.719 60.673  110.829 1.00 34.59  ? 1091 THR A N   1 
ATOM   8472  C  CA  . THR A 1 1091 ? 114.574 60.052  112.135 1.00 34.66  ? 1091 THR A CA  1 
ATOM   8473  C  C   . THR A 1 1091 ? 113.541 58.921  112.114 1.00 34.21  ? 1091 THR A C   1 
ATOM   8474  O  O   . THR A 1 1091 ? 113.814 57.819  112.632 1.00 34.46  ? 1091 THR A O   1 
ATOM   8475  C  CB  . THR A 1 1091 ? 114.289 61.106  113.245 1.00 35.41  ? 1091 THR A CB  1 
ATOM   8476  O  OG1 . THR A 1 1091 ? 115.463 61.901  113.445 1.00 36.27  ? 1091 THR A OG1 1 
ATOM   8477  C  CG2 . THR A 1 1091 ? 113.915 60.462  114.569 1.00 35.01  ? 1091 THR A CG2 1 
ATOM   8478  N  N   . PHE A 1 1092 ? 112.387 59.166  111.492 1.00 32.80  ? 1092 PHE A N   1 
ATOM   8479  C  CA  . PHE A 1 1092 ? 111.311 58.175  111.503 1.00 32.34  ? 1092 PHE A CA  1 
ATOM   8480  C  C   . PHE A 1 1092 ? 111.691 56.881  110.781 1.00 31.99  ? 1092 PHE A C   1 
ATOM   8481  O  O   . PHE A 1 1092 ? 111.500 55.782  111.319 1.00 32.44  ? 1092 PHE A O   1 
ATOM   8482  C  CB  . PHE A 1 1092 ? 110.026 58.761  110.933 1.00 32.05  ? 1092 PHE A CB  1 
ATOM   8483  C  CG  . PHE A 1 1092 ? 109.674 60.111  111.495 1.00 33.08  ? 1092 PHE A CG  1 
ATOM   8484  C  CD1 . PHE A 1 1092 ? 109.146 61.097  110.673 1.00 31.98  ? 1092 PHE A CD1 1 
ATOM   8485  C  CD2 . PHE A 1 1092 ? 109.882 60.398  112.850 1.00 33.79  ? 1092 PHE A CD2 1 
ATOM   8486  C  CE1 . PHE A 1 1092 ? 108.828 62.341  111.183 1.00 32.69  ? 1092 PHE A CE1 1 
ATOM   8487  C  CE2 . PHE A 1 1092 ? 109.576 61.636  113.368 1.00 34.10  ? 1092 PHE A CE2 1 
ATOM   8488  C  CZ  . PHE A 1 1092 ? 109.042 62.616  112.526 1.00 34.75  ? 1092 PHE A CZ  1 
ATOM   8489  N  N   . VAL A 1 1093 ? 112.238 57.009  109.574 1.00 30.93  ? 1093 VAL A N   1 
ATOM   8490  C  CA  . VAL A 1 1093 ? 112.692 55.836  108.827 1.00 30.72  ? 1093 VAL A CA  1 
ATOM   8491  C  C   . VAL A 1 1093 ? 113.968 55.262  109.449 1.00 31.28  ? 1093 VAL A C   1 
ATOM   8492  O  O   . VAL A 1 1093 ? 114.049 54.060  109.670 1.00 31.63  ? 1093 VAL A O   1 
ATOM   8493  C  CB  . VAL A 1 1093 ? 112.909 56.127  107.316 1.00 30.07  ? 1093 VAL A CB  1 
ATOM   8494  C  CG1 . VAL A 1 1093 ? 113.038 54.826  106.564 1.00 29.34  ? 1093 VAL A CG1 1 
ATOM   8495  C  CG2 . VAL A 1 1093 ? 111.745 56.922  106.755 1.00 29.77  ? 1093 VAL A CG2 1 
ATOM   8496  N  N   . GLY A 1 1094 ? 114.938 56.133  109.742 1.00 31.31  ? 1094 GLY A N   1 
ATOM   8497  C  CA  . GLY A 1 1094 ? 116.223 55.734  110.288 1.00 32.60  ? 1094 GLY A CA  1 
ATOM   8498  C  C   . GLY A 1 1094 ? 116.115 54.907  111.555 1.00 34.70  ? 1094 GLY A C   1 
ATOM   8499  O  O   . GLY A 1 1094 ? 116.636 53.780  111.617 1.00 36.09  ? 1094 GLY A O   1 
ATOM   8500  N  N   . LEU A 1 1095 ? 115.428 55.438  112.567 1.00 35.13  ? 1095 LEU A N   1 
ATOM   8501  C  CA  . LEU A 1 1095 ? 115.268 54.700  113.812 1.00 36.45  ? 1095 LEU A CA  1 
ATOM   8502  C  C   . LEU A 1 1095 ? 114.488 53.403  113.631 1.00 37.35  ? 1095 LEU A C   1 
ATOM   8503  O  O   . LEU A 1 1095 ? 114.832 52.396  114.261 1.00 38.93  ? 1095 LEU A O   1 
ATOM   8504  C  CB  . LEU A 1 1095 ? 114.650 55.555  114.916 1.00 36.53  ? 1095 LEU A CB  1 
ATOM   8505  C  CG  . LEU A 1 1095 ? 115.512 56.637  115.571 1.00 36.95  ? 1095 LEU A CG  1 
ATOM   8506  C  CD1 . LEU A 1 1095 ? 114.726 57.316  116.701 1.00 37.14  ? 1095 LEU A CD1 1 
ATOM   8507  C  CD2 . LEU A 1 1095 ? 116.858 56.103  116.075 1.00 36.61  ? 1095 LEU A CD2 1 
ATOM   8508  N  N   . LYS A 1 1096 ? 113.458 53.409  112.781 1.00 36.84  ? 1096 LYS A N   1 
ATOM   8509  C  CA  . LYS A 1 1096 ? 112.707 52.182  112.513 1.00 37.63  ? 1096 LYS A CA  1 
ATOM   8510  C  C   . LYS A 1 1096 ? 113.701 51.133  112.004 1.00 38.03  ? 1096 LYS A C   1 
ATOM   8511  O  O   . LYS A 1 1096 ? 113.766 50.008  112.518 1.00 39.06  ? 1096 LYS A O   1 
ATOM   8512  C  CB  . LYS A 1 1096 ? 111.574 52.418  111.501 1.00 37.00  ? 1096 LYS A CB  1 
ATOM   8513  C  CG  . LYS A 1 1096 ? 110.401 51.406  111.552 1.00 38.80  ? 1096 LYS A CG  1 
ATOM   8514  C  CD  . LYS A 1 1096 ? 109.543 51.381  110.260 1.00 39.93  ? 1096 LYS A CD  1 
ATOM   8515  C  CE  . LYS A 1 1096 ? 109.067 52.810  109.790 1.00 41.08  ? 1096 LYS A CE  1 
ATOM   8516  N  NZ  . LYS A 1 1096 ? 108.488 52.919  108.370 1.00 39.07  ? 1096 LYS A NZ  1 
ATOM   8517  N  N   . ALA A 1 1097 ? 114.521 51.528  111.038 1.00 37.15  ? 1097 ALA A N   1 
ATOM   8518  C  CA  . ALA A 1 1097 ? 115.426 50.582  110.401 1.00 37.93  ? 1097 ALA A CA  1 
ATOM   8519  C  C   . ALA A 1 1097 ? 116.499 50.064  111.359 1.00 39.31  ? 1097 ALA A C   1 
ATOM   8520  O  O   . ALA A 1 1097 ? 116.775 48.867  111.385 1.00 40.45  ? 1097 ALA A O   1 
ATOM   8521  C  CB  . ALA A 1 1097 ? 116.044 51.182  109.147 1.00 36.82  ? 1097 ALA A CB  1 
ATOM   8522  N  N   . LEU A 1 1098 ? 117.087 50.959  112.149 1.00 39.40  ? 1098 LEU A N   1 
ATOM   8523  C  CA  . LEU A 1 1098 ? 118.149 50.581  113.081 1.00 40.97  ? 1098 LEU A CA  1 
ATOM   8524  C  C   . LEU A 1 1098 ? 117.621 49.627  114.140 1.00 42.61  ? 1098 LEU A C   1 
ATOM   8525  O  O   . LEU A 1 1098 ? 118.239 48.632  114.495 1.00 43.97  ? 1098 LEU A O   1 
ATOM   8526  C  CB  . LEU A 1 1098 ? 118.739 51.830  113.737 1.00 40.74  ? 1098 LEU A CB  1 
ATOM   8527  C  CG  . LEU A 1 1098 ? 119.660 52.665  112.845 1.00 39.77  ? 1098 LEU A CG  1 
ATOM   8528  C  CD1 . LEU A 1 1098 ? 120.239 53.843  113.604 1.00 39.72  ? 1098 LEU A CD1 1 
ATOM   8529  C  CD2 . LEU A 1 1098 ? 120.775 51.794  112.293 1.00 40.29  ? 1098 LEU A CD2 1 
ATOM   8530  N  N   . THR A 1 1099 ? 116.433 49.951  114.605 1.00 43.03  ? 1099 THR A N   1 
ATOM   8531  C  CA  . THR A 1 1099 ? 115.746 49.239  115.652 1.00 44.80  ? 1099 THR A CA  1 
ATOM   8532  C  C   . THR A 1 1099 ? 115.331 47.833  115.214 1.00 45.73  ? 1099 THR A C   1 
ATOM   8533  O  O   . THR A 1 1099 ? 115.478 46.881  115.974 1.00 47.60  ? 1099 THR A O   1 
ATOM   8534  C  CB  . THR A 1 1099 ? 114.584 50.147  116.130 1.00 44.27  ? 1099 THR A CB  1 
ATOM   8535  O  OG1 . THR A 1 1099 ? 114.926 50.683  117.412 1.00 46.61  ? 1099 THR A OG1 1 
ATOM   8536  C  CG2 . THR A 1 1099 ? 113.210 49.459  116.158 1.00 44.66  ? 1099 THR A CG2 1 
ATOM   8537  N  N   . LYS A 1 1100 ? 114.846 47.712  113.979 1.00 44.72  ? 1100 LYS A N   1 
ATOM   8538  C  CA  . LYS A 1 1100 ? 114.465 46.429  113.409 1.00 45.73  ? 1100 LYS A CA  1 
ATOM   8539  C  C   . LYS A 1 1100 ? 115.687 45.560  113.232 1.00 46.60  ? 1100 LYS A C   1 
ATOM   8540  O  O   . LYS A 1 1100 ? 115.658 44.378  113.567 1.00 48.68  ? 1100 LYS A O   1 
ATOM   8541  C  CB  . LYS A 1 1100 ? 113.763 46.611  112.055 1.00 44.57  ? 1100 LYS A CB  1 
ATOM   8542  C  CG  . LYS A 1 1100 ? 112.370 47.223  112.135 1.00 45.40  ? 1100 LYS A CG  1 
ATOM   8543  C  CD  . LYS A 1 1100 ? 111.353 46.240  112.665 1.00 50.55  ? 1100 LYS A CD  1 
ATOM   8544  C  CE  . LYS A 1 1100 ? 109.980 46.883  112.825 1.00 52.74  ? 1100 LYS A CE  1 
ATOM   8545  N  NZ  . LYS A 1 1100 ? 109.042 45.976  113.574 1.00 57.17  ? 1100 LYS A NZ  1 
ATOM   8546  N  N   . MET A 1 1101 ? 116.759 46.150  112.708 1.00 45.75  ? 1101 MET A N   1 
ATOM   8547  C  CA  . MET A 1 1101 ? 118.018 45.434  112.504 1.00 47.19  ? 1101 MET A CA  1 
ATOM   8548  C  C   . MET A 1 1101 ? 118.606 45.001  113.847 1.00 49.39  ? 1101 MET A C   1 
ATOM   8549  O  O   . MET A 1 1101 ? 119.033 43.859  114.000 1.00 51.22  ? 1101 MET A O   1 
ATOM   8550  C  CB  . MET A 1 1101 ? 119.007 46.283  111.696 1.00 45.72  ? 1101 MET A CB  1 
ATOM   8551  C  CG  . MET A 1 1101 ? 120.400 45.678  111.498 1.00 46.85  ? 1101 MET A CG  1 
ATOM   8552  S  SD  . MET A 1 1101 ? 120.532 44.207  110.450 1.00 48.36  ? 1101 MET A SD  1 
ATOM   8553  C  CE  . MET A 1 1101 ? 119.954 44.795  108.891 1.00 48.87  ? 1101 MET A CE  1 
ATOM   8554  N  N   . ALA A 1 1102 ? 118.595 45.909  114.821 1.00 49.54  ? 1102 ALA A N   1 
ATOM   8555  C  CA  . ALA A 1 1102 ? 119.059 45.599  116.163 1.00 51.90  ? 1102 ALA A CA  1 
ATOM   8556  C  C   . ALA A 1 1102 ? 118.349 44.385  116.777 1.00 54.26  ? 1102 ALA A C   1 
ATOM   8557  O  O   . ALA A 1 1102 ? 119.020 43.457  117.221 1.00 56.12  ? 1102 ALA A O   1 
ATOM   8558  C  CB  . ALA A 1 1102 ? 118.933 46.807  117.057 1.00 51.37  ? 1102 ALA A CB  1 
ATOM   8559  N  N   . GLU A 1 1103 ? 117.013 44.372  116.783 1.00 54.37  ? 1103 GLU A N   1 
ATOM   8560  C  CA  . GLU A 1 1103 ? 116.270 43.260  117.399 1.00 57.47  ? 1103 GLU A CA  1 
ATOM   8561  C  C   . GLU A 1 1103 ? 116.751 41.913  116.903 1.00 58.87  ? 1103 GLU A C   1 
ATOM   8562  O  O   . GLU A 1 1103 ? 116.793 40.954  117.665 1.00 61.60  ? 1103 GLU A O   1 
ATOM   8563  C  CB  . GLU A 1 1103 ? 114.775 43.344  117.124 1.00 57.05  ? 1103 GLU A CB  1 
ATOM   8564  C  CG  . GLU A 1 1103 ? 114.078 44.525  117.749 1.00 59.28  ? 1103 GLU A CG  1 
ATOM   8565  C  CD  . GLU A 1 1103 ? 112.930 45.055  116.876 1.00 61.46  ? 1103 GLU A CD  1 
ATOM   8566  O  OE1 . GLU A 1 1103 ? 112.344 44.252  116.091 1.00 62.59  ? 1103 GLU A OE1 1 
ATOM   8567  O  OE2 . GLU A 1 1103 ? 112.621 46.276  116.979 1.00 60.04  ? 1103 GLU A OE2 1 
ATOM   8568  N  N   . LYS A 1 1104 ? 117.114 41.849  115.626 1.00 57.58  ? 1104 LYS A N   1 
ATOM   8569  C  CA  . LYS A 1 1104 ? 117.431 40.582  114.980 1.00 58.96  ? 1104 LYS A CA  1 
ATOM   8570  C  C   . LYS A 1 1104 ? 118.894 40.151  115.104 1.00 60.24  ? 1104 LYS A C   1 
ATOM   8571  O  O   . LYS A 1 1104 ? 119.183 38.956  115.075 1.00 62.56  ? 1104 LYS A O   1 
ATOM   8572  C  CB  . LYS A 1 1104 ? 116.987 40.601  113.513 1.00 57.45  ? 1104 LYS A CB  1 
ATOM   8573  C  CG  . LYS A 1 1104 ? 115.472 40.719  113.320 1.00 57.33  ? 1104 LYS A CG  1 
ATOM   8574  C  CD  . LYS A 1 1104 ? 114.819 39.345  113.164 1.00 61.41  ? 1104 LYS A CD  1 
ATOM   8575  C  CE  . LYS A 1 1104 ? 113.353 39.322  113.623 1.00 62.53  ? 1104 LYS A CE  1 
ATOM   8576  N  NZ  . LYS A 1 1104 ? 112.441 40.193  112.824 1.00 59.32  ? 1104 LYS A NZ  1 
ATOM   8577  N  N   . ILE A 1 1105 ? 119.815 41.097  115.262 1.00 59.25  ? 1105 ILE A N   1 
ATOM   8578  C  CA  . ILE A 1 1105 ? 121.242 40.739  115.263 1.00 60.70  ? 1105 ILE A CA  1 
ATOM   8579  C  C   . ILE A 1 1105 ? 121.922 40.687  116.629 1.00 62.88  ? 1105 ILE A C   1 
ATOM   8580  O  O   . ILE A 1 1105 ? 122.982 40.087  116.759 1.00 65.02  ? 1105 ILE A O   1 
ATOM   8581  C  CB  . ILE A 1 1105 ? 122.102 41.630  114.310 1.00 58.81  ? 1105 ILE A CB  1 
ATOM   8582  C  CG1 . ILE A 1 1105 ? 122.123 43.092  114.779 1.00 57.09  ? 1105 ILE A CG1 1 
ATOM   8583  C  CG2 . ILE A 1 1105 ? 121.636 41.487  112.862 1.00 57.15  ? 1105 ILE A CG2 1 
ATOM   8584  C  CD1 . ILE A 1 1105 ? 123.288 43.902  114.228 1.00 55.88  ? 1105 ILE A CD1 1 
ATOM   8585  N  N   . SER A 1 1106 ? 121.334 41.312  117.640 1.00 63.01  ? 1106 SER A N   1 
ATOM   8586  C  CA  . SER A 1 1106 ? 122.024 41.440  118.921 1.00 65.19  ? 1106 SER A CA  1 
ATOM   8587  C  C   . SER A 1 1106 ? 121.842 40.236  119.837 1.00 68.75  ? 1106 SER A C   1 
ATOM   8588  O  O   . SER A 1 1106 ? 120.763 39.643  119.884 1.00 69.25  ? 1106 SER A O   1 
ATOM   8589  C  CB  . SER A 1 1106 ? 121.683 42.760  119.634 1.00 63.73  ? 1106 SER A CB  1 
ATOM   8590  O  OG  . SER A 1 1106 ? 120.463 43.317  119.192 1.00 61.52  ? 1106 SER A OG  1 
ATOM   8591  N  N   . PRO A 1 1107 ? 122.915 39.856  120.554 1.00 71.58  ? 1107 PRO A N   1 
ATOM   8592  C  CA  . PRO A 1 1107 ? 122.905 38.685  121.424 1.00 75.40  ? 1107 PRO A CA  1 
ATOM   8593  C  C   . PRO A 1 1107 ? 121.815 38.720  122.489 1.00 77.06  ? 1107 PRO A C   1 
ATOM   8594  O  O   . PRO A 1 1107 ? 121.277 39.787  122.805 1.00 75.54  ? 1107 PRO A O   1 
ATOM   8595  C  CB  . PRO A 1 1107 ? 124.282 38.739  122.087 1.00 77.23  ? 1107 PRO A CB  1 
ATOM   8596  C  CG  . PRO A 1 1107 ? 125.126 39.485  121.140 1.00 74.93  ? 1107 PRO A CG  1 
ATOM   8597  C  CD  . PRO A 1 1107 ? 124.231 40.523  120.561 1.00 71.48  ? 1107 PRO A CD  1 
ATOM   8598  N  N   . SER A 1 1108 ? 121.498 37.546  123.030 1.00 80.85  ? 1108 SER A N   1 
ATOM   8599  C  CA  . SER A 1 1108 ? 120.578 37.415  124.158 1.00 83.24  ? 1108 SER A CA  1 
ATOM   8600  C  C   . SER A 1 1108 ? 121.058 38.205  125.375 1.00 84.52  ? 1108 SER A C   1 
ATOM   8601  O  O   . SER A 1 1108 ? 120.256 38.823  126.072 1.00 84.42  ? 1108 SER A O   1 
ATOM   8602  C  CB  . SER A 1 1108 ? 120.409 35.940  124.537 1.00 86.83  ? 1108 SER A CB  1 
ATOM   8603  O  OG  . SER A 1 1108 ? 119.798 35.217  123.484 1.00 86.76  ? 1108 SER A OG  1 
ATOM   8604  N  N   . ARG A 1 1109 ? 122.367 38.185  125.618 1.00 86.12  ? 1109 ARG A N   1 
ATOM   8605  C  CA  . ARG A 1 1109 ? 122.940 38.790  126.819 1.00 88.09  ? 1109 ARG A CA  1 
ATOM   8606  C  C   . ARG A 1 1109 ? 124.163 39.655  126.520 1.00 86.58  ? 1109 ARG A C   1 
ATOM   8607  O  O   . ARG A 1 1109 ? 124.975 39.315  125.654 1.00 86.27  ? 1109 ARG A O   1 
ATOM   8608  C  CB  . ARG A 1 1109 ? 123.308 37.698  127.835 1.00 92.68  ? 1109 ARG A CB  1 
ATOM   8609  C  CG  . ARG A 1 1109 ? 122.123 37.132  128.611 1.00 96.08  ? 1109 ARG A CG  1 
ATOM   8610  C  CD  . ARG A 1 1109 ? 122.579 36.089  129.630 1.00 103.44 ? 1109 ARG A CD  1 
ATOM   8611  N  NE  . ARG A 1 1109 ? 121.699 36.025  130.800 1.00 107.13 ? 1109 ARG A NE  1 
ATOM   8612  C  CZ  . ARG A 1 1109 ? 121.879 35.211  131.841 1.00 112.51 ? 1109 ARG A CZ  1 
ATOM   8613  N  NH1 . ARG A 1 1109 ? 122.912 34.374  131.875 1.00 115.45 ? 1109 ARG A NH1 1 
ATOM   8614  N  NH2 . ARG A 1 1109 ? 121.021 35.233  132.854 1.00 114.91 ? 1109 ARG A NH2 1 
ATOM   8615  N  N   . ASN A 1 1110 ? 124.281 40.770  127.244 1.00 85.84  ? 1110 ASN A N   1 
ATOM   8616  C  CA  . ASN A 1 1110 ? 125.465 41.629  127.185 1.00 84.94  ? 1110 ASN A CA  1 
ATOM   8617  C  C   . ASN A 1 1110 ? 126.356 41.371  128.383 1.00 88.30  ? 1110 ASN A C   1 
ATOM   8618  O  O   . ASN A 1 1110 ? 125.897 41.411  129.516 1.00 90.19  ? 1110 ASN A O   1 
ATOM   8619  C  CB  . ASN A 1 1110 ? 125.082 43.111  127.169 1.00 82.40  ? 1110 ASN A CB  1 
ATOM   8620  C  CG  . ASN A 1 1110 ? 124.177 43.474  126.018 1.00 78.79  ? 1110 ASN A CG  1 
ATOM   8621  O  OD1 . ASN A 1 1110 ? 124.373 43.025  124.886 1.00 77.87  ? 1110 ASN A OD1 1 
ATOM   8622  N  ND2 . ASN A 1 1110 ? 123.179 44.304  126.299 1.00 77.15  ? 1110 ASN A ND2 1 
ATOM   8623  N  N   . ASP A 1 1111 ? 127.631 41.112  128.113 1.00 89.28  ? 1111 ASP A N   1 
ATOM   8624  C  CA  . ASP A 1 1111 ? 128.635 40.817  129.131 1.00 92.64  ? 1111 ASP A CA  1 
ATOM   8625  C  C   . ASP A 1 1111 ? 129.999 41.239  128.590 1.00 92.09  ? 1111 ASP A C   1 
ATOM   8626  O  O   . ASP A 1 1111 ? 130.722 40.416  128.010 1.00 92.98  ? 1111 ASP A O   1 
ATOM   8627  C  CB  . ASP A 1 1111 ? 128.626 39.322  129.477 1.00 96.05  ? 1111 ASP A CB  1 
ATOM   8628  C  CG  . ASP A 1 1111 ? 129.679 38.948  130.519 1.00 101.07 ? 1111 ASP A CG  1 
ATOM   8629  O  OD1 . ASP A 1 1111 ? 129.706 39.579  131.602 1.00 103.06 ? 1111 ASP A OD1 1 
ATOM   8630  O  OD2 . ASP A 1 1111 ? 130.475 38.013  130.254 1.00 103.68 ? 1111 ASP A OD2 1 
ATOM   8631  N  N   . TYR A 1 1112 ? 130.343 42.528  128.763 1.00 90.59  ? 1112 TYR A N   1 
ATOM   8632  C  CA  . TYR A 1 1112 ? 131.590 43.043  128.202 1.00 90.10  ? 1112 TYR A CA  1 
ATOM   8633  C  C   . TYR A 1 1112 ? 132.290 44.137  129.013 1.00 91.14  ? 1112 TYR A C   1 
ATOM   8634  O  O   . TYR A 1 1112 ? 131.690 44.764  129.894 1.00 91.18  ? 1112 TYR A O   1 
ATOM   8635  C  CB  . TYR A 1 1112 ? 131.408 43.475  126.737 1.00 86.33  ? 1112 TYR A CB  1 
ATOM   8636  C  CG  . TYR A 1 1112 ? 130.321 44.503  126.462 1.00 82.68  ? 1112 TYR A CG  1 
ATOM   8637  C  CD1 . TYR A 1 1112 ? 129.058 44.109  125.990 1.00 80.93  ? 1112 TYR A CD1 1 
ATOM   8638  C  CD2 . TYR A 1 1112 ? 130.567 45.869  126.623 1.00 81.80  ? 1112 TYR A CD2 1 
ATOM   8639  C  CE1 . TYR A 1 1112 ? 128.053 45.049  125.704 1.00 78.69  ? 1112 TYR A CE1 1 
ATOM   8640  C  CE2 . TYR A 1 1112 ? 129.571 46.820  126.342 1.00 79.86  ? 1112 TYR A CE2 1 
ATOM   8641  C  CZ  . TYR A 1 1112 ? 128.319 46.401  125.880 1.00 77.89  ? 1112 TYR A CZ  1 
ATOM   8642  O  OH  . TYR A 1 1112 ? 127.338 47.330  125.608 1.00 74.72  ? 1112 TYR A OH  1 
ATOM   8643  N  N   . THR A 1 1113 ? 133.570 44.341  128.669 1.00 91.94  ? 1113 THR A N   1 
ATOM   8644  C  CA  . THR A 1 1113 ? 134.404 45.374  129.257 1.00 93.11  ? 1113 THR A CA  1 
ATOM   8645  C  C   . THR A 1 1113 ? 134.835 46.342  128.164 1.00 90.60  ? 1113 THR A C   1 
ATOM   8646  O  O   . THR A 1 1113 ? 135.220 45.921  127.073 1.00 89.60  ? 1113 THR A O   1 
ATOM   8647  C  CB  . THR A 1 1113 ? 135.677 44.779  129.891 1.00 97.45  ? 1113 THR A CB  1 
ATOM   8648  O  OG1 . THR A 1 1113 ? 135.419 43.449  130.367 1.00 99.48  ? 1113 THR A OG1 1 
ATOM   8649  C  CG2 . THR A 1 1113 ? 136.169 45.653  131.041 1.00 99.78  ? 1113 THR A CG2 1 
ATOM   8650  N  N   . VAL A 1 1114 ? 134.763 47.639  128.450 1.00 89.77  ? 1114 VAL A N   1 
ATOM   8651  C  CA  . VAL A 1 1114 ? 135.280 48.647  127.528 1.00 88.03  ? 1114 VAL A CA  1 
ATOM   8652  C  C   . VAL A 1 1114 ? 136.368 49.449  128.225 1.00 91.01  ? 1114 VAL A C   1 
ATOM   8653  O  O   . VAL A 1 1114 ? 136.139 50.043  129.278 1.00 92.21  ? 1114 VAL A O   1 
ATOM   8654  C  CB  . VAL A 1 1114 ? 134.170 49.588  126.987 1.00 84.18  ? 1114 VAL A CB  1 
ATOM   8655  C  CG1 . VAL A 1 1114 ? 134.775 50.740  126.196 1.00 82.92  ? 1114 VAL A CG1 1 
ATOM   8656  C  CG2 . VAL A 1 1114 ? 133.190 48.817  126.116 1.00 81.15  ? 1114 VAL A CG2 1 
ATOM   8657  N  N   . GLN A 1 1115 ? 137.557 49.440  127.634 1.00 92.64  ? 1115 GLN A N   1 
ATOM   8658  C  CA  . GLN A 1 1115 ? 138.675 50.217  128.143 1.00 95.93  ? 1115 GLN A CA  1 
ATOM   8659  C  C   . GLN A 1 1115 ? 138.933 51.394  127.212 1.00 94.41  ? 1115 GLN A C   1 
ATOM   8660  O  O   . GLN A 1 1115 ? 139.167 51.215  126.013 1.00 92.94  ? 1115 GLN A O   1 
ATOM   8661  C  CB  . GLN A 1 1115 ? 139.923 49.344  128.274 1.00 99.42  ? 1115 GLN A CB  1 
ATOM   8662  C  CG  . GLN A 1 1115 ? 141.125 50.072  128.843 1.00 103.08 ? 1115 GLN A CG  1 
ATOM   8663  C  CD  . GLN A 1 1115 ? 142.420 49.290  128.702 1.00 106.60 ? 1115 GLN A CD  1 
ATOM   8664  O  OE1 . GLN A 1 1115 ? 142.784 48.851  127.609 1.00 105.80 ? 1115 GLN A OE1 1 
ATOM   8665  N  NE2 . GLN A 1 1115 ? 143.130 49.125  129.810 1.00 110.12 ? 1115 GLN A NE2 1 
ATOM   8666  N  N   . LEU A 1 1116 ? 138.869 52.596  127.773 1.00 95.19  ? 1116 LEU A N   1 
ATOM   8667  C  CA  . LEU A 1 1116 ? 139.107 53.815  127.018 1.00 94.30  ? 1116 LEU A CA  1 
ATOM   8668  C  C   . LEU A 1 1116 ? 140.499 54.334  127.342 1.00 98.45  ? 1116 LEU A C   1 
ATOM   8669  O  O   . LEU A 1 1116 ? 140.749 54.824  128.444 1.00 100.86 ? 1116 LEU A O   1 
ATOM   8670  C  CB  . LEU A 1 1116 ? 138.044 54.865  127.356 1.00 92.18  ? 1116 LEU A CB  1 
ATOM   8671  C  CG  . LEU A 1 1116 ? 138.126 56.239  126.688 1.00 90.90  ? 1116 LEU A CG  1 
ATOM   8672  C  CD1 . LEU A 1 1116 ? 137.774 56.152  125.213 1.00 87.69  ? 1116 LEU A CD1 1 
ATOM   8673  C  CD2 . LEU A 1 1116 ? 137.212 57.229  127.397 1.00 89.99  ? 1116 LEU A CD2 1 
ATOM   8674  N  N   . LYS A 1 1117 ? 141.407 54.207  126.380 1.00 99.54  ? 1117 LYS A N   1 
ATOM   8675  C  CA  . LYS A 1 1117 ? 142.782 54.654  126.567 1.00 103.82 ? 1117 LYS A CA  1 
ATOM   8676  C  C   . LYS A 1 1117 ? 143.044 55.908  125.743 1.00 103.24 ? 1117 LYS A C   1 
ATOM   8677  O  O   . LYS A 1 1117 ? 142.797 55.931  124.531 1.00 100.69 ? 1117 LYS A O   1 
ATOM   8678  C  CB  . LYS A 1 1117 ? 143.774 53.546  126.197 1.00 105.93 ? 1117 LYS A CB  1 
ATOM   8679  C  CG  . LYS A 1 1117 ? 145.163 53.753  126.777 1.00 111.39 ? 1117 LYS A CG  1 
ATOM   8680  C  CD  . LYS A 1 1117 ? 146.183 52.769  126.218 1.00 114.10 ? 1117 LYS A CD  1 
ATOM   8681  C  CE  . LYS A 1 1117 ? 147.568 53.060  126.788 1.00 119.27 ? 1117 LYS A CE  1 
ATOM   8682  N  NZ  . LYS A 1 1117 ? 148.627 52.192  126.205 1.00 122.04 ? 1117 LYS A NZ  1 
ATOM   8683  N  N   . TYR A 1 1118 ? 143.520 56.953  126.416 1.00 105.97 ? 1118 TYR A N   1 
ATOM   8684  C  CA  . TYR A 1 1118 ? 143.892 58.203  125.756 1.00 106.42 ? 1118 TYR A CA  1 
ATOM   8685  C  C   . TYR A 1 1118 ? 145.065 58.860  126.471 1.00 111.40 ? 1118 TYR A C   1 
ATOM   8686  O  O   . TYR A 1 1118 ? 145.181 58.766  127.694 1.00 114.00 ? 1118 TYR A O   1 
ATOM   8687  C  CB  . TYR A 1 1118 ? 142.697 59.168  125.650 1.00 103.06 ? 1118 TYR A CB  1 
ATOM   8688  C  CG  . TYR A 1 1118 ? 142.081 59.579  126.971 1.00 103.39 ? 1118 TYR A CG  1 
ATOM   8689  C  CD1 . TYR A 1 1118 ? 141.042 58.841  127.539 1.00 101.13 ? 1118 TYR A CD1 1 
ATOM   8690  C  CD2 . TYR A 1 1118 ? 142.528 60.714  127.646 1.00 106.08 ? 1118 TYR A CD2 1 
ATOM   8691  C  CE1 . TYR A 1 1118 ? 140.472 59.217  128.752 1.00 102.04 ? 1118 TYR A CE1 1 
ATOM   8692  C  CE2 . TYR A 1 1118 ? 141.967 61.098  128.861 1.00 107.03 ? 1118 TYR A CE2 1 
ATOM   8693  C  CZ  . TYR A 1 1118 ? 140.940 60.346  129.408 1.00 105.14 ? 1118 TYR A CZ  1 
ATOM   8694  O  OH  . TYR A 1 1118 ? 140.387 60.728  130.609 1.00 106.34 ? 1118 TYR A OH  1 
ATOM   8695  N  N   . LYS A 1 1119 ? 145.924 59.517  125.692 1.00 113.27 ? 1119 LYS A N   1 
ATOM   8696  C  CA  . LYS A 1 1119 ? 147.122 60.210  126.189 1.00 118.31 ? 1119 LYS A CA  1 
ATOM   8697  C  C   . LYS A 1 1119 ? 147.905 59.413  127.243 1.00 122.44 ? 1119 LYS A C   1 
ATOM   8698  O  O   . LYS A 1 1119 ? 148.830 58.677  126.901 1.00 124.71 ? 1119 LYS A O   1 
ATOM   8699  C  CB  . LYS A 1 1119 ? 146.786 61.630  126.684 1.00 118.74 ? 1119 LYS A CB  1 
ATOM   8700  C  CG  . LYS A 1 1119 ? 148.001 62.554  126.747 1.00 123.45 ? 1119 LYS A CG  1 
ATOM   8701  C  CD  . LYS A 1 1119 ? 147.660 63.944  127.360 1.00 124.92 ? 1119 LYS A CD  1 
ATOM   8702  C  CE  . LYS A 1 1119 ? 149.041 64.509  127.964 1.00 130.82 ? 1119 LYS A CE  1 
ATOM   8703  N  NZ  . LYS A 1 1119 ? 148.861 65.903  128.487 1.00 131.85 ? 1119 LYS A NZ  1 
ATOM   8704  N  N   . LYS A 1 1120 ? 147.528 59.559  128.513 1.00 123.83 ? 1120 LYS A N   1 
ATOM   8705  C  CA  . LYS A 1 1120 ? 148.197 58.860  129.612 1.00 127.99 ? 1120 LYS A CA  1 
ATOM   8706  C  C   . LYS A 1 1120 ? 147.236 58.076  130.509 1.00 126.77 ? 1120 LYS A C   1 
ATOM   8707  O  O   . LYS A 1 1120 ? 147.674 57.270  131.333 1.00 129.78 ? 1120 LYS A O   1 
ATOM   8708  C  CB  . LYS A 1 1120 ? 149.013 59.843  130.460 1.00 132.43 ? 1120 LYS A CB  1 
ATOM   8709  C  CG  . LYS A 1 1120 ? 150.424 60.096  129.944 1.00 136.24 ? 1120 LYS A CG  1 
ATOM   8710  C  CD  . LYS A 1 1120 ? 151.313 60.695  131.035 1.00 141.52 ? 1120 LYS A CD  1 
ATOM   8711  C  CE  . LYS A 1 1120 ? 152.785 60.669  130.641 1.00 145.56 ? 1120 LYS A CE  1 
ATOM   8712  N  NZ  . LYS A 1 1120 ? 153.680 60.989  131.791 1.00 150.95 ? 1120 LYS A NZ  1 
ATOM   8713  N  N   . SER A 1 1121 ? 145.936 58.310  130.345 1.00 122.68 ? 1121 SER A N   1 
ATOM   8714  C  CA  . SER A 1 1121 ? 144.926 57.738  131.241 1.00 121.61 ? 1121 SER A CA  1 
ATOM   8715  C  C   . SER A 1 1121 ? 144.224 56.501  130.683 1.00 118.49 ? 1121 SER A C   1 
ATOM   8716  O  O   . SER A 1 1121 ? 144.462 56.091  129.542 1.00 116.87 ? 1121 SER A O   1 
ATOM   8717  C  CB  . SER A 1 1121 ? 143.891 58.801  131.632 1.00 119.67 ? 1121 SER A CB  1 
ATOM   8718  O  OG  . SER A 1 1121 ? 144.383 59.639  132.664 1.00 123.46 ? 1121 SER A OG  1 
ATOM   8719  N  N   . ALA A 1 1122 ? 143.370 55.908  131.517 1.00 117.94 ? 1122 ALA A N   1 
ATOM   8720  C  CA  . ALA A 1 1122 ? 142.571 54.746  131.145 1.00 115.32 ? 1122 ALA A CA  1 
ATOM   8721  C  C   . ALA A 1 1122 ? 141.269 54.687  131.944 1.00 113.84 ? 1122 ALA A C   1 
ATOM   8722  O  O   . ALA A 1 1122 ? 141.291 54.590  133.170 1.00 116.63 ? 1122 ALA A O   1 
ATOM   8723  C  CB  . ALA A 1 1122 ? 143.370 53.461  131.330 1.00 118.07 ? 1122 ALA A CB  1 
ATOM   8724  N  N   . LYS A 1 1123 ? 140.141 54.752  131.240 1.00 109.80 ? 1123 LYS A N   1 
ATOM   8725  C  CA  . LYS A 1 1123 ? 138.823 54.627  131.865 1.00 108.23 ? 1123 LYS A CA  1 
ATOM   8726  C  C   . LYS A 1 1123 ? 138.183 53.287  131.530 1.00 106.57 ? 1123 LYS A C   1 
ATOM   8727  O  O   . LYS A 1 1123 ? 138.271 52.807  130.398 1.00 104.47 ? 1123 LYS A O   1 
ATOM   8728  C  CB  . LYS A 1 1123 ? 137.900 55.792  131.472 1.00 105.02 ? 1123 LYS A CB  1 
ATOM   8729  C  CG  . LYS A 1 1123 ? 138.212 57.127  132.175 1.00 107.26 ? 1123 LYS A CG  1 
ATOM   8730  C  CD  . LYS A 1 1123 ? 137.832 57.118  133.666 1.00 110.03 ? 1123 LYS A CD  1 
ATOM   8731  C  CE  . LYS A 1 1123 ? 138.375 58.347  134.395 1.00 112.84 ? 1123 LYS A CE  1 
ATOM   8732  N  NZ  . LYS A 1 1123 ? 138.224 58.243  135.886 1.00 115.63 ? 1123 LYS A NZ  1 
ATOM   8733  N  N   . TYR A 1 1124 ? 137.548 52.688  132.532 1.00 107.83 ? 1124 TYR A N   1 
ATOM   8734  C  CA  . TYR A 1 1124 ? 136.986 51.353  132.410 1.00 107.39 ? 1124 TYR A CA  1 
ATOM   8735  C  C   . TYR A 1 1124 ? 135.481 51.368  132.555 1.00 104.88 ? 1124 TYR A C   1 
ATOM   8736  O  O   . TYR A 1 1124 ? 134.934 52.058  133.423 1.00 105.27 ? 1124 TYR A O   1 
ATOM   8737  C  CB  . TYR A 1 1124 ? 137.580 50.416  133.464 1.00 111.78 ? 1124 TYR A CB  1 
ATOM   8738  C  CG  . TYR A 1 1124 ? 139.041 50.109  133.265 1.00 114.62 ? 1124 TYR A CG  1 
ATOM   8739  C  CD1 . TYR A 1 1124 ? 140.022 50.874  133.893 1.00 118.07 ? 1124 TYR A CD1 1 
ATOM   8740  C  CD2 . TYR A 1 1124 ? 139.445 49.052  132.452 1.00 114.58 ? 1124 TYR A CD2 1 
ATOM   8741  C  CE1 . TYR A 1 1124 ? 141.372 50.597  133.716 1.00 121.33 ? 1124 TYR A CE1 1 
ATOM   8742  C  CE2 . TYR A 1 1124 ? 140.793 48.765  132.268 1.00 117.70 ? 1124 TYR A CE2 1 
ATOM   8743  C  CZ  . TYR A 1 1124 ? 141.751 49.541  132.902 1.00 121.09 ? 1124 TYR A CZ  1 
ATOM   8744  O  OH  . TYR A 1 1124 ? 143.089 49.263  132.731 1.00 124.59 ? 1124 TYR A OH  1 
ATOM   8745  N  N   . PHE A 1 1125 ? 134.826 50.591  131.695 1.00 102.62 ? 1125 PHE A N   1 
ATOM   8746  C  CA  . PHE A 1 1125 ? 133.381 50.435  131.724 1.00 100.57 ? 1125 PHE A CA  1 
ATOM   8747  C  C   . PHE A 1 1125 ? 133.027 48.961  131.607 1.00 101.42 ? 1125 PHE A C   1 
ATOM   8748  O  O   . PHE A 1 1125 ? 133.640 48.214  130.826 1.00 101.29 ? 1125 PHE A O   1 
ATOM   8749  C  CB  . PHE A 1 1125 ? 132.719 51.211  130.580 1.00 96.22  ? 1125 PHE A CB  1 
ATOM   8750  C  CG  . PHE A 1 1125 ? 133.097 52.665  130.530 1.00 95.22  ? 1125 PHE A CG  1 
ATOM   8751  C  CD1 . PHE A 1 1125 ? 134.074 53.101  129.632 1.00 94.26  ? 1125 PHE A CD1 1 
ATOM   8752  C  CD2 . PHE A 1 1125 ? 132.472 53.603  131.373 1.00 94.43  ? 1125 PHE A CD2 1 
ATOM   8753  C  CE1 . PHE A 1 1125 ? 134.429 54.448  129.578 1.00 93.61  ? 1125 PHE A CE1 1 
ATOM   8754  C  CE2 . PHE A 1 1125 ? 132.820 54.951  131.327 1.00 93.79  ? 1125 PHE A CE2 1 
ATOM   8755  C  CZ  . PHE A 1 1125 ? 133.800 55.375  130.428 1.00 93.38  ? 1125 PHE A CZ  1 
ATOM   8756  N  N   . LYS A 1 1126 ? 132.032 48.555  132.390 1.00 102.64 ? 1126 LYS A N   1 
ATOM   8757  C  CA  . LYS A 1 1126 ? 131.551 47.183  132.373 1.00 104.01 ? 1126 LYS A CA  1 
ATOM   8758  C  C   . LYS A 1 1126 ? 130.045 47.153  132.189 1.00 101.85 ? 1126 LYS A C   1 
ATOM   8759  O  O   . LYS A 1 1126 ? 129.301 47.810  132.923 1.00 101.98 ? 1126 LYS A O   1 
ATOM   8760  C  CB  . LYS A 1 1126 ? 131.946 46.453  133.658 1.00 108.42 ? 1126 LYS A CB  1 
ATOM   8761  C  CG  . LYS A 1 1126 ? 133.409 46.043  133.704 1.00 111.95 ? 1126 LYS A CG  1 
ATOM   8762  C  CD  . LYS A 1 1126 ? 133.863 45.716  135.120 1.00 117.02 ? 1126 LYS A CD  1 
ATOM   8763  C  CE  . LYS A 1 1126 ? 135.355 45.435  135.159 1.00 120.19 ? 1126 LYS A CE  1 
ATOM   8764  N  NZ  . LYS A 1 1126 ? 135.860 45.407  136.560 1.00 125.80 ? 1126 LYS A NZ  1 
ATOM   8765  N  N   . ILE A 1 1127 ? 129.607 46.390  131.197 1.00 100.30 ? 1127 ILE A N   1 
ATOM   8766  C  CA  . ILE A 1 1127 ? 128.191 46.185  130.958 1.00 98.70  ? 1127 ILE A CA  1 
ATOM   8767  C  C   . ILE A 1 1127 ? 127.882 44.691  130.994 1.00 100.89 ? 1127 ILE A C   1 
ATOM   8768  O  O   . ILE A 1 1127 ? 128.414 43.910  130.199 1.00 100.71 ? 1127 ILE A O   1 
ATOM   8769  C  CB  . ILE A 1 1127 ? 127.747 46.881  129.656 1.00 94.43  ? 1127 ILE A CB  1 
ATOM   8770  C  CG1 . ILE A 1 1127 ? 127.352 48.323  129.977 1.00 92.90  ? 1127 ILE A CG1 1 
ATOM   8771  C  CG2 . ILE A 1 1127 ? 126.585 46.154  129.013 1.00 92.31  ? 1127 ILE A CG2 1 
ATOM   8772  C  CD1 . ILE A 1 1127 ? 127.859 49.326  128.997 1.00 90.29  ? 1127 ILE A CD1 1 
ATOM   8773  N  N   . ASN A 1 1128 ? 127.038 44.308  131.950 1.00 103.52 ? 1128 ASN A N   1 
ATOM   8774  C  CA  . ASN A 1 1128 ? 126.768 42.899  132.227 1.00 106.98 ? 1128 ASN A CA  1 
ATOM   8775  C  C   . ASN A 1 1128 ? 125.287 42.523  132.277 1.00 106.97 ? 1128 ASN A C   1 
ATOM   8776  O  O   . ASN A 1 1128 ? 124.947 41.339  132.336 1.00 108.78 ? 1128 ASN A O   1 
ATOM   8777  C  CB  . ASN A 1 1128 ? 127.505 42.425  133.495 1.00 111.51 ? 1128 ASN A CB  1 
ATOM   8778  C  CG  . ASN A 1 1128 ? 127.353 43.383  134.676 1.00 112.80 ? 1128 ASN A CG  1 
ATOM   8779  O  OD1 . ASN A 1 1128 ? 128.348 43.824  135.256 1.00 114.24 ? 1128 ASN A OD1 1 
ATOM   8780  N  ND2 . ASN A 1 1128 ? 126.111 43.701  135.041 1.00 111.77 ? 1128 ASN A ND2 1 
ATOM   8781  N  N   . SER A 1 1129 ? 124.413 43.526  132.258 1.00 105.66 ? 1129 SER A N   1 
ATOM   8782  C  CA  . SER A 1 1129 ? 122.977 43.274  132.119 1.00 105.53 ? 1129 SER A CA  1 
ATOM   8783  C  C   . SER A 1 1129 ? 122.545 43.409  130.661 1.00 102.46 ? 1129 SER A C   1 
ATOM   8784  O  O   . SER A 1 1129 ? 123.237 44.030  129.858 1.00 100.23 ? 1129 SER A O   1 
ATOM   8785  C  CB  . SER A 1 1129 ? 122.140 44.180  133.036 1.00 105.59 ? 1129 SER A CB  1 
ATOM   8786  O  OG  . SER A 1 1129 ? 122.503 45.541  132.918 1.00 102.98 ? 1129 SER A OG  1 
ATOM   8787  N  N   . GLU A 1 1130 ? 121.425 42.777  130.325 1.00 103.03 ? 1130 GLU A N   1 
ATOM   8788  C  CA  . GLU A 1 1130 ? 120.782 42.953  129.029 1.00 100.67 ? 1130 GLU A CA  1 
ATOM   8789  C  C   . GLU A 1 1130 ? 119.724 44.043  129.181 1.00 99.21  ? 1130 GLU A C   1 
ATOM   8790  O  O   . GLU A 1 1130 ? 119.465 44.819  128.252 1.00 95.90  ? 1130 GLU A O   1 
ATOM   8791  C  CB  . GLU A 1 1130 ? 120.140 41.638  128.582 1.00 101.67 ? 1130 GLU A CB  1 
ATOM   8792  C  CG  . GLU A 1 1130 ? 119.171 41.773  127.405 1.00 99.46  ? 1130 GLU A CG  1 
ATOM   8793  C  CD  . GLU A 1 1130 ? 118.221 40.588  127.281 1.00 102.06 ? 1130 GLU A CD  1 
ATOM   8794  O  OE1 . GLU A 1 1130 ? 117.871 39.973  128.320 1.00 105.49 ? 1130 GLU A OE1 1 
ATOM   8795  O  OE2 . GLU A 1 1130 ? 117.824 40.275  126.137 1.00 100.11 ? 1130 GLU A OE2 1 
ATOM   8796  N  N   . GLN A 1 1131 ? 119.135 44.089  130.380 1.00 102.02 ? 1131 GLN A N   1 
ATOM   8797  C  CA  . GLN A 1 1131 ? 118.084 45.051  130.734 1.00 101.39 ? 1131 GLN A CA  1 
ATOM   8798  C  C   . GLN A 1 1131 ? 118.671 46.391  131.208 1.00 100.71 ? 1131 GLN A C   1 
ATOM   8799  O  O   . GLN A 1 1131 ? 118.048 47.142  131.973 1.00 101.19 ? 1131 GLN A O   1 
ATOM   8800  C  CB  . GLN A 1 1131 ? 117.116 44.447  131.770 1.00 104.58 ? 1131 GLN A CB  1 
ATOM   8801  C  CG  . GLN A 1 1131 ? 116.385 43.183  131.277 1.00 106.24 ? 1131 GLN A CG  1 
ATOM   8802  C  CD  . GLN A 1 1131 ? 114.992 43.021  131.875 1.00 108.67 ? 1131 GLN A CD  1 
ATOM   8803  O  OE1 . GLN A 1 1131 ? 114.836 42.591  133.022 1.00 111.55 ? 1131 GLN A OE1 1 
ATOM   8804  N  NE2 . GLN A 1 1131 ? 113.969 43.355  131.087 1.00 106.35 ? 1131 GLN A NE2 1 
ATOM   8805  N  N   . ILE A 1 1132 ? 119.893 46.658  130.753 1.00 99.69  ? 1132 ILE A N   1 
ATOM   8806  C  CA  . ILE A 1 1132 ? 120.481 47.985  130.791 1.00 98.12  ? 1132 ILE A CA  1 
ATOM   8807  C  C   . ILE A 1 1132 ? 119.728 48.789  129.769 1.00 93.99  ? 1132 ILE A C   1 
ATOM   8808  O  O   . ILE A 1 1132 ? 119.326 48.260  128.730 1.00 92.41  ? 1132 ILE A O   1 
ATOM   8809  C  CB  . ILE A 1 1132 ? 121.957 47.974  130.343 1.00 98.36  ? 1132 ILE A CB  1 
ATOM   8810  C  CG1 . ILE A 1 1132 ? 122.204 46.781  129.413 1.00 98.42  ? 1132 ILE A CG1 1 
ATOM   8811  C  CG2 . ILE A 1 1132 ? 122.901 47.981  131.554 1.00 102.10 ? 1132 ILE A CG2 1 
ATOM   8812  C  CD1 . ILE A 1 1132 ? 123.590 46.687  128.867 1.00 99.73  ? 1132 ILE A CD1 1 
ATOM   8813  N  N   . ASP A 1 1133 ? 119.532 50.063  130.072 1.00 92.41  ? 1133 ASP A N   1 
ATOM   8814  C  CA  . ASP A 1 1133 ? 118.946 50.997  129.135 1.00 88.32  ? 1133 ASP A CA  1 
ATOM   8815  C  C   . ASP A 1 1133 ? 119.044 52.397  129.717 1.00 87.87  ? 1133 ASP A C   1 
ATOM   8816  O  O   . ASP A 1 1133 ? 119.654 53.263  129.107 1.00 86.37  ? 1133 ASP A O   1 
ATOM   8817  C  CB  . ASP A 1 1133 ? 117.505 50.619  128.831 1.00 87.43  ? 1133 ASP A CB  1 
ATOM   8818  C  CG  . ASP A 1 1133 ? 117.184 50.718  127.373 1.00 84.43  ? 1133 ASP A CG  1 
ATOM   8819  O  OD1 . ASP A 1 1133 ? 117.141 51.860  126.864 1.00 83.34  ? 1133 ASP A OD1 1 
ATOM   8820  O  OD2 . ASP A 1 1133 ? 116.968 49.659  126.740 1.00 83.47  ? 1133 ASP A OD2 1 
ATOM   8821  N  N   . VAL A 1 1134 ? 118.473 52.611  130.903 1.00 89.15  ? 1134 VAL A N   1 
ATOM   8822  C  CA  . VAL A 1 1134 ? 118.626 53.884  131.607 1.00 89.32  ? 1134 VAL A CA  1 
ATOM   8823  C  C   . VAL A 1 1134 ? 120.009 53.917  132.245 1.00 91.17  ? 1134 VAL A C   1 
ATOM   8824  O  O   . VAL A 1 1134 ? 120.128 53.903  133.476 1.00 94.21  ? 1134 VAL A O   1 
ATOM   8825  C  CB  . VAL A 1 1134 ? 117.576 54.090  132.740 1.00 91.31  ? 1134 VAL A CB  1 
ATOM   8826  C  CG1 . VAL A 1 1134 ? 117.193 55.568  132.856 1.00 90.09  ? 1134 VAL A CG1 1 
ATOM   8827  C  CG2 . VAL A 1 1134 ? 116.344 53.216  132.541 1.00 91.35  ? 1134 VAL A CG2 1 
ATOM   8828  N  N   . GLU A 1 1135 ? 121.053 53.942  131.419 1.00 89.34  ? 1135 GLU A N   1 
ATOM   8829  C  CA  . GLU A 1 1135 ? 122.419 53.941  131.937 1.00 91.11  ? 1135 GLU A CA  1 
ATOM   8830  C  C   . GLU A 1 1135 ? 123.338 54.925  131.227 1.00 89.33  ? 1135 GLU A C   1 
ATOM   8831  O  O   . GLU A 1 1135 ? 123.476 54.897  130.005 1.00 86.95  ? 1135 GLU A O   1 
ATOM   8832  C  CB  . GLU A 1 1135 ? 123.020 52.525  131.944 1.00 92.61  ? 1135 GLU A CB  1 
ATOM   8833  C  CG  . GLU A 1 1135 ? 122.519 51.607  133.081 1.00 96.42  ? 1135 GLU A CG  1 
ATOM   8834  C  CD  . GLU A 1 1135 ? 123.090 51.951  134.485 1.00 102.26 ? 1135 GLU A CD  1 
ATOM   8835  O  OE1 . GLU A 1 1135 ? 122.933 53.106  134.957 1.00 102.55 ? 1135 GLU A OE1 1 
ATOM   8836  O  OE2 . GLU A 1 1135 ? 123.674 51.046  135.135 1.00 105.07 ? 1135 GLU A OE2 1 
ATOM   8837  N  N   . ASN A 1 1136 ? 123.948 55.803  132.017 1.00 90.71  ? 1136 ASN A N   1 
ATOM   8838  C  CA  . ASN A 1 1136 ? 124.965 56.728  131.537 1.00 90.01  ? 1136 ASN A CA  1 
ATOM   8839  C  C   . ASN A 1 1136 ? 126.345 56.095  131.637 1.00 91.76  ? 1136 ASN A C   1 
