data_1QX1
# 
_entry.id   1QX1 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.279 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   1QX1         
RCSB  RCSB020171   
WWPDB D_1000020171 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 1QWN . unspecified 
PDB 1QWU . unspecified 
PDB 1PS3 . unspecified 
PDB 1HTY . unspecified 
PDB 1HWW . unspecified 
PDB 1HXK . unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        1QX1 
_pdbx_database_status.recvd_initial_deposition_date   2003-09-04 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Numao, S.'     1 
'Kuntz, D.A.'   2 
'Withers, S.G.' 3 
'Rose, D.R.'    4 
# 
_citation.id                        primary 
_citation.title                     
;Insights into the mechanism of Drosophila melanogaster Golgi alpha-mannosidase II through the structural analysis of covalent reaction intermediates.
;
_citation.journal_abbrev            J.Biol.Chem. 
_citation.journal_volume            278 
_citation.page_first                48074 
_citation.page_last                 48083 
_citation.year                      2003 
_citation.journal_id_ASTM           JBCHA3 
_citation.country                   US 
_citation.journal_id_ISSN           0021-9258 
_citation.journal_id_CSD            0071 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   12960159 
_citation.pdbx_database_id_DOI      10.1074/jbc.M309249200 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Numao, S.'     1 
primary 'Kuntz, D.A.'   2 
primary 'Withers, S.G.' 3 
primary 'Rose, D.R.'    4 
# 
_cell.entry_id           1QX1 
_cell.length_a           69.046 
_cell.length_b           109.826 
_cell.length_c           138.907 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         1QX1 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Alpha-mannosidase II'                   119700.633 1    3.2.1.114 D341N 
'Family 38 catalytic domain (residues 94-1108)' ? 
2 non-polymer man N-ACETYL-D-GLUCOSAMINE                   221.208    1    ?         ?     ? ? 
3 non-polymer syn 'ZINC ION'                               65.409     1    ?         ?     ? ? 
4 non-polymer syn '2-DEOXY-2-FLUOROHEXOPYRANOSYL FLUORIDE' 184.138    1    ?         ?     ? ? 
5 non-polymer syn '(4S)-2-METHYL-2,4-PENTANEDIOL'          118.174    1    ?         ?     ? ? 
6 water       nat water                                    18.015     1042 ?         ?     ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Mannosyl-oligosaccharide 1,3-1,6-alpha-mannosidase, MAN II, Golgi alpha-mannosidase II, AMAN II' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;RSSHHHHHHGEFDDPIRPPLKVARSPRPGQCQDVVQDVPNVDVQMLELYDRMSFKDIDGGVWKQGWNIKYDPLKYNAHHK
LKVFVVPHSHNDPGWIQTFEEYYQHDTKHILSNALRHLHDNPEMKFIWAEISYFARFYHDLGENKKLQMKSIVKNGQLEF
VTGGWVMPDEANSHWRNVLLQLTEGQTWLKQFMNVTPTASWAIDPFGHSPTMPYILQKSGFKNMLIQRTHYSVKKELAQQ
RQLEFLWRQIWDNKGDTALFTHMMPFYSYDIPHTCGPDPKVCCQFDFKRMGSFGLSCPWKVPPRTISDQNVAARSDLLVD
QWKKKAELYRTNVLLIPLGDNFRFKQNTEWDVQRVNYERLFEHINSQAHFNVQAQFGTLQEYFDAVHQAERAGQAEFPTL
SGDFFTYADRSDNYWSGYYTSRPYHKRMDRVLMHYVRAAEMLSAWHSWDGMARIEERLEQARRELSLFQHHDGITGTAKT
HVVVDYEQRMQEALKACQMVMQQSVYRLLTKPSIYSPDFSFSYFTLDDSRWPGSGVEDSRTTIILGEDILPSKHVVMHNT
LPHWREQLVDFYVSSPFVSVTDLANNPVEAQVSPVWSWHHDTLTKTIHPQGSTTKYRIIFKARVPPMGLATYVLTISDSK
PEHTSYASNLLLRKNPTSLPLGQYPEDVKFGDPREISLRVGNGPTLAFSEQGLLKSIQLTQDSPHVPVHFKFLKYGVRSH
GDRSGAYLFLPNGPASPVELGQPVVLVTKGKLESSVSVGLPSVVHQTIMRGGAPEIRNLVDIGSLDNTEIVMRLETHIDS
GDIFYTDLNGLQFIKRRRLDKLPLQANYYPIPSGMFIEDANTRLTLLTGQPLGGSSLASGELEIMQDRRLASDDERGLGQ
GVLDNKPVLHIYRLVLEKVNNCVRPSKLHPAGYLTSAAHKASQSLLDPLDKFIFAENEWIGAQGQFGGDHPSAREDLDVS
VMRRLTKSSAKTQRVGYVLHRTNLMQCGTPEEHTQKLDVCHLLPNVARCERTTLTFLQNLEHLDGMVAPEVCPMETAAYV
SSHSS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;RSSHHHHHHGEFDDPIRPPLKVARSPRPGQCQDVVQDVPNVDVQMLELYDRMSFKDIDGGVWKQGWNIKYDPLKYNAHHK
LKVFVVPHSHNDPGWIQTFEEYYQHDTKHILSNALRHLHDNPEMKFIWAEISYFARFYHDLGENKKLQMKSIVKNGQLEF
VTGGWVMPDEANSHWRNVLLQLTEGQTWLKQFMNVTPTASWAIDPFGHSPTMPYILQKSGFKNMLIQRTHYSVKKELAQQ
RQLEFLWRQIWDNKGDTALFTHMMPFYSYDIPHTCGPDPKVCCQFDFKRMGSFGLSCPWKVPPRTISDQNVAARSDLLVD
QWKKKAELYRTNVLLIPLGDNFRFKQNTEWDVQRVNYERLFEHINSQAHFNVQAQFGTLQEYFDAVHQAERAGQAEFPTL
SGDFFTYADRSDNYWSGYYTSRPYHKRMDRVLMHYVRAAEMLSAWHSWDGMARIEERLEQARRELSLFQHHDGITGTAKT
HVVVDYEQRMQEALKACQMVMQQSVYRLLTKPSIYSPDFSFSYFTLDDSRWPGSGVEDSRTTIILGEDILPSKHVVMHNT
LPHWREQLVDFYVSSPFVSVTDLANNPVEAQVSPVWSWHHDTLTKTIHPQGSTTKYRIIFKARVPPMGLATYVLTISDSK
PEHTSYASNLLLRKNPTSLPLGQYPEDVKFGDPREISLRVGNGPTLAFSEQGLLKSIQLTQDSPHVPVHFKFLKYGVRSH
GDRSGAYLFLPNGPASPVELGQPVVLVTKGKLESSVSVGLPSVVHQTIMRGGAPEIRNLVDIGSLDNTEIVMRLETHIDS
GDIFYTDLNGLQFIKRRRLDKLPLQANYYPIPSGMFIEDANTRLTLLTGQPLGGSSLASGELEIMQDRRLASDDERGLGQ
GVLDNKPVLHIYRLVLEKVNNCVRPSKLHPAGYLTSAAHKASQSLLDPLDKFIFAENEWIGAQGQFGGDHPSAREDLDVS
VMRRLTKSSAKTQRVGYVLHRTNLMQCGTPEEHTQKLDVCHLLPNVARCERTTLTFLQNLEHLDGMVAPEVCPMETAAYV
SSHSS
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1    ARG n 
1 2    SER n 
1 3    SER n 
1 4    HIS n 
1 5    HIS n 
1 6    HIS n 
1 7    HIS n 
1 8    HIS n 
1 9    HIS n 
1 10   GLY n 
1 11   GLU n 
1 12   PHE n 
1 13   ASP n 
1 14   ASP n 
1 15   PRO n 
1 16   ILE n 
1 17   ARG n 
1 18   PRO n 
1 19   PRO n 
1 20   LEU n 
1 21   LYS n 
1 22   VAL n 
1 23   ALA n 
1 24   ARG n 
1 25   SER n 
1 26   PRO n 
1 27   ARG n 
1 28   PRO n 
1 29   GLY n 
1 30   GLN n 
1 31   CYS n 
1 32   GLN n 
1 33   ASP n 
1 34   VAL n 
1 35   VAL n 
1 36   GLN n 
1 37   ASP n 
1 38   VAL n 
1 39   PRO n 
1 40   ASN n 
1 41   VAL n 
1 42   ASP n 
1 43   VAL n 
1 44   GLN n 
1 45   MET n 
1 46   LEU n 
1 47   GLU n 
1 48   LEU n 
1 49   TYR n 
1 50   ASP n 
1 51   ARG n 
1 52   MET n 
1 53   SER n 
1 54   PHE n 
1 55   LYS n 
1 56   ASP n 
1 57   ILE n 
1 58   ASP n 
1 59   GLY n 
1 60   GLY n 
1 61   VAL n 
1 62   TRP n 
1 63   LYS n 
1 64   GLN n 
1 65   GLY n 
1 66   TRP n 
1 67   ASN n 
1 68   ILE n 
1 69   LYS n 
1 70   TYR n 
1 71   ASP n 
1 72   PRO n 
1 73   LEU n 
1 74   LYS n 
1 75   TYR n 
1 76   ASN n 
1 77   ALA n 
1 78   HIS n 
1 79   HIS n 
1 80   LYS n 
1 81   LEU n 
1 82   LYS n 
1 83   VAL n 
1 84   PHE n 
1 85   VAL n 
1 86   VAL n 
1 87   PRO n 
1 88   HIS n 
1 89   SER n 
1 90   HIS n 
1 91   ASN n 
1 92   ASP n 
1 93   PRO n 
1 94   GLY n 
1 95   TRP n 
1 96   ILE n 
1 97   GLN n 
1 98   THR n 
1 99   PHE n 
1 100  GLU n 
1 101  GLU n 
1 102  TYR n 
1 103  TYR n 
1 104  GLN n 
1 105  HIS n 
1 106  ASP n 
1 107  THR n 
1 108  LYS n 
1 109  HIS n 
1 110  ILE n 
1 111  LEU n 
1 112  SER n 
1 113  ASN n 
1 114  ALA n 
1 115  LEU n 
1 116  ARG n 
1 117  HIS n 
1 118  LEU n 
1 119  HIS n 
1 120  ASP n 
1 121  ASN n 
1 122  PRO n 
1 123  GLU n 
1 124  MET n 
1 125  LYS n 
1 126  PHE n 
1 127  ILE n 
1 128  TRP n 
1 129  ALA n 
1 130  GLU n 
1 131  ILE n 
1 132  SER n 
1 133  TYR n 
1 134  PHE n 
1 135  ALA n 
1 136  ARG n 
1 137  PHE n 
1 138  TYR n 
1 139  HIS n 
1 140  ASP n 
1 141  LEU n 
1 142  GLY n 
1 143  GLU n 
1 144  ASN n 
1 145  LYS n 
1 146  LYS n 
1 147  LEU n 
1 148  GLN n 
1 149  MET n 
1 150  LYS n 
1 151  SER n 
1 152  ILE n 
1 153  VAL n 
1 154  LYS n 
1 155  ASN n 
1 156  GLY n 
1 157  GLN n 
1 158  LEU n 
1 159  GLU n 
1 160  PHE n 
1 161  VAL n 
1 162  THR n 
1 163  GLY n 
1 164  GLY n 
1 165  TRP n 
1 166  VAL n 
1 167  MET n 
1 168  PRO n 
1 169  ASP n 
1 170  GLU n 
1 171  ALA n 
1 172  ASN n 
1 173  SER n 
1 174  HIS n 
1 175  TRP n 
1 176  ARG n 
1 177  ASN n 
1 178  VAL n 
1 179  LEU n 
1 180  LEU n 
1 181  GLN n 
1 182  LEU n 
1 183  THR n 
1 184  GLU n 
1 185  GLY n 
1 186  GLN n 
1 187  THR n 
1 188  TRP n 
1 189  LEU n 
1 190  LYS n 
1 191  GLN n 
1 192  PHE n 
1 193  MET n 
1 194  ASN n 
1 195  VAL n 
1 196  THR n 
1 197  PRO n 
1 198  THR n 
1 199  ALA n 
1 200  SER n 
1 201  TRP n 
1 202  ALA n 
1 203  ILE n 
1 204  ASP n 
1 205  PRO n 
1 206  PHE n 
1 207  GLY n 
1 208  HIS n 
1 209  SER n 
1 210  PRO n 
1 211  THR n 
1 212  MET n 
1 213  PRO n 
1 214  TYR n 
1 215  ILE n 
1 216  LEU n 
1 217  GLN n 
1 218  LYS n 
1 219  SER n 
1 220  GLY n 
1 221  PHE n 
1 222  LYS n 
1 223  ASN n 
1 224  MET n 
1 225  LEU n 
1 226  ILE n 
1 227  GLN n 
1 228  ARG n 
1 229  THR n 
1 230  HIS n 
1 231  TYR n 
1 232  SER n 
1 233  VAL n 
1 234  LYS n 
1 235  LYS n 
1 236  GLU n 
1 237  LEU n 
1 238  ALA n 
1 239  GLN n 
1 240  GLN n 
1 241  ARG n 
1 242  GLN n 
1 243  LEU n 
1 244  GLU n 
1 245  PHE n 
1 246  LEU n 
1 247  TRP n 
1 248  ARG n 
1 249  GLN n 
1 250  ILE n 
1 251  TRP n 
1 252  ASP n 
1 253  ASN n 
1 254  LYS n 
1 255  GLY n 
1 256  ASP n 
1 257  THR n 
1 258  ALA n 
1 259  LEU n 
1 260  PHE n 
1 261  THR n 
1 262  HIS n 
1 263  MET n 
1 264  MET n 
1 265  PRO n 
1 266  PHE n 
1 267  TYR n 
1 268  SER n 
1 269  TYR n 
1 270  ASP n 
1 271  ILE n 
1 272  PRO n 
1 273  HIS n 
1 274  THR n 
1 275  CYS n 
1 276  GLY n 
1 277  PRO n 
1 278  ASP n 
1 279  PRO n 
1 280  LYS n 
1 281  VAL n 
1 282  CYS n 
1 283  CYS n 
1 284  GLN n 
1 285  PHE n 
1 286  ASP n 
1 287  PHE n 
1 288  LYS n 
1 289  ARG n 
1 290  MET n 
1 291  GLY n 
1 292  SER n 
1 293  PHE n 
1 294  GLY n 
1 295  LEU n 
1 296  SER n 
1 297  CYS n 
1 298  PRO n 
1 299  TRP n 
1 300  LYS n 
1 301  VAL n 
1 302  PRO n 
1 303  PRO n 
1 304  ARG n 
1 305  THR n 
1 306  ILE n 
1 307  SER n 
1 308  ASP n 
1 309  GLN n 
1 310  ASN n 
1 311  VAL n 
1 312  ALA n 
1 313  ALA n 
1 314  ARG n 
1 315  SER n 
1 316  ASP n 
1 317  LEU n 
1 318  LEU n 
1 319  VAL n 
1 320  ASP n 
1 321  GLN n 
1 322  TRP n 
1 323  LYS n 
1 324  LYS n 
1 325  LYS n 
1 326  ALA n 
1 327  GLU n 
1 328  LEU n 
1 329  TYR n 
1 330  ARG n 
1 331  THR n 
1 332  ASN n 
1 333  VAL n 
1 334  LEU n 
1 335  LEU n 
1 336  ILE n 
1 337  PRO n 
1 338  LEU n 
1 339  GLY n 
1 340  ASP n 
1 341  ASN n 
1 342  PHE n 
1 343  ARG n 
1 344  PHE n 
1 345  LYS n 
1 346  GLN n 
1 347  ASN n 
1 348  THR n 
1 349  GLU n 
1 350  TRP n 
1 351  ASP n 
1 352  VAL n 
1 353  GLN n 
1 354  ARG n 
1 355  VAL n 
1 356  ASN n 
1 357  TYR n 
1 358  GLU n 
1 359  ARG n 
1 360  LEU n 
1 361  PHE n 
1 362  GLU n 
1 363  HIS n 
1 364  ILE n 
1 365  ASN n 
1 366  SER n 
1 367  GLN n 
1 368  ALA n 
1 369  HIS n 
1 370  PHE n 
1 371  ASN n 
1 372  VAL n 
1 373  GLN n 
1 374  ALA n 
1 375  GLN n 
1 376  PHE n 
1 377  GLY n 
1 378  THR n 
1 379  LEU n 
1 380  GLN n 
1 381  GLU n 
1 382  TYR n 
1 383  PHE n 
1 384  ASP n 
1 385  ALA n 
1 386  VAL n 
1 387  HIS n 
1 388  GLN n 
1 389  ALA n 
1 390  GLU n 
1 391  ARG n 
1 392  ALA n 
1 393  GLY n 
1 394  GLN n 
1 395  ALA n 
1 396  GLU n 
1 397  PHE n 
1 398  PRO n 
1 399  THR n 
1 400  LEU n 
1 401  SER n 
1 402  GLY n 
1 403  ASP n 
1 404  PHE n 
1 405  PHE n 
1 406  THR n 
1 407  TYR n 
1 408  ALA n 
1 409  ASP n 
1 410  ARG n 
1 411  SER n 
1 412  ASP n 
1 413  ASN n 
1 414  TYR n 
1 415  TRP n 
1 416  SER n 
1 417  GLY n 
1 418  TYR n 
1 419  TYR n 
1 420  THR n 
1 421  SER n 
1 422  ARG n 
1 423  PRO n 
1 424  TYR n 
1 425  HIS n 
1 426  LYS n 
1 427  ARG n 
1 428  MET n 
1 429  ASP n 
1 430  ARG n 
1 431  VAL n 
1 432  LEU n 
1 433  MET n 
1 434  HIS n 
1 435  TYR n 
1 436  VAL n 
1 437  ARG n 
1 438  ALA n 
1 439  ALA n 
1 440  GLU n 
1 441  MET n 
1 442  LEU n 
1 443  SER n 
1 444  ALA n 
1 445  TRP n 
1 446  HIS n 
1 447  SER n 
1 448  TRP n 
1 449  ASP n 
1 450  GLY n 
1 451  MET n 
1 452  ALA n 
1 453  ARG n 
1 454  ILE n 
1 455  GLU n 
1 456  GLU n 
1 457  ARG n 
1 458  LEU n 
1 459  GLU n 
1 460  GLN n 
1 461  ALA n 
1 462  ARG n 
1 463  ARG n 
1 464  GLU n 
1 465  LEU n 
1 466  SER n 
1 467  LEU n 
1 468  PHE n 
1 469  GLN n 
1 470  HIS n 
1 471  HIS n 
1 472  ASP n 
1 473  GLY n 
1 474  ILE n 
1 475  THR n 
1 476  GLY n 
1 477  THR n 
1 478  ALA n 
1 479  LYS n 
1 480  THR n 
1 481  HIS n 
1 482  VAL n 
1 483  VAL n 
1 484  VAL n 
1 485  ASP n 
1 486  TYR n 
1 487  GLU n 
1 488  GLN n 
1 489  ARG n 
1 490  MET n 
1 491  GLN n 
1 492  GLU n 
1 493  ALA n 
1 494  LEU n 
1 495  LYS n 
1 496  ALA n 
1 497  CYS n 
1 498  GLN n 
1 499  MET n 
1 500  VAL n 
1 501  MET n 
1 502  GLN n 
1 503  GLN n 
1 504  SER n 
1 505  VAL n 
1 506  TYR n 
1 507  ARG n 
1 508  LEU n 
1 509  LEU n 
1 510  THR n 
1 511  LYS n 
1 512  PRO n 
1 513  SER n 
1 514  ILE n 
1 515  TYR n 
1 516  SER n 
1 517  PRO n 
1 518  ASP n 
1 519  PHE n 
1 520  SER n 
1 521  PHE n 
1 522  SER n 
1 523  TYR n 
1 524  PHE n 
1 525  THR n 
1 526  LEU n 
1 527  ASP n 
1 528  ASP n 
1 529  SER n 
1 530  ARG n 
1 531  TRP n 
1 532  PRO n 
1 533  GLY n 
1 534  SER n 
1 535  GLY n 
1 536  VAL n 
1 537  GLU n 
1 538  ASP n 
1 539  SER n 
1 540  ARG n 
1 541  THR n 
1 542  THR n 
1 543  ILE n 
1 544  ILE n 
1 545  LEU n 
1 546  GLY n 
1 547  GLU n 
1 548  ASP n 
1 549  ILE n 
1 550  LEU n 
1 551  PRO n 
1 552  SER n 
1 553  LYS n 
1 554  HIS n 
1 555  VAL n 
1 556  VAL n 
1 557  MET n 
1 558  HIS n 
1 559  ASN n 
1 560  THR n 
1 561  LEU n 
1 562  PRO n 
1 563  HIS n 
1 564  TRP n 
1 565  ARG n 
1 566  GLU n 
1 567  GLN n 
1 568  LEU n 
1 569  VAL n 
1 570  ASP n 
1 571  PHE n 
1 572  TYR n 
1 573  VAL n 
1 574  SER n 
1 575  SER n 
1 576  PRO n 
1 577  PHE n 
1 578  VAL n 
1 579  SER n 
1 580  VAL n 
1 581  THR n 
1 582  ASP n 
1 583  LEU n 
1 584  ALA n 
1 585  ASN n 
1 586  ASN n 
1 587  PRO n 
1 588  VAL n 
1 589  GLU n 
1 590  ALA n 
1 591  GLN n 
1 592  VAL n 
1 593  SER n 
1 594  PRO n 
1 595  VAL n 
1 596  TRP n 
1 597  SER n 
1 598  TRP n 
1 599  HIS n 
1 600  HIS n 
1 601  ASP n 
1 602  THR n 
1 603  LEU n 
1 604  THR n 
1 605  LYS n 
1 606  THR n 
1 607  ILE n 
1 608  HIS n 
1 609  PRO n 
1 610  GLN n 
1 611  GLY n 
1 612  SER n 
1 613  THR n 
1 614  THR n 
1 615  LYS n 
1 616  TYR n 
1 617  ARG n 
1 618  ILE n 
1 619  ILE n 
1 620  PHE n 
1 621  LYS n 
1 622  ALA n 
1 623  ARG n 
1 624  VAL n 
1 625  PRO n 
1 626  PRO n 
1 627  MET n 
1 628  GLY n 
1 629  LEU n 
1 630  ALA n 
1 631  THR n 
1 632  TYR n 
1 633  VAL n 
1 634  LEU n 
1 635  THR n 
1 636  ILE n 
1 637  SER n 
1 638  ASP n 
1 639  SER n 
1 640  LYS n 
1 641  PRO n 
1 642  GLU n 
1 643  HIS n 
1 644  THR n 
1 645  SER n 
1 646  TYR n 
1 647  ALA n 
1 648  SER n 
1 649  ASN n 
1 650  LEU n 
1 651  LEU n 
1 652  LEU n 
1 653  ARG n 
1 654  LYS n 
1 655  ASN n 
1 656  PRO n 
1 657  THR n 
1 658  SER n 
1 659  LEU n 
1 660  PRO n 
1 661  LEU n 
1 662  GLY n 
1 663  GLN n 
1 664  TYR n 
1 665  PRO n 
1 666  GLU n 
1 667  ASP n 
1 668  VAL n 
1 669  LYS n 
1 670  PHE n 
1 671  GLY n 
1 672  ASP n 
1 673  PRO n 
1 674  ARG n 
1 675  GLU n 
1 676  ILE n 
1 677  SER n 
1 678  LEU n 
1 679  ARG n 
1 680  VAL n 
1 681  GLY n 
1 682  ASN n 
1 683  GLY n 
1 684  PRO n 
1 685  THR n 
1 686  LEU n 
1 687  ALA n 
1 688  PHE n 
1 689  SER n 
1 690  GLU n 
1 691  GLN n 
1 692  GLY n 
1 693  LEU n 
1 694  LEU n 
1 695  LYS n 
1 696  SER n 
1 697  ILE n 
1 698  GLN n 
1 699  LEU n 
1 700  THR n 
1 701  GLN n 
1 702  ASP n 
1 703  SER n 
1 704  PRO n 
1 705  HIS n 
1 706  VAL n 
1 707  PRO n 
1 708  VAL n 
1 709  HIS n 
1 710  PHE n 
1 711  LYS n 
1 712  PHE n 
1 713  LEU n 
1 714  LYS n 
1 715  TYR n 
1 716  GLY n 
1 717  VAL n 
1 718  ARG n 
1 719  SER n 
1 720  HIS n 
1 721  GLY n 
1 722  ASP n 
1 723  ARG n 
1 724  SER n 
1 725  GLY n 
1 726  ALA n 
1 727  TYR n 
1 728  LEU n 
1 729  PHE n 
1 730  LEU n 
1 731  PRO n 
1 732  ASN n 
1 733  GLY n 
1 734  PRO n 
1 735  ALA n 
1 736  SER n 
1 737  PRO n 
1 738  VAL n 
1 739  GLU n 
1 740  LEU n 
1 741  GLY n 
1 742  GLN n 
1 743  PRO n 
1 744  VAL n 
1 745  VAL n 
1 746  LEU n 
1 747  VAL n 
1 748  THR n 
1 749  LYS n 
1 750  GLY n 
1 751  LYS n 
1 752  LEU n 
1 753  GLU n 
1 754  SER n 
1 755  SER n 
1 756  VAL n 
1 757  SER n 
1 758  VAL n 
1 759  GLY n 
1 760  LEU n 
1 761  PRO n 
1 762  SER n 
1 763  VAL n 
1 764  VAL n 
1 765  HIS n 
1 766  GLN n 
1 767  THR n 
1 768  ILE n 
1 769  MET n 
1 770  ARG n 
1 771  GLY n 
1 772  GLY n 
1 773  ALA n 
1 774  PRO n 
1 775  GLU n 
1 776  ILE n 
1 777  ARG n 
1 778  ASN n 
1 779  LEU n 
1 780  VAL n 
1 781  ASP n 
1 782  ILE n 
1 783  GLY n 
1 784  SER n 
1 785  LEU n 
1 786  ASP n 
1 787  ASN n 
1 788  THR n 
1 789  GLU n 
1 790  ILE n 
1 791  VAL n 
1 792  MET n 
1 793  ARG n 
1 794  LEU n 
1 795  GLU n 
1 796  THR n 
1 797  HIS n 
1 798  ILE n 
1 799  ASP n 
1 800  SER n 
1 801  GLY n 
1 802  ASP n 
1 803  ILE n 
1 804  PHE n 
1 805  TYR n 
1 806  THR n 
1 807  ASP n 
1 808  LEU n 
1 809  ASN n 
1 810  GLY n 
1 811  LEU n 
1 812  GLN n 
1 813  PHE n 
1 814  ILE n 
1 815  LYS n 
1 816  ARG n 
1 817  ARG n 
1 818  ARG n 
1 819  LEU n 
1 820  ASP n 
1 821  LYS n 
1 822  LEU n 
1 823  PRO n 
1 824  LEU n 
1 825  GLN n 
1 826  ALA n 
1 827  ASN n 
1 828  TYR n 
1 829  TYR n 
1 830  PRO n 
1 831  ILE n 
1 832  PRO n 
1 833  SER n 
1 834  GLY n 
1 835  MET n 
1 836  PHE n 
1 837  ILE n 
1 838  GLU n 
1 839  ASP n 
1 840  ALA n 
1 841  ASN n 
1 842  THR n 
1 843  ARG n 
1 844  LEU n 
1 845  THR n 
1 846  LEU n 
1 847  LEU n 
1 848  THR n 
1 849  GLY n 
1 850  GLN n 
1 851  PRO n 
1 852  LEU n 
1 853  GLY n 
1 854  GLY n 
1 855  SER n 
1 856  SER n 
1 857  LEU n 
1 858  ALA n 
1 859  SER n 
1 860  GLY n 
1 861  GLU n 
1 862  LEU n 
1 863  GLU n 
1 864  ILE n 
1 865  MET n 
1 866  GLN n 
1 867  ASP n 
1 868  ARG n 
1 869  ARG n 
1 870  LEU n 
1 871  ALA n 
1 872  SER n 
1 873  ASP n 
1 874  ASP n 
1 875  GLU n 
1 876  ARG n 
1 877  GLY n 
1 878  LEU n 
1 879  GLY n 
1 880  GLN n 
1 881  GLY n 
1 882  VAL n 
1 883  LEU n 
1 884  ASP n 
1 885  ASN n 
1 886  LYS n 
1 887  PRO n 
1 888  VAL n 
1 889  LEU n 
1 890  HIS n 
1 891  ILE n 
1 892  TYR n 
1 893  ARG n 
1 894  LEU n 
1 895  VAL n 
1 896  LEU n 
1 897  GLU n 
1 898  LYS n 
1 899  VAL n 
1 900  ASN n 
1 901  ASN n 
1 902  CYS n 
1 903  VAL n 
1 904  ARG n 
1 905  PRO n 
1 906  SER n 
1 907  LYS n 
1 908  LEU n 
1 909  HIS n 
1 910  PRO n 
1 911  ALA n 
1 912  GLY n 
1 913  TYR n 
1 914  LEU n 
1 915  THR n 
1 916  SER n 
1 917  ALA n 
1 918  ALA n 
1 919  HIS n 
1 920  LYS n 
1 921  ALA n 
1 922  SER n 
1 923  GLN n 
1 924  SER n 
1 925  LEU n 
1 926  LEU n 
1 927  ASP n 
1 928  PRO n 
1 929  LEU n 
1 930  ASP n 
1 931  LYS n 
1 932  PHE n 
1 933  ILE n 
1 934  PHE n 
1 935  ALA n 
1 936  GLU n 
1 937  ASN n 
1 938  GLU n 
1 939  TRP n 
1 940  ILE n 
1 941  GLY n 
1 942  ALA n 
1 943  GLN n 
1 944  GLY n 
1 945  GLN n 
1 946  PHE n 
1 947  GLY n 
1 948  GLY n 
1 949  ASP n 
1 950  HIS n 
1 951  PRO n 
1 952  SER n 
1 953  ALA n 
1 954  ARG n 
1 955  GLU n 
1 956  ASP n 
1 957  LEU n 
1 958  ASP n 
1 959  VAL n 
1 960  SER n 
1 961  VAL n 
1 962  MET n 
1 963  ARG n 
1 964  ARG n 
1 965  LEU n 
1 966  THR n 
1 967  LYS n 
1 968  SER n 
1 969  SER n 
1 970  ALA n 
1 971  LYS n 
1 972  THR n 
1 973  GLN n 
1 974  ARG n 
1 975  VAL n 
1 976  GLY n 
1 977  TYR n 
1 978  VAL n 
1 979  LEU n 
1 980  HIS n 
1 981  ARG n 
1 982  THR n 
1 983  ASN n 
1 984  LEU n 
1 985  MET n 
1 986  GLN n 
1 987  CYS n 
1 988  GLY n 
1 989  THR n 
1 990  PRO n 
1 991  GLU n 
1 992  GLU n 
1 993  HIS n 
1 994  THR n 
1 995  GLN n 
1 996  LYS n 
1 997  LEU n 
1 998  ASP n 
1 999  VAL n 
1 1000 CYS n 
1 1001 HIS n 
1 1002 LEU n 
1 1003 LEU n 
1 1004 PRO n 
1 1005 ASN n 
1 1006 VAL n 
1 1007 ALA n 
1 1008 ARG n 
1 1009 CYS n 
1 1010 GLU n 
1 1011 ARG n 
1 1012 THR n 
1 1013 THR n 
1 1014 LEU n 
1 1015 THR n 
1 1016 PHE n 
1 1017 LEU n 
1 1018 GLN n 
1 1019 ASN n 
1 1020 LEU n 
1 1021 GLU n 
1 1022 HIS n 
1 1023 LEU n 
1 1024 ASP n 
1 1025 GLY n 
1 1026 MET n 
1 1027 VAL n 
1 1028 ALA n 
1 1029 PRO n 
1 1030 GLU n 
1 1031 VAL n 
1 1032 CYS n 
1 1033 PRO n 
1 1034 MET n 
1 1035 GLU n 
1 1036 THR n 
1 1037 ALA n 
1 1038 ALA n 
1 1039 TYR n 
1 1040 VAL n 
1 1041 SER n 
1 1042 SER n 
1 1043 HIS n 
1 1044 SER n 
1 1045 SER n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               'fruit fly' 
_entity_src_gen.gene_src_genus                     Drosophila 
_entity_src_gen.pdbx_gene_src_gene                 'ALPHA-MAN-II OR GMII OR CG18474/CG18802/CG8139' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Drosophila melanogaster' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     7227 
_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               'fruit fly' 
_entity_src_gen.pdbx_host_org_scientific_name      'Drosophila melanogaster' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7227 
_entity_src_gen.host_org_genus                     Drosophila 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               S2 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    MAN2_DROME 
_struct_ref.pdbx_db_accession          Q24451 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;DDPIRPPLKVARSPRPGQCQDVVQDVPNVDVQMLELYDRMSFKDIDGGVWKQGWNIKYDPLKYNAHHKLKVFVVPHSHND
PGWIQTFEEYYQHDTKHILSNALRHLHDNPEMKFIWAEISYFARFYHDLGENKKLQMKSIVKNGQLEFVTGGWVMPDEAN
SHWRNVLLQLTEGQTWLKQFMNVTPTASWAIDPFGHSPTMPYILQKSGFKNMLIQRTHYSVKKELAQQRQLEFLWRQIWD
NKGDTALFTHMMPFYSYDIPHTCGPDPKVCCQFDFKRMGSFGLSCPWKVPPRTISDQNVAARSDLLVDQWKKKAELYRTN
VLLIPLGDDFRFKQNTEWDVQRVNYERLFEHINSQAHFNVQAQFGTLQEYFDAVHQAERAGQAEFPTLSGDFFTYADRSD
NYWSGYYTSRPYHKRMDRVLMHYVRAAEMLSAWHSWDGMARIEERLEQARRELSLFQHHDGITGTAKTHVVVDYEQRMQE
ALKACQMVMQQSVYRLLTKPSIYSPDFSFSYFTLDDSRWPGSGVEDSRTTIILGEDILPSKHVVMHNTLPHWREQLVDFY
VSSPFVSVTDLANNPVEAQVSPVWSWHHDTLTKTIHPQGSTTKYRIIFKARVPPMGLATYVLTISDSKPEHTSYASNLLL
RKNPTSLPLGQYPEDVKFGDPREISLRVGNGPTLAFSEQGLLKSIQLTQDSPHVPVHFKFLKYGVRSHGDRSGAYLFLPN
GPASPVELGQPVVLVTKGKLESSVSVGLPSVVHQTIMRGGAPEIRNLVDIGSLDNTEIVMRLETHIDSGDIFYTDLNGLQ
FIKRRRLDKLPLQANYYPIPSGMFIEDANTRLTLLTGQPLGGSSLASGELEIMQDRRLASDDERGLGQGVLDNKPVLHIY
RLVLEKVNNCVRPSELHPAGYLTSAAHKASQSLLDPLDKFIFAENEWIGAQGQFGGDHPSAREDLDVSVMRRLTKSSAKT
QRVGYVLHRTNLMQCGTPEEHTQKLDVCHLLPNVARCERTTLTFLQNLEHLDGMVAPEVCPMETAAYVSSHSS
;
_struct_ref.pdbx_align_begin           76 
_struct_ref.pdbx_db_isoform            ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              1QX1 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 13 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 1045 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q24451 
_struct_ref_seq.db_align_beg                  76 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1108 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       13 
_struct_ref_seq.pdbx_auth_seq_align_end       1045 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 1QX1 ARG A 1   ? UNP Q24451 ?   ?   'CLONING ARTIFACT' 1   1  
1 1QX1 SER A 2   ? UNP Q24451 ?   ?   'CLONING ARTIFACT' 2   2  
1 1QX1 SER A 3   ? UNP Q24451 ?   ?   'CLONING ARTIFACT' 3   3  
1 1QX1 HIS A 4   ? UNP Q24451 ?   ?   'EXPRESSION TAG'   4   4  
1 1QX1 HIS A 5   ? UNP Q24451 ?   ?   'EXPRESSION TAG'   5   5  
1 1QX1 HIS A 6   ? UNP Q24451 ?   ?   'EXPRESSION TAG'   6   6  
1 1QX1 HIS A 7   ? UNP Q24451 ?   ?   'EXPRESSION TAG'   7   7  
1 1QX1 HIS A 8   ? UNP Q24451 ?   ?   'EXPRESSION TAG'   8   8  
1 1QX1 HIS A 9   ? UNP Q24451 ?   ?   'EXPRESSION TAG'   9   9  
1 1QX1 GLY A 10  ? UNP Q24451 ?   ?   'CLONING ARTIFACT' 10  10 
1 1QX1 GLU A 11  ? UNP Q24451 ?   ?   'CLONING ARTIFACT' 11  11 
1 1QX1 PHE A 12  ? UNP Q24451 ?   ?   'CLONING ARTIFACT' 12  12 
1 1QX1 ASN A 341 ? UNP Q24451 ASP 404 ENGINEERED         341 13 
1 1QX1 LYS A 907 ? UNP Q24451 GLU 970 'SEE REMARK 999'   907 14 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                  ?                                            'C3 H7 N O2'     
89.093  
ARG 'L-peptide linking' y ARGININE                                 ?                                            'C6 H15 N4 O2 1' 
175.209 
ASN 'L-peptide linking' y ASPARAGINE                               ?                                            'C4 H8 N2 O3'    
132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                          ?                                            'C4 H7 N O4'     
133.103 
CYS 'L-peptide linking' y CYSTEINE                                 ?                                            'C3 H7 N O2 S'   
121.158 
FMF non-polymer         . '2-DEOXY-2-FLUOROHEXOPYRANOSYL FLUORIDE' '2-DEOXY-2-FLUORO-ALPHA-D-MANNOSYL FLUORIDE' 'C6 H10 F2 O4'   
184.138 
GLN 'L-peptide linking' y GLUTAMINE                                ?                                            'C5 H10 N2 O3'   
146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                          ?                                            'C5 H9 N O4'     
147.129 
GLY 'peptide linking'   y GLYCINE                                  ?                                            'C2 H5 N O2'     
75.067  
HIS 'L-peptide linking' y HISTIDINE                                ?                                            'C6 H10 N3 O2 1' 
156.162 
HOH non-polymer         . WATER                                    ?                                            'H2 O'           
18.015  
ILE 'L-peptide linking' y ISOLEUCINE                               ?                                            'C6 H13 N O2'    
131.173 
LEU 'L-peptide linking' y LEUCINE                                  ?                                            'C6 H13 N O2'    
131.173 
LYS 'L-peptide linking' y LYSINE                                   ?                                            'C6 H15 N2 O2 1' 
147.195 
MET 'L-peptide linking' y METHIONINE                               ?                                            'C5 H11 N O2 S'  
149.211 
MPD non-polymer         . '(4S)-2-METHYL-2,4-PENTANEDIOL'          ?                                            'C6 H14 O2'      
118.174 
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 
ZN  non-polymer         . 'ZINC ION'                               ?                                            'Zn 2'           
65.409  
# 
_exptl.entry_id          1QX1 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.20 
_exptl_crystal.density_percent_sol   44.06 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              7 
_exptl_crystal_grow.pdbx_details    'PEG 6000, MPD, Tris, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 298K' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'ADSC QUANTUM 4' 
_diffrn_detector.pdbx_collection_date   2002-03-22 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'Si(111)' 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.95 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'CHESS BEAMLINE F1' 
_diffrn_source.pdbx_synchrotron_site       CHESS 
_diffrn_source.pdbx_synchrotron_beamline   F1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        0.95 
# 
_reflns.entry_id                     1QX1 
_reflns.observed_criterion_sigma_I   2.0 
_reflns.observed_criterion_sigma_F   2.9 
_reflns.d_resolution_low             30 
_reflns.d_resolution_high            1.3 
_reflns.number_obs                   246051 
_reflns.number_all                   258750 
_reflns.percent_possible_obs         95.3 
_reflns.pdbx_Rmerge_I_obs            0.106 
_reflns.pdbx_Rsym_value              0.106 
_reflns.pdbx_netI_over_sigmaI        14.7 
_reflns.B_iso_Wilson_estimate        12.9 
_reflns.pdbx_redundancy              6.5 
_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_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high             1.3 
_reflns_shell.d_res_low              1.38 
_reflns_shell.percent_possible_all   83.2 
_reflns_shell.Rmerge_I_obs           0.586 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    2.9 
_reflns_shell.pdbx_redundancy        ? 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      ? 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.pdbx_diffrn_id         1 
# 
_refine.entry_id                                 1QX1 
_refine.ls_number_reflns_obs                     239861 
_refine.ls_number_reflns_all                     258759 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.0 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             29.23 
_refine.ls_d_res_high                            1.30 
_refine.ls_percent_reflns_obs                    92.7 
_refine.ls_R_factor_obs                          0.17 
_refine.ls_R_factor_all                          0.17 
_refine.ls_R_factor_R_work                       0.17 
_refine.ls_R_factor_R_free                       0.189 
_refine.ls_R_factor_R_free_error                 0.004 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 0.9 
_refine.ls_number_reflns_R_free                  2180 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               16.1 
_refine.aniso_B[1][1]                            0.08 
_refine.aniso_B[2][2]                            0.22 
_refine.aniso_B[3][3]                            -0.30 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    'FLAT MODEL' 
_refine.solvent_model_param_ksol                 0.369171 
_refine.solvent_model_param_bsol                 54.9168 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      1HTY 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             RESTRAINED 
_refine.pdbx_stereochemistry_target_values       'Engh & Huber' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_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_analyze.entry_id                        1QX1 
_refine_analyze.Luzzati_coordinate_error_obs    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   0.15 
_refine_analyze.Luzzati_sigma_a_free            0.12 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        8181 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         34 
_refine_hist.number_atoms_solvent             1042 
_refine_hist.number_atoms_total               9257 
_refine_hist.d_res_high                       1.30 
_refine_hist.d_res_low                        29.23 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
c_bond_d                0.022 ?    ? ? 'X-RAY DIFFRACTION' ? 
c_bond_d_na             ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_bond_d_prot           ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_d               ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_d_na            ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_d_prot          ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg             2.0   ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg_na          ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg_prot        ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d      25.4  ?    ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d_na   ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d_prot ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d      1.42  ?    ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d_na   ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d_prot ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_mcbond_it             1.56  1.50 ? ? 'X-RAY DIFFRACTION' ? 
c_mcangle_it            2.16  2.00 ? ? 'X-RAY DIFFRACTION' ? 
c_scbond_it             2.90  2.00 ? ? 'X-RAY DIFFRACTION' ? 
c_scangle_it            4.03  2.50 ? ? 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_total_number_of_bins_used   6 
_refine_ls_shell.d_res_high                       1.30 
_refine_ls_shell.d_res_low                        1.38 
_refine_ls_shell.number_reflns_R_work             35149 
_refine_ls_shell.R_factor_R_work                  0.231 
_refine_ls_shell.percent_reflns_obs               83.2 
_refine_ls_shell.R_factor_R_free                  0.263 
_refine_ls_shell.R_factor_R_free_error            0.014 
_refine_ls_shell.percent_reflns_R_free            1.0 
_refine_ls_shell.number_reflns_R_free             352 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.R_factor_all                     ? 
# 
loop_
_pdbx_xplor_file.serial_no 
_pdbx_xplor_file.param_file 
_pdbx_xplor_file.topol_file 
_pdbx_xplor_file.pdbx_refine_id 
1 PROTEIN_REP.PARAM  PROTEIN_REP.TOP  'X-RAY DIFFRACTION' 
2 CARBOHYDRATE.PARAM CARBOHYDRATE.TOP 'X-RAY DIFFRACTION' 
3 CIS_PEPTIDE.PARAM  CIS_PEPTIDE.TOP  'X-RAY DIFFRACTION' 
4 WATER_REP.PARAM    WATER_REP.TOP    'X-RAY DIFFRACTION' 
5 ION.PARAM          ION.TOP          'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  1QX1 
_struct.title                     'Golgi alpha-mannosidase II D341N mutant complex with 2-F-mannosyl-F' 
_struct.pdbx_descriptor           'Alpha-mannosidase II (E.C.3.2.1.114)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        1QX1 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            'Glycosyl hydrolase family 38, covalent catalytic intermediate, HYDROLASE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
# 
_struct_biol.id   1 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  1  MET A 45   ? MET A 52   ? MET A 45   MET A 52   1 ? 8  
HELX_P HELX_P2  2  ASP A 71   ? TYR A 75   ? ASP A 71   TYR A 75   5 ? 5  
HELX_P HELX_P3  3  THR A 98   ? ASP A 106  ? THR A 98   ASP A 106  1 ? 9  
HELX_P HELX_P4  4  ASP A 106  ? ASN A 121  ? ASP A 106  ASN A 121  1 ? 16 
HELX_P HELX_P5  5  GLU A 130  ? LEU A 141  ? GLU A 130  LEU A 141  1 ? 12 
HELX_P HELX_P6  6  GLY A 142  ? ASN A 155  ? GLY A 142  ASN A 155  1 ? 14 
HELX_P HELX_P7  7  HIS A 174  ? ASN A 194  ? HIS A 174  ASN A 194  1 ? 21 
HELX_P HELX_P8  8  PRO A 210  ? LYS A 218  ? PRO A 210  LYS A 218  1 ? 9  
HELX_P HELX_P9  9  HIS A 230  ? GLN A 240  ? HIS A 230  GLN A 240  1 ? 11 
HELX_P HELX_P10 10 ASP A 270  ? THR A 274  ? ASP A 270  THR A 274  5 ? 5  
HELX_P HELX_P11 11 ASP A 278  ? CYS A 283  ? ASP A 278  CYS A 283  1 ? 6  
HELX_P HELX_P12 12 GLN A 284  ? MET A 290  ? GLN A 284  MET A 290  5 ? 7  
HELX_P HELX_P13 13 ASN A 310  ? GLU A 327  ? ASN A 310  GLU A 327  1 ? 18 
HELX_P HELX_P14 14 GLN A 346  ? GLN A 367  ? GLN A 346  GLN A 367  1 ? 22 
HELX_P HELX_P15 15 ALA A 368  ? PHE A 370  ? ALA A 368  PHE A 370  5 ? 3  
HELX_P HELX_P16 16 THR A 378  ? ALA A 392  ? THR A 378  ALA A 392  1 ? 15 
HELX_P HELX_P17 17 SER A 416  ? THR A 420  ? SER A 416  THR A 420  5 ? 5  
HELX_P HELX_P18 18 ARG A 422  ? TRP A 445  ? ARG A 422  TRP A 445  1 ? 24 
HELX_P HELX_P19 19 ASP A 449  ? ALA A 452  ? ASP A 449  ALA A 452  5 ? 4  
HELX_P HELX_P20 20 ARG A 453  ? GLN A 469  ? ARG A 453  GLN A 469  1 ? 17 
HELX_P HELX_P21 21 LYS A 479  ? LEU A 509  ? LYS A 479  LEU A 509  1 ? 31 
HELX_P HELX_P22 22 PRO A 823  ? TYR A 828  ? PRO A 823  TYR A 828  5 ? 6  
HELX_P HELX_P23 23 THR A 915  ? ASP A 927  ? THR A 915  ASP A 927  1 ? 13 
HELX_P HELX_P24 24 ASP A 998  ? LEU A 1002 ? ASP A 998  LEU A 1002 5 ? 5  
HELX_P HELX_P25 25 ASP A 1024 ? VAL A 1027 ? ASP A 1024 VAL A 1027 5 ? 4  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1 disulf ? ? A CYS 31   SG  ? ? ? 1_555 A CYS 1032 SG  ? ? A CYS 31   A CYS 1032 1_555 ? ? ? ? ? ? ? 2.054 ? 
disulf2 disulf ? ? A CYS 275  SG  ? ? ? 1_555 A CYS 282  SG  ? ? A CYS 275  A CYS 282  1_555 ? ? ? ? ? ? ? 2.044 ? 
disulf3 disulf ? ? A CYS 283  SG  ? ? ? 1_555 A CYS 297  SG  ? ? A CYS 283  A CYS 297  1_555 ? ? ? ? ? ? ? 2.100 ? 
disulf4 disulf ? ? A CYS 902  SG  ? ? ? 1_555 A CYS 987  SG  ? ? A CYS 902  A CYS 987  1_555 ? ? ? ? ? ? ? 2.068 ? 
disulf5 disulf ? ? A CYS 1000 SG  ? ? ? 1_555 A CYS 1009 SG  ? ? A CYS 1000 A CYS 1009 1_555 ? ? ? ? ? ? ? 2.014 ? 
covale1 covale ? ? A ASN 194  ND2 ? ? ? 1_555 B NAG .    C1  ? ? A ASN 194  A NAG 2001 1_555 ? ? ? ? ? ? ? 1.891 ? 
covale2 covale ? ? A ASP 204  OD1 ? ? ? 1_555 D FMF .    C1  A ? A ASP 204  A FMF 2003 1_555 ? ? ? ? ? ? ? 2.173 ? 
covale3 covale ? ? A ASP 204  OD1 ? ? ? 1_555 D FMF .    C1  B ? A ASP 204  A FMF 2003 1_555 ? ? ? ? ? ? ? 1.503 ? 
metalc1 metalc ? ? C ZN  .    ZN  ? ? ? 1_555 A ASP 92   OD1 ? ? A ZN  2004 A ASP 92   1_555 ? ? ? ? ? ? ? 2.044 ? 
metalc2 metalc ? ? C ZN  .    ZN  ? ? ? 1_555 D FMF .    F2  B ? A ZN  2004 A FMF 2003 1_555 ? ? ? ? ? ? ? 2.484 ? 
metalc3 metalc ? ? C ZN  .    ZN  ? ? ? 1_555 D FMF .    O3  A ? A ZN  2004 A FMF 2003 1_555 ? ? ? ? ? ? ? 2.078 ? 
metalc4 metalc ? ? C ZN  .    ZN  ? ? ? 1_555 D FMF .    O3  B ? A ZN  2004 A FMF 2003 1_555 ? ? ? ? ? ? ? 2.197 ? 
metalc5 metalc ? ? C ZN  .    ZN  ? ? ? 1_555 A HIS 471  NE2 ? ? A ZN  2004 A HIS 471  1_555 ? ? ? ? ? ? ? 2.081 ? 
metalc6 metalc ? ? C ZN  .    ZN  ? ? ? 1_555 A HIS 90   NE2 ? ? A ZN  2004 A HIS 90   1_555 ? ? ? ? ? ? ? 2.072 ? 
metalc7 metalc ? ? C ZN  .    ZN  ? ? ? 1_555 D FMF .    F2  A ? A ZN  2004 A FMF 2003 1_555 ? ? ? ? ? ? ? 2.551 ? 
metalc8 metalc ? ? C ZN  .    ZN  ? ? ? 1_555 A ASP 204  OD1 ? ? A ZN  2004 A ASP 204  1_555 ? ? ? ? ? ? ? 2.696 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
metalc ? ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 PHE 405 A . ? PHE 405 A THR 406 A ? THR 406 A 1 -2.26 
2 TRP 531 A . ? TRP 531 A PRO 532 A ? PRO 532 A 1 -1.19 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 6  ? 
B ? 3  ? 
C ? 2  ? 
D ? 2  ? 
E ? 6  ? 
F ? 5  ? 
G ? 5  ? 
H ? 12 ? 
I ? 5  ? 
J ? 8  ? 