ATOM   8840  O  O   . ASN A 1 1136 ? 126.660 55.442  132.630 1.00 94.57  ? 1136 ASN A O   1 
ATOM   8841  C  CB  . ASN A 1 1136 ? 124.948 58.030  132.355 1.00 91.51  ? 1136 ASN A CB  1 
ATOM   8842  C  CG  . ASN A 1 1136 ? 123.781 58.946  132.001 1.00 89.14  ? 1136 ASN A CG  1 
ATOM   8843  O  OD1 . ASN A 1 1136 ? 123.416 59.088  130.836 1.00 87.45  ? 1136 ASN A OD1 1 
ATOM   8844  N  ND2 . ASN A 1 1136 ? 123.209 59.589  133.008 1.00 89.81  ? 1136 ASN A ND2 1 
ATOM   8845  N  N   . PHE A 1 1137 ? 127.151 56.268  130.592 1.00 90.23  ? 1137 PHE A N   1 
ATOM   8846  C  CA  . PHE A 1 1137 ? 128.580 55.966  130.645 1.00 92.01  ? 1137 PHE A CA  1 
ATOM   8847  C  C   . PHE A 1 1137 ? 129.359 57.026  129.879 1.00 91.12  ? 1137 PHE A C   1 
ATOM   8848  O  O   . PHE A 1 1137 ? 130.256 56.731  129.091 1.00 90.91  ? 1137 PHE A O   1 
ATOM   8849  C  CB  . PHE A 1 1137 ? 128.882 54.550  130.153 1.00 91.97  ? 1137 PHE A CB  1 
ATOM   8850  C  CG  . PHE A 1 1137 ? 128.448 53.484  131.108 1.00 94.17  ? 1137 PHE A CG  1 
ATOM   8851  C  CD1 . PHE A 1 1137 ? 127.360 52.673  130.813 1.00 93.02  ? 1137 PHE A CD1 1 
ATOM   8852  C  CD2 . PHE A 1 1137 ? 129.110 53.310  132.326 1.00 99.04  ? 1137 PHE A CD2 1 
ATOM   8853  C  CE1 . PHE A 1 1137 ? 126.941 51.682  131.704 1.00 96.24  ? 1137 PHE A CE1 1 
ATOM   8854  C  CE2 . PHE A 1 1137 ? 128.705 52.324  133.234 1.00 101.66 ? 1137 PHE A CE2 1 
ATOM   8855  C  CZ  . PHE A 1 1137 ? 127.617 51.505  132.923 1.00 100.49 ? 1137 PHE A CZ  1 
ATOM   8856  N  N   . VAL A 1 1138 ? 128.974 58.272  130.138 1.00 90.79  ? 1138 VAL A N   1 
ATOM   8857  C  CA  . VAL A 1 1138 ? 129.608 59.467  129.601 1.00 90.48  ? 1138 VAL A CA  1 
ATOM   8858  C  C   . VAL A 1 1138 ? 131.034 59.618  130.143 1.00 93.71  ? 1138 VAL A C   1 
ATOM   8859  O  O   . VAL A 1 1138 ? 131.348 59.112  131.224 1.00 96.33  ? 1138 VAL A O   1 
ATOM   8860  C  CB  . VAL A 1 1138 ? 128.713 60.721  129.918 1.00 89.93  ? 1138 VAL A CB  1 
ATOM   8861  C  CG1 . VAL A 1 1138 ? 129.412 61.754  130.840 1.00 93.02  ? 1138 VAL A CG1 1 
ATOM   8862  C  CG2 . VAL A 1 1138 ? 128.177 61.353  128.633 1.00 86.80  ? 1138 VAL A CG2 1 
ATOM   8863  N  N   . ASP A 1 1139 ? 131.890 60.290  129.371 1.00 93.62  ? 1139 ASP A N   1 
ATOM   8864  C  CA  . ASP A 1 1139 ? 133.251 60.647  129.798 1.00 96.85  ? 1139 ASP A CA  1 
ATOM   8865  C  C   . ASP A 1 1139 ? 133.807 61.792  128.947 1.00 96.12  ? 1139 ASP A C   1 
ATOM   8866  O  O   . ASP A 1 1139 ? 133.483 61.889  127.769 1.00 93.45  ? 1139 ASP A O   1 
ATOM   8867  C  CB  . ASP A 1 1139 ? 134.178 59.436  129.723 1.00 98.52  ? 1139 ASP A CB  1 
ATOM   8868  C  CG  . ASP A 1 1139 ? 135.474 59.658  130.463 1.00 103.82 ? 1139 ASP A CG  1 
ATOM   8869  O  OD1 . ASP A 1 1139 ? 135.621 59.124  131.583 1.00 107.94 ? 1139 ASP A OD1 1 
ATOM   8870  O  OD2 . ASP A 1 1139 ? 136.340 60.388  129.936 1.00 106.35 ? 1139 ASP A OD2 1 
ATOM   8871  N  N   . ILE A 1 1140 ? 134.653 62.638  129.537 1.00 98.70  ? 1140 ILE A N   1 
ATOM   8872  C  CA  . ILE A 1 1140 ? 135.139 63.848  128.866 1.00 98.54  ? 1140 ILE A CA  1 
ATOM   8873  C  C   . ILE A 1 1140 ? 136.635 63.787  128.525 1.00 100.93 ? 1140 ILE A C   1 
ATOM   8874  O  O   . ILE A 1 1140 ? 137.454 64.173  129.349 1.00 104.71 ? 1140 ILE A O   1 
ATOM   8875  C  CB  . ILE A 1 1140 ? 134.878 65.135  129.734 1.00 100.21 ? 1140 ILE A CB  1 
ATOM   8876  C  CG1 . ILE A 1 1140 ? 133.518 65.090  130.460 1.00 98.75  ? 1140 ILE A CG1 1 
ATOM   8877  C  CG2 . ILE A 1 1140 ? 135.056 66.414  128.902 1.00 99.85  ? 1140 ILE A CG2 1 
ATOM   8878  C  CD1 . ILE A 1 1140 ? 132.266 65.237  129.567 1.00 93.97  ? 1140 ILE A CD1 1 
ATOM   8879  N  N   . PRO A 1 1141 ? 137.007 63.273  127.329 1.00 99.33  ? 1141 PRO A N   1 
ATOM   8880  C  CA  . PRO A 1 1141 ? 138.375 63.477  126.862 1.00 101.73 ? 1141 PRO A CA  1 
ATOM   8881  C  C   . PRO A 1 1141 ? 138.710 64.950  126.731 1.00 103.36 ? 1141 PRO A C   1 
ATOM   8882  O  O   . PRO A 1 1141 ? 137.873 65.742  126.294 1.00 101.13 ? 1141 PRO A O   1 
ATOM   8883  C  CB  . PRO A 1 1141 ? 138.377 62.825  125.475 1.00 98.84  ? 1141 PRO A CB  1 
ATOM   8884  C  CG  . PRO A 1 1141 ? 137.349 61.796  125.562 1.00 96.20  ? 1141 PRO A CG  1 
ATOM   8885  C  CD  . PRO A 1 1141 ? 136.258 62.428  126.385 1.00 95.97  ? 1141 PRO A CD  1 
ATOM   8886  N  N   . GLU A 1 1142 ? 139.933 65.304  127.115 1.00 107.49 ? 1142 GLU A N   1 
ATOM   8887  C  CA  . GLU A 1 1142 ? 140.403 66.675  127.030 1.00 109.84 ? 1142 GLU A CA  1 
ATOM   8888  C  C   . GLU A 1 1142 ? 140.819 67.017  125.602 1.00 108.96 ? 1142 GLU A C   1 
ATOM   8889  O  O   . GLU A 1 1142 ? 140.434 66.333  124.650 1.00 106.15 ? 1142 GLU A O   1 
ATOM   8890  C  CB  . GLU A 1 1142 ? 141.565 66.892  128.005 1.00 114.91 ? 1142 GLU A CB  1 
ATOM   8891  C  CG  . GLU A 1 1142 ? 141.226 66.648  129.481 1.00 117.04 ? 1142 GLU A CG  1 
ATOM   8892  C  CD  . GLU A 1 1142 ? 140.235 67.660  130.058 1.00 117.02 ? 1142 GLU A CD  1 
ATOM   8893  O  OE1 . GLU A 1 1142 ? 140.649 68.457  130.935 1.00 119.95 ? 1142 GLU A OE1 1 
ATOM   8894  O  OE2 . GLU A 1 1142 ? 139.049 67.654  129.638 1.00 112.76 ? 1142 GLU A OE2 1 
ATOM   8895  N  N   . ASP A 1 1143 ? 141.596 68.083  125.455 1.00 111.84 ? 1143 ASP A N   1 
ATOM   8896  C  CA  . ASP A 1 1143 ? 142.140 68.468  124.160 1.00 111.86 ? 1143 ASP A CA  1 
ATOM   8897  C  C   . ASP A 1 1143 ? 143.302 67.534  123.806 1.00 113.43 ? 1143 ASP A C   1 
ATOM   8898  O  O   . ASP A 1 1143 ? 144.466 67.819  124.120 1.00 117.45 ? 1143 ASP A O   1 
ATOM   8899  C  CB  . ASP A 1 1143 ? 142.584 69.938  124.185 1.00 114.98 ? 1143 ASP A CB  1 
ATOM   8900  C  CG  . ASP A 1 1143 ? 141.479 70.883  124.669 1.00 114.12 ? 1143 ASP A CG  1 
ATOM   8901  O  OD1 . ASP A 1 1143 ? 140.399 70.932  124.032 1.00 109.97 ? 1143 ASP A OD1 1 
ATOM   8902  O  OD2 . ASP A 1 1143 ? 141.704 71.583  125.686 1.00 117.27 ? 1143 ASP A OD2 1 
ATOM   8903  N  N   . THR A 1 1144 ? 142.959 66.405  123.177 1.00 110.18 ? 1144 THR A N   1 
ATOM   8904  C  CA  . THR A 1 1144 ? 143.924 65.357  122.820 1.00 111.04 ? 1144 THR A CA  1 
ATOM   8905  C  C   . THR A 1 1144 ? 143.884 65.055  121.319 1.00 108.72 ? 1144 THR A C   1 
ATOM   8906  O  O   . THR A 1 1144 ? 142.989 65.521  120.608 1.00 105.94 ? 1144 THR A O   1 
ATOM   8907  C  CB  . THR A 1 1144 ? 143.704 64.032  123.626 1.00 110.45 ? 1144 THR A CB  1 
ATOM   8908  O  OG1 . THR A 1 1144 ? 142.919 63.109  122.864 1.00 106.04 ? 1144 THR A OG1 1 
ATOM   8909  C  CG2 . THR A 1 1144 ? 143.037 64.281  124.977 1.00 110.56 ? 1144 THR A CG2 1 
ATOM   8910  N  N   . LYS A 1 1145 ? 144.844 64.259  120.850 1.00 110.04 ? 1145 LYS A N   1 
ATOM   8911  C  CA  . LYS A 1 1145 ? 144.983 63.944  119.423 1.00 108.34 ? 1145 LYS A CA  1 
ATOM   8912  C  C   . LYS A 1 1145 ? 144.353 62.609  119.001 1.00 104.80 ? 1145 LYS A C   1 
ATOM   8913  O  O   . LYS A 1 1145 ? 143.709 62.520  117.953 1.00 101.67 ? 1145 LYS A O   1 
ATOM   8914  C  CB  . LYS A 1 1145 ? 146.463 63.967  119.015 1.00 112.42 ? 1145 LYS A CB  1 
ATOM   8915  C  CG  . LYS A 1 1145 ? 147.044 65.355  118.787 1.00 115.29 ? 1145 LYS A CG  1 
ATOM   8916  C  CD  . LYS A 1 1145 ? 148.445 65.264  118.193 1.00 119.42 ? 1145 LYS A CD  1 
ATOM   8917  C  CE  . LYS A 1 1145 ? 149.086 66.638  118.074 1.00 123.00 ? 1145 LYS A CE  1 
ATOM   8918  N  NZ  . LYS A 1 1145 ? 150.555 66.549  117.849 1.00 127.48 ? 1145 LYS A NZ  1 
ATOM   8919  N  N   . LYS A 1 1146 ? 144.563 61.574  119.809 1.00 105.36 ? 1146 LYS A N   1 
ATOM   8920  C  CA  . LYS A 1 1146 ? 144.132 60.219  119.471 1.00 102.77 ? 1146 LYS A CA  1 
ATOM   8921  C  C   . LYS A 1 1146 ? 143.303 59.590  120.579 1.00 100.96 ? 1146 LYS A C   1 
ATOM   8922  O  O   . LYS A 1 1146 ? 143.208 60.130  121.682 1.00 102.25 ? 1146 LYS A O   1 
ATOM   8923  C  CB  . LYS A 1 1146 ? 145.347 59.332  119.166 1.00 105.80 ? 1146 LYS A CB  1 
ATOM   8924  C  CG  . LYS A 1 1146 ? 145.582 59.057  117.683 1.00 105.52 ? 1146 LYS A CG  1 
ATOM   8925  C  CD  . LYS A 1 1146 ? 146.853 58.230  117.478 1.00 110.08 ? 1146 LYS A CD  1 
ATOM   8926  C  CE  . LYS A 1 1146 ? 147.031 57.816  116.017 1.00 109.75 ? 1146 LYS A CE  1 
ATOM   8927  N  NZ  . LYS A 1 1146 ? 148.409 57.301  115.754 1.00 113.20 ? 1146 LYS A NZ  1 
ATOM   8928  N  N   . LEU A 1 1147 ? 142.720 58.435  120.277 1.00 98.00  ? 1147 LEU A N   1 
ATOM   8929  C  CA  . LEU A 1 1147 ? 141.861 57.727  121.211 1.00 96.24  ? 1147 LEU A CA  1 
ATOM   8930  C  C   . LEU A 1 1147 ? 141.852 56.226  120.897 1.00 95.32  ? 1147 LEU A C   1 
ATOM   8931  O  O   . LEU A 1 1147 ? 141.821 55.829  119.729 1.00 93.69  ? 1147 LEU A O   1 
ATOM   8932  C  CB  . LEU A 1 1147 ? 140.451 58.317  121.139 1.00 92.82  ? 1147 LEU A CB  1 
ATOM   8933  C  CG  . LEU A 1 1147 ? 139.361 57.928  122.133 1.00 91.35  ? 1147 LEU A CG  1 
ATOM   8934  C  CD1 . LEU A 1 1147 ? 138.399 59.084  122.315 1.00 89.25  ? 1147 LEU A CD1 1 
ATOM   8935  C  CD2 . LEU A 1 1147 ? 138.630 56.713  121.624 1.00 89.10  ? 1147 LEU A CD2 1 
ATOM   8936  N  N   . GLU A 1 1148 ? 141.883 55.404  121.947 1.00 96.27  ? 1148 GLU A N   1 
ATOM   8937  C  CA  . GLU A 1 1148 ? 141.907 53.944  121.803 1.00 95.69  ? 1148 GLU A CA  1 
ATOM   8938  C  C   . GLU A 1 1148 ? 140.847 53.251  122.660 1.00 93.85  ? 1148 GLU A C   1 
ATOM   8939  O  O   . GLU A 1 1148 ? 140.830 53.405  123.886 1.00 95.41  ? 1148 GLU A O   1 
ATOM   8940  C  CB  . GLU A 1 1148 ? 143.298 53.397  122.139 1.00 99.93  ? 1148 GLU A CB  1 
ATOM   8941  C  CG  . GLU A 1 1148 ? 143.395 51.880  122.069 1.00 101.19 ? 1148 GLU A CG  1 
ATOM   8942  C  CD  . GLU A 1 1148 ? 144.812 51.366  122.220 1.00 106.46 ? 1148 GLU A CD  1 
ATOM   8943  O  OE1 . GLU A 1 1148 ? 145.519 51.796  123.159 1.00 110.35 ? 1148 GLU A OE1 1 
ATOM   8944  O  OE2 . GLU A 1 1148 ? 145.217 50.517  121.397 1.00 107.42 ? 1148 GLU A OE2 1 
ATOM   8945  N  N   . ILE A 1 1149 ? 139.974 52.486  122.004 1.00 90.35  ? 1149 ILE A N   1 
ATOM   8946  C  CA  . ILE A 1 1149 ? 138.902 51.760  122.685 1.00 88.58  ? 1149 ILE A CA  1 
ATOM   8947  C  C   . ILE A 1 1149 ? 139.057 50.258  122.509 1.00 89.15  ? 1149 ILE A C   1 
ATOM   8948  O  O   . ILE A 1 1149 ? 138.932 49.739  121.400 1.00 87.53  ? 1149 ILE A O   1 
ATOM   8949  C  CB  . ILE A 1 1149 ? 137.499 52.176  122.179 1.00 84.49  ? 1149 ILE A CB  1 
ATOM   8950  C  CG1 . ILE A 1 1149 ? 137.205 53.625  122.540 1.00 83.68  ? 1149 ILE A CG1 1 
ATOM   8951  C  CG2 . ILE A 1 1149 ? 136.416 51.284  122.782 1.00 83.48  ? 1149 ILE A CG2 1 
ATOM   8952  C  CD1 . ILE A 1 1149 ? 136.083 54.236  121.730 1.00 80.67  ? 1149 ILE A CD1 1 
ATOM   8953  N  N   . ASN A 1 1150 ? 139.318 49.565  123.611 1.00 91.51  ? 1150 ASN A N   1 
ATOM   8954  C  CA  . ASN A 1 1150 ? 139.393 48.109  123.591 1.00 92.34  ? 1150 ASN A CA  1 
ATOM   8955  C  C   . ASN A 1 1150 ? 138.142 47.483  124.187 1.00 90.89  ? 1150 ASN A C   1 
ATOM   8956  O  O   . ASN A 1 1150 ? 137.842 47.666  125.376 1.00 92.08  ? 1150 ASN A O   1 
ATOM   8957  C  CB  . ASN A 1 1150 ? 140.635 47.607  124.324 1.00 96.73  ? 1150 ASN A CB  1 
ATOM   8958  C  CG  . ASN A 1 1150 ? 141.897 48.327  123.897 1.00 98.63  ? 1150 ASN A CG  1 
ATOM   8959  O  OD1 . ASN A 1 1150 ? 142.118 48.579  122.713 1.00 96.72  ? 1150 ASN A OD1 1 
ATOM   8960  N  ND2 . ASN A 1 1150 ? 142.738 48.663  124.869 1.00 102.79 ? 1150 ASN A ND2 1 
ATOM   8961  N  N   . VAL A 1 1151 ? 137.410 46.759  123.345 1.00 88.23  ? 1151 VAL A N   1 
ATOM   8962  C  CA  . VAL A 1 1151 ? 136.220 46.037  123.774 1.00 86.69  ? 1151 VAL A CA  1 
ATOM   8963  C  C   . VAL A 1 1151 ? 136.549 44.555  123.888 1.00 88.64  ? 1151 VAL A C   1 
ATOM   8964  O  O   . VAL A 1 1151 ? 137.274 44.005  123.063 1.00 89.17  ? 1151 VAL A O   1 
ATOM   8965  C  CB  . VAL A 1 1151 ? 135.037 46.243  122.806 1.00 82.75  ? 1151 VAL A CB  1 
ATOM   8966  C  CG1 . VAL A 1 1151 ? 133.764 45.629  123.373 1.00 81.87  ? 1151 VAL A CG1 1 
ATOM   8967  C  CG2 . VAL A 1 1151 ? 134.822 47.730  122.528 1.00 80.73  ? 1151 VAL A CG2 1 
ATOM   8968  N  N   . GLY A 1 1152 ? 136.020 43.928  124.930 1.00 89.73  ? 1152 GLY A N   1 
ATOM   8969  C  CA  . GLY A 1 1152 ? 136.187 42.504  125.146 1.00 91.69  ? 1152 GLY A CA  1 
ATOM   8970  C  C   . GLY A 1 1152 ? 135.000 41.910  125.873 1.00 91.37  ? 1152 GLY A C   1 
ATOM   8971  O  O   . GLY A 1 1152 ? 134.575 42.421  126.914 1.00 91.72  ? 1152 GLY A O   1 
ATOM   8972  N  N   . GLY A 1 1153 ? 134.461 40.830  125.312 1.00 90.75  ? 1153 GLY A N   1 
ATOM   8973  C  CA  . GLY A 1 1153 ? 133.377 40.098  125.949 1.00 91.09  ? 1153 GLY A CA  1 
ATOM   8974  C  C   . GLY A 1 1153 ? 132.324 39.654  124.956 1.00 88.30  ? 1153 GLY A C   1 
ATOM   8975  O  O   . GLY A 1 1153 ? 132.642 39.113  123.892 1.00 87.75  ? 1153 GLY A O   1 
ATOM   8976  N  N   . ILE A 1 1154 ? 131.067 39.909  125.310 1.00 86.54  ? 1154 ILE A N   1 
ATOM   8977  C  CA  . ILE A 1 1154 ? 129.912 39.444  124.553 1.00 84.17  ? 1154 ILE A CA  1 
ATOM   8978  C  C   . ILE A 1 1154 ? 128.778 40.468  124.618 1.00 80.86  ? 1154 ILE A C   1 
ATOM   8979  O  O   . ILE A 1 1154 ? 128.481 41.007  125.682 1.00 81.48  ? 1154 ILE A O   1 
ATOM   8980  C  CB  . ILE A 1 1154 ? 129.465 38.037  125.061 1.00 87.14  ? 1154 ILE A CB  1 
ATOM   8981  C  CG1 . ILE A 1 1154 ? 129.983 36.959  124.106 1.00 88.44  ? 1154 ILE A CG1 1 
ATOM   8982  C  CG2 . ILE A 1 1154 ? 127.942 37.929  125.223 1.00 86.04  ? 1154 ILE A CG2 1 
ATOM   8983  C  CD1 . ILE A 1 1154 ? 129.996 35.564  124.692 1.00 93.48  ? 1154 ILE A CD1 1 
ATOM   8984  N  N   . GLY A 1 1155 ? 128.165 40.754  123.472 1.00 77.37  ? 1155 GLY A N   1 
ATOM   8985  C  CA  . GLY A 1 1155 ? 126.996 41.623  123.445 1.00 74.15  ? 1155 GLY A CA  1 
ATOM   8986  C  C   . GLY A 1 1155 ? 127.024 42.741  122.424 1.00 70.54  ? 1155 GLY A C   1 
ATOM   8987  O  O   . GLY A 1 1155 ? 127.792 42.703  121.464 1.00 70.15  ? 1155 GLY A O   1 
ATOM   8988  N  N   . PHE A 1 1156 ? 126.175 43.738  122.655 1.00 68.08  ? 1156 PHE A N   1 
ATOM   8989  C  CA  . PHE A 1 1156 ? 125.949 44.834  121.731 1.00 64.43  ? 1156 PHE A CA  1 
ATOM   8990  C  C   . PHE A 1 1156 ? 126.228 46.187  122.389 1.00 64.13  ? 1156 PHE A C   1 
ATOM   8991  O  O   . PHE A 1 1156 ? 125.859 46.426  123.546 1.00 65.56  ? 1156 PHE A O   1 
ATOM   8992  C  CB  . PHE A 1 1156 ? 124.501 44.787  121.254 1.00 62.25  ? 1156 PHE A CB  1 
ATOM   8993  C  CG  . PHE A 1 1156 ? 124.124 45.915  120.346 1.00 58.87  ? 1156 PHE A CG  1 
ATOM   8994  C  CD1 . PHE A 1 1156 ? 124.198 45.767  118.969 1.00 56.79  ? 1156 PHE A CD1 1 
ATOM   8995  C  CD2 . PHE A 1 1156 ? 123.687 47.124  120.865 1.00 57.91  ? 1156 PHE A CD2 1 
ATOM   8996  C  CE1 . PHE A 1 1156 ? 123.851 46.809  118.118 1.00 53.81  ? 1156 PHE A CE1 1 
ATOM   8997  C  CE2 . PHE A 1 1156 ? 123.339 48.176  120.022 1.00 55.84  ? 1156 PHE A CE2 1 
ATOM   8998  C  CZ  . PHE A 1 1156 ? 123.418 48.014  118.643 1.00 53.48  ? 1156 PHE A CZ  1 
ATOM   8999  N  N   . GLY A 1 1157 ? 126.862 47.083  121.642 1.00 62.34  ? 1157 GLY A N   1 
ATOM   9000  C  CA  . GLY A 1 1157 ? 127.181 48.402  122.165 1.00 61.38  ? 1157 GLY A CA  1 
ATOM   9001  C  C   . GLY A 1 1157 ? 127.478 49.447  121.115 1.00 58.79  ? 1157 GLY A C   1 
ATOM   9002  O  O   . GLY A 1 1157 ? 127.841 49.132  119.981 1.00 57.87  ? 1157 GLY A O   1 
ATOM   9003  N  N   . LEU A 1 1158 ? 127.318 50.702  121.516 1.00 57.74  ? 1158 LEU A N   1 
ATOM   9004  C  CA  . LEU A 1 1158 ? 127.597 51.843  120.674 1.00 55.58  ? 1158 LEU A CA  1 
ATOM   9005  C  C   . LEU A 1 1158 ? 128.727 52.634  121.297 1.00 57.47  ? 1158 LEU A C   1 
ATOM   9006  O  O   . LEU A 1 1158 ? 128.702 52.948  122.488 1.00 58.81  ? 1158 LEU A O   1 
ATOM   9007  C  CB  . LEU A 1 1158 ? 126.362 52.717  120.552 1.00 53.21  ? 1158 LEU A CB  1 
ATOM   9008  C  CG  . LEU A 1 1158 ? 125.143 52.086  119.893 1.00 51.27  ? 1158 LEU A CG  1 
ATOM   9009  C  CD1 . LEU A 1 1158 ? 123.894 52.774  120.392 1.00 50.33  ? 1158 LEU A CD1 1 
ATOM   9010  C  CD2 . LEU A 1 1158 ? 125.234 52.177  118.373 1.00 49.95  ? 1158 LEU A CD2 1 
ATOM   9011  N  N   . LEU A 1 1159 ? 129.732 52.928  120.484 1.00 57.71  ? 1159 LEU A N   1 
ATOM   9012  C  CA  . LEU A 1 1159 ? 130.889 53.686  120.924 1.00 59.66  ? 1159 LEU A CA  1 
ATOM   9013  C  C   . LEU A 1 1159 ? 130.824 55.030  120.231 1.00 58.23  ? 1159 LEU A C   1 
ATOM   9014  O  O   . LEU A 1 1159 ? 131.022 55.121  119.016 1.00 57.09  ? 1159 LEU A O   1 
ATOM   9015  C  CB  . LEU A 1 1159 ? 132.178 52.942  120.567 1.00 61.54  ? 1159 LEU A CB  1 
ATOM   9016  C  CG  . LEU A 1 1159 ? 132.354 51.547  121.176 1.00 63.19  ? 1159 LEU A CG  1 
ATOM   9017  C  CD1 . LEU A 1 1159 ? 133.495 50.823  120.498 1.00 64.57  ? 1159 LEU A CD1 1 
ATOM   9018  C  CD2 . LEU A 1 1159 ? 132.574 51.607  122.693 1.00 65.40  ? 1159 LEU A CD2 1 
ATOM   9019  N  N   . GLU A 1 1160 ? 130.519 56.068  121.001 1.00 58.47  ? 1160 GLU A N   1 
ATOM   9020  C  CA  . GLU A 1 1160 ? 130.221 57.372  120.419 1.00 57.02  ? 1160 GLU A CA  1 
ATOM   9021  C  C   . GLU A 1 1160 ? 131.229 58.408  120.860 1.00 59.21  ? 1160 GLU A C   1 
ATOM   9022  O  O   . GLU A 1 1160 ? 131.665 58.404  122.007 1.00 61.21  ? 1160 GLU A O   1 
ATOM   9023  C  CB  . GLU A 1 1160 ? 128.809 57.830  120.799 1.00 55.28  ? 1160 GLU A CB  1 
ATOM   9024  C  CG  . GLU A 1 1160 ? 127.744 56.763  120.653 1.00 52.86  ? 1160 GLU A CG  1 
ATOM   9025  C  CD  . GLU A 1 1160 ? 126.409 57.154  121.261 1.00 51.68  ? 1160 GLU A CD  1 
ATOM   9026  O  OE1 . GLU A 1 1160 ? 126.371 57.984  122.194 1.00 50.96  ? 1160 GLU A OE1 1 
ATOM   9027  O  OE2 . GLU A 1 1160 ? 125.385 56.615  120.794 1.00 51.27  ? 1160 GLU A OE2 1 
ATOM   9028  N  N   . VAL A 1 1161 ? 131.600 59.277  119.926 1.00 59.04  ? 1161 VAL A N   1 
ATOM   9029  C  CA  . VAL A 1 1161 ? 132.396 60.457  120.221 1.00 61.79  ? 1161 VAL A CA  1 
ATOM   9030  C  C   . VAL A 1 1161 ? 131.569 61.675  119.834 1.00 61.12  ? 1161 VAL A C   1 
ATOM   9031  O  O   . VAL A 1 1161 ? 131.032 61.734  118.730 1.00 59.19  ? 1161 VAL A O   1 
ATOM   9032  C  CB  . VAL A 1 1161 ? 133.753 60.459  119.467 1.00 63.14  ? 1161 VAL A CB  1 
ATOM   9033  C  CG1 . VAL A 1 1161 ? 134.504 61.744  119.718 1.00 64.51  ? 1161 VAL A CG1 1 
ATOM   9034  C  CG2 . VAL A 1 1161 ? 134.601 59.282  119.894 1.00 64.44  ? 1161 VAL A CG2 1 
ATOM   9035  N  N   . VAL A 1 1162 ? 131.454 62.634  120.748 1.00 63.53  ? 1162 VAL A N   1 
ATOM   9036  C  CA  . VAL A 1 1162 ? 130.671 63.839  120.500 1.00 63.62  ? 1162 VAL A CA  1 
ATOM   9037  C  C   . VAL A 1 1162 ? 131.575 65.067  120.467 1.00 67.06  ? 1162 VAL A C   1 
ATOM   9038  O  O   . VAL A 1 1162 ? 132.311 65.332  121.412 1.00 69.40  ? 1162 VAL A O   1 
ATOM   9039  C  CB  . VAL A 1 1162 ? 129.555 64.038  121.556 1.00 62.93  ? 1162 VAL A CB  1 
ATOM   9040  C  CG1 . VAL A 1 1162 ? 128.679 65.207  121.179 1.00 61.28  ? 1162 VAL A CG1 1 
ATOM   9041  C  CG2 . VAL A 1 1162 ? 128.714 62.787  121.699 1.00 61.07  ? 1162 VAL A CG2 1 
ATOM   9042  N  N   . TYR A 1 1163 ? 131.501 65.810  119.368 1.00 68.01  ? 1163 TYR A N   1 
ATOM   9043  C  CA  . TYR A 1 1163 ? 132.274 67.032  119.195 1.00 72.14  ? 1163 TYR A CA  1 
ATOM   9044  C  C   . TYR A 1 1163 ? 131.375 68.254  119.337 1.00 73.17  ? 1163 TYR A C   1 
ATOM   9045  O  O   . TYR A 1 1163 ? 130.287 68.292  118.774 1.00 70.72  ? 1163 TYR A O   1 
ATOM   9046  C  CB  . TYR A 1 1163 ? 132.929 67.050  117.815 1.00 71.93  ? 1163 TYR A CB  1 
ATOM   9047  C  CG  . TYR A 1 1163 ? 133.823 65.870  117.516 1.00 72.11  ? 1163 TYR A CG  1 
ATOM   9048  C  CD1 . TYR A 1 1163 ? 133.301 64.699  116.977 1.00 69.41  ? 1163 TYR A CD1 1 
ATOM   9049  C  CD2 . TYR A 1 1163 ? 135.196 65.933  117.754 1.00 74.96  ? 1163 TYR A CD2 1 
ATOM   9050  C  CE1 . TYR A 1 1163 ? 134.117 63.615  116.692 1.00 70.37  ? 1163 TYR A CE1 1 
ATOM   9051  C  CE2 . TYR A 1 1163 ? 136.023 64.853  117.475 1.00 75.67  ? 1163 TYR A CE2 1 
ATOM   9052  C  CZ  . TYR A 1 1163 ? 135.476 63.696  116.942 1.00 73.95  ? 1163 TYR A CZ  1 
ATOM   9053  O  OH  . TYR A 1 1163 ? 136.285 62.615  116.656 1.00 75.55  ? 1163 TYR A OH  1 
ATOM   9054  N  N   . GLN A 1 1164 ? 131.834 69.250  120.086 1.00 63.43  ? 1164 GLN A N   1 
ATOM   9055  C  CA  . GLN A 1 1164 ? 131.099 70.500  120.241 1.00 64.89  ? 1164 GLN A CA  1 
ATOM   9056  C  C   . GLN A 1 1164 ? 131.923 71.664  119.688 1.00 66.26  ? 1164 GLN A C   1 
ATOM   9057  O  O   . GLN A 1 1164 ? 132.493 72.451  120.451 1.00 66.84  ? 1164 GLN A O   1 
ATOM   9058  C  CB  . GLN A 1 1164 ? 130.751 70.742  121.716 1.00 64.80  ? 1164 GLN A CB  1 
ATOM   9059  C  CG  . GLN A 1 1164 ? 129.691 69.804  122.301 1.00 66.73  ? 1164 GLN A CG  1 
ATOM   9060  C  CD  . GLN A 1 1164 ? 128.261 70.221  121.955 1.00 68.55  ? 1164 GLN A CD  1 
ATOM   9061  O  OE1 . GLN A 1 1164 ? 127.962 71.414  121.811 1.00 69.49  ? 1164 GLN A OE1 1 
ATOM   9062  N  NE2 . GLN A 1 1164 ? 127.370 69.235  121.822 1.00 68.47  ? 1164 GLN A NE2 1 
ATOM   9063  N  N   . PHE A 1 1165 ? 131.982 71.772  118.361 1.00 67.77  ? 1165 PHE A N   1 
ATOM   9064  C  CA  . PHE A 1 1165 ? 132.807 72.785  117.694 1.00 69.31  ? 1165 PHE A CA  1 
ATOM   9065  C  C   . PHE A 1 1165 ? 132.386 74.200  118.068 1.00 69.48  ? 1165 PHE A C   1 
ATOM   9066  O  O   . PHE A 1 1165 ? 131.219 74.440  118.355 1.00 68.76  ? 1165 PHE A O   1 
ATOM   9067  C  CB  . PHE A 1 1165 ? 132.754 72.623  116.173 1.00 69.45  ? 1165 PHE A CB  1 
ATOM   9068  C  CG  . PHE A 1 1165 ? 133.130 71.250  115.692 1.00 70.90  ? 1165 PHE A CG  1 
ATOM   9069  C  CD1 . PHE A 1 1165 ? 134.403 70.731  115.935 1.00 72.45  ? 1165 PHE A CD1 1 
ATOM   9070  C  CD2 . PHE A 1 1165 ? 132.217 70.476  114.985 1.00 71.14  ? 1165 PHE A CD2 1 
ATOM   9071  C  CE1 . PHE A 1 1165 ? 134.756 69.452  115.489 1.00 73.23  ? 1165 PHE A CE1 1 
ATOM   9072  C  CE2 . PHE A 1 1165 ? 132.563 69.195  114.530 1.00 72.56  ? 1165 PHE A CE2 1 
ATOM   9073  C  CZ  . PHE A 1 1165 ? 133.838 68.684  114.783 1.00 73.08  ? 1165 PHE A CZ  1 
ATOM   9074  N  N   . ASN A 1 1166 ? 133.350 75.122  118.078 1.00 71.01  ? 1166 ASN A N   1 
ATOM   9075  C  CA  . ASN A 1 1166 ? 133.081 76.539  118.350 1.00 71.49  ? 1166 ASN A CA  1 
ATOM   9076  C  C   . ASN A 1 1166 ? 133.601 77.444  117.235 1.00 71.81  ? 1166 ASN A C   1 
ATOM   9077  O  O   . ASN A 1 1166 ? 134.370 78.391  117.479 1.00 72.32  ? 1166 ASN A O   1 
ATOM   9078  C  CB  . ASN A 1 1166 ? 133.653 76.954  119.703 1.00 72.03  ? 1166 ASN A CB  1 
ATOM   9079  C  CG  . ASN A 1 1166 ? 132.896 76.343  120.854 1.00 73.59  ? 1166 ASN A CG  1 
ATOM   9080  O  OD1 . ASN A 1 1166 ? 131.858 76.865  121.282 1.00 74.52  ? 1166 ASN A OD1 1 
ATOM   9081  N  ND2 . ASN A 1 1166 ? 133.403 75.219  121.365 1.00 75.60  ? 1166 ASN A ND2 1 
ATOM   9082  N  N   . LEU A 1 1167 ? 133.157 77.142  116.014 1.00 71.39  ? 1167 LEU A N   1 
ATOM   9083  C  CA  . LEU A 1 1167 ? 133.546 77.886  114.821 1.00 71.18  ? 1167 LEU A CA  1 
ATOM   9084  C  C   . LEU A 1 1167 ? 133.150 79.367  114.922 1.00 70.12  ? 1167 LEU A C   1 
ATOM   9085  O  O   . LEU A 1 1167 ? 132.166 79.726  115.583 1.00 69.50  ? 1167 LEU A O   1 
ATOM   9086  C  CB  . LEU A 1 1167 ? 132.931 77.256  113.565 1.00 71.33  ? 1167 LEU A CB  1 
ATOM   9087  C  CG  . LEU A 1 1167 ? 132.479 75.789  113.601 1.00 71.97  ? 1167 LEU A CG  1 
ATOM   9088  C  CD1 . LEU A 1 1167 ? 130.991 75.687  113.995 1.00 72.18  ? 1167 LEU A CD1 1 
ATOM   9089  C  CD2 . LEU A 1 1167 ? 132.720 75.111  112.259 1.00 72.57  ? 1167 LEU A CD2 1 
ATOM   9090  N  N   . ASN A 1 1168 ? 133.952 80.212  114.276 1.00 69.68  ? 1168 ASN A N   1 
ATOM   9091  C  CA  . ASN A 1 1168 ? 133.721 81.652  114.173 1.00 68.16  ? 1168 ASN A CA  1 
ATOM   9092  C  C   . ASN A 1 1168 ? 132.359 81.922  113.544 1.00 65.78  ? 1168 ASN A C   1 
ATOM   9093  O  O   . ASN A 1 1168 ? 131.877 81.121  112.737 1.00 65.71  ? 1168 ASN A O   1 
ATOM   9094  C  CB  . ASN A 1 1168 ? 134.831 82.269  113.299 1.00 69.68  ? 1168 ASN A CB  1 
ATOM   9095  C  CG  . ASN A 1 1168 ? 135.043 83.771  113.550 1.00 71.09  ? 1168 ASN A CG  1 
ATOM   9096  O  OD1 . ASN A 1 1168 ? 134.258 84.431  114.249 1.00 72.86  ? 1168 ASN A OD1 1 
ATOM   9097  N  ND2 . ASN A 1 1168 ? 136.119 84.312  112.973 1.00 71.88  ? 1168 ASN A ND2 1 
ATOM   9098  N  N   . LEU A 1 1169 ? 131.734 83.036  113.915 1.00 63.06  ? 1169 LEU A N   1 
ATOM   9099  C  CA  . LEU A 1 1169 ? 130.466 83.421  113.313 1.00 60.08  ? 1169 LEU A CA  1 
ATOM   9100  C  C   . LEU A 1 1169 ? 130.724 84.251  112.066 1.00 58.88  ? 1169 LEU A C   1 
ATOM   9101  O  O   . LEU A 1 1169 ? 131.191 85.389  112.144 1.00 59.07  ? 1169 LEU A O   1 
ATOM   9102  C  CB  . LEU A 1 1169 ? 129.612 84.191  114.313 1.00 59.61  ? 1169 LEU A CB  1 
ATOM   9103  C  CG  . LEU A 1 1169 ? 128.193 84.590  113.906 1.00 58.62  ? 1169 LEU A CG  1 
ATOM   9104  C  CD1 . LEU A 1 1169 ? 127.327 83.375  113.573 1.00 57.39  ? 1169 LEU A CD1 1 
ATOM   9105  C  CD2 . LEU A 1 1169 ? 127.588 85.387  115.034 1.00 58.21  ? 1169 LEU A CD2 1 
ATOM   9106  N  N   . VAL A 1 1170 ? 130.409 83.674  110.916 1.00 56.96  ? 1170 VAL A N   1 
ATOM   9107  C  CA  . VAL A 1 1170 ? 130.831 84.221  109.630 1.00 55.65  ? 1170 VAL A CA  1 
ATOM   9108  C  C   . VAL A 1 1170 ? 129.699 84.123  108.614 1.00 53.81  ? 1170 VAL A C   1 
ATOM   9109  O  O   . VAL A 1 1170 ? 128.904 83.182  108.659 1.00 53.51  ? 1170 VAL A O   1 
ATOM   9110  C  CB  . VAL A 1 1170 ? 132.093 83.453  109.110 1.00 56.63  ? 1170 VAL A CB  1 
ATOM   9111  C  CG1 . VAL A 1 1170 ? 132.351 83.707  107.645 1.00 56.90  ? 1170 VAL A CG1 1 
ATOM   9112  C  CG2 . VAL A 1 1170 ? 133.318 83.827  109.924 1.00 57.16  ? 1170 VAL A CG2 1 
ATOM   9113  N  N   . ASN A 1 1171 ? 129.631 85.103  107.713 1.00 52.08  ? 1171 ASN A N   1 
ATOM   9114  C  CA  . ASN A 1 1171 ? 128.735 85.057  106.562 1.00 50.32  ? 1171 ASN A CA  1 
ATOM   9115  C  C   . ASN A 1 1171 ? 129.022 83.872  105.653 1.00 50.30  ? 1171 ASN A C   1 
ATOM   9116  O  O   . ASN A 1 1171 ? 130.175 83.539  105.379 1.00 51.33  ? 1171 ASN A O   1 
ATOM   9117  C  CB  . ASN A 1 1171 ? 128.855 86.329  105.737 1.00 50.22  ? 1171 ASN A CB  1 
ATOM   9118  C  CG  . ASN A 1 1171 ? 128.116 87.490  106.340 1.00 49.28  ? 1171 ASN A CG  1 
ATOM   9119  O  OD1 . ASN A 1 1171 ? 127.522 87.388  107.417 1.00 48.58  ? 1171 ASN A OD1 1 
ATOM   9120  N  ND2 . ASN A 1 1171 ? 128.132 88.612  105.638 1.00 48.23  ? 1171 ASN A ND2 1 
ATOM   9121  N  N   . PHE A 1 1172 ? 127.963 83.254  105.161 1.00 48.81  ? 1172 PHE A N   1 
ATOM   9122  C  CA  . PHE A 1 1172 ? 128.084 82.095  104.310 1.00 48.18  ? 1172 PHE A CA  1 
ATOM   9123  C  C   . PHE A 1 1172 ? 126.815 81.999  103.483 1.00 47.34  ? 1172 PHE A C   1 
ATOM   9124  O  O   . PHE A 1 1172 ? 125.755 82.429  103.924 1.00 46.91  ? 1172 PHE A O   1 
ATOM   9125  C  CB  . PHE A 1 1172 ? 128.250 80.853  105.191 1.00 48.04  ? 1172 PHE A CB  1 
ATOM   9126  C  CG  . PHE A 1 1172 ? 128.217 79.557  104.445 1.00 47.82  ? 1172 PHE A CG  1 
ATOM   9127  C  CD1 . PHE A 1 1172 ? 129.362 79.065  103.827 1.00 48.31  ? 1172 PHE A CD1 1 
ATOM   9128  C  CD2 . PHE A 1 1172 ? 127.044 78.817  104.369 1.00 47.06  ? 1172 PHE A CD2 1 
ATOM   9129  C  CE1 . PHE A 1 1172 ? 129.339 77.847  103.136 1.00 48.09  ? 1172 PHE A CE1 1 
ATOM   9130  C  CE2 . PHE A 1 1172 ? 127.007 77.602  103.673 1.00 46.98  ? 1172 PHE A CE2 1 
ATOM   9131  C  CZ  . PHE A 1 1172 ? 128.158 77.116  103.062 1.00 47.13  ? 1172 PHE A CZ  1 
ATOM   9132  N  N   . GLU A 1 1173 ? 126.919 81.463  102.275 1.00 47.09  ? 1173 GLU A N   1 
ATOM   9133  C  CA  . GLU A 1 1173 ? 125.726 81.108  101.519 1.00 46.01  ? 1173 GLU A CA  1 
ATOM   9134  C  C   . GLU A 1 1173 ? 125.972 80.004  100.520 1.00 45.34  ? 1173 GLU A C   1 
ATOM   9135  O  O   . GLU A 1 1173 ? 126.969 80.008  99.826  1.00 46.01  ? 1173 GLU A O   1 
ATOM   9136  C  CB  . GLU A 1 1173 ? 125.044 82.323  100.874 1.00 46.16  ? 1173 GLU A CB  1 
ATOM   9137  C  CG  . GLU A 1 1173 ? 125.843 83.154  99.906  1.00 48.68  ? 1173 GLU A CG  1 
ATOM   9138  C  CD  . GLU A 1 1173 ? 125.078 84.426  99.499  1.00 51.81  ? 1173 GLU A CD  1 
ATOM   9139  O  OE1 . GLU A 1 1173 ? 124.390 85.047  100.374 1.00 49.43  ? 1173 GLU A OE1 1 
ATOM   9140  O  OE2 . GLU A 1 1173 ? 125.163 84.790  98.296  1.00 52.76  ? 1173 GLU A OE2 1 
ATOM   9141  N  N   . ASN A 1 1174 ? 125.060 79.042  100.496 1.00 43.84  ? 1174 ASN A N   1 
ATOM   9142  C  CA  . ASN A 1 1174 ? 125.081 77.963  99.530  1.00 43.10  ? 1174 ASN A CA  1 
ATOM   9143  C  C   . ASN A 1 1174 ? 123.665 77.722  99.046  1.00 42.35  ? 1174 ASN A C   1 
ATOM   9144  O  O   . ASN A 1 1174 ? 122.852 77.104  99.744  1.00 41.55  ? 1174 ASN A O   1 
ATOM   9145  C  CB  . ASN A 1 1174 ? 125.662 76.686  100.137 1.00 43.06  ? 1174 ASN A CB  1 
ATOM   9146  C  CG  . ASN A 1 1174 ? 125.669 75.529  99.158  1.00 43.29  ? 1174 ASN A CG  1 
ATOM   9147  O  OD1 . ASN A 1 1174 ? 126.020 75.688  97.986  1.00 43.51  ? 1174 ASN A OD1 1 
ATOM   9148  N  ND2 . ASN A 1 1174 ? 125.280 74.358  99.630  1.00 42.39  ? 1174 ASN A ND2 1 
ATOM   9149  N  N   . ARG A 1 1175 ? 123.377 78.246  97.859  1.00 42.13  ? 1175 ARG A N   1 
ATOM   9150  C  CA  . ARG A 1 1175 ? 122.090 78.062  97.180  1.00 41.82  ? 1175 ARG A CA  1 
ATOM   9151  C  C   . ARG A 1 1175 ? 120.942 78.909  97.728  1.00 41.06  ? 1175 ARG A C   1 
ATOM   9152  O  O   . ARG A 1 1175 ? 119.786 78.713  97.364  1.00 41.13  ? 1175 ARG A O   1 
ATOM   9153  C  CB  . ARG A 1 1175 ? 121.714 76.571  97.078  1.00 42.02  ? 1175 ARG A CB  1 
ATOM   9154  C  CG  . ARG A 1 1175 ? 122.637 75.795  96.150  1.00 41.73  ? 1175 ARG A CG  1 
ATOM   9155  C  CD  . ARG A 1 1175 ? 122.246 75.957  94.690  1.00 42.02  ? 1175 ARG A CD  1 
ATOM   9156  N  NE  . ARG A 1 1175 ? 121.506 74.773  94.249  1.00 44.80  ? 1175 ARG A NE  1 
ATOM   9157  C  CZ  . ARG A 1 1175 ? 120.287 74.784  93.721  1.00 44.23  ? 1175 ARG A CZ  1 
ATOM   9158  N  NH1 . ARG A 1 1175 ? 119.641 75.920  93.517  1.00 43.44  ? 1175 ARG A NH1 1 
ATOM   9159  N  NH2 . ARG A 1 1175 ? 119.717 73.646  93.387  1.00 45.20  ? 1175 ARG A NH2 1 
ATOM   9160  N  N   . PHE A 1 1176 ? 121.273 79.856  98.593  1.00 40.65  ? 1176 PHE A N   1 
ATOM   9161  C  CA  . PHE A 1 1176 ? 120.319 80.837  99.072  1.00 40.07  ? 1176 PHE A CA  1 
ATOM   9162  C  C   . PHE A 1 1176 ? 121.007 82.194  99.074  1.00 40.83  ? 1176 PHE A C   1 
ATOM   9163  O  O   . PHE A 1 1176 ? 122.224 82.286  99.234  1.00 41.28  ? 1176 PHE A O   1 
ATOM   9164  C  CB  . PHE A 1 1176 ? 119.849 80.499  100.491 1.00 39.09  ? 1176 PHE A CB  1 
ATOM   9165  C  CG  . PHE A 1 1176 ? 118.693 79.517  100.556 1.00 37.76  ? 1176 PHE A CG  1 
ATOM   9166  C  CD1 . PHE A 1 1176 ? 118.925 78.151  100.699 1.00 36.53  ? 1176 PHE A CD1 1 
ATOM   9167  C  CD2 . PHE A 1 1176 ? 117.375 79.965  100.516 1.00 35.54  ? 1176 PHE A CD2 1 
ATOM   9168  C  CE1 . PHE A 1 1176 ? 117.861 77.241  100.780 1.00 35.91  ? 1176 PHE A CE1 1 
ATOM   9169  C  CE2 . PHE A 1 1176 ? 116.307 79.063  100.594 1.00 35.15  ? 1176 PHE A CE2 1 
ATOM   9170  C  CZ  . PHE A 1 1176 ? 116.551 77.697  100.729 1.00 34.93  ? 1176 PHE A CZ  1 
ATOM   9171  N  N   . GLN A 1 1177 ? 120.232 83.246  98.865  1.00 41.52  ? 1177 GLN A N   1 
ATOM   9172  C  CA  . GLN A 1 1177 ? 120.724 84.597  99.034  1.00 42.38  ? 1177 GLN A CA  1 
ATOM   9173  C  C   . GLN A 1 1177 ? 119.948 85.184  100.193 1.00 41.85  ? 1177 GLN A C   1 
ATOM   9174  O  O   . GLN A 1 1177 ? 118.724 85.045  100.260 1.00 41.81  ? 1177 GLN A O   1 
ATOM   9175  C  CB  . GLN A 1 1177 ? 120.528 85.427  97.765  1.00 42.85  ? 1177 GLN A CB  1 
ATOM   9176  C  CG  . GLN A 1 1177 ? 121.206 86.790  97.838  1.00 45.86  ? 1177 GLN A CG  1 
ATOM   9177  C  CD  . GLN A 1 1177 ? 121.228 87.522  96.509  1.00 50.51  ? 1177 GLN A CD  1 
ATOM   9178  O  OE1 . GLN A 1 1177 ? 121.648 86.970  95.478  1.00 53.65  ? 1177 GLN A OE1 1 
ATOM   9179  N  NE2 . GLN A 1 1177 ? 120.785 88.783  96.522  1.00 50.78  ? 1177 GLN A NE2 1 
ATOM   9180  N  N   . LEU A 1 1178 ? 120.664 85.812  101.117 1.00 42.07  ? 1178 LEU A N   1 
ATOM   9181  C  CA  . LEU A 1 1178 ? 120.060 86.401  102.301 1.00 41.58  ? 1178 LEU A CA  1 
ATOM   9182  C  C   . LEU A 1 1178 ? 120.681 87.767  102.542 1.00 42.39  ? 1178 LEU A C   1 
ATOM   9183  O  O   . LEU A 1 1178 ? 121.895 87.870  102.688 1.00 42.95  ? 1178 LEU A O   1 
ATOM   9184  C  CB  . LEU A 1 1178 ? 120.287 85.490  103.501 1.00 40.85  ? 1178 LEU A CB  1 
ATOM   9185  C  CG  . LEU A 1 1178 ? 119.815 85.944  104.887 1.00 39.49  ? 1178 LEU A CG  1 
ATOM   9186  C  CD1 . LEU A 1 1178 ? 118.305 85.985  104.967 1.00 36.86  ? 1178 LEU A CD1 1 
ATOM   9187  C  CD2 . LEU A 1 1178 ? 120.378 85.005  105.954 1.00 38.37  ? 1178 LEU A CD2 1 
ATOM   9188  N  N   . ASP A 1 1179 ? 119.856 88.810  102.565 1.00 42.97  ? 1179 ASP A N   1 
ATOM   9189  C  CA  . ASP A 1 1179 ? 120.337 90.173  102.802 1.00 44.10  ? 1179 ASP A CA  1 
ATOM   9190  C  C   . ASP A 1 1179 ? 119.626 90.769  103.997 1.00 43.95  ? 1179 ASP A C   1 
ATOM   9191  O  O   . ASP A 1 1179 ? 118.390 90.695  104.094 1.00 44.14  ? 1179 ASP A O   1 
ATOM   9192  C  CB  . ASP A 1 1179 ? 120.078 91.076  101.593 1.00 44.68  ? 1179 ASP A CB  1 
ATOM   9193  C  CG  . ASP A 1 1179 ? 120.682 90.536  100.302 1.00 47.60  ? 1179 ASP A CG  1 
ATOM   9194  O  OD1 . ASP A 1 1179 ? 121.880 90.163  100.296 1.00 50.03  ? 1179 ASP A OD1 1 
ATOM   9195  O  OD2 . ASP A 1 1179 ? 119.953 90.503  99.284  1.00 48.63  ? 1179 ASP A OD2 1 
ATOM   9196  N  N   . LEU A 1 1180 ? 120.393 91.373  104.899 1.00 44.12  ? 1180 LEU A N   1 
ATOM   9197  C  CA  . LEU A 1 1180 ? 119.813 92.072  106.037 1.00 43.83  ? 1180 LEU A CA  1 
ATOM   9198  C  C   . LEU A 1 1180 ? 120.056 93.552  105.925 1.00 45.15  ? 1180 LEU A C   1 
ATOM   9199  O  O   . LEU A 1 1180 ? 121.109 93.982  105.469 1.00 45.81  ? 1180 LEU A O   1 
ATOM   9200  C  CB  . LEU A 1 1180 ? 120.455 91.605  107.332 1.00 43.01  ? 1180 LEU A CB  1 
ATOM   9201  C  CG  . LEU A 1 1180 ? 120.618 90.113  107.529 1.00 41.41  ? 1180 LEU A CG  1 
ATOM   9202  C  CD1 . LEU A 1 1180 ? 121.487 89.867  108.732 1.00 37.98  ? 1180 LEU A CD1 1 
ATOM   9203  C  CD2 . LEU A 1 1180 ? 119.233 89.471  107.651 1.00 40.52  ? 1180 LEU A CD2 1 
ATOM   9204  N  N   . GLU A 1 1181 ? 119.095 94.344  106.359 1.00 46.13  ? 1181 GLU A N   1 
ATOM   9205  C  CA  . GLU A 1 1181 ? 119.396 95.740  106.594 1.00 48.16  ? 1181 GLU A CA  1 
ATOM   9206  C  C   . GLU A 1 1181 ? 118.596 96.330  107.744 1.00 47.91  ? 1181 GLU A C   1 
ATOM   9207  O  O   . GLU A 1 1181 ? 117.404 96.063  107.899 1.00 47.34  ? 1181 GLU A O   1 
ATOM   9208  C  CB  . GLU A 1 1181 ? 119.274 96.572  105.320 1.00 48.90  ? 1181 GLU A CB  1 
ATOM   9209  C  CG  . GLU A 1 1181 ? 117.889 96.672  104.782 1.00 51.91  ? 1181 GLU A CG  1 
ATOM   9210  C  CD  . GLU A 1 1181 ? 117.769 97.783  103.780 1.00 57.23  ? 1181 GLU A CD  1 
ATOM   9211  O  OE1 . GLU A 1 1181 ? 118.272 97.621  102.638 1.00 59.89  ? 1181 GLU A OE1 1 
ATOM   9212  O  OE2 . GLU A 1 1181 ? 117.171 98.819  104.145 1.00 58.90  ? 1181 GLU A OE2 1 
ATOM   9213  N  N   . LYS A 1 1182 ? 119.296 97.106  108.560 1.00 48.83  ? 1182 LYS A N   1 
ATOM   9214  C  CA  . LYS A 1 1182 ? 118.706 97.790  109.685 1.00 49.55  ? 1182 LYS A CA  1 
ATOM   9215  C  C   . LYS A 1 1182 ? 118.085 99.077  109.186 1.00 50.24  ? 1182 LYS A C   1 
ATOM   9216  O  O   . LYS A 1 1182 ? 118.724 99.852  108.491 1.00 50.86  ? 1182 LYS A O   1 
ATOM   9217  C  CB  . LYS A 1 1182 ? 119.770 98.093  110.733 1.00 49.62  ? 1182 LYS A CB  1 
ATOM   9218  C  CG  . LYS A 1 1182 ? 120.417 96.866  111.341 1.00 50.36  ? 1182 LYS A CG  1 
ATOM   9219  C  CD  . LYS A 1 1182 ? 121.411 97.255  112.423 1.00 52.62  ? 1182 LYS A CD  1 
ATOM   9220  C  CE  . LYS A 1 1182 ? 122.732 97.708  111.797 1.00 56.11  ? 1182 LYS A CE  1 
ATOM   9221  N  NZ  . LYS A 1 1182 ? 123.749 98.128  112.803 1.00 57.41  ? 1182 LYS A NZ  1 
ATOM   9222  N  N   . GLN A 1 1183 ? 116.824 99.290  109.528 1.00 50.98  ? 1183 GLN A N   1 
ATOM   9223  C  CA  . GLN A 1 1183 ? 116.116 100.495 109.133 1.00 52.12  ? 1183 GLN A CA  1 
ATOM   9224  C  C   . GLN A 1 1183 ? 116.256 101.543 110.233 1.00 52.73  ? 1183 GLN A C   1 
ATOM   9225  O  O   . GLN A 1 1183 ? 116.471 101.199 111.396 1.00 52.50  ? 1183 GLN A O   1 
ATOM   9226  C  CB  . GLN A 1 1183 ? 114.656 100.166 108.848 1.00 51.73  ? 1183 GLN A CB  1 
ATOM   9227  C  CG  . GLN A 1 1183 ? 114.471 99.308  107.603 1.00 53.06  ? 1183 GLN A CG  1 
ATOM   9228  C  CD  . GLN A 1 1183 ? 113.025 98.912  107.366 1.00 54.12  ? 1183 GLN A CD  1 
ATOM   9229  O  OE1 . GLN A 1 1183 ? 112.223 98.884  108.285 1.00 54.12  ? 1183 GLN A OE1 1 
ATOM   9230  N  NE2 . GLN A 1 1183 ? 112.692 98.595  106.123 1.00 56.48  ? 1183 GLN A NE2 1 
ATOM   9231  N  N   . ASN A 1 1184 ? 116.160 102.819 109.873 1.00 53.89  ? 1184 ASN A N   1 
ATOM   9232  C  CA  . ASN A 1 1184 ? 116.363 103.861 110.865 1.00 54.62  ? 1184 ASN A CA  1 
ATOM   9233  C  C   . ASN A 1 1184 ? 115.108 104.114 111.689 1.00 54.03  ? 1184 ASN A C   1 
ATOM   9234  O  O   . ASN A 1 1184 ? 114.086 104.589 111.180 1.00 54.35  ? 1184 ASN A O   1 
ATOM   9235  C  CB  . ASN A 1 1184 ? 116.897 105.145 110.240 1.00 55.82  ? 1184 ASN A CB  1 
ATOM   9236  C  CG  . ASN A 1 1184 ? 117.991 105.793 111.096 1.00 58.55  ? 1184 ASN A CG  1 
ATOM   9237  O  OD1 . ASN A 1 1184 ? 117.736 106.284 112.212 1.00 59.38  ? 1184 ASN A OD1 1 
ATOM   9238  N  ND2 . ASN A 1 1184 ? 119.224 105.776 110.580 1.00 60.71  ? 1184 ASN A ND2 1 
ATOM   9239  N  N   . THR A 1 1185 ? 115.197 103.776 112.972 1.00 53.26  ? 1185 THR A N   1 
ATOM   9240  C  CA  . THR A 1 1185 ? 114.044 103.804 113.854 1.00 51.82  ? 1185 THR A CA  1 
ATOM   9241  C  C   . THR A 1 1185 ? 113.910 105.137 114.563 1.00 51.68  ? 1185 THR A C   1 
ATOM   9242  O  O   . THR A 1 1185 ? 112.809 105.525 114.945 1.00 51.54  ? 1185 THR A O   1 
ATOM   9243  C  CB  . THR A 1 1185 ? 114.114 102.685 114.905 1.00 51.48  ? 1185 THR A CB  1 
ATOM   9244  O  OG1 . THR A 1 1185 ? 115.348 102.778 115.624 1.00 51.35  ? 1185 THR A OG1 1 
ATOM   9245  C  CG2 . THR A 1 1185 ? 114.016 101.320 114.237 1.00 51.16  ? 1185 THR A CG2 1 
ATOM   9246  N  N   . GLY A 1 1186 ? 115.029 105.835 114.744 1.00 51.73  ? 1186 GLY A N   1 
ATOM   9247  C  CA  . GLY A 1 1186 ? 115.030 107.090 115.494 1.00 51.24  ? 1186 GLY A CA  1 
ATOM   9248  C  C   . GLY A 1 1186 ? 115.084 106.912 117.005 1.00 50.58  ? 1186 GLY A C   1 
ATOM   9249  O  O   . GLY A 1 1186 ? 115.044 107.889 117.741 1.00 51.01  ? 1186 GLY A O   1 
ATOM   9250  N  N   . SER A 1 1187 ? 115.166 105.664 117.466 1.00 49.59  ? 1187 SER A N   1 
ATOM   9251  C  CA  . SER A 1 1187 ? 115.305 105.348 118.879 1.00 48.53  ? 1187 SER A CA  1 
ATOM   9252  C  C   . SER A 1 1187 ? 116.430 104.348 119.037 1.00 48.49  ? 1187 SER A C   1 
ATOM   9253  O  O   . SER A 1 1187 ? 116.521 103.417 118.252 1.00 48.83  ? 1187 SER A O   1 
ATOM   9254  C  CB  . SER A 1 1187 ? 114.013 104.732 119.409 1.00 47.75  ? 1187 SER A CB  1 
ATOM   9255  O  OG  . SER A 1 1187 ? 114.206 104.194 120.708 1.00 46.61  ? 1187 SER A OG  1 
ATOM   9256  N  N   . ASP A 1 1188 ? 117.278 104.529 120.043 1.00 48.43  ? 1188 ASP A N   1 
ATOM   9257  C  CA  . ASP A 1 1188 ? 118.319 103.546 120.345 1.00 48.63  ? 1188 ASP A CA  1 
ATOM   9258  C  C   . ASP A 1 1188 ? 117.752 102.207 120.844 1.00 47.72  ? 1188 ASP A C   1 
ATOM   9259  O  O   . ASP A 1 1188 ? 118.452 101.195 120.811 1.00 47.89  ? 1188 ASP A O   1 
ATOM   9260  C  CB  . ASP A 1 1188 ? 119.312 104.092 121.371 1.00 49.30  ? 1188 ASP A CB  1 
ATOM   9261  C  CG  . ASP A 1 1188 ? 120.171 105.222 120.825 1.00 52.21  ? 1188 ASP A CG  1 
ATOM   9262  O  OD1 . ASP A 1 1188 ? 120.273 105.362 119.584 1.00 54.28  ? 1188 ASP A OD1 1 
ATOM   9263  O  OD2 . ASP A 1 1188 ? 120.760 105.973 121.646 1.00 54.57  ? 1188 ASP A OD2 1 
ATOM   9264  N  N   . TYR A 1 1189 ? 116.496 102.210 121.298 1.00 46.66  ? 1189 TYR A N   1 
ATOM   9265  C  CA  . TYR A 1 1189 ? 115.873 101.031 121.913 1.00 45.86  ? 1189 TYR A CA  1 
ATOM   9266  C  C   . TYR A 1 1189 ? 115.047 100.194 120.942 1.00 44.55  ? 1189 TYR A C   1 
ATOM   9267  O  O   . TYR A 1 1189 ? 114.496 99.158  121.316 1.00 44.03  ? 1189 TYR A O   1 
ATOM   9268  C  CB  . TYR A 1 1189 ? 114.986 101.438 123.101 1.00 46.33  ? 1189 TYR A CB  1 
ATOM   9269  C  CG  . TYR A 1 1189 ? 115.644 102.413 124.036 1.00 47.93  ? 1189 TYR A CG  1 
ATOM   9270  C  CD1 . TYR A 1 1189 ? 115.196 103.723 124.119 1.00 49.52  ? 1189 TYR A CD1 1 
ATOM   9271  C  CD2 . TYR A 1 1189 ? 116.730 102.031 124.821 1.00 49.53  ? 1189 TYR A CD2 1 
ATOM   9272  C  CE1 . TYR A 1 1189 ? 115.809 104.633 124.966 1.00 51.18  ? 1189 TYR A CE1 1 
ATOM   9273  C  CE2 . TYR A 1 1189 ? 117.353 102.933 125.669 1.00 51.12  ? 1189 TYR A CE2 1 
ATOM   9274  C  CZ  . TYR A 1 1189 ? 116.889 104.233 125.733 1.00 51.34  ? 1189 TYR A CZ  1 
ATOM   9275  O  OH  . TYR A 1 1189 ? 117.491 105.136 126.568 1.00 51.21  ? 1189 TYR A OH  1 
ATOM   9276  N  N   . GLU A 1 1190 ? 114.948 100.648 119.702 1.00 43.69  ? 1190 GLU A N   1 
ATOM   9277  C  CA  . GLU A 1 1190 ? 114.186 99.907  118.715 1.00 42.85  ? 1190 GLU A CA  1 
ATOM   9278  C  C   . GLU A 1 1190 ? 115.064 99.454  117.557 1.00 42.21  ? 1190 GLU A C   1 
ATOM   9279  O  O   . GLU A 1 1190 ? 115.867 100.223 117.027 1.00 42.28  ? 1190 GLU A O   1 
ATOM   9280  C  CB  . GLU A 1 1190 ? 112.976 100.708 118.222 1.00 42.87  ? 1190 GLU A CB  1 
ATOM   9281  C  CG  . GLU A 1 1190 ? 112.122 99.953  117.221 1.00 43.87  ? 1190 GLU A CG  1 
ATOM   9282  C  CD  . GLU A 1 1190 ? 111.006 100.788 116.631 1.00 45.86  ? 1190 GLU A CD  1 
ATOM   9283  O  OE1 . GLU A 1 1190 ? 110.544 101.741 117.293 1.00 48.11  ? 1190 GLU A OE1 1 
ATOM   9284  O  OE2 . GLU A 1 1190 ? 110.575 100.478 115.503 1.00 46.87  ? 1190 GLU A OE2 1 
ATOM   9285  N  N   . LEU A 1 1191 ? 114.894 98.187  117.190 1.00 41.08  ? 1191 LEU A N   1 
ATOM   9286  C  CA  . LEU A 1 1191 ? 115.572 97.586  116.057 1.00 40.33  ? 1191 LEU A CA  1 
ATOM   9287  C  C   . LEU A 1 1191 ? 114.532 97.135  115.040 1.00 39.57  ? 1191 LEU A C   1 
ATOM   9288  O  O   . LEU A 1 1191 ? 113.626 96.371  115.371 1.00 39.16  ? 1191 LEU A O   1 
ATOM   9289  C  CB  . LEU A 1 1191 ? 116.413 96.402  116.529 1.00 40.27  ? 1191 LEU A CB  1 
ATOM   9290  C  CG  . LEU A 1 1191 ? 116.805 95.348  115.494 1.00 40.53  ? 1191 LEU A CG  1 
ATOM   9291  C  CD1 . LEU A 1 1191 ? 117.986 95.815  114.671 1.00 39.31  ? 1191 LEU A CD1 1 
ATOM   9292  C  CD2 . LEU A 1 1191 ? 117.104 94.020  116.180 1.00 39.33  ? 1191 LEU A CD2 1 
ATOM   9293  N  N   . ARG A 1 1192 ? 114.647 97.655  113.820 1.00 39.24  ? 1192 ARG A N   1 
ATOM   9294  C  CA  . ARG A 1 1192 ? 113.854 97.201  112.680 1.00 38.78  ? 1192 ARG A CA  1 
ATOM   9295  C  C   . ARG A 1 1192 ? 114.784 96.585  111.651 1.00 38.39  ? 1192 ARG A C   1 
ATOM   9296  O  O   . ARG A 1 1192 ? 115.551 97.284  110.981 1.00 38.87  ? 1192 ARG A O   1 
ATOM   9297  C  CB  . ARG A 1 1192 ? 113.065 98.345  112.053 1.00 39.11  ? 1192 ARG A CB  1 
ATOM   9298  C  CG  . ARG A 1 1192 ? 111.806 98.681  112.816 1.00 41.59  ? 1192 ARG A CG  1 
ATOM   9299  C  CD  . ARG A 1 1192 ? 111.050 99.850  112.191 1.00 45.64  ? 1192 ARG A CD  1 
ATOM   9300  N  NE  . ARG A 1 1192 ? 109.849 99.415  111.478 1.00 48.61  ? 1192 ARG A NE  1 
ATOM   9301  C  CZ  . ARG A 1 1192 ? 109.684 99.499  110.158 1.00 49.86  ? 1192 ARG A CZ  1 
ATOM   9302  N  NH1 . ARG A 1 1192 ? 110.648 100.012 109.409 1.00 50.94  ? 1192 ARG A NH1 1 
ATOM   9303  N  NH2 . ARG A 1 1192 ? 108.555 99.083  109.587 1.00 49.15  ? 1192 ARG A NH2 1 
ATOM   9304  N  N   . LEU A 1 1193 ? 114.726 95.265  111.545 1.00 37.06  ? 1193 LEU A N   1 
ATOM   9305  C  CA  . LEU A 1 1193 ? 115.611 94.528  110.668 1.00 36.27  ? 1193 LEU A CA  1 
ATOM   9306  C  C   . LEU A 1 1193 ? 114.837 94.045  109.437 1.00 35.92  ? 1193 LEU A C   1 
ATOM   9307  O  O   . LEU A 1 1193 ? 113.905 93.251  109.560 1.00 35.72  ? 1193 LEU A O   1 
ATOM   9308  C  CB  . LEU A 1 1193 ? 116.230 93.365  111.451 1.00 35.62  ? 1193 LEU A CB  1 
ATOM   9309  C  CG  . LEU A 1 1193 ? 117.231 92.412  110.806 1.00 36.36  ? 1193 LEU A CG  1 
ATOM   9310  C  CD1 . LEU A 1 1193 ? 118.529 93.109  110.457 1.00 37.48  ? 1193 LEU A CD1 1 
ATOM   9311  C  CD2 . LEU A 1 1193 ? 117.514 91.269  111.740 1.00 36.45  ? 1193 LEU A CD2 1 
ATOM   9312  N  N   . LYS A 1 1194 ? 115.205 94.540  108.255 1.00 35.92  ? 1194 LYS A N   1 
ATOM   9313  C  CA  . LYS A 1 1194 ? 114.616 94.046  106.992 1.00 35.69  ? 1194 LYS A CA  1 
ATOM   9314  C  C   . LYS A 1 1194 ? 115.330 92.786  106.530 1.00 35.27  ? 1194 LYS A C   1 
ATOM   9315  O  O   . LYS A 1 1194 ? 116.538 92.787  106.359 1.00 36.21  ? 1194 LYS A O   1 
ATOM   9316  C  CB  . LYS A 1 1194 ? 114.662 95.110  105.886 1.00 36.17  ? 1194 LYS A CB  1 
ATOM   9317  C  CG  . LYS A 1 1194 ? 113.537 94.986  104.848 1.00 36.93  ? 1194 LYS A CG  1 
ATOM   9318  C  CD  . LYS A 1 1194 ? 113.866 95.707  103.542 1.00 39.37  ? 1194 LYS A CD  1 
ATOM   9319  C  CE  . LYS A 1 1194 ? 112.858 95.378  102.430 1.00 41.70  ? 1194 LYS A CE  1 
ATOM   9320  N  NZ  . LYS A 1 1194 ? 111.444 95.854  102.746 1.00 42.99  ? 1194 LYS A NZ  1 
ATOM   9321  N  N   . VAL A 1 1195 ? 114.585 91.707  106.348 1.00 34.53  ? 1195 VAL A N   1 
ATOM   9322  C  CA  . VAL A 1 1195 ? 115.161 90.444  105.918 1.00 34.32  ? 1195 VAL A CA  1 
ATOM   9323  C  C   . VAL A 1 1195 ? 114.640 90.099  104.529 1.00 34.81  ? 1195 VAL A C   1 
ATOM   9324  O  O   . VAL A 1 1195 ? 113.437 90.194  104.277 1.00 34.76  ? 1195 VAL A O   1 
ATOM   9325  C  CB  . VAL A 1 1195 ? 114.820 89.311  106.896 1.00 33.87  ? 1195 VAL A CB  1 
ATOM   9326  C  CG1 . VAL A 1 1195 ? 115.482 88.014  106.461 1.00 34.52  ? 1195 VAL A CG1 1 
ATOM   9327  C  CG2 . VAL A 1 1195 ? 115.263 89.672  108.320 1.00 33.24  ? 1195 VAL A CG2 1 
ATOM   9328  N  N   . CYS A 1 1196 ? 115.543 89.740  103.615 1.00 35.22  ? 1196 CYS A N   1 
ATOM   9329  C  CA  . CYS A 1 1196 ? 115.140 89.209  102.306 1.00 35.62  ? 1196 CYS A CA  1 
ATOM   9330  C  C   . CYS A 1 1196 ? 115.908 87.942  102.025 1.00 35.33  ? 1196 CYS A C   1 
ATOM   9331  O  O   . CYS A 1 1196 ? 117.128 87.905  102.186 1.00 36.13  ? 1196 CYS A O   1 
ATOM   9332  C  CB  . CYS A 1 1196 ? 115.358 90.220  101.177 1.00 35.85  ? 1196 CYS A CB  1 
ATOM   9333  S  SG  . CYS A 1 1196 ? 114.335 91.686  101.340 1.00 38.56  ? 1196 CYS A SG  1 
ATOM   9334  N  N   . ALA A 1 1197 ? 115.187 86.906  101.619 1.00 34.48  ? 1197 ALA A N   1 
ATOM   9335  C  CA  . ALA A 1 1197 ? 115.790 85.645  101.252 1.00 34.23  ? 1197 ALA A CA  1 
ATOM   9336  C  C   . ALA A 1 1197 ? 115.212 85.203  99.919  1.00 34.68  ? 1197 ALA A C   1 
ATOM   9337  O  O   . ALA A 1 1197 ? 114.062 85.498  99.604  1.00 34.40  ? 1197 ALA A O   1 
ATOM   9338  C  CB  . ALA A 1 1197 ? 115.515 84.599  102.314 1.00 33.72  ? 1197 ALA A CB  1 
ATOM   9339  N  N   . SER A 1 1198 ? 116.019 84.501  99.138  1.00 34.98  ? 1198 SER A N   1 
ATOM   9340  C  CA  . SER A 1 1198 ? 115.539 83.851  97.941  1.00 35.67  ? 1198 SER A CA  1 
ATOM   9341  C  C   . SER A 1 1198 ? 116.442 82.678  97.651  1.00 35.81  ? 1198 SER A C   1 
ATOM   9342  O  O   . SER A 1 1198 ? 117.607 82.688  98.038  1.00 36.09  ? 1198 SER A O   1 
ATOM   9343  C  CB  . SER A 1 1198 ? 115.518 84.817  96.755  1.00 36.32  ? 1198 SER A CB  1 
ATOM   9344  O  OG  . SER A 1 1198 ? 116.637 85.676  96.798  1.00 38.43  ? 1198 SER A OG  1 
ATOM   9345  N  N   . TYR A 1 1199 ? 115.879 81.671  96.987  1.00 35.38  ? 1199 TYR A N   1 
ATOM   9346  C  CA  . TYR A 1 1199 ? 116.590 80.474  96.572  1.00 35.66  ? 1199 TYR A CA  1 
ATOM   9347  C  C   . TYR A 1 1199 ? 117.313 80.742  95.250  1.00 36.80  ? 1199 TYR A C   1 
ATOM   9348  O  O   . TYR A 1 1199 ? 116.824 81.517  94.428  1.00 37.16  ? 1199 TYR A O   1 
ATOM   9349  C  CB  . TYR A 1 1199 ? 115.559 79.370  96.391  1.00 34.99  ? 1199 TYR A CB  1 
ATOM   9350  C  CG  . TYR A 1 1199 ? 116.073 77.966  96.205  1.00 34.68  ? 1199 TYR A CG  1 
ATOM   9351  C  CD1 . TYR A 1 1199 ? 116.823 77.335  97.184  1.00 32.87  ? 1199 TYR A CD1 1 
ATOM   9352  C  CD2 . TYR A 1 1199 ? 115.745 77.237  95.065  1.00 35.57  ? 1199 TYR A CD2 1 
ATOM   9353  C  CE1 . TYR A 1 1199 ? 117.254 76.038  97.022  1.00 32.35  ? 1199 TYR A CE1 1 
ATOM   9354  C  CE2 . TYR A 1 1199 ? 116.169 75.936  94.902  1.00 34.65  ? 1199 TYR A CE2 1 
ATOM   9355  C  CZ  . TYR A 1 1199 ? 116.922 75.340  95.886  1.00 33.84  ? 1199 TYR A CZ  1 
ATOM   9356  O  OH  . TYR A 1 1199 ? 117.347 74.032  95.720  1.00 36.17  ? 1199 TYR A OH  1 
ATOM   9357  N  N   . ILE A 1 1200 ? 118.473 80.120  95.049  1.00 37.59  ? 1200 ILE A N   1 
ATOM   9358  C  CA  . ILE A 1 1200 ? 119.200 80.269  93.790  1.00 38.93  ? 1200 ILE A CA  1 
ATOM   9359  C  C   . ILE A 1 1200 ? 118.891 79.083  92.885  1.00 40.37  ? 1200 ILE A C   1 
ATOM   9360  O  O   . ILE A 1 1200 ? 119.503 78.025  93.019  1.00 40.68  ? 1200 ILE A O   1 
ATOM   9361  C  CB  . ILE A 1 1200 ? 120.734 80.399  93.986  1.00 39.17  ? 1200 ILE A CB  1 
ATOM   9362  C  CG1 . ILE A 1 1200 ? 121.073 81.606  94.865  1.00 38.27  ? 1200 ILE A CG1 1 
ATOM   9363  C  CG2 . ILE A 1 1200 ? 121.433 80.537  92.639  1.00 38.64  ? 1200 ILE A CG2 1 
ATOM   9364  C  CD1 . ILE A 1 1200 ? 122.444 81.525  95.508  1.00 37.43  ? 1200 ILE A CD1 1 
ATOM   9365  N  N   . PRO A 1 1201 ? 117.939 79.256  91.957  1.00 41.34  ? 1201 PRO A N   1 
ATOM   9366  C  CA  . PRO A 1 1201 ? 117.521 78.120  91.155  1.00 42.75  ? 1201 PRO A CA  1 
ATOM   9367  C  C   . PRO A 1 1201 ? 118.634 77.722  90.218  1.00 44.78  ? 1201 PRO A C   1 
ATOM   9368  O  O   . PRO A 1 1201 ? 119.366 78.586  89.735  1.00 45.19  ? 1201 PRO A O   1 
ATOM   9369  C  CB  . PRO A 1 1201 ? 116.334 78.659  90.360  1.00 42.84  ? 1201 PRO A CB  1 
ATOM   9370  C  CG  . PRO A 1 1201 ? 116.483 80.121  90.355  1.00 41.92  ? 1201 PRO A CG  1 
ATOM   9371  C  CD  . PRO A 1 1201 ? 117.235 80.496  91.589  1.00 41.07  ? 1201 PRO A CD  1 
ATOM   9372  N  N   . GLN A 1 1202 ? 118.784 76.422  89.996  1.00 46.50  ? 1202 GLN A N   1 
ATOM   9373  C  CA  . GLN A 1 1202 ? 119.795 75.931  89.083  1.00 48.76  ? 1202 GLN A CA  1 
ATOM   9374  C  C   . GLN A 1 1202 ? 119.246 74.762  88.291  1.00 49.88  ? 1202 GLN A C   1 
ATOM   9375  O  O   . GLN A 1 1202 ? 118.674 73.834  88.856  1.00 50.04  ? 1202 GLN A O   1 
ATOM   9376  C  CB  . GLN A 1 1202 ? 121.118 75.619  89.800  1.00 48.81  ? 1202 GLN A CB  1 
ATOM   9377  C  CG  . GLN A 1 1202 ? 121.219 74.263  90.477  1.00 51.29  ? 1202 GLN A CG  1 
ATOM   9378  C  CD  . GLN A 1 1202 ? 122.641 73.943  90.957  1.00 54.43  ? 1202 GLN A CD  1 
ATOM   9379  O  OE1 . GLN A 1 1202 ? 123.370 74.831  91.436  1.00 55.13  ? 1202 GLN A OE1 1 
ATOM   9380  N  NE2 . GLN A 1 1202 ? 123.036 72.669  90.837  1.00 53.46  ? 1202 GLN A NE2 1 
ATOM   9381  N  N   . LEU A 1 1203 ? 119.391 74.846  86.973  1.00 51.36  ? 1203 LEU A N   1 
ATOM   9382  C  CA  . LEU A 1 1203 ? 118.789 73.890  86.059  1.00 52.60  ? 1203 LEU A CA  1 
ATOM   9383  C  C   . LEU A 1 1203 ? 117.312 73.692  86.390  1.00 52.28  ? 1203 LEU A C   1 
ATOM   9384  O  O   . LEU A 1 1203 ? 116.592 74.666  86.605  1.00 51.47  ? 1203 LEU A O   1 
ATOM   9385  C  CB  . LEU A 1 1203 ? 119.569 72.573  86.084  1.00 53.38  ? 1203 LEU A CB  1 
ATOM   9386  C  CG  . LEU A 1 1203 ? 121.041 72.729  85.668  1.00 54.73  ? 1203 LEU A CG  1 
ATOM   9387  C  CD1 . LEU A 1 1203 ? 121.889 71.490  86.018  1.00 55.30  ? 1203 LEU A CD1 1 
ATOM   9388  C  CD2 . LEU A 1 1203 ? 121.166 73.121  84.177  1.00 54.27  ? 1203 LEU A CD2 1 
ATOM   9389  N  N   . THR A 1 1204 ? 116.883 72.434  86.441  1.00 53.06  ? 1204 THR A N   1 
ATOM   9390  C  CA  . THR A 1 1204 ? 115.498 72.051  86.746  1.00 53.18  ? 1204 THR A CA  1 
ATOM   9391  C  C   . THR A 1 1204 ? 115.087 72.251  88.225  1.00 51.73  ? 1204 THR A C   1 
ATOM   9392  O  O   . THR A 1 1204 ? 113.902 72.171  88.561  1.00 51.55  ? 1204 THR A O   1 
ATOM   9393  C  CB  . THR A 1 1204 ? 115.223 70.584  86.318  1.00 54.37  ? 1204 THR A CB  1 
ATOM   9394  O  OG1 . THR A 1 1204 ? 114.143 70.056  87.097  1.00 55.36  ? 1204 THR A OG1 1 
ATOM   9395  C  CG2 . THR A 1 1204 ? 116.460 69.692  86.537  1.00 55.41  ? 1204 THR A CG2 1 
ATOM   9396  N  N   . ASP A 1 1205 ? 116.061 72.516  89.093  1.00 50.57  ? 1205 ASP A N   1 
ATOM   9397  C  CA  . ASP A 1 1205 ? 115.828 72.749  90.518  1.00 48.89  ? 1205 ASP A CA  1 
ATOM   9398  C  C   . ASP A 1 1205 ? 115.490 74.234  90.747  1.00 47.70  ? 1205 ASP A C   1 
ATOM   9399  O  O   . ASP A 1 1205 ? 116.359 75.035  91.102  1.00 47.32  ? 1205 ASP A O   1 
ATOM   9400  C  CB  . ASP A 1 1205 ? 117.091 72.329  91.292  1.00 49.00  ? 1205 ASP A CB  1 
ATOM   9401  C  CG  . ASP A 1 1205 ? 116.948 72.432  92.809  1.00 48.56  ? 1205 ASP A CG  1 
ATOM   9402  O  OD1 . ASP A 1 1205 ? 116.031 73.095  93.324  1.00 48.26  ? 1205 ASP A OD1 1 
ATOM   9403  O  OD2 . ASP A 1 1205 ? 117.797 71.838  93.500  1.00 49.46  ? 1205 ASP A OD2 1 
ATOM   9404  N  N   . ARG A 1 1206 ? 114.224 74.590  90.551  1.00 46.79  ? 1206 ARG A N   1 
ATOM   9405  C  CA  . ARG A 1 1206 ? 113.800 75.998  90.575  1.00 45.51  ? 1206 ARG A CA  1 
ATOM   9406  C  C   . ARG A 1 1206 ? 113.366 76.498  91.956  1.00 43.13  ? 1206 ARG A C   1 
ATOM   9407  O  O   . ARG A 1 1206 ? 113.552 77.674  92.264  1.00 42.95  ? 1206 ARG A O   1 
ATOM   9408  C  CB  . ARG A 1 1206 ? 112.687 76.253  89.552  1.00 46.46  ? 1206 ARG A CB  1 
ATOM   9409  C  CG  . ARG A 1 1206 ? 113.042 75.943  88.079  1.00 50.33  ? 1206 ARG A CG  1 
ATOM   9410  C  CD  . ARG A 1 1206 ? 113.623 77.164  87.348  1.00 55.26  ? 1206 ARG A CD  1 
ATOM   9411  N  NE  . ARG A 1 1206 ? 115.003 76.977  86.881  1.00 59.34  ? 1206 ARG A NE  1 
ATOM   9412  C  CZ  . ARG A 1 1206 ? 115.877 77.968  86.661  1.00 61.48  ? 1206 ARG A CZ  1 
ATOM   9413  N  NH1 . ARG A 1 1206 ? 115.537 79.242  86.886  1.00 61.13  ? 1206 ARG A NH1 1 
ATOM   9414  N  NH2 . ARG A 1 1206 ? 117.106 77.685  86.229  1.00 61.98  ? 1206 ARG A NH2 1 
ATOM   9415  N  N   . ARG A 1 1207 ? 112.774 75.619  92.767  1.00 40.95  ? 1207 ARG A N   1 
ATOM   9416  C  CA  . ARG A 1 1207 ? 112.350 75.958  94.134  1.00 38.23  ? 1207 ARG A CA  1 
ATOM   9417  C  C   . ARG A 1 1207 ? 112.940 74.984  95.166  1.00 36.89  ? 1207 ARG A C   1 
ATOM   9418  O  O   . ARG A 1 1207 ? 113.266 73.850  94.852  1.00 36.66  ? 1207 ARG A O   1 
ATOM   9419  C  CB  . ARG A 1 1207 ? 110.817 75.961  94.307  1.00 37.61  ? 1207 ARG A CB  1 
ATOM   9420  C  CG  . ARG A 1 1207 ? 109.970 76.217  93.075  1.00 37.95  ? 1207 ARG A CG  1 
ATOM   9421  C  CD  . ARG A 1 1207 ? 109.159 77.514  93.072  1.00 35.79  ? 1207 ARG A CD  1 
ATOM   9422  N  NE  . ARG A 1 1207 ? 108.599 77.869  94.364  1.00 34.64  ? 1207 ARG A NE  1 
ATOM   9423  C  CZ  . ARG A 1 1207 ? 108.561 79.119  94.829  1.00 34.36  ? 1207 ARG A CZ  1 
ATOM   9424  N  NH1 . ARG A 1 1207 ? 109.040 80.120  94.089  1.00 34.05  ? 1207 ARG A NH1 1 
ATOM   9425  N  NH2 . ARG A 1 1207 ? 108.066 79.374  96.036  1.00 31.89  ? 1207 ARG A NH2 1 
ATOM   9426  N  N   . SER A 1 1208 ? 113.044 75.441  96.411  1.00 35.10  ? 1208 SER A N   1 
ATOM   9427  C  CA  . SER A 1 1208 ? 113.529 74.615  97.504  1.00 33.97  ? 1208 SER A CA  1 
ATOM   9428  C  C   . SER A 1 1208 ? 112.431 73.695  98.044  1.00 33.32  ? 1208 SER A C   1 
ATOM   9429  O  O   . SER A 1 1208 ? 111.293 73.718  97.566  1.00 33.46  ? 1208 SER A O   1 
ATOM   9430  C  CB  . SER A 1 1208 ? 114.042 75.510  98.620  1.00 32.84  ? 1208 SER A CB  1 
ATOM   9431  O  OG  . SER A 1 1208 ? 112.963 76.208  99.212  1.00 33.02  ? 1208 SER A OG  1 
ATOM   9432  N  N   . ASN A 1 1209 ? 112.781 72.873  99.030  1.00 32.46  ? 1209 ASN A N   1 
ATOM   9433  C  CA  . ASN A 1 1209 ? 111.782 72.219  99.850  1.00 31.98  ? 1209 ASN A CA  1 
ATOM   9434  C  C   . ASN A 1 1209 ? 111.198 73.283  100.780 1.00 31.14  ? 1209 ASN A C   1 
ATOM   9435  O  O   . ASN A 1 1209 ? 111.444 74.473  100.589 1.00 31.32  ? 1209 ASN A O   1 
ATOM   9436  C  CB  . ASN A 1 1209 ? 112.420 71.109  100.673 1.00 31.95  ? 1209 ASN A CB  1 
ATOM   9437  C  CG  . ASN A 1 1209 ? 113.079 70.057  99.823  1.00 34.18  ? 1209 ASN A CG  1 
ATOM   9438  O  OD1 . ASN A 1 1209 ? 112.442 69.425  98.961  1.00 34.14  ? 1209 ASN A OD1 1 
ATOM   9439  N  ND2 . ASN A 1 1209 ? 114.372 69.843  100.069 1.00 34.63  ? 1209 ASN A ND2 1 
ATOM   9440  N  N   . MET A 1 1210 ? 110.441 72.866  101.788 1.00 30.55  ? 1210 MET A N   1 
ATOM   9441  C  CA  . MET A 1 1210 ? 110.070 73.753  102.869 1.00 29.85  ? 1210 MET A CA  1 
ATOM   9442  C  C   . MET A 1 1210 ? 111.330 74.435  103.399 1.00 30.00  ? 1210 MET A C   1 
ATOM   9443  O  O   . MET A 1 1210 ? 112.348 73.774  103.629 1.00 29.86  ? 1210 MET A O   1 
ATOM   9444  C  CB  . MET A 1 1210 ? 109.359 72.984  103.979 1.00 29.47  ? 1210 MET A CB  1 
ATOM   9445  C  CG  . MET A 1 1210 ? 108.874 73.861  105.131 1.00 30.00  ? 1210 MET A CG  1 
ATOM   9446  S  SD  . MET A 1 1210 ? 108.161 72.924  106.497 1.00 33.21  ? 1210 MET A SD  1 
ATOM   9447  C  CE  . MET A 1 1210 ? 109.536 71.901  106.998 1.00 32.51  ? 1210 MET A CE  1 
ATOM   9448  N  N   . ALA A 1 1211 ? 111.246 75.760  103.564 1.00 29.95  ? 1211 ALA A N   1 
ATOM   9449  C  CA  . ALA A 1 1211 ? 112.354 76.579  104.020 1.00 30.14  ? 1211 ALA A CA  1 
ATOM   9450  C  C   . ALA A 1 1211 ? 111.978 77.355  105.278 1.00 30.28  ? 1211 ALA A C   1 
ATOM   9451  O  O   . ALA A 1 1211 ? 110.846 77.861  105.395 1.00 30.12  ? 1211 ALA A O   1 
ATOM   9452  C  CB  . ALA A 1 1211 ? 112.753 77.539  102.945 1.00 30.38  ? 1211 ALA A CB  1 
ATOM   9453  N  N   . LEU A 1 1212 ? 112.928 77.453  106.211 1.00 30.20  ? 1212 LEU A N   1 
ATOM   9454  C  CA  . LEU A 1 1212 ? 112.742 78.276  107.387 1.00 30.05  ? 1212 LEU A CA  1 
ATOM   9455  C  C   . LEU A 1 1212 ? 113.707 79.439  107.403 1.00 30.38  ? 1212 LEU A C   1 
ATOM   9456  O  O   . LEU A 1 1212 ? 114.837 79.336  106.924 1.00 31.02  ? 1212 LEU A O   1 
ATOM   9457  C  CB  . LEU A 1 1212 ? 112.971 77.493  108.677 1.00 29.48  ? 1212 LEU A CB  1 
ATOM   9458  C  CG  . LEU A 1 1212 ? 112.424 76.098  108.929 1.00 30.77  ? 1212 LEU A CG  1 
ATOM   9459  C  CD1 . LEU A 1 1212 ? 112.320 75.851  110.437 1.00 29.54  ? 1212 LEU A CD1 1 
ATOM   9460  C  CD2 . LEU A 1 1212 ? 111.109 75.839  108.229 1.00 30.30  ? 1212 LEU A CD2 1 
ATOM   9461  N  N   . ILE A 1 1213 ? 113.261 80.539  107.989 1.00 29.98  ? 1213 ILE A N   1 
ATOM   9462  C  CA  . ILE A 1 1213 ? 114.172 81.569  108.413 1.00 30.43  ? 1213 ILE A CA  1 
ATOM   9463  C  C   . ILE A 1 1213 ? 114.143 81.622  109.948 1.00 30.59  ? 1213 ILE A C   1 
ATOM   9464  O  O   . ILE A 1 1213 ? 113.064 81.658  110.552 1.00 30.44  ? 1213 ILE A O   1 
ATOM   9465  C  CB  . ILE A 1 1213 ? 113.807 82.924  107.783 1.00 30.21  ? 1213 ILE A CB  1 
ATOM   9466  C  CG1 . ILE A 1 1213 ? 113.947 82.845  106.247 1.00 30.89  ? 1213 ILE A CG1 1 
ATOM   9467  C  CG2 . ILE A 1 1213 ? 114.681 84.031  108.347 1.00 29.90  ? 1213 ILE A CG2 1 
ATOM   9468  C  CD1 . ILE A 1 1213 ? 113.338 84.022  105.470 1.00 29.62  ? 1213 ILE A CD1 1 
ATOM   9469  N  N   A GLU A 1 1214 ? 115.315 81.573  110.574 0.50 30.83  ? 1214 GLU A N   1 
ATOM   9470  N  N   B GLU A 1 1214 ? 115.324 81.583  110.563 0.50 30.81  ? 1214 GLU A N   1 
ATOM   9471  C  CA  A GLU A 1 1214 ? 115.407 81.898  111.985 0.50 30.60  ? 1214 GLU A CA  1 
ATOM   9472  C  CA  B GLU A 1 1214 ? 115.479 81.848  111.988 0.50 30.59  ? 1214 GLU A CA  1 
ATOM   9473  C  C   A GLU A 1 1214 ? 116.132 83.213  112.131 0.50 30.98  ? 1214 GLU A C   1 
ATOM   9474  C  C   B GLU A 1 1214 ? 116.150 83.210  112.139 0.50 30.95  ? 1214 GLU A C   1 
ATOM   9475  O  O   A GLU A 1 1214 ? 117.183 83.431  111.516 0.50 31.79  ? 1214 GLU A O   1 
ATOM   9476  O  O   B GLU A 1 1214 ? 117.192 83.458  111.520 0.50 31.77  ? 1214 GLU A O   1 
ATOM   9477  C  CB  A GLU A 1 1214 ? 116.136 80.825  112.789 0.50 30.84  ? 1214 GLU A CB  1 
ATOM   9478  C  CB  B GLU A 1 1214 ? 116.351 80.783  112.663 0.50 30.81  ? 1214 GLU A CB  1 
ATOM   9479  C  CG  A GLU A 1 1214 ? 115.862 80.920  114.291 0.50 29.82  ? 1214 GLU A CG  1 
ATOM   9480  C  CG  B GLU A 1 1214 ? 115.728 79.377  112.790 0.50 30.35  ? 1214 GLU A CG  1 
ATOM   9481  C  CD  A GLU A 1 1214 ? 116.940 80.284  115.141 0.50 30.47  ? 1214 GLU A CD  1 
ATOM   9482  C  CD  B GLU A 1 1214 ? 116.741 78.323  113.238 0.50 29.29  ? 1214 GLU A CD  1 
ATOM   9483  O  OE1 A GLU A 1 1214 ? 117.761 79.511  114.592 0.50 30.21  ? 1214 GLU A OE1 1 
ATOM   9484  O  OE1 B GLU A 1 1214 ? 117.655 78.680  114.024 0.50 28.97  ? 1214 GLU A OE1 1 
ATOM   9485  O  OE2 A GLU A 1 1214 ? 116.967 80.566  116.367 0.50 30.45  ? 1214 GLU A OE2 1 
ATOM   9486  O  OE2 B GLU A 1 1214 ? 116.630 77.152  112.794 0.50 26.77  ? 1214 GLU A OE2 1 
ATOM   9487  N  N   . VAL A 1 1215 ? 115.557 84.092  112.941 1.00 30.65  ? 1215 VAL A N   1 
ATOM   9488  C  CA  . VAL A 1 1215 ? 116.198 85.347  113.289 1.00 30.62  ? 1215 VAL A CA  1 
ATOM   9489  C  C   . VAL A 1 1215 ? 116.593 85.238  114.753 1.00 31.46  ? 1215 VAL A C   1 
ATOM   9490  O  O   . VAL A 1 1215 ? 115.798 84.841  115.609 1.00 31.46  ? 1215 VAL A O   1 
ATOM   9491  C  CB  . VAL A 1 1215 ? 115.297 86.557  113.010 1.00 30.23  ? 1215 VAL A CB  1 
ATOM   9492  C  CG1 . VAL A 1 1215 ? 115.949 87.829  113.481 1.00 28.77  ? 1215 VAL A CG1 1 
ATOM   9493  C  CG2 . VAL A 1 1215 ? 114.979 86.647  111.496 1.00 30.17  ? 1215 VAL A CG2 1 
ATOM   9494  N  N   . THR A 1 1216 ? 117.859 85.526  115.003 1.00 32.53  ? 1216 THR A N   1 
ATOM   9495  C  CA  . THR A 1 1216 ? 118.454 85.537  116.312 1.00 33.27  ? 1216 THR A CA  1 
ATOM   9496  C  C   . THR A 1 1216 ? 118.643 87.009  116.670 1.00 33.36  ? 1216 THR A C   1 
ATOM   9497  O  O   . THR A 1 1216 ? 118.960 87.817  115.802 1.00 33.80  ? 1216 THR A O   1 
ATOM   9498  C  CB  . THR A 1 1216 ? 119.789 84.788  116.241 1.00 34.14  ? 1216 THR A CB  1 
ATOM   9499  O  OG1 . THR A 1 1216 ? 119.536 83.396  116.454 1.00 35.81  ? 1216 THR A OG1 1 
ATOM   9500  C  CG2 . THR A 1 1216 ? 120.803 85.276  117.279 1.00 35.75  ? 1216 THR A CG2 1 
ATOM   9501  N  N   . LEU A 1 1217 ? 118.421 87.360  117.933 1.00 33.44  ? 1217 LEU A N   1 
ATOM   9502  C  CA  . LEU A 1 1217 ? 118.526 88.747  118.359 1.00 33.75  ? 1217 LEU A CA  1 
ATOM   9503  C  C   . LEU A 1 1217 ? 119.797 88.987  119.156 1.00 34.45  ? 1217 LEU A C   1 
ATOM   9504  O  O   . LEU A 1 1217 ? 120.360 88.040  119.719 1.00 35.57  ? 1217 LEU A O   1 
ATOM   9505  C  CB  . LEU A 1 1217 ? 117.296 89.152  119.170 1.00 32.95  ? 1217 LEU A CB  1 
ATOM   9506  C  CG  . LEU A 1 1217 ? 115.998 89.277  118.369 1.00 33.84  ? 1217 LEU A CG  1 
ATOM   9507  C  CD1 . LEU A 1 1217 ? 114.816 89.489  119.314 1.00 34.69  ? 1217 LEU A CD1 1 
ATOM   9508  C  CD2 . LEU A 1 1217 ? 116.069 90.391  117.333 1.00 32.65  ? 1217 LEU A CD2 1 
ATOM   9509  N  N   . PRO A 1 1218 ? 120.277 90.240  119.191 1.00 34.56  ? 1218 PRO A N   1 
ATOM   9510  C  CA  . PRO A 1 1218 ? 121.358 90.545  120.119 1.00 34.91  ? 1218 PRO A CA  1 
ATOM   9511  C  C   . PRO A 1 1218 ? 120.874 90.361  121.544 1.00 34.73  ? 1218 PRO A C   1 
ATOM   9512  O  O   . PRO A 1 1218 ? 119.674 90.462  121.806 1.00 34.30  ? 1218 PRO A O   1 
ATOM   9513  C  CB  . PRO A 1 1218 ? 121.638 92.028  119.867 1.00 35.18  ? 1218 PRO A CB  1 
ATOM   9514  C  CG  . PRO A 1 1218 ? 121.064 92.318  118.528 1.00 35.01  ? 1218 PRO A CG  1 
ATOM   9515  C  CD  . PRO A 1 1218 ? 119.879 91.418  118.398 1.00 34.63  ? 1218 PRO A CD  1 
ATOM   9516  N  N   . SER A 1 1219 ? 121.803 90.091  122.454 1.00 35.23  ? 1219 SER A N   1 
ATOM   9517  C  CA  . SER A 1 1219 ? 121.485 89.949  123.864 1.00 35.58  ? 1219 SER A CA  1 
ATOM   9518  C  C   . SER A 1 1219 ? 120.702 91.141  124.381 1.00 35.04  ? 1219 SER A C   1 
ATOM   9519  O  O   . SER A 1 1219 ? 121.020 92.272  124.076 1.00 35.68  ? 1219 SER A O   1 
ATOM   9520  C  CB  . SER A 1 1219 ? 122.763 89.770  124.681 1.00 36.25  ? 1219 SER A CB  1 
ATOM   9521  O  OG  . SER A 1 1219 ? 123.296 88.473  124.472 1.00 37.56  ? 1219 SER A OG  1 
ATOM   9522  N  N   . GLY A 1 1220 ? 119.655 90.884  125.140 1.00 34.88  ? 1220 GLY A N   1 
ATOM   9523  C  CA  . GLY A 1 1220 ? 118.886 91.967  125.739 1.00 35.31  ? 1220 GLY A CA  1 
ATOM   9524  C  C   . GLY A 1 1220 ? 117.755 92.534  124.907 1.00 35.10  ? 1220 GLY A C   1 
ATOM   9525  O  O   . GLY A 1 1220 ? 116.996 93.363  125.397 1.00 34.76  ? 1220 GLY A O   1 
ATOM   9526  N  N   . TYR A 1 1221 ? 117.648 92.102  123.653 1.00 35.80  ? 1221 TYR A N   1 
ATOM   9527  C  CA  . TYR A 1 1221 ? 116.526 92.492  122.796 1.00 36.07  ? 1221 TYR A CA  1 
ATOM   9528  C  C   . TYR A 1 1221 ? 115.398 91.468  122.866 1.00 36.23  ? 1221 TYR A C   1 
ATOM   9529  O  O   . TYR A 1 1221 ? 115.647 90.280  123.067 1.00 36.43  ? 1221 TYR A O   1 
ATOM   9530  C  CB  . TYR A 1 1221 ? 116.981 92.674  121.352 1.00 36.23  ? 1221 TYR A CB  1 
ATOM   9531  C  CG  . TYR A 1 1221 ? 117.695 93.971  121.089 1.00 36.00  ? 1221 TYR A CG  1 
ATOM   9532  C  CD1 . TYR A 1 1221 ? 117.045 95.021  120.456 1.00 35.06  ? 1221 TYR A CD1 1 
ATOM   9533  C  CD2 . TYR A 1 1221 ? 119.029 94.145  121.455 1.00 36.94  ? 1221 TYR A CD2 1 
ATOM   9534  C  CE1 . TYR A 1 1221 ? 117.692 96.223  120.205 1.00 36.01  ? 1221 TYR A CE1 1 
ATOM   9535  C  CE2 . TYR A 1 1221 ? 119.694 95.352  121.201 1.00 37.95  ? 1221 TYR A CE2 1 
ATOM   9536  C  CZ  . TYR A 1 1221 ? 119.015 96.385  120.575 1.00 37.86  ? 1221 TYR A CZ  1 
ATOM   9537  O  OH  . TYR A 1 1221 ? 119.653 97.588  120.324 1.00 39.29  ? 1221 TYR A OH  1 
ATOM   9538  N  N   . VAL A 1 1222 ? 114.168 91.946  122.714 1.00 36.71  ? 1222 VAL A N   1 
ATOM   9539  C  CA  . VAL A 1 1222 ? 112.965 91.117  122.779 1.00 37.76  ? 1222 VAL A CA  1 
ATOM   9540  C  C   . VAL A 1 1222 ? 112.027 91.617  121.692 1.00 39.30  ? 1222 VAL A C   1 
ATOM   9541  O  O   . VAL A 1 1222 ? 111.969 92.815  121.437 1.00 39.70  ? 1222 VAL A O   1 
ATOM   9542  C  CB  . VAL A 1 1222 ? 112.260 91.220  124.178 1.00 37.15  ? 1222 VAL A CB  1 
ATOM   9543  C  CG1 . VAL A 1 1222 ? 110.989 90.388  124.221 1.00 35.91  ? 1222 VAL A CG1 1 
ATOM   9544  C  CG2 . VAL A 1 1222 ? 113.201 90.809  125.313 1.00 36.34  ? 1222 VAL A CG2 1 
ATOM   9545  N  N   . VAL A 1 1223 ? 111.320 90.711  121.032 1.00 41.61  ? 1223 VAL A N   1 
ATOM   9546  C  CA  . VAL A 1 1223 ? 110.360 91.094  119.997 1.00 44.10  ? 1223 VAL A CA  1 
ATOM   9547  C  C   . VAL A 1 1223 ? 109.022 91.322  120.655 1.00 45.86  ? 1223 VAL A C   1 
ATOM   9548  O  O   . VAL A 1 1223 ? 108.682 90.615  121.613 1.00 45.88  ? 1223 VAL A O   1 
ATOM   9549  C  CB  . VAL A 1 1223 ? 110.162 89.986  118.929 1.00 43.77  ? 1223 VAL A CB  1 
ATOM   9550  C  CG1 . VAL A 1 1223 ? 111.380 89.842  118.074 1.00 44.80  ? 1223 VAL A CG1 1 
ATOM   9551  C  CG2 . VAL A 1 1223 ? 109.836 88.682  119.577 1.00 43.81  ? 1223 VAL A CG2 1 
ATOM   9552  N  N   . ASP A 1 1224 ? 108.238 92.273  120.147 1.00 48.31  ? 1224 ASP A N   1 
ATOM   9553  C  CA  . ASP A 1 1224 ? 106.898 92.449  120.727 1.00 50.93  ? 1224 ASP A CA  1 
ATOM   9554  C  C   . ASP A 1 1224 ? 105.865 91.479  120.164 1.00 51.73  ? 1224 ASP A C   1 
ATOM   9555  O  O   . ASP A 1 1224 ? 106.222 90.463  119.553 1.00 51.86  ? 1224 ASP A O   1 
ATOM   9556  C  CB  . ASP A 1 1224 ? 106.404 93.918  120.730 1.00 51.51  ? 1224 ASP A CB  1 
ATOM   9557  C  CG  . ASP A 1 1224 ? 106.494 94.573  119.367 1.00 54.37  ? 1224 ASP A CG  1 
ATOM   9558  O  OD1 . ASP A 1 1224 ? 107.212 94.017  118.487 1.00 56.77  ? 1224 ASP A OD1 1 
ATOM   9559  O  OD2 . ASP A 1 1224 ? 105.858 95.647  119.195 1.00 55.41  ? 1224 ASP A OD2 1 
ATOM   9560  N  N   . ARG A 1 1225 ? 104.593 91.799  120.401 1.00 52.90  ? 1225 ARG A N   1 
ATOM   9561  C  CA  . ARG A 1 1225 ? 103.487 90.867  120.215 1.00 53.90  ? 1225 ARG A CA  1 
ATOM   9562  C  C   . ARG A 1 1225 ? 103.402 90.337  118.777 1.00 53.35  ? 1225 ARG A C   1 
ATOM   9563  O  O   . ARG A 1 1225 ? 103.401 89.115  118.555 1.00 53.87  ? 1225 ARG A O   1 
ATOM   9564  C  CB  . ARG A 1 1225 ? 102.160 91.491  120.713 1.00 54.98  ? 1225 ARG A CB  1 
ATOM   9565  C  CG  . ARG A 1 1225 ? 101.480 92.564  119.803 1.00 59.38  ? 1225 ARG A CG  1 
ATOM   9566  C  CD  . ARG A 1 1225 ? 102.257 93.889  119.706 1.00 65.78  ? 1225 ARG A CD  1 
ATOM   9567  N  NE  . ARG A 1 1225 ? 101.588 94.878  118.844 1.00 70.10  ? 1225 ARG A NE  1 
ATOM   9568  C  CZ  . ARG A 1 1225 ? 100.660 95.750  119.251 1.00 72.18  ? 1225 ARG A CZ  1 
ATOM   9569  N  NH1 . ARG A 1 1225 ? 100.250 95.777  120.520 1.00 72.75  ? 1225 ARG A NH1 1 
ATOM   9570  N  NH2 . ARG A 1 1225 ? 100.128 96.598  118.377 1.00 73.33  ? 1225 ARG A NH2 1 
ATOM   9571  N  N   . ASN A 1 1226 ? 103.357 91.248  117.809 1.00 51.96  ? 1226 ASN A N   1 
ATOM   9572  C  CA  . ASN A 1 1226 ? 103.433 90.854  116.412 1.00 50.84  ? 1226 ASN A CA  1 
ATOM   9573  C  C   . ASN A 1 1226 ? 104.613 91.541  115.744 1.00 48.96  ? 1226 ASN A C   1 
ATOM   9574  O  O   . ASN A 1 1226 ? 104.489 92.632  115.186 1.00 49.03  ? 1226 ASN A O   1 
ATOM   9575  C  CB  . ASN A 1 1226 ? 102.103 91.083  115.689 1.00 51.81  ? 1226 ASN A CB  1 