K ? 5  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1  2  ? parallel      
A 2  3  ? parallel      
A 3  4  ? anti-parallel 
A 4  5  ? parallel      
A 5  6  ? parallel      
B 1  2  ? parallel      
B 2  3  ? parallel      
C 1  2  ? parallel      
D 1  2  ? anti-parallel 
E 1  2  ? anti-parallel 
E 2  3  ? anti-parallel 
E 3  4  ? anti-parallel 
E 4  5  ? anti-parallel 
E 5  6  ? anti-parallel 
F 1  2  ? anti-parallel 
F 2  3  ? anti-parallel 
F 3  4  ? anti-parallel 
F 4  5  ? anti-parallel 
G 1  2  ? parallel      
G 2  3  ? anti-parallel 
G 3  4  ? anti-parallel 
G 4  5  ? parallel      
H 1  2  ? parallel      
H 2  3  ? anti-parallel 
H 3  4  ? anti-parallel 
H 4  5  ? anti-parallel 
H 5  6  ? anti-parallel 
H 6  7  ? anti-parallel 
H 7  8  ? anti-parallel 
H 8  9  ? anti-parallel 
H 9  10 ? anti-parallel 
H 10 11 ? anti-parallel 
H 11 12 ? anti-parallel 
I 1  2  ? anti-parallel 
I 2  3  ? anti-parallel 
I 3  4  ? anti-parallel 
I 4  5  ? anti-parallel 
J 1  2  ? anti-parallel 
J 2  3  ? anti-parallel 
J 3  4  ? anti-parallel 
J 4  5  ? anti-parallel 
J 5  6  ? anti-parallel 
J 6  7  ? anti-parallel 
J 7  8  ? anti-parallel 
K 1  2  ? anti-parallel 
K 2  3  ? anti-parallel 
K 3  4  ? anti-parallel 
K 4  5  ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1  VAL A 43   ? GLN A 44   ? VAL A 43   GLN A 44   
A 2  THR A 399  ? SER A 401  ? THR A 399  SER A 401  
A 3  GLU A 244  ? TRP A 247  ? GLU A 244  TRP A 247  
A 4  LEU A 259  ? MET A 263  ? LEU A 259  MET A 263  
A 5  ASN A 223  ? ILE A 226  ? ASN A 223  ILE A 226  
A 6  ALA A 199  ? ALA A 202  ? ALA A 199  ALA A 202  
B 1  VAL A 333  ? ASN A 341  ? VAL A 333  ASN A 341  
B 2  LEU A 81   ? HIS A 90   ? LEU A 81   HIS A 90   
B 3  VAL A 372  ? PHE A 376  ? VAL A 372  PHE A 376  
C 1  PHE A 126  ? TRP A 128  ? PHE A 126  TRP A 128  
C 2  LEU A 158  ? PHE A 160  ? LEU A 158  PHE A 160  
D 1  ALA A 408  ? ARG A 410  ? ALA A 408  ARG A 410  
D 2  ASN A 413  ? TYR A 414  ? ASN A 413  TYR A 414  
E 1  PHE A 524  ? ASP A 527  ? PHE A 524  ASP A 527  
E 2  ASP A 930  ? PHE A 934  ? ASP A 930  PHE A 934  
E 3  SER A 552  ? ASN A 559  ? SER A 552  ASN A 559  
E 4  GLY A 628  ? ILE A 636  ? GLY A 628  ILE A 636  
E 5  VAL A 578  ? ASP A 582  ? VAL A 578  ASP A 582  
E 6  PRO A 587  ? VAL A 588  ? PRO A 587  VAL A 588  
F 1  PHE A 524  ? ASP A 527  ? PHE A 524  ASP A 527  
F 2  ASP A 930  ? PHE A 934  ? ASP A 930  PHE A 934  
F 3  SER A 552  ? ASN A 559  ? SER A 552  ASN A 559  
F 4  GLY A 628  ? ILE A 636  ? GLY A 628  ILE A 636  
F 5  GLN A 945  ? PHE A 946  ? GLN A 945  PHE A 946  
G 1  THR A 542  ? ILE A 543  ? THR A 542  ILE A 543  
G 2  ARG A 565  ? VAL A 573  ? ARG A 565  VAL A 573  
G 3  THR A 606  ? VAL A 624  ? THR A 606  VAL A 624  
G 4  ALA A 590  ? ASP A 601  ? ALA A 590  ASP A 601  
G 5  THR A 644  ? TYR A 646  ? THR A 644  TYR A 646  
H 1  LYS A 669  ? GLY A 671  ? LYS A 669  GLY A 671  
H 2  SER A 648  ? LEU A 652  ? SER A 648  LEU A 652  
H 3  VAL A 745  ? LYS A 749  ? VAL A 745  LYS A 749  
H 4  SER A 754  ? LEU A 760  ? SER A 754  LEU A 760  
H 5  VAL A 763  ? MET A 769  ? VAL A 763  MET A 769  
H 6  GLU A 775  ? VAL A 780  ? GLU A 775  VAL A 780  
H 7  VAL A 888  ? LYS A 898  ? VAL A 888  LYS A 898  
H 8  THR A 842  ? THR A 848  ? THR A 842  THR A 848  
H 9  GLY A 834  ? GLU A 838  ? GLY A 834  GLU A 838  
H 10 ILE A 803  ? LEU A 808  ? ILE A 803  LEU A 808  
H 11 GLN A 812  ? ARG A 817  ? GLN A 812  ARG A 817  
H 12 ALA A 911  ? GLY A 912  ? ALA A 911  GLY A 912  
I 1  ILE A 676  ? ARG A 679  ? ILE A 676  ARG A 679  
I 2  THR A 685  ? PHE A 688  ? THR A 685  PHE A 688  
I 3  LEU A 694  ? GLN A 698  ? LEU A 694  GLN A 698  
I 4  HIS A 705  ? TYR A 715  ? HIS A 705  TYR A 715  
I 5  SER A 736  ? PRO A 737  ? SER A 736  PRO A 737  
J 1  ILE A 676  ? ARG A 679  ? ILE A 676  ARG A 679  
J 2  THR A 685  ? PHE A 688  ? THR A 685  PHE A 688  
J 3  LEU A 694  ? GLN A 698  ? LEU A 694  GLN A 698  
J 4  HIS A 705  ? TYR A 715  ? HIS A 705  TYR A 715  
J 5  THR A 788  ? THR A 796  ? THR A 788  THR A 796  
J 6  GLU A 861  ? ARG A 869  ? GLU A 861  ARG A 869  
J 7  LEU A 852  ? SER A 855  ? LEU A 852  SER A 855  
J 8  TYR A 829  ? ILE A 831  ? TYR A 829  ILE A 831  
K 1  LEU A 957  ? ARG A 964  ? LEU A 957  ARG A 964  
K 2  GLN A 973  ? ARG A 981  ? GLN A 973  ARG A 981  
K 3  THR A 1036 ? HIS A 1043 ? THR A 1036 HIS A 1043 
K 4  VAL A 1006 ? THR A 1012 ? VAL A 1006 THR A 1012 
K 5  ASN A 1019 ? HIS A 1022 ? ASN A 1019 HIS A 1022 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1  2  N VAL A 43   ? N VAL A 43   O SER A 401  ? O SER A 401  
A 2  3  O LEU A 400  ? O LEU A 400  N LEU A 246  ? N LEU A 246  
A 3  4  N PHE A 245  ? N PHE A 245  O THR A 261  ? O THR A 261  
A 4  5  O HIS A 262  ? O HIS A 262  N MET A 224  ? N MET A 224  
A 5  6  O LEU A 225  ? O LEU A 225  N ALA A 202  ? N ALA A 202  
B 1  2  O LEU A 334  ? O LEU A 334  N LYS A 82   ? N LYS A 82   
B 2  3  N VAL A 85   ? N VAL A 85   O GLN A 375  ? O GLN A 375  
C 1  2  N PHE A 126  ? N PHE A 126  O GLU A 159  ? O GLU A 159  
D 1  2  N ARG A 410  ? N ARG A 410  O ASN A 413  ? O ASN A 413  
E 1  2  N THR A 525  ? N THR A 525  O ILE A 933  ? O ILE A 933  
E 2  3  O PHE A 932  ? O PHE A 932  N VAL A 556  ? N VAL A 556  
E 3  4  N VAL A 555  ? N VAL A 555  O TYR A 632  ? O TYR A 632  
E 4  5  O VAL A 633  ? O VAL A 633  N THR A 581  ? N THR A 581  
E 5  6  N VAL A 580  ? N VAL A 580  O VAL A 588  ? O VAL A 588  
F 1  2  N THR A 525  ? N THR A 525  O ILE A 933  ? O ILE A 933  
F 2  3  O PHE A 932  ? O PHE A 932  N VAL A 556  ? N VAL A 556  
F 3  4  N VAL A 555  ? N VAL A 555  O TYR A 632  ? O TYR A 632  
F 4  5  N LEU A 629  ? N LEU A 629  O PHE A 946  ? O PHE A 946  
G 1  2  N ILE A 543  ? N ILE A 543  O TYR A 572  ? O TYR A 572  
G 2  3  N GLN A 567  ? N GLN A 567  O ALA A 622  ? O ALA A 622  
G 3  4  O GLN A 610  ? O GLN A 610  N SER A 597  ? N SER A 597  
G 4  5  N VAL A 592  ? N VAL A 592  O SER A 645  ? O SER A 645  
H 1  2  O LYS A 669  ? O LYS A 669  N LEU A 651  ? N LEU A 651  
H 2  3  N LEU A 652  ? N LEU A 652  O VAL A 745  ? O VAL A 745  
H 3  4  N LEU A 746  ? N LEU A 746  O SER A 757  ? O SER A 757  
H 4  5  N SER A 754  ? N SER A 754  O MET A 769  ? O MET A 769  
H 5  6  N ILE A 768  ? N ILE A 768  O GLU A 775  ? O GLU A 775  
H 6  7  N VAL A 780  ? N VAL A 780  O VAL A 888  ? O VAL A 888  
H 7  8  O VAL A 895  ? O VAL A 895  N THR A 845  ? N THR A 845  
H 8  9  O LEU A 846  ? O LEU A 846  N MET A 835  ? N MET A 835  
H 9  10 O PHE A 836  ? O PHE A 836  N TYR A 805  ? N TYR A 805  
H 10 11 N PHE A 804  ? N PHE A 804  O ARG A 816  ? O ARG A 816  
H 11 12 N PHE A 813  ? N PHE A 813  O GLY A 912  ? O GLY A 912  
I 1  2  N ILE A 676  ? N ILE A 676  O PHE A 688  ? O PHE A 688  
I 2  3  N ALA A 687  ? N ALA A 687  O LYS A 695  ? O LYS A 695  
I 3  4  N ILE A 697  ? N ILE A 697  O VAL A 706  ? O VAL A 706  
I 4  5  N LYS A 714  ? N LYS A 714  O SER A 736  ? O SER A 736  
J 1  2  N ILE A 676  ? N ILE A 676  O PHE A 688  ? O PHE A 688  
J 2  3  N ALA A 687  ? N ALA A 687  O LYS A 695  ? O LYS A 695  
J 3  4  N ILE A 697  ? N ILE A 697  O VAL A 706  ? O VAL A 706  
J 4  5  N LYS A 711  ? N LYS A 711  O ARG A 793  ? O ARG A 793  
J 5  6  N ILE A 790  ? N ILE A 790  O GLN A 866  ? O GLN A 866  
J 6  7  O GLU A 863  ? O GLU A 863  N SER A 855  ? N SER A 855  
J 7  8  O GLY A 854  ? O GLY A 854  N TYR A 829  ? N TYR A 829  
K 1  2  N ARG A 963  ? N ARG A 963  O GLY A 976  ? O GLY A 976  
K 2  3  N TYR A 977  ? N TYR A 977  O TYR A 1039 ? O TYR A 1039 
K 3  4  O SER A 1042 ? O SER A 1042 N ARG A 1008 ? N ARG A 1008 
K 4  5  N ARG A 1011 ? N ARG A 1011 O LEU A 1020 ? O LEU A 1020 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 2  'BINDING SITE FOR RESIDUE NAG A 2001' 
AC2 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE ZN A 2004'  
AC3 Software ? ? ? ? 15 'BINDING SITE FOR RESIDUE FMF A 2003' 
AC4 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE MPD A 2002' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 2  ASN A 194 ? ASN A 194  . ? 1_555 ? 
2  AC1 2  HOH F .   ? HOH A 2914 . ? 1_555 ? 
3  AC2 5  HIS A 90  ? HIS A 90   . ? 1_555 ? 
4  AC2 5  ASP A 92  ? ASP A 92   . ? 1_555 ? 
5  AC2 5  ASP A 204 ? ASP A 204  . ? 1_555 ? 
6  AC2 5  HIS A 471 ? HIS A 471  . ? 1_555 ? 
7  AC2 5  FMF D .   ? FMF A 2003 . ? 1_555 ? 
8  AC3 15 HIS A 90  ? HIS A 90   . ? 1_555 ? 
9  AC3 15 ASP A 92  ? ASP A 92   . ? 1_555 ? 
10 AC3 15 TRP A 95  ? TRP A 95   . ? 1_555 ? 
11 AC3 15 ASP A 204 ? ASP A 204  . ? 1_555 ? 
12 AC3 15 ARG A 228 ? ARG A 228  . ? 1_555 ? 
13 AC3 15 TYR A 269 ? TYR A 269  . ? 1_555 ? 
14 AC3 15 TRP A 415 ? TRP A 415  . ? 1_555 ? 
15 AC3 15 HIS A 471 ? HIS A 471  . ? 1_555 ? 
16 AC3 15 ASP A 472 ? ASP A 472  . ? 1_555 ? 
17 AC3 15 TYR A 727 ? TYR A 727  . ? 1_555 ? 
18 AC3 15 ARG A 876 ? ARG A 876  . ? 1_555 ? 
19 AC3 15 ZN  C .   ? ZN  A 2004 . ? 1_555 ? 
20 AC3 15 HOH F .   ? HOH A 2876 . ? 1_555 ? 
21 AC3 15 HOH F .   ? HOH A 2895 . ? 1_555 ? 
22 AC3 15 HOH F .   ? HOH A 3046 . ? 1_555 ? 
23 AC4 7  LYS A 63  ? LYS A 63   . ? 1_555 ? 
24 AC4 7  GLN A 64  ? GLN A 64   . ? 1_555 ? 
25 AC4 7  HIS A 273 ? HIS A 273  . ? 1_555 ? 
26 AC4 7  HOH F .   ? HOH A 2152 . ? 1_555 ? 
27 AC4 7  HOH F .   ? HOH A 2622 . ? 1_555 ? 
28 AC4 7  HOH F .   ? HOH A 2693 . ? 1_555 ? 
29 AC4 7  HOH F .   ? HOH A 2844 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          1QX1 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    1QX1 
_atom_sites.fract_transf_matrix[1][1]   0.014483 
_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]   0.009105 
_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]   0.007199 
_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  
F  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . CYS A 1 31   ? 44.269 36.133  -19.178 1.00 27.01 ? 31   CYS A N   1 
ATOM   2    C  CA  . CYS A 1 31   ? 43.568 37.380  -18.707 1.00 21.20 ? 31   CYS A CA  1 
ATOM   3    C  C   . CYS A 1 31   ? 42.080 37.186  -18.792 1.00 21.87 ? 31   CYS A C   1 
ATOM   4    O  O   . CYS A 1 31   ? 41.594 36.645  -19.807 1.00 24.89 ? 31   CYS A O   1 
ATOM   5    C  CB  . CYS A 1 31   ? 43.868 38.556  -19.610 1.00 20.89 ? 31   CYS A CB  1 
ATOM   6    S  SG  . CYS A 1 31   ? 45.571 39.183  -19.580 1.00 25.51 ? 31   CYS A SG  1 
ATOM   7    N  N   . GLN A 1 32   ? 41.351 37.644  -17.784 1.00 19.48 ? 32   GLN A N   1 
ATOM   8    C  CA  . GLN A 1 32   ? 39.883 37.602  -17.781 1.00 19.86 ? 32   GLN A CA  1 
ATOM   9    C  C   . GLN A 1 32   ? 39.344 38.522  -18.872 1.00 16.99 ? 32   GLN A C   1 
ATOM   10   O  O   . GLN A 1 32   ? 39.916 39.594  -19.170 1.00 17.18 ? 32   GLN A O   1 
ATOM   11   C  CB  . GLN A 1 32   ? 39.286 38.194  -16.483 1.00 21.82 ? 32   GLN A CB  1 
ATOM   12   C  CG  . GLN A 1 32   ? 39.461 37.381  -15.212 1.00 27.73 ? 32   GLN A CG  1 
ATOM   13   C  CD  . GLN A 1 32   ? 38.379 37.714  -14.156 1.00 31.13 ? 32   GLN A CD  1 
ATOM   14   O  OE1 . GLN A 1 32   ? 37.266 37.207  -14.226 1.00 30.18 ? 32   GLN A OE1 1 
ATOM   15   N  NE2 . GLN A 1 32   ? 38.711 38.572  -13.179 1.00 30.10 ? 32   GLN A NE2 1 
ATOM   16   N  N   . ASP A 1 33   ? 38.216 38.142  -19.440 1.00 19.96 ? 33   ASP A N   1 
ATOM   17   C  CA  . ASP A 1 33   ? 37.569 38.950  -20.477 1.00 14.99 ? 33   ASP A CA  1 
ATOM   18   C  C   . ASP A 1 33   ? 36.648 39.931  -19.721 1.00 18.83 ? 33   ASP A C   1 
ATOM   19   O  O   . ASP A 1 33   ? 35.686 39.543  -19.080 1.00 21.14 ? 33   ASP A O   1 
ATOM   20   C  CB  . ASP A 1 33   ? 36.791 37.993  -21.417 1.00 16.75 ? 33   ASP A CB  1 
ATOM   21   C  CG  . ASP A 1 33   ? 36.087 38.683  -22.568 1.00 20.37 ? 33   ASP A CG  1 
ATOM   22   O  OD1 . ASP A 1 33   ? 35.901 38.001  -23.598 1.00 22.00 ? 33   ASP A OD1 1 
ATOM   23   O  OD2 . ASP A 1 33   ? 35.634 39.850  -22.472 1.00 19.28 ? 33   ASP A OD2 1 
ATOM   24   N  N   . VAL A 1 34   ? 36.918 41.220  -19.834 1.00 12.41 ? 34   VAL A N   1 
ATOM   25   C  CA  . VAL A 1 34   ? 36.160 42.213  -19.080 1.00 11.11 ? 34   VAL A CA  1 
ATOM   26   C  C   . VAL A 1 34   ? 34.953 42.771  -19.813 1.00 10.53 ? 34   VAL A C   1 
ATOM   27   O  O   . VAL A 1 34   ? 34.227 43.658  -19.319 1.00 10.67 ? 34   VAL A O   1 
ATOM   28   C  CB  . VAL A 1 34   ? 37.102 43.370  -18.597 1.00 12.14 ? 34   VAL A CB  1 
ATOM   29   C  CG1 . VAL A 1 34   ? 38.311 42.797  -17.836 1.00 13.44 ? 34   VAL A CG1 1 
ATOM   30   C  CG2 . VAL A 1 34   ? 37.566 44.211  -19.807 1.00 11.72 ? 34   VAL A CG2 1 
ATOM   31   N  N   . VAL A 1 35   ? 34.736 42.253  -21.031 1.00 11.17 ? 35   VAL A N   1 
ATOM   32   C  CA  . VAL A 1 35   ? 33.634 42.710  -21.862 1.00 11.11 ? 35   VAL A CA  1 
ATOM   33   C  C   . VAL A 1 35   ? 32.428 41.781  -22.053 1.00 10.88 ? 35   VAL A C   1 
ATOM   34   O  O   . VAL A 1 35   ? 31.295 42.189  -22.006 1.00 12.02 ? 35   VAL A O   1 
ATOM   35   C  CB  . VAL A 1 35   ? 34.165 43.030  -23.278 1.00 12.06 ? 35   VAL A CB  1 
ATOM   36   C  CG1 . VAL A 1 35   ? 33.030 43.499  -24.224 1.00 12.86 ? 35   VAL A CG1 1 
ATOM   37   C  CG2 . VAL A 1 35   ? 35.250 44.140  -23.174 1.00 12.62 ? 35   VAL A CG2 1 
ATOM   38   N  N   . GLN A 1 36   ? 32.770 40.522  -22.298 1.00 12.94 ? 36   GLN A N   1 
ATOM   39   C  CA  . GLN A 1 36   ? 31.775 39.521  -22.773 1.00 14.04 ? 36   GLN A CA  1 
ATOM   40   C  C   . GLN A 1 36   ? 31.125 38.612  -21.781 1.00 19.76 ? 36   GLN A C   1 
ATOM   41   O  O   . GLN A 1 36   ? 30.159 37.934  -22.126 1.00 23.65 ? 36   GLN A O   1 
ATOM   42   C  CB  . GLN A 1 36   ? 32.491 38.698  -23.851 1.00 12.60 ? 36   GLN A CB  1 
ATOM   43   C  CG  . GLN A 1 36   ? 33.060 39.558  -24.962 1.00 16.47 ? 36   GLN A CG  1 
ATOM   44   C  CD  . GLN A 1 36   ? 33.557 38.736  -26.141 1.00 15.06 ? 36   GLN A CD  1 
ATOM   45   O  OE1 . GLN A 1 36   ? 32.828 38.585  -27.132 1.00 18.96 ? 36   GLN A OE1 1 
ATOM   46   N  NE2 . GLN A 1 36   ? 34.755 38.235  -26.058 1.00 16.30 ? 36   GLN A NE2 1 
ATOM   47   N  N   . ASP A 1 37   ? 31.621 38.568  -20.557 1.00 17.69 ? 37   ASP A N   1 
ATOM   48   C  CA  . ASP A 1 37   ? 31.087 37.706  -19.498 1.00 18.41 ? 37   ASP A CA  1 
ATOM   49   C  C   . ASP A 1 37   ? 30.443 38.546  -18.378 1.00 16.31 ? 37   ASP A C   1 
ATOM   50   O  O   . ASP A 1 37   ? 31.197 39.179  -17.584 1.00 24.21 ? 37   ASP A O   1 
ATOM   51   C  CB  . ASP A 1 37   ? 32.247 36.866  -18.879 1.00 23.75 ? 37   ASP A CB  1 
ATOM   52   C  CG  . ASP A 1 37   ? 32.908 35.900  -19.874 1.00 28.85 ? 37   ASP A CG  1 
ATOM   53   O  OD1 . ASP A 1 37   ? 32.171 35.281  -20.657 1.00 30.22 ? 37   ASP A OD1 1 
ATOM   54   O  OD2 . ASP A 1 37   ? 34.165 35.771  -19.843 1.00 27.76 ? 37   ASP A OD2 1 
ATOM   55   N  N   . VAL A 1 38   ? 29.121 38.546  -18.293 1.00 15.77 ? 38   VAL A N   1 
ATOM   56   C  CA  . VAL A 1 38   ? 28.445 39.307  -17.243 1.00 14.39 ? 38   VAL A CA  1 
ATOM   57   C  C   . VAL A 1 38   ? 28.631 38.578  -15.901 1.00 16.52 ? 38   VAL A C   1 
ATOM   58   O  O   . VAL A 1 38   ? 28.195 37.422  -15.737 1.00 16.43 ? 38   VAL A O   1 
ATOM   59   C  CB  . VAL A 1 38   ? 26.943 39.439  -17.542 1.00 15.25 ? 38   VAL A CB  1 
ATOM   60   C  CG1 . VAL A 1 38   ? 26.233 40.190  -16.435 1.00 17.12 ? 38   VAL A CG1 1 
ATOM   61   C  CG2 . VAL A 1 38   ? 26.747 40.107  -18.943 1.00 16.36 ? 38   VAL A CG2 1 
ATOM   62   N  N   . PRO A 1 39   ? 29.267 39.229  -14.900 1.00 13.54 ? 39   PRO A N   1 
ATOM   63   C  CA  . PRO A 1 39   ? 29.451 38.539  -13.613 1.00 14.06 ? 39   PRO A CA  1 
ATOM   64   C  C   . PRO A 1 39   ? 28.159 38.180  -12.967 1.00 13.51 ? 39   PRO A C   1 
ATOM   65   O  O   . PRO A 1 39   ? 27.155 38.892  -13.031 1.00 14.03 ? 39   PRO A O   1 
ATOM   66   C  CB  . PRO A 1 39   ? 30.219 39.570  -12.765 1.00 14.36 ? 39   PRO A CB  1 
ATOM   67   C  CG  . PRO A 1 39   ? 31.018 40.362  -13.840 1.00 12.43 ? 39   PRO A CG  1 
ATOM   68   C  CD  . PRO A 1 39   ? 29.971 40.547  -14.915 1.00 14.28 ? 39   PRO A CD  1 
ATOM   69   N  N   . ASN A 1 40   ? 28.175 37.004  -12.312 1.00 14.27 ? 40   ASN A N   1 
ATOM   70   C  CA  . ASN A 1 40   ? 27.001 36.593  -11.561 1.00 16.37 ? 40   ASN A CA  1 
ATOM   71   C  C   . ASN A 1 40   ? 27.224 36.970  -10.081 1.00 15.75 ? 40   ASN A C   1 
ATOM   72   O  O   . ASN A 1 40   ? 28.090 36.375  -9.402  1.00 17.45 ? 40   ASN A O   1 
ATOM   73   C  CB  . ASN A 1 40   ? 26.805 35.065  -11.741 1.00 22.66 ? 40   ASN A CB  1 
ATOM   74   C  CG  . ASN A 1 40   ? 25.751 34.508  -10.827 1.00 28.89 ? 40   ASN A CG  1 
ATOM   75   O  OD1 . ASN A 1 40   ? 24.713 35.130  -10.594 1.00 32.86 ? 40   ASN A OD1 1 
ATOM   76   N  ND2 . ASN A 1 40   ? 26.020 33.321  -10.273 1.00 35.19 ? 40   ASN A ND2 1 
ATOM   77   N  N   . VAL A 1 41   ? 26.501 37.972  -9.606  1.00 12.70 ? 41   VAL A N   1 
ATOM   78   C  CA  . VAL A 1 41   ? 26.669 38.424  -8.206  1.00 11.91 ? 41   VAL A CA  1 
ATOM   79   C  C   . VAL A 1 41   ? 25.329 38.427  -7.512  1.00 12.93 ? 41   VAL A C   1 
ATOM   80   O  O   . VAL A 1 41   ? 24.277 38.572  -8.132  1.00 14.45 ? 41   VAL A O   1 
ATOM   81   C  CB  . VAL A 1 41   ? 27.288 39.871  -8.133  1.00 11.43 ? 41   VAL A CB  1 
ATOM   82   C  CG1 . VAL A 1 41   ? 28.730 39.807  -8.601  1.00 11.96 ? 41   VAL A CG1 1 
ATOM   83   C  CG2 . VAL A 1 41   ? 26.448 40.879  -9.016  1.00 12.29 ? 41   VAL A CG2 1 
ATOM   84   N  N   . ASP A 1 42   ? 25.293 38.317  -6.189  1.00 11.23 ? 42   ASP A N   1 
ATOM   85   C  CA  . ASP A 1 42   ? 24.023 38.344  -5.485  1.00 11.15 ? 42   ASP A CA  1 
ATOM   86   C  C   . ASP A 1 42   ? 23.327 39.680  -5.501  1.00 11.41 ? 42   ASP A C   1 
ATOM   87   O  O   . ASP A 1 42   ? 22.076 39.804  -5.500  1.00 13.07 ? 42   ASP A O   1 
ATOM   88   C  CB  . ASP A 1 42   ? 24.228 37.915  -4.019  1.00 12.22 ? 42   ASP A CB  1 
ATOM   89   C  CG  . ASP A 1 42   ? 24.761 36.509  -3.908  1.00 17.32 ? 42   ASP A CG  1 
ATOM   90   O  OD1 . ASP A 1 42   ? 24.081 35.571  -4.451  1.00 19.03 ? 42   ASP A OD1 1 
ATOM   91   O  OD2 . ASP A 1 42   ? 25.849 36.243  -3.335  1.00 14.88 ? 42   ASP A OD2 1 
ATOM   92   N  N   . VAL A 1 43   ? 24.124 40.754  -5.431  1.00 10.31 ? 43   VAL A N   1 
ATOM   93   C  CA  . VAL A 1 43   ? 23.579 42.131  -5.433  1.00 11.38 ? 43   VAL A CA  1 
ATOM   94   C  C   . VAL A 1 43   ? 24.341 42.926  -6.499  1.00 10.03 ? 43   VAL A C   1 
ATOM   95   O  O   . VAL A 1 43   ? 25.595 43.004  -6.442  1.00 10.68 ? 43   VAL A O   1 
ATOM   96   C  CB  . VAL A 1 43   ? 23.794 42.858  -4.071  1.00 10.74 ? 43   VAL A CB  1 
ATOM   97   C  CG1 . VAL A 1 43   ? 23.186 44.288  -4.148  1.00 12.66 ? 43   VAL A CG1 1 
ATOM   98   C  CG2 . VAL A 1 43   ? 23.098 42.055  -2.929  1.00 14.50 ? 43   VAL A CG2 1 
ATOM   99   N  N   . GLN A 1 44   ? 23.642 43.426  -7.506  1.00 8.87  ? 44   GLN A N   1 
ATOM   100  C  CA  . GLN A 1 44   ? 24.276 44.276  -8.538  1.00 9.20  ? 44   GLN A CA  1 
ATOM   101  C  C   . GLN A 1 44   ? 23.549 45.588  -8.393  1.00 9.60  ? 44   GLN A C   1 
ATOM   102  O  O   . GLN A 1 44   ? 22.318 45.667  -8.539  1.00 9.65  ? 44   GLN A O   1 
ATOM   103  C  CB  . GLN A 1 44   ? 24.109 43.619  -9.935  1.00 9.97  ? 44   GLN A CB  1 
ATOM   104  C  CG  . GLN A 1 44   ? 25.212 44.058  -10.885 1.00 9.24  ? 44   GLN A CG  1 
ATOM   105  C  CD  . GLN A 1 44   ? 25.271 45.566  -11.034 1.00 10.20 ? 44   GLN A CD  1 
ATOM   106  O  OE1 . GLN A 1 44   ? 24.270 46.194  -11.370 1.00 10.48 ? 44   GLN A OE1 1 
ATOM   107  N  NE2 . GLN A 1 44   ? 26.452 46.161  -10.736 1.00 9.36  ? 44   GLN A NE2 1 
ATOM   108  N  N   . MET A 1 45   ? 24.268 46.665  -8.021  1.00 8.75  ? 45   MET A N   1 
ATOM   109  C  CA  . MET A 1 45   ? 23.565 47.892  -7.632  1.00 8.39  ? 45   MET A CA  1 
ATOM   110  C  C   . MET A 1 45   ? 22.672 48.538  -8.686  1.00 8.67  ? 45   MET A C   1 
ATOM   111  O  O   . MET A 1 45   ? 21.685 49.150  -8.288  1.00 9.58  ? 45   MET A O   1 
ATOM   112  C  CB  . MET A 1 45   ? 24.564 48.936  -7.033  1.00 8.90  ? 45   MET A CB  1 
ATOM   113  C  CG  . MET A 1 45   ? 25.220 48.461  -5.715  1.00 9.29  ? 45   MET A CG  1 
ATOM   114  S  SD  . MET A 1 45   ? 24.005 48.133  -4.423  1.00 11.75 ? 45   MET A SD  1 
ATOM   115  C  CE  . MET A 1 45   ? 23.291 49.822  -4.279  1.00 13.59 ? 45   MET A CE  1 
ATOM   116  N  N   . LEU A 1 46   ? 23.032 48.419  -9.952  1.00 9.06  ? 46   LEU A N   1 
ATOM   117  C  CA  . LEU A 1 46   ? 22.156 49.026  -10.981 1.00 8.19  ? 46   LEU A CA  1 
ATOM   118  C  C   . LEU A 1 46   ? 20.818 48.240  -11.026 1.00 10.44 ? 46   LEU A C   1 
ATOM   119  O  O   . LEU A 1 46   ? 19.762 48.840  -11.154 1.00 10.92 ? 46   LEU A O   1 
ATOM   120  C  CB  . LEU A 1 46   ? 22.858 48.998  -12.322 1.00 11.22 ? 46   LEU A CB  1 
ATOM   121  C  CG  . LEU A 1 46   ? 22.065 49.710  -13.429 1.00 9.99  ? 46   LEU A CG  1 
ATOM   122  C  CD1 . LEU A 1 46   ? 22.096 51.262  -13.211 1.00 12.13 ? 46   LEU A CD1 1 
ATOM   123  C  CD2 . LEU A 1 46   ? 22.661 49.425  -14.786 1.00 13.58 ? 46   LEU A CD2 1 
ATOM   124  N  N   . GLU A 1 47   ? 20.893 46.926  -10.869 1.00 10.09 ? 47   GLU A N   1 
ATOM   125  C  CA  . GLU A 1 47   ? 19.711 46.068  -10.920 1.00 12.19 ? 47   GLU A CA  1 
ATOM   126  C  C   . GLU A 1 47   ? 18.914 46.343  -9.668  1.00 11.66 ? 47   GLU A C   1 
ATOM   127  O  O   . GLU A 1 47   ? 17.659 46.488  -9.701  1.00 12.79 ? 47   GLU A O   1 
ATOM   128  C  CB  . GLU A 1 47   ? 20.140 44.624  -11.005 1.00 13.18 ? 47   GLU A CB  1 
ATOM   129  C  CG  . GLU A 1 47   ? 18.929 43.652  -11.238 1.00 17.47 ? 47   GLU A CG  1 
ATOM   130  C  CD  . GLU A 1 47   ? 18.143 43.302  -9.978  1.00 25.69 ? 47   GLU A CD  1 
ATOM   131  O  OE1 . GLU A 1 47   ? 18.652 43.424  -8.850  1.00 20.21 ? 47   GLU A OE1 1 
ATOM   132  O  OE2 . GLU A 1 47   ? 16.950 42.859  -10.096 1.00 27.63 ? 47   GLU A OE2 1 
ATOM   133  N  N   . LEU A 1 48   ? 19.578 46.503  -8.514  1.00 11.11 ? 48   LEU A N   1 
ATOM   134  C  CA  . LEU A 1 48   ? 18.858 46.814  -7.311  1.00 11.08 ? 48   LEU A CA  1 
ATOM   135  C  C   . LEU A 1 48   ? 18.112 48.120  -7.414  1.00 11.04 ? 48   LEU A C   1 
ATOM   136  O  O   . LEU A 1 48   ? 16.921 48.237  -7.034  1.00 13.67 ? 48   LEU A O   1 
ATOM   137  C  CB  . LEU A 1 48   ? 19.837 46.839  -6.114  1.00 12.85 ? 48   LEU A CB  1 
ATOM   138  C  CG  . LEU A 1 48   ? 19.196 47.068  -4.746  1.00 13.54 ? 48   LEU A CG  1 
ATOM   139  C  CD1 . LEU A 1 48   ? 18.127 45.987  -4.466  1.00 20.99 ? 48   LEU A CD1 1 
ATOM   140  C  CD2 . LEU A 1 48   ? 20.254 47.108  -3.637  1.00 18.95 ? 48   LEU A CD2 1 
ATOM   141  N  N   . TYR A 1 49   ? 18.789 49.160  -7.937  1.00 10.57 ? 49   TYR A N   1 
ATOM   142  C  CA  . TYR A 1 49   ? 18.142 50.462  -8.127  1.00 11.04 ? 49   TYR A CA  1 
ATOM   143  C  C   . TYR A 1 49   ? 16.886 50.390  -9.038  1.00 11.59 ? 49   TYR A C   1 
ATOM   144  O  O   . TYR A 1 49   ? 15.920 51.092  -8.784  1.00 12.62 ? 49   TYR A O   1 
ATOM   145  C  CB  . TYR A 1 49   ? 19.164 51.455  -8.755  1.00 10.03 ? 49   TYR A CB  1 
ATOM   146  C  CG  . TYR A 1 49   ? 19.775 52.367  -7.714  1.00 11.09 ? 49   TYR A CG  1 
ATOM   147  C  CD1 . TYR A 1 49   ? 20.240 51.875  -6.454  1.00 10.33 ? 49   TYR A CD1 1 
ATOM   148  C  CD2 . TYR A 1 49   ? 19.809 53.723  -7.952  1.00 11.31 ? 49   TYR A CD2 1 
ATOM   149  C  CE1 . TYR A 1 49   ? 20.677 52.720  -5.468  1.00 11.01 ? 49   TYR A CE1 1 
ATOM   150  C  CE2 . TYR A 1 49   ? 20.261 54.619  -6.951  1.00 11.48 ? 49   TYR A CE2 1 
ATOM   151  C  CZ  . TYR A 1 49   ? 20.675 54.102  -5.701  1.00 9.23  ? 49   TYR A CZ  1 
ATOM   152  O  OH  . TYR A 1 49   ? 21.034 54.917  -4.694  1.00 10.71 ? 49   TYR A OH  1 
ATOM   153  N  N   . ASP A 1 50   ? 16.949 49.523  -10.048 1.00 11.59 ? 50   ASP A N   1 
ATOM   154  C  CA  . ASP A 1 50   ? 15.827 49.425  -10.988 1.00 15.14 ? 50   ASP A CA  1 
ATOM   155  C  C   . ASP A 1 50   ? 14.618 48.857  -10.254 1.00 16.50 ? 50   ASP A C   1 
ATOM   156  O  O   . ASP A 1 50   ? 13.446 49.284  -10.541 1.00 16.18 ? 50   ASP A O   1 
ATOM   157  C  CB  . ASP A 1 50   ? 16.256 48.514  -12.129 1.00 15.68 ? 50   ASP A CB  1 
ATOM   158  C  CG  . ASP A 1 50   ? 15.456 48.728  -13.395 1.00 23.55 ? 50   ASP A CG  1 
ATOM   159  O  OD1 . ASP A 1 50   ? 15.551 47.837  -14.271 1.00 27.98 ? 50   ASP A OD1 1 
ATOM   160  O  OD2 . ASP A 1 50   ? 14.794 49.773  -13.523 1.00 24.33 ? 50   ASP A OD2 1 
ATOM   161  N  N   . ARG A 1 51   ? 14.862 47.927  -9.328  1.00 15.80 ? 51   ARG A N   1 
ATOM   162  C  CA  . ARG A 1 51   ? 13.753 47.297  -8.608  1.00 16.78 ? 51   ARG A CA  1 
ATOM   163  C  C   . ARG A 1 51   ? 13.263 47.977  -7.343  1.00 17.35 ? 51   ARG A C   1 
ATOM   164  O  O   . ARG A 1 51   ? 12.081 47.890  -6.991  1.00 19.50 ? 51   ARG A O   1 
ATOM   165  C  CB  . ARG A 1 51   ? 14.057 45.782  -8.395  1.00 23.94 ? 51   ARG A CB  1 
ATOM   166  C  CG  . ARG A 1 51   ? 15.242 45.370  -7.588  1.00 30.80 ? 51   ARG A CG  1 
ATOM   167  C  CD  . ARG A 1 51   ? 15.251 43.830  -7.412  1.00 34.22 ? 51   ARG A CD  1 
ATOM   168  N  NE  . ARG A 1 51   ? 15.940 43.528  -6.167  1.00 39.05 ? 51   ARG A NE  1 
ATOM   169  C  CZ  . ARG A 1 51   ? 17.128 42.956  -6.111  1.00 38.17 ? 51   ARG A CZ  1 
ATOM   170  N  NH1 . ARG A 1 51   ? 17.724 42.614  -7.235  1.00 42.66 ? 51   ARG A NH1 1 
ATOM   171  N  NH2 . ARG A 1 51   ? 17.734 42.763  -4.946  1.00 43.50 ? 51   ARG A NH2 1 
ATOM   172  N  N   . MET A 1 52   ? 14.111 48.701  -6.632  1.00 16.45 ? 52   MET A N   1 
ATOM   173  C  CA  . MET A 1 52   ? 13.718 49.399  -5.406  1.00 17.58 ? 52   MET A CA  1 
ATOM   174  C  C   . MET A 1 52   ? 12.714 50.520  -5.605  1.00 15.57 ? 52   MET A C   1 
ATOM   175  O  O   . MET A 1 52   ? 12.803 51.246  -6.615  1.00 17.34 ? 52   MET A O   1 
ATOM   176  C  CB  . MET A 1 52   ? 14.944 50.100  -4.776  1.00 16.68 ? 52   MET A CB  1 
ATOM   177  C  CG  . MET A 1 52   ? 15.886 49.149  -4.146  1.00 15.49 ? 52   MET A CG  1 
ATOM   178  S  SD  . MET A 1 52   ? 17.530 50.017  -3.679  1.00 20.86 ? 52   MET A SD  1 
ATOM   179  C  CE  . MET A 1 52   ? 16.952 51.361  -2.655  1.00 17.61 ? 52   MET A CE  1 
ATOM   180  N  N   A SER A 1 53   ? 11.846 50.755  -4.601  0.50 16.91 ? 53   SER A N   1 
ATOM   181  N  N   B SER A 1 53   ? 11.846 50.755  -4.601  0.50 17.36 ? 53   SER A N   1 
ATOM   182  C  CA  A SER A 1 53   ? 10.840 51.839  -4.702  0.50 18.17 ? 53   SER A CA  1 
ATOM   183  C  CA  B SER A 1 53   ? 10.840 51.839  -4.702  0.50 19.18 ? 53   SER A CA  1 
ATOM   184  C  C   A SER A 1 53   ? 11.272 53.172  -4.069  0.50 16.34 ? 53   SER A C   1 
ATOM   185  C  C   B SER A 1 53   ? 11.272 53.172  -4.069  0.50 16.86 ? 53   SER A C   1 
ATOM   186  O  O   A SER A 1 53   ? 10.671 54.225  -4.303  0.50 17.62 ? 53   SER A O   1 
ATOM   187  O  O   B SER A 1 53   ? 10.671 54.225  -4.303  0.50 18.16 ? 53   SER A O   1 
ATOM   188  C  CB  A SER A 1 53   ? 9.528  51.344  -4.070  0.50 18.69 ? 53   SER A CB  1 
ATOM   189  C  CB  B SER A 1 53   ? 9.528  51.344  -4.070  0.50 20.32 ? 53   SER A CB  1 
ATOM   190  O  OG  A SER A 1 53   ? 9.101  50.231  -4.847  0.50 19.47 ? 53   SER A OG  1 
ATOM   191  O  OG  B SER A 1 53   ? 9.639  51.582  -2.672  0.50 26.25 ? 53   SER A OG  1 
ATOM   192  N  N   . PHE A 1 54   ? 12.257 53.116  -3.181  1.00 16.80 ? 54   PHE A N   1 
ATOM   193  C  CA  . PHE A 1 54   ? 12.799 54.308  -2.520  1.00 14.28 ? 54   PHE A CA  1 
ATOM   194  C  C   . PHE A 1 54   ? 11.765 55.083  -1.726  1.00 16.54 ? 54   PHE A C   1 
ATOM   195  O  O   . PHE A 1 54   ? 11.848 56.311  -1.583  1.00 17.05 ? 54   PHE A O   1 
ATOM   196  C  CB  . PHE A 1 54   ? 13.473 55.277  -3.539  1.00 15.12 ? 54   PHE A CB  1 
ATOM   197  C  CG  . PHE A 1 54   ? 14.728 54.722  -4.209  1.00 13.35 ? 54   PHE A CG  1 
ATOM   198  C  CD1 . PHE A 1 54   ? 14.654 53.893  -5.321  1.00 12.98 ? 54   PHE A CD1 1 
ATOM   199  C  CD2 . PHE A 1 54   ? 15.972 55.070  -3.700  1.00 12.42 ? 54   PHE A CD2 1 
ATOM   200  C  CE1 . PHE A 1 54   ? 15.814 53.396  -5.946  1.00 13.24 ? 54   PHE A CE1 1 
ATOM   201  C  CE2 . PHE A 1 54   ? 17.139 54.600  -4.314  1.00 13.44 ? 54   PHE A CE2 1 
ATOM   202  C  CZ  . PHE A 1 54   ? 17.069 53.761  -5.436  1.00 13.93 ? 54   PHE A CZ  1 
ATOM   203  N  N   . LYS A 1 55   ? 10.745 54.396  -1.194  1.00 15.01 ? 55   LYS A N   1 
ATOM   204  C  CA  . LYS A 1 55   ? 9.757  55.143  -0.384  1.00 17.44 ? 55   LYS A CA  1 
ATOM   205  C  C   . LYS A 1 55   ? 10.339 55.593  0.936   1.00 17.69 ? 55   LYS A C   1 
ATOM   206  O  O   . LYS A 1 55   ? 11.019 54.843  1.611   1.00 19.83 ? 55   LYS A O   1 
ATOM   207  C  CB  . LYS A 1 55   ? 8.502  54.276  -0.093  1.00 19.21 ? 55   LYS A CB  1 
ATOM   208  C  CG  . LYS A 1 55   ? 7.777  53.845  -1.346  1.00 20.96 ? 55   LYS A CG  1 
ATOM   209  C  CD  . LYS A 1 55   ? 7.531  55.000  -2.342  1.00 19.26 ? 55   LYS A CD  1 
ATOM   210  C  CE  . LYS A 1 55   ? 6.643  54.528  -3.526  1.00 23.57 ? 55   LYS A CE  1 
ATOM   211  N  NZ  . LYS A 1 55   ? 6.457  55.587  -4.588  1.00 23.18 ? 55   LYS A NZ  1 
ATOM   212  N  N   . ASP A 1 56   ? 10.080 56.825  1.320   1.00 15.89 ? 56   ASP A N   1 
ATOM   213  C  CA  . ASP A 1 56   ? 10.588 57.412  2.519   1.00 15.26 ? 56   ASP A CA  1 
ATOM   214  C  C   . ASP A 1 56   ? 9.516  57.367  3.627   1.00 18.29 ? 56   ASP A C   1 
ATOM   215  O  O   . ASP A 1 56   ? 8.926  58.390  3.987   1.00 20.44 ? 56   ASP A O   1 
ATOM   216  C  CB  . ASP A 1 56   ? 11.031 58.851  2.201   1.00 16.45 ? 56   ASP A CB  1 
ATOM   217  C  CG  . ASP A 1 56   ? 11.728 59.521  3.363   1.00 16.78 ? 56   ASP A CG  1 
ATOM   218  O  OD1 . ASP A 1 56   ? 12.221 58.829  4.288   1.00 16.69 ? 56   ASP A OD1 1 
ATOM   219  O  OD2 . ASP A 1 56   ? 11.787 60.767  3.398   1.00 20.12 ? 56   ASP A OD2 1 
ATOM   220  N  N   . ILE A 1 57   ? 9.314  56.201  4.197   1.00 19.19 ? 57   ILE A N   1 
ATOM   221  C  CA  . ILE A 1 57   ? 8.298  56.115  5.225   1.00 22.02 ? 57   ILE A CA  1 
ATOM   222  C  C   . ILE A 1 57   ? 8.890  56.120  6.598   1.00 20.83 ? 57   ILE A C   1 
ATOM   223  O  O   . ILE A 1 57   ? 10.042 55.764  6.819   1.00 21.50 ? 57   ILE A O   1 
ATOM   224  C  CB  . ILE A 1 57   ? 7.315  54.899  4.994   1.00 28.87 ? 57   ILE A CB  1 
ATOM   225  C  CG1 . ILE A 1 57   ? 7.712  53.711  5.818   1.00 29.88 ? 57   ILE A CG1 1 
ATOM   226  C  CG2 . ILE A 1 57   ? 7.177  54.549  3.519   1.00 31.05 ? 57   ILE A CG2 1 
ATOM   227  C  CD1 . ILE A 1 57   ? 6.978  53.722  7.109   1.00 36.02 ? 57   ILE A CD1 1 
ATOM   228  N  N   . ASP A 1 58   ? 8.093  56.561  7.557   1.00 21.44 ? 58   ASP A N   1 
ATOM   229  C  CA  . ASP A 1 58   ? 8.504  56.649  8.941   1.00 19.82 ? 58   ASP A CA  1 
ATOM   230  C  C   . ASP A 1 58   ? 8.532  55.241  9.518   1.00 20.69 ? 58   ASP A C   1 
ATOM   231  O  O   . ASP A 1 58   ? 7.490  54.605  9.686   1.00 21.98 ? 58   ASP A O   1 
ATOM   232  C  CB  . ASP A 1 58   ? 7.505  57.519  9.685   1.00 20.47 ? 58   ASP A CB  1 
ATOM   233  C  CG  . ASP A 1 58   ? 7.889  57.781  11.109  1.00 25.77 ? 58   ASP A CG  1 
ATOM   234  O  OD1 . ASP A 1 58   ? 7.317  58.735  11.692  1.00 31.45 ? 58   ASP A OD1 1 
ATOM   235  O  OD2 . ASP A 1 58   ? 8.741  57.073  11.692  1.00 22.84 ? 58   ASP A OD2 1 
ATOM   236  N  N   . GLY A 1 59   ? 9.730  54.729  9.788   1.00 17.31 ? 59   GLY A N   1 
ATOM   237  C  CA  . GLY A 1 59   ? 9.841  53.393  10.314  1.00 16.82 ? 59   GLY A CA  1 
ATOM   238  C  C   . GLY A 1 59   ? 9.750  53.287  11.826  1.00 14.48 ? 59   GLY A C   1 
ATOM   239  O  O   . GLY A 1 59   ? 9.973  52.186  12.316  1.00 16.84 ? 59   GLY A O   1 
ATOM   240  N  N   . GLY A 1 60   ? 9.493  54.380  12.516  1.00 15.81 ? 60   GLY A N   1 
ATOM   241  C  CA  . GLY A 1 60   ? 9.425  54.305  13.964  1.00 17.41 ? 60   GLY A CA  1 
ATOM   242  C  C   . GLY A 1 60   ? 10.694 54.931  14.566  1.00 16.47 ? 60   GLY A C   1 
ATOM   243  O  O   . GLY A 1 60   ? 11.208 55.924  14.021  1.00 18.26 ? 60   GLY A O   1 
ATOM   244  N  N   . VAL A 1 61   ? 11.192 54.405  15.687  1.00 15.47 ? 61   VAL A N   1 
ATOM   245  C  CA  . VAL A 1 61   ? 12.376 54.998  16.304  1.00 15.11 ? 61   VAL A CA  1 
ATOM   246  C  C   . VAL A 1 61   ? 13.552 54.888  15.296  1.00 13.16 ? 61   VAL A C   1 
ATOM   247  O  O   . VAL A 1 61   ? 14.389 55.826  15.265  1.00 14.98 ? 61   VAL A O   1 
ATOM   248  C  CB  . VAL A 1 61   ? 12.754 54.386  17.665  1.00 14.76 ? 61   VAL A CB  1 
ATOM   249  C  CG1 . VAL A 1 61   ? 11.650 54.766  18.712  1.00 18.47 ? 61   VAL A CG1 1 
ATOM   250  C  CG2 . VAL A 1 61   ? 12.967 52.876  17.595  1.00 15.73 ? 61   VAL A CG2 1 
ATOM   251  N  N   . TRP A 1 62   ? 13.630 53.817  14.533  1.00 13.20 ? 62   TRP A N   1 
ATOM   252  C  CA  . TRP A 1 62   ? 14.641 53.735  13.452  1.00 11.55 ? 62   TRP A CA  1 
ATOM   253  C  C   . TRP A 1 62   ? 13.831 54.404  12.338  1.00 14.36 ? 62   TRP A C   1 
ATOM   254  O  O   . TRP A 1 62   ? 13.052 53.754  11.612  1.00 13.46 ? 62   TRP A O   1 
ATOM   255  C  CB  . TRP A 1 62   ? 14.984 52.290  13.125  1.00 12.09 ? 62   TRP A CB  1 
ATOM   256  C  CG  . TRP A 1 62   ? 15.999 52.186  12.011  1.00 9.78  ? 62   TRP A CG  1 
ATOM   257  C  CD1 . TRP A 1 62   ? 16.672 53.248  11.393  1.00 10.82 ? 62   TRP A CD1 1 
ATOM   258  C  CD2 . TRP A 1 62   ? 16.372 51.011  11.324  1.00 10.75 ? 62   TRP A CD2 1 
ATOM   259  N  NE1 . TRP A 1 62   ? 17.411 52.752  10.362  1.00 10.43 ? 62   TRP A NE1 1 
ATOM   260  C  CE2 . TRP A 1 62   ? 17.269 51.399  10.277  1.00 11.61 ? 62   TRP A CE2 1 
ATOM   261  C  CE3 . TRP A 1 62   ? 16.025 49.653  11.458  1.00 10.39 ? 62   TRP A CE3 1 
ATOM   262  C  CZ2 . TRP A 1 62   ? 17.829 50.495  9.368   1.00 11.56 ? 62   TRP A CZ2 1 
ATOM   263  C  CZ3 . TRP A 1 62   ? 16.575 48.731  10.550  1.00 11.58 ? 62   TRP A CZ3 1 