ATOM   9576  C  CG  . ASN A 1 1226 ? 100.984 90.202  116.252 1.00 54.43  ? 1226 ASN A CG  1 
ATOM   9577  O  OD1 . ASN A 1 1226 ? 100.623 89.167  115.665 1.00 57.44  ? 1226 ASN A OD1 1 
ATOM   9578  N  ND2 . ASN A 1 1226 ? 100.451 90.592  117.416 1.00 56.13  ? 1226 ASN A ND2 1 
ATOM   9579  N  N   . PRO A 1 1227 ? 105.782 90.899  115.827 1.00 46.95  ? 1227 PRO A N   1 
ATOM   9580  C  CA  . PRO A 1 1227 ? 107.040 91.486  115.420 1.00 45.63  ? 1227 PRO A CA  1 
ATOM   9581  C  C   . PRO A 1 1227 ? 107.208 91.653  113.907 1.00 44.40  ? 1227 PRO A C   1 
ATOM   9582  O  O   . PRO A 1 1227 ? 108.123 92.352  113.465 1.00 44.43  ? 1227 PRO A O   1 
ATOM   9583  C  CB  . PRO A 1 1227 ? 108.059 90.483  115.960 1.00 45.85  ? 1227 PRO A CB  1 
ATOM   9584  C  CG  . PRO A 1 1227 ? 107.339 89.197  115.954 1.00 46.13  ? 1227 PRO A CG  1 
ATOM   9585  C  CD  . PRO A 1 1227 ? 105.956 89.529  116.339 1.00 46.55  ? 1227 PRO A CD  1 
ATOM   9586  N  N   . ILE A 1 1228 ? 106.350 91.019  113.120 1.00 42.85  ? 1228 ILE A N   1 
ATOM   9587  C  CA  . ILE A 1 1228 ? 106.561 91.000  111.679 1.00 42.00  ? 1228 ILE A CA  1 
ATOM   9588  C  C   . ILE A 1 1228 ? 105.654 91.975  110.931 1.00 41.15  ? 1228 ILE A C   1 
ATOM   9589  O  O   . ILE A 1 1228 ? 104.450 91.974  111.127 1.00 40.70  ? 1228 ILE A O   1 
ATOM   9590  C  CB  . ILE A 1 1228 ? 106.483 89.554  111.089 1.00 42.31  ? 1228 ILE A CB  1 
ATOM   9591  C  CG1 . ILE A 1 1228 ? 107.777 88.788  111.365 1.00 41.23  ? 1228 ILE A CG1 1 
ATOM   9592  C  CG2 . ILE A 1 1228 ? 106.314 89.593  109.580 1.00 42.97  ? 1228 ILE A CG2 1 
ATOM   9593  C  CD1 . ILE A 1 1228 ? 107.787 88.035  112.611 1.00 40.38  ? 1228 ILE A CD1 1 
ATOM   9594  N  N   . SER A 1 1229 ? 106.256 92.808  110.086 1.00 40.70  ? 1229 SER A N   1 
ATOM   9595  C  CA  . SER A 1 1229 ? 105.511 93.699  109.185 1.00 40.31  ? 1229 SER A CA  1 
ATOM   9596  C  C   . SER A 1 1229 ? 106.145 93.741  107.776 1.00 40.77  ? 1229 SER A C   1 
ATOM   9597  O  O   . SER A 1 1229 ? 107.230 93.193  107.568 1.00 40.41  ? 1229 SER A O   1 
ATOM   9598  C  CB  . SER A 1 1229 ? 105.397 95.104  109.791 1.00 39.85  ? 1229 SER A CB  1 
ATOM   9599  O  OG  . SER A 1 1229 ? 106.655 95.583  110.250 1.00 38.99  ? 1229 SER A OG  1 
ATOM   9600  N  N   . GLU A 1 1230 ? 105.449 94.367  106.820 1.00 41.29  ? 1230 GLU A N   1 
ATOM   9601  C  CA  . GLU A 1 1230 ? 105.950 94.564  105.437 1.00 42.27  ? 1230 GLU A CA  1 
ATOM   9602  C  C   . GLU A 1 1230 ? 106.406 93.262  104.763 1.00 41.94  ? 1230 GLU A C   1 
ATOM   9603  O  O   . GLU A 1 1230 ? 107.448 93.218  104.099 1.00 41.97  ? 1230 GLU A O   1 
ATOM   9604  C  CB  . GLU A 1 1230 ? 107.066 95.627  105.399 1.00 42.69  ? 1230 GLU A CB  1 
ATOM   9605  C  CG  . GLU A 1 1230 ? 106.721 96.903  106.194 1.00 45.86  ? 1230 GLU A CG  1 
ATOM   9606  C  CD  . GLU A 1 1230 ? 107.838 97.949  106.232 1.00 49.95  ? 1230 GLU A CD  1 
ATOM   9607  O  OE1 . GLU A 1 1230 ? 107.495 99.145  106.353 1.00 50.89  ? 1230 GLU A OE1 1 
ATOM   9608  O  OE2 . GLU A 1 1230 ? 109.046 97.593  106.153 1.00 52.51  ? 1230 GLU A OE2 1 
ATOM   9609  N  N   . GLN A 1 1231 ? 105.613 92.213  104.974 1.00 41.41  ? 1231 GLN A N   1 
ATOM   9610  C  CA  . GLN A 1 1231 ? 105.787 90.895  104.368 1.00 41.47  ? 1231 GLN A CA  1 
ATOM   9611  C  C   . GLN A 1 1231 ? 105.519 90.976  102.888 1.00 41.42  ? 1231 GLN A C   1 
ATOM   9612  O  O   . GLN A 1 1231 ? 104.551 91.599  102.478 1.00 41.61  ? 1231 GLN A O   1 
ATOM   9613  C  CB  . GLN A 1 1231 ? 104.749 89.907  104.922 1.00 41.57  ? 1231 GLN A CB  1 
ATOM   9614  C  CG  . GLN A 1 1231 ? 104.812 89.602  106.402 1.00 42.90  ? 1231 GLN A CG  1 
ATOM   9615  C  CD  . GLN A 1 1231 ? 103.890 90.473  107.275 1.00 45.53  ? 1231 GLN A CD  1 
ATOM   9616  O  OE1 . GLN A 1 1231 ? 103.384 89.998  108.297 1.00 47.85  ? 1231 GLN A OE1 1 
ATOM   9617  N  NE2 . GLN A 1 1231 ? 103.691 91.745  106.898 1.00 44.39  ? 1231 GLN A NE2 1 
ATOM   9618  N  N   . THR A 1 1232 ? 106.344 90.324  102.082 1.00 41.31  ? 1232 THR A N   1 
ATOM   9619  C  CA  . THR A 1 1232 ? 106.013 90.159  100.669 1.00 41.64  ? 1232 THR A CA  1 
ATOM   9620  C  C   . THR A 1 1232 ? 104.814 89.205  100.530 1.00 41.41  ? 1232 THR A C   1 
ATOM   9621  O  O   . THR A 1 1232 ? 104.610 88.329  101.369 1.00 40.84  ? 1232 THR A O   1 
ATOM   9622  C  CB  . THR A 1 1232 ? 107.225 89.686  99.845  1.00 42.20  ? 1232 THR A CB  1 
ATOM   9623  O  OG1 . THR A 1 1232 ? 107.973 88.712  100.586 1.00 41.61  ? 1232 THR A OG1 1 
ATOM   9624  C  CG2 . THR A 1 1232 ? 108.131 90.861  99.536  1.00 42.41  ? 1232 THR A CG2 1 
ATOM   9625  N  N   . LYS A 1 1233 ? 104.003 89.394  99.499  1.00 41.62  ? 1233 LYS A N   1 
ATOM   9626  C  CA  . LYS A 1 1233 ? 102.756 88.633  99.396  1.00 42.04  ? 1233 LYS A CA  1 
ATOM   9627  C  C   . LYS A 1 1233 ? 102.844 87.462  98.438  1.00 42.30  ? 1233 LYS A C   1 
ATOM   9628  O  O   . LYS A 1 1233 ? 101.992 86.581  98.483  1.00 42.51  ? 1233 LYS A O   1 
ATOM   9629  C  CB  . LYS A 1 1233 ? 101.563 89.522  99.022  1.00 42.32  ? 1233 LYS A CB  1 
ATOM   9630  C  CG  . LYS A 1 1233 ? 101.453 90.767  99.861  1.00 43.63  ? 1233 LYS A CG  1 
ATOM   9631  C  CD  . LYS A 1 1233 ? 100.071 90.960  100.427 1.00 46.81  ? 1233 LYS A CD  1 
ATOM   9632  C  CE  . LYS A 1 1233 ? 100.132 91.909  101.628 1.00 48.66  ? 1233 LYS A CE  1 
ATOM   9633  N  NZ  . LYS A 1 1233 ? 98.891  91.807  102.458 1.00 51.92  ? 1233 LYS A NZ  1 
ATOM   9634  N  N   . VAL A 1 1234 ? 103.871 87.455  97.587  1.00 42.47  ? 1234 VAL A N   1 
ATOM   9635  C  CA  . VAL A 1 1234 ? 104.065 86.412  96.581  1.00 42.58  ? 1234 VAL A CA  1 
ATOM   9636  C  C   . VAL A 1 1234 ? 103.998 85.035  97.207  1.00 42.16  ? 1234 VAL A C   1 
ATOM   9637  O  O   . VAL A 1 1234 ? 103.337 84.134  96.684  1.00 43.07  ? 1234 VAL A O   1 
ATOM   9638  C  CB  . VAL A 1 1234 ? 105.474 86.446  95.965  1.00 43.31  ? 1234 VAL A CB  1 
ATOM   9639  C  CG1 . VAL A 1 1234 ? 105.417 86.159  94.462  1.00 42.67  ? 1234 VAL A CG1 1 
ATOM   9640  C  CG2 . VAL A 1 1234 ? 106.184 87.739  96.291  1.00 42.95  ? 1234 VAL A CG2 1 
ATOM   9641  N  N   . ASN A 1 1235 ? 104.713 84.889  98.318  1.00 40.48  ? 1235 ASN A N   1 
ATOM   9642  C  CA  . ASN A 1 1235 ? 104.988 83.607  98.924  1.00 39.43  ? 1235 ASN A CA  1 
ATOM   9643  C  C   . ASN A 1 1235 ? 104.902 83.833  100.425 1.00 38.68  ? 1235 ASN A C   1 
ATOM   9644  O  O   . ASN A 1 1235 ? 105.897 84.144  101.087 1.00 38.74  ? 1235 ASN A O   1 
ATOM   9645  C  CB  . ASN A 1 1235 ? 106.376 83.175  98.489  1.00 39.28  ? 1235 ASN A CB  1 
ATOM   9646  C  CG  . ASN A 1 1235 ? 106.746 81.808  98.962  1.00 38.65  ? 1235 ASN A CG  1 
ATOM   9647  O  OD1 . ASN A 1 1235 ? 105.889 80.972  99.246  1.00 38.27  ? 1235 ASN A OD1 1 
ATOM   9648  N  ND2 . ASN A 1 1235 ? 108.051 81.554  99.028  1.00 38.15  ? 1235 ASN A ND2 1 
ATOM   9649  N  N   . PRO A 1 1236 ? 103.688 83.733  100.968 1.00 38.14  ? 1236 PRO A N   1 
ATOM   9650  C  CA  . PRO A 1 1236 ? 103.442 84.154  102.347 1.00 36.85  ? 1236 PRO A CA  1 
ATOM   9651  C  C   . PRO A 1 1236 ? 104.109 83.286  103.402 1.00 35.86  ? 1236 PRO A C   1 
ATOM   9652  O  O   . PRO A 1 1236 ? 104.322 82.094  103.199 1.00 36.28  ? 1236 PRO A O   1 
ATOM   9653  C  CB  . PRO A 1 1236 ? 101.914 84.058  102.477 1.00 36.74  ? 1236 PRO A CB  1 
ATOM   9654  C  CG  . PRO A 1 1236 ? 101.500 83.100  101.446 1.00 38.09  ? 1236 PRO A CG  1 
ATOM   9655  C  CD  . PRO A 1 1236 ? 102.470 83.233  100.310 1.00 38.58  ? 1236 PRO A CD  1 
ATOM   9656  N  N   . ILE A 1 1237 ? 104.437 83.905  104.523 1.00 34.75  ? 1237 ILE A N   1 
ATOM   9657  C  CA  . ILE A 1 1237 ? 104.878 83.192  105.704 1.00 33.76  ? 1237 ILE A CA  1 
ATOM   9658  C  C   . ILE A 1 1237 ? 103.718 82.360  106.229 1.00 33.67  ? 1237 ILE A C   1 
ATOM   9659  O  O   . ILE A 1 1237 ? 102.687 82.896  106.609 1.00 33.52  ? 1237 ILE A O   1 
ATOM   9660  C  CB  . ILE A 1 1237 ? 105.348 84.170  106.780 1.00 32.58  ? 1237 ILE A CB  1 
ATOM   9661  C  CG1 . ILE A 1 1237 ? 106.545 84.958  106.259 1.00 32.76  ? 1237 ILE A CG1 1 
ATOM   9662  C  CG2 . ILE A 1 1237 ? 105.693 83.423  108.060 1.00 32.39  ? 1237 ILE A CG2 1 
ATOM   9663  C  CD1 . ILE A 1 1237 ? 106.893 86.171  107.080 1.00 32.78  ? 1237 ILE A CD1 1 
ATOM   9664  N  N   . GLN A 1 1238 ? 103.889 81.048  106.240 1.00 34.05  ? 1238 GLN A N   1 
ATOM   9665  C  CA  . GLN A 1 1238 ? 102.827 80.155  106.664 1.00 34.48  ? 1238 GLN A CA  1 
ATOM   9666  C  C   . GLN A 1 1238 ? 102.741 80.026  108.181 1.00 34.29  ? 1238 GLN A C   1 
ATOM   9667  O  O   . GLN A 1 1238 ? 101.708 79.652  108.711 1.00 34.32  ? 1238 GLN A O   1 
ATOM   9668  C  CB  . GLN A 1 1238 ? 103.007 78.777  106.038 1.00 35.07  ? 1238 GLN A CB  1 
ATOM   9669  C  CG  . GLN A 1 1238 ? 102.950 78.739  104.519 1.00 36.10  ? 1238 GLN A CG  1 
ATOM   9670  C  CD  . GLN A 1 1238 ? 101.630 79.206  103.961 1.00 37.07  ? 1238 GLN A CD  1 
ATOM   9671  O  OE1 . GLN A 1 1238 ? 100.577 78.748  104.356 1.00 37.00  ? 1238 GLN A OE1 1 
ATOM   9672  N  NE2 . GLN A 1 1238 ? 101.688 80.128  103.025 1.00 41.84  ? 1238 GLN A NE2 1 
ATOM   9673  N  N   . LYS A 1 1239 ? 103.830 80.317  108.879 1.00 34.69  ? 1239 LYS A N   1 
ATOM   9674  C  CA  . LYS A 1 1239 ? 103.838 80.224  110.330 1.00 34.80  ? 1239 LYS A CA  1 
ATOM   9675  C  C   . LYS A 1 1239 ? 104.921 81.088  110.952 1.00 34.52  ? 1239 LYS A C   1 
ATOM   9676  O  O   . LYS A 1 1239 ? 106.051 81.132  110.465 1.00 35.10  ? 1239 LYS A O   1 
ATOM   9677  C  CB  . LYS A 1 1239 ? 104.008 78.774  110.785 1.00 35.19  ? 1239 LYS A CB  1 
ATOM   9678  C  CG  . LYS A 1 1239 ? 103.979 78.602  112.300 1.00 36.34  ? 1239 LYS A CG  1 
ATOM   9679  C  CD  . LYS A 1 1239 ? 103.838 77.151  112.678 1.00 41.22  ? 1239 LYS A CD  1 
ATOM   9680  C  CE  . LYS A 1 1239 ? 103.321 76.992  114.111 1.00 43.79  ? 1239 LYS A CE  1 
ATOM   9681  N  NZ  . LYS A 1 1239 ? 102.703 75.638  114.280 1.00 45.54  ? 1239 LYS A NZ  1 
ATOM   9682  N  N   . THR A 1 1240 ? 104.567 81.754  112.042 1.00 33.90  ? 1240 THR A N   1 
ATOM   9683  C  CA  . THR A 1 1240 ? 105.510 82.550  112.794 1.00 33.78  ? 1240 THR A CA  1 
ATOM   9684  C  C   . THR A 1 1240 ? 105.583 81.968  114.190 1.00 34.14  ? 1240 THR A C   1 
ATOM   9685  O  O   . THR A 1 1240 ? 104.567 81.879  114.881 1.00 33.58  ? 1240 THR A O   1 
ATOM   9686  C  CB  . THR A 1 1240 ? 105.049 84.011  112.870 1.00 33.32  ? 1240 THR A CB  1 
ATOM   9687  O  OG1 . THR A 1 1240 ? 104.747 84.488  111.550 1.00 34.08  ? 1240 THR A OG1 1 
ATOM   9688  C  CG2 . THR A 1 1240 ? 106.112 84.889  113.507 1.00 31.86  ? 1240 THR A CG2 1 
ATOM   9689  N  N   . GLU A 1 1241 ? 106.773 81.542  114.605 1.00 34.81  ? 1241 GLU A N   1 
ATOM   9690  C  CA  . GLU A 1 1241 ? 106.915 81.091  115.974 1.00 35.55  ? 1241 GLU A CA  1 
ATOM   9691  C  C   . GLU A 1 1241 ? 107.972 81.866  116.756 1.00 35.63  ? 1241 GLU A C   1 
ATOM   9692  O  O   . GLU A 1 1241 ? 109.103 82.088  116.297 1.00 36.12  ? 1241 GLU A O   1 
ATOM   9693  C  CB  . GLU A 1 1241 ? 107.029 79.552  116.087 1.00 35.84  ? 1241 GLU A CB  1 
ATOM   9694  C  CG  . GLU A 1 1241 ? 108.414 78.949  116.093 1.00 39.34  ? 1241 GLU A CG  1 
ATOM   9695  C  CD  . GLU A 1 1241 ? 108.409 77.428  116.317 1.00 43.92  ? 1241 GLU A CD  1 
ATOM   9696  O  OE1 . GLU A 1 1241 ? 107.644 76.707  115.627 1.00 43.59  ? 1241 GLU A OE1 1 
ATOM   9697  O  OE2 . GLU A 1 1241 ? 109.184 76.955  117.192 1.00 46.01  ? 1241 GLU A OE2 1 
ATOM   9698  N  N   . ILE A 1 1242 ? 107.557 82.331  117.926 1.00 35.26  ? 1242 ILE A N   1 
ATOM   9699  C  CA  . ILE A 1 1242 ? 108.398 83.139  118.766 1.00 35.20  ? 1242 ILE A CA  1 
ATOM   9700  C  C   . ILE A 1 1242 ? 108.850 82.266  119.917 1.00 35.46  ? 1242 ILE A C   1 
ATOM   9701  O  O   . ILE A 1 1242 ? 108.018 81.675  120.601 1.00 35.41  ? 1242 ILE A O   1 
ATOM   9702  C  CB  . ILE A 1 1242 ? 107.633 84.389  119.235 1.00 34.82  ? 1242 ILE A CB  1 
ATOM   9703  C  CG1 . ILE A 1 1242 ? 107.169 85.184  118.003 1.00 35.11  ? 1242 ILE A CG1 1 
ATOM   9704  C  CG2 . ILE A 1 1242 ? 108.503 85.246  120.150 1.00 34.21  ? 1242 ILE A CG2 1 
ATOM   9705  C  CD1 . ILE A 1 1242 ? 106.234 86.348  118.289 1.00 35.38  ? 1242 ILE A CD1 1 
ATOM   9706  N  N   . ARG A 1 1243 ? 110.166 82.143  120.094 1.00 35.84  ? 1243 ARG A N   1 
ATOM   9707  C  CA  . ARG A 1 1243 ? 110.718 81.292  121.159 1.00 36.45  ? 1243 ARG A CA  1 
ATOM   9708  C  C   . ARG A 1 1243 ? 111.830 81.949  121.973 1.00 36.83  ? 1243 ARG A C   1 
ATOM   9709  O  O   . ARG A 1 1243 ? 112.223 83.088  121.701 1.00 36.96  ? 1243 ARG A O   1 
ATOM   9710  C  CB  . ARG A 1 1243 ? 111.155 79.905  120.647 1.00 36.36  ? 1243 ARG A CB  1 
ATOM   9711  C  CG  . ARG A 1 1243 ? 111.434 79.802  119.168 1.00 37.31  ? 1243 ARG A CG  1 
ATOM   9712  C  CD  . ARG A 1 1243 ? 112.890 79.585  118.826 1.00 38.50  ? 1243 ARG A CD  1 
ATOM   9713  N  NE  . ARG A 1 1243 ? 113.177 78.197  118.468 1.00 39.29  ? 1243 ARG A NE  1 
ATOM   9714  C  CZ  . ARG A 1 1243 ? 114.242 77.795  117.770 1.00 39.75  ? 1243 ARG A CZ  1 
ATOM   9715  N  NH1 . ARG A 1 1243 ? 115.139 78.670  117.319 1.00 38.27  ? 1243 ARG A NH1 1 
ATOM   9716  N  NH2 . ARG A 1 1243 ? 114.413 76.504  117.522 1.00 39.84  ? 1243 ARG A NH2 1 
ATOM   9717  N  N   . TYR A 1 1244 ? 112.294 81.231  122.993 1.00 37.12  ? 1244 TYR A N   1 
ATOM   9718  C  CA  . TYR A 1 1244 ? 113.392 81.662  123.832 1.00 37.77  ? 1244 TYR A CA  1 
ATOM   9719  C  C   . TYR A 1 1244 ? 113.143 83.070  124.384 1.00 37.84  ? 1244 TYR A C   1 
ATOM   9720  O  O   . TYR A 1 1244 ? 113.945 83.984  124.169 1.00 38.06  ? 1244 TYR A O   1 
ATOM   9721  C  CB  . TYR A 1 1244 ? 114.724 81.590  123.055 1.00 38.46  ? 1244 TYR A CB  1 
ATOM   9722  C  CG  . TYR A 1 1244 ? 115.025 80.254  122.392 1.00 38.78  ? 1244 TYR A CG  1 
ATOM   9723  C  CD1 . TYR A 1 1244 ? 114.384 79.071  122.803 1.00 39.40  ? 1244 TYR A CD1 1 
ATOM   9724  C  CD2 . TYR A 1 1244 ? 115.973 80.164  121.373 1.00 39.56  ? 1244 TYR A CD2 1 
ATOM   9725  C  CE1 . TYR A 1 1244 ? 114.656 77.845  122.196 1.00 38.98  ? 1244 TYR A CE1 1 
ATOM   9726  C  CE2 . TYR A 1 1244 ? 116.262 78.936  120.760 1.00 40.52  ? 1244 TYR A CE2 1 
ATOM   9727  C  CZ  . TYR A 1 1244 ? 115.600 77.783  121.183 1.00 40.74  ? 1244 TYR A CZ  1 
ATOM   9728  O  OH  . TYR A 1 1244 ? 115.882 76.573  120.592 1.00 41.50  ? 1244 TYR A OH  1 
ATOM   9729  N  N   . GLY A 1 1245 ? 112.016 83.240  125.078 1.00 37.65  ? 1245 GLY A N   1 
ATOM   9730  C  CA  . GLY A 1 1245 ? 111.653 84.523  125.683 1.00 36.98  ? 1245 GLY A CA  1 
ATOM   9731  C  C   . GLY A 1 1245 ? 111.799 85.666  124.704 1.00 37.13  ? 1245 GLY A C   1 
ATOM   9732  O  O   . GLY A 1 1245 ? 112.564 86.603  124.958 1.00 37.66  ? 1245 GLY A O   1 
ATOM   9733  N  N   . GLY A 1 1246 ? 111.096 85.561  123.570 1.00 36.49  ? 1246 GLY A N   1 
ATOM   9734  C  CA  . GLY A 1 1246 ? 111.090 86.586  122.518 1.00 35.94  ? 1246 GLY A CA  1 
ATOM   9735  C  C   . GLY A 1 1246 ? 112.447 86.907  121.910 1.00 36.27  ? 1246 GLY A C   1 
ATOM   9736  O  O   . GLY A 1 1246 ? 112.670 88.012  121.399 1.00 36.36  ? 1246 GLY A O   1 
ATOM   9737  N  N   . THR A 1 1247 ? 113.341 85.921  121.936 1.00 36.28  ? 1247 THR A N   1 
ATOM   9738  C  CA  . THR A 1 1247 ? 114.754 86.114  121.615 1.00 36.08  ? 1247 THR A CA  1 
ATOM   9739  C  C   . THR A 1 1247 ? 115.090 85.565  120.246 1.00 35.78  ? 1247 THR A C   1 
ATOM   9740  O  O   . THR A 1 1247 ? 116.097 85.939  119.635 1.00 36.04  ? 1247 THR A O   1 
ATOM   9741  C  CB  . THR A 1 1247 ? 115.594 85.456  122.716 1.00 36.42  ? 1247 THR A CB  1 
ATOM   9742  O  OG1 . THR A 1 1247 ? 116.014 86.470  123.637 1.00 37.79  ? 1247 THR A OG1 1 
ATOM   9743  C  CG2 . THR A 1 1247 ? 116.798 84.714  122.198 1.00 37.89  ? 1247 THR A CG2 1 
ATOM   9744  N  N   . SER A 1 1248 ? 114.225 84.676  119.771 1.00 34.96  ? 1248 SER A N   1 
ATOM   9745  C  CA  . SER A 1 1248 ? 114.410 84.002  118.511 1.00 34.66  ? 1248 SER A CA  1 
ATOM   9746  C  C   . SER A 1 1248 ? 113.077 83.903  117.783 1.00 34.00  ? 1248 SER A C   1 
ATOM   9747  O  O   . SER A 1 1248 ? 112.070 83.563  118.402 1.00 34.62  ? 1248 SER A O   1 
ATOM   9748  C  CB  . SER A 1 1248 ? 114.950 82.612  118.770 1.00 34.74  ? 1248 SER A CB  1 
ATOM   9749  O  OG  . SER A 1 1248 ? 114.775 81.798  117.626 1.00 36.10  ? 1248 SER A OG  1 
ATOM   9750  N  N   . VAL A 1 1249 ? 113.064 84.204  116.488 1.00 32.93  ? 1249 VAL A N   1 
ATOM   9751  C  CA  . VAL A 1 1249 ? 111.842 84.104  115.691 1.00 32.16  ? 1249 VAL A CA  1 
ATOM   9752  C  C   . VAL A 1 1249 ? 112.054 83.183  114.485 1.00 32.41  ? 1249 VAL A C   1 
ATOM   9753  O  O   . VAL A 1 1249 ? 112.974 83.382  113.685 1.00 32.78  ? 1249 VAL A O   1 
ATOM   9754  C  CB  . VAL A 1 1249 ? 111.331 85.507  115.204 1.00 31.94  ? 1249 VAL A CB  1 
ATOM   9755  C  CG1 . VAL A 1 1249 ? 110.109 85.370  114.298 1.00 30.32  ? 1249 VAL A CG1 1 
ATOM   9756  C  CG2 . VAL A 1 1249 ? 111.004 86.410  116.383 1.00 31.73  ? 1249 VAL A CG2 1 
ATOM   9757  N  N   . VAL A 1 1250 ? 111.190 82.182  114.359 1.00 32.03  ? 1250 VAL A N   1 
ATOM   9758  C  CA  . VAL A 1 1250 ? 111.247 81.243  113.243 1.00 31.89  ? 1250 VAL A CA  1 
ATOM   9759  C  C   . VAL A 1 1250 ? 110.067 81.455  112.305 1.00 31.81  ? 1250 VAL A C   1 
ATOM   9760  O  O   . VAL A 1 1250 ? 108.906 81.434  112.736 1.00 31.45  ? 1250 VAL A O   1 
ATOM   9761  C  CB  . VAL A 1 1250 ? 111.249 79.777  113.719 1.00 31.84  ? 1250 VAL A CB  1 
ATOM   9762  C  CG1 . VAL A 1 1250 ? 111.530 78.839  112.552 1.00 31.25  ? 1250 VAL A CG1 1 
ATOM   9763  C  CG2 . VAL A 1 1250 ? 112.268 79.581  114.815 1.00 31.66  ? 1250 VAL A CG2 1 
ATOM   9764  N  N   . LEU A 1 1251 ? 110.376 81.643  111.025 1.00 31.83  ? 1251 LEU A N   1 
ATOM   9765  C  CA  . LEU A 1 1251 ? 109.361 81.847  110.002 1.00 31.95  ? 1251 LEU A CA  1 
ATOM   9766  C  C   . LEU A 1 1251 ? 109.432 80.731  108.988 1.00 32.13  ? 1251 LEU A C   1 
ATOM   9767  O  O   . LEU A 1 1251 ? 110.525 80.384  108.527 1.00 32.90  ? 1251 LEU A O   1 
ATOM   9768  C  CB  . LEU A 1 1251 ? 109.551 83.198  109.317 1.00 32.23  ? 1251 LEU A CB  1 
ATOM   9769  C  CG  . LEU A 1 1251 ? 109.753 84.330  110.339 1.00 33.16  ? 1251 LEU A CG  1 
ATOM   9770  C  CD1 . LEU A 1 1251 ? 111.221 84.774  110.421 1.00 32.00  ? 1251 LEU A CD1 1 
ATOM   9771  C  CD2 . LEU A 1 1251 ? 108.860 85.489  109.984 1.00 34.21  ? 1251 LEU A CD2 1 
ATOM   9772  N  N   . TYR A 1 1252 ? 108.267 80.175  108.652 1.00 31.40  ? 1252 TYR A N   1 
ATOM   9773  C  CA  . TYR A 1 1252 ? 108.160 79.001  107.803 1.00 31.05  ? 1252 TYR A CA  1 
ATOM   9774  C  C   . TYR A 1 1252 ? 107.536 79.351  106.461 1.00 31.19  ? 1252 TYR A C   1 
ATOM   9775  O  O   . TYR A 1 1252 ? 106.571 80.115  106.406 1.00 30.97  ? 1252 TYR A O   1 
ATOM   9776  C  CB  . TYR A 1 1252 ? 107.242 77.983  108.452 1.00 31.08  ? 1252 TYR A CB  1 
ATOM   9777  C  CG  . TYR A 1 1252 ? 107.731 77.361  109.717 1.00 30.57  ? 1252 TYR A CG  1 
ATOM   9778  C  CD1 . TYR A 1 1252 ? 107.691 78.060  110.922 1.00 30.81  ? 1252 TYR A CD1 1 
ATOM   9779  C  CD2 . TYR A 1 1252 ? 108.177 76.049  109.732 1.00 30.18  ? 1252 TYR A CD2 1 
ATOM   9780  C  CE1 . TYR A 1 1252 ? 108.126 77.477  112.102 1.00 30.05  ? 1252 TYR A CE1 1 
ATOM   9781  C  CE2 . TYR A 1 1252 ? 108.612 75.456  110.904 1.00 30.30  ? 1252 TYR A CE2 1 
ATOM   9782  C  CZ  . TYR A 1 1252 ? 108.576 76.173  112.085 1.00 31.43  ? 1252 TYR A CZ  1 
ATOM   9783  O  OH  . TYR A 1 1252 ? 109.008 75.589  113.261 1.00 33.43  ? 1252 TYR A OH  1 
ATOM   9784  N  N   . TYR A 1 1253 ? 108.070 78.760  105.393 1.00 31.06  ? 1253 TYR A N   1 
ATOM   9785  C  CA  . TYR A 1 1253 ? 107.565 78.934  104.037 1.00 30.87  ? 1253 TYR A CA  1 
ATOM   9786  C  C   . TYR A 1 1253 ? 107.375 77.560  103.426 1.00 31.53  ? 1253 TYR A C   1 
ATOM   9787  O  O   . TYR A 1 1253 ? 108.089 76.622  103.777 1.00 32.28  ? 1253 TYR A O   1 
ATOM   9788  C  CB  . TYR A 1 1253 ? 108.583 79.683  103.190 1.00 30.81  ? 1253 TYR A CB  1 
ATOM   9789  C  CG  . TYR A 1 1253 ? 108.898 81.076  103.655 1.00 29.94  ? 1253 TYR A CG  1 
ATOM   9790  C  CD1 . TYR A 1 1253 ? 109.741 81.293  104.740 1.00 29.39  ? 1253 TYR A CD1 1 
ATOM   9791  C  CD2 . TYR A 1 1253 ? 108.372 82.185  102.989 1.00 29.70  ? 1253 TYR A CD2 1 
ATOM   9792  C  CE1 . TYR A 1 1253 ? 110.043 82.572  105.171 1.00 29.54  ? 1253 TYR A CE1 1 
ATOM   9793  C  CE2 . TYR A 1 1253 ? 108.667 83.471  103.406 1.00 30.08  ? 1253 TYR A CE2 1 
ATOM   9794  C  CZ  . TYR A 1 1253 ? 109.507 83.658  104.502 1.00 29.87  ? 1253 TYR A CZ  1 
ATOM   9795  O  OH  . TYR A 1 1253 ? 109.810 84.931  104.933 1.00 28.95  ? 1253 TYR A OH  1 
ATOM   9796  N  N   . ASP A 1 1254 ? 106.436 77.430  102.502 1.00 31.50  ? 1254 ASP A N   1 
ATOM   9797  C  CA  . ASP A 1 1254 ? 106.218 76.158  101.843 1.00 32.19  ? 1254 ASP A CA  1 
ATOM   9798  C  C   . ASP A 1 1254 ? 107.428 75.741  101.047 1.00 32.64  ? 1254 ASP A C   1 
ATOM   9799  O  O   . ASP A 1 1254 ? 107.760 74.550  100.962 1.00 33.10  ? 1254 ASP A O   1 
ATOM   9800  C  CB  . ASP A 1 1254 ? 105.014 76.240  100.920 1.00 32.67  ? 1254 ASP A CB  1 
ATOM   9801  C  CG  . ASP A 1 1254 ? 103.711 76.271  101.678 1.00 34.24  ? 1254 ASP A CG  1 
ATOM   9802  O  OD1 . ASP A 1 1254 ? 103.674 75.802  102.848 1.00 33.43  ? 1254 ASP A OD1 1 
ATOM   9803  O  OD2 . ASP A 1 1254 ? 102.716 76.761  101.094 1.00 37.35  ? 1254 ASP A OD2 1 
ATOM   9804  N  N   . ASN A 1 1255 ? 108.063 76.742  100.448 1.00 32.65  ? 1255 ASN A N   1 
ATOM   9805  C  CA  . ASN A 1 1255 ? 109.243 76.585  99.611  1.00 33.05  ? 1255 ASN A CA  1 
ATOM   9806  C  C   . ASN A 1 1255 ? 109.671 77.962  99.110  1.00 33.15  ? 1255 ASN A C   1 
ATOM   9807  O  O   . ASN A 1 1255 ? 108.950 78.940  99.310  1.00 32.69  ? 1255 ASN A O   1 
ATOM   9808  C  CB  . ASN A 1 1255 ? 108.962 75.623  98.456  1.00 33.48  ? 1255 ASN A CB  1 
ATOM   9809  C  CG  . ASN A 1 1255 ? 107.633 75.886  97.791  1.00 33.41  ? 1255 ASN A CG  1 
ATOM   9810  O  OD1 . ASN A 1 1255 ? 107.460 76.903  97.125  1.00 35.62  ? 1255 ASN A OD1 1 
ATOM   9811  N  ND2 . ASN A 1 1255 ? 106.685 74.969  97.958  1.00 30.84  ? 1255 ASN A ND2 1 
ATOM   9812  N  N   . MET A 1 1256 ? 110.849 78.050  98.497  1.00 33.79  ? 1256 MET A N   1 
ATOM   9813  C  CA  . MET A 1 1256 ? 111.308 79.311  97.911  1.00 34.15  ? 1256 MET A CA  1 
ATOM   9814  C  C   . MET A 1 1256 ? 111.935 79.101  96.556  1.00 35.31  ? 1256 MET A C   1 
ATOM   9815  O  O   . MET A 1 1256 ? 112.633 78.105  96.328  1.00 35.62  ? 1256 MET A O   1 
ATOM   9816  C  CB  . MET A 1 1256 ? 112.358 79.991  98.789  1.00 33.63  ? 1256 MET A CB  1 
ATOM   9817  C  CG  . MET A 1 1256 ? 111.884 80.499  100.122 1.00 33.23  ? 1256 MET A CG  1 
ATOM   9818  S  SD  . MET A 1 1256 ? 113.217 81.437  100.881 1.00 34.06  ? 1256 MET A SD  1 
ATOM   9819  C  CE  . MET A 1 1256 ? 112.462 81.868  102.455 1.00 30.34  ? 1256 MET A CE  1 
ATOM   9820  N  N   . GLY A 1 1257 ? 111.698 80.068  95.674  1.00 35.89  ? 1257 GLY A N   1 
ATOM   9821  C  CA  . GLY A 1 1257 ? 112.470 80.236  94.451  1.00 36.85  ? 1257 GLY A CA  1 
ATOM   9822  C  C   . GLY A 1 1257 ? 113.190 81.575  94.446  1.00 37.00  ? 1257 GLY A C   1 
ATOM   9823  O  O   . GLY A 1 1257 ? 113.599 82.080  95.489  1.00 36.44  ? 1257 GLY A O   1 
ATOM   9824  N  N   . SER A 1 1258 ? 113.334 82.157  93.263  1.00 38.10  ? 1258 SER A N   1 
ATOM   9825  C  CA  . SER A 1 1258 ? 114.087 83.394  93.091  1.00 38.52  ? 1258 SER A CA  1 
ATOM   9826  C  C   . SER A 1 1258 ? 113.302 84.676  93.429  1.00 38.22  ? 1258 SER A C   1 
ATOM   9827  O  O   . SER A 1 1258 ? 113.881 85.766  93.455  1.00 38.48  ? 1258 SER A O   1 
ATOM   9828  C  CB  . SER A 1 1258 ? 114.623 83.472  91.671  1.00 39.29  ? 1258 SER A CB  1 
ATOM   9829  O  OG  . SER A 1 1258 ? 113.550 83.422  90.758  1.00 40.77  ? 1258 SER A OG  1 
ATOM   9830  N  N   . GLU A 1 1259 ? 112.000 84.569  93.684  1.00 37.73  ? 1259 GLU A N   1 
ATOM   9831  C  CA  . GLU A 1 1259 ? 111.275 85.715  94.233  1.00 37.28  ? 1259 GLU A CA  1 
ATOM   9832  C  C   . GLU A 1 1259 ? 111.986 86.139  95.514  1.00 37.16  ? 1259 GLU A C   1 
ATOM   9833  O  O   . GLU A 1 1259 ? 112.630 85.318  96.173  1.00 37.34  ? 1259 GLU A O   1 
ATOM   9834  C  CB  . GLU A 1 1259 ? 109.793 85.400  94.497  1.00 36.59  ? 1259 GLU A CB  1 
ATOM   9835  C  CG  . GLU A 1 1259 ? 109.490 84.550  95.732  1.00 35.43  ? 1259 GLU A CG  1 
ATOM   9836  C  CD  . GLU A 1 1259 ? 109.836 83.083  95.562  1.00 36.49  ? 1259 GLU A CD  1 
ATOM   9837  O  OE1 . GLU A 1 1259 ? 109.870 82.568  94.406  1.00 37.23  ? 1259 GLU A OE1 1 
ATOM   9838  O  OE2 . GLU A 1 1259 ? 110.071 82.438  96.600  1.00 35.61  ? 1259 GLU A OE2 1 
ATOM   9839  N  N   A ARG A 1 1260 ? 111.865 87.415  95.859  0.50 36.85  ? 1260 ARG A N   1 
ATOM   9840  N  N   B ARG A 1 1260 ? 111.898 87.419  95.860  0.50 37.14  ? 1260 ARG A N   1 
ATOM   9841  C  CA  A ARG A 1 1260 ? 112.514 87.947  97.040  0.50 36.22  ? 1260 ARG A CA  1 
ATOM   9842  C  CA  B ARG A 1 1260 ? 112.562 87.902  97.062  0.50 36.81  ? 1260 ARG A CA  1 
ATOM   9843  C  C   A ARG A 1 1260 ? 111.503 87.914  98.178  0.50 35.81  ? 1260 ARG A C   1 
ATOM   9844  C  C   B ARG A 1 1260 ? 111.568 87.960  98.209  0.50 36.15  ? 1260 ARG A C   1 
ATOM   9845  O  O   A ARG A 1 1260 ? 110.509 88.641  98.150  0.50 35.87  ? 1260 ARG A O   1 
ATOM   9846  O  O   B ARG A 1 1260 ? 110.660 88.794  98.220  0.50 36.18  ? 1260 ARG A O   1 
ATOM   9847  C  CB  A ARG A 1 1260 ? 113.025 89.371  96.771  0.50 36.17  ? 1260 ARG A CB  1 
ATOM   9848  C  CB  B ARG A 1 1260 ? 113.253 89.253  96.829  0.50 37.07  ? 1260 ARG A CB  1 
ATOM   9849  C  CG  A ARG A 1 1260 ? 113.668 89.559  95.380  0.50 36.36  ? 1260 ARG A CG  1 
ATOM   9850  C  CG  B ARG A 1 1260 ? 114.268 89.232  95.682  0.50 38.73  ? 1260 ARG A CG  1 
ATOM   9851  C  CD  A ARG A 1 1260 ? 115.162 89.224  95.349  0.50 35.05  ? 1260 ARG A CD  1 
ATOM   9852  C  CD  B ARG A 1 1260 ? 115.484 90.108  95.946  0.50 40.08  ? 1260 ARG A CD  1 
ATOM   9853  N  NE  A ARG A 1 1260 ? 115.466 88.237  94.315  0.50 34.46  ? 1260 ARG A NE  1 
ATOM   9854  N  NE  B ARG A 1 1260 ? 116.487 89.444  96.776  0.50 41.14  ? 1260 ARG A NE  1 
ATOM   9855  C  CZ  A ARG A 1 1260 ? 116.676 87.747  94.054  0.50 34.65  ? 1260 ARG A CZ  1 
ATOM   9856  C  CZ  B ARG A 1 1260 ? 117.087 89.990  97.833  0.50 41.01  ? 1260 ARG A CZ  1 
ATOM   9857  N  NH1 A ARG A 1 1260 ? 117.737 88.155  94.734  0.50 34.59  ? 1260 ARG A NH1 1 
ATOM   9858  N  NH1 B ARG A 1 1260 ? 116.810 91.235  98.211  0.50 39.54  ? 1260 ARG A NH1 1 
ATOM   9859  N  NH2 A ARG A 1 1260 ? 116.826 86.839  93.100  0.50 35.06  ? 1260 ARG A NH2 1 
ATOM   9860  N  NH2 B ARG A 1 1260 ? 117.977 89.277  98.514  0.50 41.48  ? 1260 ARG A NH2 1 
ATOM   9861  N  N   . ASN A 1 1261 ? 111.747 87.046  99.159  1.00 35.63  ? 1261 ASN A N   1 
ATOM   9862  C  CA  . ASN A 1 1261 ? 110.864 86.908  100.307 1.00 35.09  ? 1261 ASN A CA  1 
ATOM   9863  C  C   . ASN A 1 1261 ? 111.350 87.776  101.447 1.00 35.06  ? 1261 ASN A C   1 
ATOM   9864  O  O   . ASN A 1 1261 ? 112.328 87.437  102.122 1.00 35.40  ? 1261 ASN A O   1 
ATOM   9865  C  CB  . ASN A 1 1261 ? 110.781 85.450  100.740 1.00 34.79  ? 1261 ASN A CB  1 
ATOM   9866  C  CG  . ASN A 1 1261 ? 110.278 84.548  99.630  1.00 35.55  ? 1261 ASN A CG  1 
ATOM   9867  O  OD1 . ASN A 1 1261 ? 111.062 83.878  98.952  1.00 35.95  ? 1261 ASN A OD1 1 
ATOM   9868  N  ND2 . ASN A 1 1261 ? 108.975 84.546  99.420  1.00 34.44  ? 1261 ASN A ND2 1 
ATOM   9869  N  N   . CYS A 1 1262 ? 110.668 88.901  101.649 1.00 34.74  ? 1262 CYS A N   1 
ATOM   9870  C  CA  . CYS A 1 1262 ? 111.116 89.901  102.597 1.00 34.46  ? 1262 CYS A CA  1 
ATOM   9871  C  C   . CYS A 1 1262 ? 110.096 90.092  103.688 1.00 33.74  ? 1262 CYS A C   1 
ATOM   9872  O  O   . CYS A 1 1262 ? 108.924 89.750  103.521 1.00 33.88  ? 1262 CYS A O   1 
ATOM   9873  C  CB  . CYS A 1 1262 ? 111.355 91.237  101.900 1.00 34.82  ? 1262 CYS A CB  1 
ATOM   9874  S  SG  . CYS A 1 1262 ? 112.501 91.159  100.533 1.00 37.89  ? 1262 CYS A SG  1 
ATOM   9875  N  N   . PHE A 1 1263 ? 110.563 90.634  104.807 1.00 33.19  ? 1263 PHE A N   1 
ATOM   9876  C  CA  . PHE A 1 1263 ? 109.721 91.044  105.918 1.00 32.50  ? 1263 PHE A CA  1 
ATOM   9877  C  C   . PHE A 1 1263 ? 110.538 91.956  106.810 1.00 32.54  ? 1263 PHE A C   1 
ATOM   9878  O  O   . PHE A 1 1263 ? 111.765 92.018  106.686 1.00 33.36  ? 1263 PHE A O   1 
ATOM   9879  C  CB  . PHE A 1 1263 ? 109.212 89.833  106.708 1.00 31.95  ? 1263 PHE A CB  1 
ATOM   9880  C  CG  . PHE A 1 1263 ? 110.289 89.041  107.373 1.00 31.25  ? 1263 PHE A CG  1 
ATOM   9881  C  CD1 . PHE A 1 1263 ? 110.756 87.862  106.799 1.00 31.24  ? 1263 PHE A CD1 1 
ATOM   9882  C  CD2 . PHE A 1 1263 ? 110.834 89.457  108.582 1.00 29.60  ? 1263 PHE A CD2 1 
ATOM   9883  C  CE1 . PHE A 1 1263 ? 111.754 87.116  107.424 1.00 29.20  ? 1263 PHE A CE1 1 
ATOM   9884  C  CE2 . PHE A 1 1263 ? 111.826 88.724  109.197 1.00 28.36  ? 1263 PHE A CE2 1 
ATOM   9885  C  CZ  . PHE A 1 1263 ? 112.279 87.547  108.619 1.00 28.44  ? 1263 PHE A CZ  1 
ATOM   9886  N  N   . THR A 1 1264 ? 109.875 92.665  107.710 1.00 31.98  ? 1264 THR A N   1 
ATOM   9887  C  CA  . THR A 1 1264 ? 110.594 93.493  108.661 1.00 32.11  ? 1264 THR A CA  1 
ATOM   9888  C  C   . THR A 1 1264 ? 110.287 93.037  110.080 1.00 31.99  ? 1264 THR A C   1 
ATOM   9889  O  O   . THR A 1 1264 ? 109.123 92.785  110.425 1.00 31.71  ? 1264 THR A O   1 
ATOM   9890  C  CB  . THR A 1 1264 ? 110.260 94.966  108.459 1.00 32.40  ? 1264 THR A CB  1 
ATOM   9891  O  OG1 . THR A 1 1264 ? 110.642 95.350  107.130 1.00 31.89  ? 1264 THR A OG1 1 
ATOM   9892  C  CG2 . THR A 1 1264 ? 110.988 95.852  109.496 1.00 32.57  ? 1264 THR A CG2 1 
ATOM   9893  N  N   . LEU A 1 1265 ? 111.340 92.890  110.884 1.00 32.46  ? 1265 LEU A N   1 
ATOM   9894  C  CA  . LEU A 1 1265 ? 111.197 92.431  112.262 1.00 32.89  ? 1265 LEU A CA  1 
ATOM   9895  C  C   . LEU A 1 1265 ? 111.461 93.575  113.232 1.00 33.19  ? 1265 LEU A C   1 
ATOM   9896  O  O   . LEU A 1 1265 ? 112.510 94.221  113.162 1.00 33.48  ? 1265 LEU A O   1 
ATOM   9897  C  CB  . LEU A 1 1265 ? 112.117 91.233  112.547 1.00 32.81  ? 1265 LEU A CB  1 
ATOM   9898  C  CG  . LEU A 1 1265 ? 112.048 90.639  113.968 1.00 33.11  ? 1265 LEU A CG  1 
ATOM   9899  C  CD1 . LEU A 1 1265 ? 112.090 89.115  113.979 1.00 32.68  ? 1265 LEU A CD1 1 
ATOM   9900  C  CD2 . LEU A 1 1265 ? 113.147 91.187  114.856 1.00 32.23  ? 1265 LEU A CD2 1 
ATOM   9901  N  N   . THR A 1 1266 ? 110.505 93.837  114.120 1.00 33.18  ? 1266 THR A N   1 
ATOM   9902  C  CA  . THR A 1 1266 ? 110.699 94.859  115.147 1.00 33.85  ? 1266 THR A CA  1 
ATOM   9903  C  C   . THR A 1 1266 ? 111.008 94.243  116.504 1.00 33.95  ? 1266 THR A C   1 
ATOM   9904  O  O   . THR A 1 1266 ? 110.268 93.373  116.974 1.00 34.39  ? 1266 THR A O   1 
ATOM   9905  C  CB  . THR A 1 1266 ? 109.480 95.801  115.250 1.00 33.60  ? 1266 THR A CB  1 
ATOM   9906  O  OG1 . THR A 1 1266 ? 109.373 96.550  114.034 1.00 35.45  ? 1266 THR A OG1 1 
ATOM   9907  C  CG2 . THR A 1 1266 ? 109.633 96.781  116.401 1.00 32.28  ? 1266 THR A CG2 1 
ATOM   9908  N  N   . ALA A 1 1267 ? 112.095 94.695  117.127 1.00 34.11  ? 1267 ALA A N   1 
ATOM   9909  C  CA  . ALA A 1 1267 ? 112.453 94.256  118.475 1.00 34.33  ? 1267 ALA A CA  1 
ATOM   9910  C  C   . ALA A 1 1267 ? 112.859 95.441  119.352 1.00 34.82  ? 1267 ALA A C   1 
ATOM   9911  O  O   . ALA A 1 1267 ? 113.325 96.466  118.839 1.00 35.13  ? 1267 ALA A O   1 
ATOM   9912  C  CB  . ALA A 1 1267 ? 113.564 93.224  118.417 1.00 34.56  ? 1267 ALA A CB  1 
ATOM   9913  N  N   . TYR A 1 1268 ? 112.680 95.309  120.667 1.00 35.01  ? 1268 TYR A N   1 
ATOM   9914  C  CA  . TYR A 1 1268 ? 113.033 96.397  121.599 1.00 35.62  ? 1268 TYR A CA  1 
ATOM   9915  C  C   . TYR A 1 1268 ? 114.142 96.019  122.556 1.00 35.77  ? 1268 TYR A C   1 
ATOM   9916  O  O   . TYR A 1 1268 ? 114.203 94.880  123.028 1.00 35.79  ? 1268 TYR A O   1 
ATOM   9917  C  CB  . TYR A 1 1268 ? 111.812 96.868  122.392 1.00 35.43  ? 1268 TYR A CB  1 
ATOM   9918  C  CG  . TYR A 1 1268 ? 110.745 97.448  121.518 1.00 36.15  ? 1268 TYR A CG  1 
ATOM   9919  C  CD1 . TYR A 1 1268 ? 109.659 96.679  121.111 1.00 37.74  ? 1268 TYR A CD1 1 
ATOM   9920  C  CD2 . TYR A 1 1268 ? 110.831 98.758  121.065 1.00 37.12  ? 1268 TYR A CD2 1 
ATOM   9921  C  CE1 . TYR A 1 1268 ? 108.671 97.204  120.285 1.00 37.58  ? 1268 TYR A CE1 1 
ATOM   9922  C  CE2 . TYR A 1 1268 ? 109.855 99.290  120.239 1.00 37.93  ? 1268 TYR A CE2 1 
ATOM   9923  C  CZ  . TYR A 1 1268 ? 108.779 98.511  119.858 1.00 37.89  ? 1268 TYR A CZ  1 
ATOM   9924  O  OH  . TYR A 1 1268 ? 107.807 99.045  119.043 1.00 38.58  ? 1268 TYR A OH  1 
ATOM   9925  N  N   . ARG A 1 1269 ? 115.012 96.974  122.855 1.00 36.05  ? 1269 ARG A N   1 
ATOM   9926  C  CA  . ARG A 1 1269 ? 116.080 96.717  123.803 1.00 36.64  ? 1269 ARG A CA  1 
ATOM   9927  C  C   . ARG A 1 1269 ? 115.551 96.751  125.218 1.00 36.47  ? 1269 ARG A C   1 
ATOM   9928  O  O   . ARG A 1 1269 ? 115.340 97.816  125.790 1.00 36.61  ? 1269 ARG A O   1 
ATOM   9929  C  CB  . ARG A 1 1269 ? 117.216 97.713  123.651 1.00 37.25  ? 1269 ARG A CB  1 
ATOM   9930  C  CG  . ARG A 1 1269 ? 118.527 97.166  124.196 1.00 38.47  ? 1269 ARG A CG  1 
ATOM   9931  C  CD  . ARG A 1 1269 ? 119.676 98.043  123.809 1.00 40.13  ? 1269 ARG A CD  1 
ATOM   9932  N  NE  . ARG A 1 1269 ? 119.577 99.325  124.497 1.00 41.28  ? 1269 ARG A NE  1 
ATOM   9933  C  CZ  . ARG A 1 1269 ? 120.176 100.437 124.097 1.00 41.24  ? 1269 ARG A CZ  1 
ATOM   9934  N  NH1 . ARG A 1 1269 ? 120.936 100.441 123.008 1.00 42.82  ? 1269 ARG A NH1 1 
ATOM   9935  N  NH2 . ARG A 1 1269 ? 120.008 101.543 124.792 1.00 41.11  ? 1269 ARG A NH2 1 
ATOM   9936  N  N   . ARG A 1 1270 ? 115.366 95.573  125.787 1.00 36.49  ? 1270 ARG A N   1 
ATOM   9937  C  CA  . ARG A 1 1270 ? 114.678 95.447  127.058 1.00 36.84  ? 1270 ARG A CA  1 
ATOM   9938  C  C   . ARG A 1 1270 ? 115.586 95.393  128.265 1.00 37.13  ? 1270 ARG A C   1 
ATOM   9939  O  O   . ARG A 1 1270 ? 115.124 95.643  129.381 1.00 37.28  ? 1270 ARG A O   1 
ATOM   9940  C  CB  . ARG A 1 1270 ? 113.805 94.200  127.052 1.00 36.66  ? 1270 ARG A CB  1 
ATOM   9941  C  CG  . ARG A 1 1270 ? 112.625 94.317  126.158 1.00 37.89  ? 1270 ARG A CG  1 
ATOM   9942  C  CD  . ARG A 1 1270 ? 111.583 95.164  126.788 1.00 40.49  ? 1270 ARG A CD  1 
ATOM   9943  N  NE  . ARG A 1 1270 ? 110.302 94.948  126.139 1.00 43.08  ? 1270 ARG A NE  1 
ATOM   9944  C  CZ  . ARG A 1 1270 ? 109.147 95.234  126.713 1.00 44.68  ? 1270 ARG A CZ  1 
ATOM   9945  N  NH1 . ARG A 1 1270 ? 109.143 95.740  127.951 1.00 45.36  ? 1270 ARG A NH1 1 
ATOM   9946  N  NH2 . ARG A 1 1270 ? 108.010 95.018  126.057 1.00 44.10  ? 1270 ARG A NH2 1 
ATOM   9947  N  N   . PHE A 1 1271 ? 116.851 95.042  128.042 1.00 37.29  ? 1271 PHE A N   1 
ATOM   9948  C  CA  . PHE A 1 1271 ? 117.809 94.834  129.120 1.00 38.01  ? 1271 PHE A CA  1 
ATOM   9949  C  C   . PHE A 1 1271 ? 119.122 95.488  128.747 1.00 39.05  ? 1271 PHE A C   1 
ATOM   9950  O  O   . PHE A 1 1271 ? 119.493 95.518  127.572 1.00 39.84  ? 1271 PHE A O   1 
ATOM   9951  C  CB  . PHE A 1 1271 ? 118.014 93.340  129.399 1.00 37.72  ? 1271 PHE A CB  1 
ATOM   9952  C  CG  . PHE A 1 1271 ? 116.740 92.605  129.745 1.00 37.70  ? 1271 PHE A CG  1 
ATOM   9953  C  CD1 . PHE A 1 1271 ? 116.017 91.928  128.756 1.00 36.70  ? 1271 PHE A CD1 1 
ATOM   9954  C  CD2 . PHE A 1 1271 ? 116.253 92.600  131.052 1.00 37.83  ? 1271 PHE A CD2 1 
ATOM   9955  C  CE1 . PHE A 1 1271 ? 114.837 91.259  129.056 1.00 35.26  ? 1271 PHE A CE1 1 
ATOM   9956  C  CE2 . PHE A 1 1271 ? 115.067 91.929  131.370 1.00 37.81  ? 1271 PHE A CE2 1 
ATOM   9957  C  CZ  . PHE A 1 1271 ? 114.358 91.258  130.364 1.00 37.58  ? 1271 PHE A CZ  1 
ATOM   9958  N  N   . LYS A 1 1272 ? 119.822 96.020  129.742 1.00 39.46  ? 1272 LYS A N   1 
ATOM   9959  C  CA  . LYS A 1 1272 ? 121.069 96.715  129.492 1.00 40.17  ? 1272 LYS A CA  1 
ATOM   9960  C  C   . LYS A 1 1272 ? 122.205 95.717  129.336 1.00 40.32  ? 1272 LYS A C   1 
ATOM   9961  O  O   . LYS A 1 1272 ? 122.544 95.003  130.284 1.00 40.70  ? 1272 LYS A O   1 
ATOM   9962  C  CB  . LYS A 1 1272 ? 121.356 97.700  130.613 1.00 40.69  ? 1272 LYS A CB  1 
ATOM   9963  C  CG  . LYS A 1 1272 ? 120.271 98.752  130.794 1.00 42.17  ? 1272 LYS A CG  1 
ATOM   9964  C  CD  . LYS A 1 1272 ? 120.362 99.349  132.192 1.00 47.09  ? 1272 LYS A CD  1 
ATOM   9965  C  CE  . LYS A 1 1272 ? 119.735 100.738 132.282 1.00 49.42  ? 1272 LYS A CE  1 
ATOM   9966  N  NZ  . LYS A 1 1272 ? 120.540 101.633 133.196 1.00 51.37  ? 1272 LYS A NZ  1 
ATOM   9967  N  N   . VAL A 1 1273 ? 122.764 95.649  128.127 1.00 39.91  ? 1273 VAL A N   1 
ATOM   9968  C  CA  . VAL A 1 1273 ? 123.893 94.770  127.841 1.00 40.09  ? 1273 VAL A CA  1 
ATOM   9969  C  C   . VAL A 1 1273 ? 124.951 95.512  127.035 1.00 41.04  ? 1273 VAL A C   1 
ATOM   9970  O  O   . VAL A 1 1273 ? 124.654 96.105  125.998 1.00 40.48  ? 1273 VAL A O   1 
ATOM   9971  C  CB  . VAL A 1 1273 ? 123.496 93.469  127.070 1.00 39.50  ? 1273 VAL A CB  1 
ATOM   9972  C  CG1 . VAL A 1 1273 ? 124.708 92.567  126.917 1.00 39.63  ? 1273 VAL A CG1 1 
ATOM   9973  C  CG2 . VAL A 1 1273 ? 122.385 92.711  127.767 1.00 38.53  ? 1273 VAL A CG2 1 
ATOM   9974  N  N   . ALA A 1 1274 ? 126.187 95.454  127.523 1.00 42.28  ? 1274 ALA A N   1 
ATOM   9975  C  CA  . ALA A 1 1274 ? 127.318 96.113  126.900 1.00 43.48  ? 1274 ALA A CA  1 
ATOM   9976  C  C   . ALA A 1 1274 ? 128.313 95.095  126.330 1.00 44.63  ? 1274 ALA A C   1 
ATOM   9977  O  O   . ALA A 1 1274 ? 128.342 93.926  126.738 1.00 44.90  ? 1274 ALA A O   1 
ATOM   9978  C  CB  . ALA A 1 1274 ? 128.002 97.015  127.895 1.00 43.86  ? 1274 ALA A CB  1 
ATOM   9979  N  N   . LEU A 1 1275 ? 129.136 95.552  125.387 1.00 45.43  ? 1275 LEU A N   1 
ATOM   9980  C  CA  . LEU A 1 1275 ? 130.123 94.695  124.744 1.00 46.29  ? 1275 LEU A CA  1 
ATOM   9981  C  C   . LEU A 1 1275 ? 129.397 93.500  124.138 1.00 45.99  ? 1275 LEU A C   1 
ATOM   9982  O  O   . LEU A 1 1275 ? 129.862 92.362  124.219 1.00 46.39  ? 1275 LEU A O   1 
ATOM   9983  C  CB  . LEU A 1 1275 ? 131.208 94.223  125.737 1.00 46.89  ? 1275 LEU A CB  1 
ATOM   9984  C  CG  . LEU A 1 1275 ? 131.632 95.103  126.925 1.00 47.61  ? 1275 LEU A CG  1 
ATOM   9985  C  CD1 . LEU A 1 1275 ? 132.512 94.323  127.891 1.00 47.04  ? 1275 LEU A CD1 1 
ATOM   9986  C  CD2 . LEU A 1 1275 ? 132.326 96.378  126.467 1.00 48.32  ? 1275 LEU A CD2 1 
ATOM   9987  N  N   . LYS A 1 1276 ? 128.245 93.739  123.530 1.00 45.54  ? 1276 LYS A N   1 
ATOM   9988  C  CA  . LYS A 1 1276 ? 127.529 92.593  123.007 1.00 45.25  ? 1276 LYS A CA  1 
ATOM   9989  C  C   . LYS A 1 1276 ? 128.096 92.018  121.709 1.00 45.83  ? 1276 LYS A C   1 
ATOM   9990  O  O   . LYS A 1 1276 ? 128.679 92.730  120.879 1.00 46.54  ? 1276 LYS A O   1 
ATOM   9991  C  CB  . LYS A 1 1276 ? 125.998 92.731  123.033 1.00 44.18  ? 1276 LYS A CB  1 
ATOM   9992  C  CG  . LYS A 1 1276 ? 125.359 93.920  122.393 1.00 43.22  ? 1276 LYS A CG  1 
ATOM   9993  C  CD  . LYS A 1 1276 ? 123.932 94.005  122.942 1.00 41.71  ? 1276 LYS A CD  1 
ATOM   9994  C  CE  . LYS A 1 1276 ? 123.228 95.285  122.547 1.00 43.10  ? 1276 LYS A CE  1 
ATOM   9995  N  NZ  . LYS A 1 1276 ? 123.849 96.502  123.162 1.00 44.91  ? 1276 LYS A NZ  1 
ATOM   9996  N  N   . ARG A 1 1277 ? 127.972 90.702  121.595 1.00 45.71  ? 1277 ARG A N   1 
ATOM   9997  C  CA  . ARG A 1 1277 ? 128.476 89.969  120.454 1.00 45.86  ? 1277 ARG A CA  1 
ATOM   9998  C  C   . ARG A 1 1277 ? 127.470 90.101  119.326 1.00 44.19  ? 1277 ARG A C   1 
ATOM   9999  O  O   . ARG A 1 1277 ? 126.292 90.345  119.576 1.00 44.04  ? 1277 ARG A O   1 
ATOM   10000 C  CB  . ARG A 1 1277 ? 128.752 88.516  120.858 1.00 46.48  ? 1277 ARG A CB  1 
ATOM   10001 C  CG  . ARG A 1 1277 ? 129.933 88.426  121.854 1.00 50.66  ? 1277 ARG A CG  1 
ATOM   10002 C  CD  . ARG A 1 1277 ? 130.258 86.998  122.288 1.00 58.57  ? 1277 ARG A CD  1 
ATOM   10003 N  NE  . ARG A 1 1277 ? 131.635 86.878  122.786 1.00 64.81  ? 1277 ARG A NE  1 
ATOM   10004 C  CZ  . ARG A 1 1277 ? 132.383 85.768  122.730 1.00 68.62  ? 1277 ARG A CZ  1 
ATOM   10005 N  NH1 . ARG A 1 1277 ? 131.911 84.637  122.194 1.00 69.10  ? 1277 ARG A NH1 1 
ATOM   10006 N  NH2 . ARG A 1 1277 ? 133.625 85.788  123.210 1.00 70.62  ? 1277 ARG A NH2 1 
ATOM   10007 N  N   . PRO A 1 1278 ? 127.927 90.014  118.073 1.00 43.69  ? 1278 PRO A N   1 
ATOM   10008 C  CA  . PRO A 1 1278 ? 126.931 90.121  116.998 1.00 42.37  ? 1278 PRO A CA  1 
ATOM   10009 C  C   . PRO A 1 1278 ? 125.872 89.007  117.007 1.00 40.88  ? 1278 PRO A C   1 
ATOM   10010 O  O   . PRO A 1 1278 ? 126.061 87.965  117.629 1.00 40.65  ? 1278 PRO A O   1 
ATOM   10011 C  CB  . PRO A 1 1278 ? 127.779 90.083  115.720 1.00 42.89  ? 1278 PRO A CB  1 
ATOM   10012 C  CG  . PRO A 1 1278 ? 129.108 89.558  116.132 1.00 43.47  ? 1278 PRO A CG  1 
ATOM   10013 C  CD  . PRO A 1 1278 ? 129.304 89.866  117.563 1.00 44.09  ? 1278 PRO A CD  1 
ATOM   10014 N  N   . ALA A 1 1279 ? 124.751 89.260  116.346 1.00 39.68  ? 1279 ALA A N   1 
ATOM   10015 C  CA  . ALA A 1 1279 ? 123.712 88.256  116.151 1.00 38.45  ? 1279 ALA A CA  1 
ATOM   10016 C  C   . ALA A 1 1279 ? 123.688 87.862  114.675 1.00 38.34  ? 1279 ALA A C   1 
ATOM   10017 O  O   . ALA A 1 1279 ? 124.479 88.379  113.882 1.00 38.75  ? 1279 ALA A O   1 
ATOM   10018 C  CB  . ALA A 1 1279 ? 122.370 88.803  116.587 1.00 37.57  ? 1279 ALA A CB  1 
ATOM   10019 N  N   . TYR A 1 1280 ? 122.789 86.950  114.308 1.00 37.64  ? 1280 TYR A N   1 
ATOM   10020 C  CA  . TYR A 1 1280 ? 122.701 86.460  112.929 1.00 37.15  ? 1280 TYR A CA  1 
ATOM   10021 C  C   . TYR A 1 1280 ? 121.277 86.104  112.508 1.00 36.08  ? 1280 TYR A C   1 
ATOM   10022 O  O   . TYR A 1 1280 ? 120.362 86.007  113.333 1.00 35.21  ? 1280 TYR A O   1 
ATOM   10023 C  CB  . TYR A 1 1280 ? 123.608 85.241  112.731 1.00 37.91  ? 1280 TYR A CB  1 
ATOM   10024 C  CG  . TYR A 1 1280 ? 123.224 84.058  113.588 1.00 37.73  ? 1280 TYR A CG  1 
ATOM   10025 C  CD1 . TYR A 1 1280 ? 123.752 83.909  114.863 1.00 38.28  ? 1280 TYR A CD1 1 
ATOM   10026 C  CD2 . TYR A 1 1280 ? 122.330 83.094  113.131 1.00 38.32  ? 1280 TYR A CD2 1 
ATOM   10027 C  CE1 . TYR A 1 1280 ? 123.413 82.844  115.663 1.00 37.54  ? 1280 TYR A CE1 1 
ATOM   10028 C  CE2 . TYR A 1 1280 ? 121.977 82.010  113.938 1.00 38.86  ? 1280 TYR A CE2 1 
ATOM   10029 C  CZ  . TYR A 1 1280 ? 122.533 81.901  115.209 1.00 38.50  ? 1280 TYR A CZ  1 
ATOM   10030 O  OH  . TYR A 1 1280 ? 122.199 80.853  116.045 1.00 39.53  ? 1280 TYR A OH  1 
ATOM   10031 N  N   . VAL A 1 1281 ? 121.123 85.914  111.205 1.00 35.52  ? 1281 VAL A N   1 
ATOM   10032 C  CA  . VAL A 1 1281 ? 119.910 85.393  110.606 1.00 34.65  ? 1281 VAL A CA  1 
ATOM   10033 C  C   . VAL A 1 1281 ? 120.285 84.186  109.744 1.00 34.69  ? 1281 VAL A C   1 
ATOM   10034 O  O   . VAL A 1 1281 ? 121.331 84.187  109.093 1.00 35.03  ? 1281 VAL A O   1 
ATOM   10035 C  CB  . VAL A 1 1281 ? 119.224 86.453  109.725 1.00 34.50  ? 1281 VAL A CB  1 
ATOM   10036 C  CG1 . VAL A 1 1281 ? 118.012 85.848  108.996 1.00 34.35  ? 1281 VAL A CG1 1 
ATOM   10037 C  CG2 . VAL A 1 1281 ? 118.798 87.646  110.566 1.00 33.07  ? 1281 VAL A CG2 1 
ATOM   10038 N  N   . VAL A 1 1282 ? 119.442 83.157  109.760 1.00 33.79  ? 1282 VAL A N   1 
ATOM   10039 C  CA  . VAL A 1 1282 ? 119.649 81.979  108.922 1.00 33.98  ? 1282 VAL A CA  1 
ATOM   10040 C  C   . VAL A 1 1282 ? 118.423 81.734  108.044 1.00 33.56  ? 1282 VAL A C   1 
ATOM   10041 O  O   . VAL A 1 1282 ? 117.294 82.015  108.451 1.00 32.99  ? 1282 VAL A O   1 
ATOM   10042 C  CB  . VAL A 1 1282 ? 119.899 80.711  109.770 1.00 33.95  ? 1282 VAL A CB  1 
ATOM   10043 C  CG1 . VAL A 1 1282 ? 120.004 79.502  108.885 1.00 35.74  ? 1282 VAL A CG1 1 
ATOM   10044 C  CG2 . VAL A 1 1282 ? 121.179 80.833  110.537 1.00 34.70  ? 1282 VAL A CG2 1 
ATOM   10045 N  N   . VAL A 1 1283 ? 118.661 81.237  106.834 1.00 33.82  ? 1283 VAL A N   1 
ATOM   10046 C  CA  . VAL A 1 1283 ? 117.624 80.636  106.001 1.00 33.56  ? 1283 VAL A CA  1 
ATOM   10047 C  C   . VAL A 1 1283 ? 118.199 79.311  105.548 1.00 34.43  ? 1283 VAL A C   1 
ATOM   10048 O  O   . VAL A 1 1283 ? 119.395 79.226  105.297 1.00 35.37  ? 1283 VAL A O   1 
ATOM   10049 C  CB  . VAL A 1 1283 ? 117.262 81.511  104.777 1.00 33.72  ? 1283 VAL A CB  1 
ATOM   10050 C  CG1 . VAL A 1 1283 ? 118.484 81.783  103.885 1.00 33.37  ? 1283 VAL A CG1 1 
ATOM   10051 C  CG2 . VAL A 1 1283 ? 116.125 80.877  103.967 1.00 33.48  ? 1283 VAL A CG2 1 
ATOM   10052 N  N   . TYR A 1 1284 ? 117.371 78.273  105.472 1.00 34.26  ? 1284 TYR A N   1 
ATOM   10053 C  CA  . TYR A 1 1284 ? 117.834 76.966  105.022 1.00 34.83  ? 1284 TYR A CA  1 
ATOM   10054 C  C   . TYR A 1 1284 ? 116.695 76.111  104.515 1.00 35.20  ? 1284 TYR A C   1 
ATOM   10055 O  O   . TYR A 1 1284 ? 115.532 76.348  104.846 1.00 34.71  ? 1284 TYR A O   1 
ATOM   10056 C  CB  . TYR A 1 1284 ? 118.619 76.217  106.114 1.00 34.67  ? 1284 TYR A CB  1 
ATOM   10057 C  CG  . TYR A 1 1284 ? 117.865 76.001  107.404 1.00 34.13  ? 1284 TYR A CG  1 
ATOM   10058 C  CD1 . TYR A 1 1284 ? 117.850 76.983  108.400 1.00 33.56  ? 1284 TYR A CD1 1 
ATOM   10059 C  CD2 . TYR A 1 1284 ? 117.172 74.821  107.637 1.00 34.14  ? 1284 TYR A CD2 1 
ATOM   10060 C  CE1 . TYR A 1 1284 ? 117.163 76.796  109.587 1.00 32.69  ? 1284 TYR A CE1 1 
ATOM   10061 C  CE2 . TYR A 1 1284 ? 116.469 74.624  108.826 1.00 33.89  ? 1284 TYR A CE2 1 
ATOM   10062 C  CZ  . TYR A 1 1284 ? 116.475 75.611  109.795 1.00 33.99  ? 1284 TYR A CZ  1 
ATOM   10063 O  OH  . TYR A 1 1284 ? 115.782 75.419  110.971 1.00 34.38  ? 1284 TYR A OH  1 
ATOM   10064 N  N   . ASP A 1 1285 ? 117.055 75.127  103.692 1.00 36.18  ? 1285 ASP A N   1 
ATOM   10065 C  CA  . ASP A 1 1285 ? 116.139 74.128  103.165 1.00 36.59  ? 1285 ASP A CA  1 
ATOM   10066 C  C   . ASP A 1 1285 ? 115.995 73.011  104.195 1.00 36.61  ? 1285 ASP A C   1 
ATOM   10067 O  O   . ASP A 1 1285 ? 116.959 72.313  104.511 1.00 37.52  ? 1285 ASP A O   1 
ATOM   10068 C  CB  . ASP A 1 1285 ? 116.698 73.585  101.851 1.00 37.46  ? 1285 ASP A CB  1 
ATOM   10069 C  CG  . ASP A 1 1285 ? 115.820 72.537  101.231 1.00 38.16  ? 1285 ASP A CG  1 
ATOM   10070 O  OD1 . ASP A 1 1285 ? 115.254 72.818  100.156 1.00 38.35  ? 1285 ASP A OD1 1 
ATOM   10071 O  OD2 . ASP A 1 1285 ? 115.697 71.435  101.811 1.00 39.16  ? 1285 ASP A OD2 1 
ATOM   10072 N  N   . TYR A 1 1286 ? 114.789 72.835  104.713 1.00 35.94  ? 1286 TYR A N   1 
ATOM   10073 C  CA  . TYR A 1 1286 ? 114.574 71.924  105.831 1.00 35.53  ? 1286 TYR A CA  1 
ATOM   10074 C  C   . TYR A 1 1286 ? 115.006 70.480  105.569 1.00 36.22  ? 1286 TYR A C   1 
ATOM   10075 O  O   . TYR A 1 1286 ? 115.604 69.834  106.435 1.00 36.39  ? 1286 TYR A O   1 
ATOM   10076 C  CB  . TYR A 1 1286 ? 113.113 71.954  106.247 1.00 34.70  ? 1286 TYR A CB  1 
ATOM   10077 C  CG  . TYR A 1 1286 ? 112.875 71.454  107.644 1.00 34.54  ? 1286 TYR A CG  1 
ATOM   10078 C  CD1 . TYR A 1 1286 ? 112.980 72.314  108.745 1.00 33.56  ? 1286 TYR A CD1 1 
ATOM   10079 C  CD2 . TYR A 1 1286 ? 112.527 70.123  107.874 1.00 34.87  ? 1286 TYR A CD2 1 
ATOM   10080 C  CE1 . TYR A 1 1286 ? 112.742 71.852  110.036 1.00 32.98  ? 1286 TYR A CE1 1 
ATOM   10081 C  CE2 . TYR A 1 1286 ? 112.291 69.660  109.150 1.00 34.31  ? 1286 TYR A CE2 1 
ATOM   10082 C  CZ  . TYR A 1 1286 ? 112.400 70.526  110.226 1.00 33.76  ? 1286 TYR A CZ  1 
ATOM   10083 O  OH  . TYR A 1 1286 ? 112.164 70.046  111.493 1.00 34.38  ? 1286 TYR A OH  1 
ATOM   10084 N  N   . TYR A 1 1287 ? 114.703 69.976  104.381 1.00 36.51  ? 1287 TYR A N   1 
ATOM   10085 C  CA  . TYR A 1 1287 ? 114.955 68.571  104.080 1.00 37.30  ? 1287 TYR A CA  1 
ATOM   10086 C  C   . TYR A 1 1287 ? 116.311 68.349  103.427 1.00 37.92  ? 1287 TYR A C   1 
ATOM   10087 O  O   . TYR A 1 1287 ? 116.695 67.210  103.145 1.00 38.81  ? 1287 TYR A O   1 
ATOM   10088 C  CB  . TYR A 1 1287 ? 113.797 67.972  103.274 1.00 37.45  ? 1287 TYR A CB  1 
ATOM   10089 C  CG  . TYR A 1 1287 ? 112.505 67.994  104.072 1.00 37.05  ? 1287 TYR A CG  1 
ATOM   10090 C  CD1 . TYR A 1 1287 ? 112.277 67.062  105.080 1.00 36.01  ? 1287 TYR A CD1 1 
ATOM   10091 C  CD2 . TYR A 1 1287 ? 111.532 68.973  103.846 1.00 35.64  ? 1287 TYR A CD2 1 
ATOM   10092 C  CE1 . TYR A 1 1287 ? 111.111 67.084  105.829 1.00 35.85  ? 1287 TYR A CE1 1 
ATOM   10093 C  CE2 . TYR A 1 1287 ? 110.362 68.999  104.594 1.00 35.08  ? 1287 TYR A CE2 1 
ATOM   10094 C  CZ  . TYR A 1 1287 ? 110.162 68.047  105.585 1.00 35.00  ? 1287 TYR A CZ  1 
ATOM   10095 O  OH  . TYR A 1 1287 ? 109.015 68.052  106.341 1.00 34.63  ? 1287 TYR A OH  1 
ATOM   10096 N  N   . ASN A 1 1288 ? 117.034 69.449  103.227 1.00 37.43  ? 1288 ASN A N   1 
ATOM   10097 C  CA  . ASN A 1 1288 ? 118.408 69.418  102.778 1.00 37.85  ? 1288 ASN A CA  1 
ATOM   10098 C  C   . ASN A 1 1288 ? 119.153 70.635  103.336 1.00 37.72  ? 1288 ASN A C   1 
ATOM   10099 O  O   . ASN A 1 1288 ? 119.355 71.648  102.638 1.00 37.72  ? 1288 ASN A O   1 
ATOM   10100 C  CB  . ASN A 1 1288 ? 118.469 69.357  101.253 1.00 38.39  ? 1288 ASN A CB  1 
ATOM   10101 C  CG  . ASN A 1 1288 ? 119.892 69.267  100.715 1.00 38.82  ? 1288 ASN A CG  1 
ATOM   10102 O  OD1 . ASN A 1 1288 ? 120.867 69.180  101.460 1.00 39.10  ? 1288 ASN A OD1 1 
ATOM   10103 N  ND2 . ASN A 1 1288 ? 120.008 69.287  99.403  1.00 40.25  ? 1288 ASN A ND2 1 
ATOM   10104 N  N   . THR A 1 1289 ? 119.573 70.520  104.595 1.00 37.22  ? 1289 THR A N   1 
ATOM   10105 C  CA  . THR A 1 1289 ? 120.156 71.650  105.318 1.00 37.04  ? 1289 THR A CA  1 
ATOM   10106 C  C   . THR A 1 1289 ? 121.519 72.089  104.783 1.00 37.85  ? 1289 THR A C   1 
ATOM   10107 O  O   . THR A 1 1289 ? 122.047 73.111  105.210 1.00 37.96  ? 1289 THR A O   1 
ATOM   10108 C  CB  . THR A 1 1289 ? 120.262 71.383  106.841 1.00 36.46  ? 1289 THR A CB  1 
ATOM   10109 O  OG1 . THR A 1 1289 ? 121.231 70.362  107.069 1.00 38.21  ? 1289 THR A OG1 1 
ATOM   10110 C  CG2 . THR A 1 1289 ? 118.922 70.948  107.422 1.00 34.74  ? 1289 THR A CG2 1 
ATOM   10111 N  N   . ASN A 1 1290 ? 122.092 71.330  103.855 1.00 39.08  ? 1290 ASN A N   1 
ATOM   10112 C  CA  . ASN A 1 1290 ? 123.301 71.780  103.173 1.00 39.98  ? 1290 ASN A CA  1 
ATOM   10113 C  C   . ASN A 1 1290 ? 123.040 73.064  102.405 1.00 39.66  ? 1290 ASN A C   1 
ATOM   10114 O  O   . ASN A 1 1290 ? 123.937 73.874  102.238 1.00 40.20  ? 1290 ASN A O   1 
ATOM   10115 C  CB  . ASN A 1 1290 ? 123.857 70.710  102.236 1.00 40.86  ? 1290 ASN A CB  1 
ATOM   10116 C  CG  . ASN A 1 1290 ? 124.549 69.578  102.980 1.00 42.92  ? 1290 ASN A CG  1 
ATOM   10117 O  OD1 . ASN A 1 1290 ? 125.014 69.740  104.115 1.00 43.79  ? 1290 ASN A OD1 1 
ATOM   10118 N  ND2 . ASN A 1 1290 ? 124.630 68.419  102.336 1.00 45.01  ? 1290 ASN A ND2 1 
ATOM   10119 N  N   . LEU A 1 1291 ? 121.805 73.247  101.948 1.00 39.23  ? 1291 LEU A N   1 
ATOM   10120 C  CA  . LEU A 1 1291 ? 121.432 74.467  101.252 1.00 38.99  ? 1291 LEU A CA  1 
ATOM   10121 C  C   . LEU A 1 1291 ? 120.938 75.479  102.278 1.00 38.41  ? 1291 LEU A C   1 
ATOM   10122 O  O   . LEU A 1 1291 ? 119.883 75.306  102.886 1.00 37.83  ? 1291 LEU A O   1 
ATOM   10123 C  CB  . LEU A 1 1291 ? 120.389 74.199  100.155 1.00 38.63  ? 1291 LEU A CB  1 
ATOM   10124 C  CG  . LEU A 1 1291 ? 120.571 72.982  99.217  1.00 39.62  ? 1291 LEU A CG  1 
ATOM   10125 C  CD1 . LEU A 1 1291 ? 119.535 72.991  98.085  1.00 39.22  ? 1291 LEU A CD1 1 
ATOM   10126 C  CD2 . LEU A 1 1291 ? 121.971 72.871  98.643  1.00 37.60  ? 1291 LEU A CD2 1 
ATOM   10127 N  N   . ASN A 1 1292 ? 121.729 76.527  102.474 1.00 38.86  ? 1292 ASN A N   1 
ATOM   10128 C  CA  . ASN A 1 1292 ? 121.455 77.540  103.489 1.00 38.66  ? 1292 ASN A CA  1 
ATOM   10129 C  C   . ASN A 1 1292 ? 122.315 78.779  103.306 1.00 39.33  ? 1292 ASN A C   1 
ATOM   10130 O  O   . ASN A 1 1292 ? 123.312 78.770  102.575 1.00 40.23  ? 1292 ASN A O   1 
ATOM   10131 C  CB  . ASN A 1 1292 ? 121.727 76.979  104.876 1.00 38.36  ? 1292 ASN A CB  1 
ATOM   10132 C  CG  . ASN A 1 1292 ? 123.198 76.697  105.101 1.00 38.87  ? 1292 ASN A CG  1 
ATOM   10133 O  OD1 . ASN A 1 1292 ? 123.964 77.586  105.458 1.00 37.79  ? 1292 ASN A OD1 1 
ATOM   10134 N  ND2 . ASN A 1 1292 ? 123.598 75.453  104.883 1.00 39.50  ? 1292 ASN A ND2 1 
ATOM   10135 N  N   . ALA A 1 1293 ? 121.928 79.843  103.991 1.00 39.25  ? 1293 ALA A N   1 
ATOM   10136 C  CA  . ALA A 1 1293 ? 122.719 81.053  104.044 1.00 40.04  ? 1293 ALA A CA  1 
ATOM   10137 C  C   . ALA A 1 1293 ? 122.628 81.594  105.452 1.00 40.14  ? 1293 ALA A C   1 
ATOM   10138 O  O   . ALA A 1 1293 ? 121.638 81.367  106.152 1.00 39.86  ? 1293 ALA A O   1 
ATOM   10139 C  CB  . ALA A 1 1293 ? 122.214 82.079  103.038 1.00 39.73  ? 1293 ALA A CB  1 
ATOM   10140 N  N   . ILE A 1 1294 ? 123.668 82.310  105.860 1.00 41.28  ? 1294 ILE A N   1 
ATOM   10141 C  CA  . ILE A 1 1294 ? 123.741 82.909  107.176 1.00 41.66  ? 1294 ILE A CA  1 
ATOM   10142 C  C   . ILE A 1 1294 ? 124.417 84.272  107.033 1.00 42.49  ? 1294 ILE A C   1 
ATOM   10143 O  O   . ILE A 1 1294 ? 125.441 84.386  106.370 1.00 43.37  ? 1294 ILE A O   1 
ATOM   10144 C  CB  . ILE A 1 1294 ? 124.446 81.940  108.184 1.00 41.96  ? 1294 ILE A CB  1 
ATOM   10145 C  CG1 . ILE A 1 1294 ? 124.257 82.382  109.649 1.00 42.54  ? 1294 ILE A CG1 1 
ATOM   10146 C  CG2 . ILE A 1 1294 ? 125.905 81.687  107.810 1.00 42.44  ? 1294 ILE A CG2 1 
ATOM   10147 C  CD1 . ILE A 1 1294 ? 125.380 83.214  110.223 1.00 44.75  ? 1294 ILE A CD1 1 
ATOM   10148 N  N   . LYS A 1 1295 ? 123.802 85.305  107.605 1.00 42.88  ? 1295 LYS A N   1 
ATOM   10149 C  CA  . LYS A 1 1295 ? 124.339 86.665  107.593 1.00 44.01  ? 1295 LYS A CA  1 
ATOM   10150 C  C   . LYS A 1 1295 ? 124.387 87.214  109.009 1.00 44.56  ? 1295 LYS A C   1 
ATOM   10151 O  O   . LYS A 1 1295 ? 123.423 87.079  109.768 1.00 43.86  ? 1295 LYS A O   1 
ATOM   10152 C  CB  . LYS A 1 1295 ? 123.480 87.593  106.740 1.00 43.71  ? 1295 LYS A CB  1 
ATOM   10153 C  CG  . LYS A 1 1295 ? 123.679 87.458  105.260 1.00 45.14  ? 1295 LYS A CG  1 
ATOM   10154 C  CD  . LYS A 1 1295 ? 124.914 88.216  104.804 1.00 46.95  ? 1295 LYS A CD  1 
ATOM   10155 C  CE  . LYS A 1 1295 ? 125.400 87.717  103.454 1.00 46.69  ? 1295 LYS A CE  1 
ATOM   10156 N  NZ  . LYS A 1 1295 ? 124.680 88.403  102.356 1.00 47.79  ? 1295 LYS A NZ  1 
ATOM   10157 N  N   . VAL A 1 1296 ? 125.509 87.831  109.367 1.00 45.98  ? 1296 VAL A N   1 
ATOM   10158 C  CA  . VAL A 1 1296 ? 125.656 88.378  110.702 1.00 46.98  ? 1296 VAL A CA  1 
ATOM   10159 C  C   . VAL A 1 1296 ? 125.205 89.827  110.685 1.00 47.52  ? 1296 VAL A C   1 
ATOM   10160 O  O   . VAL A 1 1296 ? 125.183 90.458  109.631 1.00 47.80  ? 1296 VAL A O   1 
ATOM   10161 C  CB  . VAL A 1 1296 ? 127.105 88.256  111.250 1.00 47.58  ? 1296 VAL A CB  1 
ATOM   10162 C  CG1 . VAL A 1 1296 ? 127.684 86.871  110.969 1.00 47.37  ? 1296 VAL A CG1 1 
ATOM   10163 C  CG2 . VAL A 1 1296 ? 127.994 89.327  110.663 1.00 49.25  ? 1296 VAL A CG2 1 
ATOM   10164 N  N   . TYR A 1 1297 ? 124.815 90.337  111.849 1.00 48.27  ? 1297 TYR A N   1 
ATOM   10165 C  CA  . TYR A 1 1297 ? 124.489 91.746  111.994 1.00 49.47  ? 1297 TYR A CA  1 
ATOM   10166 C  C   . TYR A 1 1297 ? 124.825 92.229  113.404 1.00 50.86  ? 1297 TYR A C   1 
ATOM   10167 O  O   . TYR A 1 1297 ? 124.897 91.432  114.341 1.00 50.30  ? 1297 TYR A O   1 
ATOM   10168 C  CB  . TYR A 1 1297 ? 123.032 92.027  111.596 1.00 48.31  ? 1297 TYR A CB  1 
ATOM   10169 C  CG  . TYR A 1 1297 ? 121.980 91.572  112.583 1.00 47.46  ? 1297 TYR A CG  1 
ATOM   10170 C  CD1 . TYR A 1 1297 ? 121.567 90.237  112.642 1.00 46.48  ? 1297 TYR A CD1 1 
ATOM   10171 C  CD2 . TYR A 1 1297 ? 121.384 92.484  113.452 1.00 46.20  ? 1297 TYR A CD2 1 
ATOM   10172 C  CE1 . TYR A 1 1297 ? 120.597 89.828  113.556 1.00 45.22  ? 1297 TYR A CE1 1 
ATOM   10173 C  CE2 . TYR A 1 1297 ? 120.415 92.087  114.352 1.00 45.26  ? 1297 TYR A CE2 1 
ATOM   10174 C  CZ  . TYR A 1 1297 ? 120.026 90.765  114.404 1.00 44.88  ? 1297 TYR A CZ  1 
ATOM   10175 O  OH  . TYR A 1 1297 ? 119.059 90.395  115.310 1.00 44.81  ? 1297 TYR A OH  1 
ATOM   10176 N  N   . GLU A 1 1298 ? 125.078 93.529  113.530 1.00 53.35  ? 1298 GLU A N   1 
ATOM   10177 C  CA  . GLU A 1 1298 ? 125.425 94.138  114.812 1.00 56.02  ? 1298 GLU A CA  1 
ATOM   10178 C  C   . GLU A 1 1298 ? 124.460 95.243  115.145 1.00 56.98  ? 1298 GLU A C   1 
ATOM   10179 O  O   . GLU A 1 1298 ? 123.965 95.929  114.257 1.00 57.12  ? 1298 GLU A O   1 
ATOM   10180 C  CB  . GLU A 1 1298 ? 126.835 94.720  114.781 1.00 56.60  ? 1298 GLU A CB  1 
ATOM   10181 C  CG  . GLU A 1 1298 ? 127.907 93.745  115.169 1.00 59.44  ? 1298 GLU A CG  1 
ATOM   10182 C  CD  . GLU A 1 1298 ? 129.305 94.344  115.063 1.00 63.95  ? 1298 GLU A CD  1 
ATOM   10183 O  OE1 . GLU A 1 1298 ? 129.615 95.292  115.832 1.00 65.98  ? 1298 GLU A OE1 1 
ATOM   10184 O  OE2 . GLU A 1 1298 ? 130.097 93.858  114.217 1.00 64.58  ? 1298 GLU A OE2 1 
ATOM   10185 N  N   . VAL A 1 1299 ? 124.197 95.425  116.429 1.00 58.89  ? 1299 VAL A N   1 
ATOM   10186 C  CA  . VAL A 1 1299 ? 123.425 96.571  116.855 1.00 60.79  ? 1299 VAL A CA  1 
ATOM   10187 C  C   . VAL A 1 1299 ? 124.370 97.591  117.476 1.00 63.15  ? 1299 VAL A C   1 
ATOM   10188 O  O   . VAL A 1 1299 ? 125.442 97.229  117.974 1.00 63.75  ? 1299 VAL A O   1 
ATOM   10189 C  CB  . VAL A 1 1299 ? 122.283 96.176  117.806 1.00 59.85  ? 1299 VAL A CB  1 
ATOM   10190 C  CG1 . VAL A 1 1299 ? 121.553 97.408  118.298 1.00 60.44  ? 1299 VAL A CG1 1 
ATOM   10191 C  CG2 . VAL A 1 1299 ? 121.299 95.307  117.076 1.00 59.41  ? 1299 VAL A CG2 1 
ATOM   10192 N  N   . ASP A 1 1300 ? 123.976 98.864  117.416 1.00 65.57  ? 1300 ASP A N   1 
ATOM   10193 C  CA  . ASP A 1 1300 ? 124.721 99.951  118.050 1.00 68.42  ? 1300 ASP A CA  1 
ATOM   10194 C  C   . ASP A 1 1300 ? 125.215 99.546  119.424 1.00 69.67  ? 1300 ASP A C   1 
ATOM   10195 O  O   . ASP A 1 1300 ? 124.431 99.278  120.332 1.00 69.42  ? 1300 ASP A O   1 
ATOM   10196 C  CB  . ASP A 1 1300 ? 123.883 101.235 118.127 1.00 68.34  ? 1300 ASP A CB  1 
ATOM   10197 C  CG  . ASP A 1 1300 ? 124.060 102.126 116.899 1.00 70.04  ? 1300 ASP A CG  1 
ATOM   10198 O  OD1 . ASP A 1 1300 ? 125.011 101.901 116.103 1.00 70.91  ? 1300 ASP A OD1 1 
ATOM   10199 O  OD2 . ASP A 1 1300 ? 123.243 103.062 116.737 1.00 71.40  ? 1300 ASP A OD2 1 
ATOM   10200 N  N   . LYS A 1 1301 ? 126.531 99.474  119.545 1.00 72.13  ? 1301 LYS A N   1 
ATOM   10201 C  CA  . LYS A 1 1301 ? 127.161 98.994  120.751 1.00 74.09  ? 1301 LYS A CA  1 
ATOM   10202 C  C   . LYS A 1 1301 ? 127.041 100.007 121.885 1.00 74.93  ? 1301 LYS A C   1 
ATOM   10203 O  O   . LYS A 1 1301 ? 127.610 101.098 121.806 1.00 75.76  ? 1301 LYS A O   1 
ATOM   10204 C  CB  . LYS A 1 1301 ? 128.629 98.632  120.483 1.00 75.33  ? 1301 LYS A CB  1 
ATOM   10205 C  CG  . LYS A 1 1301 ? 128.859 97.166  120.071 1.00 76.30  ? 1301 LYS A CG  1 
ATOM   10206 C  CD  . LYS A 1 1301 ? 130.349 96.863  119.871 1.00 79.07  ? 1301 LYS A CD  1 
ATOM   10207 C  CE  . LYS A 1 1301 ? 130.580 95.401  119.468 1.00 80.22  ? 1301 LYS A CE  1 
ATOM   10208 N  NZ  . LYS A 1 1301 ? 131.850 95.201  118.694 1.00 80.40  ? 1301 LYS A NZ  1 
ATOM   10209 N  N   . GLN A 1 1302 ? 126.275 99.633  122.917 1.00 75.27  ? 1302 GLN A N   1 
ATOM   10210 C  CA  . GLN A 1 1302 ? 126.231 100.356 124.186 1.00 76.18  ? 1302 GLN A CA  1 
ATOM   10211 C  C   . GLN A 1 1302 ? 127.592 100.293 124.865 1.00 77.86  ? 1302 GLN A C   1 
ATOM   10212 O  O   . GLN A 1 1302 ? 128.325 99.296  124.760 1.00 78.21  ? 1302 GLN A O   1 
ATOM   10213 C  CB  . GLN A 1 1302 ? 125.206 99.748  125.137 1.00 75.40  ? 1302 GLN A CB  1 
ATOM   10214 C  CG  . GLN A 1 1302 ? 123.759 100.005 124.804 1.00 75.05  ? 1302 GLN A CG  1 
ATOM   10215 C  CD  . GLN A 1 1302 ? 122.845 99.713  125.987 1.00 75.43  ? 1302 GLN A CD  1 
ATOM   10216 O  OE1 . GLN A 1 1302 ? 122.729 100.525 126.901 1.00 76.06  ? 1302 GLN A OE1 1 
ATOM   10217 N  NE2 . GLN A 1 1302 ? 122.193 98.550  125.975 1.00 74.69  ? 1302 GLN A NE2 1 
ATOM   10218 N  N   . ASN A 1 1303 ? 127.914 101.373 125.564 1.00 79.29  ? 1303 ASN A N   1 
ATOM   10219 C  CA  . ASN A 1 1303 ? 129.172 101.518 126.288 1.00 81.25  ? 1303 ASN A CA  1 
ATOM   10220 C  C   . ASN A 1 1303 ? 129.020 101.060 127.731 1.00 81.51  ? 1303 ASN A C   1 
ATOM   10221 O  O   . ASN A 1 1303 ? 128.019 101.363 128.382 1.00 80.74  ? 1303 ASN A O   1 
ATOM   10222 C  CB  . ASN A 1 1303 ? 129.649 102.979 126.234 1.00 81.96  ? 1303 ASN A CB  1 
ATOM   10223 C  CG  . ASN A 1 1303 ? 128.485 103.997 126.292 1.00 82.37  ? 1303 ASN A CG  1 
ATOM   10224 O  OD1 . ASN A 1 1303 ? 128.713 105.196 126.463 1.00 84.28  ? 1303 ASN A OD1 1 
ATOM   10225 N  ND2 . ASN A 1 1303 ? 127.245 103.520 126.144 1.00 81.23  ? 1303 ASN A ND2 1 
ATOM   10226 N  N   . LEU A 1 1304 ? 130.017 100.331 128.220 1.00 82.85  ? 1304 LEU A N   1 
ATOM   10227 C  CA  . LEU A 1 1304 ? 130.039 99.864  129.604 1.00 83.96  ? 1304 LEU A CA  1 
ATOM   10228 C  C   . LEU A 1 1304 ? 129.893 101.005 130.627 1.00 85.02  ? 1304 LEU A C   1 
ATOM   10229 O  O   . LEU A 1 1304 ? 129.312 100.814 131.693 1.00 84.55  ? 1304 LEU A O   1 
ATOM   10230 C  CB  . LEU A 1 1304 ? 131.315 99.053  129.868 1.00 84.57  ? 1304 LEU A CB  1 
ATOM   10231 C  CG  . LEU A 1 1304 ? 131.528 98.386  131.234 1.00 84.57  ? 1304 LEU A CG  1 
ATOM   10232 C  CD1 . LEU A 1 1304 ? 130.521 97.291  131.494 1.00 83.31  ? 1304 LEU A CD1 1 
ATOM   10233 C  CD2 . LEU A 1 1304 ? 132.928 97.823  131.340 1.00 85.87  ? 1304 LEU A CD2 1 
ATOM   10234 N  N   . CYS A 1 1305 ? 130.406 102.185 130.283 1.00 86.90  ? 1305 CYS A N   1 
ATOM   10235 C  CA  . CYS A 1 1305 ? 130.375 103.349 131.171 1.00 88.76  ? 1305 CYS A CA  1 
ATOM   10236 C  C   . CYS A 1 1305 ? 128.990 103.967 131.312 1.00 88.47  ? 1305 CYS A C   1 
ATOM   10237 O  O   . CYS A 1 1305 ? 128.725 104.679 132.277 1.00 88.62  ? 1305 CYS A O   1 
ATOM   10238 C  CB  . CYS A 1 1305 ? 131.371 104.416 130.711 1.00 89.92  ? 1305 CYS A CB  1 
ATOM   10239 S  SG  . CYS A 1 1305 ? 133.110 103.901 130.690 1.00 93.04  ? 1305 CYS A SG  1 
ATOM   10240 N  N   . GLU A 1 1306 ? 128.115 103.706 130.347 1.00 88.62  ? 1306 GLU A N   1 
ATOM   10241 C  CA  . GLU A 1 1306 ? 126.731 104.154 130.433 1.00 88.93  ? 1306 GLU A CA  1 
ATOM   10242 C  C   . GLU A 1 1306 ? 125.900 103.128 131.206 1.00 88.77  ? 1306 GLU A C   1 
ATOM   10243 O  O   . GLU A 1 1306 ? 124.936 103.482 131.886 1.00 88.42  ? 1306 GLU A O   1 
ATOM   10244 C  CB  . GLU A 1 1306 ? 126.154 104.361 129.030 1.00 88.60  ? 1306 GLU A CB  1 
ATOM   10245 C  CG  . GLU A 1 1306 ? 124.767 105.023 128.986 1.00 89.09  ? 1306 GLU A CG  1 
ATOM   10246 C  CD  . GLU A 1 1306 ? 123.863 104.442 127.895 1.00 89.50  ? 1306 GLU A CD  1 
ATOM   10247 O  OE1 . GLU A 1 1306 ? 124.323 104.291 126.730 1.00 90.12  ? 1306 GLU A OE1 1 
ATOM   10248 O  OE2 . GLU A 1 1306 ? 122.688 104.137 128.209 1.00 88.24  ? 1306 GLU A OE2 1 
ATOM   10249 N  N   . ILE A 1 1307 ? 126.314 101.866 131.109 1.00 89.48  ? 1307 ILE A N   1 
ATOM   10250 C  CA  . ILE A 1 1307 ? 125.571 100.704 131.616 1.00 89.55  ? 1307 ILE A CA  1 
ATOM   10251 C  C   . ILE A 1 1307 ? 125.565 100.563 133.142 1.00 90.46  ? 1307 ILE A C   1 
ATOM   10252 O  O   . ILE A 1 1307 ? 124.555 100.173 133.730 1.00 89.94  ? 1307 ILE A O   1 
ATOM   10253 C  CB  . ILE A 1 1307 ? 126.088 99.395  130.921 1.00 89.40  ? 1307 ILE A CB  1 
ATOM   10254 C  CG1 . ILE A 1 1307 ? 125.475 99.248  129.525 1.00 89.06  ? 1307 ILE A CG1 1 
ATOM   10255 C  CG2 . ILE A 1 1307 ? 125.837 98.146  131.743 1.00 88.95  ? 1307 ILE A CG2 1 
ATOM   10256 C  CD1 . ILE A 1 1307 ? 124.035 99.713  129.413 1.00 88.59  ? 1307 ILE A CD1 1 
ATOM   10257 N  N   . CYS A 1 1308 ? 126.690 100.884 133.773 1.00 92.28  ? 1308 CYS A N   1 
ATOM   10258 C  CA  . CYS A 1 1308 ? 126.843 100.724 135.219 1.00 93.72  ? 1308 CYS A CA  1 
ATOM   10259 C  C   . CYS A 1 1308 ? 126.163 101.835 136.038 1.00 94.16  ? 1308 CYS A C   1 
ATOM   10260 O  O   . CYS A 1 1308 ? 125.847 102.904 135.512 1.00 94.11  ? 1308 CYS A O   1 
ATOM   10261 C  CB  . CYS A 1 1308 ? 128.335 100.618 135.582 1.00 94.92  ? 1308 CYS A CB  1 
ATOM   10262 S  SG  . CYS A 1 1308 ? 129.411 101.950 134.951 1.00 96.24  ? 1308 CYS A SG  1 
ATOM   10263 N  N   . ASP A 1 1309 ? 125.909 101.561 137.316 1.00 94.91  ? 1309 ASP A N   1 
ATOM   10264 C  CA  . ASP A 1 1309 ? 125.634 102.623 138.284 1.00 95.84  ? 1309 ASP A CA  1 
ATOM   10265 C  C   . ASP A 1 1309 ? 126.952 102.958 138.968 1.00 97.31  ? 1309 ASP A C   1 
ATOM   10266 O  O   . ASP A 1 1309 ? 127.848 102.114 139.032 1.00 97.76  ? 1309 ASP A O   1 
ATOM   10267 C  CB  . ASP A 1 1309 ? 124.538 102.243 139.293 1.00 95.36  ? 1309 ASP A CB  1 
ATOM   10268 C  CG  . ASP A 1 1309 ? 124.690 100.828 139.840 1.00 95.92  ? 1309 ASP A CG  1 
ATOM   10269 O  OD1 . ASP A 1 1309 ? 125.748 100.510 140.430 1.00 97.31  ? 1309 ASP A OD1 1 
ATOM   10270 O  OD2 . ASP A 1 1309 ? 123.732 100.034 139.695 1.00 95.29  ? 1309 ASP A OD2 1 
ATOM   10271 N  N   . GLU A 1 1310 ? 127.057 104.185 139.471 1.00 98.41  ? 1310 GLU A N   1 
ATOM   10272 C  CA  . GLU A 1 1310 ? 128.333 104.784 139.910 1.00 100.25 ? 1310 GLU A CA  1 
ATOM   10273 C  C   . GLU A 1 1310 ? 129.236 103.918 140.807 1.00 101.15 ? 1310 GLU A C   1 
ATOM   10274 O  O   . GLU A 1 1310 ? 130.461 104.055 140.770 1.00 101.99 ? 1310 GLU A O   1 
ATOM   10275 C  CB  . GLU A 1 1310 ? 128.077 106.155 140.555 1.00 100.77 ? 1310 GLU A CB  1 
ATOM   10276 C  CG  . GLU A 1 1310 ? 127.638 107.241 139.557 1.00 101.44 ? 1310 GLU A CG  1 
ATOM   10277 C  CD  . GLU A 1 1310 ? 126.396 108.014 140.007 1.00 102.16 ? 1310 GLU A CD  1 
ATOM   10278 O  OE1 . GLU A 1 1310 ? 126.283 108.333 141.211 1.00 103.27 ? 1310 GLU A OE1 1 
ATOM   10279 O  OE2 . GLU A 1 1310 ? 125.527 108.305 139.153 1.00 101.34 ? 1310 GLU A OE2 1 
ATOM   10280 N  N   . GLU A 1 1311 ? 128.627 103.026 141.588 1.00 101.09 ? 1311 GLU A N   1 
ATOM   10281 C  CA  . GLU A 1 1311 ? 129.355 102.148 142.513 1.00 101.97 ? 1311 GLU A CA  1 
ATOM   10282 C  C   . GLU A 1 1311 ? 130.306 101.164 141.835 1.00 102.13 ? 1311 GLU A C   1 
ATOM   10283 O  O   . GLU A 1 1311 ? 131.470 101.061 142.214 1.00 103.12 ? 1311 GLU A O   1 
ATOM   10284 C  CB  . GLU A 1 1311 ? 128.377 101.379 143.408 1.00 101.56 ? 1311 GLU A CB  1 
ATOM   10285 C  CG  . GLU A 1 1311 ? 128.099 102.046 144.753 1.00 102.61 ? 1311 GLU A CG  1 
ATOM   10286 C  CD  . GLU A 1 1311 ? 126.859 101.494 145.443 1.00 102.77 ? 1311 GLU A CD  1 
ATOM   10287 O  OE1 . GLU A 1 1311 ? 126.663 100.252 145.452 1.00 102.41 ? 1311 GLU A OE1 1 
ATOM   10288 O  OE2 . GLU A 1 1311 ? 126.078 102.312 145.979 1.00 102.65 ? 1311 GLU A OE2 1 
ATOM   10289 N  N   . ASP A 1 1312 ? 129.804 100.444 140.838 1.00 101.28 ? 1312 ASP A N   1 
ATOM   10290 C  CA  . ASP A 1 1312 ? 130.546 99.325  140.259 1.00 101.52 ? 1312 ASP A CA  1 
ATOM   10291 C  C   . ASP A 1 1312 ? 131.280 99.652  138.954 1.00 101.58 ? 1312 ASP A C   1 
ATOM   10292 O  O   . ASP A 1 1312 ? 131.932 98.777  138.378 1.00 101.82 ? 1312 ASP A O   1 
ATOM   10293 C  CB  . ASP A 1 1312 ? 129.642 98.086  140.105 1.00 100.68 ? 1312 ASP A CB  1 
ATOM   10294 C  CG  . ASP A 1 1312 ? 128.240 98.427  139.601 1.00 100.12 ? 1312 ASP A CG  1 
ATOM   10295 O  OD1 . ASP A 1 1312 ? 128.119 99.205  138.626 1.00 99.81  ? 1312 ASP A OD1 1 
ATOM   10296 O  OD2 . ASP A 1 1312 ? 127.258 97.905  140.181 1.00 100.02 ? 1312 ASP A OD2 1 
ATOM   10297 N  N   . CYS A 1 1313 ? 131.193 100.905 138.505 1.00 101.43 ? 1313 CYS A N   1 
ATOM   10298 C  CA  . CYS A 1 1313 ? 131.915 101.347 137.305 1.00 101.49 ? 1313 CYS A CA  1 
ATOM   10299 C  C   . CYS A 1 1313 ? 133.431 101.162 137.474 1.00 102.81 ? 1313 CYS A C   1 
ATOM   10300 O  O   . CYS A 1 1313 ? 134.022 101.724 138.400 1.00 103.78 ? 1313 CYS A O   1 
ATOM   10301 C  CB  . CYS A 1 1313 ? 131.571 102.798 136.958 1.00 101.12 ? 1313 CYS A CB  1 
ATOM   10302 S  SG  . CYS A 1 1313 ? 129.812 103.100 136.596 1.00 99.29  ? 1313 CYS A SG  1 
ATOM   10303 N  N   . PRO A 1 1314 ? 134.059 100.365 136.583 1.00 103.02 ? 1314 PRO A N   1 
ATOM   10304 C  CA  . PRO A 1 1314 ? 135.460 99.956  136.733 1.00 104.18 ? 1314 PRO A CA  1 
ATOM   10305 C  C   . PRO A 1 1314 ? 136.469 101.086 136.482 1.00 105.16 ? 1314 PRO A C   1 
ATOM   10306 O  O   . PRO A 1 1314 ? 136.075 102.229 136.224 1.00 104.97 ? 1314 PRO A O   1 
ATOM   10307 C  CB  . PRO A 1 1314 ? 135.612 98.852  135.680 1.00 103.79 ? 1314 PRO A CB  1 
ATOM   10308 C  CG  . PRO A 1 1314 ? 134.641 99.225  134.621 1.00 102.77 ? 1314 PRO A CG  1 
ATOM   10309 C  CD  . PRO A 1 1314 ? 133.462 99.811  135.351 1.00 102.21 ? 1314 PRO A CD  1 
ATOM   10310 N  N   . ALA A 1 1315 ? 137.757 100.748 136.560 1.00 106.15 ? 1315 ALA A N   1 
ATOM   10311 C  CA  . ALA A 1 1315 ? 138.852 101.711 136.417 1.00 107.20 ? 1315 ALA A CA  1 