ATOM   264  C  CH2 . TRP A 1 62   ? 17.472 49.150  9.511   1.00 12.27 ? 62   TRP A CH2 1 
ATOM   265  N  N   . LYS A 1 63   ? 14.052 55.704  12.145  1.00 13.43 ? 63   LYS A N   1 
ATOM   266  C  CA  . LYS A 1 63   ? 13.182 56.452  11.225  1.00 13.66 ? 63   LYS A CA  1 
ATOM   267  C  C   . LYS A 1 63   ? 13.185 55.990  9.810   1.00 15.31 ? 63   LYS A C   1 
ATOM   268  O  O   . LYS A 1 63   ? 12.185 56.112  9.120   1.00 15.73 ? 63   LYS A O   1 
ATOM   269  C  CB  . LYS A 1 63   ? 13.529 57.946  11.273  1.00 14.63 ? 63   LYS A CB  1 
ATOM   270  C  CG  . LYS A 1 63   ? 13.197 58.666  12.628  1.00 22.16 ? 63   LYS A CG  1 
ATOM   271  C  CD  . LYS A 1 63   ? 11.672 58.964  12.792  1.00 26.85 ? 63   LYS A CD  1 
ATOM   272  C  CE  . LYS A 1 63   ? 11.267 59.617  14.153  1.00 32.90 ? 63   LYS A CE  1 
ATOM   273  N  NZ  . LYS A 1 63   ? 11.388 58.907  15.539  1.00 32.55 ? 63   LYS A NZ  1 
ATOM   274  N  N   . GLN A 1 64   ? 14.316 55.456  9.332   1.00 13.25 ? 64   GLN A N   1 
ATOM   275  C  CA  . GLN A 1 64   ? 14.389 55.013  7.961   1.00 12.73 ? 64   GLN A CA  1 
ATOM   276  C  C   . GLN A 1 64   ? 14.472 53.500  7.811   1.00 12.16 ? 64   GLN A C   1 
ATOM   277  O  O   . GLN A 1 64   ? 14.805 52.984  6.731   1.00 11.74 ? 64   GLN A O   1 
ATOM   278  C  CB  . GLN A 1 64   ? 15.596 55.694  7.282   1.00 12.95 ? 64   GLN A CB  1 
ATOM   279  C  CG  . GLN A 1 64   ? 15.484 57.217  7.318   1.00 12.43 ? 64   GLN A CG  1 
ATOM   280  C  CD  . GLN A 1 64   ? 16.862 57.886  7.163   1.00 12.07 ? 64   GLN A CD  1 
ATOM   281  O  OE1 . GLN A 1 64   ? 17.826 57.524  7.881   1.00 12.95 ? 64   GLN A OE1 1 
ATOM   282  N  NE2 . GLN A 1 64   ? 16.949 58.848  6.243   1.00 12.09 ? 64   GLN A NE2 1 
ATOM   283  N  N   . GLY A 1 65   ? 14.076 52.797  8.897   1.00 13.08 ? 65   GLY A N   1 
ATOM   284  C  CA  . GLY A 1 65   ? 14.056 51.326  8.878   1.00 13.69 ? 65   GLY A CA  1 
ATOM   285  C  C   . GLY A 1 65   ? 12.684 50.765  9.288   1.00 14.42 ? 65   GLY A C   1 
ATOM   286  O  O   . GLY A 1 65   ? 11.665 51.172  8.682   1.00 14.31 ? 65   GLY A O   1 
ATOM   287  N  N   . TRP A 1 66   ? 12.684 49.872  10.273  1.00 15.36 ? 66   TRP A N   1 
ATOM   288  C  CA  . TRP A 1 66   ? 11.410 49.253  10.771  1.00 14.43 ? 66   TRP A CA  1 
ATOM   289  C  C   . TRP A 1 66   ? 11.706 48.896  12.202  1.00 14.80 ? 66   TRP A C   1 
ATOM   290  O  O   . TRP A 1 66   ? 12.829 49.056  12.694  1.00 14.17 ? 66   TRP A O   1 
ATOM   291  C  CB  . TRP A 1 66   ? 11.043 48.018  9.920   1.00 13.48 ? 66   TRP A CB  1 
ATOM   292  C  CG  . TRP A 1 66   ? 12.021 46.885  10.103  1.00 13.97 ? 66   TRP A CG  1 
ATOM   293  C  CD1 . TRP A 1 66   ? 11.912 45.841  10.972  1.00 13.40 ? 66   TRP A CD1 1 
ATOM   294  C  CD2 . TRP A 1 66   ? 13.247 46.662  9.390   1.00 13.14 ? 66   TRP A CD2 1 
ATOM   295  N  NE1 . TRP A 1 66   ? 12.972 44.978  10.857  1.00 14.97 ? 66   TRP A NE1 1 
ATOM   296  C  CE2 . TRP A 1 66   ? 13.817 45.462  9.881   1.00 13.14 ? 66   TRP A CE2 1 
ATOM   297  C  CE3 . TRP A 1 66   ? 13.926 47.367  8.354   1.00 14.06 ? 66   TRP A CE3 1 
ATOM   298  C  CZ2 . TRP A 1 66   ? 15.034 44.933  9.398   1.00 15.55 ? 66   TRP A CZ2 1 
ATOM   299  C  CZ3 . TRP A 1 66   ? 15.132 46.834  7.877   1.00 14.25 ? 66   TRP A CZ3 1 
ATOM   300  C  CH2 . TRP A 1 66   ? 15.673 45.647  8.394   1.00 13.30 ? 66   TRP A CH2 1 
ATOM   301  N  N   . ASN A 1 67   ? 10.680 48.468  12.964  1.00 15.67 ? 67   ASN A N   1 
ATOM   302  C  CA  . ASN A 1 67   ? 10.874 48.062  14.373  1.00 14.12 ? 67   ASN A CA  1 
ATOM   303  C  C   . ASN A 1 67   ? 11.471 46.655  14.384  1.00 14.83 ? 67   ASN A C   1 
ATOM   304  O  O   . ASN A 1 67   ? 10.790 45.625  14.083  1.00 15.58 ? 67   ASN A O   1 
ATOM   305  C  CB  . ASN A 1 67   ? 9.516  47.990  15.120  1.00 18.11 ? 67   ASN A CB  1 
ATOM   306  C  CG  . ASN A 1 67   ? 8.889  49.327  15.331  1.00 21.91 ? 67   ASN A CG  1 
ATOM   307  O  OD1 . ASN A 1 67   ? 9.547  50.366  15.382  1.00 22.16 ? 67   ASN A OD1 1 
ATOM   308  N  ND2 . ASN A 1 67   ? 7.570  49.323  15.510  1.00 25.81 ? 67   ASN A ND2 1 
ATOM   309  N  N   . ILE A 1 68   ? 12.756 46.567  14.716  1.00 13.62 ? 68   ILE A N   1 
ATOM   310  C  CA  . ILE A 1 68   ? 13.430 45.298  14.668  1.00 14.47 ? 68   ILE A CA  1 
ATOM   311  C  C   . ILE A 1 68   ? 12.962 44.390  15.808  1.00 14.21 ? 68   ILE A C   1 
ATOM   312  O  O   . ILE A 1 68   ? 12.900 44.834  16.953  1.00 16.47 ? 68   ILE A O   1 
ATOM   313  C  CB  . ILE A 1 68   ? 15.019 45.492  14.762  1.00 14.15 ? 68   ILE A CB  1 
ATOM   314  C  CG1 . ILE A 1 68   ? 15.537 46.301  13.551  1.00 14.25 ? 68   ILE A CG1 1 
ATOM   315  C  CG2 . ILE A 1 68   ? 15.725 44.142  14.822  1.00 16.52 ? 68   ILE A CG2 1 
ATOM   316  C  CD1 . ILE A 1 68   ? 16.956 46.861  13.789  1.00 12.73 ? 68   ILE A CD1 1 
ATOM   317  N  N   . LYS A 1 69   ? 12.744 43.121  15.454  1.00 16.61 ? 69   LYS A N   1 
ATOM   318  C  CA  . LYS A 1 69   ? 12.347 42.115  16.467  1.00 17.10 ? 69   LYS A CA  1 
ATOM   319  C  C   . LYS A 1 69   ? 13.400 41.028  16.472  1.00 18.52 ? 69   LYS A C   1 
ATOM   320  O  O   . LYS A 1 69   ? 14.035 40.766  15.455  1.00 19.02 ? 69   LYS A O   1 
ATOM   321  C  CB  . LYS A 1 69   ? 10.987 41.518  16.091  1.00 21.06 ? 69   LYS A CB  1 
ATOM   322  C  CG  . LYS A 1 69   ? 9.868  42.521  16.317  1.00 25.49 ? 69   LYS A CG  1 
ATOM   323  C  CD  . LYS A 1 69   ? 8.591  41.996  15.671  1.00 35.56 ? 69   LYS A CD  1 
ATOM   324  C  CE  . LYS A 1 69   ? 7.530  43.083  15.651  1.00 38.50 ? 69   LYS A CE  1 
ATOM   325  N  NZ  . LYS A 1 69   ? 6.704  42.873  14.419  1.00 40.86 ? 69   LYS A NZ  1 
ATOM   326  N  N   . TYR A 1 70   ? 13.625 40.403  17.622  1.00 18.05 ? 70   TYR A N   1 
ATOM   327  C  CA  . TYR A 1 70   ? 14.576 39.314  17.669  1.00 16.68 ? 70   TYR A CA  1 
ATOM   328  C  C   . TYR A 1 70   ? 14.027 38.256  18.637  1.00 18.39 ? 70   TYR A C   1 
ATOM   329  O  O   . TYR A 1 70   ? 13.229 38.563  19.522  1.00 20.53 ? 70   TYR A O   1 
ATOM   330  C  CB  . TYR A 1 70   ? 15.988 39.795  18.137  1.00 17.84 ? 70   TYR A CB  1 
ATOM   331  C  CG  . TYR A 1 70   ? 16.053 40.371  19.522  1.00 15.99 ? 70   TYR A CG  1 
ATOM   332  C  CD1 . TYR A 1 70   ? 16.251 39.555  20.648  1.00 19.75 ? 70   TYR A CD1 1 
ATOM   333  C  CD2 . TYR A 1 70   ? 15.883 41.732  19.727  1.00 18.07 ? 70   TYR A CD2 1 
ATOM   334  C  CE1 . TYR A 1 70   ? 16.288 40.132  21.938  1.00 19.86 ? 70   TYR A CE1 1 
ATOM   335  C  CE2 . TYR A 1 70   ? 15.912 42.317  20.981  1.00 19.30 ? 70   TYR A CE2 1 
ATOM   336  C  CZ  . TYR A 1 70   ? 16.110 41.513  22.104  1.00 19.17 ? 70   TYR A CZ  1 
ATOM   337  O  OH  . TYR A 1 70   ? 16.084 42.137  23.353  1.00 21.81 ? 70   TYR A OH  1 
ATOM   338  N  N   . ASP A 1 71   ? 14.493 37.032  18.448  1.00 20.67 ? 71   ASP A N   1 
ATOM   339  C  CA  . ASP A 1 71   ? 14.090 35.919  19.303  1.00 21.44 ? 71   ASP A CA  1 
ATOM   340  C  C   . ASP A 1 71   ? 15.064 35.876  20.475  1.00 23.54 ? 71   ASP A C   1 
ATOM   341  O  O   . ASP A 1 71   ? 16.276 35.637  20.283  1.00 21.83 ? 71   ASP A O   1 
ATOM   342  C  CB  . ASP A 1 71   ? 14.195 34.646  18.500  1.00 24.39 ? 71   ASP A CB  1 
ATOM   343  C  CG  . ASP A 1 71   ? 13.805 33.408  19.310  1.00 29.35 ? 71   ASP A CG  1 
ATOM   344  O  OD1 . ASP A 1 71   ? 13.589 33.540  20.533  1.00 33.80 ? 71   ASP A OD1 1 
ATOM   345  O  OD2 . ASP A 1 71   ? 13.735 32.330  18.698  1.00 34.64 ? 71   ASP A OD2 1 
ATOM   346  N  N   . PRO A 1 72   ? 14.577 36.135  21.710  1.00 25.57 ? 72   PRO A N   1 
ATOM   347  C  CA  . PRO A 1 72   ? 15.519 36.093  22.830  1.00 26.58 ? 72   PRO A CA  1 
ATOM   348  C  C   . PRO A 1 72   ? 16.274 34.773  22.972  1.00 25.73 ? 72   PRO A C   1 
ATOM   349  O  O   . PRO A 1 72   ? 17.375 34.747  23.494  1.00 25.74 ? 72   PRO A O   1 
ATOM   350  C  CB  . PRO A 1 72   ? 14.651 36.458  24.049  1.00 27.51 ? 72   PRO A CB  1 
ATOM   351  C  CG  . PRO A 1 72   ? 13.289 36.129  23.625  1.00 30.55 ? 72   PRO A CG  1 
ATOM   352  C  CD  . PRO A 1 72   ? 13.222 36.473  22.174  1.00 26.71 ? 72   PRO A CD  1 
ATOM   353  N  N   . LEU A 1 73   ? 15.712 33.691  22.451  1.00 25.51 ? 73   LEU A N   1 
ATOM   354  C  CA  . LEU A 1 73   ? 16.370 32.400  22.536  1.00 26.90 ? 73   LEU A CA  1 
ATOM   355  C  C   . LEU A 1 73   ? 17.511 32.168  21.528  1.00 24.88 ? 73   LEU A C   1 
ATOM   356  O  O   . LEU A 1 73   ? 18.193 31.139  21.554  1.00 26.29 ? 73   LEU A O   1 
ATOM   357  C  CB  . LEU A 1 73   ? 15.316 31.289  22.384  1.00 27.51 ? 73   LEU A CB  1 
ATOM   358  C  CG  . LEU A 1 73   ? 14.191 31.364  23.428  1.00 31.04 ? 73   LEU A CG  1 
ATOM   359  C  CD1 . LEU A 1 73   ? 13.187 30.243  23.156  1.00 32.64 ? 73   LEU A CD1 1 
ATOM   360  C  CD2 . LEU A 1 73   ? 14.789 31.250  24.847  1.00 32.42 ? 73   LEU A CD2 1 
ATOM   361  N  N   . LYS A 1 74   ? 17.740 33.140  20.626  1.00 20.84 ? 74   LYS A N   1 
ATOM   362  C  CA  . LYS A 1 74   ? 18.797 32.974  19.645  1.00 22.16 ? 74   LYS A CA  1 
ATOM   363  C  C   . LYS A 1 74   ? 20.201 32.820  20.251  1.00 19.14 ? 74   LYS A C   1 
ATOM   364  O  O   . LYS A 1 74   ? 21.054 32.073  19.762  1.00 22.11 ? 74   LYS A O   1 
ATOM   365  C  CB  . LYS A 1 74   ? 18.753 34.162  18.701  1.00 22.15 ? 74   LYS A CB  1 
ATOM   366  C  CG  . LYS A 1 74   ? 19.830 34.173  17.648  1.00 26.26 ? 74   LYS A CG  1 
ATOM   367  C  CD  . LYS A 1 74   ? 19.463 35.314  16.683  1.00 25.15 ? 74   LYS A CD  1 
ATOM   368  C  CE  . LYS A 1 74   ? 20.538 35.621  15.697  1.00 33.36 ? 74   LYS A CE  1 
ATOM   369  N  NZ  . LYS A 1 74   ? 21.011 34.392  15.049  1.00 38.12 ? 74   LYS A NZ  1 
ATOM   370  N  N   A TYR A 1 75   ? 20.441 33.554  21.323  0.50 20.98 ? 75   TYR A N   1 
ATOM   371  N  N   B TYR A 1 75   ? 20.441 33.554  21.323  0.50 22.55 ? 75   TYR A N   1 
ATOM   372  C  CA  A TYR A 1 75   ? 21.743 33.463  21.991  0.50 19.09 ? 75   TYR A CA  1 
ATOM   373  C  CA  B TYR A 1 75   ? 21.743 33.463  21.991  0.50 22.35 ? 75   TYR A CA  1 
ATOM   374  C  C   A TYR A 1 75   ? 21.525 32.682  23.318  0.50 21.11 ? 75   TYR A C   1 
ATOM   375  C  C   B TYR A 1 75   ? 21.550 32.579  23.256  0.50 23.20 ? 75   TYR A C   1 
ATOM   376  O  O   A TYR A 1 75   ? 20.506 32.842  23.964  0.50 23.18 ? 75   TYR A O   1 
ATOM   377  O  O   B TYR A 1 75   ? 20.523 32.652  23.905  0.50 25.74 ? 75   TYR A O   1 
ATOM   378  C  CB  A TYR A 1 75   ? 22.298 34.887  22.218  0.50 20.18 ? 75   TYR A CB  1 
ATOM   379  C  CB  B TYR A 1 75   ? 22.243 34.886  22.326  0.50 26.01 ? 75   TYR A CB  1 
ATOM   380  C  CG  A TYR A 1 75   ? 22.678 35.540  20.902  0.50 13.19 ? 75   TYR A CG  1 
ATOM   381  C  CG  B TYR A 1 75   ? 21.997 35.836  21.168  0.50 27.14 ? 75   TYR A CG  1 
ATOM   382  C  CD1 A TYR A 1 75   ? 21.911 36.555  20.339  0.50 18.70 ? 75   TYR A CD1 1 
ATOM   383  C  CD1 B TYR A 1 75   ? 20.949 36.752  21.182  0.50 28.84 ? 75   TYR A CD1 1 
ATOM   384  C  CD2 A TYR A 1 75   ? 23.736 35.045  20.173  0.50 12.79 ? 75   TYR A CD2 1 
ATOM   385  C  CD2 B TYR A 1 75   ? 22.743 35.720  20.017  0.50 28.72 ? 75   TYR A CD2 1 
ATOM   386  C  CE1 A TYR A 1 75   ? 22.204 37.031  19.076  0.50 16.28 ? 75   TYR A CE1 1 
ATOM   387  C  CE1 B TYR A 1 75   ? 20.667 37.504  20.058  0.50 27.93 ? 75   TYR A CE1 1 
ATOM   388  C  CE2 A TYR A 1 75   ? 24.048 35.509  18.870  0.50 18.16 ? 75   TYR A CE2 1 
ATOM   389  C  CE2 B TYR A 1 75   ? 22.464 36.472  18.848  0.50 31.44 ? 75   TYR A CE2 1 
ATOM   390  C  CZ  A TYR A 1 75   ? 23.281 36.494  18.318  0.50 15.89 ? 75   TYR A CZ  1 
ATOM   391  C  CZ  B TYR A 1 75   ? 21.424 37.357  18.864  0.50 31.65 ? 75   TYR A CZ  1 
ATOM   392  O  OH  A TYR A 1 75   ? 23.569 36.902  16.964  0.50 17.61 ? 75   TYR A OH  1 
ATOM   393  O  OH  B TYR A 1 75   ? 21.111 38.059  17.643  0.50 35.12 ? 75   TYR A OH  1 
ATOM   394  N  N   . ASN A 1 76   ? 22.493 31.854  23.671  1.00 21.00 ? 76   ASN A N   1 
ATOM   395  C  CA  . ASN A 1 76   ? 22.428 30.992  24.863  1.00 22.25 ? 76   ASN A CA  1 
ATOM   396  C  C   . ASN A 1 76   ? 23.856 30.656  25.283  1.00 22.04 ? 76   ASN A C   1 
ATOM   397  O  O   . ASN A 1 76   ? 24.839 31.095  24.671  1.00 24.58 ? 76   ASN A O   1 
ATOM   398  C  CB  . ASN A 1 76   ? 21.633 29.699  24.556  1.00 24.44 ? 76   ASN A CB  1 
ATOM   399  C  CG  . ASN A 1 76   ? 22.186 28.920  23.385  1.00 23.07 ? 76   ASN A CG  1 
ATOM   400  O  OD1 . ASN A 1 76   ? 23.385 28.706  23.265  1.00 27.48 ? 76   ASN A OD1 1 
ATOM   401  N  ND2 . ASN A 1 76   ? 21.285 28.465  22.505  1.00 32.38 ? 76   ASN A ND2 1 
ATOM   402  N  N   . ALA A 1 77   ? 24.003 29.875  26.362  1.00 26.24 ? 77   ALA A N   1 
ATOM   403  C  CA  . ALA A 1 77   ? 25.361 29.581  26.831  1.00 26.14 ? 77   ALA A CA  1 
ATOM   404  C  C   . ALA A 1 77   ? 26.315 29.017  25.785  1.00 27.43 ? 77   ALA A C   1 
ATOM   405  O  O   . ALA A 1 77   ? 27.533 29.226  25.850  1.00 29.01 ? 77   ALA A O   1 
ATOM   406  C  CB  . ALA A 1 77   ? 25.302 28.635  28.027  1.00 31.22 ? 77   ALA A CB  1 
ATOM   407  N  N   . HIS A 1 78   ? 25.790 28.322  24.795  1.00 31.20 ? 78   HIS A N   1 
ATOM   408  C  CA  . HIS A 1 78   ? 26.710 27.755  23.812  1.00 32.56 ? 78   HIS A CA  1 
ATOM   409  C  C   . HIS A 1 78   ? 26.834 28.580  22.540  1.00 31.40 ? 78   HIS A C   1 
ATOM   410  O  O   . HIS A 1 78   ? 27.536 28.188  21.610  1.00 32.65 ? 78   HIS A O   1 
ATOM   411  C  CB  . HIS A 1 78   ? 26.296 26.300  23.509  1.00 36.39 ? 78   HIS A CB  1 
ATOM   412  C  CG  . HIS A 1 78   ? 26.070 25.490  24.750  1.00 41.39 ? 78   HIS A CG  1 
ATOM   413  N  ND1 . HIS A 1 78   ? 27.034 25.350  25.732  1.00 43.75 ? 78   HIS A ND1 1 
ATOM   414  C  CD2 . HIS A 1 78   ? 24.956 24.881  25.227  1.00 43.09 ? 78   HIS A CD2 1 
ATOM   415  C  CE1 . HIS A 1 78   ? 26.521 24.697  26.762  1.00 45.86 ? 78   HIS A CE1 1 
ATOM   416  N  NE2 . HIS A 1 78   ? 25.261 24.402  26.483  1.00 47.37 ? 78   HIS A NE2 1 
ATOM   417  N  N   . HIS A 1 79   ? 26.188 29.747  22.543  1.00 27.01 ? 79   HIS A N   1 
ATOM   418  C  CA  . HIS A 1 79   ? 26.193 30.635  21.372  1.00 22.58 ? 79   HIS A CA  1 
ATOM   419  C  C   . HIS A 1 79   ? 25.944 32.062  21.858  1.00 15.70 ? 79   HIS A C   1 
ATOM   420  O  O   . HIS A 1 79   ? 24.810 32.528  21.879  1.00 19.08 ? 79   HIS A O   1 
ATOM   421  C  CB  . HIS A 1 79   ? 25.071 30.241  20.438  1.00 22.99 ? 79   HIS A CB  1 
ATOM   422  C  CG  . HIS A 1 79   ? 25.166 30.902  19.092  1.00 22.77 ? 79   HIS A CG  1 
ATOM   423  N  ND1 . HIS A 1 79   ? 24.260 31.846  18.649  1.00 26.50 ? 79   HIS A ND1 1 
ATOM   424  C  CD2 . HIS A 1 79   ? 26.116 30.812  18.129  1.00 24.13 ? 79   HIS A CD2 1 
ATOM   425  C  CE1 . HIS A 1 79   ? 24.655 32.318  17.477  1.00 21.62 ? 79   HIS A CE1 1 
ATOM   426  N  NE2 . HIS A 1 79   ? 25.777 31.708  17.141  1.00 23.83 ? 79   HIS A NE2 1 
ATOM   427  N  N   . LYS A 1 80   ? 27.023 32.702  22.291  1.00 15.77 ? 80   LYS A N   1 
ATOM   428  C  CA  . LYS A 1 80   ? 26.874 34.026  22.850  1.00 15.58 ? 80   LYS A CA  1 
ATOM   429  C  C   . LYS A 1 80   ? 27.079 35.113  21.768  1.00 15.28 ? 80   LYS A C   1 
ATOM   430  O  O   . LYS A 1 80   ? 27.687 34.845  20.718  1.00 17.84 ? 80   LYS A O   1 
ATOM   431  C  CB  . LYS A 1 80   ? 27.921 34.259  23.908  1.00 16.23 ? 80   LYS A CB  1 
ATOM   432  C  CG  . LYS A 1 80   ? 27.845 33.201  25.044  1.00 18.85 ? 80   LYS A CG  1 
ATOM   433  C  CD  . LYS A 1 80   ? 29.053 33.266  25.939  1.00 27.28 ? 80   LYS A CD  1 
ATOM   434  C  CE  . LYS A 1 80   ? 29.025 34.483  26.820  1.00 28.29 ? 80   LYS A CE  1 
ATOM   435  N  NZ  . LYS A 1 80   ? 29.917 34.252  28.048  1.00 31.25 ? 80   LYS A NZ  1 
ATOM   436  N  N   . LEU A 1 81   ? 26.550 36.282  22.027  1.00 13.46 ? 81   LEU A N   1 
ATOM   437  C  CA  . LEU A 1 81   ? 26.795 37.443  21.128  1.00 11.81 ? 81   LEU A CA  1 
ATOM   438  C  C   . LEU A 1 81   ? 28.109 38.116  21.608  1.00 13.96 ? 81   LEU A C   1 
ATOM   439  O  O   . LEU A 1 81   ? 28.216 38.521  22.779  1.00 13.96 ? 81   LEU A O   1 
ATOM   440  C  CB  . LEU A 1 81   ? 25.639 38.410  21.258  1.00 12.30 ? 81   LEU A CB  1 
ATOM   441  C  CG  . LEU A 1 81   ? 25.742 39.686  20.390  1.00 12.98 ? 81   LEU A CG  1 
ATOM   442  C  CD1 . LEU A 1 81   ? 25.774 39.271  18.914  1.00 13.41 ? 81   LEU A CD1 1 
ATOM   443  C  CD2 . LEU A 1 81   ? 24.582 40.640  20.719  1.00 16.15 ? 81   LEU A CD2 1 
ATOM   444  N  N   A LYS A 1 82   ? 29.117 38.200  20.760  0.50 11.61 ? 82   LYS A N   1 
ATOM   445  N  N   B LYS A 1 82   ? 29.109 38.154  20.772  0.50 13.05 ? 82   LYS A N   1 
ATOM   446  C  CA  A LYS A 1 82   ? 30.372 38.824  21.133  0.50 10.31 ? 82   LYS A CA  1 
ATOM   447  C  CA  B LYS A 1 82   ? 30.345 38.836  21.116  0.50 12.04 ? 82   LYS A CA  1 
ATOM   448  C  C   A LYS A 1 82   ? 30.283 40.244  20.625  0.50 9.55  ? 82   LYS A C   1 
ATOM   449  C  C   B LYS A 1 82   ? 30.318 40.278  20.630  0.50 11.57 ? 82   LYS A C   1 
ATOM   450  O  O   A LYS A 1 82   ? 30.046 40.439  19.401  0.50 12.02 ? 82   LYS A O   1 
ATOM   451  O  O   B LYS A 1 82   ? 29.975 40.444  19.419  0.50 13.94 ? 82   LYS A O   1 
ATOM   452  C  CB  A LYS A 1 82   ? 31.502 38.101  20.436  0.50 11.55 ? 82   LYS A CB  1 
ATOM   453  C  CB  B LYS A 1 82   ? 31.541 38.080  20.543  0.50 15.80 ? 82   LYS A CB  1 
ATOM   454  C  CG  A LYS A 1 82   ? 32.883 38.677  20.633  0.50 15.46 ? 82   LYS A CG  1 
ATOM   455  C  CG  B LYS A 1 82   ? 31.440 36.570  20.688  0.50 19.19 ? 82   LYS A CG  1 
ATOM   456  C  CD  A LYS A 1 82   ? 33.369 38.559  22.085  0.50 23.93 ? 82   LYS A CD  1 
ATOM   457  C  CD  B LYS A 1 82   ? 32.710 35.883  20.217  0.50 28.43 ? 82   LYS A CD  1 
ATOM   458  C  CE  A LYS A 1 82   ? 34.878 38.204  22.068  0.50 25.56 ? 82   LYS A CE  1 
ATOM   459  C  CE  B LYS A 1 82   ? 32.394 34.708  19.304  0.50 33.36 ? 82   LYS A CE  1 
ATOM   460  N  NZ  A LYS A 1 82   ? 35.386 38.011  23.445  0.50 30.24 ? 82   LYS A NZ  1 
ATOM   461  N  NZ  B LYS A 1 82   ? 32.679 33.403  19.959  0.50 33.51 ? 82   LYS A NZ  1 
ATOM   462  N  N   . VAL A 1 83   ? 30.468 41.229  21.489  1.00 9.35  ? 83   VAL A N   1 
ATOM   463  C  CA  . VAL A 1 83   ? 30.309 42.637  21.128  1.00 9.92  ? 83   VAL A CA  1 
ATOM   464  C  C   . VAL A 1 83   ? 31.655 43.340  21.276  1.00 10.00 ? 83   VAL A C   1 
ATOM   465  O  O   . VAL A 1 83   ? 32.289 43.316  22.366  1.00 11.71 ? 83   VAL A O   1 
ATOM   466  C  CB  . VAL A 1 83   ? 29.284 43.290  22.067  1.00 9.44  ? 83   VAL A CB  1 
ATOM   467  C  CG1 . VAL A 1 83   ? 29.066 44.803  21.708  1.00 11.96 ? 83   VAL A CG1 1 
ATOM   468  C  CG2 . VAL A 1 83   ? 27.930 42.543  21.903  1.00 11.48 ? 83   VAL A CG2 1 
ATOM   469  N  N   . PHE A 1 84   ? 32.075 44.052  20.209  1.00 10.47 ? 84   PHE A N   1 
ATOM   470  C  CA  . PHE A 1 84   ? 33.319 44.830  20.234  1.00 10.44 ? 84   PHE A CA  1 
ATOM   471  C  C   . PHE A 1 84   ? 32.951 46.307  20.182  1.00 9.64  ? 84   PHE A C   1 
ATOM   472  O  O   . PHE A 1 84   ? 32.407 46.790  19.166  1.00 10.15 ? 84   PHE A O   1 
ATOM   473  C  CB  . PHE A 1 84   ? 34.198 44.476  19.042  1.00 12.39 ? 84   PHE A CB  1 
ATOM   474  C  CG  . PHE A 1 84   ? 34.831 43.142  19.181  1.00 11.97 ? 84   PHE A CG  1 
ATOM   475  C  CD1 . PHE A 1 84   ? 34.384 42.059  18.473  1.00 14.59 ? 84   PHE A CD1 1 
ATOM   476  C  CD2 . PHE A 1 84   ? 35.913 42.987  20.055  1.00 15.64 ? 84   PHE A CD2 1 
ATOM   477  C  CE1 . PHE A 1 84   ? 35.034 40.798  18.610  1.00 18.25 ? 84   PHE A CE1 1 
ATOM   478  C  CE2 . PHE A 1 84   ? 36.586 41.735  20.209  1.00 14.92 ? 84   PHE A CE2 1 
ATOM   479  C  CZ  . PHE A 1 84   ? 36.142 40.653  19.468  1.00 17.64 ? 84   PHE A CZ  1 
ATOM   480  N  N   . VAL A 1 85   ? 33.238 47.045  21.259  1.00 9.67  ? 85   VAL A N   1 
ATOM   481  C  CA  . VAL A 1 85   ? 32.965 48.501  21.325  1.00 9.32  ? 85   VAL A CA  1 
ATOM   482  C  C   . VAL A 1 85   ? 34.287 49.133  20.914  1.00 9.17  ? 85   VAL A C   1 
ATOM   483  O  O   . VAL A 1 85   ? 35.327 48.937  21.575  1.00 9.69  ? 85   VAL A O   1 
ATOM   484  C  CB  . VAL A 1 85   ? 32.555 48.899  22.743  1.00 8.85  ? 85   VAL A CB  1 
ATOM   485  C  CG1 . VAL A 1 85   ? 32.383 50.421  22.857  1.00 12.07 ? 85   VAL A CG1 1 
ATOM   486  C  CG2 . VAL A 1 85   ? 31.210 48.190  23.104  1.00 11.30 ? 85   VAL A CG2 1 
ATOM   487  N  N   . VAL A 1 86   ? 34.243 49.878  19.821  1.00 8.05  ? 86   VAL A N   1 
ATOM   488  C  CA  . VAL A 1 86   ? 35.496 50.395  19.202  1.00 8.90  ? 86   VAL A CA  1 
ATOM   489  C  C   . VAL A 1 86   ? 35.565 51.912  19.322  1.00 8.28  ? 86   VAL A C   1 
ATOM   490  O  O   . VAL A 1 86   ? 34.902 52.631  18.555  1.00 9.27  ? 86   VAL A O   1 
ATOM   491  C  CB  . VAL A 1 86   ? 35.532 49.942  17.717  1.00 9.30  ? 86   VAL A CB  1 
ATOM   492  C  CG1 . VAL A 1 86   ? 36.836 50.496  17.030  1.00 11.70 ? 86   VAL A CG1 1 
ATOM   493  C  CG2 . VAL A 1 86   ? 35.501 48.377  17.604  1.00 10.70 ? 86   VAL A CG2 1 
ATOM   494  N  N   . PRO A 1 87   ? 36.341 52.433  20.290  1.00 7.78  ? 87   PRO A N   1 
ATOM   495  C  CA  . PRO A 1 87   ? 36.435 53.899  20.452  1.00 8.65  ? 87   PRO A CA  1 
ATOM   496  C  C   . PRO A 1 87   ? 37.161 54.551  19.244  1.00 8.34  ? 87   PRO A C   1 
ATOM   497  O  O   . PRO A 1 87   ? 38.185 53.989  18.742  1.00 8.19  ? 87   PRO A O   1 
ATOM   498  C  CB  . PRO A 1 87   ? 37.278 54.064  21.738  1.00 8.08  ? 87   PRO A CB  1 
ATOM   499  C  CG  . PRO A 1 87   ? 36.986 52.754  22.425  1.00 10.19 ? 87   PRO A CG  1 
ATOM   500  C  CD  . PRO A 1 87   ? 37.045 51.718  21.373  1.00 9.40  ? 87   PRO A CD  1 
ATOM   501  N  N   . HIS A 1 88   ? 36.662 55.715  18.841  1.00 7.40  ? 88   HIS A N   1 
ATOM   502  C  CA  . HIS A 1 88   ? 37.236 56.403  17.637  1.00 8.53  ? 88   HIS A CA  1 
ATOM   503  C  C   . HIS A 1 88   ? 36.958 57.881  17.750  1.00 9.00  ? 88   HIS A C   1 
ATOM   504  O  O   . HIS A 1 88   ? 36.130 58.351  18.549  1.00 8.38  ? 88   HIS A O   1 
ATOM   505  C  CB  . HIS A 1 88   ? 36.640 55.805  16.319  1.00 8.58  ? 88   HIS A CB  1 
ATOM   506  C  CG  . HIS A 1 88   ? 35.189 56.107  16.122  1.00 8.35  ? 88   HIS A CG  1 
ATOM   507  N  ND1 . HIS A 1 88   ? 34.750 57.165  15.344  1.00 8.94  ? 88   HIS A ND1 1 
ATOM   508  C  CD2 . HIS A 1 88   ? 34.077 55.472  16.587  1.00 8.14  ? 88   HIS A CD2 1 
ATOM   509  C  CE1 . HIS A 1 88   ? 33.427 57.158  15.330  1.00 9.49  ? 88   HIS A CE1 1 
ATOM   510  N  NE2 . HIS A 1 88   ? 32.987 56.142  16.084  1.00 10.00 ? 88   HIS A NE2 1 
ATOM   511  N  N   . SER A 1 89   ? 37.640 58.670  16.916  1.00 8.61  ? 89   SER A N   1 
ATOM   512  C  CA  . SER A 1 89   ? 37.518 60.109  16.900  1.00 8.98  ? 89   SER A CA  1 
ATOM   513  C  C   . SER A 1 89   ? 37.673 60.555  15.419  1.00 8.33  ? 89   SER A C   1 
ATOM   514  O  O   . SER A 1 89   ? 38.782 60.355  14.851  1.00 9.25  ? 89   SER A O   1 
ATOM   515  C  CB  . SER A 1 89   ? 38.648 60.666  17.780  1.00 9.23  ? 89   SER A CB  1 
ATOM   516  O  OG  . SER A 1 89   ? 38.609 62.095  17.730  1.00 9.73  ? 89   SER A OG  1 
ATOM   517  N  N   . HIS A 1 90   ? 36.659 61.184  14.892  1.00 8.42  ? 90   HIS A N   1 
ATOM   518  C  CA  . HIS A 1 90   ? 36.731 61.597  13.477  1.00 7.93  ? 90   HIS A CA  1 
ATOM   519  C  C   . HIS A 1 90   ? 37.381 62.977  13.397  1.00 8.60  ? 90   HIS A C   1 
ATOM   520  O  O   . HIS A 1 90   ? 36.849 63.971  13.857  1.00 10.01 ? 90   HIS A O   1 
ATOM   521  C  CB  . HIS A 1 90   ? 35.336 61.575  12.866  1.00 9.10  ? 90   HIS A CB  1 
ATOM   522  C  CG  . HIS A 1 90   ? 35.327 61.942  11.407  1.00 8.75  ? 90   HIS A CG  1 
ATOM   523  N  ND1 . HIS A 1 90   ? 35.856 61.129  10.428  1.00 10.65 ? 90   HIS A ND1 1 
ATOM   524  C  CD2 . HIS A 1 90   ? 34.908 63.058  10.795  1.00 10.03 ? 90   HIS A CD2 1 
ATOM   525  C  CE1 . HIS A 1 90   ? 35.765 61.772  9.257   1.00 8.30  ? 90   HIS A CE1 1 
ATOM   526  N  NE2 . HIS A 1 90   ? 35.215 62.945  9.444   1.00 9.75  ? 90   HIS A NE2 1 
ATOM   527  N  N   . ASN A 1 91   ? 38.569 62.989  12.811  1.00 9.25  ? 91   ASN A N   1 
ATOM   528  C  CA  . ASN A 1 91   ? 39.384 64.207  12.722  1.00 9.02  ? 91   ASN A CA  1 
ATOM   529  C  C   . ASN A 1 91   ? 39.552 64.674  11.279  1.00 9.82  ? 91   ASN A C   1 
ATOM   530  O  O   . ASN A 1 91   ? 40.198 63.976  10.466  1.00 15.69 ? 91   ASN A O   1 
ATOM   531  C  CB  . ASN A 1 91   ? 40.788 63.959  13.315  1.00 10.28 ? 91   ASN A CB  1 
ATOM   532  C  CG  . ASN A 1 91   ? 40.755 63.874  14.828  1.00 9.62  ? 91   ASN A CG  1 
ATOM   533  O  OD1 . ASN A 1 91   ? 40.149 62.945  15.385  1.00 12.28 ? 91   ASN A OD1 1 
ATOM   534  N  ND2 . ASN A 1 91   ? 41.375 64.781  15.494  1.00 7.67  ? 91   ASN A ND2 1 
ATOM   535  N  N   . ASP A 1 92   ? 38.989 65.796  10.942  1.00 8.62  ? 92   ASP A N   1 
ATOM   536  C  CA  . ASP A 1 92   ? 39.114 66.306  9.563   1.00 10.24 ? 92   ASP A CA  1 
ATOM   537  C  C   . ASP A 1 92   ? 40.349 67.134  9.374   1.00 9.75  ? 92   ASP A C   1 
ATOM   538  O  O   . ASP A 1 92   ? 40.554 68.096  10.111  1.00 10.70 ? 92   ASP A O   1 
ATOM   539  C  CB  . ASP A 1 92   ? 37.943 67.250  9.307   1.00 11.49 ? 92   ASP A CB  1 
ATOM   540  C  CG  . ASP A 1 92   ? 36.708 66.526  9.199   1.00 13.97 ? 92   ASP A CG  1 
ATOM   541  O  OD1 . ASP A 1 92   ? 36.692 65.603  8.430   1.00 13.04 ? 92   ASP A OD1 1 
ATOM   542  O  OD2 . ASP A 1 92   ? 35.723 66.841  9.909   1.00 16.72 ? 92   ASP A OD2 1 
ATOM   543  N  N   . PRO A 1 93   ? 41.188 66.825  8.354   1.00 9.45  ? 93   PRO A N   1 
ATOM   544  C  CA  . PRO A 1 93   ? 42.406 67.624  8.070   1.00 9.35  ? 93   PRO A CA  1 
ATOM   545  C  C   . PRO A 1 93   ? 41.977 68.892  7.285   1.00 10.86 ? 93   PRO A C   1 
ATOM   546  O  O   . PRO A 1 93   ? 42.308 69.061  6.089   1.00 12.61 ? 93   PRO A O   1 
ATOM   547  C  CB  . PRO A 1 93   ? 43.265 66.689  7.225   1.00 10.58 ? 93   PRO A CB  1 
ATOM   548  C  CG  . PRO A 1 93   ? 42.712 65.296  7.489   1.00 16.38 ? 93   PRO A CG  1 
ATOM   549  C  CD  . PRO A 1 93   ? 41.186 65.509  7.650   1.00 8.56  ? 93   PRO A CD  1 
ATOM   550  N  N   . GLY A 1 94   ? 41.166 69.719  7.965   1.00 9.48  ? 94   GLY A N   1 
ATOM   551  C  CA  . GLY A 1 94   ? 40.589 70.950  7.403   1.00 9.38  ? 94   GLY A CA  1 
ATOM   552  C  C   . GLY A 1 94   ? 39.107 70.734  7.148   1.00 9.82  ? 94   GLY A C   1 
ATOM   553  O  O   . GLY A 1 94   ? 38.701 69.673  6.610   1.00 11.11 ? 94   GLY A O   1 
ATOM   554  N  N   . TRP A 1 95   ? 38.273 71.701  7.563   1.00 9.94  ? 95   TRP A N   1 
ATOM   555  C  CA  . TRP A 1 95   ? 36.840 71.702  7.251   1.00 8.50  ? 95   TRP A CA  1 
ATOM   556  C  C   . TRP A 1 95   ? 36.361 73.119  7.669   1.00 10.11 ? 95   TRP A C   1 
ATOM   557  O  O   . TRP A 1 95   ? 36.318 74.043  6.858   1.00 9.97  ? 95   TRP A O   1 
ATOM   558  C  CB  . TRP A 1 95   ? 36.058 70.577  7.939   1.00 8.97  ? 95   TRP A CB  1 
ATOM   559  C  CG  . TRP A 1 95   ? 34.609 70.668  7.609   1.00 10.06 ? 95   TRP A CG  1 
ATOM   560  C  CD1 . TRP A 1 95   ? 34.036 71.122  6.448   1.00 9.87  ? 95   TRP A CD1 1 
ATOM   561  C  CD2 . TRP A 1 95   ? 33.551 70.236  8.459   1.00 12.46 ? 95   TRP A CD2 1 
ATOM   562  N  NE1 . TRP A 1 95   ? 32.656 71.034  6.538   1.00 11.09 ? 95   TRP A NE1 1 
ATOM   563  C  CE2 . TRP A 1 95   ? 32.345 70.462  7.752   1.00 11.73 ? 95   TRP A CE2 1 
ATOM   564  C  CE3 . TRP A 1 95   ? 33.510 69.631  9.755   1.00 15.13 ? 95   TRP A CE3 1 
ATOM   565  C  CZ2 . TRP A 1 95   ? 31.085 70.103  8.283   1.00 14.24 ? 95   TRP A CZ2 1 
ATOM   566  C  CZ3 . TRP A 1 95   ? 32.220 69.267  10.287  1.00 17.26 ? 95   TRP A CZ3 1 
ATOM   567  C  CH2 . TRP A 1 95   ? 31.050 69.511  9.541   1.00 18.06 ? 95   TRP A CH2 1 
ATOM   568  N  N   . ILE A 1 96   ? 36.047 73.290  8.957   1.00 9.55  ? 96   ILE A N   1 
ATOM   569  C  CA  . ILE A 1 96   ? 35.595 74.576  9.536   1.00 11.45 ? 96   ILE A CA  1 
ATOM   570  C  C   . ILE A 1 96   ? 36.854 75.354  9.949   1.00 11.29 ? 96   ILE A C   1 
ATOM   571  O  O   . ILE A 1 96   ? 36.812 76.598  10.007  1.00 13.71 ? 96   ILE A O   1 
ATOM   572  C  CB  . ILE A 1 96   ? 34.726 74.336  10.850  1.00 16.25 ? 96   ILE A CB  1 
ATOM   573  C  CG1 . ILE A 1 96   ? 33.505 73.483  10.552  1.00 18.60 ? 96   ILE A CG1 1 
ATOM   574  C  CG2 . ILE A 1 96   ? 34.365 75.689  11.509  1.00 18.92 ? 96   ILE A CG2 1 
ATOM   575  C  CD1 . ILE A 1 96   ? 32.928 73.849  9.179   1.00 18.05 ? 96   ILE A CD1 1 
ATOM   576  N  N   . GLN A 1 97   ? 37.934 74.656  10.289  1.00 9.17  ? 97   GLN A N   1 
ATOM   577  C  CA  . GLN A 1 97   ? 39.230 75.263  10.607  1.00 9.85  ? 97   GLN A CA  1 
ATOM   578  C  C   . GLN A 1 97   ? 40.238 74.633  9.652   1.00 9.65  ? 97   GLN A C   1 
ATOM   579  O  O   . GLN A 1 97   ? 39.953 73.624  8.978   1.00 9.07  ? 97   GLN A O   1 
ATOM   580  C  CB  . GLN A 1 97   ? 39.633 74.966  12.058  1.00 11.24 ? 97   GLN A CB  1 
ATOM   581  C  CG  . GLN A 1 97   ? 38.581 75.454  13.125  1.00 13.50 ? 97   GLN A CG  1 
ATOM   582  C  CD  . GLN A 1 97   ? 39.067 75.193  14.542  1.00 17.82 ? 97   GLN A CD  1 
ATOM   583  O  OE1 . GLN A 1 97   ? 40.205 75.537  14.890  1.00 24.02 ? 97   GLN A OE1 1 
ATOM   584  N  NE2 . GLN A 1 97   ? 38.233 74.544  15.367  1.00 21.28 ? 97   GLN A NE2 1 
ATOM   585  N  N   . THR A 1 98   ? 41.426 75.231  9.539   1.00 9.56  ? 98   THR A N   1 
ATOM   586  C  CA  . THR A 1 98   ? 42.476 74.652  8.703   1.00 8.39  ? 98   THR A CA  1 
ATOM   587  C  C   . THR A 1 98   ? 43.090 73.457  9.405   1.00 9.34  ? 98   THR A C   1 
ATOM   588  O  O   . THR A 1 98   ? 42.869 73.225  10.615  1.00 9.83  ? 98   THR A O   1 
ATOM   589  C  CB  . THR A 1 98   ? 43.588 75.641  8.455   1.00 9.64  ? 98   THR A CB  1 
ATOM   590  O  OG1 . THR A 1 98   ? 44.174 75.973  9.724   1.00 10.12 ? 98   THR A OG1 1 
ATOM   591  C  CG2 . THR A 1 98   ? 43.042 76.963  7.834   1.00 10.47 ? 98   THR A CG2 1 
ATOM   592  N  N   . PHE A 1 99   ? 43.857 72.690  8.657   1.00 9.27  ? 99   PHE A N   1 
ATOM   593  C  CA  . PHE A 1 99   ? 44.605 71.602  9.222   1.00 8.84  ? 99   PHE A CA  1 
ATOM   594  C  C   . PHE A 1 99   ? 45.374 72.049  10.477  1.00 9.34  ? 99   PHE A C   1 
ATOM   595  O  O   . PHE A 1 99   ? 45.320 71.406  11.562  1.00 9.62  ? 99   PHE A O   1 
ATOM   596  C  CB  . PHE A 1 99   ? 45.610 71.038  8.192   1.00 10.11 ? 99   PHE A CB  1 
ATOM   597  C  CG  . PHE A 1 99   ? 46.465 69.957  8.738   1.00 9.78  ? 99   PHE A CG  1 
ATOM   598  C  CD1 . PHE A 1 99   ? 46.080 68.617  8.601   1.00 9.99  ? 99   PHE A CD1 1 
ATOM   599  C  CD2 . PHE A 1 99   ? 47.687 70.253  9.373   1.00 11.24 ? 99   PHE A CD2 1 
ATOM   600  C  CE1 . PHE A 1 99   ? 46.893 67.608  9.094   1.00 10.03 ? 99   PHE A CE1 1 
ATOM   601  C  CE2 . PHE A 1 99   ? 48.505 69.261  9.887   1.00 12.72 ? 99   PHE A CE2 1 
ATOM   602  C  CZ  . PHE A 1 99   ? 48.102 67.901  9.745   1.00 11.04 ? 99   PHE A CZ  1 
ATOM   603  N  N   . GLU A 1 100  ? 46.135 73.116  10.358  1.00 9.34  ? 100  GLU A N   1 
ATOM   604  C  CA  . GLU A 1 100  ? 46.951 73.548  11.482  1.00 9.78  ? 100  GLU A CA  1 
ATOM   605  C  C   . GLU A 1 100  ? 46.138 74.081  12.637  1.00 9.68  ? 100  GLU A C   1 
ATOM   606  O  O   . GLU A 1 100  ? 46.504 73.830  13.815  1.00 10.20 ? 100  GLU A O   1 
ATOM   607  C  CB  . GLU A 1 100  ? 48.009 74.586  11.041  1.00 12.11 ? 100  GLU A CB  1 
ATOM   608  C  CG  . GLU A 1 100  ? 49.015 74.962  12.156  1.00 14.00 ? 100  GLU A CG  1 
ATOM   609  C  CD  . GLU A 1 100  ? 49.866 73.805  12.587  1.00 15.70 ? 100  GLU A CD  1 
ATOM   610  O  OE1 . GLU A 1 100  ? 50.006 72.785  11.855  1.00 16.75 ? 100  GLU A OE1 1 
ATOM   611  O  OE2 . GLU A 1 100  ? 50.509 73.951  13.681  1.00 16.99 ? 100  GLU A OE2 1 
ATOM   612  N  N   . GLU A 1 101  ? 45.033 74.768  12.369  1.00 9.02  ? 101  GLU A N   1 
ATOM   613  C  CA  . GLU A 1 101  ? 44.184 75.275  13.453  1.00 10.18 ? 101  GLU A CA  1 
ATOM   614  C  C   . GLU A 1 101  ? 43.583 74.087  14.211  1.00 9.69  ? 101  GLU A C   1 
ATOM   615  O  O   . GLU A 1 101  ? 43.578 74.057  15.473  1.00 9.90  ? 101  GLU A O   1 
ATOM   616  C  CB  . GLU A 1 101  ? 43.054 76.122  12.881  1.00 11.37 ? 101  GLU A CB  1 
ATOM   617  C  CG  . GLU A 1 101  ? 43.523 77.543  12.466  1.00 15.26 ? 101  GLU A CG  1 
ATOM   618  C  CD  . GLU A 1 101  ? 42.517 78.290  11.560  1.00 18.29 ? 101  GLU A CD  1 
ATOM   619  O  OE1 . GLU A 1 101  ? 41.486 77.727  11.040  1.00 14.09 ? 101  GLU A OE1 1 
ATOM   620  O  OE2 . GLU A 1 101  ? 42.777 79.519  11.321  1.00 22.25 ? 101  GLU A OE2 1 
ATOM   621  N  N   . TYR A 1 102  ? 43.019 73.112  13.484  1.00 9.38  ? 102  TYR A N   1 
ATOM   622  C  CA  . TYR A 1 102  ? 42.494 71.951  14.218  1.00 9.13  ? 102  TYR A CA  1 
ATOM   623  C  C   . TYR A 1 102  ? 43.597 71.202  14.972  1.00 8.51  ? 102  TYR A C   1 
ATOM   624  O  O   . TYR A 1 102  ? 43.348 70.677  16.063  1.00 10.05 ? 102  TYR A O   1 
ATOM   625  C  CB  . TYR A 1 102  ? 41.837 70.916  13.289  1.00 10.04 ? 102  TYR A CB  1 
ATOM   626  C  CG  . TYR A 1 102  ? 40.445 71.218  12.807  1.00 10.29 ? 102  TYR A CG  1 
ATOM   627  C  CD1 . TYR A 1 102  ? 39.373 71.487  13.710  1.00 10.80 ? 102  TYR A CD1 1 
ATOM   628  C  CD2 . TYR A 1 102  ? 40.129 71.088  11.435  1.00 10.24 ? 102  TYR A CD2 1 
ATOM   629  C  CE1 . TYR A 1 102  ? 38.060 71.611  13.249  1.00 10.91 ? 102  TYR A CE1 1 
ATOM   630  C  CE2 . TYR A 1 102  ? 38.816 71.176  10.968  1.00 10.26 ? 102  TYR A CE2 1 
ATOM   631  C  CZ  . TYR A 1 102  ? 37.786 71.439  11.870  1.00 9.81  ? 102  TYR A CZ  1 
ATOM   632  O  OH  . TYR A 1 102  ? 36.500 71.483  11.405  1.00 11.87 ? 102  TYR A OH  1 
ATOM   633  N  N   . TYR A 1 103  ? 44.791 71.097  14.393  1.00 9.84  ? 103  TYR A N   1 
ATOM   634  C  CA  . TYR A 1 103  ? 45.841 70.399  15.075  1.00 10.67 ? 103  TYR A CA  1 