ATOM   10312 C  C   . ALA A 1 1315 ? 138.750 102.578 135.156 1.00 106.83 ? 1315 ALA A C   1 
ATOM   10313 O  O   . ALA A 1 1315 ? 138.709 103.810 135.247 1.00 107.06 ? 1315 ALA A O   1 
ATOM   10314 C  CB  . ALA A 1 1315 ? 140.200 100.992 136.472 1.00 108.33 ? 1315 ALA A CB  1 
ATOM   10315 N  N   . GLU A 1 1316 ? 138.695 101.931 133.991 1.00 106.14 ? 1316 GLU A N   1 
ATOM   10316 C  CA  . GLU A 1 1316 ? 138.641 102.634 132.702 1.00 105.71 ? 1316 GLU A CA  1 
ATOM   10317 C  C   . GLU A 1 1316 ? 137.253 103.219 132.338 1.00 104.36 ? 1316 GLU A C   1 
ATOM   10318 O  O   . GLU A 1 1316 ? 136.592 102.752 131.392 1.00 103.51 ? 1316 GLU A O   1 
ATOM   10319 C  CB  . GLU A 1 1316 ? 139.215 101.755 131.572 1.00 105.75 ? 1316 GLU A CB  1 
ATOM   10320 C  CG  . GLU A 1 1316 ? 138.936 100.243 131.698 1.00 105.43 ? 1316 GLU A CG  1 
ATOM   10321 C  CD  . GLU A 1 1316 ? 137.710 99.755  130.906 1.00 104.05 ? 1316 GLU A CD  1 
ATOM   10322 O  OE1 . GLU A 1 1316 ? 137.307 100.410 129.916 1.00 103.27 ? 1316 GLU A OE1 1 
ATOM   10323 O  OE2 . GLU A 1 1316 ? 137.160 98.689  131.268 1.00 102.97 ? 1316 GLU A OE2 1 
ATOM   10324 N  N   . CYS A 1 1317 ? 136.828 104.241 133.097 1.00 104.02 ? 1317 CYS A N   1 
ATOM   10325 C  CA  . CYS A 1 1317 ? 135.554 104.955 132.860 1.00 102.49 ? 1317 CYS A CA  1 
ATOM   10326 C  C   . CYS A 1 1317 ? 135.608 106.403 133.374 1.00 103.14 ? 1317 CYS A C   1 
ATOM   10327 O  O   . CYS A 1 1317 ? 136.668 106.879 133.798 1.00 104.22 ? 1317 CYS A O   1 
ATOM   10328 C  CB  . CYS A 1 1317 ? 134.367 104.222 133.512 1.00 101.19 ? 1317 CYS A CB  1 
ATOM   10329 S  SG  . CYS A 1 1317 ? 133.445 103.003 132.494 1.00 98.03  ? 1317 CYS A SG  1 
ATOM   10330 N  N   . GLY A 1 1318 ? 134.462 107.090 133.327 1.00 102.37 ? 1318 GLY A N   1 
ATOM   10331 C  CA  . GLY A 1 1318 ? 134.316 108.437 133.896 1.00 102.84 ? 1318 GLY A CA  1 
ATOM   10332 C  C   . GLY A 1 1318 ? 134.107 109.557 132.815 1.00 102.78 ? 1318 GLY A C   1 
ATOM   10333 O  O   . GLY A 1 1318 ? 135.062 110.603 133.069 1.00 103.88 ? 1318 GLY A O   1 
HETATM 10334 C  C1  . NAG B 2 .    ? 79.614  71.169  124.691 1.00 66.67  ? 1326 NAG A C1  1 
HETATM 10335 C  C2  . NAG B 2 .    ? 79.195  72.210  123.649 1.00 71.78  ? 1326 NAG A C2  1 
HETATM 10336 C  C3  . NAG B 2 .    ? 77.677  72.347  123.599 1.00 72.32  ? 1326 NAG A C3  1 
HETATM 10337 C  C4  . NAG B 2 .    ? 76.974  71.000  123.448 1.00 72.33  ? 1326 NAG A C4  1 
HETATM 10338 C  C5  . NAG B 2 .    ? 77.637  69.798  124.146 1.00 71.37  ? 1326 NAG A C5  1 
HETATM 10339 C  C6  . NAG B 2 .    ? 77.389  68.545  123.291 1.00 72.45  ? 1326 NAG A C6  1 
HETATM 10340 C  C7  . NAG B 2 .    ? 80.493  74.178  122.951 1.00 74.36  ? 1326 NAG A C7  1 
HETATM 10341 C  C8  . NAG B 2 .    ? 81.249  75.409  123.380 1.00 73.53  ? 1326 NAG A C8  1 
HETATM 10342 N  N2  . NAG B 2 .    ? 79.808  73.515  123.897 1.00 73.60  ? 1326 NAG A N2  1 
HETATM 10343 O  O3  . NAG B 2 .    ? 77.309  73.149  122.492 1.00 73.25  ? 1326 NAG A O3  1 
HETATM 10344 O  O4  . NAG B 2 .    ? 75.658  71.159  123.938 1.00 73.12  ? 1326 NAG A O4  1 
HETATM 10345 O  O5  . NAG B 2 .    ? 79.032  69.901  124.420 1.00 69.13  ? 1326 NAG A O5  1 
HETATM 10346 O  O6  . NAG B 2 .    ? 78.528  68.129  122.558 1.00 72.92  ? 1326 NAG A O6  1 
HETATM 10347 O  O7  . NAG B 2 .    ? 80.522  73.820  121.768 1.00 75.35  ? 1326 NAG A O7  1 
HETATM 10348 C  C1  . NAG C 2 .    ? 99.013  110.638 151.960 1.00 53.69  ? 1327 NAG A C1  1 
HETATM 10349 C  C2  . NAG C 2 .    ? 98.700  110.361 153.428 1.00 54.68  ? 1327 NAG A C2  1 
HETATM 10350 C  C3  . NAG C 2 .    ? 99.739  111.052 154.305 1.00 55.92  ? 1327 NAG A C3  1 
HETATM 10351 C  C4  . NAG C 2 .    ? 101.112 110.483 153.984 1.00 56.74  ? 1327 NAG A C4  1 
HETATM 10352 C  C5  . NAG C 2 .    ? 101.373 110.676 152.477 1.00 56.00  ? 1327 NAG A C5  1 
HETATM 10353 C  C6  . NAG C 2 .    ? 102.657 109.995 152.045 1.00 55.82  ? 1327 NAG A C6  1 
HETATM 10354 C  C7  . NAG C 2 .    ? 96.616  109.993 154.576 1.00 53.38  ? 1327 NAG A C7  1 
HETATM 10355 C  C8  . NAG C 2 .    ? 95.331  110.593 155.080 1.00 53.29  ? 1327 NAG A C8  1 
HETATM 10356 N  N2  . NAG C 2 .    ? 97.356  110.764 153.781 1.00 53.57  ? 1327 NAG A N2  1 
HETATM 10357 O  O3  . NAG C 2 .    ? 99.467  110.825 155.661 1.00 58.12  ? 1327 NAG A O3  1 
HETATM 10358 O  O4  . NAG C 2 .    ? 102.096 111.069 154.838 1.00 57.48  ? 1327 NAG A O4  1 
HETATM 10359 O  O5  . NAG C 2 .    ? 100.316 110.127 151.686 1.00 55.31  ? 1327 NAG A O5  1 
HETATM 10360 O  O6  . NAG C 2 .    ? 102.523 108.630 152.371 1.00 57.48  ? 1327 NAG A O6  1 
HETATM 10361 O  O7  . NAG C 2 .    ? 96.948  108.849 154.897 1.00 52.44  ? 1327 NAG A O7  1 
HETATM 10362 C  C1  . NAG D 2 .    ? 110.618 106.351 124.058 1.00 58.48  ? 1328 NAG A C1  1 
HETATM 10363 C  C2  . NAG D 2 .    ? 111.561 106.134 122.866 1.00 60.52  ? 1328 NAG A C2  1 
HETATM 10364 C  C3  . NAG D 2 .    ? 113.014 106.538 123.152 1.00 61.28  ? 1328 NAG A C3  1 
HETATM 10365 C  C4  . NAG D 2 .    ? 113.135 107.844 123.957 1.00 62.31  ? 1328 NAG A C4  1 
HETATM 10366 C  C5  . NAG D 2 .    ? 112.109 107.855 125.099 1.00 62.81  ? 1328 NAG A C5  1 
HETATM 10367 C  C6  . NAG D 2 .    ? 112.124 109.160 125.889 1.00 63.90  ? 1328 NAG A C6  1 
HETATM 10368 C  C7  . NAG D 2 .    ? 110.951 104.400 121.262 1.00 59.28  ? 1328 NAG A C7  1 
HETATM 10369 C  C8  . NAG D 2 .    ? 110.777 102.929 121.033 1.00 58.46  ? 1328 NAG A C8  1 
HETATM 10370 N  N2  . NAG D 2 .    ? 111.521 104.749 122.419 1.00 59.84  ? 1328 NAG A N2  1 
HETATM 10371 O  O3  . NAG D 2 .    ? 113.658 106.680 121.907 1.00 60.86  ? 1328 NAG A O3  1 
HETATM 10372 O  O4  . NAG D 2 .    ? 114.451 108.031 124.455 1.00 61.56  ? 1328 NAG A O4  1 
HETATM 10373 O  O5  . NAG D 2 .    ? 110.811 107.662 124.555 1.00 61.31  ? 1328 NAG A O5  1 
HETATM 10374 O  O6  . NAG D 2 .    ? 111.490 110.153 125.112 1.00 65.57  ? 1328 NAG A O6  1 
HETATM 10375 O  O7  . NAG D 2 .    ? 110.573 105.212 120.411 1.00 58.64  ? 1328 NAG A O7  1 
HETATM 10376 C  C1  . NAG E 2 .    ? 88.961  61.114  147.036 1.00 79.35  ? 1329 NAG A C1  1 
HETATM 10377 C  C2  . NAG E 2 .    ? 89.272  60.138  148.180 1.00 83.00  ? 1329 NAG A C2  1 
HETATM 10378 C  C3  . NAG E 2 .    ? 89.597  58.727  147.659 1.00 84.30  ? 1329 NAG A C3  1 
HETATM 10379 C  C4  . NAG E 2 .    ? 88.672  58.254  146.522 1.00 85.17  ? 1329 NAG A C4  1 
HETATM 10380 C  C5  . NAG E 2 .    ? 88.409  59.388  145.514 1.00 83.74  ? 1329 NAG A C5  1 
HETATM 10381 C  C6  . NAG E 2 .    ? 87.366  59.038  144.459 1.00 83.79  ? 1329 NAG A C6  1 
HETATM 10382 C  C7  . NAG E 2 .    ? 90.396  60.607  150.326 1.00 83.77  ? 1329 NAG A C7  1 
HETATM 10383 C  C8  . NAG E 2 .    ? 91.744  60.381  150.949 1.00 84.07  ? 1329 NAG A C8  1 
HETATM 10384 N  N2  . NAG E 2 .    ? 90.369  60.654  148.990 1.00 83.41  ? 1329 NAG A N2  1 
HETATM 10385 O  O3  . NAG E 2 .    ? 89.562  57.792  148.721 1.00 84.48  ? 1329 NAG A O3  1 
HETATM 10386 O  O4  . NAG E 2 .    ? 89.303  57.148  145.895 1.00 88.01  ? 1329 NAG A O4  1 
HETATM 10387 O  O5  . NAG E 2 .    ? 87.978  60.561  146.179 1.00 81.52  ? 1329 NAG A O5  1 
HETATM 10388 O  O6  . NAG E 2 .    ? 87.306  60.075  143.505 1.00 84.06  ? 1329 NAG A O6  1 
HETATM 10389 O  O7  . NAG E 2 .    ? 89.402  60.739  151.045 1.00 83.73  ? 1329 NAG A O7  1 
HETATM 10390 C  C1  . NAG F 2 .    ? 88.463  55.970  145.856 1.00 90.11  ? 1330 NAG A C1  1 
HETATM 10391 C  C2  . NAG F 2 .    ? 88.946  55.069  144.719 1.00 90.55  ? 1330 NAG A C2  1 
HETATM 10392 C  C3  . NAG F 2 .    ? 88.126  53.782  144.626 1.00 91.56  ? 1330 NAG A C3  1 
HETATM 10393 C  C4  . NAG F 2 .    ? 87.899  53.124  145.993 1.00 92.01  ? 1330 NAG A C4  1 
HETATM 10394 C  C5  . NAG F 2 .    ? 87.532  54.145  147.080 1.00 91.97  ? 1330 NAG A C5  1 
HETATM 10395 C  C6  . NAG F 2 .    ? 87.573  53.509  148.468 1.00 92.96  ? 1330 NAG A C6  1 
HETATM 10396 C  C7  . NAG F 2 .    ? 89.948  56.292  142.848 1.00 90.27  ? 1330 NAG A C7  1 
HETATM 10397 C  C8  . NAG F 2 .    ? 89.851  56.398  141.352 1.00 90.01  ? 1330 NAG A C8  1 
HETATM 10398 N  N2  . NAG F 2 .    ? 88.876  55.787  143.460 1.00 90.15  ? 1330 NAG A N2  1 
HETATM 10399 O  O3  . NAG F 2 .    ? 88.792  52.879  143.766 1.00 91.77  ? 1330 NAG A O3  1 
HETATM 10400 O  O4  . NAG F 2 .    ? 86.889  52.139  145.877 1.00 92.12  ? 1330 NAG A O4  1 
HETATM 10401 O  O5  . NAG F 2 .    ? 88.432  55.243  147.074 1.00 91.24  ? 1330 NAG A O5  1 
HETATM 10402 O  O6  . NAG F 2 .    ? 86.269  53.152  148.880 1.00 93.97  ? 1330 NAG A O6  1 
HETATM 10403 O  O7  . NAG F 2 .    ? 90.965  56.668  143.441 1.00 89.80  ? 1330 NAG A O7  1 
HETATM 10404 NA NA  . NA  G 3 .    ? 101.149 65.147  99.398  1.00 21.93  ? 1331 NA  A NA  1 
HETATM 10405 NA NA  . NA  H 3 .    ? 130.971 58.153  106.864 1.00 43.97  ? 1332 NA  A NA  1 
HETATM 10406 NA NA  . NA  I 3 .    ? 127.090 96.735  123.156 1.00 53.60  ? 1333 NA  A NA  1 
HETATM 10407 O  O   . HOH J 4 .    ? 35.341  88.665  144.671 1.00 65.10  ? 1334 HOH A O   1 
HETATM 10408 O  O   . HOH J 4 .    ? 47.250  82.858  130.291 1.00 47.43  ? 1335 HOH A O   1 
HETATM 10409 O  O   . HOH J 4 .    ? 90.429  59.036  125.669 1.00 64.16  ? 1336 HOH A O   1 
HETATM 10410 O  O   . HOH J 4 .    ? 85.793  54.871  131.519 1.00 67.29  ? 1337 HOH A O   1 
HETATM 10411 O  O   . HOH J 4 .    ? 102.839 69.560  122.373 1.00 56.66  ? 1338 HOH A O   1 
HETATM 10412 O  O   . HOH J 4 .    ? 95.259  77.087  118.834 1.00 54.51  ? 1339 HOH A O   1 
HETATM 10413 O  O   . HOH J 4 .    ? 99.151  106.987 148.046 1.00 44.52  ? 1340 HOH A O   1 
HETATM 10414 O  O   . HOH J 4 .    ? 93.186  109.380 149.674 1.00 39.11  ? 1341 HOH A O   1 
HETATM 10415 O  O   . HOH J 4 .    ? 86.305  115.935 155.968 1.00 45.97  ? 1342 HOH A O   1 
HETATM 10416 O  O   . HOH J 4 .    ? 105.848 105.965 144.494 1.00 39.06  ? 1343 HOH A O   1 
HETATM 10417 O  O   . HOH J 4 .    ? 99.896  118.218 144.594 1.00 54.10  ? 1344 HOH A O   1 
HETATM 10418 O  O   . HOH J 4 .    ? 108.612 105.173 129.809 1.00 49.27  ? 1345 HOH A O   1 
HETATM 10419 O  O   . HOH J 4 .    ? 110.194 99.057  128.480 1.00 73.21  ? 1346 HOH A O   1 
HETATM 10420 O  O   . HOH J 4 .    ? 92.140  103.964 128.137 1.00 37.55  ? 1347 HOH A O   1 
HETATM 10421 O  O   . HOH J 4 .    ? 90.054  103.585 131.440 1.00 21.67  ? 1348 HOH A O   1 
HETATM 10422 O  O   . HOH J 4 .    ? 90.352  105.588 129.464 1.00 22.87  ? 1349 HOH A O   1 
HETATM 10423 O  O   . HOH J 4 .    ? 87.400  107.193 146.838 1.00 44.05  ? 1350 HOH A O   1 
HETATM 10424 O  O   . HOH J 4 .    ? 61.889  104.521 154.789 1.00 58.06  ? 1351 HOH A O   1 
HETATM 10425 O  O   . HOH J 4 .    ? 54.542  98.326  162.202 1.00 48.20  ? 1352 HOH A O   1 
HETATM 10426 O  O   . HOH J 4 .    ? 68.576  113.516 165.783 1.00 51.03  ? 1353 HOH A O   1 
HETATM 10427 O  O   . HOH J 4 .    ? 77.852  112.926 167.876 1.00 49.79  ? 1354 HOH A O   1 
HETATM 10428 O  O   . HOH J 4 .    ? 79.887  113.695 165.749 1.00 59.56  ? 1355 HOH A O   1 
HETATM 10429 O  O   . HOH J 4 .    ? 69.654  111.957 154.827 1.00 45.49  ? 1356 HOH A O   1 
HETATM 10430 O  O   . HOH J 4 .    ? 45.181  101.364 150.107 1.00 63.19  ? 1357 HOH A O   1 
HETATM 10431 O  O   . HOH J 4 .    ? 54.055  96.153  145.953 1.00 59.17  ? 1358 HOH A O   1 
HETATM 10432 O  O   . HOH J 4 .    ? 49.875  76.063  168.684 1.00 49.52  ? 1359 HOH A O   1 
HETATM 10433 O  O   . HOH J 4 .    ? 54.353  85.995  160.939 1.00 56.61  ? 1360 HOH A O   1 
HETATM 10434 O  O   . HOH J 4 .    ? 49.414  93.199  160.822 1.00 54.51  ? 1361 HOH A O   1 
HETATM 10435 O  O   . HOH J 4 .    ? 40.735  83.325  162.865 1.00 42.99  ? 1362 HOH A O   1 
HETATM 10436 O  O   . HOH J 4 .    ? 45.151  88.399  164.978 1.00 64.33  ? 1363 HOH A O   1 
HETATM 10437 O  O   . HOH J 4 .    ? 46.999  66.363  163.246 1.00 72.04  ? 1364 HOH A O   1 
HETATM 10438 O  O   . HOH J 4 .    ? 47.502  63.700  163.355 1.00 73.02  ? 1365 HOH A O   1 
HETATM 10439 O  O   . HOH J 4 .    ? 46.168  96.512  144.772 1.00 90.58  ? 1366 HOH A O   1 
HETATM 10440 O  O   . HOH J 4 .    ? 62.495  84.106  135.424 1.00 72.89  ? 1367 HOH A O   1 
HETATM 10441 O  O   . HOH J 4 .    ? 57.485  71.490  139.110 1.00 64.98  ? 1368 HOH A O   1 
HETATM 10442 O  O   . HOH J 4 .    ? 54.697  81.051  133.315 1.00 48.91  ? 1369 HOH A O   1 
HETATM 10443 O  O   . HOH J 4 .    ? 47.348  85.570  135.295 1.00 48.12  ? 1370 HOH A O   1 
HETATM 10444 O  O   . HOH J 4 .    ? 52.693  94.390  141.541 1.00 45.80  ? 1371 HOH A O   1 
HETATM 10445 O  O   . HOH J 4 .    ? 56.493  94.869  146.211 1.00 50.65  ? 1372 HOH A O   1 
HETATM 10446 O  O   . HOH J 4 .    ? 89.695  66.249  144.984 1.00 60.13  ? 1373 HOH A O   1 
HETATM 10447 O  O   . HOH J 4 .    ? 83.423  59.566  151.515 1.00 59.21  ? 1374 HOH A O   1 
HETATM 10448 O  O   . HOH J 4 .    ? 86.513  61.545  149.779 1.00 77.34  ? 1375 HOH A O   1 
HETATM 10449 O  O   . HOH J 4 .    ? 114.688 87.709  127.089 1.00 32.70  ? 1376 HOH A O   1 
HETATM 10450 O  O   . HOH J 4 .    ? 122.154 86.212  123.645 1.00 44.72  ? 1377 HOH A O   1 
HETATM 10451 O  O   . HOH J 4 .    ? 107.289 98.290  148.846 1.00 37.81  ? 1378 HOH A O   1 
HETATM 10452 O  O   . HOH J 4 .    ? 108.090 104.427 157.453 1.00 47.69  ? 1379 HOH A O   1 
HETATM 10453 O  O   . HOH J 4 .    ? 112.573 106.137 150.204 1.00 37.54  ? 1380 HOH A O   1 
HETATM 10454 O  O   . HOH J 4 .    ? 115.000 106.350 153.062 1.00 51.82  ? 1381 HOH A O   1 
HETATM 10455 O  O   . HOH J 4 .    ? 126.009 82.131  139.364 1.00 47.26  ? 1382 HOH A O   1 
HETATM 10456 O  O   . HOH J 4 .    ? 133.795 89.098  140.118 1.00 41.34  ? 1383 HOH A O   1 
HETATM 10457 O  O   . HOH J 4 .    ? 125.113 96.479  151.483 1.00 35.04  ? 1384 HOH A O   1 
HETATM 10458 O  O   . HOH J 4 .    ? 115.129 103.313 155.620 1.00 35.31  ? 1385 HOH A O   1 
HETATM 10459 O  O   . HOH J 4 .    ? 107.815 102.032 142.362 1.00 33.53  ? 1386 HOH A O   1 
HETATM 10460 O  O   . HOH J 4 .    ? 110.747 103.281 143.923 1.00 47.87  ? 1387 HOH A O   1 
HETATM 10461 O  O   . HOH J 4 .    ? 117.495 101.589 143.843 1.00 30.51  ? 1388 HOH A O   1 
HETATM 10462 O  O   . HOH J 4 .    ? 120.900 99.094  142.218 1.00 36.45  ? 1389 HOH A O   1 
HETATM 10463 O  O   . HOH J 4 .    ? 117.847 92.016  156.723 1.00 53.48  ? 1390 HOH A O   1 
HETATM 10464 O  O   . HOH J 4 .    ? 109.041 85.337  145.645 1.00 49.94  ? 1391 HOH A O   1 
HETATM 10465 O  O   . HOH J 4 .    ? 129.708 61.821  112.149 1.00 46.47  ? 1392 HOH A O   1 
HETATM 10466 O  O   . HOH J 4 .    ? 126.807 59.681  114.712 1.00 42.66  ? 1393 HOH A O   1 
HETATM 10467 O  O   . HOH J 4 .    ? 121.540 46.834  125.939 1.00 59.70  ? 1394 HOH A O   1 
HETATM 10468 O  O   . HOH J 4 .    ? 117.238 49.371  120.322 1.00 44.30  ? 1395 HOH A O   1 
HETATM 10469 O  O   . HOH J 4 .    ? 120.247 48.793  120.132 1.00 51.51  ? 1396 HOH A O   1 
HETATM 10470 O  O   . HOH J 4 .    ? 120.132 55.648  118.034 1.00 36.26  ? 1397 HOH A O   1 
HETATM 10471 O  O   . HOH J 4 .    ? 121.285 55.420  122.717 1.00 57.52  ? 1398 HOH A O   1 
HETATM 10472 O  O   . HOH J 4 .    ? 123.072 57.163  121.300 1.00 44.40  ? 1399 HOH A O   1 
HETATM 10473 O  O   . HOH J 4 .    ? 118.872 68.324  114.565 1.00 46.96  ? 1400 HOH A O   1 
HETATM 10474 O  O   . HOH J 4 .    ? 116.184 74.392  116.891 1.00 44.01  ? 1401 HOH A O   1 
HETATM 10475 O  O   . HOH J 4 .    ? 109.758 74.131  117.217 1.00 39.25  ? 1402 HOH A O   1 
HETATM 10476 O  O   . HOH J 4 .    ? 106.078 70.497  117.346 1.00 57.49  ? 1403 HOH A O   1 
HETATM 10477 O  O   . HOH J 4 .    ? 107.794 63.202  122.327 1.00 50.52  ? 1404 HOH A O   1 
HETATM 10478 O  O   . HOH J 4 .    ? 104.964 64.361  122.948 1.00 44.04  ? 1405 HOH A O   1 
HETATM 10479 O  O   . HOH J 4 .    ? 94.182  69.112  120.602 1.00 38.63  ? 1406 HOH A O   1 
HETATM 10480 O  O   . HOH J 4 .    ? 93.274  72.431  112.200 1.00 35.73  ? 1407 HOH A O   1 
HETATM 10481 O  O   . HOH J 4 .    ? 89.874  62.842  110.154 1.00 33.79  ? 1408 HOH A O   1 
HETATM 10482 O  O   . HOH J 4 .    ? 89.013  71.056  104.665 1.00 42.12  ? 1409 HOH A O   1 
HETATM 10483 O  O   . HOH J 4 .    ? 100.522 75.869  111.774 1.00 23.19  ? 1410 HOH A O   1 
HETATM 10484 O  O   . HOH J 4 .    ? 88.666  68.510  100.064 1.00 50.02  ? 1411 HOH A O   1 
HETATM 10485 O  O   . HOH J 4 .    ? 97.160  77.731  109.136 1.00 42.16  ? 1412 HOH A O   1 
HETATM 10486 O  O   . HOH J 4 .    ? 99.119  73.063  101.756 1.00 34.38  ? 1413 HOH A O   1 
HETATM 10487 O  O   . HOH J 4 .    ? 94.475  76.555  98.615  1.00 55.85  ? 1414 HOH A O   1 
HETATM 10488 O  O   . HOH J 4 .    ? 93.365  54.398  120.898 1.00 86.47  ? 1415 HOH A O   1 
HETATM 10489 O  O   . HOH J 4 .    ? 94.916  57.241  86.078  1.00 50.76  ? 1416 HOH A O   1 
HETATM 10490 O  O   . HOH J 4 .    ? 100.828 69.488  100.983 1.00 37.66  ? 1417 HOH A O   1 
HETATM 10491 O  O   . HOH J 4 .    ? 103.879 74.216  96.632  1.00 42.73  ? 1418 HOH A O   1 
HETATM 10492 O  O   . HOH J 4 .    ? 112.464 66.705  99.023  1.00 45.51  ? 1419 HOH A O   1 
HETATM 10493 O  O   . HOH J 4 .    ? 115.790 69.624  93.641  1.00 41.94  ? 1420 HOH A O   1 
HETATM 10494 O  O   . HOH J 4 .    ? 110.750 66.403  92.746  1.00 31.36  ? 1421 HOH A O   1 
HETATM 10495 O  O   . HOH J 4 .    ? 105.769 60.880  94.237  1.00 42.22  ? 1422 HOH A O   1 
HETATM 10496 O  O   . HOH J 4 .    ? 107.308 61.350  90.579  1.00 27.89  ? 1423 HOH A O   1 
HETATM 10497 O  O   . HOH J 4 .    ? 108.537 59.367  92.575  1.00 31.68  ? 1424 HOH A O   1 
HETATM 10498 O  O   . HOH J 4 .    ? 109.605 64.021  91.263  1.00 43.75  ? 1425 HOH A O   1 
HETATM 10499 O  O   . HOH J 4 .    ? 107.301 58.432  107.677 1.00 40.45  ? 1426 HOH A O   1 
HETATM 10500 O  O   . HOH J 4 .    ? 100.836 43.752  91.328  1.00 39.35  ? 1427 HOH A O   1 
HETATM 10501 O  O   . HOH J 4 .    ? 115.039 50.831  85.351  1.00 57.36  ? 1428 HOH A O   1 
HETATM 10502 O  O   . HOH J 4 .    ? 119.091 57.384  92.318  1.00 42.86  ? 1429 HOH A O   1 
HETATM 10503 O  O   . HOH J 4 .    ? 113.889 48.959  100.753 1.00 31.15  ? 1430 HOH A O   1 
HETATM 10504 O  O   . HOH J 4 .    ? 111.284 39.221  92.186  1.00 52.78  ? 1431 HOH A O   1 
HETATM 10505 O  O   . HOH J 4 .    ? 121.846 42.313  92.851  1.00 47.89  ? 1432 HOH A O   1 
HETATM 10506 O  O   . HOH J 4 .    ? 122.590 55.233  95.477  1.00 46.06  ? 1433 HOH A O   1 
HETATM 10507 O  O   . HOH J 4 .    ? 118.506 61.851  94.546  1.00 49.31  ? 1434 HOH A O   1 
HETATM 10508 O  O   . HOH J 4 .    ? 122.579 63.314  94.905  1.00 60.63  ? 1435 HOH A O   1 
HETATM 10509 O  O   . HOH J 4 .    ? 118.578 62.060  104.269 1.00 37.65  ? 1436 HOH A O   1 
HETATM 10510 O  O   . HOH J 4 .    ? 110.298 58.834  104.076 1.00 32.30  ? 1437 HOH A O   1 
HETATM 10511 O  O   . HOH J 4 .    ? 108.704 55.307  106.895 1.00 47.86  ? 1438 HOH A O   1 
HETATM 10512 O  O   . HOH J 4 .    ? 123.340 39.046  104.296 1.00 36.51  ? 1439 HOH A O   1 
HETATM 10513 O  O   . HOH J 4 .    ? 123.011 37.021  107.064 1.00 44.96  ? 1440 HOH A O   1 
HETATM 10514 O  O   . HOH J 4 .    ? 123.853 63.436  109.785 1.00 42.80  ? 1441 HOH A O   1 
HETATM 10515 O  O   . HOH J 4 .    ? 119.739 64.747  108.550 1.00 64.57  ? 1442 HOH A O   1 
HETATM 10516 O  O   . HOH J 4 .    ? 115.631 69.389  109.074 1.00 39.32  ? 1443 HOH A O   1 
HETATM 10517 O  O   . HOH J 4 .    ? 114.272 64.299  107.275 1.00 40.71  ? 1444 HOH A O   1 
HETATM 10518 O  O   . HOH J 4 .    ? 108.943 55.183  111.419 1.00 79.91  ? 1445 HOH A O   1 
HETATM 10519 O  O   . HOH J 4 .    ? 120.504 45.777  120.718 1.00 45.55  ? 1446 HOH A O   1 
HETATM 10520 O  O   . HOH J 4 .    ? 123.243 90.947  104.669 1.00 38.57  ? 1447 HOH A O   1 
HETATM 10521 O  O   . HOH J 4 .    ? 122.176 97.202  107.929 1.00 45.34  ? 1448 HOH A O   1 
HETATM 10522 O  O   . HOH J 4 .    ? 116.824 99.237  113.103 1.00 46.38  ? 1449 HOH A O   1 
HETATM 10523 O  O   . HOH J 4 .    ? 109.767 94.286  100.080 1.00 32.06  ? 1450 HOH A O   1 
HETATM 10524 O  O   . HOH J 4 .    ? 116.411 71.966  97.507  1.00 38.70  ? 1451 HOH A O   1 
HETATM 10525 O  O   . HOH J 4 .    ? 112.269 72.801  91.922  1.00 49.35  ? 1452 HOH A O   1 
HETATM 10526 O  O   . HOH J 4 .    ? 116.215 68.251  97.991  1.00 42.62  ? 1453 HOH A O   1 
HETATM 10527 O  O   . HOH J 4 .    ? 122.113 98.412  121.340 1.00 41.39  ? 1454 HOH A O   1 
HETATM 10528 O  O   . HOH J 4 .    ? 107.760 94.775  112.472 1.00 29.01  ? 1455 HOH A O   1 
HETATM 10529 O  O   . HOH J 4 .    ? 109.989 94.170  104.574 1.00 41.78  ? 1456 HOH A O   1 
HETATM 10530 O  O   . HOH J 4 .    ? 107.154 94.283  101.558 1.00 46.43  ? 1457 HOH A O   1 
HETATM 10531 O  O   . HOH J 4 .    ? 107.165 86.307  100.231 1.00 38.22  ? 1458 HOH A O   1 
HETATM 10532 O  O   . HOH J 4 .    ? 105.660 86.780  103.213 1.00 50.06  ? 1459 HOH A O   1 
HETATM 10533 O  O   . HOH J 4 .    ? 105.380 79.810  101.549 1.00 38.82  ? 1460 HOH A O   1 
HETATM 10534 O  O   . HOH J 4 .    ? 101.885 81.808  112.778 1.00 32.66  ? 1461 HOH A O   1 
HETATM 10535 O  O   . HOH J 4 .    ? 102.450 83.538  110.258 1.00 45.81  ? 1462 HOH A O   1 
HETATM 10536 O  O   . HOH J 4 .    ? 104.990 81.808  118.530 1.00 44.64  ? 1463 HOH A O   1 
HETATM 10537 O  O   . HOH J 4 .    ? 110.822 78.920  124.026 1.00 41.96  ? 1464 HOH A O   1 
HETATM 10538 O  O   . HOH J 4 .    ? 109.378 83.340  123.521 1.00 52.25  ? 1465 HOH A O   1 
HETATM 10539 O  O   . HOH J 4 .    ? 108.506 87.029  103.390 1.00 35.67  ? 1466 HOH A O   1 
HETATM 10540 O  O   . HOH J 4 .    ? 119.514 99.894  127.001 1.00 61.34  ? 1467 HOH A O   1 
HETATM 10541 O  O   . HOH J 4 .    ? 107.817 93.447  123.746 1.00 67.75  ? 1468 HOH A O   1 
HETATM 10542 O  O   . HOH J 4 .    ? 121.646 95.930  125.374 1.00 80.74  ? 1469 HOH A O   1 
HETATM 10543 O  O   . HOH J 4 .    ? 125.179 92.619  118.313 1.00 43.86  ? 1470 HOH A O   1 
HETATM 10544 O  O   . HOH J 4 .    ? 118.936 67.944  105.492 1.00 52.81  ? 1471 HOH A O   1 
HETATM 10545 O  O   . HOH J 4 .    ? 125.270 95.203  111.234 1.00 36.78  ? 1472 HOH A O   1 
HETATM 10546 O  O   . HOH J 4 .    ? 118.993 95.299  132.322 1.00 40.01  ? 1473 HOH A O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1    LEU 1    1    1    LEU LEU A . n 
A 1 2    LEU 2    2    2    LEU LEU A . n 
A 1 3    VAL 3    3    3    VAL VAL A . n 
A 1 4    VAL 4    4    4    VAL VAL A . n 
A 1 5    GLY 5    5    5    GLY GLY A . n 
A 1 6    PRO 6    6    6    PRO PRO A . n 
A 1 7    LYS 7    7    7    LYS LYS A . n 
A 1 8    PHE 8    8    8    PHE PHE A . n 
A 1 9    ILE 9    9    9    ILE ILE A . n 
A 1 10   ARG 10   10   10   ARG ARG A . n 
A 1 11   ALA 11   11   11   ALA ALA A . n 
A 1 12   ASN 12   12   12   ASN ASN A . n 
A 1 13   GLN 13   13   13   GLN GLN A . n 
A 1 14   GLU 14   14   14   GLU GLU A . n 
A 1 15   TYR 15   15   15   TYR TYR A . n 
A 1 16   THR 16   16   16   THR THR A . n 
A 1 17   LEU 17   17   17   LEU LEU A . n 
A 1 18   VAL 18   18   18   VAL VAL A . n 
A 1 19   ILE 19   19   19   ILE ILE A . n 
A 1 20   SER 20   20   20   SER SER A . n 
A 1 21   ASN 21   21   21   ASN ASN A . n 
A 1 22   PHE 22   22   22   PHE PHE A . n 
A 1 23   ASN 23   23   23   ASN ASN A . n 
A 1 24   SER 24   24   24   SER SER A . n 
A 1 25   GLN 25   25   25   GLN GLN A . n 
A 1 26   LEU 26   26   26   LEU LEU A . n 
A 1 27   SER 27   27   27   SER SER A . n 
A 1 28   LYS 28   28   28   LYS LYS A . n 
A 1 29   VAL 29   29   29   VAL VAL A . n 
A 1 30   ASP 30   30   30   ASP ASP A . n 
A 1 31   LEU 31   31   31   LEU LEU A . n 
A 1 32   LEU 32   32   32   LEU LEU A . n 
A 1 33   LEU 33   33   33   LEU LEU A . n 
A 1 34   LYS 34   34   34   LYS LYS A . n 
A 1 35   LEU 35   35   35   LEU LEU A . n 
A 1 36   GLU 36   36   36   GLU GLU A . n 
A 1 37   GLY 37   37   ?    ?   ?   A . n 
A 1 38   GLU 38   38   ?    ?   ?   A . n 
A 1 39   THR 39   39   ?    ?   ?   A . n 
A 1 40   ASP 40   40   ?    ?   ?   A . n 
A 1 41   ASN 41   41   ?    ?   ?   A . n 
A 1 42   GLY 42   42   ?    ?   ?   A . n 
A 1 43   LEU 43   43   43   LEU LEU A . n 
A 1 44   SER 44   44   44   SER SER A . n 
A 1 45   VAL 45   45   45   VAL VAL A . n 
A 1 46   LEU 46   46   46   LEU LEU A . n 
A 1 47   ASN 47   47   47   ASN ASN A . n 
A 1 48   VAL 48   48   48   VAL VAL A . n 
A 1 49   THR 49   49   49   THR THR A . n 
A 1 50   LYS 50   50   50   LYS LYS A . n 
A 1 51   MET 51   51   51   MET MET A . n 
A 1 52   VAL 52   52   52   VAL VAL A . n 
A 1 53   ASP 53   53   53   ASP ASP A . n 
A 1 54   VAL 54   54   54   VAL VAL A . n 
A 1 55   ARG 55   55   55   ARG ARG A . n 
A 1 56   ARG 56   56   56   ARG ARG A . n 
A 1 57   ASN 57   57   57   ASN ASN A . n 
A 1 58   MET 58   58   58   MET MET A . n 
A 1 59   ASN 59   59   59   ASN ASN A . n 
A 1 60   ARG 60   60   60   ARG ARG A . n 
A 1 61   MET 61   61   61   MET MET A . n 
A 1 62   ILE 62   62   62   ILE ILE A . n 
A 1 63   ASN 63   63   63   ASN ASN A . n 
A 1 64   PHE 64   64   64   PHE PHE A . n 
A 1 65   ASN 65   65   65   ASN ASN A . n 
A 1 66   MET 66   66   66   MET MET A . n 
A 1 67   PRO 67   67   67   PRO PRO A . n 
A 1 68   GLU 68   68   68   GLU GLU A . n 
A 1 69   ASP 69   69   69   ASP ASP A . n 
A 1 70   LEU 70   70   70   LEU LEU A . n 
A 1 71   THR 71   71   71   THR THR A . n 
A 1 72   ALA 72   72   72   ALA ALA A . n 
A 1 73   GLY 73   73   73   GLY GLY A . n 
A 1 74   ASN 74   74   74   ASN ASN A . n 
A 1 75   TYR 75   75   75   TYR TYR A . n 
A 1 76   LYS 76   76   76   LYS LYS A . n 
A 1 77   ILE 77   77   77   ILE ILE A . n 
A 1 78   THR 78   78   78   THR THR A . n 
A 1 79   ILE 79   79   79   ILE ILE A . n 
A 1 80   ASP 80   80   80   ASP ASP A . n 
A 1 81   GLY 81   81   81   GLY GLY A . n 
A 1 82   GLN 82   82   82   GLN GLN A . n 
A 1 83   ARG 83   83   83   ARG ARG A . n 
A 1 84   GLY 84   84   84   GLY GLY A . n 
A 1 85   PHE 85   85   85   PHE PHE A . n 
A 1 86   SER 86   86   86   SER SER A . n 
A 1 87   PHE 87   87   87   PHE PHE A . n 
A 1 88   HIS 88   88   88   HIS HIS A . n 
A 1 89   LYS 89   89   89   LYS LYS A . n 
A 1 90   GLU 90   90   90   GLU GLU A . n 
A 1 91   ALA 91   91   91   ALA ALA A . n 
A 1 92   GLU 92   92   92   GLU GLU A . n 
A 1 93   LEU 93   93   93   LEU LEU A . n 
A 1 94   VAL 94   94   94   VAL VAL A . n 
A 1 95   TYR 95   95   95   TYR TYR A . n 
A 1 96   LEU 96   96   96   LEU LEU A . n 
A 1 97   SER 97   97   97   SER SER A . n 
A 1 98   LYS 98   98   98   LYS LYS A . n 
A 1 99   SER 99   99   99   SER SER A . n 
A 1 100  ILE 100  100  100  ILE ILE A . n 
A 1 101  SER 101  101  101  SER SER A . n 
A 1 102  GLY 102  102  102  GLY GLY A . n 
A 1 103  LEU 103  103  103  LEU LEU A . n 
A 1 104  ILE 104  104  104  ILE ILE A . n 
A 1 105  GLN 105  105  105  GLN GLN A . n 
A 1 106  VAL 106  106  106  VAL VAL A . n 
A 1 107  ASP 107  107  107  ASP ASP A . n 
A 1 108  LYS 108  108  108  LYS LYS A . n 
A 1 109  PRO 109  109  109  PRO PRO A . n 
A 1 110  VAL 110  110  110  VAL VAL A . n 
A 1 111  PHE 111  111  111  PHE PHE A . n 
A 1 112  LYS 112  112  112  LYS LYS A . n 
A 1 113  PRO 113  113  113  PRO PRO A . n 
A 1 114  GLY 114  114  114  GLY GLY A . n 
A 1 115  ASP 115  115  115  ASP ASP A . n 
A 1 116  THR 116  116  116  THR THR A . n 
A 1 117  VAL 117  117  117  VAL VAL A . n 
A 1 118  ASN 118  118  118  ASN ASN A . n 
A 1 119  PHE 119  119  119  PHE PHE A . n 
A 1 120  ARG 120  120  120  ARG ARG A . n 
A 1 121  VAL 121  121  121  VAL VAL A . n 
A 1 122  ILE 122  122  122  ILE ILE A . n 
A 1 123  VAL 123  123  123  VAL VAL A . n 
A 1 124  LEU 124  124  124  LEU LEU A . n 
A 1 125  ASP 125  125  125  ASP ASP A . n 
A 1 126  THR 126  126  126  THR THR A . n 
A 1 127  GLU 127  127  127  GLU GLU A . n 
A 1 128  LEU 128  128  128  LEU LEU A . n 
A 1 129  LYS 129  129  129  LYS LYS A . n 
A 1 130  PRO 130  130  130  PRO PRO A . n 
A 1 131  PRO 131  131  131  PRO PRO A . n 
A 1 132  ALA 132  132  132  ALA ALA A . n 
A 1 133  ARG 133  133  133  ARG ARG A . n 
A 1 134  VAL 134  134  134  VAL VAL A . n 
A 1 135  LYS 135  135  135  LYS LYS A . n 
A 1 136  SER 136  136  136  SER SER A . n 
A 1 137  VAL 137  137  137  VAL VAL A . n 
A 1 138  TYR 138  138  138  TYR TYR A . n 
A 1 139  VAL 139  139  139  VAL VAL A . n 
A 1 140  THR 140  140  140  THR THR A . n 
A 1 141  ILE 141  141  141  ILE ILE A . n 
A 1 142  ARG 142  142  142  ARG ARG A . n 
A 1 143  ASP 143  143  143  ASP ASP A . n 
A 1 144  PRO 144  144  144  PRO PRO A . n 
A 1 145  GLN 145  145  145  GLN GLN A . n 
A 1 146  ARG 146  146  146  ARG ARG A . n 
A 1 147  ASN 147  147  147  ASN ASN A . n 
A 1 148  VAL 148  148  148  VAL VAL A . n 
A 1 149  ILE 149  149  149  ILE ILE A . n 
A 1 150  ARG 150  150  150  ARG ARG A . n 
A 1 151  LYS 151  151  151  LYS LYS A . n 
A 1 152  TRP 152  152  152  TRP TRP A . n 
A 1 153  SER 153  153  153  SER SER A . n 
A 1 154  THR 154  154  154  THR THR A . n 
A 1 155  ALA 155  155  155  ALA ALA A . n 
A 1 156  LYS 156  156  156  LYS LYS A . n 
A 1 157  LEU 157  157  157  LEU LEU A . n 
A 1 158  TYR 158  158  158  TYR TYR A . n 
A 1 159  ALA 159  159  159  ALA ALA A . n 
A 1 160  GLY 160  160  160  GLY GLY A . n 
A 1 161  VAL 161  161  161  VAL VAL A . n 
A 1 162  PHE 162  162  162  PHE PHE A . n 
A 1 163  GLU 163  163  163  GLU GLU A . n 
A 1 164  SER 164  164  164  SER SER A . n 
A 1 165  ASP 165  165  165  ASP ASP A . n 
A 1 166  LEU 166  166  166  LEU LEU A . n 
A 1 167  GLN 167  167  167  GLN GLN A . n 
A 1 168  ILE 168  168  168  ILE ILE A . n 
A 1 169  ALA 169  169  169  ALA ALA A . n 
A 1 170  PRO 170  170  170  PRO PRO A . n 
A 1 171  THR 171  171  171  THR THR A . n 
A 1 172  PRO 172  172  172  PRO PRO A . n 
A 1 173  MET 173  173  173  MET MET A . n 
A 1 174  LEU 174  174  174  LEU LEU A . n 
A 1 175  GLY 175  175  175  GLY GLY A . n 
A 1 176  VAL 176  176  176  VAL VAL A . n 
A 1 177  TRP 177  177  177  TRP TRP A . n 
A 1 178  ASN 178  178  178  ASN ASN A . n 
A 1 179  ILE 179  179  179  ILE ILE A . n 
A 1 180  SER 180  180  180  SER SER A . n 
A 1 181  VAL 181  181  181  VAL VAL A . n 
A 1 182  GLU 182  182  182  GLU GLU A . n 
A 1 183  VAL 183  183  183  VAL VAL A . n 
A 1 184  GLU 184  184  184  GLU GLU A . n 
A 1 185  GLY 185  185  185  GLY GLY A . n 
A 1 186  GLU 186  186  186  GLU GLU A . n 
A 1 187  GLU 187  187  187  GLU GLU A . n 
A 1 188  LEU 188  188  188  LEU LEU A . n 
A 1 189  VAL 189  189  189  VAL VAL A . n 
A 1 190  SER 190  190  190  SER SER A . n 
A 1 191  LYS 191  191  191  LYS LYS A . n 
A 1 192  THR 192  192  192  THR THR A . n 
A 1 193  PHE 193  193  193  PHE PHE A . n 
A 1 194  GLU 194  194  194  GLU GLU A . n 
A 1 195  VAL 195  195  195  VAL VAL A . n 
A 1 196  LYS 196  196  196  LYS LYS A . n 
A 1 197  GLU 197  197  197  GLU GLU A . n 
A 1 198  TYR 198  198  198  TYR TYR A . n 
A 1 199  VAL 199  199  199  VAL VAL A . n 
A 1 200  LEU 200  200  200  LEU LEU A . n 
A 1 201  SER 201  201  201  SER SER A . n 
A 1 202  THR 202  202  202  THR THR A . n 
A 1 203  PHE 203  203  203  PHE PHE A . n 
A 1 204  ASP 204  204  204  ASP ASP A . n 
A 1 205  VAL 205  205  205  VAL VAL A . n 
A 1 206  GLN 206  206  206  GLN GLN A . n 
A 1 207  VAL 207  207  207  VAL VAL A . n 
A 1 208  MET 208  208  208  MET MET A . n 
A 1 209  PRO 209  209  209  PRO PRO A . n 
A 1 210  SER 210  210  210  SER SER A . n 
A 1 211  VAL 211  211  211  VAL VAL A . n 
A 1 212  ILE 212  212  212  ILE ILE A . n 
A 1 213  PRO 213  213  213  PRO PRO A . n 
A 1 214  LEU 214  214  214  LEU LEU A . n 
A 1 215  GLU 215  215  215  GLU GLU A . n 
A 1 216  GLU 216  216  216  GLU GLU A . n 
A 1 217  HIS 217  217  217  HIS HIS A . n 
A 1 218  GLN 218  218  218  GLN GLN A . n 
A 1 219  ALA 219  219  219  ALA ALA A . n 
A 1 220  VAL 220  220  220  VAL VAL A . n 
A 1 221  ASN 221  221  221  ASN ASN A . n 
A 1 222  LEU 222  222  222  LEU LEU A . n 
A 1 223  THR 223  223  223  THR THR A . n 
A 1 224  ILE 224  224  224  ILE ILE A . n 
A 1 225  GLU 225  225  225  GLU GLU A . n 
A 1 226  ALA 226  226  226  ALA ALA A . n 
A 1 227  ASN 227  227  227  ASN ASN A . n 
A 1 228  TYR 228  228  228  TYR TYR A . n 
A 1 229  HIS 229  229  229  HIS HIS A . n 
A 1 230  PHE 230  230  230  PHE PHE A . n 
A 1 231  GLY 231  231  231  GLY GLY A . n 
A 1 232  LYS 232  232  232  LYS LYS A . n 
A 1 233  PRO 233  233  233  PRO PRO A . n 
A 1 234  VAL 234  234  234  VAL VAL A . n 
A 1 235  GLN 235  235  235  GLN GLN A . n 
A 1 236  GLY 236  236  236  GLY GLY A . n 
A 1 237  VAL 237  237  237  VAL VAL A . n 
A 1 238  ALA 238  238  238  ALA ALA A . n 
A 1 239  LYS 239  239  239  LYS LYS A . n 
A 1 240  VAL 240  240  240  VAL VAL A . n 
A 1 241  GLU 241  241  241  GLU GLU A . n 
A 1 242  LEU 242  242  242  LEU LEU A . n 
A 1 243  TYR 243  243  243  TYR TYR A . n 
A 1 244  LEU 244  244  244  LEU LEU A . n 
A 1 245  ASP 245  245  245  ASP ASP A . n 
A 1 246  ASP 246  246  246  ASP ASP A . n 
A 1 247  ASP 247  247  247  ASP ASP A . n 
A 1 248  LYS 248  248  248  LYS LYS A . n 
A 1 249  LEU 249  249  249  LEU LEU A . n 
A 1 250  LYS 250  250  250  LYS LYS A . n 
A 1 251  LEU 251  251  251  LEU LEU A . n 
A 1 252  LYS 252  252  252  LYS LYS A . n 
A 1 253  LYS 253  253  253  LYS LYS A . n 
A 1 254  GLU 254  254  254  GLU GLU A . n 
A 1 255  LEU 255  255  255  LEU LEU A . n 
A 1 256  THR 256  256  256  THR THR A . n 
A 1 257  VAL 257  257  257  VAL VAL A . n 
A 1 258  TYR 258  258  258  TYR TYR A . n 
A 1 259  GLY 259  259  259  GLY GLY A . n 
A 1 260  LYS 260  260  260  LYS LYS A . n 
A 1 261  GLY 261  261  261  GLY GLY A . n 
A 1 262  GLN 262  262  262  GLN GLN A . n 
A 1 263  VAL 263  263  263  VAL VAL A . n 
A 1 264  GLU 264  264  264  GLU GLU A . n 
A 1 265  LEU 265  265  265  LEU LEU A . n 
A 1 266  ARG 266  266  266  ARG ARG A . n 
A 1 267  PHE 267  267  267  PHE PHE A . n 
A 1 268  ASP 268  268  268  ASP ASP A . n 
A 1 269  ASN 269  269  269  ASN ASN A . n 
A 1 270  PHE 270  270  270  PHE PHE A . n 
A 1 271  ALA 271  271  271  ALA ALA A . n 
A 1 272  MET 272  272  272  MET MET A . n 
A 1 273  ASP 273  273  273  ASP ASP A . n 
A 1 274  ALA 274  274  274  ALA ALA A . n 
A 1 275  ASP 275  275  275  ASP ASP A . n 
A 1 276  GLN 276  276  276  GLN GLN A . n 
A 1 277  GLN 277  277  277  GLN GLN A . n 
A 1 278  ASP 278  278  278  ASP ASP A . n 
A 1 279  VAL 279  279  279  VAL VAL A . n 
A 1 280  PRO 280  280  280  PRO PRO A . n 
A 1 281  VAL 281  281  281  VAL VAL A . n 
A 1 282  LYS 282  282  282  LYS LYS A . n 
A 1 283  VAL 283  283  283  VAL VAL A . n 
A 1 284  SER 284  284  284  SER SER A . n 
A 1 285  PHE 285  285  285  PHE PHE A . n 
A 1 286  VAL 286  286  286  VAL VAL A . n 
A 1 287  GLU 287  287  287  GLU GLU A . n 
A 1 288  GLN 288  288  288  GLN GLN A . n 
A 1 289  TYR 289  289  289  TYR TYR A . n 
A 1 290  THR 290  290  290  THR THR A . n 
A 1 291  ASN 291  291  291  ASN ASN A . n 
A 1 292  ARG 292  292  292  ARG ARG A . n 
A 1 293  THR 293  293  293  THR THR A . n 
A 1 294  VAL 294  294  294  VAL VAL A . n 
A 1 295  VAL 295  295  295  VAL VAL A . n 
A 1 296  LYS 296  296  296  LYS LYS A . n 
A 1 297  GLN 297  297  297  GLN GLN A . n 
A 1 298  SER 298  298  298  SER SER A . n 
A 1 299  GLN 299  299  299  GLN GLN A . n 
A 1 300  ILE 300  300  300  ILE ILE A . n 
A 1 301  THR 301  301  301  THR THR A . n 
A 1 302  VAL 302  302  302  VAL VAL A . n 
A 1 303  TYR 303  303  303  TYR TYR A . n 
A 1 304  ARG 304  304  304  ARG ARG A . n 
A 1 305  TYR 305  305  305  TYR TYR A . n 
A 1 306  ALA 306  306  306  ALA ALA A . n 
A 1 307  TYR 307  307  307  TYR TYR A . n 
A 1 308  ARG 308  308  308  ARG ARG A . n 
A 1 309  VAL 309  309  309  VAL VAL A . n 
A 1 310  GLU 310  310  310  GLU GLU A . n 
A 1 311  LEU 311  311  311  LEU LEU A . n 
A 1 312  ILE 312  312  312  ILE ILE A . n 
A 1 313  LYS 313  313  313  LYS LYS A . n 
A 1 314  GLU 314  314  314  GLU GLU A . n 
A 1 315  SER 315  315  315  SER SER A . n 
A 1 316  PRO 316  316  316  PRO PRO A . n 
A 1 317  GLN 317  317  317  GLN GLN A . n 
A 1 318  PHE 318  318  318  PHE PHE A . n 
A 1 319  ARG 319  319  319  ARG ARG A . n 
A 1 320  PRO 320  320  320  PRO PRO A . n 
A 1 321  GLY 321  321  321  GLY GLY A . n 
A 1 322  LEU 322  322  322  LEU LEU A . n 
A 1 323  PRO 323  323  323  PRO PRO A . n 
A 1 324  PHE 324  324  324  PHE PHE A . n 
A 1 325  LYS 325  325  325  LYS LYS A . n 
A 1 326  CYS 326  326  326  CYS CYS A . n 
A 1 327  ALA 327  327  327  ALA ALA A . n 
A 1 328  LEU 328  328  328  LEU LEU A . n 
A 1 329  GLN 329  329  329  GLN GLN A . n 
A 1 330  PHE 330  330  330  PHE PHE A . n 
A 1 331  THR 331  331  331  THR THR A . n 
A 1 332  HIS 332  332  332  HIS HIS A . n 
A 1 333  HIS 333  333  333  HIS HIS A . n 
A 1 334  ASP 334  334  334  ASP ASP A . n 
A 1 335  GLY 335  335  335  GLY GLY A . n 
A 1 336  THR 336  336  336  THR THR A . n 
A 1 337  PRO 337  337  337  PRO PRO A . n 
A 1 338  ALA 338  338  338  ALA ALA A . n 
A 1 339  LYS 339  339  339  LYS LYS A . n 
A 1 340  GLY 340  340  340  GLY GLY A . n 
A 1 341  ILE 341  341  341  ILE ILE A . n 
A 1 342  SER 342  342  342  SER SER A . n 
A 1 343  GLY 343  343  343  GLY GLY A . n 
A 1 344  LYS 344  344  344  LYS LYS A . n 
A 1 345  VAL 345  345  345  VAL VAL A . n 
A 1 346  GLU 346  346  346  GLU GLU A . n 
A 1 347  VAL 347  347  347  VAL VAL A . n 
A 1 348  SER 348  348  348  SER SER A . n 
A 1 349  ASP 349  349  349  ASP ASP A . n 
A 1 350  VAL 350  350  350  VAL VAL A . n 
A 1 351  ARG 351  351  351  ARG ARG A . n 
A 1 352  PHE 352  352  352  PHE PHE A . n 
A 1 353  GLU 353  353  353  GLU GLU A . n 
A 1 354  THR 354  354  354  THR THR A . n 
A 1 355  THR 355  355  355  THR THR A . n 
A 1 356  THR 356  356  356  THR THR A . n 
A 1 357  THR 357  357  357  THR THR A . n 
A 1 358  SER 358  358  358  SER SER A . n 
A 1 359  ASP 359  359  359  ASP ASP A . n 
A 1 360  ASN 360  360  360  ASN ASN A . n 
A 1 361  ASP 361  361  361  ASP ASP A . n 
A 1 362  GLY 362  362  362  GLY GLY A . n 
A 1 363  LEU 363  363  363  LEU LEU A . n 
A 1 364  ILE 364  364  364  ILE ILE A . n 
A 1 365  LYS 365  365  365  LYS LYS A . n 
A 1 366  LEU 366  366  366  LEU LEU A . n 
A 1 367  GLU 367  367  367  GLU GLU A . n 
A 1 368  LEU 368  368  368  LEU LEU A . n 
A 1 369  GLN 369  369  369  GLN GLN A . n 
A 1 370  PRO 370  370  370  PRO PRO A . n 
A 1 371  SER 371  371  371  SER SER A . n 
A 1 372  GLU 372  372  372  GLU GLU A . n 
A 1 373  GLY 373  373  373  GLY GLY A . n 
A 1 374  THR 374  374  374  THR THR A . n 
A 1 375  GLU 375  375  375  GLU GLU A . n 
A 1 376  GLN 376  376  376  GLN GLN A . n 
A 1 377  LEU 377  377  377  LEU LEU A . n 
A 1 378  SER 378  378  378  SER SER A . n 
A 1 379  ILE 379  379  379  ILE ILE A . n 
A 1 380  HIS 380  380  380  HIS HIS A . n 
A 1 381  PHE 381  381  381  PHE PHE A . n 
A 1 382  ASN 382  382  382  ASN ASN A . n 
A 1 383  ALA 383  383  383  ALA ALA A . n 
A 1 384  VAL 384  384  384  VAL VAL A . n 
A 1 385  ASP 385  385  385  ASP ASP A . n 
A 1 386  GLY 386  386  386  GLY GLY A . n 
A 1 387  PHE 387  387  387  PHE PHE A . n 
A 1 388  PHE 388  388  388  PHE PHE A . n 
A 1 389  PHE 389  389  389  PHE PHE A . n 
A 1 390  TYR 390  390  390  TYR TYR A . n 
A 1 391  GLU 391  391  391  GLU GLU A . n 
A 1 392  ASP 392  392  392  ASP ASP A . n 
A 1 393  VAL 393  393  393  VAL VAL A . n 
A 1 394  ASN 394  394  394  ASN ASN A . n 
A 1 395  LYS 395  395  395  LYS LYS A . n 
A 1 396  VAL 396  396  396  VAL VAL A . n 
A 1 397  GLU 397  397  397  GLU GLU A . n 
A 1 398  THR 398  398  398  THR THR A . n 
A 1 399  VAL 399  399  399  VAL VAL A . n 
A 1 400  THR 400  400  400  THR THR A . n 
A 1 401  ASP 401  401  401  ASP ASP A . n 
A 1 402  ALA 402  402  402  ALA ALA A . n 
A 1 403  TYR 403  403  403  TYR TYR A . n 
A 1 404  ILE 404  404  404  ILE ILE A . n 
A 1 405  LYS 405  405  405  LYS LYS A . n 
A 1 406  LEU 406  406  406  LEU LEU A . n 
A 1 407  GLU 407  407  407  GLU GLU A . n 
A 1 408  LEU 408  408  408  LEU LEU A . n 
A 1 409  LYS 409  409  409  LYS LYS A . n 
A 1 410  SER 410  410  410  SER SER A . n 
A 1 411  PRO 411  411  411  PRO PRO A . n 
A 1 412  ILE 412  412  412  ILE ILE A . n 
A 1 413  LYS 413  413  413  LYS LYS A . n 
A 1 414  ARG 414  414  414  ARG ARG A . n 
A 1 415  ASN 415  415  415  ASN ASN A . n 
A 1 416  LYS 416  416  416  LYS LYS A . n 
A 1 417  LEU 417  417  417  LEU LEU A . n 
A 1 418  MET 418  418  418  MET MET A . n 
A 1 419  ARG 419  419  419  ARG ARG A . n 
A 1 420  PHE 420  420  420  PHE PHE A . n 
A 1 421  MET 421  421  421  MET MET A . n 
A 1 422  VAL 422  422  422  VAL VAL A . n 
A 1 423  THR 423  423  423  THR THR A . n 
A 1 424  CYS 424  424  424  CYS CYS A . n 
A 1 425  THR 425  425  425  THR THR A . n 
A 1 426  GLU 426  426  426  GLU GLU A . n 
A 1 427  ARG 427  427  427  ARG ARG A . n 
A 1 428  MET 428  428  428  MET MET A . n 
A 1 429  THR 429  429  429  THR THR A . n 
A 1 430  PHE 430  430  430  PHE PHE A . n 
A 1 431  PHE 431  431  431  PHE PHE A . n 
A 1 432  VAL 432  432  432  VAL VAL A . n 
A 1 433  TYR 433  433  433  TYR TYR A . n 
A 1 434  TYR 434  434  434  TYR TYR A . n 
A 1 435  VAL 435  435  435  VAL VAL A . n 
A 1 436  MET 436  436  436  MET MET A . n 
A 1 437  SER 437  437  437  SER SER A . n 
A 1 438  LYS 438  438  438  LYS LYS A . n 
A 1 439  GLY 439  439  439  GLY GLY A . n 
A 1 440  ASN 440  440  440  ASN ASN A . n 
A 1 441  ILE 441  441  441  ILE ILE A . n 
A 1 442  ILE 442  442  442  ILE ILE A . n 
A 1 443  ASP 443  443  443  ASP ASP A . n 
A 1 444  ALA 444  444  444  ALA ALA A . n 
A 1 445  GLY 445  445  445  GLY GLY A . n 
A 1 446  PHE 446  446  446  PHE PHE A . n 
A 1 447  MET 447  447  447  MET MET A . n 
A 1 448  ARG 448  448  448  ARG ARG A . n 
A 1 449  PRO 449  449  449  PRO PRO A . n 
A 1 450  ASN 450  450  450  ASN ASN A . n 
A 1 451  LYS 451  451  451  LYS LYS A . n 
A 1 452  GLN 452  452  452  GLN GLN A . n 
A 1 453  PRO 453  453  453  PRO PRO A . n 
A 1 454  LYS 454  454  454  LYS LYS A . n 
A 1 455  TYR 455  455  455  TYR TYR A . n 
A 1 456  LEU 456  456  456  LEU LEU A . n 
A 1 457  LEU 457  457  457  LEU LEU A . n 
A 1 458  GLN 458  458  458  GLN GLN A . n 
A 1 459  LEU 459  459  459  LEU LEU A . n 
A 1 460  ASN 460  460  460  ASN ASN A . n 
A 1 461  ALA 461  461  461  ALA ALA A . n 
A 1 462  THR 462  462  462  THR THR A . n 
A 1 463  GLU 463  463  463  GLU GLU A . n 
A 1 464  LYS 464  464  464  LYS LYS A . n 
A 1 465  MET 465  465  465  MET MET A . n 
A 1 466  ILE 466  466  466  ILE ILE A . n 
A 1 467  PRO 467  467  467  PRO PRO A . n 
A 1 468  ARG 468  468  468  ARG ARG A . n 
A 1 469  ALA 469  469  469  ALA ALA A . n 
A 1 470  LYS 470  470  470  LYS LYS A . n 
A 1 471  ILE 471  471  471  ILE ILE A . n 
A 1 472  LEU 472  472  472  LEU LEU A . n 
A 1 473  ILE 473  473  473  ILE ILE A . n 
A 1 474  ALA 474  474  474  ALA ALA A . n 
A 1 475  THR 475  475  475  THR THR A . n 
A 1 476  VAL 476  476  476  VAL VAL A . n 
A 1 477  ALA 477  477  477  ALA ALA A . n 
A 1 478  GLY 478  478  478  GLY GLY A . n 
A 1 479  ARG 479  479  479  ARG ARG A . n 
A 1 480  THR 480  480  480  THR THR A . n 
A 1 481  VAL 481  481  481  VAL VAL A . n 
A 1 482  VAL 482  482  482  VAL VAL A . n 
A 1 483  TYR 483  483  483  TYR TYR A . n 
A 1 484  ASP 484  484  484  ASP ASP A . n 
A 1 485  PHE 485  485  485  PHE PHE A . n 
A 1 486  ALA 486  486  486  ALA ALA A . n 
A 1 487  ASP 487  487  487  ASP ASP A . n 
A 1 488  LEU 488  488  488  LEU LEU A . n 
A 1 489  ALA 489  489  489  ALA ALA A . n 
A 1 490  PHE 490  490  490  PHE PHE A . n 
A 1 491  GLN 491  491  491  GLN GLN A . n 
A 1 492  GLU 492  492  492  GLU GLU A . n 
A 1 493  LEU 493  493  493  LEU LEU A . n 
A 1 494  ARG 494  494  494  ARG ARG A . n 
A 1 495  ASN 495  495  495  ASN ASN A . n 
A 1 496  ASN 496  496  496  ASN ASN A . n 
A 1 497  PHE 497  497  497  PHE PHE A . n 
A 1 498  ASP 498  498  498  ASP ASP A . n 
A 1 499  LEU 499  499  499  LEU LEU A . n 
A 1 500  SER 500  500  500  SER SER A . n 
A 1 501  ILE 501  501  501  ILE ILE A . n 
A 1 502  ASP 502  502  502  ASP ASP A . n 
A 1 503  GLU 503  503  503  GLU GLU A . n 
A 1 504  GLN 504  504  504  GLN GLN A . n 
A 1 505  GLU 505  505  505  GLU GLU A . n 
A 1 506  ILE 506  506  506  ILE ILE A . n 
A 1 507  LYS 507  507  507  LYS LYS A . n 
A 1 508  PRO 508  508  508  PRO PRO A . n 
A 1 509  GLY 509  509  509  GLY GLY A . n 
A 1 510  ARG 510  510  510  ARG ARG A . n 
A 1 511  GLN 511  511  511  GLN GLN A . n 
A 1 512  ILE 512  512  512  ILE ILE A . n 
A 1 513  GLU 513  513  513  GLU GLU A . n 
A 1 514  LEU 514  514  514  LEU LEU A . n 
A 1 515  SER 515  515  515  SER SER A . n 
A 1 516  MET 516  516  516  MET MET A . n 
A 1 517  SER 517  517  517  SER SER A . n 
A 1 518  GLY 518  518  518  GLY GLY A . n 
A 1 519  ARG 519  519  519  ARG ARG A . n 
A 1 520  PRO 520  520  520  PRO PRO A . n 
A 1 521  GLY 521  521  521  GLY GLY A . n 
A 1 522  ALA 522  522  522  ALA ALA A . n 
A 1 523  TYR 523  523  523  TYR TYR A . n 
A 1 524  VAL 524  524  524  VAL VAL A . n 
A 1 525  GLY 525  525  525  GLY GLY A . n 
A 1 526  LEU 526  526  526  LEU LEU A . n 
A 1 527  ALA 527  527  527  ALA ALA A . n 
A 1 528  ALA 528  528  528  ALA ALA A . n 
A 1 529  TYR 529  529  529  TYR TYR A . n 
A 1 530  ASP 530  530  530  ASP ASP A . n 
A 1 531  LYS 531  531  531  LYS LYS A . n 
A 1 532  ALA 532  532  532  ALA ALA A . n 
A 1 533  LEU 533  533  533  LEU LEU A . n 
A 1 534  LEU 534  534  534  LEU LEU A . n 
A 1 535  LEU 535  535  535  LEU LEU A . n 
A 1 536  PHE 536  536  536  PHE PHE A . n 
A 1 537  ASN 537  537  537  ASN ASN A . n 
A 1 538  LYS 538  538  538  LYS LYS A . n 
A 1 539  ASN 539  539  539  ASN ASN A . n 
A 1 540  HIS 540  540  540  HIS HIS A . n 
A 1 541  ASP 541  541  541  ASP ASP A . n 
A 1 542  LEU 542  542  542  LEU LEU A . n 
A 1 543  PHE 543  543  543  PHE PHE A . n 
A 1 544  TRP 544  544  544  TRP TRP A . n 
A 1 545  GLU 545  545  545  GLU GLU A . n 
A 1 546  ASP 546  546  546  ASP ASP A . n 
A 1 547  ILE 547  547  547  ILE ILE A . n 
A 1 548  GLY 548  548  548  GLY GLY A . n 
A 1 549  GLN 549  549  549  GLN GLN A . n 
A 1 550  VAL 550  550  550  VAL VAL A . n 
A 1 551  PHE 551  551  551  PHE PHE A . n 
A 1 552  ASP 552  552  552  ASP ASP A . n 
A 1 553  GLY 553  553  553  GLY GLY A . n 
A 1 554  PHE 554  554  554  PHE PHE A . n 
A 1 555  HIS 555  555  555  HIS HIS A . n 
A 1 556  ALA 556  556  ?    ?   ?   A . n 
A 1 557  ILE 557  557  ?    ?   ?   A . n 
A 1 558  ASN 558  558  ?    ?   ?   A . n 
A 1 559  GLU 559  559  559  GLU GLU A . n 
A 1 560  ASN 560  560  560  ASN ASN A . n 
A 1 561  GLU 561  561  561  GLU GLU A . n 
A 1 562  PHE 562  562  562  PHE PHE A . n 
A 1 563  ASP 563  563  563  ASP ASP A . n 
A 1 564  ILE 564  564  564  ILE ILE A . n 
A 1 565  PHE 565  565  565  PHE PHE A . n 
A 1 566  HIS 566  566  566  HIS HIS A . n 
A 1 567  SER 567  567  567  SER SER A . n 
A 1 568  LEU 568  568  568  LEU LEU A . n 
A 1 569  GLY 569  569  569  GLY GLY A . n 
A 1 570  LEU 570  570  570  LEU LEU A . n 
A 1 571  PHE 571  571  571  PHE PHE A . n 
A 1 572  ALA 572  572  572  ALA ALA A . n 
A 1 573  ARG 573  573  573  ARG ARG A . n 
A 1 574  THR 574  574  574  THR THR A . n 
A 1 575  LEU 575  575  575  LEU LEU A . n 
A 1 576  ASP 576  576  576  ASP ASP A . n 
A 1 577  ASP 577  577  577  ASP ASP A . n 
A 1 578  ILE 578  578  578  ILE ILE A . n 
A 1 579  LEU 579  579  579  LEU LEU A . n 
A 1 580  PHE 580  580  580  PHE PHE A . n 
A 1 581  ASP 581  581  581  ASP ASP A . n 
A 1 582  SER 582  582  582  SER SER A . n 
A 1 583  ALA 583  583  ?    ?   ?   A . n 
A 1 584  ASN 584  584  ?    ?   ?   A . n 
A 1 585  GLU 585  585  ?    ?   ?   A . n 
A 1 586  LYS 586  586  ?    ?   ?   A . n 
A 1 587  THR 587  587  ?    ?   ?   A . n 
A 1 588  GLY 588  588  ?    ?   ?   A . n 
A 1 589  ARG 589  589  ?    ?   ?   A . n 
A 1 590  ASN 590  590  ?    ?   ?   A . n 
A 1 591  ALA 591  591  ?    ?   ?   A . n 
A 1 592  LEU 592  592  ?    ?   ?   A . n 
A 1 593  GLN 593  593  ?    ?   ?   A . n 
A 1 594  SER 594  594  ?    ?   ?   A . n 
A 1 595  GLY 595  595  ?    ?   ?   A . n 
A 1 596  LYS 596  596  ?    ?   ?   A . n 
A 1 597  PRO 597  597  ?    ?   ?   A . n 
A 1 598  ILE 598  598  ?    ?   ?   A . n 
A 1 599  GLY 599  599  ?    ?   ?   A . n 
A 1 600  LYS 600  600  ?    ?   ?   A . n 
A 1 601  LEU 601  601  ?    ?   ?   A . n 
A 1 602  VAL 602  602  ?    ?   ?   A . n 
A 1 603  SER 603  603  ?    ?   ?   A . n 
A 1 604  TYR 604  604  ?    ?   ?   A . n 
A 1 605  ARG 605  605  ?    ?   ?   A . n 
A 1 606  THR 606  606  ?    ?   ?   A . n 
A 1 607  ASN 607  607  ?    ?   ?   A . n 
A 1 608  PHE 608  608  ?    ?   ?   A . n 
A 1 609  GLN 609  609  609  GLN GLN A . n 
A 1 610  GLU 610  610  610  GLU GLU A . n 
A 1 611  SER 611  611  611  SER SER A . n 
A 1 612  TRP 612  612  612  TRP TRP A . n 
A 1 613  LEU 613  613  613  LEU LEU A . n 
A 1 614  TRP 614  614  614  TRP TRP A . n 
A 1 615  LYS 615  615  615  LYS LYS A . n 
A 1 616  ASN 616  616  616  ASN ASN A . n 
A 1 617  VAL 617  617  617  VAL VAL A . n 
A 1 618  SER 618  618  618  SER SER A . n 
A 1 619  ILE 619  619  619  ILE ILE A . n 
A 1 620  GLY 620  620  620  GLY GLY A . n 
A 1 621  ARG 621  621  621  ARG ARG A . n 
A 1 622  SER 622  622  622  SER SER A . n 
A 1 623  GLY 623  623  623  GLY GLY A . n 
A 1 624  SER 624  624  624  SER SER A . n 
A 1 625  ARG 625  625  625  ARG ARG A . n 
A 1 626  LYS 626  626  626  LYS LYS A . n 
A 1 627  LEU 627  627  627  LEU LEU A . n 
A 1 628  ILE 628  628  628  ILE ILE A . n 
A 1 629  GLU 629  629  629  GLU GLU A . n 
A 1 630  VAL 630  630  630  VAL VAL A . n 
A 1 631  VAL 631  631  631  VAL VAL A . n 
A 1 632  PRO 632  632  632  PRO PRO A . n 
A 1 633  ASP 633  633  633  ASP ASP A . n 
A 1 634  THR 634  634  634  THR THR A . n 
A 1 635  THR 635  635  635  THR THR A . n 
A 1 636  THR 636  636  636  THR THR A . n 
A 1 637  SER 637  637  637  SER SER A . n 
A 1 638  TRP 638  638  638  TRP TRP A . n 
A 1 639  TYR 639  639  639  TYR TYR A . n 
A 1 640  LEU 640  640  640  LEU LEU A . n 
A 1 641  THR 641  641  641  THR THR A . n 
A 1 642  GLY 642  642  642  GLY GLY A . n 
A 1 643  PHE 643  643  643  PHE PHE A . n 
A 1 644  SER 644  644  644  SER SER A . n 
A 1 645  ILE 645  645  645  ILE ILE A . n 
A 1 646  ASP 646  646  646  ASP ASP A . n 
A 1 647  PRO 647  647  647  PRO PRO A . n 
A 1 648  VAL 648  648  648  VAL VAL A . n 
A 1 649  TYR 649  649  649  TYR TYR A . n 
A 1 650  GLY 650  650  650  GLY GLY A . n 
A 1 651  LEU 651  651  651  LEU LEU A . n 
A 1 652  GLY 652  652  652  GLY GLY A . n 
A 1 653  ILE 653  653  653  ILE ILE A . n 
A 1 654  ILE 654  654  654  ILE ILE A . n 
A 1 655  LYS 655  655  655  LYS LYS A . n 
A 1 656  LYS 656  656  656  LYS LYS A . n 
A 1 657  PRO 657  657  657  PRO PRO A . n 
A 1 658  ILE 658  658  658  ILE ILE A . n 
A 1 659  GLN 659  659  659  GLN GLN A . n 
A 1 660  PHE 660  660  660  PHE PHE A . n 
A 1 661  THR 661  661  661  THR THR A . n 
A 1 662  THR 662  662  662  THR THR A . n 
A 1 663  VAL 663  663  663  VAL VAL A . n 
A 1 664  GLN 664  664  664  GLN GLN A . n 
A 1 665  PRO 665  665  665  PRO PRO A . n 
A 1 666  PHE 666  666  666  PHE PHE A . n 
A 1 667  TYR 667  667  667  TYR TYR A . n 
A 1 668  ILE 668  668  668  ILE ILE A . n 
A 1 669  VAL 669  669  669  VAL VAL A . n 
A 1 670  GLU 670  670  670  GLU GLU A . n 
A 1 671  ASN 671  671  671  ASN ASN A . n 
A 1 672  LEU 672  672  672  LEU LEU A . n 
A 1 673  PRO 673  673  673  PRO PRO A . n 
A 1 674  TYR 674  674  674  TYR TYR A . n 
A 1 675  SER 675  675  675  SER SER A . n 
A 1 676  ILE 676  676  676  ILE ILE A . n 
A 1 677  LYS 677  677  677  LYS LYS A . n 
A 1 678  ARG 678  678  678  ARG ARG A . n 
A 1 679  GLY 679  679  679  GLY GLY A . n 
A 1 680  GLU 680  680  680  GLU GLU A . n 
A 1 681  ALA 681  681  681  ALA ALA A . n 
A 1 682  VAL 682  682  682  VAL VAL A . n 
A 1 683  VAL 683  683  683  VAL VAL A . n 
A 1 684  LEU 684  684  684  LEU LEU A . n 
A 1 685  GLN 685  685  685  GLN GLN A . n 
A 1 686  PHE 686  686  686  PHE PHE A . n 
A 1 687  THR 687  687  687  THR THR A . n 
A 1 688  LEU 688  688  688  LEU LEU A . n 
A 1 689  PHE 689  689  689  PHE PHE A . n 
A 1 690  ASN 690  690  690  ASN ASN A . n 
A 1 691  ASN 691  691  691  ASN ASN A . n 
A 1 692  LEU 692  692  692  LEU LEU A . n 
A 1 693  GLY 693  693  693  GLY GLY A . n 
A 1 694  ALA 694  694  694  ALA ALA A . n 
A 1 695  GLU 695  695  695  GLU GLU A . n 
A 1 696  TYR 696  696  696  TYR TYR A . n 
A 1 697  ILE 697  697  697  ILE ILE A . n 
A 1 698  ALA 698  698  698  ALA ALA A . n 
A 1 699  ASP 699  699  699  ASP ASP A . n 
A 1 700  VAL 700  700  700  VAL VAL A . n 
A 1 701  THR 701  701  701  THR THR A . n 
A 1 702  LEU 702  702  702  LEU LEU A . n 
A 1 703  TYR 703  703  703  TYR TYR A . n 
A 1 704  ASN 704  704  704  ASN ASN A . n 
A 1 705  VAL 705  705  705  VAL VAL A . n 
A 1 706  ALA 706  706  706  ALA ALA A . n 
A 1 707  ASN 707  707  707  ASN ASN A . n 
A 1 708  GLN 708  708  708  GLN GLN A . n 
A 1 709  THR 709  709  709  THR THR A . n 
A 1 710  GLU 710  710  710  GLU GLU A . n 
A 1 711  PHE 711  711  711  PHE PHE A . n 
A 1 712  VAL 712  712  712  VAL VAL A . n 
A 1 713  GLY 713  713  713  GLY GLY A . n 
A 1 714  ARG 714  714  714  ARG ARG A . n 
A 1 715  PRO 715  715  715  PRO PRO A . n 
A 1 716  ASN 716  716  716  ASN ASN A . n 
A 1 717  THR 717  717  717  THR THR A . n 
A 1 718  ASP 718  718  718  ASP ASP A . n 
A 1 719  LEU 719  719  719  LEU LEU A . n 
A 1 720  SER 720  720  720  SER SER A . n 
A 1 721  TYR 721  721  721  TYR TYR A . n 
A 1 722  THR 722  722  722  THR THR A . n 
A 1 723  LYS 723  723  723  LYS LYS A . n 
A 1 724  SER 724  724  724  SER SER A . n 
A 1 725  VAL 725  725  725  VAL VAL A . n 
A 1 726  SER 726  726  726  SER SER A . n 
A 1 727  VAL 727  727  727  VAL VAL A . n 
A 1 728  PRO 728  728  728  PRO PRO A . n 
A 1 729  PRO 729  729  729  PRO PRO A . n 
A 1 730  LYS 730  730  730  LYS LYS A . n 
A 1 731  VAL 731  731  731  VAL VAL A . n 
A 1 732  GLY 732  732  732  GLY GLY A . n 
A 1 733  VAL 733  733  733  VAL VAL A . n 
A 1 734  PRO 734  734  734  PRO PRO A . n 
A 1 735  ILE 735  735  735  ILE ILE A . n 
A 1 736  SER 736  736  736  SER SER A . n 
A 1 737  PHE 737  737  737  PHE PHE A . n 
A 1 738  LEU 738  738  738  LEU LEU A . n 
A 1 739  ILE 739  739  739  ILE ILE A . n 
A 1 740  LYS 740  740  740  LYS LYS A . n 
A 1 741  ALA 741  741  741  ALA ALA A . n 
A 1 742  ARG 742  742  742  ARG ARG A . n 
A 1 743  LYS 743  743  743  LYS LYS A . n 
A 1 744  LEU 744  744  744  LEU LEU A . n 
A 1 745  GLY 745  745  745  GLY GLY A . n 
A 1 746  GLU 746  746  746  GLU GLU A . n 
A 1 747  MET 747  747  747  MET MET A . n 
A 1 748  ALA 748  748  748  ALA ALA A . n 
A 1 749  VAL 749  749  749  VAL VAL A . n 
A 1 750  ARG 750  750  750  ARG ARG A . n 
A 1 751  VAL 751  751  751  VAL VAL A . n 
A 1 752  LYS 752  752  752  LYS LYS A . n 
A 1 753  ALA 753  753  753  ALA ALA A . n 
A 1 754  SER 754  754  754  SER SER A . n 
A 1 755  ILE 755  755  755  ILE ILE A . n 
A 1 756  MET 756  756  756  MET MET A . n 
A 1 757  LEU 757  757  757  LEU LEU A . n 
A 1 758  GLY 758  758  758  GLY GLY A . n 
A 1 759  HIS 759  759  759  HIS HIS A . n 
A 1 760  GLU 760  760  760  GLU GLU A . n 
A 1 761  THR 761  761  761  THR THR A . n 
A 1 762  ASP 762  762  762  ASP ASP A . n 
A 1 763  ALA 763  763  763  ALA ALA A . n 
A 1 764  LEU 764  764  764  LEU LEU A . n 
A 1 765  GLU 765  765  765  GLU GLU A . n 
A 1 766  LYS 766  766  766  LYS LYS A . n 
A 1 767  VAL 767  767  767  VAL VAL A . n 
A 1 768  ILE 768  768  768  ILE ILE A . n 
A 1 769  ARG 769  769  769  ARG ARG A . n 
A 1 770  VAL 770  770  770  VAL VAL A . n 
A 1 771  MET 771  771  771  MET MET A . n 
A 1 772  PRO 772  772  772  PRO PRO A . n 
A 1 773  GLU 773  773  773  GLU GLU A . n 
A 1 774  SER 774  774  774  SER SER A . n 
A 1 775  LEU 775  775  775  LEU LEU A . n 
A 1 776  VAL 776  776  776  VAL VAL A . n 
A 1 777  GLN 777  777  777  GLN GLN A . n 
A 1 778  PRO 778  778  778  PRO PRO A . n 
A 1 779  ARG 779  779  779  ARG ARG A . n 
A 1 780  MET 780  780  780  MET MET A . n 
A 1 781  ASP 781  781  781  ASP ASP A . n 
A 1 782  THR 782  782  782  THR THR A . n 
A 1 783  ARG 783  783  783  ARG ARG A . n 
A 1 784  PHE 784  784  784  PHE PHE A . n 
A 1 785  PHE 785  785  785  PHE PHE A . n 
A 1 786  CYS 786  786  786  CYS CYS A . n 
A 1 787  PHE 787  787  787  PHE PHE A . n 
A 1 788  ASP 788  788  788  ASP ASP A . n 
A 1 789  ASP 789  789  789  ASP ASP A . n 
A 1 790  HIS 790  790  790  HIS HIS A . n 
A 1 791  LYS 791  791  791  LYS LYS A . n 
A 1 792  ASN 792  792  792  ASN ASN A . n 
A 1 793  GLN 793  793  793  GLN GLN A . n 
A 1 794  THR 794  794  794  THR THR A . n 
A 1 795  PHE 795  795  795  PHE PHE A . n 
A 1 796  PRO 796  796  796  PRO PRO A . n 
A 1 797  ILE 797  797  797  ILE ILE A . n 
A 1 798  ASN 798  798  798  ASN ASN A . n 
A 1 799  LEU 799  799  799  LEU LEU A . n 
A 1 800  ASP 800  800  800  ASP ASP A . n 
A 1 801  ILE 801  801  801  ILE ILE A . n 
A 1 802  ASN 802  802  802  ASN ASN A . n 
A 1 803  LYS 803  803  803  LYS LYS A . n 
A 1 804  LYS 804  804  804  LYS LYS A . n 
A 1 805  ALA 805  805  805  ALA ALA A . n 
A 1 806  ASP 806  806  806  ASP ASP A . n 
A 1 807  SER 807  807  807  SER SER A . n 
A 1 808  GLY 808  808  808  GLY GLY A . n 
A 1 809  SER 809  809  809  SER SER A . n 
A 1 810  THR 810  810  810  THR THR A . n 
A 1 811  LYS 811  811  811  LYS LYS A . n 
A 1 812  ILE 812  812  812  ILE ILE A . n 
A 1 813  GLU 813  813  813  GLU GLU A . n 
A 1 814  PHE 814  814  814  PHE PHE A . n 
A 1 815  ARG 815  815  815  ARG ARG A . n 
A 1 816  LEU 816  816  816  LEU LEU A . n 
A 1 817  ASN 817  817  817  ASN ASN A . n 
A 1 818  PRO 818  818  818  PRO PRO A . n 
A 1 819  ASN 819  819  819  ASN ASN A . n 
A 1 820  LEU 820  820  820  LEU LEU A . n 
A 1 821  LEU 821  821  821  LEU LEU A . n 
A 1 822  THR 822  822  822  THR THR A . n 
A 1 823  THR 823  823  823  THR THR A . n 
A 1 824  VAL 824  824  824  VAL VAL A . n 
A 1 825  ILE 825  825  825  ILE ILE A . n 
A 1 826  LYS 826  826  826  LYS LYS A . n 
A 1 827  ASN 827  827  827  ASN ASN A . n 
A 1 828  LEU 828  828  828  LEU LEU A . n 
A 1 829  ASP 829  829  829  ASP ASP A . n 
A 1 830  HIS 830  830  830  HIS HIS A . n 
A 1 831  LEU 831  831  831  LEU LEU A . n 
A 1 832  LEU 832  832  832  LEU LEU A . n 
A 1 833  GLY 833  833  833  GLY GLY A . n 
A 1 834  VAL 834  834  834  VAL VAL A . n 
A 1 835  PRO 835  835  835  PRO PRO A . n 
A 1 836  THR 836  836  836  THR THR A . n 
A 1 837  GLY 837  837  837  GLY GLY A . n 
A 1 838  CYS 838  838  838  CYS CYS A . n 
A 1 839  GLY 839  839  839  GLY GLY A . n 
A 1 840  GLU 840  840  840  GLU GLU A . n 
A 1 841  GLN 841  841  841  GLN GLN A . n 
A 1 842  ASN 842  842  842  ASN ASN A . n 
A 1 843  MET 843  843  843  MET MET A . n 
A 1 844  VAL 844  844  844  VAL VAL A . n 
A 1 845  LYS 845  845  845  LYS LYS A . n 
A 1 846  PHE 846  846  846  PHE PHE A . n 
A 1 847  VAL 847  847  847  VAL VAL A . n 
A 1 848  PRO 848  848  848  PRO PRO A . n 
A 1 849  ASN 849  849  849  ASN ASN A . n 
A 1 850  ILE 850  850  850  ILE ILE A . n 
A 1 851  LEU 851  851  851  LEU LEU A . n 
A 1 852  VAL 852  852  852  VAL VAL A . n 
A 1 853  LEU 853  853  853  LEU LEU A . n 
A 1 854  ASP 854  854  854  ASP ASP A . n 
A 1 855  TYR 855  855  855  TYR TYR A . n 
A 1 856  LEU 856  856  856  LEU LEU A . n 
A 1 857  HIS 857  857  857  HIS HIS A . n 
A 1 858  ALA 858  858  858  ALA ALA A . n 
A 1 859  ILE 859  859  859  ILE ILE A . n 
A 1 860  GLY 860  860  860  GLY GLY A . n 
A 1 861  SER 861  861  861  SER SER A . n 
A 1 862  LYS 862  862  862  LYS LYS A . n 
A 1 863  GLU 863  863  863  GLU GLU A . n 
A 1 864  GLN 864  864  864  GLN GLN A . n 
A 1 865  HIS 865  865  865  HIS HIS A . n 
A 1 866  LEU 866  866  866  LEU LEU A . n 
A 1 867  ILE 867  867  867  ILE ILE A . n 
A 1 868  ASP 868  868  868  ASP ASP A . n 
A 1 869  LYS 869  869  869  LYS LYS A . n 
A 1 870  ALA 870  870  870  ALA ALA A . n 
A 1 871  THR 871  871  871  THR THR A . n 
A 1 872  ASN 872  872  872  ASN ASN A . n 
A 1 873  LEU 873  873  873  LEU LEU A . n 
A 1 874  LEU 874  874  874  LEU LEU A . n 
A 1 875  ARG 875  875  875  ARG ARG A . n 
A 1 876  GLN 876  876  876  GLN GLN A . n 
A 1 877  GLY 877  877  877  GLY GLY A . n 
A 1 878  TYR 878  878  878  TYR TYR A . n 
A 1 879  GLN 879  879  879  GLN GLN A . n 
A 1 880  ASN 880  880  880  ASN ASN A . n 
A 1 881  GLN 881  881  881  GLN GLN A . n 
A 1 882  MET 882  882  882  MET MET A . n 
A 1 883  ARG 883  883  883  ARG ARG A . n 
A 1 884  TYR 884  884  884  TYR TYR A . n 
A 1 885  ARG 885  885  885  ARG ARG A . n 
A 1 886  GLN 886  886  886  GLN GLN A . n 
A 1 887  THR 887  887  887  THR THR A . n 
A 1 888  ASP 888  888  888  ASP ASP A . n 
A 1 889  GLY 889  889  889  GLY GLY A . n 
A 1 890  SER 890  890  890  SER SER A . n 
A 1 891  PHE 891  891  891  PHE PHE A . n 
A 1 892  GLY 892  892  892  GLY GLY A . n 
A 1 893  LEU 893  893  893  LEU LEU A . n 
A 1 894  TRP 894  894  894  TRP TRP A . n 
A 1 895  GLU 895  895  895  GLU GLU A . n 
A 1 896  THR 896  896  896  THR THR A . n 
A 1 897  THR 897  897  897  THR THR A . n 
A 1 898  ASN 898  898  898  ASN ASN A . n 
A 1 899  GLY 899  899  899  GLY GLY A . n 
A 1 900  SER 900  900  900  SER SER A . n 
A 1 901  VAL 901  901  901  VAL VAL A . n 
A 1 902  PHE 902  902  902  PHE PHE A . n 
A 1 903  LEU 903  903  903  LEU LEU A . n 
A 1 904  THR 904  904  904  THR THR A . n 
A 1 905  ALA 905  905  905  ALA ALA A . n 
A 1 906  PHE 906  906  906  PHE PHE A . n 
A 1 907  VAL 907  907  907  VAL VAL A . n 
A 1 908  GLY 908  908  908  GLY GLY A . n 
A 1 909  THR 909  909  909  THR THR A . n 
A 1 910  SER 910  910  910  SER SER A . n 
A 1 911  MET 911  911  911  MET MET A . n 
A 1 912  GLN 912  912  912  GLN GLN A . n 
A 1 913  THR 913  913  913  THR THR A . n 
A 1 914  ALA 914  914  914  ALA ALA A . n 
A 1 915  VAL 915  915  915  VAL VAL A . n 
A 1 916  LYS 916  916  916  LYS LYS A . n 
A 1 917  TYR 917  917  917  TYR TYR A . n 
A 1 918  ILE 918  918  918  ILE ILE A . n 
A 1 919  SER 919  919  919  SER SER A . n 
A 1 920  ASP 920  920  920  ASP ASP A . n 
A 1 921  ILE 921  921  921  ILE ILE A . n 
A 1 922  ASP 922  922  922  ASP ASP A . n 
A 1 923  ALA 923  923  923  ALA ALA A . n 
A 1 924  ALA 924  924  924  ALA ALA A . n 
A 1 925  MET 925  925  925  MET MET A . n 
A 1 926  VAL 926  926  926  VAL VAL A . n 
A 1 927  GLU 927  927  927  GLU GLU A . n 
A 1 928  LYS 928  928  928  LYS LYS A . n 
A 1 929  ALA 929  929  929  ALA ALA A . n 
A 1 930  LEU 930  930  930  LEU LEU A . n 
A 1 931  ASP 931  931  931  ASP ASP A . n 
A 1 932  TRP 932  932  932  TRP TRP A . n 
A 1 933  LEU 933  933  933  LEU LEU A . n 
A 1 934  ALA 934  934  934  ALA ALA A . n 
A 1 935  SER 935  935  935  SER SER A . n 
A 1 936  LYS 936  936  936  LYS LYS A . n 
A 1 937  GLN 937  937  937  GLN GLN A . n 
A 1 938  HIS 938  938  938  HIS HIS A . n 
A 1 939  PHE 939  939  939  PHE PHE A . n 
A 1 940  SER 940  940  940  SER SER A . n 
A 1 941  GLY 941  941  941  GLY GLY A . n 
A 1 942  ARG 942  942  942  ARG ARG A . n 
A 1 943  PHE 943  943  943  PHE PHE A . n 
A 1 944  ASP 944  944  944  ASP ASP A . n 
A 1 945  LYS 945  945  945  LYS LYS A . n 
A 1 946  ALA 946  946  946  ALA ALA A . n 
A 1 947  GLY 947  947  947  GLY GLY A . n 
A 1 948  ALA 948  948  948  ALA ALA A . n 
A 1 949  GLU 949  949  949  GLU GLU A . n 
A 1 950  TYR 950  950  950  TYR TYR A . n 
A 1 951  HIS 951  951  951  HIS HIS A . n 
A 1 952  LYS 952  952  952  LYS LYS A . n 
A 1 953  GLU 953  953  953  GLU GLU A . n 
A 1 954  MET 954  954  954  MET MET A . n 
A 1 955  GLN 955  955  955  GLN GLN A . n 
A 1 956  GLY 956  956  956  GLY GLY A . n 
A 1 957  GLY 957  957  957  GLY GLY A . n 
A 1 958  LEU 958  958  958  LEU LEU A . n 
A 1 959  ARG 959  959  959  ARG ARG A . n 
A 1 960  ASN 960  960  960  ASN ASN A . n 
A 1 961  GLY 961  961  961  GLY GLY A . n 
A 1 962  VAL 962  962  962  VAL VAL A . n 
A 1 963  ALA 963  963  963  ALA ALA A . n 
A 1 964  LEU 964  964  964  LEU LEU A . n 
A 1 965  THR 965  965  965  THR THR A . n 
A 1 966  SER 966  966  966  SER SER A . n 
A 1 967  TYR 967  967  967  TYR TYR A . n 
A 1 968  VAL 968  968  968  VAL VAL A . n 
A 1 969  LEU 969  969  969  LEU LEU A . n 
A 1 970  MET 970  970  970  MET MET A . n 
A 1 971  ALA 971  971  971  ALA ALA A . n 
A 1 972  LEU 972  972  972  LEU LEU A . n 
A 1 973  LEU 973  973  973  LEU LEU A . n 
A 1 974  GLU 974  974  974  GLU GLU A . n 
A 1 975  ASN 975  975  975  ASN ASN A . n 
A 1 976  ASP 976  976  976  ASP ASP A . n 
A 1 977  ILE 977  977  977  ILE ILE A . n 
A 1 978  ALA 978  978  978  ALA ALA A . n 
A 1 979  LYS 979  979  979  LYS LYS A . n 
A 1 980  ALA 980  980  980  ALA ALA A . n 
A 1 981  LYS 981  981  981  LYS LYS A . n 
A 1 982  HIS 982  982  982  HIS HIS A . n 
A 1 983  ALA 983  983  983  ALA ALA A . n 
A 1 984  GLU 984  984  984  GLU GLU A . n 
A 1 985  VAL 985  985  985  VAL VAL A . n 
A 1 986  ILE 986  986  986  ILE ILE A . n 
A 1 987  GLN 987  987  987  GLN GLN A . n 
A 1 988  LYS 988  988  988  LYS LYS A . n 
A 1 989  GLY 989  989  989  GLY GLY A . n 
A 1 990  MET 990  990  990  MET MET A . n 
A 1 991  THR 991  991  991  THR THR A . n 
A 1 992  TYR 992  992  992  TYR TYR A . n 
A 1 993  LEU 993  993  993  LEU LEU A . n 
A 1 994  SER 994  994  994  SER SER A . n 
A 1 995  ASN 995  995  995  ASN ASN A . n 
A 1 996  GLN 996  996  996  GLN GLN A . n 
A 1 997  PHE 997  997  997  PHE PHE A . n 
A 1 998  GLY 998  998  998  GLY GLY A . n 
A 1 999  SER 999  999  999  SER SER A . n 
A 1 1000 ILE 1000 1000 1000 ILE ILE A . n 
A 1 1001 ASN 1001 1001 1001 ASN ASN A . n 
A 1 1002 ASN 1002 1002 1002 ASN ASN A . n 
A 1 1003 ALA 1003 1003 1003 ALA ALA A . n 
A 1 1004 TYR 1004 1004 1004 TYR TYR A . n 
A 1 1005 ASP 1005 1005 1005 ASP ASP A . n 
A 1 1006 LEU 1006 1006 1006 LEU LEU A . n 
A 1 1007 SER 1007 1007 1007 SER SER A . n 
A 1 1008 ILE 1008 1008 1008 ILE ILE A . n 
A 1 1009 ALA 1009 1009 1009 ALA ALA A . n 
A 1 1010 THR 1010 1010 1010 THR THR A . n 
A 1 1011 TYR 1011 1011 1011 TYR TYR A . n 
A 1 1012 ALA 1012 1012 1012 ALA ALA A . n 
A 1 1013 MET 1013 1013 1013 MET MET A . n 
A 1 1014 MET 1014 1014 1014 MET MET A . n 
A 1 1015 LEU 1015 1015 1015 LEU LEU A . n 
A 1 1016 ASN 1016 1016 1016 ASN ASN A . n 
A 1 1017 GLY 1017 1017 1017 GLY GLY A . n 
A 1 1018 HIS 1018 1018 1018 HIS HIS A . n 
A 1 1019 THR 1019 1019 1019 THR THR A . n 
A 1 1020 MET 1020 1020 1020 MET MET A . n 
A 1 1021 LYS 1021 1021 1021 LYS LYS A . n 
A 1 1022 GLU 1022 1022 1022 GLU GLU A . n 
A 1 1023 GLU 1023 1023 1023 GLU GLU A . n 
A 1 1024 ALA 1024 1024 1024 ALA ALA A . n 
A 1 1025 LEU 1025 1025 1025 LEU LEU A . n 
A 1 1026 ASN 1026 1026 1026 ASN ASN A . n 
A 1 1027 LYS 1027 1027 1027 LYS LYS A . n 
A 1 1028 LEU 1028 1028 1028 LEU LEU A . n 
A 1 1029 ILE 1029 1029 1029 ILE ILE A . n 
A 1 1030 ASP 1030 1030 1030 ASP ASP A . n 
A 1 1031 MET 1031 1031 1031 MET MET A . n 
A 1 1032 SER 1032 1032 1032 SER SER A . n 
A 1 1033 PHE 1033 1033 1033 PHE PHE A . n 
A 1 1034 ILE 1034 1034 1034 ILE ILE A . n 
A 1 1035 ASP 1035 1035 1035 ASP ASP A . n 
A 1 1036 ALA 1036 1036 1036 ALA ALA A . n 
A 1 1037 ASP 1037 1037 1037 ASP ASP A . n 
A 1 1038 LYS 1038 1038 1038 LYS LYS A . n 
A 1 1039 ASN 1039 1039 1039 ASN ASN A . n 
A 1 1040 GLU 1040 1040 1040 GLU GLU A . n 
A 1 1041 ARG 1041 1041 1041 ARG ARG A . n 
A 1 1042 PHE 1042 1042 1042 PHE PHE A . n 
A 1 1043 TRP 1043 1043 1043 TRP TRP A . n 
A 1 1044 ASN 1044 1044 1044 ASN ASN A . n 
A 1 1045 THR 1045 1045 1045 THR THR A . n 
A 1 1046 THR 1046 1046 1046 THR THR A . n 
A 1 1047 ASN 1047 1047 1047 ASN ASN A . n 
A 1 1048 PRO 1048 1048 1048 PRO PRO A . n 
A 1 1049 ILE 1049 1049 1049 ILE ILE A . n 
A 1 1050 GLU 1050 1050 1050 GLU GLU A . n 
A 1 1051 THR 1051 1051 1051 THR THR A . n 
A 1 1052 THR 1052 1052 1052 THR THR A . n 
A 1 1053 ALA 1053 1053 1053 ALA ALA A . n 
A 1 1054 TYR 1054 1054 1054 TYR TYR A . n 
A 1 1055 ALA 1055 1055 1055 ALA ALA A . n 
A 1 1056 LEU 1056 1056 1056 LEU LEU A . n 
A 1 1057 LEU 1057 1057 1057 LEU LEU A . n 
A 1 1058 SER 1058 1058 1058 SER SER A . n 
A 1 1059 PHE 1059 1059 1059 PHE PHE A . n 
A 1 1060 VAL 1060 1060 1060 VAL VAL A . n 
A 1 1061 MET 1061 1061 1061 MET MET A . n 
A 1 1062 ALA 1062 1062 1062 ALA ALA A . n 
A 1 1063 GLU 1063 1063 1063 GLU GLU A . n 
A 1 1064 LYS 1064 1064 1064 LYS LYS A . n 
A 1 1065 TYR 1065 1065 1065 TYR TYR A . n 
A 1 1066 THR 1066 1066 1066 THR THR A . n 
A 1 1067 ASP 1067 1067 1067 ASP ASP A . n 
A 1 1068 GLY 1068 1068 1068 GLY GLY A . n 
A 1 1069 ILE 1069 1069 1069 ILE ILE A . n 
A 1 1070 PRO 1070 1070 1070 PRO PRO A . n 
A 1 1071 VAL 1071 1071 1071 VAL VAL A . n 
A 1 1072 MET 1072 1072 1072 MET MET A . n 
A 1 1073 ASN 1073 1073 1073 ASN ASN A . n 
A 1 1074 TRP 1074 1074 1074 TRP TRP A . n 
A 1 1075 LEU 1075 1075 1075 LEU LEU A . n 
A 1 1076 VAL 1076 1076 1076 VAL VAL A . n 
A 1 1077 ASN 1077 1077 1077 ASN ASN A . n 
A 1 1078 GLN 1078 1078 1078 GLN GLN A . n 
A 1 1079 ARG 1079 1079 1079 ARG ARG A . n 
A 1 1080 TYR 1080 1080 1080 TYR TYR A . n 
A 1 1081 VAL 1081 1081 1081 VAL VAL A . n 
A 1 1082 THR 1082 1082 1082 THR THR A . n 
A 1 1083 GLY 1083 1083 1083 GLY GLY A . n 