ATOM   635  C  C   . TYR A 1 103  ? 46.113 71.054  16.426  1.00 10.43 ? 103  TYR A C   1 
ATOM   636  O  O   . TYR A 1 103  ? 46.247 70.366  17.468  1.00 10.77 ? 103  TYR A O   1 
ATOM   637  C  CB  . TYR A 1 103  ? 47.114 70.375  14.239  1.00 10.77 ? 103  TYR A CB  1 
ATOM   638  C  CG  . TYR A 1 103  ? 48.232 69.706  14.975  1.00 11.78 ? 103  TYR A CG  1 
ATOM   639  C  CD1 . TYR A 1 103  ? 48.220 68.318  15.189  1.00 12.41 ? 103  TYR A CD1 1 
ATOM   640  C  CD2 . TYR A 1 103  ? 49.304 70.464  15.503  1.00 11.86 ? 103  TYR A CD2 1 
ATOM   641  C  CE1 . TYR A 1 103  ? 49.214 67.692  15.907  1.00 11.78 ? 103  TYR A CE1 1 
ATOM   642  C  CE2 . TYR A 1 103  ? 50.346 69.846  16.247  1.00 11.32 ? 103  TYR A CE2 1 
ATOM   643  C  CZ  . TYR A 1 103  ? 50.278 68.459  16.448  1.00 12.32 ? 103  TYR A CZ  1 
ATOM   644  O  OH  . TYR A 1 103  ? 51.243 67.827  17.245  1.00 15.05 ? 103  TYR A OH  1 
ATOM   645  N  N   . GLN A 1 104  ? 46.207 72.385  16.412  1.00 10.71 ? 104  GLN A N   1 
ATOM   646  C  CA  . GLN A 1 104  ? 46.530 73.104  17.660  1.00 10.55 ? 104  GLN A CA  1 
ATOM   647  C  C   . GLN A 1 104  ? 45.410 73.115  18.633  1.00 13.49 ? 104  GLN A C   1 
ATOM   648  O  O   . GLN A 1 104  ? 45.673 73.008  19.872  1.00 14.52 ? 104  GLN A O   1 
ATOM   649  C  CB  . GLN A 1 104  ? 46.938 74.579  17.346  1.00 14.14 ? 104  GLN A CB  1 
ATOM   650  C  CG  . GLN A 1 104  ? 48.224 74.744  16.609  1.00 12.66 ? 104  GLN A CG  1 
ATOM   651  C  CD  . GLN A 1 104  ? 49.413 74.222  17.400  1.00 15.50 ? 104  GLN A CD  1 
ATOM   652  O  OE1 . GLN A 1 104  ? 49.392 74.308  18.647  1.00 16.04 ? 104  GLN A OE1 1 
ATOM   653  N  NE2 . GLN A 1 104  ? 50.427 73.682  16.722  1.00 14.57 ? 104  GLN A NE2 1 
ATOM   654  N  N   . HIS A 1 105  ? 44.173 73.200  18.166  1.00 11.33 ? 105  HIS A N   1 
ATOM   655  C  CA  . HIS A 1 105  ? 43.037 73.349  19.100  1.00 12.68 ? 105  HIS A CA  1 
ATOM   656  C  C   . HIS A 1 105  ? 42.435 72.043  19.554  1.00 14.09 ? 105  HIS A C   1 
ATOM   657  O  O   . HIS A 1 105  ? 41.902 71.967  20.649  1.00 15.23 ? 105  HIS A O   1 
ATOM   658  C  CB  . HIS A 1 105  ? 41.928 74.174  18.445  1.00 14.44 ? 105  HIS A CB  1 
ATOM   659  C  CG  . HIS A 1 105  ? 42.373 75.540  17.987  1.00 17.03 ? 105  HIS A CG  1 
ATOM   660  N  ND1 . HIS A 1 105  ? 41.820 76.161  16.884  1.00 22.65 ? 105  HIS A ND1 1 
ATOM   661  C  CD2 . HIS A 1 105  ? 43.336 76.376  18.456  1.00 23.65 ? 105  HIS A CD2 1 
ATOM   662  C  CE1 . HIS A 1 105  ? 42.438 77.317  16.687  1.00 22.54 ? 105  HIS A CE1 1 
ATOM   663  N  NE2 . HIS A 1 105  ? 43.360 77.473  17.625  1.00 23.30 ? 105  HIS A NE2 1 
ATOM   664  N  N   . ASP A 1 106  ? 42.591 71.003  18.739  1.00 12.23 ? 106  ASP A N   1 
ATOM   665  C  CA  . ASP A 1 106  ? 41.924 69.750  19.010  1.00 12.39 ? 106  ASP A CA  1 
ATOM   666  C  C   . ASP A 1 106  ? 42.761 68.519  18.888  1.00 10.42 ? 106  ASP A C   1 
ATOM   667  O  O   . ASP A 1 106  ? 42.945 67.793  19.882  1.00 11.14 ? 106  ASP A O   1 
ATOM   668  C  CB  . ASP A 1 106  ? 40.725 69.585  18.049  1.00 13.60 ? 106  ASP A CB  1 
ATOM   669  C  CG  . ASP A 1 106  ? 39.652 70.660  18.280  1.00 19.13 ? 106  ASP A CG  1 
ATOM   670  O  OD1 . ASP A 1 106  ? 38.861 70.534  19.278  1.00 20.19 ? 106  ASP A OD1 1 
ATOM   671  O  OD2 . ASP A 1 106  ? 39.656 71.650  17.487  1.00 20.80 ? 106  ASP A OD2 1 
ATOM   672  N  N   . THR A 1 107  ? 43.329 68.262  17.702  1.00 10.70 ? 107  THR A N   1 
ATOM   673  C  CA  . THR A 1 107  ? 43.942 66.956  17.450  1.00 8.93  ? 107  THR A CA  1 
ATOM   674  C  C   . THR A 1 107  ? 45.170 66.681  18.284  1.00 9.29  ? 107  THR A C   1 
ATOM   675  O  O   . THR A 1 107  ? 45.372 65.528  18.727  1.00 9.25  ? 107  THR A O   1 
ATOM   676  C  CB  . THR A 1 107  ? 44.219 66.804  15.924  1.00 8.83  ? 107  THR A CB  1 
ATOM   677  O  OG1 . THR A 1 107  ? 42.994 67.040  15.242  1.00 10.16 ? 107  THR A OG1 1 
ATOM   678  C  CG2 . THR A 1 107  ? 44.762 65.417  15.608  1.00 10.29 ? 107  THR A CG2 1 
ATOM   679  N  N   . LYS A 1 108  ? 46.028 67.680  18.519  1.00 9.60  ? 108  LYS A N   1 
ATOM   680  C  CA  . LYS A 1 108  ? 47.190 67.350  19.335  1.00 10.01 ? 108  LYS A CA  1 
ATOM   681  C  C   . LYS A 1 108  ? 46.793 66.932  20.770  1.00 8.55  ? 108  LYS A C   1 
ATOM   682  O  O   . LYS A 1 108  ? 47.480 66.111  21.343  1.00 11.06 ? 108  LYS A O   1 
ATOM   683  C  CB  . LYS A 1 108  ? 48.168 68.539  19.326  1.00 11.86 ? 108  LYS A CB  1 
ATOM   684  C  CG  . LYS A 1 108  ? 47.899 69.720  20.263  1.00 12.09 ? 108  LYS A CG  1 
ATOM   685  C  CD  . LYS A 1 108  ? 49.013 70.748  20.118  1.00 13.79 ? 108  LYS A CD  1 
ATOM   686  C  CE  . LYS A 1 108  ? 48.820 71.909  21.025  1.00 15.14 ? 108  LYS A CE  1 
ATOM   687  N  NZ  . LYS A 1 108  ? 50.005 72.852  20.970  1.00 18.59 ? 108  LYS A NZ  1 
ATOM   688  N  N   . HIS A 1 109  ? 45.695 67.494  21.268  1.00 9.70  ? 109  HIS A N   1 
ATOM   689  C  CA  . HIS A 1 109  ? 45.204 67.147  22.615  1.00 10.17 ? 109  HIS A CA  1 
ATOM   690  C  C   . HIS A 1 109  ? 44.582 65.760  22.614  1.00 9.43  ? 109  HIS A C   1 
ATOM   691  O  O   . HIS A 1 109  ? 44.783 64.943  23.543  1.00 11.40 ? 109  HIS A O   1 
ATOM   692  C  CB  . HIS A 1 109  ? 44.209 68.179  23.076  1.00 12.20 ? 109  HIS A CB  1 
ATOM   693  C  CG  . HIS A 1 109  ? 44.784 69.547  23.117  1.00 13.99 ? 109  HIS A CG  1 
ATOM   694  N  ND1 . HIS A 1 109  ? 45.769 69.891  24.021  1.00 21.17 ? 109  HIS A ND1 1 
ATOM   695  C  CD2 . HIS A 1 109  ? 44.592 70.629  22.324  1.00 18.03 ? 109  HIS A CD2 1 
ATOM   696  C  CE1 . HIS A 1 109  ? 46.170 71.132  23.771  1.00 18.65 ? 109  HIS A CE1 1 
ATOM   697  N  NE2 . HIS A 1 109  ? 45.476 71.597  22.751  1.00 18.68 ? 109  HIS A NE2 1 
ATOM   698  N  N   . ILE A 1 110  ? 43.824 65.433  21.535  1.00 9.99  ? 110  ILE A N   1 
ATOM   699  C  CA  . ILE A 1 110  ? 43.237 64.084  21.416  1.00 9.65  ? 110  ILE A CA  1 
ATOM   700  C  C   . ILE A 1 110  ? 44.366 63.043  21.391  1.00 8.53  ? 110  ILE A C   1 
ATOM   701  O  O   . ILE A 1 110  ? 44.299 62.020  22.114  1.00 9.86  ? 110  ILE A O   1 
ATOM   702  C  CB  . ILE A 1 110  ? 42.398 63.991  20.107  1.00 9.35  ? 110  ILE A CB  1 
ATOM   703  C  CG1 . ILE A 1 110  ? 41.215 64.935  20.230  1.00 9.51  ? 110  ILE A CG1 1 
ATOM   704  C  CG2 . ILE A 1 110  ? 41.976 62.529  19.816  1.00 9.55  ? 110  ILE A CG2 1 
ATOM   705  C  CD1 . ILE A 1 110  ? 40.449 65.171  18.882  1.00 9.66  ? 110  ILE A CD1 1 
ATOM   706  N  N   . LEU A 1 111  ? 45.400 63.248  20.574  1.00 8.27  ? 111  LEU A N   1 
ATOM   707  C  CA  . LEU A 1 111  ? 46.450 62.265  20.526  1.00 8.33  ? 111  LEU A CA  1 
ATOM   708  C  C   . LEU A 1 111  ? 47.316 62.188  21.792  1.00 8.63  ? 111  LEU A C   1 
ATOM   709  O  O   . LEU A 1 111  ? 47.704 61.112  22.214  1.00 10.11 ? 111  LEU A O   1 
ATOM   710  C  CB  . LEU A 1 111  ? 47.344 62.505  19.263  1.00 9.37  ? 111  LEU A CB  1 
ATOM   711  C  CG  . LEU A 1 111  ? 46.596 62.199  17.934  1.00 9.43  ? 111  LEU A CG  1 
ATOM   712  C  CD1 . LEU A 1 111  ? 47.425 62.676  16.727  1.00 10.17 ? 111  LEU A CD1 1 
ATOM   713  C  CD2 . LEU A 1 111  ? 46.364 60.710  17.858  1.00 12.81 ? 111  LEU A CD2 1 
ATOM   714  N  N   A SER A 1 112  ? 47.572 63.345  22.374  0.50 8.26  ? 112  SER A N   1 
ATOM   715  N  N   B SER A 1 112  ? 47.572 63.345  22.374  0.50 10.08 ? 112  SER A N   1 
ATOM   716  C  CA  A SER A 1 112  ? 48.339 63.345  23.647  0.50 8.80  ? 112  SER A CA  1 
ATOM   717  C  CA  B SER A 1 112  ? 48.339 63.345  23.647  0.50 12.25 ? 112  SER A CA  1 
ATOM   718  C  C   A SER A 1 112  ? 47.559 62.612  24.760  0.50 9.62  ? 112  SER A C   1 
ATOM   719  C  C   B SER A 1 112  ? 47.559 62.612  24.760  0.50 11.72 ? 112  SER A C   1 
ATOM   720  O  O   A SER A 1 112  ? 48.131 61.830  25.532  0.50 10.89 ? 112  SER A O   1 
ATOM   721  O  O   B SER A 1 112  ? 48.131 61.830  25.532  0.50 12.17 ? 112  SER A O   1 
ATOM   722  C  CB  A SER A 1 112  ? 48.595 64.797  24.043  0.50 8.65  ? 112  SER A CB  1 
ATOM   723  C  CB  B SER A 1 112  ? 48.595 64.797  24.043  0.50 14.85 ? 112  SER A CB  1 
ATOM   724  O  OG  A SER A 1 112  ? 49.386 64.788  25.240  0.50 9.52  ? 112  SER A OG  1 
ATOM   725  O  OG  B SER A 1 112  ? 49.442 65.378  23.041  0.50 19.79 ? 112  SER A OG  1 
ATOM   726  N  N   . ASN A 1 113  ? 46.257 62.853  24.823  1.00 9.90  ? 113  ASN A N   1 
ATOM   727  C  CA  . ASN A 1 113  ? 45.475 62.181  25.855  1.00 11.73 ? 113  ASN A CA  1 
ATOM   728  C  C   . ASN A 1 113  ? 45.227 60.744  25.511  1.00 11.96 ? 113  ASN A C   1 
ATOM   729  O  O   . ASN A 1 113  ? 45.154 59.909  26.437  1.00 12.34 ? 113  ASN A O   1 
ATOM   730  C  CB  . ASN A 1 113  ? 44.220 62.997  26.168  1.00 12.63 ? 113  ASN A CB  1 
ATOM   731  C  CG  . ASN A 1 113  ? 44.619 64.318  26.856  1.00 15.67 ? 113  ASN A CG  1 
ATOM   732  O  OD1 . ASN A 1 113  ? 45.713 64.408  27.450  1.00 22.97 ? 113  ASN A OD1 1 
ATOM   733  N  ND2 . ASN A 1 113  ? 43.833 65.333  26.724  1.00 15.61 ? 113  ASN A ND2 1 
ATOM   734  N  N   . ALA A 1 114  ? 45.193 60.371  24.218  1.00 10.20 ? 114  ALA A N   1 
ATOM   735  C  CA  . ALA A 1 114  ? 45.032 58.943  23.878  1.00 10.05 ? 114  ALA A CA  1 
ATOM   736  C  C   . ALA A 1 114  ? 46.319 58.224  24.325  1.00 10.27 ? 114  ALA A C   1 
ATOM   737  O  O   . ALA A 1 114  ? 46.249 57.114  24.885  1.00 11.74 ? 114  ALA A O   1 
ATOM   738  C  CB  . ALA A 1 114  ? 44.871 58.774  22.361  1.00 10.86 ? 114  ALA A CB  1 
ATOM   739  N  N   . LEU A 1 115  ? 47.482 58.830  24.103  1.00 9.70  ? 115  LEU A N   1 
ATOM   740  C  CA  . LEU A 1 115  ? 48.711 58.176  24.516  1.00 12.27 ? 115  LEU A CA  1 
ATOM   741  C  C   . LEU A 1 115  ? 48.723 57.957  26.056  1.00 12.61 ? 115  LEU A C   1 
ATOM   742  O  O   . LEU A 1 115  ? 48.997 56.825  26.532  1.00 12.63 ? 115  LEU A O   1 
ATOM   743  C  CB  . LEU A 1 115  ? 49.909 59.024  24.074  1.00 11.00 ? 115  LEU A CB  1 
ATOM   744  C  CG  . LEU A 1 115  ? 51.291 58.503  24.522  1.00 12.08 ? 115  LEU A CG  1 
ATOM   745  C  CD1 . LEU A 1 115  ? 51.546 57.073  24.085  1.00 15.25 ? 115  LEU A CD1 1 
ATOM   746  C  CD2 . LEU A 1 115  ? 52.351 59.468  23.956  1.00 14.84 ? 115  LEU A CD2 1 
ATOM   747  N  N   . ARG A 1 116  ? 48.360 59.006  26.789  1.00 11.74 ? 116  ARG A N   1 
ATOM   748  C  CA  . ARG A 1 116  ? 48.338 58.869  28.251  1.00 12.56 ? 116  ARG A CA  1 
ATOM   749  C  C   . ARG A 1 116  ? 47.285 57.823  28.723  1.00 12.39 ? 116  ARG A C   1 
ATOM   750  O  O   . ARG A 1 116  ? 47.592 56.910  29.547  1.00 13.08 ? 116  ARG A O   1 
ATOM   751  C  CB  . ARG A 1 116  ? 48.045 60.222  28.868  1.00 14.79 ? 116  ARG A CB  1 
ATOM   752  C  CG  . ARG A 1 116  ? 47.803 60.193  30.388  1.00 21.45 ? 116  ARG A CG  1 
ATOM   753  C  CD  . ARG A 1 116  ? 47.068 61.506  30.774  1.00 26.83 ? 116  ARG A CD  1 
ATOM   754  N  NE  . ARG A 1 116  ? 46.521 61.402  32.134  1.00 31.94 ? 116  ARG A NE  1 
ATOM   755  C  CZ  . ARG A 1 116  ? 46.051 62.425  32.846  1.00 33.41 ? 116  ARG A CZ  1 
ATOM   756  N  NH1 . ARG A 1 116  ? 46.040 63.662  32.336  1.00 28.19 ? 116  ARG A NH1 1 
ATOM   757  N  NH2 . ARG A 1 116  ? 45.635 62.199  34.093  1.00 33.03 ? 116  ARG A NH2 1 
ATOM   758  N  N   A HIS A 1 117  ? 46.060 57.921  28.229  0.50 9.51  ? 117  HIS A N   1 
ATOM   759  N  N   B HIS A 1 117  ? 46.060 57.921  28.229  0.50 13.78 ? 117  HIS A N   1 
ATOM   760  C  CA  A HIS A 1 117  ? 45.029 57.023  28.701  0.50 9.54  ? 117  HIS A CA  1 
ATOM   761  C  CA  B HIS A 1 117  ? 45.029 57.023  28.701  0.50 14.90 ? 117  HIS A CA  1 
ATOM   762  C  C   A HIS A 1 117  ? 45.216 55.613  28.294  0.50 9.58  ? 117  HIS A C   1 
ATOM   763  C  C   B HIS A 1 117  ? 45.315 55.590  28.466  0.50 17.04 ? 117  HIS A C   1 
ATOM   764  O  O   A HIS A 1 117  ? 44.929 54.725  29.113  0.50 7.19  ? 117  HIS A O   1 
ATOM   765  O  O   B HIS A 1 117  ? 44.990 54.778  29.347  0.50 20.14 ? 117  HIS A O   1 
ATOM   766  C  CB  A HIS A 1 117  ? 43.669 57.551  28.320  0.50 9.81  ? 117  HIS A CB  1 
ATOM   767  C  CB  B HIS A 1 117  ? 43.689 57.436  28.146  0.50 16.62 ? 117  HIS A CB  1 
ATOM   768  C  CG  A HIS A 1 117  ? 43.245 58.696  29.191  0.50 12.07 ? 117  HIS A CG  1 
ATOM   769  C  CG  B HIS A 1 117  ? 42.582 57.234  29.137  0.50 13.03 ? 117  HIS A CG  1 
ATOM   770  N  ND1 A HIS A 1 117  ? 42.559 58.495  30.380  0.50 12.22 ? 117  HIS A ND1 1 
ATOM   771  N  ND1 B HIS A 1 117  ? 41.827 56.070  29.162  0.50 16.26 ? 117  HIS A ND1 1 
ATOM   772  C  CD2 A HIS A 1 117  ? 43.527 60.020  29.123  0.50 12.56 ? 117  HIS A CD2 1 
ATOM   773  C  CD2 B HIS A 1 117  ? 42.201 57.969  30.210  0.50 16.45 ? 117  HIS A CD2 1 
ATOM   774  C  CE1 A HIS A 1 117  ? 42.458 59.662  31.014  0.50 15.70 ? 117  HIS A CE1 1 
ATOM   775  C  CE1 B HIS A 1 117  ? 41.036 56.100  30.233  0.50 13.03 ? 117  HIS A CE1 1 
ATOM   776  N  NE2 A HIS A 1 117  ? 43.039 60.600  30.278  0.50 12.98 ? 117  HIS A NE2 1 
ATOM   777  N  NE2 B HIS A 1 117  ? 41.246 57.235  30.887  0.50 18.47 ? 117  HIS A NE2 1 
ATOM   778  N  N   . LEU A 1 118  ? 45.655 55.324  27.065  1.00 10.76 ? 118  LEU A N   1 
ATOM   779  C  CA  . LEU A 1 118  ? 45.910 53.951  26.677  1.00 10.97 ? 118  LEU A CA  1 
ATOM   780  C  C   . LEU A 1 118  ? 47.117 53.445  27.462  1.00 10.42 ? 118  LEU A C   1 
ATOM   781  O  O   . LEU A 1 118  ? 47.095 52.272  27.909  1.00 11.95 ? 118  LEU A O   1 
ATOM   782  C  CB  . LEU A 1 118  ? 46.180 53.858  25.122  1.00 10.52 ? 118  LEU A CB  1 
ATOM   783  C  CG  . LEU A 1 118  ? 44.887 54.255  24.336  1.00 14.73 ? 118  LEU A CG  1 
ATOM   784  C  CD1 . LEU A 1 118  ? 45.331 54.325  22.834  1.00 16.14 ? 118  LEU A CD1 1 
ATOM   785  C  CD2 . LEU A 1 118  ? 43.711 53.330  24.515  1.00 17.22 ? 118  LEU A CD2 1 
ATOM   786  N  N   . HIS A 1 119  ? 48.181 54.224  27.609  1.00 11.64 ? 119  HIS A N   1 
ATOM   787  C  CA  . HIS A 1 119  ? 49.329 53.734  28.390  1.00 11.44 ? 119  HIS A CA  1 
ATOM   788  C  C   . HIS A 1 119  ? 48.864 53.293  29.800  1.00 13.90 ? 119  HIS A C   1 
ATOM   789  O  O   . HIS A 1 119  ? 49.190 52.189  30.247  1.00 14.16 ? 119  HIS A O   1 
ATOM   790  C  CB  . HIS A 1 119  ? 50.340 54.859  28.549  1.00 14.29 ? 119  HIS A CB  1 
ATOM   791  C  CG  . HIS A 1 119  ? 51.496 54.541  29.424  1.00 18.50 ? 119  HIS A CG  1 
ATOM   792  N  ND1 . HIS A 1 119  ? 51.550 54.897  30.761  1.00 22.46 ? 119  HIS A ND1 1 
ATOM   793  C  CD2 . HIS A 1 119  ? 52.680 53.952  29.136  1.00 19.60 ? 119  HIS A CD2 1 
ATOM   794  C  CE1 . HIS A 1 119  ? 52.726 54.538  31.257  1.00 24.04 ? 119  HIS A CE1 1 
ATOM   795  N  NE2 . HIS A 1 119  ? 53.431 53.962  30.293  1.00 23.50 ? 119  HIS A NE2 1 
ATOM   796  N  N   . ASP A 1 120  ? 48.036 54.112  30.423  1.00 12.35 ? 120  ASP A N   1 
ATOM   797  C  CA  . ASP A 1 120  ? 47.603 53.821  31.811  1.00 14.16 ? 120  ASP A CA  1 
ATOM   798  C  C   . ASP A 1 120  ? 46.468 52.800  31.999  1.00 16.06 ? 120  ASP A C   1 
ATOM   799  O  O   . ASP A 1 120  ? 46.231 52.331  33.140  1.00 16.37 ? 120  ASP A O   1 
ATOM   800  C  CB  . ASP A 1 120  ? 47.148 55.119  32.472  1.00 14.72 ? 120  ASP A CB  1 
ATOM   801  C  CG  . ASP A 1 120  ? 48.299 56.062  32.765  1.00 19.58 ? 120  ASP A CG  1 
ATOM   802  O  OD1 . ASP A 1 120  ? 49.456 55.628  32.699  1.00 21.12 ? 120  ASP A OD1 1 
ATOM   803  O  OD2 . ASP A 1 120  ? 48.042 57.253  33.054  1.00 24.29 ? 120  ASP A OD2 1 
ATOM   804  N  N   . ASN A 1 121  ? 45.746 52.419  30.940  1.00 13.55 ? 121  ASN A N   1 
ATOM   805  C  CA  . ASN A 1 121  ? 44.565 51.540  30.999  1.00 13.14 ? 121  ASN A CA  1 
ATOM   806  C  C   . ASN A 1 121  ? 44.746 50.511  29.934  1.00 14.00 ? 121  ASN A C   1 
ATOM   807  O  O   . ASN A 1 121  ? 44.246 50.656  28.808  1.00 13.00 ? 121  ASN A O   1 
ATOM   808  C  CB  . ASN A 1 121  ? 43.260 52.345  30.790  1.00 12.52 ? 121  ASN A CB  1 
ATOM   809  C  CG  . ASN A 1 121  ? 43.094 53.422  31.849  1.00 14.43 ? 121  ASN A CG  1 
ATOM   810  O  OD1 . ASN A 1 121  ? 43.441 54.612  31.646  1.00 16.48 ? 121  ASN A OD1 1 
ATOM   811  N  ND2 . ASN A 1 121  ? 42.603 53.002  33.030  1.00 14.17 ? 121  ASN A ND2 1 
ATOM   812  N  N   . PRO A 1 122  ? 45.427 49.416  30.249  1.00 12.50 ? 122  PRO A N   1 
ATOM   813  C  CA  . PRO A 1 122  ? 45.733 48.367  29.268  1.00 14.00 ? 122  PRO A CA  1 
ATOM   814  C  C   . PRO A 1 122  ? 44.636 47.752  28.463  1.00 13.11 ? 122  PRO A C   1 
ATOM   815  O  O   . PRO A 1 122  ? 44.903 47.238  27.329  1.00 15.40 ? 122  PRO A O   1 
ATOM   816  C  CB  . PRO A 1 122  ? 46.532 47.314  30.082  1.00 15.75 ? 122  PRO A CB  1 
ATOM   817  C  CG  . PRO A 1 122  ? 47.114 48.159  31.213  1.00 17.71 ? 122  PRO A CG  1 
ATOM   818  C  CD  . PRO A 1 122  ? 45.984 49.096  31.598  1.00 14.94 ? 122  PRO A CD  1 
ATOM   819  N  N   . GLU A 1 123  ? 43.408 47.747  28.979  1.00 13.83 ? 123  GLU A N   1 
ATOM   820  C  CA  . GLU A 1 123  ? 42.314 47.158  28.225  1.00 14.18 ? 123  GLU A CA  1 
ATOM   821  C  C   . GLU A 1 123  ? 41.590 48.148  27.294  1.00 13.06 ? 123  GLU A C   1 
ATOM   822  O  O   . GLU A 1 123  ? 40.761 47.720  26.514  1.00 14.87 ? 123  GLU A O   1 
ATOM   823  C  CB  . GLU A 1 123  ? 41.254 46.519  29.149  1.00 18.20 ? 123  GLU A CB  1 
ATOM   824  C  CG  . GLU A 1 123  ? 41.788 45.294  29.968  1.00 29.63 ? 123  GLU A CG  1 
ATOM   825  C  CD  . GLU A 1 123  ? 42.280 44.131  29.098  1.00 37.72 ? 123  GLU A CD  1 
ATOM   826  O  OE1 . GLU A 1 123  ? 41.468 43.494  28.365  1.00 42.86 ? 123  GLU A OE1 1 
ATOM   827  O  OE2 . GLU A 1 123  ? 43.503 43.852  29.150  1.00 43.52 ? 123  GLU A OE2 1 
ATOM   828  N  N   . MET A 1 124  ? 41.889 49.446  27.432  1.00 12.64 ? 124  MET A N   1 
ATOM   829  C  CA  . MET A 1 124  ? 41.249 50.451  26.574  1.00 10.78 ? 124  MET A CA  1 
ATOM   830  C  C   . MET A 1 124  ? 41.882 50.347  25.164  1.00 11.60 ? 124  MET A C   1 
ATOM   831  O  O   . MET A 1 124  ? 43.061 50.012  25.030  1.00 11.51 ? 124  MET A O   1 
ATOM   832  C  CB  . MET A 1 124  ? 41.500 51.836  27.167  1.00 12.53 ? 124  MET A CB  1 
ATOM   833  C  CG  . MET A 1 124  ? 40.688 52.985  26.505  1.00 13.54 ? 124  MET A CG  1 
ATOM   834  S  SD  . MET A 1 124  ? 38.923 52.597  26.388  1.00 13.50 ? 124  MET A SD  1 
ATOM   835  C  CE  . MET A 1 124  ? 38.339 54.069  25.547  1.00 15.28 ? 124  MET A CE  1 
ATOM   836  N  N   . LYS A 1 125  ? 41.064 50.685  24.152  1.00 10.74 ? 125  LYS A N   1 
ATOM   837  C  CA  . LYS A 1 125  ? 41.469 50.594  22.748  1.00 10.19 ? 125  LYS A CA  1 
ATOM   838  C  C   . LYS A 1 125  ? 41.070 51.860  22.050  1.00 11.11 ? 125  LYS A C   1 
ATOM   839  O  O   . LYS A 1 125  ? 40.222 52.615  22.520  1.00 10.54 ? 125  LYS A O   1 
ATOM   840  C  CB  . LYS A 1 125  ? 40.729 49.432  22.099  1.00 12.23 ? 125  LYS A CB  1 
ATOM   841  C  CG  . LYS A 1 125  ? 40.890 48.061  22.741  1.00 16.00 ? 125  LYS A CG  1 
ATOM   842  C  CD  . LYS A 1 125  ? 42.279 47.536  22.465  1.00 17.29 ? 125  LYS A CD  1 
ATOM   843  C  CE  . LYS A 1 125  ? 42.690 46.189  23.149  1.00 26.78 ? 125  LYS A CE  1 
ATOM   844  N  NZ  . LYS A 1 125  ? 41.621 45.229  23.052  1.00 26.61 ? 125  LYS A NZ  1 
ATOM   845  N  N   . PHE A 1 126  ? 41.671 52.086  20.855  1.00 9.36  ? 126  PHE A N   1 
ATOM   846  C  CA  . PHE A 1 126  ? 41.341 53.322  20.105  1.00 9.09  ? 126  PHE A CA  1 
ATOM   847  C  C   . PHE A 1 126  ? 41.814 53.068  18.659  1.00 8.97  ? 126  PHE A C   1 
ATOM   848  O  O   . PHE A 1 126  ? 42.844 52.441  18.454  1.00 10.12 ? 126  PHE A O   1 
ATOM   849  C  CB  . PHE A 1 126  ? 42.131 54.521  20.683  1.00 9.66  ? 126  PHE A CB  1 
ATOM   850  C  CG  . PHE A 1 126  ? 41.726 55.871  20.170  1.00 8.27  ? 126  PHE A CG  1 
ATOM   851  C  CD1 . PHE A 1 126  ? 40.409 56.318  20.210  1.00 9.41  ? 126  PHE A CD1 1 
ATOM   852  C  CD2 . PHE A 1 126  ? 42.750 56.778  19.803  1.00 11.00 ? 126  PHE A CD2 1 
ATOM   853  C  CE1 . PHE A 1 126  ? 40.099 57.698  19.891  1.00 9.74  ? 126  PHE A CE1 1 
ATOM   854  C  CE2 . PHE A 1 126  ? 42.466 58.110  19.504  1.00 10.51 ? 126  PHE A CE2 1 
ATOM   855  C  CZ  . PHE A 1 126  ? 41.164 58.572  19.546  1.00 8.46  ? 126  PHE A CZ  1 
ATOM   856  N  N   . ILE A 1 127  ? 41.069 53.566  17.693  1.00 8.20  ? 127  ILE A N   1 
ATOM   857  C  CA  . ILE A 1 127  ? 41.505 53.433  16.290  1.00 8.08  ? 127  ILE A CA  1 
ATOM   858  C  C   . ILE A 1 127  ? 41.762 54.826  15.718  1.00 8.43  ? 127  ILE A C   1 
ATOM   859  O  O   . ILE A 1 127  ? 41.139 55.824  16.134  1.00 9.03  ? 127  ILE A O   1 
ATOM   860  C  CB  . ILE A 1 127  ? 40.522 52.673  15.373  1.00 8.28  ? 127  ILE A CB  1 
ATOM   861  C  CG1 . ILE A 1 127  ? 39.136 53.294  15.390  1.00 8.75  ? 127  ILE A CG1 1 
ATOM   862  C  CG2 . ILE A 1 127  ? 40.427 51.142  15.802  1.00 9.80  ? 127  ILE A CG2 1 
ATOM   863  C  CD1 . ILE A 1 127  ? 38.142 52.738  14.274  1.00 9.27  ? 127  ILE A CD1 1 
ATOM   864  N  N   . TRP A 1 128  ? 42.692 54.897  14.767  1.00 8.77  ? 128  TRP A N   1 
ATOM   865  C  CA  . TRP A 1 128  ? 43.102 56.201  14.168  1.00 8.23  ? 128  TRP A CA  1 
ATOM   866  C  C   . TRP A 1 128  ? 43.228 56.025  12.649  1.00 7.77  ? 128  TRP A C   1 
ATOM   867  O  O   . TRP A 1 128  ? 43.891 55.093  12.201  1.00 7.78  ? 128  TRP A O   1 
ATOM   868  C  CB  . TRP A 1 128  ? 44.426 56.674  14.756  1.00 8.55  ? 128  TRP A CB  1 
ATOM   869  C  CG  . TRP A 1 128  ? 44.703 58.093  14.391  1.00 8.10  ? 128  TRP A CG  1 
ATOM   870  C  CD1 . TRP A 1 128  ? 45.456 58.574  13.334  1.00 8.92  ? 128  TRP A CD1 1 
ATOM   871  C  CD2 . TRP A 1 128  ? 44.129 59.216  15.013  1.00 7.07  ? 128  TRP A CD2 1 
ATOM   872  N  NE1 . TRP A 1 128  ? 45.330 59.955  13.275  1.00 8.95  ? 128  TRP A NE1 1 
ATOM   873  C  CE2 . TRP A 1 128  ? 44.532 60.362  14.307  1.00 8.16  ? 128  TRP A CE2 1 
ATOM   874  C  CE3 . TRP A 1 128  ? 43.256 59.353  16.135  1.00 9.09  ? 128  TRP A CE3 1 
ATOM   875  C  CZ2 . TRP A 1 128  ? 44.121 61.648  14.671  1.00 9.30  ? 128  TRP A CZ2 1 
ATOM   876  C  CZ3 . TRP A 1 128  ? 42.856 60.621  16.481  1.00 9.67  ? 128  TRP A CZ3 1 
ATOM   877  C  CH2 . TRP A 1 128  ? 43.293 61.760  15.755  1.00 9.73  ? 128  TRP A CH2 1 
ATOM   878  N  N   . ALA A 1 129  ? 42.673 56.981  11.909  1.00 8.82  ? 129  ALA A N   1 
ATOM   879  C  CA  . ALA A 1 129  ? 42.725 56.887  10.440  1.00 8.86  ? 129  ALA A CA  1 
ATOM   880  C  C   . ALA A 1 129  ? 43.644 57.851  9.702   1.00 10.33 ? 129  ALA A C   1 
ATOM   881  O  O   . ALA A 1 129  ? 44.239 57.453  8.696   1.00 11.47 ? 129  ALA A O   1 
ATOM   882  C  CB  . ALA A 1 129  ? 41.307 57.171  9.886   1.00 10.32 ? 129  ALA A CB  1 
ATOM   883  N  N   . GLU A 1 130  ? 43.744 59.108  10.153  1.00 10.01 ? 130  GLU A N   1 
ATOM   884  C  CA  . GLU A 1 130  ? 44.452 60.178  9.324   1.00 9.43  ? 130  GLU A CA  1 
ATOM   885  C  C   . GLU A 1 130  ? 45.929 60.311  9.660   1.00 9.35  ? 130  GLU A C   1 
ATOM   886  O  O   . GLU A 1 130  ? 46.308 60.882  10.748  1.00 9.75  ? 130  GLU A O   1 
ATOM   887  C  CB  . GLU A 1 130  ? 43.774 61.531  9.531   1.00 12.21 ? 130  GLU A CB  1 
ATOM   888  C  CG  . GLU A 1 130  ? 42.262 61.535  9.219   1.00 13.63 ? 130  GLU A CG  1 
ATOM   889  C  CD  . GLU A 1 130  ? 41.434 60.966  10.295  1.00 16.37 ? 130  GLU A CD  1 
ATOM   890  O  OE1 . GLU A 1 130  ? 41.912 60.786  11.476  1.00 16.79 ? 130  GLU A OE1 1 
ATOM   891  O  OE2 . GLU A 1 130  ? 40.228 60.673  10.042  1.00 20.94 ? 130  GLU A OE2 1 
ATOM   892  N  N   . ILE A 1 131  ? 46.798 59.822  8.797   1.00 8.57  ? 131  ILE A N   1 
ATOM   893  C  CA  . ILE A 1 131  ? 48.223 59.847  9.090   1.00 8.63  ? 131  ILE A CA  1 
ATOM   894  C  C   . ILE A 1 131  ? 48.783 61.246  8.921   1.00 9.96  ? 131  ILE A C   1 
ATOM   895  O  O   . ILE A 1 131  ? 49.823 61.561  9.566   1.00 10.70 ? 131  ILE A O   1 
ATOM   896  C  CB  . ILE A 1 131  ? 48.974 58.757  8.276   1.00 9.30  ? 131  ILE A CB  1 
ATOM   897  C  CG1 . ILE A 1 131  ? 48.322 57.398  8.595   1.00 9.33  ? 131  ILE A CG1 1 
ATOM   898  C  CG2 . ILE A 1 131  ? 50.461 58.753  8.587   1.00 10.60 ? 131  ILE A CG2 1 
ATOM   899  C  CD1 . ILE A 1 131  ? 48.233 57.049  10.122  1.00 11.39 ? 131  ILE A CD1 1 
ATOM   900  N  N   . SER A 1 132  ? 48.180 62.135  8.160   1.00 8.13  ? 132  SER A N   1 
ATOM   901  C  CA  . SER A 1 132  ? 48.703 63.509  8.104   1.00 7.62  ? 132  SER A CA  1 
ATOM   902  C  C   . SER A 1 132  ? 48.764 64.099  9.547   1.00 7.90  ? 132  SER A C   1 
ATOM   903  O  O   . SER A 1 132  ? 49.820 64.680  9.925   1.00 9.29  ? 132  SER A O   1 
ATOM   904  C  CB  . SER A 1 132  ? 47.773 64.356  7.231   1.00 8.63  ? 132  SER A CB  1 
ATOM   905  O  OG  . SER A 1 132  ? 46.395 64.282  7.662   1.00 8.81  ? 132  SER A OG  1 
ATOM   906  N  N   . TYR A 1 133  ? 47.706 63.901  10.332  1.00 7.97  ? 133  TYR A N   1 
ATOM   907  C  CA  . TYR A 1 133  ? 47.724 64.391  11.727  1.00 8.35  ? 133  TYR A CA  1 
ATOM   908  C  C   . TYR A 1 133  ? 48.673 63.540  12.592  1.00 9.97  ? 133  TYR A C   1 
ATOM   909  O  O   . TYR A 1 133  ? 49.393 64.126  13.437  1.00 10.83 ? 133  TYR A O   1 
ATOM   910  C  CB  . TYR A 1 133  ? 46.339 64.303  12.366  1.00 9.20  ? 133  TYR A CB  1 
ATOM   911  C  CG  . TYR A 1 133  ? 45.437 65.452  12.014  1.00 7.82  ? 133  TYR A CG  1 
ATOM   912  C  CD1 . TYR A 1 133  ? 44.173 65.241  11.517  1.00 8.30  ? 133  TYR A CD1 1 
ATOM   913  C  CD2 . TYR A 1 133  ? 45.877 66.782  12.262  1.00 9.29  ? 133  TYR A CD2 1 
ATOM   914  C  CE1 . TYR A 1 133  ? 43.298 66.302  11.291  1.00 8.75  ? 133  TYR A CE1 1 
ATOM   915  C  CE2 . TYR A 1 133  ? 45.030 67.860  12.017  1.00 9.80  ? 133  TYR A CE2 1 
ATOM   916  C  CZ  . TYR A 1 133  ? 43.734 67.586  11.540  1.00 9.66  ? 133  TYR A CZ  1 
ATOM   917  O  OH  . TYR A 1 133  ? 42.912 68.679  11.285  1.00 11.41 ? 133  TYR A OH  1 
ATOM   918  N  N   . PHE A 1 134  ? 48.662 62.228  12.437  1.00 8.27  ? 134  PHE A N   1 
ATOM   919  C  CA  . PHE A 1 134  ? 49.469 61.426  13.339  1.00 8.33  ? 134  PHE A CA  1 
ATOM   920  C  C   . PHE A 1 134  ? 50.966 61.727  13.124  1.00 9.26  ? 134  PHE A C   1 
ATOM   921  O  O   . PHE A 1 134  ? 51.733 61.826  14.112  1.00 10.20 ? 134  PHE A O   1 
ATOM   922  C  CB  . PHE A 1 134  ? 49.182 59.943  13.132  1.00 8.27  ? 134  PHE A CB  1 
ATOM   923  C  CG  . PHE A 1 134  ? 49.771 59.096  14.243  1.00 9.91  ? 134  PHE A CG  1 
ATOM   924  C  CD1 . PHE A 1 134  ? 49.055 58.911  15.449  1.00 10.32 ? 134  PHE A CD1 1 
ATOM   925  C  CD2 . PHE A 1 134  ? 51.038 58.586  14.139  1.00 11.08 ? 134  PHE A CD2 1 
ATOM   926  C  CE1 . PHE A 1 134  ? 49.647 58.207  16.535  1.00 10.42 ? 134  PHE A CE1 1 
ATOM   927  C  CE2 . PHE A 1 134  ? 51.651 57.877  15.219  1.00 12.18 ? 134  PHE A CE2 1 
ATOM   928  C  CZ  . PHE A 1 134  ? 50.910 57.711  16.416  1.00 12.20 ? 134  PHE A CZ  1 
ATOM   929  N  N   . ALA A 1 135  ? 51.417 61.873  11.875  1.00 10.12 ? 135  ALA A N   1 
ATOM   930  C  CA  . ALA A 1 135  ? 52.842 62.171  11.601  1.00 10.35 ? 135  ALA A CA  1 
ATOM   931  C  C   . ALA A 1 135  ? 53.157 63.572  12.189  1.00 11.81 ? 135  ALA A C   1 
ATOM   932  O  O   . ALA A 1 135  ? 54.275 63.728  12.773  1.00 15.58 ? 135  ALA A O   1 
ATOM   933  C  CB  . ALA A 1 135  ? 53.096 62.147  10.115  1.00 12.05 ? 135  ALA A CB  1 
ATOM   934  N  N   . ARG A 1 136  ? 52.265 64.522  12.070  1.00 11.29 ? 136  ARG A N   1 
ATOM   935  C  CA  . ARG A 1 136  ? 52.486 65.908  12.607  1.00 13.88 ? 136  ARG A CA  1 
ATOM   936  C  C   . ARG A 1 136  ? 52.717 65.780  14.144  1.00 15.36 ? 136  ARG A C   1 
ATOM   937  O  O   . ARG A 1 136  ? 53.680 66.366  14.710  1.00 19.57 ? 136  ARG A O   1 
ATOM   938  C  CB  . ARG A 1 136  ? 51.247 66.768  12.339  1.00 15.50 ? 136  ARG A CB  1 
ATOM   939  C  CG  . ARG A 1 136  ? 51.230 68.196  13.002  1.00 16.53 ? 136  ARG A CG  1 
ATOM   940  C  CD  . ARG A 1 136  ? 51.903 69.258  12.091  1.00 19.52 ? 136  ARG A CD  1 
ATOM   941  N  NE  . ARG A 1 136  ? 51.899 70.624  12.681  1.00 18.38 ? 136  ARG A NE  1 
ATOM   942  C  CZ  . ARG A 1 136  ? 52.676 70.912  13.704  1.00 18.22 ? 136  ARG A CZ  1 
ATOM   943  N  NH1 . ARG A 1 136  ? 53.507 69.967  14.173  1.00 19.39 ? 136  ARG A NH1 1 
ATOM   944  N  NH2 . ARG A 1 136  ? 52.512 72.066  14.355  1.00 15.28 ? 136  ARG A NH2 1 
ATOM   945  N  N   . PHE A 1 137  ? 51.904 64.970  14.831  1.00 11.46 ? 137  PHE A N   1 
ATOM   946  C  CA  . PHE A 1 137  ? 51.990 64.768  16.263  1.00 10.83 ? 137  PHE A CA  1 
ATOM   947  C  C   . PHE A 1 137  ? 53.241 64.023  16.636  1.00 10.38 ? 137  PHE A C   1 
ATOM   948  O  O   . PHE A 1 137  ? 54.019 64.453  17.541  1.00 13.15 ? 137  PHE A O   1 
ATOM   949  C  CB  . PHE A 1 137  ? 50.766 63.979  16.679  1.00 10.52 ? 137  PHE A CB  1 
ATOM   950  C  CG  . PHE A 1 137  ? 50.724 63.721  18.148  1.00 11.97 ? 137  PHE A CG  1 
ATOM   951  C  CD1 . PHE A 1 137  ? 50.449 64.787  19.025  1.00 12.66 ? 137  PHE A CD1 1 
ATOM   952  C  CD2 . PHE A 1 137  ? 50.978 62.473  18.635  1.00 12.79 ? 137  PHE A CD2 1 
ATOM   953  C  CE1 . PHE A 1 137  ? 50.421 64.597  20.386  1.00 15.99 ? 137  PHE A CE1 1 
ATOM   954  C  CE2 . PHE A 1 137  ? 50.970 62.277  20.081  1.00 15.12 ? 137  PHE A CE2 1 
ATOM   955  C  CZ  . PHE A 1 137  ? 50.681 63.355  20.903  1.00 14.37 ? 137  PHE A CZ  1 
ATOM   956  N  N   . TYR A 1 138  ? 53.499 62.881  16.011  1.00 11.65 ? 138  TYR A N   1 
ATOM   957  C  CA  . TYR A 1 138  ? 54.592 61.998  16.372  1.00 13.12 ? 138  TYR A CA  1 
ATOM   958  C  C   . TYR A 1 138  ? 55.950 62.687  16.217  1.00 15.10 ? 138  TYR A C   1 
ATOM   959  O  O   . TYR A 1 138  ? 56.816 62.559  17.117  1.00 14.64 ? 138  TYR A O   1 
ATOM   960  C  CB  . TYR A 1 138  ? 54.555 60.701  15.522  1.00 13.77 ? 138  TYR A CB  1 
ATOM   961  C  CG  . TYR A 1 138  ? 55.617 59.687  15.910  1.00 13.59 ? 138  TYR A CG  1 
ATOM   962  C  CD1 . TYR A 1 138  ? 55.362 58.789  16.913  1.00 14.15 ? 138  TYR A CD1 1 
ATOM   963  C  CD2 . TYR A 1 138  ? 56.834 59.630  15.251  1.00 15.33 ? 138  TYR A CD2 1 
ATOM   964  C  CE1 . TYR A 1 138  ? 56.293 57.824  17.291  1.00 17.50 ? 138  TYR A CE1 1 
ATOM   965  C  CE2 . TYR A 1 138  ? 57.810 58.649  15.615  1.00 13.59 ? 138  TYR A CE2 1 
ATOM   966  C  CZ  . TYR A 1 138  ? 57.494 57.762  16.636  1.00 14.84 ? 138  TYR A CZ  1 
ATOM   967  O  OH  . TYR A 1 138  ? 58.380 56.746  16.991  1.00 19.06 ? 138  TYR A OH  1 
ATOM   968  N  N   . HIS A 1 139  ? 56.126 63.473  15.162  1.00 14.29 ? 139  HIS A N   1 
ATOM   969  C  CA  . HIS A 1 139  ? 57.437 64.091  14.987  1.00 17.87 ? 139  HIS A CA  1 
ATOM   970  C  C   . HIS A 1 139  ? 57.692 65.150  16.073  1.00 20.07 ? 139  HIS A C   1 
ATOM   971  O  O   . HIS A 1 139  ? 58.857 65.510  16.351  1.00 23.41 ? 139  HIS A O   1 
ATOM   972  C  CB  . HIS A 1 139  ? 57.540 64.634  13.552  1.00 19.49 ? 139  HIS A CB  1 
ATOM   973  C  CG  . HIS A 1 139  ? 57.767 63.548  12.538  1.00 23.07 ? 139  HIS A CG  1 
ATOM   974  N  ND1 . HIS A 1 139  ? 58.856 62.689  12.596  1.00 29.12 ? 139  HIS A ND1 1 
ATOM   975  C  CD2 . HIS A 1 139  ? 57.054 63.185  11.437  1.00 24.70 ? 139  HIS A CD2 1 
ATOM   976  C  CE1 . HIS A 1 139  ? 58.804 61.858  11.561  1.00 29.51 ? 139  HIS A CE1 1 
ATOM   977  N  NE2 . HIS A 1 139  ? 57.727 62.144  10.838  1.00 25.74 ? 139  HIS A NE2 1 
ATOM   978  N  N   . ASP A 1 140  ? 56.648 65.681  16.681  1.00 15.20 ? 140  ASP A N   1 
ATOM   979  C  CA  . ASP A 1 140  ? 56.809 66.690  17.758  1.00 16.87 ? 140  ASP A CA  1 
ATOM   980  C  C   . ASP A 1 140  ? 56.986 66.059  19.160  1.00 15.72 ? 140  ASP A C   1 
ATOM   981  O  O   . ASP A 1 140  ? 57.328 66.782  20.125  1.00 17.66 ? 140  ASP A O   1 
ATOM   982  C  CB  . ASP A 1 140  ? 55.621 67.639  17.813  1.00 18.77 ? 140  ASP A CB  1 
ATOM   983  C  CG  . ASP A 1 140  ? 55.753 68.794  16.855  1.00 26.28 ? 140  ASP A CG  1 
ATOM   984  O  OD1 . ASP A 1 140  ? 56.613 68.716  15.982  1.00 25.68 ? 140  ASP A OD1 1 
ATOM   985  O  OD2 . ASP A 1 140  ? 54.992 69.775  17.011  1.00 27.15 ? 140  ASP A OD2 1 
ATOM   986  N  N   . LEU A 1 141  ? 56.795 64.764  19.288  1.00 15.35 ? 141  LEU A N   1 
ATOM   987  C  CA  . LEU A 1 141  ? 56.993 64.086  20.584  1.00 14.01 ? 141  LEU A CA  1 
ATOM   988  C  C   . LEU A 1 141  ? 58.450 63.893  20.944  1.00 15.49 ? 141  LEU A C   1 
ATOM   989  O  O   . LEU A 1 141  ? 59.275 63.655  20.100  1.00 15.82 ? 141  LEU A O   1 
ATOM   990  C  CB  . LEU A 1 141  ? 56.420 62.647  20.556  1.00 14.07 ? 141  LEU A CB  1 
ATOM   991  C  CG  . LEU A 1 141  ? 54.906 62.488  20.560  1.00 16.90 ? 141  LEU A CG  1 
ATOM   992  C  CD1 . LEU A 1 141  ? 54.617 60.945  20.487  1.00 14.32 ? 141  LEU A CD1 1 
ATOM   993  C  CD2 . LEU A 1 141  ? 54.265 63.156  21.818  1.00 14.91 ? 141  LEU A CD2 1 
ATOM   994  N  N   . GLY A 1 142  ? 58.742 63.998  22.254  1.00 17.17 ? 142  GLY A N   1 
ATOM   995  C  CA  . GLY A 1 142  ? 60.076 63.665  22.729  1.00 17.14 ? 142  GLY A CA  1 
ATOM   996  C  C   . GLY A 1 142  ? 60.265 62.144  22.601  1.00 17.82 ? 142  GLY A C   1 
ATOM   997  O  O   . GLY A 1 142  ? 59.283 61.363  22.458  1.00 16.73 ? 142  GLY A O   1 
ATOM   998  N  N   . GLU A 1 143  ? 61.495 61.684  22.623  1.00 17.05 ? 143  GLU A N   1 
ATOM   999  C  CA  . GLU A 1 143  ? 61.837 60.281  22.467  1.00 17.78 ? 143  GLU A CA  1 
ATOM   1000 C  C   . GLU A 1 143  ? 61.151 59.358  23.468  1.00 17.01 ? 143  GLU A C   1 
ATOM   1001 O  O   . GLU A 1 143  ? 60.701 58.246  23.097  1.00 16.77 ? 143  GLU A O   1 
ATOM   1002 C  CB  . GLU A 1 143  ? 63.365 60.086  22.514  1.00 22.88 ? 143  GLU A CB  1 
ATOM   1003 C  CG  . GLU A 1 143  ? 63.858 58.747  21.964  1.00 24.67 ? 143  GLU A CG  1 
ATOM   1004 C  CD  . GLU A 1 143  ? 63.571 58.541  20.458  1.00 31.96 ? 143  GLU A CD  1 
ATOM   1005 O  OE1 . GLU A 1 143  ? 63.411 59.525  19.687  1.00 31.33 ? 143  GLU A OE1 1 