A 1 1084 SER 1084 1084 1084 SER SER A . n 
A 1 1085 PHE 1085 1085 1085 PHE PHE A . n 
A 1 1086 PRO 1086 1086 1086 PRO PRO A . n 
A 1 1087 SER 1087 1087 1087 SER SER A . n 
A 1 1088 THR 1088 1088 1088 THR THR A . n 
A 1 1089 GLN 1089 1089 1089 GLN GLN A . n 
A 1 1090 ASP 1090 1090 1090 ASP ASP A . n 
A 1 1091 THR 1091 1091 1091 THR THR A . n 
A 1 1092 PHE 1092 1092 1092 PHE PHE A . n 
A 1 1093 VAL 1093 1093 1093 VAL VAL A . n 
A 1 1094 GLY 1094 1094 1094 GLY GLY A . n 
A 1 1095 LEU 1095 1095 1095 LEU LEU A . n 
A 1 1096 LYS 1096 1096 1096 LYS LYS A . n 
A 1 1097 ALA 1097 1097 1097 ALA ALA A . n 
A 1 1098 LEU 1098 1098 1098 LEU LEU A . n 
A 1 1099 THR 1099 1099 1099 THR THR A . n 
A 1 1100 LYS 1100 1100 1100 LYS LYS A . n 
A 1 1101 MET 1101 1101 1101 MET MET A . n 
A 1 1102 ALA 1102 1102 1102 ALA ALA A . n 
A 1 1103 GLU 1103 1103 1103 GLU GLU A . n 
A 1 1104 LYS 1104 1104 1104 LYS LYS A . n 
A 1 1105 ILE 1105 1105 1105 ILE ILE A . n 
A 1 1106 SER 1106 1106 1106 SER SER A . n 
A 1 1107 PRO 1107 1107 1107 PRO PRO A . n 
A 1 1108 SER 1108 1108 1108 SER SER A . n 
A 1 1109 ARG 1109 1109 1109 ARG ARG A . n 
A 1 1110 ASN 1110 1110 1110 ASN ASN A . n 
A 1 1111 ASP 1111 1111 1111 ASP ASP A . n 
A 1 1112 TYR 1112 1112 1112 TYR TYR A . n 
A 1 1113 THR 1113 1113 1113 THR THR A . n 
A 1 1114 VAL 1114 1114 1114 VAL VAL A . n 
A 1 1115 GLN 1115 1115 1115 GLN GLN A . n 
A 1 1116 LEU 1116 1116 1116 LEU LEU A . n 
A 1 1117 LYS 1117 1117 1117 LYS LYS A . n 
A 1 1118 TYR 1118 1118 1118 TYR TYR A . n 
A 1 1119 LYS 1119 1119 1119 LYS LYS A . n 
A 1 1120 LYS 1120 1120 1120 LYS LYS A . n 
A 1 1121 SER 1121 1121 1121 SER SER A . n 
A 1 1122 ALA 1122 1122 1122 ALA ALA A . n 
A 1 1123 LYS 1123 1123 1123 LYS LYS A . n 
A 1 1124 TYR 1124 1124 1124 TYR TYR A . n 
A 1 1125 PHE 1125 1125 1125 PHE PHE A . n 
A 1 1126 LYS 1126 1126 1126 LYS LYS A . n 
A 1 1127 ILE 1127 1127 1127 ILE ILE A . n 
A 1 1128 ASN 1128 1128 1128 ASN ASN A . n 
A 1 1129 SER 1129 1129 1129 SER SER A . n 
A 1 1130 GLU 1130 1130 1130 GLU GLU A . n 
A 1 1131 GLN 1131 1131 1131 GLN GLN A . n 
A 1 1132 ILE 1132 1132 1132 ILE ILE A . n 
A 1 1133 ASP 1133 1133 1133 ASP ASP A . n 
A 1 1134 VAL 1134 1134 1134 VAL VAL A . n 
A 1 1135 GLU 1135 1135 1135 GLU GLU A . n 
A 1 1136 ASN 1136 1136 1136 ASN ASN A . n 
A 1 1137 PHE 1137 1137 1137 PHE PHE A . n 
A 1 1138 VAL 1138 1138 1138 VAL VAL A . n 
A 1 1139 ASP 1139 1139 1139 ASP ASP A . n 
A 1 1140 ILE 1140 1140 1140 ILE ILE A . n 
A 1 1141 PRO 1141 1141 1141 PRO PRO A . n 
A 1 1142 GLU 1142 1142 1142 GLU GLU A . n 
A 1 1143 ASP 1143 1143 1143 ASP ASP A . n 
A 1 1144 THR 1144 1144 1144 THR THR A . n 
A 1 1145 LYS 1145 1145 1145 LYS LYS A . n 
A 1 1146 LYS 1146 1146 1146 LYS LYS A . n 
A 1 1147 LEU 1147 1147 1147 LEU LEU A . n 
A 1 1148 GLU 1148 1148 1148 GLU GLU A . n 
A 1 1149 ILE 1149 1149 1149 ILE ILE A . n 
A 1 1150 ASN 1150 1150 1150 ASN ASN A . n 
A 1 1151 VAL 1151 1151 1151 VAL VAL A . n 
A 1 1152 GLY 1152 1152 1152 GLY GLY A . n 
A 1 1153 GLY 1153 1153 1153 GLY GLY A . n 
A 1 1154 ILE 1154 1154 1154 ILE ILE A . n 
A 1 1155 GLY 1155 1155 1155 GLY GLY A . n 
A 1 1156 PHE 1156 1156 1156 PHE PHE A . n 
A 1 1157 GLY 1157 1157 1157 GLY GLY A . n 
A 1 1158 LEU 1158 1158 1158 LEU LEU A . n 
A 1 1159 LEU 1159 1159 1159 LEU LEU A . n 
A 1 1160 GLU 1160 1160 1160 GLU GLU A . n 
A 1 1161 VAL 1161 1161 1161 VAL VAL A . n 
A 1 1162 VAL 1162 1162 1162 VAL VAL A . n 
A 1 1163 TYR 1163 1163 1163 TYR TYR A . n 
A 1 1164 GLN 1164 1164 1164 GLN GLN A . n 
A 1 1165 PHE 1165 1165 1165 PHE PHE A . n 
A 1 1166 ASN 1166 1166 1166 ASN ASN A . n 
A 1 1167 LEU 1167 1167 1167 LEU LEU A . n 
A 1 1168 ASN 1168 1168 1168 ASN ASN A . n 
A 1 1169 LEU 1169 1169 1169 LEU LEU A . n 
A 1 1170 VAL 1170 1170 1170 VAL VAL A . n 
A 1 1171 ASN 1171 1171 1171 ASN ASN A . n 
A 1 1172 PHE 1172 1172 1172 PHE PHE A . n 
A 1 1173 GLU 1173 1173 1173 GLU GLU A . n 
A 1 1174 ASN 1174 1174 1174 ASN ASN A . n 
A 1 1175 ARG 1175 1175 1175 ARG ARG A . n 
A 1 1176 PHE 1176 1176 1176 PHE PHE A . n 
A 1 1177 GLN 1177 1177 1177 GLN GLN A . n 
A 1 1178 LEU 1178 1178 1178 LEU LEU A . n 
A 1 1179 ASP 1179 1179 1179 ASP ASP A . n 
A 1 1180 LEU 1180 1180 1180 LEU LEU A . n 
A 1 1181 GLU 1181 1181 1181 GLU GLU A . n 
A 1 1182 LYS 1182 1182 1182 LYS LYS A . n 
A 1 1183 GLN 1183 1183 1183 GLN GLN 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 GLY 1186 1186 1186 GLY GLY A . n 
A 1 1187 SER 1187 1187 1187 SER SER A . n 
A 1 1188 ASP 1188 1188 1188 ASP ASP A . n 
A 1 1189 TYR 1189 1189 1189 TYR TYR 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 ARG 1192 1192 1192 ARG ARG A . n 
A 1 1193 LEU 1193 1193 1193 LEU LEU A . n 
A 1 1194 LYS 1194 1194 1194 LYS LYS A . n 
A 1 1195 VAL 1195 1195 1195 VAL VAL A . n 
A 1 1196 CYS 1196 1196 1196 CYS CYS A . n 
A 1 1197 ALA 1197 1197 1197 ALA ALA A . n 
A 1 1198 SER 1198 1198 1198 SER SER A . n 
A 1 1199 TYR 1199 1199 1199 TYR TYR A . n 
A 1 1200 ILE 1200 1200 1200 ILE ILE A . n 
A 1 1201 PRO 1201 1201 1201 PRO PRO A . n 
A 1 1202 GLN 1202 1202 1202 GLN GLN A . n 
A 1 1203 LEU 1203 1203 1203 LEU LEU A . n 
A 1 1204 THR 1204 1204 1204 THR THR A . n 
A 1 1205 ASP 1205 1205 1205 ASP ASP A . n 
A 1 1206 ARG 1206 1206 1206 ARG ARG A . n 
A 1 1207 ARG 1207 1207 1207 ARG ARG A . n 
A 1 1208 SER 1208 1208 1208 SER SER A . n 
A 1 1209 ASN 1209 1209 1209 ASN ASN A . n 
A 1 1210 MET 1210 1210 1210 MET MET A . n 
A 1 1211 ALA 1211 1211 1211 ALA ALA A . n 
A 1 1212 LEU 1212 1212 1212 LEU LEU A . n 
A 1 1213 ILE 1213 1213 1213 ILE ILE A . n 
A 1 1214 GLU 1214 1214 1214 GLU GLU A . n 
A 1 1215 VAL 1215 1215 1215 VAL VAL A . n 
A 1 1216 THR 1216 1216 1216 THR THR A . n 
A 1 1217 LEU 1217 1217 1217 LEU LEU A . n 
A 1 1218 PRO 1218 1218 1218 PRO PRO A . n 
A 1 1219 SER 1219 1219 1219 SER SER A . n 
A 1 1220 GLY 1220 1220 1220 GLY GLY A . n 
A 1 1221 TYR 1221 1221 1221 TYR TYR A . n 
A 1 1222 VAL 1222 1222 1222 VAL VAL A . n 
A 1 1223 VAL 1223 1223 1223 VAL VAL A . n 
A 1 1224 ASP 1224 1224 1224 ASP ASP A . n 
A 1 1225 ARG 1225 1225 1225 ARG ARG 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 ILE 1228 1228 1228 ILE ILE A . n 
A 1 1229 SER 1229 1229 1229 SER SER A . n 
A 1 1230 GLU 1230 1230 1230 GLU GLU A . n 
A 1 1231 GLN 1231 1231 1231 GLN GLN A . n 
A 1 1232 THR 1232 1232 1232 THR THR A . n 
A 1 1233 LYS 1233 1233 1233 LYS LYS A . n 
A 1 1234 VAL 1234 1234 1234 VAL VAL A . n 
A 1 1235 ASN 1235 1235 1235 ASN ASN A . n 
A 1 1236 PRO 1236 1236 1236 PRO PRO A . n 
A 1 1237 ILE 1237 1237 1237 ILE ILE A . n 
A 1 1238 GLN 1238 1238 1238 GLN GLN A . n 
A 1 1239 LYS 1239 1239 1239 LYS LYS A . n 
A 1 1240 THR 1240 1240 1240 THR THR A . n 
A 1 1241 GLU 1241 1241 1241 GLU GLU A . n 
A 1 1242 ILE 1242 1242 1242 ILE ILE A . n 
A 1 1243 ARG 1243 1243 1243 ARG ARG A . n 
A 1 1244 TYR 1244 1244 1244 TYR TYR A . n 
A 1 1245 GLY 1245 1245 1245 GLY GLY A . n 
A 1 1246 GLY 1246 1246 1246 GLY GLY A . n 
A 1 1247 THR 1247 1247 1247 THR THR A . n 
A 1 1248 SER 1248 1248 1248 SER SER A . n 
A 1 1249 VAL 1249 1249 1249 VAL VAL A . n 
A 1 1250 VAL 1250 1250 1250 VAL VAL A . n 
A 1 1251 LEU 1251 1251 1251 LEU LEU A . n 
A 1 1252 TYR 1252 1252 1252 TYR TYR A . n 
A 1 1253 TYR 1253 1253 1253 TYR TYR A . n 
A 1 1254 ASP 1254 1254 1254 ASP ASP A . n 
A 1 1255 ASN 1255 1255 1255 ASN ASN A . n 
A 1 1256 MET 1256 1256 1256 MET MET A . n 
A 1 1257 GLY 1257 1257 1257 GLY GLY A . n 
A 1 1258 SER 1258 1258 1258 SER SER A . n 
A 1 1259 GLU 1259 1259 1259 GLU GLU A . n 
A 1 1260 ARG 1260 1260 1260 ARG ARG A . n 
A 1 1261 ASN 1261 1261 1261 ASN ASN A . n 
A 1 1262 CYS 1262 1262 1262 CYS CYS A . n 
A 1 1263 PHE 1263 1263 1263 PHE PHE A . n 
A 1 1264 THR 1264 1264 1264 THR THR A . n 
A 1 1265 LEU 1265 1265 1265 LEU LEU A . n 
A 1 1266 THR 1266 1266 1266 THR THR A . n 
A 1 1267 ALA 1267 1267 1267 ALA ALA A . n 
A 1 1268 TYR 1268 1268 1268 TYR TYR A . n 
A 1 1269 ARG 1269 1269 1269 ARG ARG A . n 
A 1 1270 ARG 1270 1270 1270 ARG ARG A . n 
A 1 1271 PHE 1271 1271 1271 PHE PHE A . n 
A 1 1272 LYS 1272 1272 1272 LYS LYS A . n 
A 1 1273 VAL 1273 1273 1273 VAL VAL A . n 
A 1 1274 ALA 1274 1274 1274 ALA ALA A . n 
A 1 1275 LEU 1275 1275 1275 LEU LEU A . n 
A 1 1276 LYS 1276 1276 1276 LYS LYS A . n 
A 1 1277 ARG 1277 1277 1277 ARG ARG A . n 
A 1 1278 PRO 1278 1278 1278 PRO PRO A . n 
A 1 1279 ALA 1279 1279 1279 ALA ALA A . n 
A 1 1280 TYR 1280 1280 1280 TYR TYR A . n 
A 1 1281 VAL 1281 1281 1281 VAL VAL A . n 
A 1 1282 VAL 1282 1282 1282 VAL VAL A . n 
A 1 1283 VAL 1283 1283 1283 VAL VAL A . n 
A 1 1284 TYR 1284 1284 1284 TYR TYR A . n 
A 1 1285 ASP 1285 1285 1285 ASP ASP A . n 
A 1 1286 TYR 1286 1286 1286 TYR TYR A . n 
A 1 1287 TYR 1287 1287 1287 TYR TYR A . n 
A 1 1288 ASN 1288 1288 1288 ASN ASN A . n 
A 1 1289 THR 1289 1289 1289 THR THR A . n 
A 1 1290 ASN 1290 1290 1290 ASN ASN A . n 
A 1 1291 LEU 1291 1291 1291 LEU LEU A . n 
A 1 1292 ASN 1292 1292 1292 ASN ASN A . n 
A 1 1293 ALA 1293 1293 1293 ALA ALA A . n 
A 1 1294 ILE 1294 1294 1294 ILE ILE A . n 
A 1 1295 LYS 1295 1295 1295 LYS LYS A . n 
A 1 1296 VAL 1296 1296 1296 VAL VAL A . n 
A 1 1297 TYR 1297 1297 1297 TYR TYR A . n 
A 1 1298 GLU 1298 1298 1298 GLU GLU A . n 
A 1 1299 VAL 1299 1299 1299 VAL VAL A . n 
A 1 1300 ASP 1300 1300 1300 ASP ASP A . n 
A 1 1301 LYS 1301 1301 1301 LYS LYS A . n 
A 1 1302 GLN 1302 1302 1302 GLN GLN A . n 
A 1 1303 ASN 1303 1303 1303 ASN ASN A . n 
A 1 1304 LEU 1304 1304 1304 LEU LEU A . n 
A 1 1305 CYS 1305 1305 1305 CYS CYS A . n 
A 1 1306 GLU 1306 1306 1306 GLU GLU A . n 
A 1 1307 ILE 1307 1307 1307 ILE ILE A . n 
A 1 1308 CYS 1308 1308 1308 CYS CYS 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 GLU 1311 1311 1311 GLU GLU A . n 
A 1 1312 ASP 1312 1312 1312 ASP ASP A . n 
A 1 1313 CYS 1313 1313 1313 CYS CYS A . n 
A 1 1314 PRO 1314 1314 1314 PRO PRO A . n 
A 1 1315 ALA 1315 1315 1315 ALA ALA A . n 
A 1 1316 GLU 1316 1316 1316 GLU GLU A . n 
A 1 1317 CYS 1317 1317 1317 CYS CYS A . n 
A 1 1318 GLY 1318 1318 1318 GLY GLY A . n 
A 1 1319 GLY 1319 1319 ?    ?   ?   A . n 
A 1 1320 HIS 1320 1320 ?    ?   ?   A . n 
A 1 1321 HIS 1321 1321 ?    ?   ?   A . n 
A 1 1322 HIS 1322 1322 ?    ?   ?   A . n 
A 1 1323 HIS 1323 1323 ?    ?   ?   A . n 
A 1 1324 HIS 1324 1324 ?    ?   ?   A . n 
A 1 1325 HIS 1325 1325 ?    ?   ?   A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 NAG 1   1326 1    NAG NAG A . 
C 2 NAG 1   1327 2    NAG NAG A . 
D 2 NAG 1   1328 3    NAG NAG A . 
E 2 NAG 1   1329 4    NAG NAG A . 
F 2 NAG 2   1330 5    NAG NAG A . 
G 3 NA  1   1331 1001 NA  NA  A . 
H 3 NA  1   1332 1002 NA  NA  A . 
I 3 NA  1   1333 1003 NA  NA  A . 
J 4 HOH 1   1334 1    HOH HOH A . 
J 4 HOH 2   1335 2    HOH HOH A . 
J 4 HOH 3   1336 3    HOH HOH A . 
J 4 HOH 4   1337 4    HOH HOH A . 
J 4 HOH 5   1338 5    HOH HOH A . 
J 4 HOH 6   1339 6    HOH HOH A . 
J 4 HOH 7   1340 7    HOH HOH A . 
J 4 HOH 8   1341 8    HOH HOH A . 
J 4 HOH 9   1342 9    HOH HOH A . 
J 4 HOH 10  1343 10   HOH HOH A . 
J 4 HOH 11  1344 11   HOH HOH A . 
J 4 HOH 12  1345 12   HOH HOH A . 
J 4 HOH 13  1346 13   HOH HOH A . 
J 4 HOH 14  1347 14   HOH HOH A . 
J 4 HOH 15  1348 15   HOH HOH A . 
J 4 HOH 16  1349 16   HOH HOH A . 
J 4 HOH 17  1350 17   HOH HOH A . 
J 4 HOH 18  1351 18   HOH HOH A . 
J 4 HOH 19  1352 19   HOH HOH A . 
J 4 HOH 20  1353 20   HOH HOH A . 
J 4 HOH 21  1354 21   HOH HOH A . 
J 4 HOH 22  1355 22   HOH HOH A . 
J 4 HOH 23  1356 23   HOH HOH A . 
J 4 HOH 24  1357 24   HOH HOH A . 
J 4 HOH 25  1358 25   HOH HOH A . 
J 4 HOH 26  1359 26   HOH HOH A . 
J 4 HOH 27  1360 27   HOH HOH A . 
J 4 HOH 28  1361 28   HOH HOH A . 
J 4 HOH 29  1362 29   HOH HOH A . 
J 4 HOH 30  1363 30   HOH HOH A . 
J 4 HOH 31  1364 31   HOH HOH A . 
J 4 HOH 32  1365 32   HOH HOH A . 
J 4 HOH 33  1366 33   HOH HOH A . 
J 4 HOH 34  1367 34   HOH HOH A . 
J 4 HOH 35  1368 35   HOH HOH A . 
J 4 HOH 36  1369 36   HOH HOH A . 
J 4 HOH 37  1370 37   HOH HOH A . 
J 4 HOH 38  1371 38   HOH HOH A . 
J 4 HOH 39  1372 39   HOH HOH A . 
J 4 HOH 40  1373 40   HOH HOH A . 
J 4 HOH 41  1374 41   HOH HOH A . 
J 4 HOH 42  1375 42   HOH HOH A . 
J 4 HOH 43  1376 43   HOH HOH A . 
J 4 HOH 44  1377 44   HOH HOH A . 
J 4 HOH 45  1378 45   HOH HOH A . 
J 4 HOH 46  1379 46   HOH HOH A . 
J 4 HOH 47  1380 47   HOH HOH A . 
J 4 HOH 48  1381 48   HOH HOH A . 
J 4 HOH 49  1382 49   HOH HOH A . 
J 4 HOH 50  1383 50   HOH HOH A . 
J 4 HOH 51  1384 51   HOH HOH A . 
J 4 HOH 52  1385 52   HOH HOH A . 
J 4 HOH 53  1386 53   HOH HOH A . 
J 4 HOH 54  1387 54   HOH HOH A . 
J 4 HOH 55  1388 55   HOH HOH A . 
J 4 HOH 56  1389 56   HOH HOH A . 
J 4 HOH 57  1390 57   HOH HOH A . 
J 4 HOH 58  1391 58   HOH HOH A . 
J 4 HOH 59  1392 59   HOH HOH A . 
J 4 HOH 60  1393 60   HOH HOH A . 
J 4 HOH 61  1394 61   HOH HOH A . 
J 4 HOH 62  1395 62   HOH HOH A . 
J 4 HOH 63  1396 63   HOH HOH A . 
J 4 HOH 64  1397 64   HOH HOH A . 
J 4 HOH 65  1398 65   HOH HOH A . 
J 4 HOH 66  1399 66   HOH HOH A . 
J 4 HOH 67  1400 67   HOH HOH A . 
J 4 HOH 68  1401 68   HOH HOH A . 
J 4 HOH 69  1402 69   HOH HOH A . 
J 4 HOH 70  1403 70   HOH HOH A . 
J 4 HOH 71  1404 71   HOH HOH A . 
J 4 HOH 72  1405 72   HOH HOH A . 
J 4 HOH 73  1406 73   HOH HOH A . 
J 4 HOH 74  1407 74   HOH HOH A . 
J 4 HOH 75  1408 75   HOH HOH A . 
J 4 HOH 76  1409 76   HOH HOH A . 
J 4 HOH 77  1410 77   HOH HOH A . 
J 4 HOH 78  1411 78   HOH HOH A . 
J 4 HOH 79  1412 79   HOH HOH A . 
J 4 HOH 80  1413 80   HOH HOH A . 
J 4 HOH 81  1414 81   HOH HOH A . 
J 4 HOH 82  1415 82   HOH HOH A . 
J 4 HOH 83  1416 83   HOH HOH A . 
J 4 HOH 84  1417 84   HOH HOH A . 
J 4 HOH 85  1418 85   HOH HOH A . 
J 4 HOH 86  1419 86   HOH HOH A . 
J 4 HOH 87  1420 87   HOH HOH A . 
J 4 HOH 88  1421 88   HOH HOH A . 
J 4 HOH 89  1422 89   HOH HOH A . 
J 4 HOH 90  1423 90   HOH HOH A . 
J 4 HOH 91  1424 91   HOH HOH A . 
J 4 HOH 92  1425 92   HOH HOH A . 
J 4 HOH 93  1426 93   HOH HOH A . 
J 4 HOH 94  1427 94   HOH HOH A . 
J 4 HOH 95  1428 95   HOH HOH A . 
J 4 HOH 96  1429 96   HOH HOH A . 
J 4 HOH 97  1430 97   HOH HOH A . 
J 4 HOH 98  1431 98   HOH HOH A . 
J 4 HOH 99  1432 99   HOH HOH A . 
J 4 HOH 100 1433 100  HOH HOH A . 
J 4 HOH 101 1434 101  HOH HOH A . 
J 4 HOH 102 1435 102  HOH HOH A . 
J 4 HOH 103 1436 103  HOH HOH A . 
J 4 HOH 104 1437 104  HOH HOH A . 
J 4 HOH 105 1438 105  HOH HOH A . 
J 4 HOH 106 1439 106  HOH HOH A . 
J 4 HOH 107 1440 107  HOH HOH A . 
J 4 HOH 108 1441 108  HOH HOH A . 
J 4 HOH 109 1442 109  HOH HOH A . 
J 4 HOH 110 1443 110  HOH HOH A . 
J 4 HOH 111 1444 111  HOH HOH A . 
J 4 HOH 112 1445 112  HOH HOH A . 
J 4 HOH 113 1446 113  HOH HOH A . 
J 4 HOH 114 1447 114  HOH HOH A . 
J 4 HOH 115 1448 115  HOH HOH A . 
J 4 HOH 116 1449 116  HOH HOH A . 
J 4 HOH 117 1450 117  HOH HOH A . 
J 4 HOH 118 1451 118  HOH HOH A . 
J 4 HOH 119 1452 119  HOH HOH A . 
J 4 HOH 120 1453 120  HOH HOH A . 
J 4 HOH 121 1454 121  HOH HOH A . 
J 4 HOH 122 1455 122  HOH HOH A . 
J 4 HOH 123 1456 123  HOH HOH A . 
J 4 HOH 124 1457 124  HOH HOH A . 
J 4 HOH 125 1458 125  HOH HOH A . 
J 4 HOH 126 1459 126  HOH HOH A . 
J 4 HOH 127 1460 127  HOH HOH A . 
J 4 HOH 128 1461 128  HOH HOH A . 
J 4 HOH 129 1462 129  HOH HOH A . 
J 4 HOH 130 1463 130  HOH HOH A . 
J 4 HOH 131 1464 131  HOH HOH A . 
J 4 HOH 132 1465 132  HOH HOH A . 
J 4 HOH 133 1466 133  HOH HOH A . 
J 4 HOH 134 1467 134  HOH HOH A . 
J 4 HOH 135 1468 135  HOH HOH A . 
J 4 HOH 136 1469 136  HOH HOH A . 
J 4 HOH 137 1470 137  HOH HOH A . 
J 4 HOH 138 1471 138  HOH HOH A . 
J 4 HOH 139 1472 139  HOH HOH A . 
J 4 HOH 140 1473 140  HOH HOH A . 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A ASN 178 A ASN 178 ? ASN 'GLYCOSYLATION SITE' 
2 A ASN 221 A ASN 221 ? ASN 'GLYCOSYLATION SITE' 
3 A ASN 291 A ASN 291 ? ASN 'GLYCOSYLATION SITE' 
4 A ASN 616 A ASN 616 ? ASN 'GLYCOSYLATION SITE' 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_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,F,G,H,I,J 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2007-07-24 
2 'Structure model' 1 1 2008-05-01 
3 'Structure model' 1 2 2011-07-13 
4 'Structure model' 1 3 2017-10-18 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' Advisory                    
3 3 'Structure model' 'Version format compliance' 
4 4 'Structure model' 'Refinement description'    
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    4 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            software 
# 
loop_
_diffrn_reflns.diffrn_id 
_diffrn_reflns.pdbx_d_res_high 
_diffrn_reflns.pdbx_d_res_low 
_diffrn_reflns.pdbx_number_obs 
_diffrn_reflns.pdbx_Rmerge_I_obs 
_diffrn_reflns.pdbx_Rsym_value 
_diffrn_reflns.pdbx_chi_squared 
_diffrn_reflns.av_sigmaI_over_netI 
_diffrn_reflns.pdbx_redundancy 
_diffrn_reflns.pdbx_percent_possible_obs 
_diffrn_reflns.number 
_diffrn_reflns.pdbx_observed_criterion 
_diffrn_reflns.limit_h_max 
_diffrn_reflns.limit_h_min 
_diffrn_reflns.limit_k_max 
_diffrn_reflns.limit_k_min 
_diffrn_reflns.limit_l_max 
_diffrn_reflns.limit_l_min 
1 3.650 50.000 29799 0.171 ? 1.15 4.80 8.40 99.80  251521 ? ? ? ? ? ? ? 
2 4.000 50.000 22511 0.143 ? 1.16 5.50 8.00 98.20  180036 ? ? ? ? ? ? ? 
3 4.000 50.000 22718 0.110 ? 1.11 6.60 7.90 100.00 178917 ? ? ? ? ? ? ? 
4 3.600 50.000 31388 0.130 ? 1.27 7.20 5.80 98.70  182332 ? ? ? ? ? ? ? 
# 
loop_
_pdbx_diffrn_reflns_shell.diffrn_id 
_pdbx_diffrn_reflns_shell.d_res_high 
_pdbx_diffrn_reflns_shell.d_res_low 
_pdbx_diffrn_reflns_shell.number_obs 
_pdbx_diffrn_reflns_shell.rejects 
_pdbx_diffrn_reflns_shell.Rmerge_I_obs 
_pdbx_diffrn_reflns_shell.Rsym_value 
_pdbx_diffrn_reflns_shell.chi_squared 
_pdbx_diffrn_reflns_shell.redundancy 
_pdbx_diffrn_reflns_shell.percent_possible_obs 
1 9.88  50.00 ? ? 0.039 ? 1.312 8.00 98.90  
1 7.85  9.88  ? ? 0.048 ? 1.067 8.70 99.60  
1 6.86  7.85  ? ? 0.094 ? 1.127 8.80 99.70  
1 6.24  6.86  ? ? 0.146 ? 1.163 8.90 99.90  
1 5.79  6.24  ? ? 0.176 ? 1.150 8.80 100.00 
1 5.45  5.79  ? ? 0.182 ? 1.234 8.50 100.00 
1 5.18  5.45  ? ? 0.178 ? 1.173 8.50 100.00 
1 4.95  5.18  ? ? 0.177 ? 1.153 8.60 100.00 
1 4.76  4.95  ? ? 0.183 ? 1.152 8.80 100.00 
1 4.60  4.76  ? ? 0.217 ? 1.154 8.80 99.90  
1 4.45  4.60  ? ? 0.235 ? 1.137 8.80 100.00 
1 4.33  4.45  ? ? 0.285 ? 1.198 8.90 100.00 
1 4.21  4.33  ? ? 0.325 ? 1.146 8.90 100.00 
1 4.11  4.21  ? ? 0.402 ? 1.121 8.90 100.00 
1 4.02  4.11  ? ? 0.471 ? 1.083 8.80 100.00 
1 3.93  4.02  ? ? 0.593 ? 1.107 8.60 100.00 
1 3.85  3.93  ? ? 0.659 ? 1.132 8.30 100.00 
1 3.78  3.85  ? ? 0.705 ? 1.087 7.90 99.90  
1 3.71  3.78  ? ? 0.737 ? 1.100 7.10 99.50  
1 3.65  3.71  ? ? 0.709 ? 1.111 6.20 98.10  
2 10.82 50.00 ? ? 0.047 ? 2.140 7.40 95.50  
2 8.60  10.82 ? ? 0.042 ? 1.167 8.00 96.90  
2 7.52  8.60  ? ? 0.064 ? 1.102 8.10 97.50  
2 6.84  7.52  ? ? 0.102 ? 1.027 8.20 97.50  
2 6.35  6.84  ? ? 0.141 ? 1.061 8.20 98.10  
2 5.97  6.35  ? ? 0.174 ? 1.104 8.10 97.80  
2 5.67  5.97  ? ? 0.191 ? 1.170 7.80 97.90  
2 5.43  5.67  ? ? 0.185 ? 1.154 7.60 98.50  
2 5.22  5.43  ? ? 0.185 ? 1.071 7.80 98.10  
2 5.04  5.22  ? ? 0.185 ? 1.120 7.90 98.50  
2 4.88  5.04  ? ? 0.184 ? 1.108 8.00 98.60  
2 4.74  4.88  ? ? 0.203 ? 1.108 8.00 98.80  
2 4.62  4.74  ? ? 0.243 ? 1.134 8.10 98.30  
2 4.50  4.62  ? ? 0.237 ? 1.171 8.10 98.70  
2 4.40  4.50  ? ? 0.300 ? 1.109 8.10 98.90  
2 4.31  4.40  ? ? 0.315 ? 1.107 8.10 98.90  
2 4.22  4.31  ? ? 0.362 ? 1.062 8.20 98.90  
2 4.14  4.22  ? ? 0.427 ? 1.061 8.10 98.90  
2 4.07  4.14  ? ? 0.476 ? 1.109 8.10 98.90  
2 4.00  4.07  ? ? 0.578 ? 1.093 8.10 98.90  
3 10.82 50.00 ? ? 0.036 ? 2.021 7.10 99.80  
3 8.60  10.82 ? ? 0.034 ? 1.290 7.70 100.00 
3 7.52  8.60  ? ? 0.051 ? 1.116 7.60 100.00 
3 6.84  7.52  ? ? 0.077 ? 1.016 7.40 100.00 
3 6.35  6.84  ? ? 0.106 ? 1.007 7.70 100.00 
3 5.97  6.35  ? ? 0.135 ? 1.068 7.80 100.00 
3 5.67  5.97  ? ? 0.152 ? 1.164 7.90 100.00 
3 5.43  5.67  ? ? 0.160 ? 1.064 7.90 100.00 
3 5.22  5.43  ? ? 0.172 ? 1.077 7.90 100.00 
3 5.04  5.22  ? ? 0.161 ? 1.045 8.00 100.00 
3 4.88  5.04  ? ? 0.172 ? 0.994 8.00 100.00 
3 4.74  4.88  ? ? 0.193 ? 0.980 8.00 100.00 
3 4.62  4.74  ? ? 0.225 ? 0.967 8.00 100.00 
3 4.50  4.62  ? ? 0.235 ? 0.978 8.10 100.00 
3 4.40  4.50  ? ? 0.278 ? 0.995 8.10 100.00 
3 4.31  4.40  ? ? 0.306 ? 0.940 8.10 100.00 
3 4.22  4.31  ? ? 0.358 ? 0.992 8.10 100.00 
3 4.14  4.22  ? ? 0.455 ? 1.055 8.10 100.00 
3 4.07  4.14  ? ? 0.523 ? 1.303 8.10 100.00 
3 4.00  4.07  ? ? 0.636 ? 1.036 8.10 100.00 
4 9.75  50.00 ? ? 0.043 ? 2.066 5.70 94.90  
4 7.75  9.75  ? ? 0.051 ? 1.558 5.80 97.20  
4 6.77  7.75  ? ? 0.082 ? 1.380 5.80 97.80  
4 6.15  6.77  ? ? 0.108 ? 1.324 5.90 98.00  
4 5.71  6.15  ? ? 0.122 ? 1.361 6.00 98.30  
4 5.38  5.71  ? ? 0.116 ? 1.315 6.00 98.50  
4 5.11  5.38  ? ? 0.108 ? 1.268 6.00 98.90  
4 4.89  5.11  ? ? 0.108 ? 1.306 6.00 98.70  
4 4.70  4.89  ? ? 0.118 ? 1.270 6.00 98.80  
4 4.54  4.70  ? ? 0.122 ? 1.260 6.00 98.90  
4 4.39  4.54  ? ? 0.143 ? 1.192 6.00 99.10  
4 4.27  4.39  ? ? 0.163 ? 1.193 6.00 99.10  
4 4.16  4.27  ? ? 0.184 ? 1.193 6.00 99.30  
4 4.05  4.16  ? ? 0.220 ? 1.163 6.00 99.20  
4 3.96  4.05  ? ? 0.259 ? 1.113 6.00 99.40  
4 3.88  3.96  ? ? 0.298 ? 1.110 5.90 99.40  
4 3.80  3.88  ? ? 0.292 ? 1.081 5.70 99.40  
4 3.73  3.80  ? ? 0.326 ? 0.987 5.40 99.60  
4 3.66  3.73  ? ? 0.339 ? 1.017 5.10 99.70  
4 3.60  3.66  ? ? 0.345 ? 1.000 4.80 99.60  
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.pdbx_refine_id 
1 ? refined 67.0820  73.8720 143.3500 -0.0004 0.0125  -0.1400 -0.2217 0.0454  0.0201  3.9999 0.9613 1.9637 -1.0420 -1.4872 0.1329 
-0.0223 0.1041 -0.0818 0.3909  -0.3580 0.0826  -0.1145 0.3056  -0.2903 'X-RAY DIFFRACTION' 
2 ? refined 102.6440 96.2220 135.6540 -0.0642 0.0029  -0.1005 -0.0632 -0.0031 -0.0282 0.4548 0.6881 0.5730 -0.1233 -0.2821 0.0084 
0.1249  0.0798 -0.2047 -0.1089 0.0017  -0.0895 0.0423  -0.0410 0.0788  'X-RAY DIFFRACTION' 
3 ? refined 114.7140 55.5510 111.6350 0.0760  -0.0938 -0.1951 0.0331  0.0065  -0.0197 2.5109 2.2876 2.9166 -0.9429 0.0853  0.7697 
-0.1177 0.1599 -0.0422 -0.3180 -0.0305 -0.0885 0.3622  0.3416  0.2030  'X-RAY DIFFRACTION' 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.selection_details 
1 1 A 1    A 200  ALL A 1    A 200  'X-RAY DIFFRACTION' ? 
2 1 A 400  A 660  ALL A 400  A 660  'X-RAY DIFFRACTION' ? 
3 2 A 201  A 399  ALL A 201  A 399  'X-RAY DIFFRACTION' ? 
4 2 A 661  A 771  ALL A 661  A 771  'X-RAY DIFFRACTION' ? 
5 2 A 1164 A 1318 ALL A 1164 A 1318 'X-RAY DIFFRACTION' ? 
6 3 A 772  A 1163 ALL A 772  A 1163 'X-RAY DIFFRACTION' ? 
# 
_pdbx_phasing_dm.entry_id          2PN5 
_pdbx_phasing_dm.fom_acentric      0.570 
_pdbx_phasing_dm.fom_centric       0.610 
_pdbx_phasing_dm.fom               0.580 
_pdbx_phasing_dm.reflns_acentric   64521 
_pdbx_phasing_dm.reflns_centric    7337 
_pdbx_phasing_dm.reflns            71858 
# 
loop_
_pdbx_phasing_dm_shell.d_res_high 
_pdbx_phasing_dm_shell.d_res_low 
_pdbx_phasing_dm_shell.delta_phi_final 
_pdbx_phasing_dm_shell.delta_phi_initial 
_pdbx_phasing_dm_shell.fom_acentric 
_pdbx_phasing_dm_shell.fom_centric 
_pdbx_phasing_dm_shell.fom 
_pdbx_phasing_dm_shell.reflns_acentric 
_pdbx_phasing_dm_shell.reflns_centric 
_pdbx_phasing_dm_shell.reflns 
7.700 45.866 ? ? 0.940 0.910 0.940 2493  853  3346  
4.800 7.700  ? ? 0.870 0.840 0.870 8356  1402 9758  
3.900 4.800  ? ? 0.840 0.780 0.830 10772 1299 12071 
3.400 3.900  ? ? 0.710 0.620 0.700 10965 1111 12076 
2.900 3.400  ? ? 0.430 0.390 0.420 19691 1718 21409 
2.700 2.900  ? ? 0.160 0.160 0.160 12244 954  13198 
# 
_phasing.method   MIRAS 
# 
_phasing_MIR.entry_id          2PN5 
_phasing_MIR.d_res_high        4.00 
_phasing_MIR.d_res_low         125.99 
_phasing_MIR.reflns            22771 
_phasing_MIR.FOM               0.383 
_phasing_MIR.reflns_centric    3337 
_phasing_MIR.FOM_centric       0.518 
_phasing_MIR.reflns_acentric   19434 
_phasing_MIR.FOM_acentric      0.360 
# 
loop_
_phasing_MIR_der.id 
_phasing_MIR_der.d_res_high 
_phasing_MIR_der.d_res_low 
_phasing_MIR_der.reflns_acentric 
_phasing_MIR_der.pdbx_loc_acentric 
_phasing_MIR_der.power_acentric 
_phasing_MIR_der.R_cullis_acentric 
_phasing_MIR_der.reflns_centric 
_phasing_MIR_der.pdbx_loc_centric 
_phasing_MIR_der.power_centric 
_phasing_MIR_der.R_cullis_centric 
_phasing_MIR_der.der_set_id 
_phasing_MIR_der.native_set_id 
1 4.00 126.00 19302 122.600 0.780 0.900 3071 188.000 0.540 0.860 1 . 
2 4.00 126.00 19194 191.500 0.670 0.910 3324 301.800 0.440 0.890 1 . 
3 4.00 126.00 19342 253.600 0.400 0.980 3086 357.900 0.260 0.970 1 . 
# 
loop_
_phasing_MIR_der_shell.d_res_high 
_phasing_MIR_der_shell.d_res_low 
_phasing_MIR_der_shell.pdbx_reflns_acentric 
_phasing_MIR_der_shell.pdbx_loc_acentric 
_phasing_MIR_der_shell.pdbx_power_acentric 
_phasing_MIR_der_shell.pdbx_R_cullis_acentric 
_phasing_MIR_der_shell.pdbx_reflns_centric 
_phasing_MIR_der_shell.pdbx_loc_centric 
_phasing_MIR_der_shell.pdbx_power_centric 
_phasing_MIR_der_shell.pdbx_R_cullis_centric 
_phasing_MIR_der_shell.der_id 
26.18 125.99 39   513.600  0.330 0.910 49  661.500  0.270 0.880 1 
14.61 26.18  274  251.300  0.790 0.790 151 303.200  0.590 0.780 1 
10.13 14.61  723  178.200  0.990 0.800 240 254.600  0.620 0.740 1 
7.75  10.13  1409 141.600  1.080 0.810 342 204.300  0.650 0.770 1 
6.28  7.75   2296 98.900   1.300 0.810 421 147.200  0.850 0.810 1 
5.28  6.28   3433 104.000  1.020 0.870 532 152.400  0.610 0.920 1 
4.55  5.28   4784 125.500  0.650 0.950 618 168.900  0.460 0.930 1 
4.00  4.55   6344 120.700  0.510 0.970 718 168.000  0.330 0.970 1 
26.18 125.99 38   1364.100 0.160 0.930 50  1500.000 0.130 0.920 2 
14.61 26.18  274  455.500  0.530 0.850 169 532.800  0.430 0.820 2 
10.13 14.61  729  309.500  0.700 0.860 265 418.600  0.450 0.860 2 
7.75  10.13  1418 231.400  0.840 0.850 375 327.800  0.520 0.830 2 
6.28  7.75   2311 165.500  1.010 0.850 459 230.600  0.710 0.840 2 
5.28  6.28   3450 159.300  0.870 0.890 579 225.900  0.560 0.910 2 
4.55  5.28   4782 190.300  0.590 0.950 669 272.400  0.380 0.940 2 
4.00  4.55   6192 178.200  0.490 0.960 758 244.500  0.320 0.950 2 
26.18 125.99 39   1275.300 0.100 0.990 46  1392.800 0.090 0.980 3 
14.61 26.18  273  329.900  0.370 0.990 148 401.400  0.270 0.980 3 
10.13 14.61  720  330.900  0.360 0.980 238 411.100  0.280 0.990 3 
7.75  10.13  1408 331.000  0.350 0.980 340 417.300  0.240 0.960 3 
6.28  7.75   2299 221.800  0.490 0.970 420 309.800  0.320 0.940 3 
5.28  6.28   3436 222.000  0.470 0.980 544 292.000  0.320 0.980 3 
4.55  5.28   4789 264.200  0.370 0.980 626 358.000  0.240 0.970 3 
4.00  4.55   6378 238.700  0.380 0.980 724 315.400  0.260 0.980 3 
# 
loop_
_phasing_MIR_der_site.id 
_phasing_MIR_der_site.atom_type_symbol 
_phasing_MIR_der_site.fract_x 
_phasing_MIR_der_site.fract_y 
_phasing_MIR_der_site.fract_z 
_phasing_MIR_der_site.B_iso 
_phasing_MIR_der_site.occupancy 
_phasing_MIR_der_site.der_id 
_phasing_MIR_der_site.details 
1  HG 0.166 0.728 0.011 79.732 0.687 1 ? 
2  HG 0.065 0.188 0.028 76.144 0.622 1 ? 
3  HG 0.192 0.107 0.072 92.050 0.606 1 ? 
4  HG 0.166 0.729 0.015 66.936 0.862 2 ? 
5  HG 0.065 0.187 0.026 77.731 0.928 2 ? 
6  HG 0.193 0.106 0.072 69.305 0.703 2 ? 
7  HG 0.289 0.447 0.045 81.421 0.530 2 ? 
8  HG 0.428 0.468 0.120 40.236 0.238 2 ? 
9  XE 0.167 0.055 0.109 17.647 0.783 3 ? 
10 XE 0.115 0.625 0.021 6.899  0.479 3 ? 
# 
loop_
_phasing_MIR_shell.d_res_high 
_phasing_MIR_shell.d_res_low 
_phasing_MIR_shell.reflns 
_phasing_MIR_shell.FOM 
_phasing_MIR_shell.reflns_centric 
_phasing_MIR_shell.FOM_centric 
_phasing_MIR_shell.reflns_acentric 
_phasing_MIR_shell.FOM_acentric 
26.18 125.99 90   0.574 51  0.596 39   0.546 
14.61 26.18  443  0.581 169 0.584 274  0.578 
10.13 14.61  994  0.608 265 0.597 729  0.612 
7.75  10.13  1793 0.595 375 0.612 1418 0.591 
6.28  7.75   2774 0.544 459 0.653 2315 0.522 
5.28  6.28   4036 0.433 579 0.554 3457 0.412 
4.55  5.28   5478 0.317 669 0.460 4809 0.297 
4.00  4.55   7163 0.245 770 0.368 6393 0.230 
# 
_phasing_set.id                1 
_phasing_set.pdbx_d_res_high   2.698 
_phasing_set.pdbx_d_res_low    45.866 
# 
loop_
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
_software.pdbx_ordinal 
DENZO       .     ?                package 'Zbyszek Otwinowski'       zbyszek@mix.swmed.edu                   'data reduction'  
http://www.lnls.br/infra/linhasluz/denzo-hkl.htm ?          ? 1 
SCALEPACK   .     ?                package 'Zbyszek Otwinowski'       zbyszek@mix.swmed.edu                   'data scaling'    
http://www.lnls.br/infra/linhasluz/denzo-hkl.htm ?          ? 2 
MLPHARE     .     ?                other   'Z.Otwinowski or E.Dodson' 'ccp4@dl.ac.uk, ccp4@yorvic.york.ac.uk' phasing           
http://www.ccp4.ac.uk/main.html                  Fortran_77 ? 3 
RESOLVE     2.09  25-Apr-2005      package 'Terwilliger, T. C'        terwilliger@LANL.gov                    phasing           
http://www.solve.lanl.gov/                       ?          ? 4 
REFMAC      .     ?                program 'Murshudov, G.N.'          ccp4@dl.ac.uk                           refinement        
http://www.ccp4.ac.uk/main.html                  Fortran_77 ? 5 
PDB_EXTRACT 2.000 'April. 3, 2006' package PDB                        sw-help@rcsb.rutgers.edu                'data extraction' 
http://pdb.rutgers.edu/software/                 C++        ? 6 
HKL-2000    .     ?                ?       ?                          ?                                       'data collection' ? 
?          ? 7 
HKL-2000    .     ?                ?       ?                          ?                                       'data reduction'  ? 
?          ? 8 
HKL-2000    .     ?                ?       ?                          ?                                       'data scaling'    ? 
?          ? 9 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   NH1 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   ARG 
_pdbx_validate_close_contact.auth_seq_id_1    1175 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   ILE 
_pdbx_validate_close_contact.auth_seq_id_2    1200 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.17 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            C 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            GLY 
_pdbx_validate_rmsd_bond.auth_seq_id_1             1318 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            O 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            GLY 
_pdbx_validate_rmsd_bond.auth_seq_id_2             1318 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.439 
_pdbx_validate_rmsd_bond.bond_target_value         1.232 
_pdbx_validate_rmsd_bond.bond_deviation            0.207 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.016 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             GLY 
_pdbx_validate_rmsd_angle.auth_seq_id_1              1318 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             C 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             GLY 
_pdbx_validate_rmsd_angle.auth_seq_id_2              1318 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             O 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             GLY 
_pdbx_validate_rmsd_angle.auth_seq_id_3              1318 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                107.97 
_pdbx_validate_rmsd_angle.angle_target_value         120.60 
_pdbx_validate_rmsd_angle.angle_deviation            -12.63 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.80 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
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 GLN A 25   ? ? -68.94  -72.47  
2  1 ASN A 47   ? ? -151.61 65.04   
3  1 ARG A 83   ? ? 72.18   -150.07 
4  1 PHE A 85   ? ? -161.74 101.99  
5  1 PHE A 87   ? ? -167.19 117.51  
6  1 PRO A 144  ? ? -49.97  -14.30  
7  1 VAL A 199  ? ? -62.58  5.45    
8  1 LEU A 200  ? ? -62.46  77.06   
9  1 ASP A 268  ? ? -85.47  -105.76 
10 1 ALA A 274  ? ? -110.26 -166.55 
11 1 PRO A 320  ? ? -32.91  -33.18  
12 1 ARG A 414  ? ? -27.13  -77.56  
13 1 ASN A 415  ? ? -117.29 53.57   
14 1 ARG A 479  ? ? -152.62 20.27   
15 1 ASP A 552  ? ? -102.65 -96.54  
16 1 ASN A 560  ? ? 65.13   -125.24 
17 1 LYS A 655  ? ? -48.43  -72.64  
18 1 MET A 756  ? ? -113.95 73.41   
19 1 LEU A 775  ? ? -55.74  102.45  
20 1 ASP A 800  ? ? -63.83  2.75    
21 1 ASN A 802  ? ? -159.12 26.19   
22 1 LYS A 804  ? ? -123.43 -134.19 
23 1 SER A 809  ? ? -173.64 103.53  
24 1 THR A 836  ? ? -140.95 46.54   
25 1 PHE A 846  ? ? -134.00 -66.37  
26 1 ASP A 1111 ? ? -152.81 85.44   
27 1 LYS A 1119 ? ? 43.11   -87.25  
28 1 ASP A 1133 ? ? -172.06 -57.90  
29 1 PHE A 1137 ? ? -140.64 45.08   
30 1 GLU A 1142 ? ? -79.18  -162.03 
31 1 GLN A 1164 ? ? -117.81 75.46   
32 1 LEU A 1203 ? ? 49.16   -133.37 
33 1 ASN A 1209 ? ? -73.57  -167.89 
34 1 ASN A 1255 ? ? 179.96  169.97  
# 
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 GLY 37   ? A GLY 37   
2  1 Y 1 A GLU 38   ? A GLU 38   
3  1 Y 1 A THR 39   ? A THR 39   
4  1 Y 1 A ASP 40   ? A ASP 40   
5  1 Y 1 A ASN 41   ? A ASN 41   
6  1 Y 1 A GLY 42   ? A GLY 42   
7  1 Y 1 A ALA 556  ? A ALA 556  
8  1 Y 1 A ILE 557  ? A ILE 557  
9  1 Y 1 A ASN 558  ? A ASN 558  
10 1 Y 1 A ALA 583  ? A ALA 583  
11 1 Y 1 A ASN 584  ? A ASN 584  
12 1 Y 1 A GLU 585  ? A GLU 585  
13 1 Y 1 A LYS 586  ? A LYS 586  
14 1 Y 1 A THR 587  ? A THR 587  
15 1 Y 1 A GLY 588  ? A GLY 588  
16 1 Y 1 A ARG 589  ? A ARG 589  
17 1 Y 1 A ASN 590  ? A ASN 590  
18 1 Y 1 A ALA 591  ? A ALA 591  
19 1 Y 1 A LEU 592  ? A LEU 592  
20 1 Y 1 A GLN 593  ? A GLN 593  
21 1 Y 1 A SER 594  ? A SER 594  
22 1 Y 1 A GLY 595  ? A GLY 595  
23 1 Y 1 A LYS 596  ? A LYS 596  
24 1 Y 1 A PRO 597  ? A PRO 597  
25 1 Y 1 A ILE 598  ? A ILE 598  
26 1 Y 1 A GLY 599  ? A GLY 599  
27 1 Y 1 A LYS 600  ? A LYS 600  
28 1 Y 1 A LEU 601  ? A LEU 601  
29 1 Y 1 A VAL 602  ? A VAL 602  
30 1 Y 1 A SER 603  ? A SER 603  
31 1 Y 1 A TYR 604  ? A TYR 604  
32 1 Y 1 A ARG 605  ? A ARG 605  
33 1 Y 1 A THR 606  ? A THR 606  
34 1 Y 1 A ASN 607  ? A ASN 607  
35 1 Y 1 A PHE 608  ? A PHE 608  
36 1 Y 1 A GLY 1319 ? A GLY 1319 
37 1 Y 1 A HIS 1320 ? A HIS 1320 
38 1 Y 1 A HIS 1321 ? A HIS 1321 
39 1 Y 1 A HIS 1322 ? A HIS 1322 
40 1 Y 1 A HIS 1323 ? A HIS 1323 
41 1 Y 1 A HIS 1324 ? A HIS 1324 
42 1 Y 1 A HIS 1325 ? A HIS 1325 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 N-ACETYL-D-GLUCOSAMINE NAG 
3 'SODIUM ION'           NA  
4 water                  HOH 
# 