ATOM   1006 O  OE2 . GLU A 1 143  ? 63.533 57.372  20.043  1.00 36.28 ? 143  GLU A OE2 1 
ATOM   1007 N  N   . ASN A 1 144  ? 61.016 59.773  24.727  1.00 16.94 ? 144  ASN A N   1 
ATOM   1008 C  CA  . ASN A 1 144  ? 60.379 58.901  25.702  1.00 18.44 ? 144  ASN A CA  1 
ATOM   1009 C  C   . ASN A 1 144  ? 58.925 58.580  25.274  1.00 15.97 ? 144  ASN A C   1 
ATOM   1010 O  O   . ASN A 1 144  ? 58.492 57.396  25.296  1.00 16.48 ? 144  ASN A O   1 
ATOM   1011 C  CB  . ASN A 1 144  ? 60.461 59.574  27.098  1.00 21.08 ? 144  ASN A CB  1 
ATOM   1012 C  CG  . ASN A 1 144  ? 59.721 58.810  28.189  1.00 31.68 ? 144  ASN A CG  1 
ATOM   1013 O  OD1 . ASN A 1 144  ? 58.491 58.897  28.302  1.00 34.78 ? 144  ASN A OD1 1 
ATOM   1014 N  ND2 . ASN A 1 144  ? 60.465 58.041  28.994  1.00 32.42 ? 144  ASN A ND2 1 
ATOM   1015 N  N   . LYS A 1 145  ? 58.210 59.620  24.871  1.00 16.09 ? 145  LYS A N   1 
ATOM   1016 C  CA  . LYS A 1 145  ? 56.832 59.468  24.429  1.00 14.38 ? 145  LYS A CA  1 
ATOM   1017 C  C   . LYS A 1 145  ? 56.764 58.753  23.064  1.00 13.89 ? 145  LYS A C   1 
ATOM   1018 O  O   . LYS A 1 145  ? 55.816 58.008  22.877  1.00 14.22 ? 145  LYS A O   1 
ATOM   1019 C  CB  . LYS A 1 145  ? 56.145 60.840  24.381  1.00 16.95 ? 145  LYS A CB  1 
ATOM   1020 C  CG  . LYS A 1 145  ? 55.932 61.484  25.767  1.00 21.24 ? 145  LYS A CG  1 
ATOM   1021 C  CD  . LYS A 1 145  ? 55.001 60.686  26.638  1.00 31.33 ? 145  LYS A CD  1 
ATOM   1022 C  CE  . LYS A 1 145  ? 54.657 61.497  27.923  1.00 33.74 ? 145  LYS A CE  1 
ATOM   1023 N  NZ  . LYS A 1 145  ? 55.813 62.283  28.484  1.00 41.73 ? 145  LYS A NZ  1 
ATOM   1024 N  N   . LYS A 1 146  ? 57.716 58.959  22.153  1.00 13.91 ? 146  LYS A N   1 
ATOM   1025 C  CA  . LYS A 1 146  ? 57.702 58.203  20.869  1.00 13.90 ? 146  LYS A CA  1 
ATOM   1026 C  C   . LYS A 1 146  ? 57.740 56.743  21.246  1.00 14.02 ? 146  LYS A C   1 
ATOM   1027 O  O   . LYS A 1 146  ? 56.989 55.926  20.674  1.00 14.06 ? 146  LYS A O   1 
ATOM   1028 C  CB  . LYS A 1 146  ? 58.904 58.499  19.951  1.00 13.36 ? 146  LYS A CB  1 
ATOM   1029 C  CG  . LYS A 1 146  ? 58.841 59.841  19.248  1.00 13.83 ? 146  LYS A CG  1 
ATOM   1030 C  CD  . LYS A 1 146  ? 59.993 59.954  18.262  1.00 13.72 ? 146  LYS A CD  1 
ATOM   1031 C  CE  . LYS A 1 146  ? 59.855 61.074  17.227  1.00 15.04 ? 146  LYS A CE  1 
ATOM   1032 N  NZ  . LYS A 1 146  ? 60.005 62.384  17.881  1.00 19.35 ? 146  LYS A NZ  1 
ATOM   1033 N  N   . LEU A 1 147  ? 58.595 56.348  22.209  1.00 15.31 ? 147  LEU A N   1 
ATOM   1034 C  CA  . LEU A 1 147  ? 58.698 54.948  22.607  1.00 14.25 ? 147  LEU A CA  1 
ATOM   1035 C  C   . LEU A 1 147  ? 57.400 54.425  23.251  1.00 12.79 ? 147  LEU A C   1 
ATOM   1036 O  O   . LEU A 1 147  ? 56.995 53.304  22.943  1.00 13.33 ? 147  LEU A O   1 
ATOM   1037 C  CB  . LEU A 1 147  ? 59.950 54.751  23.536  1.00 15.50 ? 147  LEU A CB  1 
ATOM   1038 C  CG  . LEU A 1 147  ? 61.300 54.908  22.827  1.00 18.74 ? 147  LEU A CG  1 
ATOM   1039 C  CD1 . LEU A 1 147  ? 62.447 54.946  23.854  1.00 20.77 ? 147  LEU A CD1 1 
ATOM   1040 C  CD2 . LEU A 1 147  ? 61.494 53.747  21.908  1.00 21.20 ? 147  LEU A CD2 1 
ATOM   1041 N  N   . GLN A 1 148  ? 56.735 55.226  24.093  1.00 13.40 ? 148  GLN A N   1 
ATOM   1042 C  CA  . GLN A 1 148  ? 55.492 54.789  24.686  1.00 12.71 ? 148  GLN A CA  1 
ATOM   1043 C  C   . GLN A 1 148  ? 54.459 54.583  23.562  1.00 12.59 ? 148  GLN A C   1 
ATOM   1044 O  O   . GLN A 1 148  ? 53.675 53.646  23.634  1.00 13.64 ? 148  GLN A O   1 
ATOM   1045 C  CB  . GLN A 1 148  ? 54.962 55.820  25.660  1.00 14.73 ? 148  GLN A CB  1 
ATOM   1046 C  CG  . GLN A 1 148  ? 55.775 55.948  26.912  1.00 19.14 ? 148  GLN A CG  1 
ATOM   1047 C  CD  . GLN A 1 148  ? 55.074 56.781  27.965  1.00 26.68 ? 148  GLN A CD  1 
ATOM   1048 O  OE1 . GLN A 1 148  ? 55.604 56.944  29.099  1.00 30.69 ? 148  GLN A OE1 1 
ATOM   1049 N  NE2 . GLN A 1 148  ? 53.890 57.294  27.640  1.00 24.51 ? 148  GLN A NE2 1 
ATOM   1050 N  N   . MET A 1 149  ? 54.449 55.486  22.571  1.00 12.71 ? 149  MET A N   1 
ATOM   1051 C  CA  . MET A 1 149  ? 53.480 55.385  21.458  1.00 11.05 ? 149  MET A CA  1 
ATOM   1052 C  C   . MET A 1 149  ? 53.733 54.129  20.643  1.00 11.75 ? 149  MET A C   1 
ATOM   1053 O  O   . MET A 1 149  ? 52.785 53.415  20.321  1.00 12.09 ? 149  MET A O   1 
ATOM   1054 C  CB  . MET A 1 149  ? 53.582 56.657  20.599  1.00 13.14 ? 149  MET A CB  1 
ATOM   1055 C  CG  . MET A 1 149  ? 52.588 56.678  19.411  1.00 12.09 ? 149  MET A CG  1 
ATOM   1056 S  SD  . MET A 1 149  ? 50.902 56.793  19.961  1.00 14.74 ? 149  MET A SD  1 
ATOM   1057 C  CE  . MET A 1 149  ? 50.725 58.551  20.071  1.00 21.46 ? 149  MET A CE  1 
ATOM   1058 N  N   . LYS A 1 150  ? 55.000 53.831  20.340  1.00 11.75 ? 150  LYS A N   1 
ATOM   1059 C  CA  . LYS A 1 150  ? 55.290 52.641  19.565  1.00 12.60 ? 150  LYS A CA  1 
ATOM   1060 C  C   . LYS A 1 150  ? 54.835 51.405  20.363  1.00 11.79 ? 150  LYS A C   1 
ATOM   1061 O  O   . LYS A 1 150  ? 54.335 50.435  19.764  1.00 14.35 ? 150  LYS A O   1 
ATOM   1062 C  CB  . LYS A 1 150  ? 56.778 52.490  19.242  1.00 14.00 ? 150  LYS A CB  1 
ATOM   1063 C  CG  . LYS A 1 150  ? 57.280 53.475  18.235  1.00 16.30 ? 150  LYS A CG  1 
ATOM   1064 C  CD  . LYS A 1 150  ? 58.639 53.079  17.771  1.00 23.99 ? 150  LYS A CD  1 
ATOM   1065 C  CE  . LYS A 1 150  ? 59.607 54.104  18.148  1.00 29.69 ? 150  LYS A CE  1 
ATOM   1066 N  NZ  . LYS A 1 150  ? 60.953 53.785  17.604  1.00 34.53 ? 150  LYS A NZ  1 
ATOM   1067 N  N   . SER A 1 151  ? 54.948 51.425  21.699  1.00 12.61 ? 151  SER A N   1 
ATOM   1068 C  CA  . SER A 1 151  ? 54.531 50.274  22.493  1.00 13.98 ? 151  SER A CA  1 
ATOM   1069 C  C   . SER A 1 151  ? 53.016 50.039  22.466  1.00 11.58 ? 151  SER A C   1 
ATOM   1070 O  O   . SER A 1 151  ? 52.576 48.885  22.359  1.00 13.37 ? 151  SER A O   1 
ATOM   1071 C  CB  . SER A 1 151  ? 54.987 50.471  23.957  1.00 15.75 ? 151  SER A CB  1 
ATOM   1072 O  OG  . SER A 1 151  ? 54.815 49.215  24.618  1.00 21.34 ? 151  SER A OG  1 
ATOM   1073 N  N   . ILE A 1 152  ? 52.200 51.101  22.596  1.00 12.06 ? 152  ILE A N   1 
ATOM   1074 C  CA  . ILE A 1 152  ? 50.746 50.905  22.543  1.00 11.69 ? 152  ILE A CA  1 
ATOM   1075 C  C   . ILE A 1 152  ? 50.263 50.489  21.149  1.00 11.06 ? 152  ILE A C   1 
ATOM   1076 O  O   . ILE A 1 152  ? 49.199 49.919  21.043  1.00 12.50 ? 152  ILE A O   1 
ATOM   1077 C  CB  . ILE A 1 152  ? 49.895 52.101  23.124  1.00 11.27 ? 152  ILE A CB  1 
ATOM   1078 C  CG1 . ILE A 1 152  ? 50.171 53.413  22.409  1.00 12.35 ? 152  ILE A CG1 1 
ATOM   1079 C  CG2 . ILE A 1 152  ? 50.180 52.221  24.672  1.00 13.46 ? 152  ILE A CG2 1 
ATOM   1080 C  CD1 . ILE A 1 152  ? 49.100 54.480  22.727  1.00 13.37 ? 152  ILE A CD1 1 
ATOM   1081 N  N   . VAL A 1 153  ? 51.039 50.796  20.101  1.00 11.26 ? 153  VAL A N   1 
ATOM   1082 C  CA  . VAL A 1 153  ? 50.698 50.326  18.741  1.00 11.48 ? 153  VAL A CA  1 
ATOM   1083 C  C   . VAL A 1 153  ? 51.137 48.866  18.616  1.00 12.51 ? 153  VAL A C   1 
ATOM   1084 O  O   . VAL A 1 153  ? 50.363 48.002  18.192  1.00 13.38 ? 153  VAL A O   1 
ATOM   1085 C  CB  . VAL A 1 153  ? 51.359 51.207  17.717  1.00 11.95 ? 153  VAL A CB  1 
ATOM   1086 C  CG1 . VAL A 1 153  ? 51.236 50.582  16.288  1.00 12.90 ? 153  VAL A CG1 1 
ATOM   1087 C  CG2 . VAL A 1 153  ? 50.726 52.587  17.775  1.00 12.08 ? 153  VAL A CG2 1 
ATOM   1088 N  N   . LYS A 1 154  ? 52.363 48.586  19.042  1.00 13.19 ? 154  LYS A N   1 
ATOM   1089 C  CA  . LYS A 1 154  ? 52.877 47.214  18.891  1.00 14.71 ? 154  LYS A CA  1 
ATOM   1090 C  C   . LYS A 1 154  ? 52.019 46.210  19.686  1.00 14.40 ? 154  LYS A C   1 
ATOM   1091 O  O   . LYS A 1 154  ? 51.816 45.056  19.234  1.00 17.22 ? 154  LYS A O   1 
ATOM   1092 C  CB  . LYS A 1 154  ? 54.348 47.158  19.347  1.00 16.20 ? 154  LYS A CB  1 
ATOM   1093 C  CG  . LYS A 1 154  ? 55.008 45.767  19.129  1.00 20.75 ? 154  LYS A CG  1 
ATOM   1094 C  CD  . LYS A 1 154  ? 56.501 45.896  19.437  1.00 22.98 ? 154  LYS A CD  1 
ATOM   1095 C  CE  . LYS A 1 154  ? 57.287 44.653  18.992  1.00 28.81 ? 154  LYS A CE  1 
ATOM   1096 N  NZ  . LYS A 1 154  ? 57.327 44.501  17.480  1.00 28.39 ? 154  LYS A NZ  1 
ATOM   1097 N  N   . ASN A 1 155  ? 51.483 46.622  20.825  1.00 14.34 ? 155  ASN A N   1 
ATOM   1098 C  CA  . ASN A 1 155  ? 50.651 45.752  21.721  1.00 15.60 ? 155  ASN A CA  1 
ATOM   1099 C  C   . ASN A 1 155  ? 49.149 45.740  21.347  1.00 16.09 ? 155  ASN A C   1 
ATOM   1100 O  O   . ASN A 1 155  ? 48.331 45.088  22.008  1.00 16.96 ? 155  ASN A O   1 
ATOM   1101 C  CB  . ASN A 1 155  ? 50.814 46.144  23.247  1.00 21.67 ? 155  ASN A CB  1 
ATOM   1102 C  CG  . ASN A 1 155  ? 49.913 47.404  23.686  1.00 24.06 ? 155  ASN A CG  1 
ATOM   1103 O  OD1 . ASN A 1 155  ? 49.156 47.875  22.877  1.00 26.36 ? 155  ASN A OD1 1 
ATOM   1104 N  ND2 . ASN A 1 155  ? 50.009 47.923  24.953  1.00 19.75 ? 155  ASN A ND2 1 
ATOM   1105 N  N   . GLY A 1 156  ? 48.765 46.490  20.321  1.00 13.44 ? 156  GLY A N   1 
ATOM   1106 C  CA  . GLY A 1 156  ? 47.375 46.418  19.850  1.00 14.25 ? 156  GLY A CA  1 
ATOM   1107 C  C   . GLY A 1 156  ? 46.358 47.309  20.502  1.00 14.92 ? 156  GLY A C   1 
ATOM   1108 O  O   . GLY A 1 156  ? 45.182 47.179  20.172  1.00 16.14 ? 156  GLY A O   1 
ATOM   1109 N  N   . GLN A 1 157  ? 46.744 48.237  21.364  1.00 12.19 ? 157  GLN A N   1 
ATOM   1110 C  CA  . GLN A 1 157  ? 45.772 49.119  21.973  1.00 11.75 ? 157  GLN A CA  1 
ATOM   1111 C  C   . GLN A 1 157  ? 45.368 50.239  21.008  1.00 10.21 ? 157  GLN A C   1 
ATOM   1112 O  O   . GLN A 1 157  ? 44.212 50.561  20.935  1.00 10.62 ? 157  GLN A O   1 
ATOM   1113 C  CB  . GLN A 1 157  ? 46.323 49.762  23.243  1.00 10.10 ? 157  GLN A CB  1 
ATOM   1114 C  CG  . GLN A 1 157  ? 46.279 48.814  24.443  1.00 12.12 ? 157  GLN A CG  1 
ATOM   1115 C  CD  . GLN A 1 157  ? 46.597 49.604  25.676  1.00 10.11 ? 157  GLN A CD  1 
ATOM   1116 O  OE1 . GLN A 1 157  ? 45.730 50.298  26.258  1.00 13.14 ? 157  GLN A OE1 1 
ATOM   1117 N  NE2 . GLN A 1 157  ? 47.871 49.594  26.006  1.00 10.21 ? 157  GLN A NE2 1 
ATOM   1118 N  N   . LEU A 1 158  ? 46.343 50.848  20.336  1.00 10.72 ? 158  LEU A N   1 
ATOM   1119 C  CA  . LEU A 1 158  ? 46.057 51.908  19.342  1.00 10.22 ? 158  LEU A CA  1 
ATOM   1120 C  C   . LEU A 1 158  ? 46.263 51.216  17.983  1.00 10.58 ? 158  LEU A C   1 
ATOM   1121 O  O   . LEU A 1 158  ? 47.355 50.717  17.694  1.00 11.97 ? 158  LEU A O   1 
ATOM   1122 C  CB  . LEU A 1 158  ? 47.068 53.038  19.518  1.00 11.77 ? 158  LEU A CB  1 
ATOM   1123 C  CG  . LEU A 1 158  ? 47.008 54.102  18.440  1.00 17.00 ? 158  LEU A CG  1 
ATOM   1124 C  CD1 . LEU A 1 158  ? 45.710 54.735  18.471  1.00 15.83 ? 158  LEU A CD1 1 
ATOM   1125 C  CD2 . LEU A 1 158  ? 48.208 55.114  18.686  1.00 17.31 ? 158  LEU A CD2 1 
ATOM   1126 N  N   . GLU A 1 159  ? 45.231 51.219  17.153  1.00 9.09  ? 159  GLU A N   1 
ATOM   1127 C  CA  . GLU A 1 159  ? 45.344 50.570  15.844  1.00 8.91  ? 159  GLU A CA  1 
ATOM   1128 C  C   . GLU A 1 159  ? 45.025 51.544  14.736  1.00 8.91  ? 159  GLU A C   1 
ATOM   1129 O  O   . GLU A 1 159  ? 44.014 52.270  14.762  1.00 9.21  ? 159  GLU A O   1 
ATOM   1130 C  CB  . GLU A 1 159  ? 44.322 49.422  15.812  1.00 10.90 ? 159  GLU A CB  1 
ATOM   1131 C  CG  . GLU A 1 159  ? 44.310 48.662  14.501  1.00 11.21 ? 159  GLU A CG  1 
ATOM   1132 C  CD  . GLU A 1 159  ? 43.301 47.541  14.556  1.00 13.47 ? 159  GLU A CD  1 
ATOM   1133 O  OE1 . GLU A 1 159  ? 43.640 46.516  15.258  1.00 14.61 ? 159  GLU A OE1 1 
ATOM   1134 O  OE2 . GLU A 1 159  ? 42.211 47.707  13.953  1.00 12.61 ? 159  GLU A OE2 1 
ATOM   1135 N  N   . PHE A 1 160  ? 45.891 51.544  13.732  1.00 8.90  ? 160  PHE A N   1 
ATOM   1136 C  CA  . PHE A 1 160  ? 45.645 52.375  12.549  1.00 8.17  ? 160  PHE A CA  1 
ATOM   1137 C  C   . PHE A 1 160  ? 44.697 51.644  11.609  1.00 8.71  ? 160  PHE A C   1 
ATOM   1138 O  O   . PHE A 1 160  ? 44.848 50.444  11.341  1.00 9.08  ? 160  PHE A O   1 
ATOM   1139 C  CB  . PHE A 1 160  ? 46.983 52.708  11.866  1.00 8.41  ? 160  PHE A CB  1 
ATOM   1140 C  CG  . PHE A 1 160  ? 47.867 53.536  12.745  1.00 8.94  ? 160  PHE A CG  1 
ATOM   1141 C  CD1 . PHE A 1 160  ? 48.944 52.950  13.434  1.00 10.16 ? 160  PHE A CD1 1 
ATOM   1142 C  CD2 . PHE A 1 160  ? 47.587 54.896  12.940  1.00 9.44  ? 160  PHE A CD2 1 
ATOM   1143 C  CE1 . PHE A 1 160  ? 49.709 53.757  14.283  1.00 10.44 ? 160  PHE A CE1 1 
ATOM   1144 C  CE2 . PHE A 1 160  ? 48.358 55.676  13.817  1.00 10.58 ? 160  PHE A CE2 1 
ATOM   1145 C  CZ  . PHE A 1 160  ? 49.388 55.101  14.451  1.00 11.75 ? 160  PHE A CZ  1 
ATOM   1146 N  N   . VAL A 1 161  ? 43.738 52.407  11.123  1.00 7.15  ? 161  VAL A N   1 
ATOM   1147 C  CA  . VAL A 1 161  ? 42.730 51.914  10.189  1.00 7.77  ? 161  VAL A CA  1 
ATOM   1148 C  C   . VAL A 1 161  ? 42.930 52.705  8.902   1.00 7.26  ? 161  VAL A C   1 
ATOM   1149 O  O   . VAL A 1 161  ? 43.057 53.943  8.906   1.00 9.35  ? 161  VAL A O   1 
ATOM   1150 C  CB  . VAL A 1 161  ? 41.269 52.001  10.764  1.00 7.10  ? 161  VAL A CB  1 
ATOM   1151 C  CG1 . VAL A 1 161  ? 41.138 50.983  11.914  1.00 9.29  ? 161  VAL A CG1 1 
ATOM   1152 C  CG2 . VAL A 1 161  ? 40.946 53.381  11.270  1.00 8.66  ? 161  VAL A CG2 1 
ATOM   1153 N  N   . THR A 1 162  ? 43.009 51.962  7.792   1.00 7.64  ? 162  THR A N   1 
ATOM   1154 C  CA  . THR A 1 162  ? 43.345 52.474  6.432   1.00 7.76  ? 162  THR A CA  1 
ATOM   1155 C  C   . THR A 1 162  ? 44.828 52.929  6.403   1.00 6.94  ? 162  THR A C   1 
ATOM   1156 O  O   . THR A 1 162  ? 45.649 52.354  5.685   1.00 9.19  ? 162  THR A O   1 
ATOM   1157 C  CB  . THR A 1 162  ? 42.459 53.631  5.923   1.00 8.73  ? 162  THR A CB  1 
ATOM   1158 O  OG1 . THR A 1 162  ? 41.073 53.269  6.016   1.00 10.34 ? 162  THR A OG1 1 
ATOM   1159 C  CG2 . THR A 1 162  ? 42.759 53.888  4.383   1.00 10.55 ? 162  THR A CG2 1 
ATOM   1160 N  N   . GLY A 1 163  ? 45.155 53.962  7.153   1.00 7.97  ? 163  GLY A N   1 
ATOM   1161 C  CA  . GLY A 1 163  ? 46.533 54.401  7.165   1.00 9.08  ? 163  GLY A CA  1 
ATOM   1162 C  C   . GLY A 1 163  ? 46.885 55.324  6.035   1.00 7.72  ? 163  GLY A C   1 
ATOM   1163 O  O   . GLY A 1 163  ? 48.056 55.519  5.741   1.00 9.18  ? 163  GLY A O   1 
ATOM   1164 N  N   . GLY A 1 164  ? 45.874 55.902  5.361   1.00 7.18  ? 164  GLY A N   1 
ATOM   1165 C  CA  . GLY A 1 164  ? 46.192 56.928  4.362   1.00 7.91  ? 164  GLY A CA  1 
ATOM   1166 C  C   . GLY A 1 164  ? 46.502 58.278  4.979   1.00 7.58  ? 164  GLY A C   1 
ATOM   1167 O  O   . GLY A 1 164  ? 46.256 58.530  6.189   1.00 7.60  ? 164  GLY A O   1 
ATOM   1168 N  N   . TRP A 1 165  ? 47.095 59.164  4.176   1.00 6.60  ? 165  TRP A N   1 
ATOM   1169 C  CA  . TRP A 1 165  ? 47.331 60.530  4.675   1.00 5.91  ? 165  TRP A CA  1 
ATOM   1170 C  C   . TRP A 1 165  ? 46.024 61.152  5.150   1.00 6.68  ? 165  TRP A C   1 
ATOM   1171 O  O   . TRP A 1 165  ? 46.018 61.897  6.159   1.00 7.12  ? 165  TRP A O   1 
ATOM   1172 C  CB  . TRP A 1 165  ? 47.999 61.345  3.520   1.00 6.19  ? 165  TRP A CB  1 
ATOM   1173 C  CG  . TRP A 1 165  ? 48.762 62.510  3.974   1.00 6.64  ? 165  TRP A CG  1 
ATOM   1174 C  CD1 . TRP A 1 165  ? 48.529 63.809  3.664   1.00 8.84  ? 165  TRP A CD1 1 
ATOM   1175 C  CD2 . TRP A 1 165  ? 49.966 62.470  4.769   1.00 8.42  ? 165  TRP A CD2 1 
ATOM   1176 N  NE1 . TRP A 1 165  ? 49.529 64.627  4.241   1.00 9.89  ? 165  TRP A NE1 1 
ATOM   1177 C  CE2 . TRP A 1 165  ? 50.395 63.824  4.915   1.00 8.24  ? 165  TRP A CE2 1 
ATOM   1178 C  CE3 . TRP A 1 165  ? 50.703 61.437  5.351   1.00 8.71  ? 165  TRP A CE3 1 
ATOM   1179 C  CZ2 . TRP A 1 165  ? 51.565 64.181  5.678   1.00 10.84 ? 165  TRP A CZ2 1 
ATOM   1180 C  CZ3 . TRP A 1 165  ? 51.892 61.798  6.098   1.00 12.39 ? 165  TRP A CZ3 1 
ATOM   1181 C  CH2 . TRP A 1 165  ? 52.275 63.147  6.235   1.00 12.14 ? 165  TRP A CH2 1 
ATOM   1182 N  N   . VAL A 1 166  ? 44.936 60.852  4.420   1.00 6.59  ? 166  VAL A N   1 
ATOM   1183 C  CA  . VAL A 1 166  ? 43.600 61.339  4.752   1.00 6.43  ? 166  VAL A CA  1 
ATOM   1184 C  C   . VAL A 1 166  ? 42.600 60.213  4.563   1.00 6.96  ? 166  VAL A C   1 
ATOM   1185 O  O   . VAL A 1 166  ? 42.957 59.080  4.276   1.00 7.43  ? 166  VAL A O   1 
ATOM   1186 C  CB  . VAL A 1 166  ? 43.170 62.561  3.827   1.00 7.00  ? 166  VAL A CB  1 
ATOM   1187 C  CG1 . VAL A 1 166  ? 44.204 63.698  3.941   1.00 7.65  ? 166  VAL A CG1 1 
ATOM   1188 C  CG2 . VAL A 1 166  ? 43.094 62.082  2.343   1.00 7.91  ? 166  VAL A CG2 1 
ATOM   1189 N  N   . MET A 1 167  ? 41.339 60.544  4.810   1.00 7.27  ? 167  MET A N   1 
ATOM   1190 C  CA  . MET A 1 167  ? 40.190 59.646  4.477   1.00 6.53  ? 167  MET A CA  1 
ATOM   1191 C  C   . MET A 1 167  ? 39.635 60.389  3.244   1.00 7.48  ? 167  MET A C   1 
ATOM   1192 O  O   . MET A 1 167  ? 38.865 61.343  3.366   1.00 8.18  ? 167  MET A O   1 
ATOM   1193 C  CB  . MET A 1 167  ? 39.224 59.619  5.648   1.00 7.75  ? 167  MET A CB  1 
ATOM   1194 C  CG  . MET A 1 167  ? 37.921 58.810  5.340   1.00 8.41  ? 167  MET A CG  1 
ATOM   1195 S  SD  . MET A 1 167  ? 36.739 58.962  6.733   1.00 9.28  ? 167  MET A SD  1 
ATOM   1196 C  CE  . MET A 1 167  ? 37.739 58.197  8.083   1.00 10.27 ? 167  MET A CE  1 
ATOM   1197 N  N   . PRO A 1 168  ? 39.957 59.914  2.058   1.00 6.38  ? 168  PRO A N   1 
ATOM   1198 C  CA  . PRO A 1 168  ? 39.567 60.683  0.875   1.00 8.38  ? 168  PRO A CA  1 
ATOM   1199 C  C   . PRO A 1 168  ? 38.164 60.709  0.431   1.00 7.41  ? 168  PRO A C   1 
ATOM   1200 O  O   . PRO A 1 168  ? 37.416 59.753  0.703   1.00 7.50  ? 168  PRO A O   1 
ATOM   1201 C  CB  . PRO A 1 168  ? 40.480 60.069  -0.244  1.00 7.90  ? 168  PRO A CB  1 
ATOM   1202 C  CG  . PRO A 1 168  ? 40.586 58.623  0.181   1.00 8.31  ? 168  PRO A CG  1 
ATOM   1203 C  CD  . PRO A 1 168  ? 40.766 58.705  1.717   1.00 7.25  ? 168  PRO A CD  1 
ATOM   1204 N  N   . ASP A 1 169  ? 37.807 61.804  -0.238  1.00 7.24  ? 169  ASP A N   1 
ATOM   1205 C  CA  . ASP A 1 169  ? 36.577 61.806  -1.031  1.00 7.66  ? 169  ASP A CA  1 
ATOM   1206 C  C   . ASP A 1 169  ? 36.700 60.635  -2.012  1.00 6.78  ? 169  ASP A C   1 
ATOM   1207 O  O   . ASP A 1 169  ? 37.808 60.255  -2.470  1.00 7.48  ? 169  ASP A O   1 
ATOM   1208 C  CB  . ASP A 1 169  ? 36.561 63.095  -1.839  1.00 7.70  ? 169  ASP A CB  1 
ATOM   1209 C  CG  . ASP A 1 169  ? 35.373 63.170  -2.790  1.00 8.16  ? 169  ASP A CG  1 
ATOM   1210 O  OD1 . ASP A 1 169  ? 34.278 62.690  -2.471  1.00 8.41  ? 169  ASP A OD1 1 
ATOM   1211 O  OD2 . ASP A 1 169  ? 35.523 63.752  -3.865  1.00 10.25 ? 169  ASP A OD2 1 
ATOM   1212 N  N   . GLU A 1 170  ? 35.565 60.018  -2.342  1.00 6.86  ? 170  GLU A N   1 
ATOM   1213 C  CA  . GLU A 1 170  ? 35.531 58.906  -3.284  1.00 6.10  ? 170  GLU A CA  1 
ATOM   1214 C  C   . GLU A 1 170  ? 34.808 59.273  -4.580  1.00 7.07  ? 170  GLU A C   1 
ATOM   1215 O  O   . GLU A 1 170  ? 34.802 58.475  -5.534  1.00 7.19  ? 170  GLU A O   1 
ATOM   1216 C  CB  . GLU A 1 170  ? 34.854 57.670  -2.632  1.00 7.87  ? 170  GLU A CB  1 
ATOM   1217 C  CG  . GLU A 1 170  ? 35.692 57.219  -1.375  1.00 8.75  ? 170  GLU A CG  1 
ATOM   1218 C  CD  . GLU A 1 170  ? 35.190 55.989  -0.675  1.00 9.78  ? 170  GLU A CD  1 
ATOM   1219 O  OE1 . GLU A 1 170  ? 34.429 55.218  -1.324  1.00 9.14  ? 170  GLU A OE1 1 
ATOM   1220 O  OE2 . GLU A 1 170  ? 35.580 55.779  0.525   1.00 10.50 ? 170  GLU A OE2 1 
ATOM   1221 N  N   . ALA A 1 171  ? 34.234 60.461  -4.665  1.00 6.70  ? 171  ALA A N   1 
ATOM   1222 C  CA  . ALA A 1 171  ? 33.517 60.829  -5.880  1.00 6.30  ? 171  ALA A CA  1 
ATOM   1223 C  C   . ALA A 1 171  ? 34.372 61.592  -6.910  1.00 6.80  ? 171  ALA A C   1 
ATOM   1224 O  O   . ALA A 1 171  ? 34.372 61.323  -8.105  1.00 7.73  ? 171  ALA A O   1 
ATOM   1225 C  CB  . ALA A 1 171  ? 32.295 61.733  -5.507  1.00 8.55  ? 171  ALA A CB  1 
ATOM   1226 N  N   . ASN A 1 172  ? 35.088 62.625  -6.420  1.00 6.90  ? 172  ASN A N   1 
ATOM   1227 C  CA  . ASN A 1 172  ? 35.818 63.509  -7.333  1.00 6.50  ? 172  ASN A CA  1 
ATOM   1228 C  C   . ASN A 1 172  ? 37.287 63.129  -7.504  1.00 6.67  ? 172  ASN A C   1 
ATOM   1229 O  O   . ASN A 1 172  ? 37.960 63.593  -8.413  1.00 7.34  ? 172  ASN A O   1 
ATOM   1230 C  CB  . ASN A 1 172  ? 35.763 64.928  -6.751  1.00 7.47  ? 172  ASN A CB  1 
ATOM   1231 C  CG  . ASN A 1 172  ? 34.362 65.464  -6.622  1.00 9.87  ? 172  ASN A CG  1 
ATOM   1232 O  OD1 . ASN A 1 172  ? 33.680 65.684  -7.619  1.00 10.99 ? 172  ASN A OD1 1 
ATOM   1233 N  ND2 . ASN A 1 172  ? 33.954 65.769  -5.406  1.00 10.23 ? 172  ASN A ND2 1 
ATOM   1234 N  N   . SER A 1 173  ? 37.814 62.349  -6.576  1.00 6.29  ? 173  SER A N   1 
ATOM   1235 C  CA  . SER A 1 173  ? 39.245 61.990  -6.560  1.00 6.60  ? 173  SER A CA  1 
ATOM   1236 C  C   . SER A 1 173  ? 39.632 61.089  -7.691  1.00 6.20  ? 173  SER A C   1 
ATOM   1237 O  O   . SER A 1 173  ? 38.890 60.175  -8.091  1.00 8.00  ? 173  SER A O   1 
ATOM   1238 C  CB  . SER A 1 173  ? 39.579 61.331  -5.240  1.00 6.84  ? 173  SER A CB  1 
ATOM   1239 O  OG  . SER A 1 173  ? 38.651 60.210  -5.050  1.00 7.75  ? 173  SER A OG  1 
ATOM   1240 N  N   . HIS A 1 174  ? 40.794 61.350  -8.266  1.00 5.77  ? 174  HIS A N   1 
ATOM   1241 C  CA  . HIS A 1 174  ? 41.313 60.445  -9.287  1.00 5.46  ? 174  HIS A CA  1 
ATOM   1242 C  C   . HIS A 1 174  ? 41.971 59.235  -8.571  1.00 5.16  ? 174  HIS A C   1 
ATOM   1243 O  O   . HIS A 1 174  ? 42.610 59.428  -7.542  1.00 6.12  ? 174  HIS A O   1 
ATOM   1244 C  CB  . HIS A 1 174  ? 42.360 61.169  -10.131 1.00 6.73  ? 174  HIS A CB  1 
ATOM   1245 C  CG  . HIS A 1 174  ? 42.604 60.495  -11.417 1.00 6.30  ? 174  HIS A CG  1 
ATOM   1246 N  ND1 . HIS A 1 174  ? 43.368 59.340  -11.536 1.00 8.10  ? 174  HIS A ND1 1 
ATOM   1247 C  CD2 . HIS A 1 174  ? 42.134 60.806  -12.648 1.00 7.91  ? 174  HIS A CD2 1 
ATOM   1248 C  CE1 . HIS A 1 174  ? 43.334 58.972  -12.813 1.00 9.84  ? 174  HIS A CE1 1 
ATOM   1249 N  NE2 . HIS A 1 174  ? 42.596 59.831  -13.492 1.00 9.73  ? 174  HIS A NE2 1 
ATOM   1250 N  N   . TRP A 1 175  ? 41.821 58.041  -9.150  1.00 5.54  ? 175  TRP A N   1 
ATOM   1251 C  CA  . TRP A 1 175  ? 42.410 56.861  -8.515  1.00 5.89  ? 175  TRP A CA  1 
ATOM   1252 C  C   . TRP A 1 175  ? 43.909 57.045  -8.290  1.00 6.06  ? 175  TRP A C   1 
ATOM   1253 O  O   . TRP A 1 175  ? 44.425 56.530  -7.278  1.00 6.84  ? 175  TRP A O   1 
ATOM   1254 C  CB  . TRP A 1 175  ? 42.122 55.595  -9.315  1.00 5.74  ? 175  TRP A CB  1 
ATOM   1255 C  CG  . TRP A 1 175  ? 42.937 55.411  -10.570 1.00 6.42  ? 175  TRP A CG  1 
ATOM   1256 C  CD1 . TRP A 1 175  ? 42.611 55.782  -11.872 1.00 6.06  ? 175  TRP A CD1 1 
ATOM   1257 C  CD2 . TRP A 1 175  ? 44.221 54.772  -10.652 1.00 6.67  ? 175  TRP A CD2 1 
ATOM   1258 N  NE1 . TRP A 1 175  ? 43.643 55.400  -12.726 1.00 7.17  ? 175  TRP A NE1 1 
ATOM   1259 C  CE2 . TRP A 1 175  ? 44.627 54.771  -11.992 1.00 6.72  ? 175  TRP A CE2 1 
ATOM   1260 C  CE3 . TRP A 1 175  ? 45.079 54.184  -9.685  1.00 7.79  ? 175  TRP A CE3 1 
ATOM   1261 C  CZ2 . TRP A 1 175  ? 45.879 54.206  -12.424 1.00 8.36  ? 175  TRP A CZ2 1 
ATOM   1262 C  CZ3 . TRP A 1 175  ? 46.301 53.626  -10.111 1.00 9.15  ? 175  TRP A CZ3 1 
ATOM   1263 C  CH2 . TRP A 1 175  ? 46.680 53.651  -11.485 1.00 9.36  ? 175  TRP A CH2 1 
ATOM   1264 N  N   . ARG A 1 176  ? 44.607 57.760  -9.194  1.00 6.67  ? 176  ARG A N   1 
ATOM   1265 C  CA  . ARG A 1 176  ? 46.057 57.923  -8.997  1.00 6.87  ? 176  ARG A CA  1 
ATOM   1266 C  C   . ARG A 1 176  ? 46.304 58.674  -7.696  1.00 5.74  ? 176  ARG A C   1 
ATOM   1267 O  O   . ARG A 1 176  ? 47.310 58.401  -7.000  1.00 6.86  ? 176  ARG A O   1 
ATOM   1268 C  CB  . ARG A 1 176  ? 46.651 58.691  -10.213 1.00 7.77  ? 176  ARG A CB  1 
ATOM   1269 C  CG  . ARG A 1 176  ? 46.642 57.813  -11.459 1.00 9.78  ? 176  ARG A CG  1 
ATOM   1270 C  CD  . ARG A 1 176  ? 46.601 58.636  -12.762 1.00 12.40 ? 176  ARG A CD  1 
ATOM   1271 N  NE  . ARG A 1 176  ? 47.703 59.546  -12.870 1.00 12.14 ? 176  ARG A NE  1 
ATOM   1272 C  CZ  . ARG A 1 176  ? 47.851 60.401  -13.907 1.00 10.20 ? 176  ARG A CZ  1 
ATOM   1273 N  NH1 . ARG A 1 176  ? 46.913 60.392  -14.870 1.00 12.58 ? 176  ARG A NH1 1 
ATOM   1274 N  NH2 . ARG A 1 176  ? 48.799 61.309  -13.876 1.00 12.17 ? 176  ARG A NH2 1 
ATOM   1275 N  N   . ASN A 1 177  ? 45.457 59.654  -7.347  1.00 5.64  ? 177  ASN A N   1 
ATOM   1276 C  CA  . ASN A 1 177  ? 45.669 60.402  -6.110  1.00 5.78  ? 177  ASN A CA  1 
ATOM   1277 C  C   . ASN A 1 177  ? 45.163 59.681  -4.882  1.00 6.54  ? 177  ASN A C   1 
ATOM   1278 O  O   . ASN A 1 177  ? 45.701 59.887  -3.778  1.00 6.90  ? 177  ASN A O   1 
ATOM   1279 C  CB  . ASN A 1 177  ? 45.076 61.828  -6.220  1.00 6.38  ? 177  ASN A CB  1 
ATOM   1280 C  CG  . ASN A 1 177  ? 45.754 62.639  -7.256  1.00 7.80  ? 177  ASN A CG  1 
ATOM   1281 O  OD1 . ASN A 1 177  ? 46.922 62.431  -7.583  1.00 8.17  ? 177  ASN A OD1 1 
ATOM   1282 N  ND2 . ASN A 1 177  ? 44.967 63.582  -7.818  1.00 10.17 ? 177  ASN A ND2 1 
ATOM   1283 N  N   . VAL A 1 178  ? 44.184 58.816  -5.043  1.00 7.08  ? 178  VAL A N   1 
ATOM   1284 C  CA  . VAL A 1 178  ? 43.751 58.002  -3.911  1.00 6.59  ? 178  VAL A CA  1 
ATOM   1285 C  C   . VAL A 1 178  ? 44.960 57.068  -3.586  1.00 6.16  ? 178  VAL A C   1 
ATOM   1286 O  O   . VAL A 1 178  ? 45.294 56.870  -2.401  1.00 7.21  ? 178  VAL A O   1 
ATOM   1287 C  CB  . VAL A 1 178  ? 42.530 57.129  -4.296  1.00 6.90  ? 178  VAL A CB  1 
ATOM   1288 C  CG1 . VAL A 1 178  ? 42.200 56.134  -3.190  1.00 8.37  ? 178  VAL A CG1 1 
ATOM   1289 C  CG2 . VAL A 1 178  ? 41.302 58.028  -4.502  1.00 8.78  ? 178  VAL A CG2 1 
ATOM   1290 N  N   . LEU A 1 179  ? 45.611 56.513  -4.609  1.00 5.83  ? 179  LEU A N   1 
ATOM   1291 C  CA  . LEU A 1 179  ? 46.760 55.674  -4.339  1.00 6.88  ? 179  LEU A CA  1 
ATOM   1292 C  C   . LEU A 1 179  ? 47.926 56.503  -3.768  1.00 6.83  ? 179  LEU A C   1 
ATOM   1293 O  O   . LEU A 1 179  ? 48.583 56.044  -2.808  1.00 7.53  ? 179  LEU A O   1 
ATOM   1294 C  CB  . LEU A 1 179  ? 47.201 54.995  -5.667  1.00 6.56  ? 179  LEU A CB  1 
ATOM   1295 C  CG  . LEU A 1 179  ? 48.533 54.173  -5.492  1.00 7.13  ? 179  LEU A CG  1 
ATOM   1296 C  CD1 . LEU A 1 179  ? 48.435 53.061  -4.412  1.00 8.83  ? 179  LEU A CD1 1 
ATOM   1297 C  CD2 . LEU A 1 179  ? 48.886 53.535  -6.859  1.00 9.95  ? 179  LEU A CD2 1 
ATOM   1298 N  N   . LEU A 1 180  ? 48.137 57.718  -4.257  1.00 5.89  ? 180  LEU A N   1 
ATOM   1299 C  CA  . LEU A 1 180  ? 49.230 58.563  -3.779  1.00 6.19  ? 180  LEU A CA  1 
ATOM   1300 C  C   . LEU A 1 180  ? 49.061 58.813  -2.281  1.00 5.79  ? 180  LEU A C   1 
ATOM   1301 O  O   . LEU A 1 180  ? 50.040 58.608  -1.487  1.00 7.17  ? 180  LEU A O   1 
ATOM   1302 C  CB  . LEU A 1 180  ? 49.219 59.884  -4.550  1.00 7.55  ? 180  LEU A CB  1 
ATOM   1303 C  CG  . LEU A 1 180  ? 50.349 60.851  -4.147  1.00 8.23  ? 180  LEU A CG  1 
ATOM   1304 C  CD1 . LEU A 1 180  ? 51.603 60.364  -4.801  1.00 11.43 ? 180  LEU A CD1 1 
ATOM   1305 C  CD2 . LEU A 1 180  ? 49.979 62.244  -4.679  1.00 10.65 ? 180  LEU A CD2 1 
ATOM   1306 N  N   . GLN A 1 181  ? 47.846 59.186  -1.852  1.00 6.28  ? 181  GLN A N   1 
ATOM   1307 C  CA  . GLN A 1 181  ? 47.690 59.513  -0.431  1.00 6.72  ? 181  GLN A CA  1 
ATOM   1308 C  C   . GLN A 1 181  ? 47.758 58.264  0.449   1.00 6.05  ? 181  GLN A C   1 
ATOM   1309 O  O   . GLN A 1 181  ? 48.269 58.325  1.598   1.00 6.68  ? 181  GLN A O   1 
ATOM   1310 C  CB  . GLN A 1 181  ? 46.421 60.353  -0.203  1.00 6.60  ? 181  GLN A CB  1 
ATOM   1311 C  CG  . GLN A 1 181  ? 45.119 59.612  -0.430  1.00 6.68  ? 181  GLN A CG  1 
ATOM   1312 C  CD  . GLN A 1 181  ? 44.728 58.705  0.701   1.00 7.03  ? 181  GLN A CD  1 
ATOM   1313 O  OE1 . GLN A 1 181  ? 45.001 58.983  1.884   1.00 8.29  ? 181  GLN A OE1 1 
ATOM   1314 N  NE2 . GLN A 1 181  ? 44.052 57.603  0.360   1.00 7.98  ? 181  GLN A NE2 1 
ATOM   1315 N  N   . LEU A 1 182  ? 47.246 57.132  -0.045  1.00 6.86  ? 182  LEU A N   1 
ATOM   1316 C  CA  . LEU A 1 182  ? 47.350 55.885  0.696   1.00 6.60  ? 182  LEU A CA  1 
ATOM   1317 C  C   . LEU A 1 182  ? 48.821 55.533  0.899   1.00 6.70  ? 182  LEU A C   1 
ATOM   1318 O  O   . LEU A 1 182  ? 49.243 55.143  2.002   1.00 7.33  ? 182  LEU A O   1 
ATOM   1319 C  CB  . LEU A 1 182  ? 46.633 54.762  -0.071  1.00 7.11  ? 182  LEU A CB  1 
ATOM   1320 C  CG  . LEU A 1 182  ? 46.730 53.428  0.640   1.00 6.91  ? 182  LEU A CG  1 
ATOM   1321 C  CD1 . LEU A 1 182  ? 45.912 53.371  1.964   1.00 9.52  ? 182  LEU A CD1 1 
ATOM   1322 C  CD2 . LEU A 1 182  ? 46.145 52.340  -0.309  1.00 8.91  ? 182  LEU A CD2 1 
ATOM   1323 N  N   . THR A 1 183  ? 49.609 55.676  -0.150  1.00 6.84  ? 183  THR A N   1 
ATOM   1324 C  CA  . THR A 1 183  ? 51.032 55.335  -0.096  1.00 6.29  ? 183  THR A CA  1 
ATOM   1325 C  C   . THR A 1 183  ? 51.750 56.295  0.829   1.00 6.92  ? 183  THR A C   1 
ATOM   1326 O  O   . THR A 1 183  ? 52.664 55.876  1.574   1.00 7.16  ? 183  THR A O   1 
ATOM   1327 C  CB  . THR A 1 183  ? 51.648 55.413  -1.518  1.00 6.92  ? 183  THR A CB  1 
ATOM   1328 O  OG1 . THR A 1 183  ? 50.971 54.494  -2.393  1.00 7.81  ? 183  THR A OG1 1 
ATOM   1329 C  CG2 . THR A 1 183  ? 53.132 54.999  -1.500  1.00 8.56  ? 183  THR A CG2 1 
ATOM   1330 N  N   . GLU A 1 184  ? 51.411 57.565  0.832   1.00 7.00  ? 184  GLU A N   1 
ATOM   1331 C  CA  . GLU A 1 184  ? 52.107 58.523  1.680   1.00 7.12  ? 184  GLU A CA  1 
ATOM   1332 C  C   . GLU A 1 184  ? 51.879 58.137  3.141   1.00 7.11  ? 184  GLU A C   1 
ATOM   1333 O  O   . GLU A 1 184  ? 52.835 58.124  3.949   1.00 8.98  ? 184  GLU A O   1 
ATOM   1334 C  CB  . GLU A 1 184  ? 51.548 59.931  1.440   1.00 8.76  ? 184  GLU A CB  1 
ATOM   1335 C  CG  . GLU A 1 184  ? 52.461 61.036  1.964   1.00 12.30 ? 184  GLU A CG  1 
ATOM   1336 C  CD  . GLU A 1 184  ? 53.823 61.092  1.233   1.00 11.27 ? 184  GLU A CD  1 
ATOM   1337 O  OE1 . GLU A 1 184  ? 53.980 60.698  0.069   1.00 12.66 ? 184  GLU A OE1 1 
ATOM   1338 O  OE2 . GLU A 1 184  ? 54.738 61.577  1.937   1.00 15.36 ? 184  GLU A OE2 1 
ATOM   1339 N  N   . GLY A 1 185  ? 50.642 57.858  3.540   1.00 6.90  ? 185  GLY A N   1 
ATOM   1340 C  CA  . GLY A 1 185  ? 50.412 57.489  4.924   1.00 7.15  ? 185  GLY A CA  1 
ATOM   1341 C  C   . GLY A 1 185  ? 51.000 56.135  5.280   1.00 7.23  ? 185  GLY A C   1 
ATOM   1342 O  O   . GLY A 1 185  ? 51.601 55.980  6.385   1.00 7.83  ? 185  GLY A O   1 
ATOM   1343 N  N   . GLN A 1 186  ? 50.874 55.139  4.399   1.00 7.48  ? 186  GLN A N   1 
ATOM   1344 C  CA  . GLN A 1 186  ? 51.350 53.800  4.787   1.00 7.05  ? 186  GLN A CA  1 
ATOM   1345 C  C   . GLN A 1 186  ? 52.856 53.758  4.786   1.00 6.92  ? 186  GLN A C   1 
ATOM   1346 O  O   . GLN A 1 186  ? 53.445 52.980  5.558   1.00 8.06  ? 186  GLN A O   1 
ATOM   1347 C  CB  . GLN A 1 186  ? 50.777 52.724  3.855   1.00 7.24  ? 186  GLN A CB  1 
ATOM   1348 C  CG  . GLN A 1 186  ? 49.235 52.555  4.096   1.00 9.45  ? 186  GLN A CG  1 
ATOM   1349 C  CD  . GLN A 1 186  ? 48.802 51.175  3.854   1.00 10.21 ? 186  GLN A CD  1 
ATOM   1350 O  OE1 . GLN A 1 186  ? 49.438 50.483  3.056   1.00 12.70 ? 186  GLN A OE1 1 
ATOM   1351 N  NE2 . GLN A 1 186  ? 47.782 50.713  4.531   1.00 10.02 ? 186  GLN A NE2 1 
ATOM   1352 N  N   . THR A 1 187  ? 53.528 54.494  3.897   1.00 8.62  ? 187  THR A N   1 
ATOM   1353 C  CA  . THR A 1 187  ? 54.989 54.498  3.902   1.00 8.32  ? 187  THR A CA  1 
ATOM   1354 C  C   . THR A 1 187  ? 55.486 55.089  5.232   1.00 8.99  ? 187  THR A C   1 
ATOM   1355 O  O   . THR A 1 187  ? 56.439 54.552  5.839   1.00 9.28  ? 187  THR A O   1 
ATOM   1356 C  CB  . THR A 1 187  ? 55.527 55.274  2.703   1.00 8.06  ? 187  THR A CB  1 
ATOM   1357 O  OG1 . THR A 1 187  ? 55.028 54.617  1.509   1.00 8.86  ? 187  THR A OG1 1 
ATOM   1358 C  CG2 . THR A 1 187  ? 57.073 55.259  2.664   1.00 9.51  ? 187  THR A CG2 1 
ATOM   1359 N  N   . TRP A 1 188  ? 54.851 56.146  5.708   1.00 7.73  ? 188  TRP A N   1 
ATOM   1360 C  CA  . TRP A 1 188  ? 55.211 56.736  7.007   1.00 9.08  ? 188  TRP A CA  1 
ATOM   1361 C  C   . TRP A 1 188  ? 54.940 55.677  8.109   1.00 8.77  ? 188  TRP A C   1 
ATOM   1362 O  O   . TRP A 1 188  ? 55.834 55.428  8.973   1.00 8.78  ? 188  TRP A O   1 
ATOM   1363 C  CB  . TRP A 1 188  ? 54.377 57.993  7.242   1.00 9.64  ? 188  TRP A CB  1 
ATOM   1364 C  CG  . TRP A 1 188  ? 54.802 58.760  8.464   1.00 9.45  ? 188  TRP A CG  1 
ATOM   1365 C  CD1 . TRP A 1 188  ? 55.712 59.785  8.486   1.00 10.72 ? 188  TRP A CD1 1 
ATOM   1366 C  CD2 . TRP A 1 188  ? 54.453 58.470  9.842   1.00 9.91  ? 188  TRP A CD2 1 
ATOM   1367 N  NE1 . TRP A 1 188  ? 55.965 60.164  9.792   1.00 11.81 ? 188  TRP A NE1 1 
ATOM   1368 C  CE2 . TRP A 1 188  ? 55.218 59.362  10.643  1.00 10.40 ? 188  TRP A CE2 1 
ATOM   1369 C  CE3 . TRP A 1 188  ? 53.604 57.544  10.461  1.00 9.64  ? 188  TRP A CE3 1 
ATOM   1370 C  CZ2 . TRP A 1 188  ? 55.156 59.351  12.041  1.00 11.24 ? 188  TRP A CZ2 1 
ATOM   1371 C  CZ3 . TRP A 1 188  ? 53.562 57.508  11.864  1.00 10.47 ? 188  TRP A CZ3 1 
ATOM   1372 C  CH2 . TRP A 1 188  ? 54.342 58.423  12.621  1.00 11.49 ? 188  TRP A CH2 1 
ATOM   1373 N  N   . LEU A 1 189  ? 53.803 55.010  8.107   1.00 8.20  ? 189  LEU A N   1 
ATOM   1374 C  CA  . LEU A 1 189  ? 53.537 54.013  9.142   1.00 8.38  ? 189  LEU A CA  1 
ATOM   1375 C  C   . LEU A 1 189  ? 54.528 52.895  9.111   1.00 9.46  ? 189  LEU A C   1 
ATOM   1376 O  O   . LEU A 1 189  ? 54.937 52.398  10.225  1.00 10.60 ? 189  LEU A O   1 
ATOM   1377 C  CB  . LEU A 1 189  ? 52.099 53.442  8.968   1.00 8.94  ? 189  LEU A CB  1 
ATOM   1378 C  CG  . LEU A 1 189  ? 50.978 54.324  9.445   1.00 7.93  ? 189  LEU A CG  1 
ATOM   1379 C  CD1 . LEU A 1 189  ? 49.622 53.662  9.124   1.00 10.46 ? 189  LEU A CD1 1 
ATOM   1380 C  CD2 . LEU A 1 189  ? 51.076 54.522  11.002  1.00 10.32 ? 189  LEU A CD2 1 
ATOM   1381 N  N   . LYS A 1 190  ? 54.927 52.406  7.961   1.00 8.43  ? 190  LYS A N   1 
ATOM   1382 C  CA  . LYS A 1 190  ? 55.868 51.298  7.948   1.00 9.34  ? 190  LYS A CA  1 
ATOM   1383 C  C   . LYS A 1 190  ? 57.217 51.776  8.548   1.00 10.37 ? 190  LYS A C   1 
ATOM   1384 O  O   . LYS A 1 190  ? 57.824 51.057  9.371   1.00 12.13 ? 190  LYS A O   1 
ATOM   1385 C  CB  . LYS A 1 190  ? 56.133 50.774  6.524   1.00 11.99 ? 190  LYS A CB  1 
ATOM   1386 C  CG  . LYS A 1 190  ? 57.065 49.554  6.514   1.00 14.48 ? 190  LYS A CG  1 
ATOM   1387 C  CD  . LYS A 1 190  ? 57.273 49.060  5.108   1.00 18.32 ? 190  LYS A CD  1 
ATOM   1388 C  CE  . LYS A 1 190  ? 58.023 47.725  5.122   1.00 24.75 ? 190  LYS A CE  1 
ATOM   1389 N  NZ  . LYS A 1 190  ? 58.421 47.374  3.670   1.00 23.55 ? 190  LYS A NZ  1 
ATOM   1390 N  N   . GLN A 1 191  ? 57.669 52.955  8.183   1.00 10.63 ? 191  GLN A N   1 
ATOM   1391 C  CA  . GLN A 1 191  ? 58.950 53.444  8.652   1.00 13.29 ? 191  GLN A CA  1 
ATOM   1392 C  C   . GLN A 1 191  ? 58.959 53.716  10.148  1.00 13.62 ? 191  GLN A C   1 
ATOM   1393 O  O   . GLN A 1 191  ? 59.902 53.255  10.849  1.00 17.86 ? 191  GLN A O   1 
ATOM   1394 C  CB  . GLN A 1 191  ? 59.330 54.721  7.885   1.00 14.30 ? 191  GLN A CB  1 
ATOM   1395 C  CG  . GLN A 1 191  ? 60.725 55.285  8.313   1.00 23.37 ? 191  GLN A CG  1 
ATOM   1396 C  CD  . GLN A 1 191  ? 61.168 56.513  7.469   1.00 24.48 ? 191  GLN A CD  1 
ATOM   1397 O  OE1 . GLN A 1 191  ? 60.498 56.920  6.495   1.00 31.05 ? 191  GLN A OE1 1 
ATOM   1398 N  NE2 . GLN A 1 191  ? 62.288 57.105  7.862   1.00 33.50 ? 191  GLN A NE2 1 
ATOM   1399 N  N   . PHE A 1 192  ? 57.981 54.418  10.681  1.00 11.86 ? 192  PHE A N   1 
ATOM   1400 C  CA  . PHE A 1 192  ? 58.000 54.833  12.066  1.00 11.54 ? 192  PHE A CA  1 
ATOM   1401 C  C   . PHE A 1 192  ? 57.248 53.961  13.036  1.00 14.99 ? 192  PHE A C   1 
ATOM   1402 O  O   . PHE A 1 192  ? 57.646 53.899  14.212  1.00 16.58 ? 192  PHE A O   1 
ATOM   1403 C  CB  . PHE A 1 192  ? 57.499 56.277  12.176  1.00 10.31 ? 192  PHE A CB  1 
ATOM   1404 C  CG  . PHE A 1 192  ? 58.404 57.258  11.455  1.00 11.97 ? 192  PHE A CG  1 
ATOM   1405 C  CD1 . PHE A 1 192  ? 58.105 57.720  10.166  1.00 12.86 ? 192  PHE A CD1 1 
ATOM   1406 C  CD2 . PHE A 1 192  ? 59.657 57.644  12.056  1.00 15.09 ? 192  PHE A CD2 1 
ATOM   1407 C  CE1 . PHE A 1 192  ? 58.986 58.541  9.477   1.00 14.32 ? 192  PHE A CE1 1 
ATOM   1408 C  CE2 . PHE A 1 192  ? 60.561 58.483  11.338  1.00 16.52 ? 192  PHE A CE2 1 
ATOM   1409 C  CZ  . PHE A 1 192  ? 60.246 58.926  10.098  1.00 14.32 ? 192  PHE A CZ  1 
ATOM   1410 N  N   . MET A 1 193  ? 56.193 53.259  12.621  1.00 11.53 ? 193  MET A N   1 
ATOM   1411 C  CA  . MET A 1 193  ? 55.388 52.454  13.531  1.00 10.83 ? 193  MET A CA  1 
ATOM   1412 C  C   . MET A 1 193  ? 55.602 50.965  13.284  1.00 11.37 ? 193  MET A C   1 
ATOM   1413 O  O   . MET A 1 193  ? 54.965 50.154  13.999  1.00 13.28 ? 193  MET A O   1 
ATOM   1414 C  CB  . MET A 1 193  ? 53.906 52.810  13.393  1.00 12.28 ? 193  MET A CB  1 
ATOM   1415 C  CG  . MET A 1 193  ? 53.583 54.257  13.728  1.00 15.61 ? 193  MET A CG  1 
ATOM   1416 S  SD  . MET A 1 193  ? 54.169 54.741  15.364  1.00 44.06 ? 193  MET A SD  1 
ATOM   1417 C  CE  . MET A 1 193  ? 55.426 55.940  14.933  1.00 30.71 ? 193  MET A CE  1 
ATOM   1418 N  N   . ASN A 1 194  ? 56.219 50.602  12.155  1.00 11.00 ? 194  ASN A N   1 
ATOM   1419 C  CA  . ASN A 1 194  ? 56.366 49.215  11.747  1.00 12.19 ? 194  ASN A CA  1 
ATOM   1420 C  C   . ASN A 1 194  ? 55.026 48.431  11.625  1.00 14.26 ? 194  ASN A C   1 
ATOM   1421 O  O   . ASN A 1 194  ? 54.906 47.289  12.090  1.00 14.30 ? 194  ASN A O   1 
ATOM   1422 C  CB  . ASN A 1 194  ? 57.295 48.487  12.769  1.00 14.11 ? 194  ASN A CB  1 
ATOM   1423 C  CG  . ASN A 1 194  ? 57.765 47.146  12.260  1.00 17.04 ? 194  ASN A CG  1 
ATOM   1424 O  OD1 . ASN A 1 194  ? 57.869 46.906  11.076  1.00 17.90 ? 194  ASN A OD1 1 
ATOM   1425 N  ND2 . ASN A 1 194  ? 58.047 46.259  13.194  1.00 20.21 ? 194  ASN A ND2 1 
ATOM   1426 N  N   . VAL A 1 195  ? 54.013 49.064  11.028  1.00 11.94 ? 195  VAL A N   1 
ATOM   1427 C  CA  . VAL A 1 195  ? 52.726 48.375  10.817  1.00 10.96 ? 195  VAL A CA  1 
ATOM   1428 C  C   . VAL A 1 195  ? 52.169 48.836  9.476   1.00 10.78 ? 195  VAL A C   1 
ATOM   1429 O  O   . VAL A 1 195  ? 52.439 49.960  9.039   1.00 10.65 ? 195  VAL A O   1 
ATOM   1430 C  CB  . VAL A 1 195  ? 51.653 48.735  11.929  1.00 12.26 ? 195  VAL A CB  1 
ATOM   1431 C  CG1 . VAL A 1 195  ? 52.026 48.241  13.329  1.00 18.97 ? 195  VAL A CG1 1 
ATOM   1432 C  CG2 . VAL A 1 195  ? 51.350 50.211  11.977  1.00 14.31 ? 195  VAL A CG2 1 
ATOM   1433 N  N   . THR A 1 196  ? 51.402 47.949  8.858   1.00 10.30 ? 196  THR A N   1 
ATOM   1434 C  CA  . THR A 1 196  ? 50.693 48.214  7.592   1.00 11.05 ? 196  THR A CA  1 
ATOM   1435 C  C   . THR A 1 196  ? 49.249 47.742  7.794   1.00 11.10 ? 196  THR A C   1 
ATOM   1436 O  O   . THR A 1 196  ? 48.971 46.531  7.869   1.00 11.56 ? 196  THR A O   1 
ATOM   1437 C  CB  . THR A 1 196  ? 51.354 47.472  6.378   1.00 10.04 ? 196  THR A CB  1 
ATOM   1438 O  OG1 . THR A 1 196  ? 52.707 47.924  6.267   1.00 12.36 ? 196  THR A OG1 1 
ATOM   1439 C  CG2 . THR A 1 196  ? 50.576 47.813  5.076   1.00 12.89 ? 196  THR A CG2 1 
ATOM   1440 N  N   . PRO A 1 197  ? 48.308 48.676  7.923   1.00 9.00  ? 197  PRO A N   1 
ATOM   1441 C  CA  . PRO A 1 197  ? 46.915 48.301  8.125   1.00 8.74  ? 197  PRO A CA  1 
ATOM   1442 C  C   . PRO A 1 197  ? 46.378 47.439  6.993   1.00 10.06 ? 197  PRO A C   1 
ATOM   1443 O  O   . PRO A 1 197  ? 46.689 47.665  5.815   1.00 9.12  ? 197  PRO A O   1 
ATOM   1444 C  CB  . PRO A 1 197  ? 46.192 49.663  8.117   1.00 9.91  ? 197  PRO A CB  1 
ATOM   1445 C  CG  . PRO A 1 197  ? 47.209 50.605  8.610   1.00 10.01 ? 197  PRO A CG  1 
ATOM   1446 C  CD  . PRO A 1 197  ? 48.516 50.138  8.053   1.00 9.80  ? 197  PRO A CD  1 
ATOM   1447 N  N   . THR A 1 198  ? 45.535 46.470  7.355   1.00 8.83  ? 198  THR A N   1 
ATOM   1448 C  CA  . THR A 1 198  ? 44.825 45.644  6.356   1.00 9.72  ? 198  THR A CA  1 
ATOM   1449 C  C   . THR A 1 198  ? 43.306 45.809  6.458   1.00 7.35  ? 198  THR A C   1 
ATOM   1450 O  O   . THR A 1 198  ? 42.584 45.116  5.711   1.00 8.27  ? 198  THR A O   1 
ATOM   1451 C  CB  . THR A 1 198  ? 45.169 44.148  6.500   1.00 10.92 ? 198  THR A CB  1 
ATOM   1452 O  OG1 . THR A 1 198  ? 44.750 43.727  7.781   1.00 12.43 ? 198  THR A OG1 1 
ATOM   1453 C  CG2 . THR A 1 198  ? 46.691 43.899  6.297   1.00 12.28 ? 198  THR A CG2 1 
ATOM   1454 N  N   . ALA A 1 199  ? 42.828 46.681  7.337   1.00 7.68  ? 199  ALA A N   1 
ATOM   1455 C  CA  . ALA A 1 199  ? 41.392 47.001  7.433   1.00 7.75  ? 199  ALA A CA  1 
ATOM   1456 C  C   . ALA A 1 199  ? 41.252 48.489  7.192   1.00 8.37  ? 199  ALA A C   1 
ATOM   1457 O  O   . ALA A 1 199  ? 42.020 49.278  7.765   1.00 8.88  ? 199  ALA A O   1 
ATOM   1458 C  CB  . ALA A 1 199  ? 40.866 46.657  8.868   1.00 9.92  ? 199  ALA A CB  1 
ATOM   1459 N  N   . SER A 1 200  ? 40.273 48.857  6.392   1.00 7.67  ? 200  SER A N   1 
ATOM   1460 C  CA  . SER A 1 200  ? 39.998 50.258  6.065   1.00 7.92  ? 200  SER A CA  1 
ATOM   1461 C  C   . SER A 1 200  ? 38.727 50.741  6.756   1.00 7.64  ? 200  SER A C   1 
ATOM   1462 O  O   . SER A 1 200  ? 37.762 49.983  6.937   1.00 8.97  ? 200  SER A O   1 
ATOM   1463 C  CB  . SER A 1 200  ? 39.858 50.393  4.543   1.00 9.29  ? 200  SER A CB  1 
ATOM   1464 O  OG  . SER A 1 200  ? 39.618 51.776  4.176   1.00 11.09 ? 200  SER A OG  1 
ATOM   1465 N  N   . TRP A 1 201  ? 38.707 52.006  7.123   1.00 7.82  ? 201  TRP A N   1 
ATOM   1466 C  CA  . TRP A 1 201  ? 37.616 52.677  7.831   1.00 7.58  ? 201  TRP A CA  1 
ATOM   1467 C  C   . TRP A 1 201  ? 37.296 53.987  7.096   1.00 8.03  ? 201  TRP A C   1 
ATOM   1468 O  O   . TRP A 1 201  ? 38.135 54.938  7.108   1.00 9.54  ? 201  TRP A O   1 
ATOM   1469 C  CB  . TRP A 1 201  ? 38.134 52.975  9.276   1.00 8.14  ? 201  TRP A CB  1 
ATOM   1470 C  CG  . TRP A 1 201  ? 37.271 53.807  10.202  1.00 9.35  ? 201  TRP A CG  1 
ATOM   1471 C  CD1 . TRP A 1 201  ? 37.413 55.154  10.508  1.00 9.75  ? 201  TRP A CD1 1 
ATOM   1472 C  CD2 . TRP A 1 201  ? 36.300 53.303  11.123  1.00 8.43  ? 201  TRP A CD2 1 
ATOM   1473 N  NE1 . TRP A 1 201  ? 36.608 55.496  11.564  1.00 9.29  ? 201  TRP A NE1 1 
ATOM   1474 C  CE2 . TRP A 1 201  ? 35.918 54.383  11.970  1.00 9.30  ? 201  TRP A CE2 1 
ATOM   1475 C  CE3 . TRP A 1 201  ? 35.733 52.049  11.333  1.00 9.69  ? 201  TRP A CE3 1 
ATOM   1476 C  CZ2 . TRP A 1 201  ? 34.982 54.227  13.030  1.00 10.16 ? 201  TRP A CZ2 1 
ATOM   1477 C  CZ3 . TRP A 1 201  ? 34.804 51.880  12.386  1.00 11.14 ? 201  TRP A CZ3 1 
ATOM   1478 C  CH2 . TRP A 1 201  ? 34.452 52.967  13.212  1.00 11.17 ? 201  TRP A CH2 1 
ATOM   1479 N  N   . ALA A 1 202  ? 36.115 54.061  6.497   1.00 8.01  ? 202  ALA A N   1 
ATOM   1480 C  CA  . ALA A 1 202  ? 35.714 55.286  5.744   1.00 8.57  ? 202  ALA A CA  1 
ATOM   1481 C  C   . ALA A 1 202  ? 34.286 55.641  6.145   1.00 8.71  ? 202  ALA A C   1 
ATOM   1482 O  O   . ALA A 1 202  ? 33.309 55.183  5.561   1.00 9.30  ? 202  ALA A O   1 
ATOM   1483 C  CB  . ALA A 1 202  ? 35.861 55.037  4.236   1.00 10.31 ? 202  ALA A CB  1 
ATOM   1484 N  N   . ILE A 1 203  ? 34.197 56.435  7.205   1.00 8.64  ? 203  ILE A N   1 
ATOM   1485 C  CA  . ILE A 1 203  ? 32.879 56.721  7.803   1.00 8.20  ? 203  ILE A CA  1 
ATOM   1486 C  C   . ILE A 1 203  ? 32.237 58.017  7.383   1.00 9.66  ? 203  ILE A C   1 
ATOM   1487 O  O   . ILE A 1 203  ? 31.052 58.232  7.659   1.00 9.75  ? 203  ILE A O   1 
ATOM   1488 C  CB  . ILE A 1 203  ? 32.953 56.662  9.374   1.00 8.80  ? 203  ILE A CB  1 
ATOM   1489 C  CG1 . ILE A 1 203  ? 34.002 57.648  9.929   1.00 10.24 ? 203  ILE A CG1 1 
ATOM   1490 C  CG2 . ILE A 1 203  ? 33.259 55.205  9.804   1.00 9.99  ? 203  ILE A CG2 1 
ATOM   1491 C  CD1 . ILE A 1 203  ? 33.865 57.880  11.426  1.00 10.76 ? 203  ILE A CD1 1 
ATOM   1492 N  N   . ASP A 1 204  ? 32.986 58.888  6.690   1.00 9.17  ? 204  ASP A N   1 
ATOM   1493 C  CA  . ASP A 1 204  ? 32.426 60.168  6.297   1.00 8.85  ? 204  ASP A CA  1 
ATOM   1494 C  C   . ASP A 1 204  ? 32.387 60.580  4.824   1.00 7.95  ? 204  ASP A C   1 
ATOM   1495 O  O   . ASP A 1 204  ? 31.672 61.560  4.556   1.00 10.07 ? 204  ASP A O   1 
ATOM   1496 C  CB  . ASP A 1 204  ? 33.060 61.299  7.107   1.00 10.24 ? 204  ASP A CB  1 
ATOM   1497 C  CG  . ASP A 1 204  ? 32.082 62.441  7.455   1.00 9.86  ? 204  ASP A CG  1 
ATOM   1498 O  OD1 . ASP A 1 204  ? 32.512 63.636  7.698   1.00 11.42 ? 204  ASP A OD1 1 
ATOM   1499 O  OD2 . ASP A 1 204  ? 30.864 62.249  7.600   1.00 10.55 ? 204  ASP A OD2 1 
ATOM   1500 N  N   . PRO A 1 205  ? 33.094 59.918  3.859   1.00 7.95  ? 205  PRO A N   1 
ATOM   1501 C  CA  . PRO A 1 205  ? 32.961 60.394  2.441   1.00 8.70  ? 205  PRO A CA  1 
ATOM   1502 C  C   . PRO A 1 205  ? 31.474 60.298  2.043   1.00 8.51  ? 205  PRO A C   1 
ATOM   1503 O  O   . PRO A 1 205  ? 30.690 59.437  2.539   1.00 9.03  ? 205  PRO A O   1 
ATOM   1504 C  CB  . PRO A 1 205  ? 33.799 59.412  1.646   1.00 9.92  ? 205  PRO A CB  1 
ATOM   1505 C  CG  . PRO A 1 205  ? 34.909 58.994  2.649   1.00 13.66 ? 205  PRO A CG  1 
ATOM   1506 C  CD  . PRO A 1 205  ? 34.060 58.800  3.942   1.00 9.51  ? 205  PRO A CD  1 
ATOM   1507 N  N   . PHE A 1 206  ? 31.058 61.174  1.118   1.00 7.65  ? 206  PHE A N   1 
ATOM   1508 C  CA  . PHE A 1 206  ? 29.592 61.317  0.856   1.00 7.80  ? 206  PHE A CA  1 
ATOM   1509 C  C   . PHE A 1 206  ? 29.170 60.404  -0.299  1.00 7.46  ? 206  PHE A C   1 
ATOM   1510 O  O   . PHE A 1 206  ? 28.955 60.803  -1.456  1.00 8.48  ? 206  PHE A O   1 
ATOM   1511 C  CB  . PHE A 1 206  ? 29.294 62.790  0.539   1.00 8.16  ? 206  PHE A CB  1 
ATOM   1512 C  CG  . PHE A 1 206  ? 30.125 63.787  1.378   1.00 7.71  ? 206  PHE A CG  1 
ATOM   1513 C  CD1 . PHE A 1 206  ? 30.340 63.586  2.717   1.00 8.19  ? 206  PHE A CD1 1 
ATOM   1514 C  CD2 . PHE A 1 206  ? 30.684 64.916  0.765   1.00 7.81  ? 206  PHE A CD2 1 
ATOM   1515 C  CE1 . PHE A 1 206  ? 31.130 64.493  3.448   1.00 9.05  ? 206  PHE A CE1 1 
ATOM   1516 C  CE2 . PHE A 1 206  ? 31.471 65.814  1.508   1.00 7.96  ? 206  PHE A CE2 1 
ATOM   1517 C  CZ  . PHE A 1 206  ? 31.686 65.590  2.846   1.00 8.94  ? 206  PHE A CZ  1 
ATOM   1518 N  N   . GLY A 1 207  ? 29.060 59.126  0.049   1.00 8.32  ? 207  GLY A N   1 
ATOM   1519 C  CA  . GLY A 1 207  ? 28.856 58.061  -0.928  1.00 7.85  ? 207  GLY A CA  1 
ATOM   1520 C  C   . GLY A 1 207  ? 30.180 57.325  -1.166  1.00 7.71  ? 207  GLY A C   1 
ATOM   1521 O  O   . GLY A 1 207  ? 31.246 57.889  -0.831  1.00 8.18  ? 207  GLY A O   1 
ATOM   1522 N  N   . HIS A 1 208  ? 30.135 56.148  -1.759  1.00 7.50  ? 208  HIS A N   1 
ATOM   1523 C  CA  . HIS A 1 208  ? 31.341 55.290  -1.842  1.00 7.35  ? 208  HIS A CA  1 
ATOM   1524 C  C   . HIS A 1 208  ? 31.517 54.678  -3.201  1.00 7.28  ? 208  HIS A C   1 
ATOM   1525 O  O   . HIS A 1 208  ? 30.551 54.352  -3.924  1.00 7.76  ? 208  HIS A O   1 
ATOM   1526 C  CB  . HIS A 1 208  ? 31.211 54.164  -0.765  1.00 7.49  ? 208  HIS A CB  1 
ATOM   1527 C  CG  . HIS A 1 208  ? 31.325 54.684  0.650   1.00 8.06  ? 208  HIS A CG  1 
ATOM   1528 N  ND1 . HIS A 1 208  ? 32.557 54.915  1.244   1.00 10.40 ? 208  HIS A ND1 1 
ATOM   1529 C  CD2 . HIS A 1 208  ? 30.380 55.019  1.554   1.00 9.42  ? 208  HIS A CD2 1 
ATOM   1530 C  CE1 . HIS A 1 208  ? 32.329 55.368  2.479   1.00 10.85 ? 208  HIS A CE1 1 
ATOM   1531 N  NE2 . HIS A 1 208  ? 31.043 55.443  2.688   1.00 11.33 ? 208  HIS A NE2 1 
ATOM   1532 N  N   . SER A 1 209  ? 32.786 54.536  -3.602  1.00 7.44  ? 209  SER A N   1 
ATOM   1533 C  CA  . SER A 1 209  ? 33.176 54.052  -4.916  1.00 6.60  ? 209  SER A CA  1 
ATOM   1534 C  C   . SER A 1 209  ? 33.894 52.727  -4.864  1.00 7.24  ? 209  SER A C   1 
ATOM   1535 O  O   . SER A 1 209  ? 34.716 52.490  -3.967  1.00 7.34  ? 209  SER A O   1 
ATOM   1536 C  CB  . SER A 1 209  ? 34.154 55.066  -5.515  1.00 7.37  ? 209  SER A CB  1 
ATOM   1537 O  OG  . SER A 1 209  ? 34.665 54.548  -6.736  1.00 7.73  ? 209  SER A OG  1 
ATOM   1538 N  N   . PRO A 1 210  ? 33.652 51.832  -5.835  1.00 6.96  ? 210  PRO A N   1 
ATOM   1539 C  CA  . PRO A 1 210  ? 34.341 50.535  -5.885  1.00 7.89  ? 210  PRO A CA  1 
ATOM   1540 C  C   . PRO A 1 210  ? 35.829 50.745  -6.206  1.00 7.41  ? 210  PRO A C   1 
ATOM   1541 O  O   . PRO A 1 210  ? 36.629 49.772  -6.173  1.00 7.36  ? 210  PRO A O   1 
ATOM   1542 C  CB  . PRO A 1 210  ? 33.601 49.752  -6.964  1.00 8.04  ? 210  PRO A CB  1 
ATOM   1543 C  CG  . PRO A 1 210  ? 33.041 50.863  -7.891  1.00 9.04  ? 210  PRO A CG  1 
ATOM   1544 C  CD  . PRO A 1 210  ? 32.649 51.976  -6.905  1.00 7.26  ? 210  PRO A CD  1 
ATOM   1545 N  N   . THR A 1 211  ? 36.255 51.973  -6.602  1.00 6.95  ? 211  THR A N   1 
ATOM   1546 C  CA  . THR A 1 211  ? 37.694 52.172  -6.779  1.00 7.85  ? 211  THR A CA  1 
ATOM   1547 C  C   . THR A 1 211  ? 38.435 51.913  -5.460  1.00 6.95  ? 211  THR A C   1 
ATOM   1548 O  O   . THR A 1 211  ? 39.621 51.536  -5.510  1.00 7.40  ? 211  THR A O   1 
ATOM   1549 C  CB  . THR A 1 211  ? 37.928 53.618  -7.273  1.00 7.44  ? 211  THR A CB  1 
ATOM   1550 O  OG1 . THR A 1 211  ? 37.366 53.679  -8.594  1.00 8.35  ? 211  THR A OG1 1 
ATOM   1551 C  CG2 . THR A 1 211  ? 39.425 53.977  -7.301  1.00 9.15  ? 211  THR A CG2 1 
ATOM   1552 N  N   . MET A 1 212  ? 37.790 52.167  -4.320  1.00 6.99  ? 212  MET A N   1 
ATOM   1553 C  CA  . MET A 1 212  ? 38.482 51.925  -3.058  1.00 7.03  ? 212  MET A CA  1 
ATOM   1554 C  C   . MET A 1 212  ? 38.820 50.435  -2.861  1.00 7.75  ? 212  MET A C   1 
ATOM   1555 O  O   . MET A 1 212  ? 40.012 50.118  -2.653  1.00 8.02  ? 212  MET A O   1 
ATOM   1556 C  CB  . MET A 1 212  ? 37.667 52.496  -1.896  1.00 9.04  ? 212  MET A CB  1 
ATOM   1557 C  CG  . MET A 1 212  ? 37.420 53.999  -1.983  1.00 10.86 ? 212  MET A CG  1 
ATOM   1558 S  SD  . MET A 1 212  ? 38.909 54.965  -2.253  1.00 14.79 ? 212  MET A SD  1 
ATOM   1559 C  CE  . MET A 1 212  ? 39.614 54.938  -0.803  1.00 15.92 ? 212  MET A CE  1 
ATOM   1560 N  N   . PRO A 1 213  ? 37.848 49.498  -2.899  1.00 7.46  ? 213  PRO A N   1 
ATOM   1561 C  CA  . PRO A 1 213  ? 38.281 48.094  -2.739  1.00 6.54  ? 213  PRO A CA  1 
ATOM   1562 C  C   . PRO A 1 213  ? 39.249 47.708  -3.855  1.00 7.80  ? 213  PRO A C   1 
ATOM   1563 O  O   . PRO A 1 213  ? 40.146 46.840  -3.614  1.00 8.16  ? 213  PRO A O   1 
ATOM   1564 C  CB  . PRO A 1 213  ? 36.966 47.277  -2.775  1.00 8.63  ? 213  PRO A CB  1 
ATOM   1565 C  CG  . PRO A 1 213  ? 35.955 48.240  -3.422  1.00 8.53  ? 213  PRO A CG  1 
ATOM   1566 C  CD  . PRO A 1 213  ? 36.379 49.608  -2.863  1.00 7.77  ? 213  PRO A CD  1 
ATOM   1567 N  N   . TYR A 1 214  ? 39.126 48.265  -5.072  1.00 7.31  ? 214  TYR A N   1 
ATOM   1568 C  CA  . TYR A 1 214  ? 40.073 47.909  -6.137  1.00 7.94  ? 214  TYR A CA  1 
ATOM   1569 C  C   . TYR A 1 214  ? 41.520 48.198  -5.677  1.00 9.37  ? 214  TYR A C   1 
ATOM   1570 O  O   . TYR A 1 214  ? 42.408 47.299  -5.763  1.00 9.07  ? 214  TYR A O   1 
ATOM   1571 C  CB  . TYR A 1 214  ? 39.792 48.732  -7.399  1.00 8.12  ? 214  TYR A CB  1 
ATOM   1572 C  CG  . TYR A 1 214  ? 40.742 48.473  -8.512  1.00 9.45  ? 214  TYR A CG  1 
ATOM   1573 C  CD1 . TYR A 1 214  ? 40.519 47.389  -9.374  1.00 14.23 ? 214  TYR A CD1 1 
ATOM   1574 C  CD2 . TYR A 1 214  ? 41.808 49.309  -8.784  1.00 8.50  ? 214  TYR A CD2 1 
ATOM   1575 C  CE1 . TYR A 1 214  ? 41.332 47.170  -10.512 1.00 15.00 ? 214  TYR A CE1 1 
ATOM   1576 C  CE2 . TYR A 1 214  ? 42.649 49.129  -9.898  1.00 9.55  ? 214  TYR A CE2 1 
ATOM   1577 C  CZ  . TYR A 1 214  ? 42.366 48.065  -10.745 1.00 12.77 ? 214  TYR A CZ  1 
ATOM   1578 O  OH  . TYR A 1 214  ? 43.113 47.945  -11.914 1.00 13.92 ? 214  TYR A OH  1 
ATOM   1579 N  N   . ILE A 1 215  ? 41.783 49.438  -5.220  1.00 7.07  ? 215  ILE A N   1 
ATOM   1580 C  CA  . ILE A 1 215  ? 43.127 49.814  -4.788  1.00 7.03  ? 215  ILE A CA  1 
ATOM   1581 C  C   . ILE A 1 215  ? 43.530 49.073  -3.507  1.00 8.21  ? 215  ILE A C   1 
ATOM   1582 O  O   . ILE A 1 215  ? 44.662 48.576  -3.380  1.00 7.81  ? 215  ILE A O   1 
ATOM   1583 C  CB  . ILE A 1 215  ? 43.183 51.333  -4.595  1.00 7.44  ? 215  ILE A CB  1 
ATOM   1584 C  CG1 . ILE A 1 215  ? 43.074 52.050  -5.928  1.00 9.16  ? 215  ILE A CG1 1 
ATOM   1585 C  CG2 . ILE A 1 215  ? 44.524 51.736  -3.868  1.00 9.13  ? 215  ILE A CG2 1 
ATOM   1586 C  CD1 . ILE A 1 215  ? 42.885 53.583  -5.748  1.00 11.99 ? 215  ILE A CD1 1 
ATOM   1587 N  N   . LEU A 1 216  ? 42.612 49.006  -2.561  1.00 6.68  ? 216  LEU A N   1 
ATOM   1588 C  CA  . LEU A 1 216  ? 42.921 48.388  -1.260  1.00 7.04  ? 216  LEU A CA  1 
ATOM   1589 C  C   . LEU A 1 216  ? 43.256 46.906  -1.402  1.00 7.74  ? 216  LEU A C   1 
ATOM   1590 O  O   . LEU A 1 216  ? 44.265 46.458  -0.792  1.00 8.15  ? 216  LEU A O   1 
ATOM   1591 C  CB  . LEU A 1 216  ? 41.742 48.554  -0.298  1.00 6.63  ? 216  LEU A CB  1 
ATOM   1592 C  CG  . LEU A 1 216  ? 41.365 49.993  0.104   1.00 7.81  ? 216  LEU A CG  1 
ATOM   1593 C  CD1 . LEU A 1 216  ? 40.056 49.970  0.878   1.00 9.37  ? 216  LEU A CD1 1 
ATOM   1594 C  CD2 . LEU A 1 216  ? 42.522 50.651  0.951   1.00 9.62  ? 216  LEU A CD2 1 
ATOM   1595 N  N   . GLN A 1 217  ? 42.496 46.165  -2.209  1.00 7.61  ? 217  GLN A N   1 
ATOM   1596 C  CA  . GLN A 1 217  ? 42.769 44.737  -2.364  1.00 8.23  ? 217  GLN A CA  1 
ATOM   1597 C  C   . GLN A 1 217  ? 44.140 44.530  -3.038  1.00 8.69  ? 217  GLN A C   1 
ATOM   1598 O  O   . GLN A 1 217  ? 44.792 43.505  -2.769  1.00 10.94 ? 217  GLN A O   1 
ATOM   1599 C  CB  . GLN A 1 217  ? 41.576 44.126  -3.097  1.00 10.83 ? 217  GLN A CB  1 
ATOM   1600 C  CG  . GLN A 1 217  ? 41.632 42.563  -3.196  1.00 10.45 ? 217  GLN A CG  1 
ATOM   1601 C  CD  . GLN A 1 217  ? 42.497 42.041  -4.303  1.00 14.73 ? 217  GLN A CD  1 
ATOM   1602 O  OE1 . GLN A 1 217  ? 42.608 42.656  -5.361  1.00 15.24 ? 217  GLN A OE1 1 
ATOM   1603 N  NE2 . GLN A 1 217  ? 43.089 40.851  -4.089  1.00 17.82 ? 217  GLN A NE2 1 
ATOM   1604 N  N   . LYS A 1 218  ? 44.609 45.450  -3.872  1.00 7.98  ? 218  LYS A N   1 
ATOM   1605 C  CA  . LYS A 1 218  ? 45.922 45.341  -4.529  1.00 7.84  ? 218  LYS A CA  1 
ATOM   1606 C  C   . LYS A 1 218  ? 47.026 45.960  -3.643  1.00 9.00  ? 218  LYS A C   1 
ATOM   1607 O  O   . LYS A 1 218  ? 48.193 46.051  -4.066  1.00 9.04  ? 218  LYS A O   1 
ATOM   1608 C  CB  . LYS A 1 218  ? 45.852 46.075  -5.879  1.00 8.44  ? 218  LYS A CB  1 
ATOM   1609 C  CG  . LYS A 1 218  ? 45.094 45.248  -6.892  1.00 9.95  ? 218  LYS A CG  1 
ATOM   1610 C  CD  . LYS A 1 218  ? 44.792 46.110  -8.177  1.00 9.31  ? 218  LYS A CD  1 
ATOM   1611 C  CE  . LYS A 1 218  ? 44.360 45.271  -9.349  1.00 13.70 ? 218  LYS A CE  1 
ATOM   1612 N  NZ  . LYS A 1 218  ? 43.259 44.311  -9.127  1.00 14.32 ? 218  LYS A NZ  1 
ATOM   1613 N  N   . SER A 1 219  ? 46.660 46.400  -2.445  1.00 7.44  ? 219  SER A N   1 
ATOM   1614 C  CA  . SER A 1 219  ? 47.561 46.996  -1.473  1.00 8.58  ? 219  SER A CA  1 
ATOM   1615 C  C   . SER A 1 219  ? 47.595 46.197  -0.140  1.00 8.07  ? 219  SER A C   1 
ATOM   1616 O  O   . SER A 1 219  ? 47.918 46.751  0.914   1.00 8.87  ? 219  SER A O   1 
ATOM   1617 C  CB  . SER A 1 219  ? 47.194 48.466  -1.189  1.00 8.04  ? 219  SER A CB  1 
ATOM   1618 O  OG  . SER A 1 219  ? 47.243 49.202  -2.442  1.00 9.59  ? 219  SER A OG  1 
ATOM   1619 N  N   . GLY A 1 220  ? 47.247 44.913  -0.225  1.00 8.69  ? 220  GLY A N   1 
ATOM   1620 C  CA  . GLY A 1 220  ? 47.319 44.033  0.957   1.00 9.55  ? 220  GLY A CA  1 
ATOM   1621 C  C   . GLY A 1 220  ? 46.098 44.004  1.854   1.00 9.14  ? 220  GLY A C   1 
ATOM   1622 O  O   . GLY A 1 220  ? 46.089 43.207  2.807   1.00 10.37 ? 220  GLY A O   1 
ATOM   1623 N  N   . PHE A 1 221  ? 45.040 44.773  1.579   1.00 9.18  ? 221  PHE A N   1 
ATOM   1624 C  CA  . PHE A 1 221  ? 43.920 44.787  2.516   1.00 8.08  ? 221  PHE A CA  1 
ATOM   1625 C  C   . PHE A 1 221  ? 43.085 43.525  2.428   1.00 8.10  ? 221  PHE A C   1 
ATOM   1626 O  O   . PHE A 1 221  ? 42.979 42.876  1.370   1.00 9.08  ? 221  PHE A O   1 
ATOM   1627 C  CB  . PHE A 1 221  ? 43.026 46.007  2.251   1.00 7.53  ? 221  PHE A CB  1 
ATOM   1628 C  CG  . PHE A 1 221  ? 43.587 47.295  2.771   1.00 7.56  ? 221  PHE A CG  1 
ATOM   1629 C  CD1 . PHE A 1 221  ? 44.720 47.906  2.190   1.00 7.69  ? 221  PHE A CD1 1 
ATOM   1630 C  CD2 . PHE A 1 221  ? 43.009 47.910  3.896   1.00 7.51  ? 221  PHE A CD2 1 
ATOM   1631 C  CE1 . PHE A 1 221  ? 45.237 49.083  2.732   1.00 7.25  ? 221  PHE A CE1 1 
ATOM   1632 C  CE2 . PHE A 1 221  ? 43.526 49.079  4.423   1.00 8.23  ? 221  PHE A CE2 1 
ATOM   1633 C  CZ  . PHE A 1 221  ? 44.650 49.693  3.834   1.00 7.58  ? 221  PHE A CZ  1 
ATOM   1634 N  N   A LYS A 1 222  ? 42.421 43.268  3.559   0.50 9.66  ? 222  LYS A N   1 
ATOM   1635 N  N   B LYS A 1 222  ? 42.421 43.268  3.559   0.50 9.78  ? 222  LYS A N   1 
ATOM   1636 C  CA  A LYS A 1 222  ? 41.515 42.148  3.712   0.50 9.50  ? 222  LYS A CA  1 
ATOM   1637 C  CA  B LYS A 1 222  ? 41.515 42.148  3.712   0.50 9.76  ? 222  LYS A CA  1 
ATOM   1638 C  C   A LYS A 1 222  ? 40.115 42.558  4.055   0.50 9.03  ? 222  LYS A C   1 
ATOM   1639 C  C   B LYS A 1 222  ? 40.115 42.558  4.055   0.50 9.20  ? 222  LYS A C   1 
ATOM   1640 O  O   A LYS A 1 222  ? 39.202 41.755  3.839   0.50 9.54  ? 222  LYS A O   1 
ATOM   1641 O  O   B LYS A 1 222  ? 39.202 41.755  3.839   0.50 9.66  ? 222  LYS A O   1 
ATOM   1642 C  CB  A LYS A 1 222  ? 42.016 41.179  4.797   0.50 13.48 ? 222  LYS A CB  1 
ATOM   1643 C  CB  B LYS A 1 222  ? 42.016 41.179  4.797   0.50 13.98 ? 222  LYS A CB  1 
ATOM   1644 C  CG  A LYS A 1 222  ? 43.401 40.627  4.510   0.50 15.55 ? 222  LYS A CG  1 
ATOM   1645 C  CG  B LYS A 1 222  ? 43.401 40.627  4.510   0.50 16.57 ? 222  LYS A CG  1 
ATOM   1646 C  CD  A LYS A 1 222  ? 43.505 40.008  3.148   0.50 22.62 ? 222  LYS A CD  1 
ATOM   1647 C  CD  B LYS A 1 222  ? 43.505 40.008  3.148   0.50 23.52 ? 222  LYS A CD  1 
ATOM   1648 C  CE  A LYS A 1 222  ? 44.913 39.444  2.889   0.50 30.46 ? 222  LYS A CE  1 
ATOM   1649 C  CE  B LYS A 1 222  ? 44.913 39.444  2.889   0.50 30.93 ? 222  LYS A CE  1 
ATOM   1650 N  NZ  A LYS A 1 222  ? 45.288 38.633  4.085   0.50 34.11 ? 222  LYS A NZ  1 
ATOM   1651 N  NZ  B LYS A 1 222  ? 45.834 40.610  2.747   0.50 35.32 ? 222  LYS A NZ  1 
ATOM   1652 N  N   . ASN A 1 223  ? 39.903 43.779  4.534   1.00 7.27  ? 223  ASN A N   1 
ATOM   1653 C  CA  . ASN A 1 223  ? 38.551 44.176  4.956   1.00 8.73  ? 223  ASN A CA  1 
ATOM   1654 C  C   . ASN A 1 223  ? 38.397 45.672  4.830   1.00 8.17  ? 223  ASN A C   1 
ATOM   1655 O  O   . ASN A 1 223  ? 39.390 46.417  4.951   1.00 7.83  ? 223  ASN A O   1 
ATOM   1656 C  CB  . ASN A 1 223  ? 38.335 43.835  6.479   1.00 8.23  ? 223  ASN A CB  1 
ATOM   1657 C  CG  . ASN A 1 223  ? 38.427 42.333  6.761   1.00 10.24 ? 223  ASN A CG  1 
ATOM   1658 O  OD1 . ASN A 1 223  ? 39.499 41.830  7.227   1.00 13.62 ? 223  ASN A OD1 1 
ATOM   1659 N  ND2 . ASN A 1 223  ? 37.396 41.638  6.453   1.00 7.87  ? 223  ASN A ND2 1 
ATOM   1660 N  N   . MET A 1 224  ? 37.156 46.117  4.690   1.00 7.34  ? 224  MET A N   1 
ATOM   1661 C  CA  . MET A 1 224  ? 36.881 47.574  4.690   1.00 6.65  ? 224  MET A CA  1 
ATOM   1662 C  C   . MET A 1 224  ? 35.500 47.874  5.245   1.00 7.72  ? 224  MET A C   1 
ATOM   1663 O  O   . MET A 1 224  ? 34.602 46.979  5.223   1.00 8.83  ? 224  MET A O   1 
ATOM   1664 C  CB  . MET A 1 224  ? 37.050 48.178  3.281   1.00 8.88  ? 224  MET A CB  1 
ATOM   1665 C  CG  . MET A 1 224  ? 36.046 47.590  2.256   1.00 8.47  ? 224  MET A CG  1 
ATOM   1666 S  SD  . MET A 1 224  ? 36.178 48.415  0.616   1.00 10.34 ? 224  MET A SD  1 
ATOM   1667 C  CE  . MET A 1 224  ? 35.851 49.994  0.986   1.00 14.46 ? 224  MET A CE  1 
ATOM   1668 N  N   . LEU A 1 225  ? 35.322 49.096  5.707   1.00 7.33  ? 225  LEU A N   1 
ATOM   1669 C  CA  . LEU A 1 225  ? 34.061 49.522  6.286   1.00 7.58  ? 225  LEU A CA  1 
ATOM   1670 C  C   . LEU A 1 225  ? 33.638 50.838  5.664   1.00 8.05  ? 225  LEU A C   1 
ATOM   1671 O  O   . LEU A 1 225  ? 34.496 51.734  5.471   1.00 8.30  ? 225  LEU A O   1 
ATOM   1672 C  CB  . LEU A 1 225  ? 34.261 49.625  7.799   1.00 8.28  ? 225  LEU A CB  1 
ATOM   1673 C  CG  . LEU A 1 225  ? 33.025 50.220  8.549   1.00 8.44  ? 225  LEU A CG  1 
ATOM   1674 C  CD1 . LEU A 1 225  ? 32.922 49.580  9.959   1.00 9.13  ? 225  LEU A CD1 1 
ATOM   1675 C  CD2 . LEU A 1 225  ? 33.071 51.744  8.614   1.00 8.67  ? 225  LEU A CD2 1 
ATOM   1676 N  N   . ILE A 1 226  ? 32.353 50.960  5.371   1.00 7.47  ? 226  ILE A N   1 
ATOM   1677 C  CA  . ILE A 1 226  ? 31.754 52.195  4.802   1.00 8.43  ? 226  ILE A CA  1 
ATOM   1678 C  C   . ILE A 1 226  ? 30.514 52.557  5.575   1.00 7.83  ? 226  ILE A C   1 
ATOM   1679 O  O   . ILE A 1 226  ? 29.942 51.721  6.304   1.00 8.49  ? 226  ILE A O   1 
ATOM   1680 C  CB  . ILE A 1 226  ? 31.449 51.996  3.280   1.00 8.42  ? 226  ILE A CB  1 
ATOM   1681 C  CG1 . ILE A 1 226  ? 30.419 50.869  3.053   1.00 8.73  ? 226  ILE A CG1 1 
ATOM   1682 C  CG2 . ILE A 1 226  ? 32.781 51.695  2.524   1.00 9.59  ? 226  ILE A CG2 1 
ATOM   1683 C  CD1 . ILE A 1 226  ? 30.055 50.730  1.565   1.00 10.23 ? 226  ILE A CD1 1 
ATOM   1684 N  N   . GLN A 1 227  ? 30.099 53.805  5.449   1.00 9.06  ? 227  GLN A N   1 
ATOM   1685 C  CA  . GLN A 1 227  ? 28.931 54.333  6.197   1.00 9.47  ? 227  GLN A CA  1 
ATOM   1686 C  C   . GLN A 1 227  ? 27.947 55.151  5.380   1.00 9.51  ? 227  GLN A C   1 
ATOM   1687 O  O   . GLN A 1 227  ? 26.730 54.889  5.484   1.00 10.16 ? 227  GLN A O   1 
ATOM   1688 C  CB  . GLN A 1 227  ? 29.442 55.186  7.369   1.00 9.62  ? 227  GLN A CB  1 
ATOM   1689 C  CG  . GLN A 1 227  ? 28.451 56.246  7.991   1.00 12.71 ? 227  GLN A CG  1 
ATOM   1690 C  CD  . GLN A 1 227  ? 27.092 55.731  8.447   1.00 11.03 ? 227  GLN A CD  1 
ATOM   1691 O  OE1 . GLN A 1 227  ? 26.946 54.529  8.719   1.00 13.72 ? 227  GLN A OE1 1 
ATOM   1692 N  NE2 . GLN A 1 227  ? 26.110 56.621  8.554   1.00 12.05 ? 227  GLN A NE2 1 
ATOM   1693 N  N   . ARG A 1 228  ? 28.359 56.138  4.601   1.00 8.51  ? 228  ARG A N   1 
ATOM   1694 C  CA  . ARG A 1 228  ? 27.362 56.982  3.973   1.00 9.16  ? 228  ARG A CA  1 
ATOM   1695 C  C   . ARG A 1 228  ? 26.874 56.439  2.689   1.00 9.33  ? 228  ARG A C   1 
ATOM   1696 O  O   . ARG A 1 228  ? 27.442 56.707  1.630   1.00 10.25 ? 228  ARG A O   1 
ATOM   1697 C  CB  . ARG A 1 228  ? 27.937 58.432  3.800   1.00 9.57  ? 228  ARG A CB  1 
ATOM   1698 C  CG  . ARG A 1 228  ? 28.118 59.182  5.074   1.00 8.85  ? 228  ARG A CG  1 
ATOM   1699 C  CD  . ARG A 1 228  ? 28.416 60.661  4.747   1.00 10.10 ? 228  ARG A CD  1 
ATOM   1700 N  NE  . ARG A 1 228  ? 28.678 61.532  5.908   1.00 9.80  ? 228  ARG A NE  1 
ATOM   1701 C  CZ  . ARG A 1 228  ? 27.742 62.236  6.537   1.00 10.63 ? 228  ARG A CZ  1 
ATOM   1702 N  NH1 . ARG A 1 228  ? 26.473 62.107  6.170   1.00 11.57 ? 228  ARG A NH1 1 
ATOM   1703 N  NH2 . ARG A 1 228  ? 28.103 63.156  7.438   1.00 12.87 ? 228  ARG A NH2 1 
ATOM   1704 N  N   . THR A 1 229  ? 25.785 55.670  2.776   1.00 9.88  ? 229  THR A N   1 
ATOM   1705 C  CA  . THR A 1 229  ? 25.098 55.139  1.613   1.00 8.39  ? 229  THR A CA  1 
ATOM   1706 C  C   . THR A 1 229  ? 23.625 55.554  1.800   1.00 8.26  ? 229  THR A C   1 
ATOM   1707 O  O   . THR A 1 229  ? 23.132 55.818  2.911   1.00 9.83  ? 229  THR A O   1 
ATOM   1708 C  CB  . THR A 1 229  ? 25.252 53.602  1.501   1.00 10.11 ? 229  THR A CB  1 
ATOM   1709 O  OG1 . THR A 1 229  ? 24.612 53.017  2.643   1.00 10.64 ? 229  THR A OG1 1 
ATOM   1710 C  CG2 . THR A 1 229  ? 26.719 53.200  1.446   1.00 9.68  ? 229  THR A CG2 1 
ATOM   1711 N  N   . HIS A 1 230  ? 22.949 55.597  0.662   1.00 8.34  ? 230  HIS A N   1 
ATOM   1712 C  CA  . HIS A 1 230  ? 21.556 56.054  0.657   1.00 9.70  ? 230  HIS A CA  1 
ATOM   1713 C  C   . HIS A 1 230  ? 20.720 55.303  1.689   1.00 8.89  ? 230  HIS A C   1 
ATOM   1714 O  O   . HIS A 1 230  ? 20.793 54.064  1.790   1.00 9.71  ? 230  HIS A O   1 
ATOM   1715 C  CB  . HIS A 1 230  ? 21.012 55.803  -0.752  1.00 9.12  ? 230  HIS A CB  1 
ATOM   1716 C  CG  . HIS A 1 230  ? 19.709 56.487  -1.087  1.00 9.98  ? 230  HIS A CG  1 
ATOM   1717 N  ND1 . HIS A 1 230  ? 18.519 56.209  -0.417  1.00 10.52 ? 230  HIS A ND1 1 
ATOM   1718 C  CD2 . HIS A 1 230  ? 19.407 57.390  -2.051  1.00 11.86 ? 230  HIS A CD2 1 
ATOM   1719 C  CE1 . HIS A 1 230  ? 17.546 56.938  -0.948  1.00 11.02 ? 230  HIS A CE1 1 
ATOM   1720 N  NE2 . HIS A 1 230  ? 18.049 57.653  -1.945  1.00 10.88 ? 230  HIS A NE2 1 
ATOM   1721 N  N   . TYR A 1 231  ? 19.894 56.046  2.422   1.00 10.18 ? 231  TYR A N   1 
ATOM   1722 C  CA  . TYR A 1 231  ? 19.074 55.385  3.445   1.00 9.82  ? 231  TYR A CA  1 
ATOM   1723 C  C   . TYR A 1 231  ? 18.194 54.276  2.886   1.00 11.06 ? 231  TYR A C   1 
ATOM   1724 O  O   . TYR A 1 231  ? 17.917 53.311  3.621   1.00 11.42 ? 231  TYR A O   1 
ATOM   1725 C  CB  . TYR A 1 231  ? 18.221 56.404  4.218   1.00 11.11 ? 231  TYR A CB  1 
ATOM   1726 C  CG  . TYR A 1 231  ? 17.236 57.194  3.347   1.00 12.01 ? 231  TYR A CG  1 
ATOM   1727 C  CD1 . TYR A 1 231  ? 15.909 56.716  3.151   1.00 12.22 ? 231  TYR A CD1 1 
ATOM   1728 C  CD2 . TYR A 1 231  ? 17.605 58.419  2.737   1.00 10.92 ? 231  TYR A CD2 1 
ATOM   1729 C  CE1 . TYR A 1 231  ? 15.007 57.438  2.379   1.00 13.03 ? 231  TYR A CE1 1 
ATOM   1730 C  CE2 . TYR A 1 231  ? 16.678 59.164  1.986   1.00 11.28 ? 231  TYR A CE2 1 
ATOM   1731 C  CZ  . TYR A 1 231  ? 15.376 58.648  1.809   1.00 11.90 ? 231  TYR A CZ  1 
ATOM   1732 O  OH  . TYR A 1 231  ? 14.460 59.389  1.048   1.00 13.33 ? 231  TYR A OH  1 
ATOM   1733 N  N   . SER A 1 232  ? 17.733 54.356  1.662   1.00 10.45 ? 232  SER A N   1 
ATOM   1734 C  CA  . SER A 1 232  ? 16.904 53.262  1.111   1.00 11.25 ? 232  SER A CA  1 
ATOM   1735 C  C   . SER A 1 232  ? 17.729 52.047  0.871   1.00 11.38 ? 232  SER A C   1 
ATOM   1736 O  O   . SER A 1 232  ? 17.235 50.895  0.976   1.00 11.70 ? 232  SER A O   1 
ATOM   1737 C  CB  . SER A 1 232  ? 16.242 53.648  -0.210  1.00 12.48 ? 232  SER A CB  1 
ATOM   1738 O  OG  . SER A 1 232  ? 15.327 54.745  -0.041  1.00 15.27 ? 232  SER A OG  1 
ATOM   1739 N  N   . VAL A 1 233  ? 19.003 52.225  0.473   1.00 10.52 ? 233  VAL A N   1 
ATOM   1740 C  CA  . VAL A 1 233  ? 19.907 51.093  0.269   1.00 11.15 ? 233  VAL A CA  1 
ATOM   1741 C  C   . VAL A 1 233  ? 20.178 50.395  1.632   1.00 9.71  ? 233  VAL A C   1 
ATOM   1742 O  O   . VAL A 1 233  ? 20.177 49.141  1.720   1.00 10.90 ? 233  VAL A O   1 
ATOM   1743 C  CB  . VAL A 1 233  ? 21.243 51.577  -0.390  1.00 11.03 ? 233  VAL A CB  1 
ATOM   1744 C  CG1 . VAL A 1 233  ? 22.272 50.443  -0.394  1.00 11.16 ? 233  VAL A CG1 1 
ATOM   1745 C  CG2 . VAL A 1 233  ? 20.939 51.944  -1.855  1.00 12.96 ? 233  VAL A CG2 1 
ATOM   1746 N  N   . LYS A 1 234  ? 20.484 51.163  2.667   1.00 9.49  ? 234  LYS A N   1 
ATOM   1747 C  CA  . LYS A 1 234  ? 20.676 50.537  3.999   1.00 9.99  ? 234  LYS A CA  1 
ATOM   1748 C  C   . LYS A 1 234  ? 19.428 49.702  4.376   1.00 9.83  ? 234  LYS A C   1 
ATOM   1749 O  O   . LYS A 1 234  ? 19.609 48.599  4.854   1.00 10.35 ? 234  LYS A O   1 
ATOM   1750 C  CB  . LYS A 1 234  ? 20.870 51.629  5.047   1.00 9.02  ? 234  LYS A CB  1 
ATOM   1751 C  CG  . LYS A 1 234  ? 22.286 52.322  4.951   1.00 11.58 ? 234  LYS A CG  1 
ATOM   1752 C  CD  . LYS A 1 234  ? 22.256 53.601  5.725   1.00 11.38 ? 234  LYS A CD  1 
ATOM   1753 C  CE  . LYS A 1 234  ? 23.712 54.252  5.718   1.00 9.58  ? 234  LYS A CE  1 
ATOM   1754 N  NZ  . LYS A 1 234  ? 24.610 53.719  6.836   1.00 9.77  ? 234  LYS A NZ  1 
ATOM   1755 N  N   . LYS A 1 235  ? 18.224 50.239  4.151   1.00 10.51 ? 235  LYS A N   1 
ATOM   1756 C  CA  . LYS A 1 235  ? 17.031 49.461  4.524   1.00 12.54 ? 235  LYS A CA  1 
ATOM   1757 C  C   . LYS A 1 235  ? 16.903 48.209  3.743   1.00 11.03 ? 235  LYS A C   1 
ATOM   1758 O  O   . LYS A 1 235  ? 16.651 47.116  4.342   1.00 12.01 ? 235  LYS A O   1 
ATOM   1759 C  CB  . LYS A 1 235  ? 15.850 50.353  4.343   1.00 12.01 ? 235  LYS A CB  1 
ATOM   1760 C  CG  . LYS A 1 235  ? 14.468 49.653  4.771   1.00 12.79 ? 235  LYS A CG  1 
ATOM   1761 C  CD  . LYS A 1 235  ? 13.322 50.626  4.712   1.00 14.71 ? 235  LYS A CD  1 
ATOM   1762 C  CE  . LYS A 1 235  ? 12.005 49.949  5.153   1.00 16.80 ? 235  LYS A CE  1 
ATOM   1763 N  NZ  . LYS A 1 235  ? 10.852 50.919  4.933   1.00 23.23 ? 235  LYS A NZ  1 
ATOM   1764 N  N   . GLU A 1 236  ? 17.102 48.264  2.436   1.00 10.62 ? 236  GLU A N   1 
ATOM   1765 C  CA  . GLU A 1 236  ? 16.985 47.081  1.595   1.00 11.33 ? 236  GLU A CA  1 
ATOM   1766 C  C   . GLU A 1 236  ? 18.018 46.011  1.936   1.00 13.65 ? 236  GLU A C   1 
ATOM   1767 O  O   . GLU A 1 236  ? 17.739 44.815  2.057   1.00 14.26 ? 236  GLU A O   1 
ATOM   1768 C  CB  . GLU A 1 236  ? 17.147 47.510  0.130   1.00 15.09 ? 236  GLU A CB  1 
ATOM   1769 C  CG  . GLU A 1 236  ? 17.005 46.418  -0.929  1.00 22.33 ? 236  GLU A CG  1 
ATOM   1770 C  CD  . GLU A 1 236  ? 15.528 46.027  -1.174  1.00 30.83 ? 236  GLU A CD  1 
ATOM   1771 O  OE1 . GLU A 1 236  ? 15.306 45.019  -1.861  1.00 34.52 ? 236  GLU A OE1 1 
ATOM   1772 O  OE2 . GLU A 1 236  ? 14.601 46.736  -0.706  1.00 30.90 ? 236  GLU A OE2 1 
ATOM   1773 N  N   . LEU A 1 237  ? 19.286 46.409  2.056   1.00 10.91 ? 237  LEU A N   1 
ATOM   1774 C  CA  . LEU A 1 237  ? 20.301 45.447  2.366   1.00 11.30 ? 237  LEU A CA  1 
ATOM   1775 C  C   . LEU A 1 237  ? 20.096 44.934  3.806   1.00 10.67 ? 237  LEU A C   1 
ATOM   1776 O  O   . LEU A 1 237  ? 20.343 43.727  4.055   1.00 12.64 ? 237  LEU A O   1 
ATOM   1777 C  CB  . LEU A 1 237  ? 21.709 46.042  2.236   1.00 11.12 ? 237  LEU A CB  1 
ATOM   1778 C  CG  . LEU A 1 237  ? 22.053 46.487  0.783   1.00 10.53 ? 237  LEU A CG  1 
ATOM   1779 C  CD1 . LEU A 1 237  ? 23.523 47.045  0.737   1.00 12.81 ? 237  LEU A CD1 1 
ATOM   1780 C  CD2 . LEU A 1 237  ? 21.977 45.321  -0.251  1.00 14.11 ? 237  LEU A CD2 1 
ATOM   1781 N  N   . ALA A 1 238  ? 19.681 45.769  4.734   1.00 11.09 ? 238  ALA A N   1 
ATOM   1782 C  CA  . ALA A 1 238  ? 19.482 45.265  6.103   1.00 11.12 ? 238  ALA A CA  1 
ATOM   1783 C  C   . ALA A 1 238  ? 18.398 44.165  6.124   1.00 12.97 ? 238  ALA A C   1 
ATOM   1784 O  O   . ALA A 1 238  ? 18.579 43.152  6.829   1.00 13.81 ? 238  ALA A O   1 
ATOM   1785 C  CB  . ALA A 1 238  ? 19.075 46.385  7.000   1.00 11.79 ? 238  ALA A CB  1 
ATOM   1786 N  N   . GLN A 1 239  ? 17.344 44.353  5.344   1.00 12.82 ? 239  GLN A N   1 
ATOM   1787 C  CA  . GLN A 1 239  ? 16.237 43.366  5.338   1.00 13.46 ? 239  GLN A CA  1 
ATOM   1788 C  C   . GLN A 1 239  ? 16.711 42.011  4.860   1.00 15.79 ? 239  GLN A C   1 
ATOM   1789 O  O   . GLN A 1 239  ? 16.130 40.989  5.247   1.00 17.89 ? 239  GLN A O   1 
ATOM   1790 C  CB  . GLN A 1 239  ? 15.122 43.888  4.438   1.00 16.54 ? 239  GLN A CB  1 
ATOM   1791 C  CG  . GLN A 1 239  ? 14.315 44.991  5.102   1.00 21.43 ? 239  GLN A CG  1 
ATOM   1792 C  CD  . GLN A 1 239  ? 13.289 45.667  4.187   1.00 26.45 ? 239  GLN A CD  1 
ATOM   1793 O  OE1 . GLN A 1 239  ? 13.414 45.669  2.966   1.00 31.33 ? 239  GLN A OE1 1 
ATOM   1794 N  NE2 . GLN A 1 239  ? 12.272 46.273  4.801   1.00 31.13 ? 239  GLN A NE2 1 
ATOM   1795 N  N   . GLN A 1 240  ? 17.721 41.951  4.009   1.00 12.49 ? 240  GLN A N   1 
ATOM   1796 C  CA  . GLN A 1 240  ? 18.235 40.693  3.490   1.00 13.05 ? 240  GLN A CA  1 
ATOM   1797 C  C   . GLN A 1 240  ? 19.541 40.274  4.147   1.00 11.16 ? 240  GLN A C   1 
ATOM   1798 O  O   . GLN A 1 240  ? 20.149 39.313  3.723   1.00 12.76 ? 240  GLN A O   1 
ATOM   1799 C  CB  . GLN A 1 240  ? 18.499 40.830  1.971   1.00 16.29 ? 240  GLN A CB  1 
ATOM   1800 C  CG  . GLN A 1 240  ? 17.334 41.407  1.179   1.00 20.49 ? 240  GLN A CG  1 
ATOM   1801 C  CD  . GLN A 1 240  ? 16.134 40.510  1.288   1.00 23.23 ? 240  GLN A CD  1 
ATOM   1802 O  OE1 . GLN A 1 240  ? 15.015 41.000  1.410   1.00 31.18 ? 240  GLN A OE1 1 
ATOM   1803 N  NE2 . GLN A 1 240  ? 16.358 39.199  1.274   1.00 23.40 ? 240  GLN A NE2 1 
ATOM   1804 N  N   . ARG A 1 241  ? 19.949 40.986  5.217   1.00 11.90 ? 241  ARG A N   1 
ATOM   1805 C  CA  . ARG A 1 241  ? 21.257 40.735  5.868   1.00 11.36 ? 241  ARG A CA  1 
ATOM   1806 C  C   . ARG A 1 241  ? 22.381 40.710  4.846   1.00 10.60 ? 241  ARG A C   1 
ATOM   1807 O  O   . ARG A 1 241  ? 23.217 39.811  4.778   1.00 11.34 ? 241  ARG A O   1 
ATOM   1808 C  CB  . ARG A 1 241  ? 21.248 39.452  6.712   1.00 12.93 ? 241  ARG A CB  1 
ATOM   1809 C  CG  . ARG A 1 241  ? 20.202 39.588  7.840   1.00 14.86 ? 241  ARG A CG  1 
ATOM   1810 C  CD  . ARG A 1 241  ? 20.248 38.409  8.802   1.00 17.37 ? 241  ARG A CD  1 
ATOM   1811 N  NE  . ARG A 1 241  ? 20.299 37.117  8.150   1.00 24.23 ? 241  ARG A NE  1 
ATOM   1812 C  CZ  . ARG A 1 241  ? 20.731 35.999  8.759   1.00 25.53 ? 241  ARG A CZ  1 
ATOM   1813 N  NH1 . ARG A 1 241  ? 21.131 36.025  10.032  1.00 25.18 ? 241  ARG A NH1 1 
ATOM   1814 N  NH2 . ARG A 1 241  ? 20.835 34.862  8.068   1.00 28.05 ? 241  ARG A NH2 1 
ATOM   1815 N  N   . GLN A 1 242  ? 22.368 41.755  3.987   1.00 10.54 ? 242  GLN A N   1 
ATOM   1816 C  CA  . GLN A 1 242  ? 23.404 41.921  2.934   1.00 9.92  ? 242  GLN A CA  1 
ATOM   1817 C  C   . GLN A 1 242  ? 24.242 43.171  3.203   1.00 9.95  ? 242  GLN A C   1 
ATOM   1818 O  O   . GLN A 1 242  ? 24.786 43.735  2.233   1.00 11.77 ? 242  GLN A O   1 
ATOM   1819 C  CB  . GLN A 1 242  ? 22.781 41.971  1.525   1.00 11.09 ? 242  GLN A CB  1 
ATOM   1820 C  CG  . GLN A 1 242  ? 22.111 40.627  1.127   1.00 12.47 ? 242  GLN A CG  1 
ATOM   1821 C  CD  . GLN A 1 242  ? 21.268 40.751  -0.127  1.00 12.11 ? 242  GLN A CD  1 
ATOM   1822 O  OE1 . GLN A 1 242  ? 20.749 41.814  -0.411  1.00 13.32 ? 242  GLN A OE1 1 
ATOM   1823 N  NE2 . GLN A 1 242  ? 21.164 39.648  -0.875  1.00 13.87 ? 242  GLN A NE2 1 
ATOM   1824 N  N   . LEU A 1 243  ? 24.376 43.566  4.472   1.00 9.29  ? 243  LEU A N   1 
ATOM   1825 C  CA  . LEU A 1 243  ? 25.192 44.742  4.820   1.00 8.31  ? 243  LEU A CA  1 
ATOM   1826 C  C   . LEU A 1 243  ? 26.661 44.342  4.869   1.00 9.47  ? 243  LEU A C   1 
ATOM   1827 O  O   . LEU A 1 243  ? 27.522 45.262  4.890   1.00 10.64 ? 243  LEU A O   1 
ATOM   1828 C  CB  . LEU A 1 243  ? 24.736 45.314  6.154   1.00 9.76  ? 243  LEU A CB  1 
ATOM   1829 C  CG  . LEU A 1 243  ? 23.354 45.959  6.107   1.00 10.10 ? 243  LEU A CG  1 
ATOM   1830 C  CD1 . LEU A 1 243  ? 22.860 46.105  7.560   1.00 13.27 ? 243  LEU A CD1 1 
ATOM   1831 C  CD2 . LEU A 1 243  ? 23.402 47.347  5.464   1.00 10.96 ? 243  LEU A CD2 1 
ATOM   1832 N  N   . GLU A 1 244  ? 27.001 43.057  4.954   1.00 8.88  ? 244  GLU A N   1 
ATOM   1833 C  CA  . GLU A 1 244  ? 28.390 42.587  4.829   1.00 8.38  ? 244  GLU A CA  1 
ATOM   1834 C  C   . GLU A 1 244  ? 28.402 41.808  3.531   1.00 9.29  ? 244  GLU A C   1 
ATOM   1835 O  O   . GLU A 1 244  ? 27.578 40.877  3.309   1.00 10.14 ? 244  GLU A O   1 
ATOM   1836 C  CB  . GLU A 1 244  ? 28.847 41.751  6.027   1.00 8.23  ? 244  GLU A CB  1 
ATOM   1837 C  CG  . GLU A 1 244  ? 29.171 42.666  7.200   1.00 9.63  ? 244  GLU A CG  1 
ATOM   1838 C  CD  . GLU A 1 244  ? 29.475 41.973  8.531   1.00 10.86 ? 244  GLU A CD  1 
ATOM   1839 O  OE1 . GLU A 1 244  ? 28.877 40.921  8.823   1.00 11.50 ? 244  GLU A OE1 1 
ATOM   1840 O  OE2 . GLU A 1 244  ? 30.309 42.536  9.297   1.00 10.72 ? 244  GLU A OE2 1 
ATOM   1841 N  N   . PHE A 1 245  ? 29.379 42.093  2.674   1.00 8.68  ? 245  PHE A N   1 
ATOM   1842 C  CA  . PHE A 1 245  ? 29.412 41.486  1.335   1.00 8.39  ? 245  PHE A CA  1 
ATOM   1843 C  C   . PHE A 1 245  ? 30.819 41.450  0.783   1.00 7.67  ? 245  PHE A C   1 
ATOM   1844 O  O   . PHE A 1 245  ? 31.676 42.239  1.249   1.00 8.96  ? 245  PHE A O   1 
ATOM   1845 C  CB  . PHE A 1 245  ? 28.456 42.263  0.372   1.00 8.65  ? 245  PHE A CB  1 
ATOM   1846 C  CG  . PHE A 1 245  ? 28.622 43.776  0.424   1.00 8.00  ? 245  PHE A CG  1 
ATOM   1847 C  CD1 . PHE A 1 245  ? 29.565 44.425  -0.384  1.00 8.29  ? 245  PHE A CD1 1 
ATOM   1848 C  CD2 . PHE A 1 245  ? 27.818 44.524  1.274   1.00 9.42  ? 245  PHE A CD2 1 
ATOM   1849 C  CE1 . PHE A 1 245  ? 29.706 45.826  -0.342  1.00 8.42  ? 245  PHE A CE1 1 
ATOM   1850 C  CE2 . PHE A 1 245  ? 27.954 45.950  1.322   1.00 9.57  ? 245  PHE A CE2 1 
ATOM   1851 C  CZ  . PHE A 1 245  ? 28.906 46.576  0.500   1.00 9.49  ? 245  PHE A CZ  1 
ATOM   1852 N  N   . LEU A 1 246  ? 31.046 40.618  -0.208  1.00 8.92  ? 246  LEU A N   1 
ATOM   1853 C  CA  . LEU A 1 246  ? 32.316 40.550  -0.906  1.00 8.34  ? 246  LEU A CA  1 
ATOM   1854 C  C   . LEU A 1 246  ? 32.170 41.469  -2.128  1.00 8.04  ? 246  LEU A C   1 
ATOM   1855 O  O   . LEU A 1 246  ? 31.501 41.151  -3.107  1.00 9.08  ? 246  LEU A O   1 
ATOM   1856 C  CB  . LEU A 1 246  ? 32.613 39.088  -1.324  1.00 10.38 ? 246  LEU A CB  1 
ATOM   1857 C  CG  . LEU A 1 246  ? 32.936 38.196  -0.085  1.00 13.35 ? 246  LEU A CG  1 
ATOM   1858 C  CD1 . LEU A 1 246  ? 32.832 36.720  -0.533  1.00 17.02 ? 246  LEU A CD1 1 
ATOM   1859 C  CD2 . LEU A 1 246  ? 34.347 38.542  0.403   1.00 19.34 ? 246  LEU A CD2 1 
ATOM   1860 N  N   . TRP A 1 247  ? 32.785 42.646  -2.025  1.00 8.22  ? 247  TRP A N   1 
ATOM   1861 C  CA  . TRP A 1 247  ? 32.611 43.684  -3.053  1.00 7.66  ? 247  TRP A CA  1 
ATOM   1862 C  C   . TRP A 1 247  ? 33.647 43.480  -4.136  1.00 7.36  ? 247  TRP A C   1 
ATOM   1863 O  O   . TRP A 1 247  ? 34.851 43.651  -3.924  1.00 8.31  ? 247  TRP A O   1 
ATOM   1864 C  CB  . TRP A 1 247  ? 32.784 45.027  -2.375  1.00 7.99  ? 247  TRP A CB  1 
ATOM   1865 C  CG  . TRP A 1 247  ? 32.336 46.216  -3.225  1.00 7.24  ? 247  TRP A CG  1 
ATOM   1866 C  CD1 . TRP A 1 247  ? 31.814 46.206  -4.493  1.00 7.92  ? 247  TRP A CD1 1 
ATOM   1867 C  CD2 . TRP A 1 247  ? 32.356 47.583  -2.788  1.00 7.14  ? 247  TRP A CD2 1 
ATOM   1868 N  NE1 . TRP A 1 247  ? 31.471 47.504  -4.870  1.00 8.05  ? 247  TRP A NE1 1 
ATOM   1869 C  CE2 . TRP A 1 247  ? 31.800 48.351  -3.839  1.00 6.68  ? 247  TRP A CE2 1 
ATOM   1870 C  CE3 . TRP A 1 247  ? 32.774 48.236  -1.602  1.00 7.77  ? 247  TRP A CE3 1 
ATOM   1871 C  CZ2 . TRP A 1 247  ? 31.679 49.772  -3.749  1.00 8.27  ? 247  TRP A CZ2 1 
ATOM   1872 C  CZ3 . TRP A 1 247  ? 32.637 49.609  -1.527  1.00 7.66  ? 247  TRP A CZ3 1 
ATOM   1873 C  CH2 . TRP A 1 247  ? 32.111 50.373  -2.585  1.00 6.96  ? 247  TRP A CH2 1 
ATOM   1874 N  N   . ARG A 1 248  ? 33.156 43.071  -5.323  1.00 7.61  ? 248  ARG A N   1 
ATOM   1875 C  CA  . ARG A 1 248  ? 34.045 42.880  -6.460  1.00 7.78  ? 248  ARG A CA  1 
ATOM   1876 C  C   . ARG A 1 248  ? 33.779 43.968  -7.523  1.00 7.82  ? 248  ARG A C   1 
ATOM   1877 O  O   . ARG A 1 248  ? 32.739 44.632  -7.490  1.00 8.04  ? 248  ARG A O   1 
ATOM   1878 C  CB  . ARG A 1 248  ? 33.841 41.495  -7.131  1.00 8.60  ? 248  ARG A CB  1 
ATOM   1879 C  CG  . ARG A 1 248  ? 32.440 41.339  -7.784  1.00 8.19  ? 248  ARG A CG  1 
ATOM   1880 C  CD  . ARG A 1 248  ? 32.381 40.037  -8.639  1.00 11.95 ? 248  ARG A CD  1 
ATOM   1881 N  NE  . ARG A 1 248  ? 32.426 38.885  -7.724  1.00 11.26 ? 248  ARG A NE  1 
ATOM   1882 C  CZ  . ARG A 1 248  ? 32.407 37.624  -8.185  1.00 13.15 ? 248  ARG A CZ  1 
ATOM   1883 N  NH1 . ARG A 1 248  ? 32.370 37.387  -9.492  1.00 14.79 ? 248  ARG A NH1 1 
ATOM   1884 N  NH2 . ARG A 1 248  ? 32.367 36.609  -7.312  1.00 15.01 ? 248  ARG A NH2 1 
ATOM   1885 N  N   . GLN A 1 249  ? 34.722 44.119  -8.459  1.00 7.67  ? 249  GLN A N   1 
ATOM   1886 C  CA  . GLN A 1 249  ? 34.532 45.096  -9.548  1.00 7.53  ? 249  GLN A CA  1 
ATOM   1887 C  C   . GLN A 1 249  ? 33.420 44.648  -10.496 1.00 8.48  ? 249  GLN A C   1 
ATOM   1888 O  O   . GLN A 1 249  ? 33.150 43.453  -10.671 1.00 10.17 ? 249  GLN A O   1 
ATOM   1889 C  CB  . GLN A 1 249  ? 35.834 45.308  -10.339 1.00 9.28  ? 249  GLN A CB  1 
ATOM   1890 C  CG  . GLN A 1 249  ? 36.958 45.790  -9.396  1.00 8.69  ? 249  GLN A CG  1 
ATOM   1891 C  CD  . GLN A 1 249  ? 36.570 47.071  -8.647  1.00 8.71  ? 249  GLN A CD  1 
ATOM   1892 O  OE1 . GLN A 1 249  ? 36.554 47.124  -7.352  1.00 10.77 ? 249  GLN A OE1 1 
ATOM   1893 N  NE2 . GLN A 1 249  ? 36.239 48.096  -9.373  1.00 7.23  ? 249  GLN A NE2 1 
ATOM   1894 N  N   . ILE A 1 250  ? 32.783 45.614  -11.151 1.00 8.35  ? 250  ILE A N   1 
ATOM   1895 C  CA  . ILE A 1 250  ? 31.623 45.316  -11.991 1.00 9.34  ? 250  ILE A CA  1 
ATOM   1896 C  C   . ILE A 1 250  ? 31.929 44.408  -13.171 1.00 9.30  ? 250  ILE A C   1 
ATOM   1897 O  O   . ILE A 1 250  ? 30.988 43.736  -13.668 1.00 11.25 ? 250  ILE A O   1 
ATOM   1898 C  CB  . ILE A 1 250  ? 30.896 46.627  -12.522 1.00 11.01 ? 250  ILE A CB  1 
ATOM   1899 C  CG1 . ILE A 1 250  ? 31.890 47.535  -13.284 1.00 11.67 ? 250  ILE A CG1 1 
ATOM   1900 C  CG2 . ILE A 1 250  ? 30.254 47.378  -11.371 1.00 11.33 ? 250  ILE A CG2 1 
ATOM   1901 C  CD1 . ILE A 1 250  ? 31.243 48.869  -13.815 1.00 12.24 ? 250  ILE A CD1 1 
ATOM   1902 N  N   . TRP A 1 251  ? 33.175 44.356  -13.604 1.00 10.36 ? 251  TRP A N   1 
ATOM   1903 C  CA  . TRP A 1 251  ? 33.551 43.500  -14.741 1.00 10.54 ? 251  TRP A CA  1 
ATOM   1904 C  C   . TRP A 1 251  ? 34.194 42.190  -14.342 1.00 15.47 ? 251  TRP A C   1 
ATOM   1905 O  O   . TRP A 1 251  ? 34.491 41.349  -15.213 1.00 16.27 ? 251  TRP A O   1 
ATOM   1906 C  CB  . TRP A 1 251  ? 34.546 44.218  -15.669 1.00 12.86 ? 251  TRP A CB  1 
ATOM   1907 C  CG  . TRP A 1 251  ? 35.779 44.349  -14.981 1.00 16.34 ? 251  TRP A CG  1 
ATOM   1908 C  CD1 . TRP A 1 251  ? 36.745 43.375  -14.816 1.00 17.91 ? 251  TRP A CD1 1 
ATOM   1909 C  CD2 . TRP A 1 251  ? 36.209 45.473  -14.260 1.00 14.46 ? 251  TRP A CD2 1 
ATOM   1910 N  NE1 . TRP A 1 251  ? 37.721 43.848  -14.048 1.00 16.28 ? 251  TRP A NE1 1 
ATOM   1911 C  CE2 . TRP A 1 251  ? 37.442 45.139  -13.669 1.00 14.70 ? 251  TRP A CE2 1 
ATOM   1912 C  CE3 . TRP A 1 251  ? 35.677 46.728  -14.033 1.00 13.93 ? 251  TRP A CE3 1 
ATOM   1913 C  CZ2 . TRP A 1 251  ? 38.168 46.012  -12.865 1.00 17.43 ? 251  TRP A CZ2 1 
ATOM   1914 C  CZ3 . TRP A 1 251  ? 36.392 47.609  -13.234 1.00 16.01 ? 251  TRP A CZ3 1 
ATOM   1915 C  CH2 . TRP A 1 251  ? 37.623 47.247  -12.663 1.00 18.78 ? 251  TRP A CH2 1 
ATOM   1916 N  N   . ASP A 1 252  ? 34.381 41.957  -13.043 1.00 13.10 ? 252  ASP A N   1 
ATOM   1917 C  CA  . ASP A 1 252  ? 35.108 40.780  -12.570 1.00 14.29 ? 252  ASP A CA  1 
ATOM   1918 C  C   . ASP A 1 252  ? 34.289 39.510  -12.482 1.00 13.75 ? 252  ASP A C   1 
ATOM   1919 O  O   . ASP A 1 252  ? 33.543 39.292  -11.563 1.00 14.48 ? 252  ASP A O   1 
ATOM   1920 C  CB  . ASP A 1 252  ? 35.720 41.177  -11.216 1.00 11.67 ? 252  ASP A CB  1 
ATOM   1921 C  CG  . ASP A 1 252  ? 36.471 40.038  -10.552 1.00 16.60 ? 252  ASP A CG  1 
ATOM   1922 O  OD1 . ASP A 1 252  ? 36.725 39.002  -11.229 1.00 18.75 ? 252  ASP A OD1 1 
ATOM   1923 O  OD2 . ASP A 1 252  ? 36.795 40.195  -9.370  1.00 15.70 ? 252  ASP A OD2 1 
ATOM   1924 N  N   A ASN A 1 253  ? 34.402 38.664  -13.504 0.50 13.24 ? 253  ASN A N   1 
ATOM   1925 N  N   B ASN A 1 253  ? 34.402 38.664  -13.504 0.50 15.59 ? 253  ASN A N   1 
ATOM   1926 C  CA  A ASN A 1 253  ? 33.639 37.422  -13.524 0.50 11.83 ? 253  ASN A CA  1 
ATOM   1927 C  CA  B ASN A 1 253  ? 33.639 37.422  -13.524 0.50 16.45 ? 253  ASN A CA  1 
ATOM   1928 C  C   A ASN A 1 253  ? 34.077 36.361  -12.503 0.50 13.45 ? 253  ASN A C   1 
ATOM   1929 C  C   B ASN A 1 253  ? 34.077 36.361  -12.503 0.50 16.15 ? 253  ASN A C   1 
ATOM   1930 O  O   A ASN A 1 253  ? 33.248 35.717  -11.904 0.50 17.48 ? 253  ASN A O   1 
ATOM   1931 O  O   B ASN A 1 253  ? 33.248 35.717  -11.904 0.50 19.07 ? 253  ASN A O   1 
ATOM   1932 C  CB  A ASN A 1 253  ? 33.741 36.816  -14.953 0.50 14.24 ? 253  ASN A CB  1 
ATOM   1933 C  CB  B ASN A 1 253  ? 33.741 36.816  -14.953 0.50 22.62 ? 253  ASN A CB  1 
ATOM   1934 C  CG  A ASN A 1 253  ? 32.932 35.570  -15.090 0.50 18.23 ? 253  ASN A CG  1 
ATOM   1935 C  CG  B ASN A 1 253  ? 32.461 36.182  -15.383 0.50 29.63 ? 253  ASN A CG  1 
ATOM   1936 O  OD1 A ASN A 1 253  ? 33.468 34.498  -15.416 0.50 19.15 ? 253  ASN A OD1 1 
ATOM   1937 O  OD1 B ASN A 1 253  ? 32.330 34.947  -15.376 0.50 36.16 ? 253  ASN A OD1 1 
ATOM   1938 N  ND2 A ASN A 1 253  ? 31.641 35.676  -14.845 0.50 13.37 ? 253  ASN A ND2 1 
ATOM   1939 N  ND2 B ASN A 1 253  ? 31.497 36.999  -15.760 0.50 29.42 ? 253  ASN A ND2 1 
ATOM   1940 N  N   . LYS A 1 254  ? 35.364 36.305  -12.274 1.00 16.64 ? 254  LYS A N   1 
ATOM   1941 C  CA  . LYS A 1 254  ? 35.892 35.269  -11.366 1.00 20.85 ? 254  LYS A CA  1 
ATOM   1942 C  C   . LYS A 1 254  ? 35.837 35.652  -9.900  1.00 20.19 ? 254  LYS A C   1 
ATOM   1943 O  O   . LYS A 1 254  ? 35.693 34.789  -9.030  1.00 22.37 ? 254  LYS A O   1 
ATOM   1944 C  CB  . LYS A 1 254  ? 37.329 34.961  -11.756 1.00 27.31 ? 254  LYS A CB  1 
ATOM   1945 C  CG  . LYS A 1 254  ? 37.985 33.759  -11.060 1.00 33.99 ? 254  LYS A CG  1 
ATOM   1946 C  CD  . LYS A 1 254  ? 39.385 33.542  -11.678 1.00 36.50 ? 254  LYS A CD  1 
ATOM   1947 C  CE  . LYS A 1 254  ? 40.155 32.356  -11.073 1.00 38.12 ? 254  LYS A CE  1 
ATOM   1948 N  NZ  . LYS A 1 254  ? 40.469 32.479  -9.620  1.00 39.80 ? 254  LYS A NZ  1 
ATOM   1949 N  N   . GLY A 1 255  ? 35.957 36.943  -9.600  1.00 16.29 ? 255  GLY A N   1 
ATOM   1950 C  CA  . GLY A 1 255  ? 35.910 37.343  -8.194  1.00 16.93 ? 255  GLY A CA  1 
ATOM   1951 C  C   . GLY A 1 255  ? 37.267 37.624  -7.559  1.00 14.93 ? 255  GLY A C   1 
ATOM   1952 O  O   . GLY A 1 255  ? 37.275 37.921  -6.368  1.00 15.10 ? 255  GLY A O   1 
ATOM   1953 N  N   . ASP A 1 256  ? 38.377 37.637  -8.293  1.00 15.87 ? 256  ASP A N   1 
ATOM   1954 C  CA  . ASP A 1 256  ? 39.677 37.887  -7.669  1.00 19.35 ? 256  ASP A CA  1 
ATOM   1955 C  C   . ASP A 1 256  ? 39.878 39.292  -7.119  1.00 16.18 ? 256  ASP A C   1 
ATOM   1956 O  O   . ASP A 1 256  ? 40.769 39.531  -6.328  1.00 16.90 ? 256  ASP A O   1 
ATOM   1957 C  CB  . ASP A 1 256  ? 40.839 37.577  -8.630  1.00 26.30 ? 256  ASP A CB  1 
ATOM   1958 C  CG  . ASP A 1 256  ? 40.897 36.095  -9.028  1.00 36.40 ? 256  ASP A CG  1 
ATOM   1959 O  OD1 . ASP A 1 256  ? 40.395 35.249  -8.253  1.00 36.86 ? 256  ASP A OD1 1 
ATOM   1960 O  OD2 . ASP A 1 256  ? 41.458 35.799  -10.115 1.00 39.66 ? 256  ASP A OD2 1 
ATOM   1961 N  N   . THR A 1 257  ? 39.029 40.239  -7.517  1.00 12.18 ? 257  THR A N   1 
ATOM   1962 C  CA  . THR A 1 257  ? 39.155 41.594  -6.958  1.00 12.08 ? 257  THR A CA  1 
ATOM   1963 C  C   . THR A 1 257  ? 38.365 41.774  -5.651  1.00 12.25 ? 257  THR A C   1 
ATOM   1964 O  O   . THR A 1 257  ? 38.427 42.853  -5.044  1.00 12.10 ? 257  THR A O   1 
ATOM   1965 C  CB  . THR A 1 257  ? 38.581 42.678  -7.958  1.00 12.47 ? 257  THR A CB  1 
ATOM   1966 O  OG1 . THR A 1 257  ? 37.176 42.459  -8.146  1.00 11.35 ? 257  THR A OG1 1 
ATOM   1967 C  CG2 . THR A 1 257  ? 39.360 42.648  -9.289  1.00 13.56 ? 257  THR A CG2 1 
ATOM   1968 N  N   . ALA A 1 258  ? 37.604 40.748  -5.251  1.00 10.57 ? 258  ALA A N   1 
ATOM   1969 C  CA  . ALA A 1 258  ? 36.713 40.886  -4.096  1.00 11.03 ? 258  ALA A CA  1 
ATOM   1970 C  C   . ALA A 1 258  ? 37.381 41.293  -2.793  1.00 9.91  ? 258  ALA A C   1 
ATOM   1971 O  O   . ALA A 1 258  ? 38.450 40.790  -2.456  1.00 11.64 ? 258  ALA A O   1 
ATOM   1972 C  CB  . ALA A 1 258  ? 35.916 39.598  -3.817  1.00 10.84 ? 258  ALA A CB  1 
ATOM   1973 N  N   . LEU A 1 259  ? 36.725 42.195  -2.078  1.00 8.61  ? 259  LEU A N   1 
ATOM   1974 C  CA  . LEU A 1 259  ? 37.183 42.629  -0.748  1.00 8.40  ? 259  LEU A CA  1 
ATOM   1975 C  C   . LEU A 1 259  ? 35.989 42.620  0.178   1.00 8.53  ? 259  LEU A C   1 
ATOM   1976 O  O   . LEU A 1 259  ? 34.945 43.238  -0.090  1.00 8.38  ? 259  LEU A O   1 
ATOM   1977 C  CB  . LEU A 1 259  ? 37.781 44.019  -0.831  1.00 9.41  ? 259  LEU A CB  1 
ATOM   1978 C  CG  . LEU A 1 259  ? 38.525 44.417  0.465   1.00 8.08  ? 259  LEU A CG  1 
ATOM   1979 C  CD1 . LEU A 1 259  ? 39.800 43.530  0.744   1.00 10.23 ? 259  LEU A CD1 1 
ATOM   1980 C  CD2 . LEU A 1 259  ? 38.990 45.884  0.296   1.00 10.95 ? 259  LEU A CD2 1 
ATOM   1981 N  N   . PHE A 1 260  ? 36.152 41.961  1.343   1.00 8.35  ? 260  PHE A N   1 
ATOM   1982 C  CA  . PHE A 1 260  ? 35.070 41.932  2.319   1.00 7.71  ? 260  PHE A CA  1 
ATOM   1983 C  C   . PHE A 1 260  ? 34.764 43.326  2.804   1.00 7.20  ? 260  PHE A C   1 
ATOM   1984 O  O   . PHE A 1 260  ? 35.681 44.065  3.259   1.00 8.23  ? 260  PHE A O   1 
ATOM   1985 C  CB  . PHE A 1 260  ? 35.500 41.011  3.509   1.00 8.36  ? 260  PHE A CB  1 
ATOM   1986 C  CG  . PHE A 1 260  ? 34.393 40.863  4.547   1.00 8.30  ? 260  PHE A CG  1 
ATOM   1987 C  CD1 . PHE A 1 260  ? 33.407 39.900  4.328   1.00 10.41 ? 260  PHE A CD1 1 
ATOM   1988 C  CD2 . PHE A 1 260  ? 34.295 41.624  5.673   1.00 8.77  ? 260  PHE A CD2 1 
ATOM   1989 C  CE1 . PHE A 1 260  ? 32.330 39.719  5.271   1.00 12.68 ? 260  PHE A CE1 1 
ATOM   1990 C  CE2 . PHE A 1 260  ? 33.230 41.478  6.634   1.00 10.50 ? 260  PHE A CE2 1 
ATOM   1991 C  CZ  . PHE A 1 260  ? 32.253 40.522  6.422   1.00 12.73 ? 260  PHE A CZ  1 
ATOM   1992 N  N   . THR A 1 261  ? 33.475 43.686  2.782   1.00 7.39  ? 261  THR A N   1 
ATOM   1993 C  CA  . THR A 1 261  ? 33.064 45.033  3.133   1.00 7.61  ? 261  THR A CA  1 
ATOM   1994 C  C   . THR A 1 261  ? 31.922 44.982  4.158   1.00 7.81  ? 261  THR A C   1 
ATOM   1995 O  O   . THR A 1 261  ? 30.955 44.215  3.983   1.00 9.11  ? 261  THR A O   1 
ATOM   1996 C  CB  . THR A 1 261  ? 32.552 45.769  1.835   1.00 8.18  ? 261  THR A CB  1 
ATOM   1997 O  OG1 . THR A 1 261  ? 33.613 45.824  0.895   1.00 8.43  ? 261  THR A OG1 1 
ATOM   1998 C  CG2 . THR A 1 261  ? 32.111 47.163  2.114   1.00 9.04  ? 261  THR A CG2 1 
ATOM   1999 N  N   . HIS A 1 262  ? 32.021 45.865  5.157   1.00 7.44  ? 262  HIS A N   1 
ATOM   2000 C  CA  . HIS A 1 262  ? 30.961 46.050  6.137   1.00 7.00  ? 262  HIS A CA  1 
ATOM   2001 C  C   . HIS A 1 262  ? 30.336 47.429  5.955   1.00 7.92  ? 262  HIS A C   1 
ATOM   2002 O  O   . HIS A 1 262  ? 31.043 48.460  6.081   1.00 8.28  ? 262  HIS A O   1 
ATOM   2003 C  CB  . HIS A 1 262  ? 31.593 45.961  7.561   1.00 8.69  ? 262  HIS A CB  1 
ATOM   2004 C  CG  . HIS A 1 262  ? 30.640 46.302  8.659   1.00 7.80  ? 262  HIS A CG  1 
ATOM   2005 N  ND1 . HIS A 1 262  ? 30.042 45.325  9.429   1.00 9.11  ? 262  HIS A ND1 1 
ATOM   2006 C  CD2 . HIS A 1 262  ? 30.171 47.491  9.106   1.00 7.99  ? 262  HIS A CD2 1 
ATOM   2007 C  CE1 . HIS A 1 262  ? 29.255 45.923  10.324  1.00 10.35 ? 262  HIS A CE1 1 
ATOM   2008 N  NE2 . HIS A 1 262  ? 29.297 47.239  10.145  1.00 9.70  ? 262  HIS A NE2 1 
ATOM   2009 N  N   . MET A 1 263  ? 29.055 47.489  5.626   1.00 7.93  ? 263  MET A N   1 
ATOM   2010 C  CA  . MET A 1 263  ? 28.327 48.732  5.564   1.00 7.30  ? 263  MET A CA  1 
ATOM   2011 C  C   . MET A 1 263  ? 27.604 48.921  6.920   1.00 8.43  ? 263  MET A C   1 
ATOM   2012 O  O   . MET A 1 263  ? 26.832 48.010  7.345   1.00 9.53  ? 263  MET A O   1 
ATOM   2013 C  CB  . MET A 1 263  ? 27.297 48.666  4.423   1.00 8.36  ? 263  MET A CB  1 
ATOM   2014 C  CG  . MET A 1 263  ? 26.506 49.975  4.301   1.00 8.88  ? 263  MET A CG  1 
ATOM   2015 S  SD  . MET A 1 263  ? 25.161 49.871  3.090   1.00 9.89  ? 263  MET A SD  1 
ATOM   2016 C  CE  . MET A 1 263  ? 26.017 49.481  1.545   1.00 10.44 ? 263  MET A CE  1 
ATOM   2017 N  N   A MET A 1 264  ? 27.815 50.057  7.588   0.50 5.95  ? 264  MET A N   1 
ATOM   2018 N  N   B MET A 1 264  ? 27.844 50.054  7.602   0.50 11.07 ? 264  MET A N   1 
ATOM   2019 C  CA  A MET A 1 264  ? 27.097 50.396  8.839   0.50 5.60  ? 264  MET A CA  1 
ATOM   2020 C  CA  B MET A 1 264  ? 27.082 50.392  8.797   0.50 13.63 ? 264  MET A CA  1 
ATOM   2021 C  C   A MET A 1 264  ? 25.625 50.609  8.439   0.50 6.25  ? 264  MET A C   1 
ATOM   2022 C  C   B MET A 1 264  ? 25.611 50.616  8.467   0.50 11.71 ? 264  MET A C   1 
ATOM   2023 O  O   A MET A 1 264  ? 25.303 51.066  7.323   0.50 8.63  ? 264  MET A O   1 
ATOM   2024 O  O   B MET A 1 264  ? 25.303 51.066  7.323   0.50 11.77 ? 264  MET A O   1 
ATOM   2025 C  CB  A MET A 1 264  ? 27.723 51.591  9.504   0.50 4.21  ? 264  MET A CB  1 
ATOM   2026 C  CB  B MET A 1 264  ? 27.673 51.629  9.476   0.50 21.14 ? 264  MET A CB  1 
ATOM   2027 C  CG  A MET A 1 264  ? 29.189 51.301  9.933   0.50 2.37  ? 264  MET A CG  1 
ATOM   2028 C  CG  B MET A 1 264  ? 29.071 51.421  10.036  0.50 31.92 ? 264  MET A CG  1 
ATOM   2029 S  SD  A MET A 1 264  ? 30.089 52.852  10.468  0.50 7.68  ? 264  MET A SD  1 
ATOM   2030 S  SD  B MET A 1 264  ? 29.334 52.292  11.592  0.50 40.26 ? 264  MET A SD  1 
ATOM   2031 C  CE  A MET A 1 264  ? 29.046 53.566  11.595  0.50 6.89  ? 264  MET A CE  1 
ATOM   2032 C  CE  B MET A 1 264  ? 29.486 53.981  11.014  0.50 41.29 ? 264  MET A CE  1 
ATOM   2033 N  N   . PRO A 1 265  ? 24.710 50.343  9.384   1.00 9.36  ? 265  PRO A N   1 
ATOM   2034 C  CA  . PRO A 1 265  ? 23.286 50.382  9.014   1.00 10.04 ? 265  PRO A CA  1 
ATOM   2035 C  C   . PRO A 1 265  ? 22.463 51.594  9.189   1.00 10.47 ? 265  PRO A C   1 
ATOM   2036 O  O   . PRO A 1 265  ? 21.391 51.646  8.592   1.00 10.83 ? 265  PRO A O   1 
ATOM   2037 C  CB  . PRO A 1 265  ? 22.687 49.224  9.898   1.00 11.35 ? 265  PRO A CB  1 
ATOM   2038 C  CG  . PRO A 1 265  ? 23.515 49.325  11.161  1.00 13.47 ? 265  PRO A CG  1 
ATOM   2039 C  CD  . PRO A 1 265  ? 24.948 49.771  10.732  1.00 9.64  ? 265  PRO A CD  1 
ATOM   2040 N  N   . PHE A 1 266  ? 22.939 52.540  9.961   1.00 9.86  ? 266  PHE A N   1 
ATOM   2041 C  CA  . PHE A 1 266  ? 22.157 53.654  10.412  1.00 10.21 ? 266  PHE A CA  1 
ATOM   2042 C  C   . PHE A 1 266  ? 22.543 55.002  9.821   1.00 10.12 ? 266  PHE A C   1 
ATOM   2043 O  O   . PHE A 1 266  ? 23.443 55.112  8.996   1.00 10.68 ? 266  PHE A O   1 
ATOM   2044 C  CB  . PHE A 1 266  ? 22.127 53.638  11.967  1.00 10.25 ? 266  PHE A CB  1 
ATOM   2045 C  CG  . PHE A 1 266  ? 21.565 52.305  12.567  1.00 11.23 ? 266  PHE A CG  1 
ATOM   2046 C  CD1 . PHE A 1 266  ? 22.201 51.737  13.664  1.00 10.98 ? 266  PHE A CD1 1 
ATOM   2047 C  CD2 . PHE A 1 266  ? 20.424 51.664  12.022  1.00 11.53 ? 266  PHE A CD2 1 
ATOM   2048 C  CE1 . PHE A 1 266  ? 21.695 50.536  14.235  1.00 11.52 ? 266  PHE A CE1 1 
ATOM   2049 C  CE2 . PHE A 1 266  ? 19.939 50.469  12.596  1.00 10.98 ? 266  PHE A CE2 1 
ATOM   2050 C  CZ  . PHE A 1 266  ? 20.563 49.926  13.675  1.00 10.69 ? 266  PHE A CZ  1 
ATOM   2051 N  N   . TYR A 1 267  ? 21.861 56.032  10.263  1.00 9.86  ? 267  TYR A N   1 
ATOM   2052 C  CA  . TYR A 1 267  ? 21.949 57.344  9.640   1.00 9.49  ? 267  TYR A CA  1 
ATOM   2053 C  C   . TYR A 1 267  ? 23.286 58.054  9.881   1.00 10.68 ? 267  TYR A C   1 
ATOM   2054 O  O   . TYR A 1 267  ? 23.686 58.868  9.039   1.00 10.86 ? 267  TYR A O   1 
ATOM   2055 C  CB  . TYR A 1 267  ? 20.787 58.183  10.198  1.00 12.29 ? 267  TYR A CB  1 
ATOM   2056 C  CG  . TYR A 1 267  ? 20.898 59.700  10.091  1.00 11.25 ? 267  TYR A CG  1 
ATOM   2057 C  CD1 . TYR A 1 267  ? 20.583 60.366  8.910   1.00 13.98 ? 267  TYR A CD1 1 
ATOM   2058 C  CD2 . TYR A 1 267  ? 21.302 60.464  11.196  1.00 12.54 ? 267  TYR A CD2 1 
ATOM   2059 C  CE1 . TYR A 1 267  ? 20.666 61.761  8.809   1.00 13.32 ? 267  TYR A CE1 1 
ATOM   2060 C  CE2 . TYR A 1 267  ? 21.378 61.840  11.107  1.00 14.35 ? 267  TYR A CE2 1 
ATOM   2061 C  CZ  . TYR A 1 267  ? 21.051 62.466  9.914   1.00 14.91 ? 267  TYR A CZ  1 
ATOM   2062 O  OH  . TYR A 1 267  ? 21.060 63.870  9.869   1.00 19.28 ? 267  TYR A OH  1 
ATOM   2063 N  N   . SER A 1 268  ? 23.984 57.754  10.963  1.00 9.93  ? 268  SER A N   1 
ATOM   2064 C  CA  . SER A 1 268  ? 25.247 58.435  11.291  1.00 10.87 ? 268  SER A CA  1 
ATOM   2065 C  C   . SER A 1 268  ? 26.190 57.487  11.972  1.00 9.63  ? 268  SER A C   1 
ATOM   2066 O  O   . SER A 1 268  ? 25.783 56.373  12.399  1.00 10.39 ? 268  SER A O   1 
ATOM   2067 C  CB  . SER A 1 268  ? 24.933 59.613  12.244  1.00 10.37 ? 268  SER A CB  1 
ATOM   2068 O  OG  . SER A 1 268  ? 26.123 60.255  12.715  1.00 12.18 ? 268  SER A OG  1 
ATOM   2069 N  N   . TYR A 1 269  ? 27.495 57.873  12.054  1.00 10.29 ? 269  TYR A N   1 
ATOM   2070 C  CA  . TYR A 1 269  ? 28.467 57.130  12.857  1.00 9.44  ? 269  TYR A CA  1 
ATOM   2071 C  C   . TYR A 1 269  ? 28.552 57.648  14.299  1.00 10.22 ? 269  TYR A C   1 
ATOM   2072 O  O   . TYR A 1 269  ? 29.400 57.180  15.059  1.00 10.19 ? 269  TYR A O   1 
ATOM   2073 C  CB  . TYR A 1 269  ? 29.883 57.231  12.195  1.00 9.42  ? 269  TYR A CB  1 
ATOM   2074 C  CG  . TYR A 1 269  ? 30.343 58.651  11.930  1.00 10.93 ? 269  TYR A CG  1 
ATOM   2075 C  CD1 . TYR A 1 269  ? 30.789 59.477  12.947  1.00 9.92  ? 269  TYR A CD1 1 
ATOM   2076 C  CD2 . TYR A 1 269  ? 30.266 59.158  10.635  1.00 11.20 ? 269  TYR A CD2 1 
ATOM   2077 C  CE1 . TYR A 1 269  ? 31.177 60.792  12.718  1.00 10.97 ? 269  TYR A CE1 1 
ATOM   2078 C  CE2 . TYR A 1 269  ? 30.662 60.504  10.362  1.00 11.47 ? 269  TYR A CE2 1 
ATOM   2079 C  CZ  . TYR A 1 269  ? 31.106 61.280  11.436  1.00 10.75 ? 269  TYR A CZ  1 
ATOM   2080 O  OH  . TYR A 1 269  ? 31.439 62.603  11.115  1.00 12.93 ? 269  TYR A OH  1 
ATOM   2081 N  N   . ASP A 1 270  ? 27.748 58.648  14.652  1.00 9.72  ? 270  ASP A N   1 
ATOM   2082 C  CA  . ASP A 1 270  ? 27.766 59.140  16.045  1.00 9.93  ? 270  ASP A CA  1 
ATOM   2083 C  C   . ASP A 1 270  ? 27.190 58.106  17.040  1.00 9.87  ? 270  ASP A C   1 
ATOM   2084 O  O   . ASP A 1 270  ? 26.637 57.086  16.605  1.00 10.04 ? 270  ASP A O   1 
ATOM   2085 C  CB  . ASP A 1 270  ? 27.103 60.534  16.125  1.00 11.66 ? 270  ASP A CB  1 
ATOM   2086 C  CG  . ASP A 1 270  ? 25.596 60.529  15.909  1.00 14.66 ? 270  ASP A CG  1 
ATOM   2087 O  OD1 . ASP A 1 270  ? 24.952 59.445  15.801  1.00 14.08 ? 270  ASP A OD1 1 
ATOM   2088 O  OD2 . ASP A 1 270  ? 25.025 61.685  15.889  1.00 16.35 ? 270  ASP A OD2 1 
ATOM   2089 N  N   . ILE A 1 271  ? 27.401 58.325  18.325  1.00 9.75  ? 271  ILE A N   1 
ATOM   2090 C  CA  . ILE A 1 271  ? 26.986 57.317  19.307  1.00 10.28 ? 271  ILE A CA  1 
ATOM   2091 C  C   . ILE A 1 271  ? 25.456 57.046  19.268  1.00 9.26  ? 271  ILE A C   1 
ATOM   2092 O  O   . ILE A 1 271  ? 25.055 55.888  19.294  1.00 10.33 ? 271  ILE A O   1 
ATOM   2093 C  CB  . ILE A 1 271  ? 27.522 57.657  20.688  1.00 11.07 ? 271  ILE A CB  1 
ATOM   2094 C  CG1 . ILE A 1 271  ? 29.061 57.533  20.621  1.00 10.22 ? 271  ILE A CG1 1 
ATOM   2095 C  CG2 . ILE A 1 271  ? 26.952 56.690  21.725  1.00 11.12 ? 271  ILE A CG2 1 
ATOM   2096 C  CD1 . ILE A 1 271  ? 29.775 58.201  21.769  1.00 10.10 ? 271  ILE A CD1 1 
ATOM   2097 N  N   . PRO A 1 272  ? 24.629 58.089  19.120  1.00 10.46 ? 272  PRO A N   1 
ATOM   2098 C  CA  . PRO A 1 272  ? 23.176 57.827  19.062  1.00 11.04 ? 272  PRO A CA  1 
ATOM   2099 C  C   . PRO A 1 272  ? 22.798 56.916  17.918  1.00 12.60 ? 272  PRO A C   1 
ATOM   2100 O  O   . PRO A 1 272  ? 21.720 56.276  17.982  1.00 12.48 ? 272  PRO A O   1 
ATOM   2101 C  CB  . PRO A 1 272  ? 22.562 59.210  18.871  1.00 11.08 ? 272  PRO A CB  1 
ATOM   2102 C  CG  . PRO A 1 272  ? 23.496 60.142  19.657  1.00 12.30 ? 272  PRO A CG  1 
ATOM   2103 C  CD  . PRO A 1 272  ? 24.891 59.543  19.279  1.00 10.35 ? 272  PRO A CD  1 
ATOM   2104 N  N   . HIS A 1 273  ? 23.625 56.796  16.860  1.00 10.68 ? 273  HIS A N   1 
ATOM   2105 C  CA  . HIS A 1 273  ? 23.253 55.953  15.699  1.00 11.10 ? 273  HIS A CA  1 
ATOM   2106 C  C   . HIS A 1 273  ? 24.196 54.781  15.501  1.00 9.57  ? 273  HIS A C   1 
ATOM   2107 O  O   . HIS A 1 273  ? 24.238 54.185  14.427  1.00 10.77 ? 273  HIS A O   1 
ATOM   2108 C  CB  . HIS A 1 273  ? 23.120 56.782  14.382  1.00 10.90 ? 273  HIS A CB  1 
ATOM   2109 C  CG  . HIS A 1 273  ? 22.119 57.897  14.496  1.00 11.44 ? 273  HIS A CG  1 
ATOM   2110 N  ND1 . HIS A 1 273  ? 20.766 57.830  14.146  1.00 12.92 ? 273  HIS A ND1 1 
ATOM   2111 C  CD2 . HIS A 1 273  ? 22.317 59.142  14.987  1.00 8.29  ? 273  HIS A CD2 1 
ATOM   2112 C  CE1 . HIS A 1 273  ? 20.192 58.993  14.421  1.00 9.13  ? 273  HIS A CE1 1 
ATOM   2113 N  NE2 . HIS A 1 273  ? 21.104 59.802  14.935  1.00 14.25 ? 273  HIS A NE2 1 
ATOM   2114 N  N   . THR A 1 274  ? 24.857 54.382  16.600  1.00 10.53 ? 274  THR A N   1 
ATOM   2115 C  CA  . THR A 1 274  ? 25.761 53.235  16.480  1.00 10.47 ? 274  THR A CA  1 
ATOM   2116 C  C   . THR A 1 274  ? 25.524 52.149  17.534  1.00 10.38 ? 274  THR A C   1 
ATOM   2117 O  O   . THR A 1 274  ? 26.069 51.047  17.381  1.00 12.71 ? 274  THR A O   1 
ATOM   2118 C  CB  . THR A 1 274  ? 27.257 53.640  16.454  1.00 10.82 ? 274  THR A CB  1 
ATOM   2119 O  OG1 . THR A 1 274  ? 27.524 54.578  17.505  1.00 10.70 ? 274  THR A OG1 1 
ATOM   2120 C  CG2 . THR A 1 274  ? 27.602 54.231  15.083  1.00 11.32 ? 274  THR A CG2 1 
ATOM   2121 N  N   . CYS A 1 275  ? 24.725 52.390  18.592  1.00 11.38 ? 275  CYS A N   1 
ATOM   2122 C  CA  . CYS A 1 275  ? 24.529 51.297  19.542  1.00 12.58 ? 275  CYS A CA  1 
ATOM   2123 C  C   . CYS A 1 275  ? 23.371 50.378  19.126  1.00 11.76 ? 275  CYS A C   1 
ATOM   2124 O  O   . CYS A 1 275  ? 23.321 49.229  19.591  1.00 13.23 ? 275  CYS A O   1 
ATOM   2125 C  CB  . CYS A 1 275  ? 24.241 51.913  20.922  1.00 11.58 ? 275  CYS A CB  1 
ATOM   2126 S  SG  . CYS A 1 275  ? 22.508 51.992  21.481  1.00 15.13 ? 275  CYS A SG  1 
ATOM   2127 N  N   . GLY A 1 276  ? 22.482 50.844  18.263  1.00 11.31 ? 276  GLY A N   1 
ATOM   2128 C  CA  . GLY A 1 276  ? 21.256 50.119  17.901  1.00 12.19 ? 276  GLY A CA  1 
ATOM   2129 C  C   . GLY A 1 276  ? 20.344 51.053  17.163  1.00 12.20 ? 276  GLY A C   1 
ATOM   2130 O  O   . GLY A 1 276  ? 20.718 52.229  16.904  1.00 12.40 ? 276  GLY A O   1 
ATOM   2131 N  N   . PRO A 1 277  ? 19.102 50.626  16.849  1.00 11.00 ? 277  PRO A N   1 
ATOM   2132 C  CA  . PRO A 1 277  ? 18.133 51.384  16.101  1.00 11.32 ? 277  PRO A CA  1 
ATOM   2133 C  C   . PRO A 1 277  ? 17.459 52.583  16.691  1.00 11.90 ? 277  PRO A C   1 
ATOM   2134 O  O   . PRO A 1 277  ? 16.884 53.367  15.927  1.00 12.19 ? 277  PRO A O   1 
ATOM   2135 C  CB  . PRO A 1 277  ? 17.082 50.306  15.707  1.00 13.86 ? 277  PRO A CB  1 
ATOM   2136 C  CG  . PRO A 1 277  ? 17.125 49.409  16.924  1.00 11.47 ? 277  PRO A CG  1 
ATOM   2137 C  CD  . PRO A 1 277  ? 18.595 49.273  17.188  1.00 12.17 ? 277  PRO A CD  1 
ATOM   2138 N  N   . ASP A 1 278  ? 17.508 52.698  18.010  1.00 13.20 ? 278  ASP A N   1 
ATOM   2139 C  CA  . ASP A 1 278  ? 16.750 53.806  18.643  1.00 12.29 ? 278  ASP A CA  1 
ATOM   2140 C  C   . ASP A 1 278  ? 17.709 54.871  19.216  1.00 12.90 ? 278  ASP A C   1 
ATOM   2141 O  O   . ASP A 1 278  ? 18.294 54.679  20.279  1.00 12.88 ? 278  ASP A O   1 
ATOM   2142 C  CB  . ASP A 1 278  ? 15.896 53.251  19.821  1.00 12.90 ? 278  ASP A CB  1 
ATOM   2143 C  CG  . ASP A 1 278  ? 14.980 54.324  20.387  1.00 15.69 ? 278  ASP A CG  1 
ATOM   2144 O  OD1 . ASP A 1 278  ? 15.110 55.509  20.037  1.00 16.63 ? 278  ASP A OD1 1 
ATOM   2145 O  OD2 . ASP A 1 278  ? 14.107 53.973  21.211  1.00 18.05 ? 278  ASP A OD2 1 
ATOM   2146 N  N   . PRO A 1 279  ? 17.838 56.001  18.506  1.00 13.76 ? 279  PRO A N   1 
ATOM   2147 C  CA  . PRO A 1 279  ? 18.752 57.025  19.026  1.00 14.26 ? 279  PRO A CA  1 
ATOM   2148 C  C   . PRO A 1 279  ? 18.425 57.635  20.354  1.00 13.19 ? 279  PRO A C   1 
ATOM   2149 O  O   . PRO A 1 279  ? 19.299 58.096  21.059  1.00 14.29 ? 279  PRO A O   1 
ATOM   2150 C  CB  . PRO A 1 279  ? 18.810 58.053  17.906  1.00 14.12 ? 279  PRO A CB  1 
ATOM   2151 C  CG  . PRO A 1 279  ? 17.503 57.930  17.197  1.00 14.11 ? 279  PRO A CG  1 
ATOM   2152 C  CD  . PRO A 1 279  ? 17.130 56.429  17.285  1.00 13.29 ? 279  PRO A CD  1 
ATOM   2153 N  N   . LYS A 1 280  ? 17.136 57.648  20.725  1.00 12.88 ? 280  LYS A N   1 
ATOM   2154 C  CA  . LYS A 1 280  ? 16.759 58.196  22.026  1.00 14.80 ? 280  LYS A CA  1 
ATOM   2155 C  C   . LYS A 1 280  ? 17.387 57.322  23.122  1.00 13.14 ? 280  LYS A C   1 
ATOM   2156 O  O   . LYS A 1 280  ? 17.752 57.821  24.193  1.00 16.45 ? 280  LYS A O   1 
ATOM   2157 C  CB  . LYS A 1 280  ? 15.232 58.222  22.130  1.00 16.31 ? 280  LYS A CB  1 
ATOM   2158 C  CG  . LYS A 1 280  ? 14.714 58.684  23.461  1.00 17.55 ? 280  LYS A CG  1 
ATOM   2159 C  CD  . LYS A 1 280  ? 13.181 58.716  23.388  1.00 23.31 ? 280  LYS A CD  1 
ATOM   2160 C  CE  . LYS A 1 280  ? 12.611 59.575  24.502  1.00 34.10 ? 280  LYS A CE  1 
ATOM   2161 N  NZ  . LYS A 1 280  ? 11.117 59.666  24.386  1.00 37.53 ? 280  LYS A NZ  1 
ATOM   2162 N  N   . VAL A 1 281  ? 17.504 56.017  22.886  1.00 13.64 ? 281  VAL A N   1 
ATOM   2163 C  CA  . VAL A 1 281  ? 18.168 55.124  23.829  1.00 14.47 ? 281  VAL A CA  1 
ATOM   2164 C  C   . VAL A 1 281  ? 19.711 55.218  23.716  1.00 14.09 ? 281  VAL A C   1 
ATOM   2165 O  O   . VAL A 1 281  ? 20.419 55.404  24.716  1.00 12.88 ? 281  VAL A O   1 
ATOM   2166 C  CB  . VAL A 1 281  ? 17.757 53.621  23.609  1.00 14.79 ? 281  VAL A CB  1 
ATOM   2167 C  CG1 . VAL A 1 281  ? 18.513 52.696  24.571  1.00 17.15 ? 281  VAL A CG1 1 
ATOM   2168 C  CG2 . VAL A 1 281  ? 16.215 53.533  23.845  1.00 15.41 ? 281  VAL A CG2 1 
ATOM   2169 N  N   . CYS A 1 282  ? 20.236 55.095  22.483  1.00 12.97 ? 282  CYS A N   1 
ATOM   2170 C  CA  . CYS A 1 282  ? 21.699 55.121  22.325  1.00 12.18 ? 282  CYS A CA  1 
ATOM   2171 C  C   . CYS A 1 282  ? 22.342 56.439  22.821  1.00 10.83 ? 282  CYS A C   1 
ATOM   2172 O  O   . CYS A 1 282  ? 23.457 56.397  23.351  1.00 11.80 ? 282  CYS A O   1 
ATOM   2173 C  CB  . CYS A 1 282  ? 22.061 54.930  20.850  1.00 12.65 ? 282  CYS A CB  1 
ATOM   2174 S  SG  . CYS A 1 282  ? 21.629 53.303  20.183  1.00 14.16 ? 282  CYS A SG  1 
ATOM   2175 N  N   . CYS A 1 283  ? 21.646 57.564  22.659  1.00 11.59 ? 283  CYS A N   1 
ATOM   2176 C  CA  . CYS A 1 283  ? 22.223 58.808  23.148  1.00 12.30 ? 283  CYS A CA  1 
ATOM   2177 C  C   . CYS A 1 283  ? 22.536 58.766  24.673  1.00 11.68 ? 283  CYS A C   1 
ATOM   2178 O  O   . CYS A 1 283  ? 23.420 59.462  25.153  1.00 11.79 ? 283  CYS A O   1 
ATOM   2179 C  CB  . CYS A 1 283  ? 21.265 59.942  22.788  1.00 13.14 ? 283  CYS A CB  1 
ATOM   2180 S  SG  . CYS A 1 283  ? 22.060 61.566  22.923  1.00 14.53 ? 283  CYS A SG  1 
ATOM   2181 N  N   . GLN A 1 284  ? 21.777 57.940  25.447  1.00 11.95 ? 284  GLN A N   1 
ATOM   2182 C  CA  . GLN A 1 284  ? 22.016 57.799  26.861  1.00 13.69 ? 284  GLN A CA  1 
ATOM   2183 C  C   . GLN A 1 284  ? 23.289 57.057  27.181  1.00 12.29 ? 284  GLN A C   1 
ATOM   2184 O  O   . GLN A 1 284  ? 23.655 56.961  28.355  1.00 14.16 ? 284  GLN A O   1 
ATOM   2185 C  CB  . GLN A 1 284  ? 20.814 57.070  27.543  1.00 13.71 ? 284  GLN A CB  1 
ATOM   2186 C  CG  . GLN A 1 284  ? 19.510 57.821  27.323  1.00 15.09 ? 284  GLN A CG  1 
ATOM   2187 C  CD  . GLN A 1 284  ? 18.306 57.028  27.855  1.00 14.28 ? 284  GLN A CD  1 
ATOM   2188 O  OE1 . GLN A 1 284  ? 18.312 56.597  29.006  1.00 19.08 ? 284  GLN A OE1 1 
ATOM   2189 N  NE2 . GLN A 1 284  ? 17.321 56.844  27.012  1.00 16.61 ? 284  GLN A NE2 1 
ATOM   2190 N  N   . PHE A 1 285  ? 23.958 56.524  26.141  1.00 10.88 ? 285  PHE A N   1 
ATOM   2191 C  CA  . PHE A 1 285  ? 25.178 55.798  26.355  1.00 11.25 ? 285  PHE A CA  1 
ATOM   2192 C  C   . PHE A 1 285  ? 26.371 56.553  25.754  1.00 10.97 ? 285  PHE A C   1 
ATOM   2193 O  O   . PHE A 1 285  ? 27.435 55.949  25.516  1.00 11.87 ? 285  PHE A O   1 
ATOM   2194 C  CB  . PHE A 1 285  ? 25.045 54.329  25.891  1.00 11.79 ? 285  PHE A CB  1 
ATOM   2195 C  CG  . PHE A 1 285  ? 24.036 53.562  26.738  1.00 11.68 ? 285  PHE A CG  1 
ATOM   2196 C  CD1 . PHE A 1 285  ? 24.447 52.959  27.907  1.00 13.68 ? 285  PHE A CD1 1 
ATOM   2197 C  CD2 . PHE A 1 285  ? 22.688 53.543  26.380  1.00 13.62 ? 285  PHE A CD2 1 
ATOM   2198 C  CE1 . PHE A 1 285  ? 23.506 52.310  28.771  1.00 13.77 ? 285  PHE A CE1 1 
ATOM   2199 C  CE2 . PHE A 1 285  ? 21.714 52.893  27.244  1.00 15.43 ? 285  PHE A CE2 1 
ATOM   2200 C  CZ  . PHE A 1 285  ? 22.157 52.282  28.435  1.00 14.99 ? 285  PHE A CZ  1 
ATOM   2201 N  N   . ASP A 1 286  ? 26.147 57.838  25.497  1.00 11.83 ? 286  ASP A N   1 
ATOM   2202 C  CA  . ASP A 1 286  ? 27.259 58.745  25.104  1.00 10.58 ? 286  ASP A CA  1 
ATOM   2203 C  C   . ASP A 1 286  ? 27.508 59.551  26.397  1.00 9.75  ? 286  ASP A C   1 
ATOM   2204 O  O   . ASP A 1 286  ? 26.811 60.558  26.607  1.00 12.30 ? 286  ASP A O   1 
ATOM   2205 C  CB  . ASP A 1 286  ? 26.844 59.641  23.966  1.00 10.44 ? 286  ASP A CB  1 
ATOM   2206 C  CG  . ASP A 1 286  ? 27.969 60.536  23.457  1.00 9.80  ? 286  ASP A CG  1 
ATOM   2207 O  OD1 . ASP A 1 286  ? 28.995 60.612  24.165  1.00 10.77 ? 286  ASP A OD1 1 
ATOM   2208 O  OD2 . ASP A 1 286  ? 27.786 61.175  22.401  1.00 11.17 ? 286  ASP A OD2 1 
ATOM   2209 N  N   . PHE A 1 287  ? 28.482 59.149  27.191  1.00 9.49  ? 287  PHE A N   1 
ATOM   2210 C  CA  . PHE A 1 287  ? 28.621 59.760  28.506  1.00 10.84 ? 287  PHE A CA  1 
ATOM   2211 C  C   . PHE A 1 287  ? 29.196 61.149  28.485  1.00 12.55 ? 287  PHE A C   1 
ATOM   2212 O  O   . PHE A 1 287  ? 29.289 61.793  29.530  1.00 13.82 ? 287  PHE A O   1 
ATOM   2213 C  CB  . PHE A 1 287  ? 29.358 58.797  29.419  1.00 11.49 ? 287  PHE A CB  1 
ATOM   2214 C  CG  . PHE A 1 287  ? 28.546 57.528  29.663  1.00 10.41 ? 287  PHE A CG  1 
ATOM   2215 C  CD1 . PHE A 1 287  ? 28.716 56.385  28.873  1.00 12.33 ? 287  PHE A CD1 1 
ATOM   2216 C  CD2 . PHE A 1 287  ? 27.553 57.510  30.678  1.00 12.73 ? 287  PHE A CD2 1 
ATOM   2217 C  CE1 . PHE A 1 287  ? 27.914 55.240  29.055  1.00 12.93 ? 287  PHE A CE1 1 
ATOM   2218 C  CE2 . PHE A 1 287  ? 26.757 56.365  30.880  1.00 11.98 ? 287  PHE A CE2 1 
ATOM   2219 C  CZ  . PHE A 1 287  ? 26.915 55.233  30.086  1.00 12.03 ? 287  PHE A CZ  1 
ATOM   2220 N  N   . LYS A 1 288  ? 29.554 61.647  27.287  1.00 11.98 ? 288  LYS A N   1 
ATOM   2221 C  CA  . LYS A 1 288  ? 30.006 63.047  27.206  1.00 12.08 ? 288  LYS A CA  1 
ATOM   2222 C  C   . LYS A 1 288  ? 28.803 63.972  27.131  1.00 13.35 ? 288  LYS A C   1 
ATOM   2223 O  O   . LYS A 1 288  ? 28.986 65.194  27.220  1.00 14.25 ? 288  LYS A O   1 
ATOM   2224 C  CB  . LYS A 1 288  ? 30.912 63.236  25.911  1.00 12.14 ? 288  LYS A CB  1 
ATOM   2225 C  CG  . LYS A 1 288  ? 31.696 64.566  25.969  1.00 11.63 ? 288  LYS A CG  1 
ATOM   2226 C  CD  . LYS A 1 288  ? 32.554 64.706  24.706  1.00 10.76 ? 288  LYS A CD  1 
ATOM   2227 C  CE  . LYS A 1 288  ? 33.384 65.988  24.881  1.00 11.52 ? 288  LYS A CE  1 
ATOM   2228 N  NZ  . LYS A 1 288  ? 34.389 66.161  23.722  1.00 14.06 ? 288  LYS A NZ  1 
ATOM   2229 N  N   . ARG A 1 289  ? 27.554 63.458  27.073  1.00 13.28 ? 289  ARG A N   1 
ATOM   2230 C  CA  . ARG A 1 289  ? 26.413 64.352  26.951  1.00 14.01 ? 289  ARG A CA  1 
ATOM   2231 C  C   . ARG A 1 289  ? 25.691 64.671  28.305  1.00 19.27 ? 289  ARG A C   1 
ATOM   2232 O  O   . ARG A 1 289  ? 24.479 64.836  28.290  1.00 19.56 ? 289  ARG A O   1 
ATOM   2233 C  CB  . ARG A 1 289  ? 25.390 63.766  25.963  1.00 14.15 ? 289  ARG A CB  1 
ATOM   2234 C  CG  . ARG A 1 289  ? 26.007 63.570  24.571  1.00 12.77 ? 289  ARG A CG  1 
ATOM   2235 C  CD  . ARG A 1 289  ? 25.000 63.181  23.585  1.00 15.20 ? 289  ARG A CD  1 
ATOM   2236 N  NE  . ARG A 1 289  ? 25.551 62.916  22.250  1.00 12.26 ? 289  ARG A NE  1 
ATOM   2237 C  CZ  . ARG A 1 289  ? 25.131 63.468  21.124  1.00 13.68 ? 289  ARG A CZ  1 
ATOM   2238 N  NH1 . ARG A 1 289  ? 24.160 64.381  21.107  1.00 15.36 ? 289  ARG A NH1 1 
ATOM   2239 N  NH2 . ARG A 1 289  ? 25.579 62.976  19.979  1.00 13.05 ? 289  ARG A NH2 1 
ATOM   2240 N  N   . MET A 1 290  ? 26.384 64.777  29.445  1.00 25.28 ? 290  MET A N   1 
ATOM   2241 C  CA  . MET A 1 290  ? 25.601 65.067  30.686  1.00 30.83 ? 290  MET A CA  1 
ATOM   2242 C  C   . MET A 1 290  ? 25.477 66.559  31.154  1.00 33.69 ? 290  MET A C   1 
ATOM   2243 O  O   . MET A 1 290  ? 24.691 66.841  32.106  1.00 36.51 ? 290  MET A O   1 
ATOM   2244 C  CB  . MET A 1 290  ? 26.008 64.117  31.871  1.00 28.71 ? 290  MET A CB  1 
ATOM   2245 C  CG  . MET A 1 290  ? 25.787 62.643  31.584  1.00 32.92 ? 290  MET A CG  1 
ATOM   2246 S  SD  . MET A 1 290  ? 26.257 61.421  32.887  1.00 31.97 ? 290  MET A SD  1 
ATOM   2247 C  CE  . MET A 1 290  ? 28.103 61.311  32.629  1.00 33.23 ? 290  MET A CE  1 
ATOM   2248 N  N   . GLY A 1 291  ? 26.192 67.497  30.491  1.00 30.83 ? 291  GLY A N   1 
ATOM   2249 C  CA  . GLY A 1 291  ? 26.120 68.929  30.816  1.00 27.70 ? 291  GLY A CA  1 
ATOM   2250 C  C   . GLY A 1 291  ? 27.429 69.773  30.864  1.00 27.01 ? 291  GLY A C   1 
ATOM   2251 O  O   . GLY A 1 291  ? 27.599 70.835  30.218  1.00 26.29 ? 291  GLY A O   1 
ATOM   2252 N  N   . SER A 1 292  ? 28.385 69.282  31.644  1.00 21.59 ? 292  SER A N   1 
ATOM   2253 C  CA  . SER A 1 292  ? 29.666 69.943  31.829  1.00 16.57 ? 292  SER A CA  1 
ATOM   2254 C  C   . SER A 1 292  ? 30.520 70.069  30.556  1.00 15.72 ? 292  SER A C   1 
ATOM   2255 O  O   . SER A 1 292  ? 31.433 70.893  30.510  1.00 15.49 ? 292  SER A O   1 
ATOM   2256 C  CB  . SER A 1 292  ? 30.430 69.208  32.915  1.00 19.75 ? 292  SER A CB  1 
ATOM   2257 O  OG  . SER A 1 292  ? 30.863 67.947  32.409  1.00 20.77 ? 292  SER A OG  1 
ATOM   2258 N  N   . PHE A 1 293  ? 30.253 69.236  29.550  1.00 13.75 ? 293  PHE A N   1 
ATOM   2259 C  CA  . PHE A 1 293  ? 30.940 69.295  28.261  1.00 13.93 ? 293  PHE A CA  1 
ATOM   2260 C  C   . PHE A 1 293  ? 30.192 70.141  27.230  1.00 12.91 ? 293  PHE A C   1 
ATOM   2261 O  O   . PHE A 1 293  ? 30.616 70.205  26.066  1.00 14.67 ? 293  PHE A O   1 
ATOM   2262 C  CB  . PHE A 1 293  ? 31.105 67.850  27.684  1.00 14.35 ? 293  PHE A CB  1 
ATOM   2263 C  CG  . PHE A 1 293  ? 32.013 66.984  28.501  1.00 12.25 ? 293  PHE A CG  1 
ATOM   2264 C  CD1 . PHE A 1 293  ? 31.488 66.061  29.383  1.00 14.90 ? 293  PHE A CD1 1 
ATOM   2265 C  CD2 . PHE A 1 293  ? 33.398 67.100  28.363  1.00 12.38 ? 293  PHE A CD2 1 
ATOM   2266 C  CE1 . PHE A 1 293  ? 32.350 65.223  30.143  1.00 14.62 ? 293  PHE A CE1 1 
ATOM   2267 C  CE2 . PHE A 1 293  ? 34.281 66.281  29.110  1.00 14.79 ? 293  PHE A CE2 1 
ATOM   2268 C  CZ  . PHE A 1 293  ? 33.735 65.353  29.995  1.00 15.06 ? 293  PHE A CZ  1 
ATOM   2269 N  N   . GLY A 1 294  ? 29.043 70.689  27.629  1.00 14.13 ? 294  GLY A N   1 
ATOM   2270 C  CA  . GLY A 1 294  ? 28.290 71.495  26.666  1.00 17.67 ? 294  GLY A CA  1 
ATOM   2271 C  C   . GLY A 1 294  ? 27.575 70.693  25.579  1.00 15.29 ? 294  GLY A C   1 
ATOM   2272 O  O   . GLY A 1 294  ? 27.312 71.178  24.474  1.00 18.36 ? 294  GLY A O   1 
ATOM   2273 N  N   . LEU A 1 295  ? 27.269 69.428  25.864  1.00 15.61 ? 295  LEU A N   1 
ATOM   2274 C  CA  . LEU A 1 295  ? 26.556 68.591  24.913  1.00 14.63 ? 295  LEU A CA  1 
ATOM   2275 C  C   . LEU A 1 295  ? 25.316 68.034  25.623  1.00 16.25 ? 295  LEU A C   1 
ATOM   2276 O  O   . LEU A 1 295  ? 25.285 67.951  26.847  1.00 17.22 ? 295  LEU A O   1 
ATOM   2277 C  CB  . LEU A 1 295  ? 27.453 67.431  24.440  1.00 15.40 ? 295  LEU A CB  1 
ATOM   2278 C  CG  . LEU A 1 295  ? 28.755 67.903  23.740  1.00 16.02 ? 295  LEU A CG  1 
ATOM   2279 C  CD1 . LEU A 1 295  ? 29.666 66.660  23.534  1.00 16.53 ? 295  LEU A CD1 1 
ATOM   2280 C  CD2 . LEU A 1 295  ? 28.441 68.527  22.373  1.00 17.83 ? 295  LEU A CD2 1 
ATOM   2281 N  N   . SER A 1 296  ? 24.311 67.709  24.819  1.00 14.86 ? 296  SER A N   1 
ATOM   2282 C  CA  . SER A 1 296  ? 23.059 67.138  25.360  1.00 17.43 ? 296  SER A CA  1 
ATOM   2283 C  C   . SER A 1 296  ? 22.461 66.202  24.312  1.00 18.48 ? 296  SER A C   1 
ATOM   2284 O  O   . SER A 1 296  ? 22.971 66.094  23.208  1.00 16.23 ? 296  SER A O   1 
ATOM   2285 C  CB  . SER A 1 296  ? 22.074 68.281  25.740  1.00 17.34 ? 296  SER A CB  1 
ATOM   2286 O  OG  . SER A 1 296  ? 21.838 69.134  24.648  1.00 21.73 ? 296  SER A OG  1 
ATOM   2287 N  N   . CYS A 1 297  ? 21.375 65.506  24.692  1.00 16.47 ? 297  CYS A N   1 
ATOM   2288 C  CA  . CYS A 1 297  ? 20.677 64.574  23.816  1.00 17.39 ? 297  CYS A CA  1 
ATOM   2289 C  C   . CYS A 1 297  ? 19.440 65.279  23.247  1.00 18.90 ? 297  CYS A C   1 
ATOM   2290 O  O   . CYS A 1 297  ? 18.540 65.697  24.025  1.00 19.32 ? 297  CYS A O   1 
ATOM   2291 C  CB  . CYS A 1 297  ? 20.231 63.334  24.624  1.00 18.13 ? 297  CYS A CB  1 
ATOM   2292 S  SG  . CYS A 1 297  ? 21.648 62.191  24.885  1.00 18.77 ? 297  CYS A SG  1 
ATOM   2293 N  N   . PRO A 1 298  ? 19.330 65.396  21.936  1.00 18.57 ? 298  PRO A N   1 
ATOM   2294 C  CA  . PRO A 1 298  ? 18.153 66.069  21.374  1.00 20.49 ? 298  PRO A CA  1 
ATOM   2295 C  C   . PRO A 1 298  ? 16.864 65.282  21.562  1.00 20.23 ? 298  PRO A C   1 
ATOM   2296 O  O   . PRO A 1 298  ? 15.769 65.870  21.448  1.00 20.67 ? 298  PRO A O   1 
ATOM   2297 C  CB  . PRO A 1 298  ? 18.499 66.300  19.903  1.00 23.38 ? 298  PRO A CB  1 
ATOM   2298 C  CG  . PRO A 1 298  ? 19.718 65.437  19.616  1.00 23.17 ? 298  PRO A CG  1 
ATOM   2299 C  CD  . PRO A 1 298  ? 20.420 65.230  20.928  1.00 16.58 ? 298  PRO A CD  1 
ATOM   2300 N  N   . TRP A 1 299  ? 16.973 64.000  21.898  1.00 17.60 ? 299  TRP A N   1 
ATOM   2301 C  CA  . TRP A 1 299  ? 15.766 63.161  22.116  1.00 17.28 ? 299  TRP A CA  1 
ATOM   2302 C  C   . TRP A 1 299  ? 15.268 63.381  23.548  1.00 19.70 ? 299  TRP A C   1 
ATOM   2303 O  O   . TRP A 1 299  ? 14.307 62.727  23.992  1.00 20.63 ? 299  TRP A O   1 
ATOM   2304 C  CB  . TRP A 1 299  ? 16.082 61.668  21.834  1.00 16.57 ? 299  TRP A CB  1 
ATOM   2305 C  CG  . TRP A 1 299  ? 16.439 61.478  20.409  1.00 16.51 ? 299  TRP A CG  1 
ATOM   2306 C  CD1 . TRP A 1 299  ? 15.608 61.278  19.388  1.00 16.79 ? 299  TRP A CD1 1 
ATOM   2307 C  CD2 . TRP A 1 299  ? 17.768 61.597  19.855  1.00 14.88 ? 299  TRP A CD2 1 
ATOM   2308 N  NE1 . TRP A 1 299  ? 16.308 61.255  18.181  1.00 18.60 ? 299  TRP A NE1 1 
ATOM   2309 C  CE2 . TRP A 1 299  ? 17.636 61.458  18.452  1.00 17.74 ? 299  TRP A CE2 1 
ATOM   2310 C  CE3 . TRP A 1 299  ? 19.030 61.807  20.414  1.00 15.02 ? 299  TRP A CE3 1 
ATOM   2311 C  CZ2 . TRP A 1 299  ? 18.728 61.530  17.579  1.00 15.69 ? 299  TRP A CZ2 1 
ATOM   2312 C  CZ3 . TRP A 1 299  ? 20.107 61.881  19.531  1.00 14.76 ? 299  TRP A CZ3 1 
ATOM   2313 C  CH2 . TRP A 1 299  ? 19.937 61.747  18.145  1.00 14.00 ? 299  TRP A CH2 1 
ATOM   2314 N  N   . LYS A 1 300  ? 15.962 64.236  24.303  1.00 19.51 ? 300  LYS A N   1 
ATOM   2315 C  CA  . LYS A 1 300  ? 15.496 64.676  25.648  1.00 20.78 ? 300  LYS A CA  1 
ATOM   2316 C  C   . LYS A 1 300  ? 15.677 63.745  26.833  1.00 21.69 ? 300  LYS A C   1 
ATOM   2317 O  O   . LYS A 1 300  ? 15.147 64.015  27.947  1.00 22.10 ? 300  LYS A O   1 
ATOM   2318 C  CB  . LYS A 1 300  ? 14.024 65.124  25.563  1.00 24.68 ? 300  LYS A CB  1 
ATOM   2319 C  CG  . LYS A 1 300  ? 13.834 66.288  24.662  1.00 23.77 ? 300  LYS A CG  1 
ATOM   2320 C  CD  . LYS A 1 300  ? 12.325 66.583  24.462  1.00 30.89 ? 300  LYS A CD  1 
ATOM   2321 C  CE  . LYS A 1 300  ? 12.095 67.871  23.707  1.00 34.39 ? 300  LYS A CE  1 
ATOM   2322 N  NZ  . LYS A 1 300  ? 12.849 67.914  22.427  1.00 37.90 ? 300  LYS A NZ  1 
ATOM   2323 N  N   . VAL A 1 301  ? 16.374 62.629  26.664  1.00 21.58 ? 301  VAL A N   1 
ATOM   2324 C  CA  . VAL A 1 301  ? 16.633 61.775  27.787  1.00 19.51 ? 301  VAL A CA  1 
ATOM   2325 C  C   . VAL A 1 301  ? 18.170 61.785  27.885  1.00 17.97 ? 301  VAL A C   1 
ATOM   2326 O  O   . VAL A 1 301  ? 18.854 61.320  26.976  1.00 21.02 ? 301  VAL A O   1 
ATOM   2327 C  CB  . VAL A 1 301  ? 16.122 60.326  27.589  1.00 20.99 ? 301  VAL A CB  1 
ATOM   2328 C  CG1 . VAL A 1 301  ? 16.398 59.557  28.867  1.00 21.34 ? 301  VAL A CG1 1 
ATOM   2329 C  CG2 . VAL A 1 301  ? 14.571 60.328  27.232  1.00 25.89 ? 301  VAL A CG2 1 
ATOM   2330 N  N   . PRO A 1 302  ? 18.727 62.288  28.968  1.00 16.22 ? 302  PRO A N   1 
ATOM   2331 C  CA  . PRO A 1 302  ? 20.171 62.350  29.099  1.00 17.73 ? 302  PRO A CA  1 
ATOM   2332 C  C   . PRO A 1 302  ? 20.815 61.085  29.583  1.00 17.50 ? 302  PRO A C   1 
ATOM   2333 O  O   . PRO A 1 302  ? 20.177 60.188  30.063  1.00 17.77 ? 302  PRO A O   1 
ATOM   2334 C  CB  . PRO A 1 302  ? 20.363 63.450  30.134  1.00 20.00 ? 302  PRO A CB  1 
ATOM   2335 C  CG  . PRO A 1 302  ? 19.182 63.233  31.071  1.00 21.48 ? 302  PRO A CG  1 
ATOM   2336 C  CD  . PRO A 1 302  ? 18.046 62.963  30.109  1.00 17.87 ? 302  PRO A CD  1 
ATOM   2337 N  N   . PRO A 1 303  ? 22.118 60.957  29.346  1.00 14.97 ? 303  PRO A N   1 
ATOM   2338 C  CA  . PRO A 1 303  ? 22.788 59.775  29.876  1.00 14.31 ? 303  PRO A CA  1 
ATOM   2339 C  C   . PRO A 1 303  ? 22.815 59.939  31.405  1.00 19.00 ? 303  PRO A C   1 
ATOM   2340 O  O   . PRO A 1 303  ? 22.734 61.066  31.925  1.00 18.29 ? 303  PRO A O   1 
ATOM   2341 C  CB  . PRO A 1 303  ? 24.246 59.886  29.374  1.00 16.26 ? 303  PRO A CB  1 
ATOM   2342 C  CG  . PRO A 1 303  ? 24.319 61.221  28.615  1.00 19.50 ? 303  PRO A CG  1 
ATOM   2343 C  CD  . PRO A 1 303  ? 23.031 61.937  28.709  1.00 16.58 ? 303  PRO A CD  1 
ATOM   2344 N  N   . ARG A 1 304  ? 22.921 58.817  32.097  1.00 18.43 ? 304  ARG A N   1 
ATOM   2345 C  CA  . ARG A 1 304  ? 23.077 58.830  33.545  1.00 19.25 ? 304  ARG A CA  1 
ATOM   2346 C  C   . ARG A 1 304  ? 24.265 57.978  33.930  1.00 14.31 ? 304  ARG A C   1 
ATOM   2347 O  O   . ARG A 1 304  ? 24.496 56.855  33.346  1.00 16.60 ? 304  ARG A O   1 
ATOM   2348 C  CB  . ARG A 1 304  ? 21.809 58.312  34.236  1.00 23.47 ? 304  ARG A CB  1 
ATOM   2349 C  CG  . ARG A 1 304  ? 20.694 59.361  34.184  1.00 27.81 ? 304  ARG A CG  1 
ATOM   2350 C  CD  . ARG A 1 304  ? 19.485 58.913  34.942  1.00 31.41 ? 304  ARG A CD  1 
ATOM   2351 N  NE  . ARG A 1 304  ? 18.699 57.948  34.185  1.00 33.75 ? 304  ARG A NE  1 
ATOM   2352 C  CZ  . ARG A 1 304  ? 18.606 56.665  34.521  1.00 37.50 ? 304  ARG A CZ  1 
ATOM   2353 N  NH1 . ARG A 1 304  ? 19.254 56.217  35.597  1.00 39.83 ? 304  ARG A NH1 1 
ATOM   2354 N  NH2 . ARG A 1 304  ? 17.856 55.836  33.804  1.00 39.94 ? 304  ARG A NH2 1 
ATOM   2355 N  N   . THR A 1 305  ? 25.057 58.495  34.862  1.00 16.64 ? 305  THR A N   1 
ATOM   2356 C  CA  . THR A 1 305  ? 26.220 57.754  35.343  1.00 15.58 ? 305  THR A CA  1 
ATOM   2357 C  C   . THR A 1 305  ? 25.840 56.356  35.760  1.00 14.88 ? 305  THR A C   1 
ATOM   2358 O  O   . THR A 1 305  ? 24.791 56.188  36.479  1.00 17.34 ? 305  THR A O   1 
ATOM   2359 C  CB  . THR A 1 305  ? 26.880 58.494  36.528  1.00 16.80 ? 305  THR A CB  1 
ATOM   2360 O  OG1 . THR A 1 305  ? 27.343 59.763  36.037  1.00 20.99 ? 305  THR A OG1 1 
ATOM   2361 C  CG2 . THR A 1 305  ? 27.959 57.727  37.173  1.00 17.72 ? 305  THR A CG2 1 
ATOM   2362 N  N   . ILE A 1 306  ? 26.592 55.341  35.364  1.00 12.75 ? 306  ILE A N   1 
ATOM   2363 C  CA  . ILE A 1 306  ? 26.273 53.969  35.745  1.00 13.47 ? 306  ILE A CA  1 
ATOM   2364 C  C   . ILE A 1 306  ? 26.705 53.747  37.188  1.00 15.62 ? 306  ILE A C   1 
ATOM   2365 O  O   . ILE A 1 306  ? 27.812 54.093  37.609  1.00 16.77 ? 306  ILE A O   1 
ATOM   2366 C  CB  . ILE A 1 306  ? 26.982 52.967  34.792  1.00 13.03 ? 306  ILE A CB  1 
ATOM   2367 C  CG1 . ILE A 1 306  ? 26.617 53.227  33.300  1.00 12.79 ? 306  ILE A CG1 1 
ATOM   2368 C  CG2 . ILE A 1 306  ? 26.539 51.485  35.158  1.00 13.47 ? 306  ILE A CG2 1 
ATOM   2369 C  CD1 . ILE A 1 306  ? 25.085 53.235  32.982  1.00 14.12 ? 306  ILE A CD1 1 
ATOM   2370 N  N   . SER A 1 307  ? 25.816 53.074  37.937  1.00 17.64 ? 307  SER A N   1 
ATOM   2371 C  CA  . SER A 1 307  ? 26.023 52.768  39.368  1.00 17.55 ? 307  SER A CA  1 
ATOM   2372 C  C   . SER A 1 307  ? 25.525 51.353  39.626  1.00 18.16 ? 307  SER A C   1 
ATOM   2373 O  O   . SER A 1 307  ? 24.777 50.782  38.796  1.00 15.77 ? 307  SER A O   1 
ATOM   2374 C  CB  . SER A 1 307  ? 25.141 53.679  40.244  1.00 18.48 ? 307  SER A CB  1 
ATOM   2375 O  OG  . SER A 1 307  ? 23.750 53.390  40.078  1.00 18.67 ? 307  SER A OG  1 
ATOM   2376 N  N   . ASP A 1 308  ? 25.801 50.847  40.833  1.00 20.01 ? 308  ASP A N   1 
ATOM   2377 C  CA  . ASP A 1 308  ? 25.274 49.505  41.134  1.00 22.46 ? 308  ASP A CA  1 
ATOM   2378 C  C   . ASP A 1 308  ? 23.728 49.496  41.201  1.00 20.35 ? 308  ASP A C   1 
ATOM   2379 O  O   . ASP A 1 308  ? 23.130 48.441  40.917  1.00 18.06 ? 308  ASP A O   1 
ATOM   2380 C  CB  . ASP A 1 308  ? 25.870 48.935  42.433  1.00 25.45 ? 308  ASP A CB  1 
ATOM   2381 C  CG  . ASP A 1 308  ? 27.395 48.722  42.370  1.00 31.64 ? 308  ASP A CG  1 
ATOM   2382 O  OD1 . ASP A 1 308  ? 28.036 48.867  41.303  1.00 32.39 ? 308  ASP A OD1 1 
ATOM   2383 O  OD2 . ASP A 1 308  ? 28.000 48.378  43.408  1.00 37.27 ? 308  ASP A OD2 1 
ATOM   2384 N  N   . GLN A 1 309  ? 23.061 50.623  41.459  1.00 20.83 ? 309  GLN A N   1 
ATOM   2385 C  CA  . GLN A 1 309  ? 21.579 50.677  41.523  1.00 21.06 ? 309  GLN A CA  1 
ATOM   2386 C  C   . GLN A 1 309  ? 20.906 50.807  40.180  1.00 23.28 ? 309  GLN A C   1 
ATOM   2387 O  O   . GLN A 1 309  ? 19.682 50.553  40.059  1.00 21.26 ? 309  GLN A O   1 
ATOM   2388 C  CB  . GLN A 1 309  ? 21.062 51.854  42.428  1.00 17.61 ? 309  GLN A CB  1 
ATOM   2389 C  CG  . GLN A 1 309  ? 21.465 51.754  43.900  1.00 22.65 ? 309  GLN A CG  1 
ATOM   2390 C  CD  . GLN A 1 309  ? 22.966 51.896  44.072  1.00 24.56 ? 309  GLN A CD  1 
ATOM   2391 O  OE1 . GLN A 1 309  ? 23.563 52.834  43.516  1.00 23.15 ? 309  GLN A OE1 1 
ATOM   2392 N  NE2 . GLN A 1 309  ? 23.597 50.965  44.817  1.00 25.22 ? 309  GLN A NE2 1 
ATOM   2393 N  N   . ASN A 1 310  ? 21.653 51.197  39.137  1.00 18.11 ? 310  ASN A N   1 
ATOM   2394 C  CA  . ASN A 1 310  ? 20.951 51.341  37.861  1.00 16.54 ? 310  ASN A CA  1 
ATOM   2395 C  C   . ASN A 1 310  ? 21.588 50.435  36.772  1.00 14.60 ? 310  ASN A C   1 
ATOM   2396 O  O   . ASN A 1 310  ? 21.046 50.340  35.701  1.00 15.47 ? 310  ASN A O   1 
ATOM   2397 C  CB  . ASN A 1 310  ? 20.919 52.813  37.413  1.00 18.09 ? 310  ASN A CB  1 
ATOM   2398 C  CG  . ASN A 1 310  ? 22.294 53.356  37.035  1.00 16.96 ? 310  ASN A CG  1 
ATOM   2399 O  OD1 . ASN A 1 310  ? 23.218 52.600  36.766  1.00 18.00 ? 310  ASN A OD1 1 
ATOM   2400 N  ND2 . ASN A 1 310  ? 22.409 54.662  37.040  1.00 19.46 ? 310  ASN A ND2 1 
ATOM   2401 N  N   . VAL A 1 311  ? 22.671 49.758  37.105  1.00 14.08 ? 311  VAL A N   1 
ATOM   2402 C  CA  . VAL A 1 311  ? 23.396 49.032  36.001  1.00 14.80 ? 311  VAL A CA  1 
ATOM   2403 C  C   . VAL A 1 311  ? 22.548 47.930  35.412  1.00 17.93 ? 311  VAL A C   1 
ATOM   2404 O  O   . VAL A 1 311  ? 22.650 47.666  34.222  1.00 16.33 ? 311  VAL A O   1 
ATOM   2405 C  CB  . VAL A 1 311  ? 24.768 48.525  36.464  1.00 12.75 ? 311  VAL A CB  1 
ATOM   2406 C  CG1 . VAL A 1 311  ? 24.646 47.429  37.536  1.00 17.99 ? 311  VAL A CG1 1 
ATOM   2407 C  CG2 . VAL A 1 311  ? 25.619 48.005  35.230  1.00 15.88 ? 311  VAL A CG2 1 
ATOM   2408 N  N   . ALA A 1 312  ? 21.682 47.285  36.196  1.00 15.92 ? 312  ALA A N   1 
ATOM   2409 C  CA  . ALA A 1 312  ? 20.877 46.233  35.565  1.00 15.02 ? 312  ALA A CA  1 
ATOM   2410 C  C   . ALA A 1 312  ? 19.861 46.781  34.594  1.00 16.07 ? 312  ALA A C   1 
ATOM   2411 O  O   . ALA A 1 312  ? 19.723 46.239  33.480  1.00 16.73 ? 312  ALA A O   1 
ATOM   2412 C  CB  . ALA A 1 312  ? 20.135 45.314  36.703  1.00 17.60 ? 312  ALA A CB  1 
ATOM   2413 N  N   . ALA A 1 313  ? 19.175 47.881  34.901  1.00 15.33 ? 313  ALA A N   1 
ATOM   2414 C  CA  . ALA A 1 313  ? 18.175 48.466  34.015  1.00 18.36 ? 313  ALA A CA  1 
ATOM   2415 C  C   . ALA A 1 313  ? 18.888 49.072  32.793  1.00 18.67 ? 313  ALA A C   1 
ATOM   2416 O  O   . ALA A 1 313  ? 18.382 48.987  31.694  1.00 17.48 ? 313  ALA A O   1 
ATOM   2417 C  CB  . ALA A 1 313  ? 17.364 49.572  34.738  1.00 17.13 ? 313  ALA A CB  1 
ATOM   2418 N  N   . ARG A 1 314  ? 20.021 49.738  33.022  1.00 16.83 ? 314  ARG A N   1 
ATOM   2419 C  CA  . ARG A 1 314  ? 20.782 50.361  31.907  1.00 16.14 ? 314  ARG A CA  1 
ATOM   2420 C  C   . ARG A 1 314  ? 21.305 49.230  31.011  1.00 14.81 ? 314  ARG A C   1 
ATOM   2421 O  O   . ARG A 1 314  ? 21.233 49.377  29.790  1.00 15.47 ? 314  ARG A O   1 
ATOM   2422 C  CB  . ARG A 1 314  ? 21.971 51.160  32.489  1.00 14.08 ? 314  ARG A CB  1 
ATOM   2423 C  CG  . ARG A 1 314  ? 21.642 52.363  33.370  1.00 16.11 ? 314  ARG A CG  1 
ATOM   2424 C  CD  . ARG A 1 314  ? 21.390 53.609  32.530  1.00 19.40 ? 314  ARG A CD  1 
ATOM   2425 N  NE  . ARG A 1 314  ? 20.041 53.614  32.027  1.00 20.18 ? 314  ARG A NE  1 
ATOM   2426 C  CZ  . ARG A 1 314  ? 19.522 54.503  31.205  1.00 19.43 ? 314  ARG A CZ  1 
ATOM   2427 N  NH1 . ARG A 1 314  ? 20.273 55.502  30.734  1.00 22.11 ? 314  ARG A NH1 1 
ATOM   2428 N  NH2 . ARG A 1 314  ? 18.219 54.487  30.892  1.00 20.60 ? 314  ARG A NH2 1 
ATOM   2429 N  N   . SER A 1 315  ? 21.810 48.140  31.587  1.00 14.35 ? 315  SER A N   1 
ATOM   2430 C  CA  . SER A 1 315  ? 22.292 47.021  30.753  1.00 15.79 ? 315  SER A CA  1 
ATOM   2431 C  C   . SER A 1 315  ? 21.166 46.387  30.003  1.00 17.57 ? 315  SER A C   1 
ATOM   2432 O  O   . SER A 1 315  ? 21.326 45.955  28.838  1.00 18.16 ? 315  SER A O   1 
ATOM   2433 C  CB  . SER A 1 315  ? 22.996 45.972  31.591  1.00 12.69 ? 315  SER A CB  1 
ATOM   2434 O  OG  . SER A 1 315  ? 24.152 46.484  32.202  1.00 15.99 ? 315  SER A OG  1 
ATOM   2435 N  N   A ASP A 1 316  ? 20.007 46.257  30.633  0.50 16.69 ? 316  ASP A N   1 
ATOM   2436 N  N   B ASP A 1 316  ? 20.007 46.257  30.633  0.50 17.96 ? 316  ASP A N   1 
ATOM   2437 C  CA  A ASP A 1 316  ? 18.882 45.679  29.910  0.50 19.11 ? 316  ASP A CA  1 
ATOM   2438 C  CA  B ASP A 1 316  ? 18.882 45.679  29.910  0.50 21.03 ? 316  ASP A CA  1 
ATOM   2439 C  C   A ASP A 1 316  ? 18.543 46.509  28.659  0.50 14.01 ? 316  ASP A C   1 
ATOM   2440 C  C   B ASP A 1 316  ? 18.797 46.239  28.479  0.50 20.11 ? 316  ASP A C   1 
ATOM   2441 O  O   A ASP A 1 316  ? 18.280 45.953  27.574  0.50 11.81 ? 316  ASP A O   1 
ATOM   2442 O  O   B ASP A 1 316  ? 18.558 45.489  27.511  0.50 22.33 ? 316  ASP A O   1 
ATOM   2443 C  CB  A ASP A 1 316  ? 17.664 45.610  30.811  0.50 22.84 ? 316  ASP A CB  1 
ATOM   2444 C  CB  B ASP A 1 316  ? 17.586 45.974  30.641  0.50 21.44 ? 316  ASP A CB  1 
ATOM   2445 C  CG  A ASP A 1 316  ? 16.783 44.443  30.457  0.50 26.82 ? 316  ASP A CG  1 
ATOM   2446 C  CG  B ASP A 1 316  ? 17.412 45.076  31.836  0.50 21.08 ? 316  ASP A CG  1 
ATOM   2447 O  OD1 A ASP A 1 316  ? 15.542 44.590  30.538  0.50 28.38 ? 316  ASP A OD1 1 
ATOM   2448 O  OD1 B ASP A 1 316  ? 16.565 45.396  32.700  0.50 20.95 ? 316  ASP A OD1 1 
ATOM   2449 O  OD2 A ASP A 1 316  ? 17.364 43.385  30.086  0.50 25.14 ? 316  ASP A OD2 1 
ATOM   2450 O  OD2 B ASP A 1 316  ? 18.134 44.041  31.878  0.50 20.13 ? 316  ASP A OD2 1 
ATOM   2451 N  N   . LEU A 1 317  ? 18.554 47.839  28.782  1.00 16.40 ? 317  LEU A N   1 
ATOM   2452 C  CA  . LEU A 1 317  ? 18.249 48.713  27.634  1.00 15.89 ? 317  LEU A CA  1 
ATOM   2453 C  C   . LEU A 1 317  ? 19.356 48.614  26.565  1.00 13.72 ? 317  LEU A C   1 
ATOM   2454 O  O   . LEU A 1 317  ? 19.031 48.510  25.393  1.00 15.52 ? 317  LEU A O   1 
ATOM   2455 C  CB  . LEU A 1 317  ? 18.133 50.210  28.043  1.00 17.94 ? 317  LEU A CB  1 
ATOM   2456 C  CG  . LEU A 1 317  ? 16.795 50.773  28.533  1.00 23.14 ? 317  LEU A CG  1 
ATOM   2457 C  CD1 . LEU A 1 317  ? 17.085 52.123  29.228  1.00 26.83 ? 317  LEU A CD1 1 
ATOM   2458 C  CD2 . LEU A 1 317  ? 15.802 50.950  27.354  1.00 23.24 ? 317  LEU A CD2 1 
ATOM   2459 N  N   . LEU A 1 318  ? 20.603 48.594  26.994  1.00 14.43 ? 318  LEU A N   1 
ATOM   2460 C  CA  . LEU A 1 318  ? 21.707 48.591  26.004  1.00 12.77 ? 318  LEU A CA  1 
ATOM   2461 C  C   . LEU A 1 318  ? 21.813 47.249  25.288  1.00 14.68 ? 318  LEU A C   1 
ATOM   2462 O  O   . LEU A 1 318  ? 21.928 47.213  24.033  1.00 13.81 ? 318  LEU A O   1 
ATOM   2463 C  CB  . LEU A 1 318  ? 22.989 48.956  26.721  1.00 12.58 ? 318  LEU A CB  1 
ATOM   2464 C  CG  . LEU A 1 318  ? 24.228 49.020  25.790  1.00 12.47 ? 318  LEU A CG  1 
ATOM   2465 C  CD1 . LEU A 1 318  ? 24.046 50.132  24.750  1.00 15.33 ? 318  LEU A CD1 1 
ATOM   2466 C  CD2 . LEU A 1 318  ? 25.446 49.273  26.657  1.00 15.02 ? 318  LEU A CD2 1 
ATOM   2467 N  N   . VAL A 1 319  ? 21.705 46.143  26.013  1.00 12.42 ? 319  VAL A N   1 
ATOM   2468 C  CA  . VAL A 1 319  ? 21.800 44.819  25.381  1.00 14.04 ? 319  VAL A CA  1 
ATOM   2469 C  C   . VAL A 1 319  ? 20.646 44.641  24.396  1.00 14.61 ? 319  VAL A C   1 
ATOM   2470 O  O   . VAL A 1 319  ? 20.838 44.023  23.341  1.00 13.47 ? 319  VAL A O   1 
ATOM   2471 C  CB  . VAL A 1 319  ? 21.816 43.674  26.435  1.00 13.60 ? 319  VAL A CB  1 
ATOM   2472 C  CG1 . VAL A 1 319  ? 21.695 42.310  25.739  1.00 13.49 ? 319  VAL A CG1 1 
ATOM   2473 C  CG2 . VAL A 1 319  ? 23.141 43.735  27.244  1.00 15.71 ? 319  VAL A CG2 1 
ATOM   2474 N  N   . ASP A 1 320  ? 19.461 45.168  24.703  1.00 14.17 ? 320  ASP A N   1 
ATOM   2475 C  CA  . ASP A 1 320  ? 18.320 45.098  23.779  1.00 15.14 ? 320  ASP A CA  1 
ATOM   2476 C  C   . ASP A 1 320  ? 18.663 45.823  22.474  1.00 13.45 ? 320  ASP A C   1 
ATOM   2477 O  O   . ASP A 1 320  ? 18.341 45.313  21.396  1.00 14.05 ? 320  ASP A O   1 
ATOM   2478 C  CB  . ASP A 1 320  ? 17.047 45.672  24.453  1.00 17.26 ? 320  ASP A CB  1 
ATOM   2479 C  CG  . ASP A 1 320  ? 15.869 45.788  23.523  1.00 14.90 ? 320  ASP A CG  1 
ATOM   2480 O  OD1 . ASP A 1 320  ? 15.421 46.902  23.150  1.00 17.86 ? 320  ASP A OD1 1 
ATOM   2481 O  OD2 . ASP A 1 320  ? 15.388 44.645  23.167  1.00 20.17 ? 320  ASP A OD2 1 
ATOM   2482 N  N   . GLN A 1 321  ? 19.267 47.024  22.568  1.00 13.37 ? 321  GLN A N   1 
ATOM   2483 C  CA  . GLN A 1 321  ? 19.686 47.733  21.331  1.00 12.26 ? 321  GLN A CA  1 
ATOM   2484 C  C   . GLN A 1 321  ? 20.724 46.882  20.560  1.00 10.71 ? 321  GLN A C   1 
ATOM   2485 O  O   . GLN A 1 321  ? 20.587 46.762  19.349  1.00 11.20 ? 321  GLN A O   1 
ATOM   2486 C  CB  . GLN A 1 321  ? 20.320 49.099  21.686  1.00 11.98 ? 321  GLN A CB  1 
ATOM   2487 C  CG  . GLN A 1 321  ? 19.302 50.162  22.158  1.00 13.58 ? 321  GLN A CG  1 
ATOM   2488 C  CD  . GLN A 1 321  ? 18.246 50.370  21.077  1.00 15.44 ? 321  GLN A CD  1 
ATOM   2489 O  OE1 . GLN A 1 321  ? 18.583 50.743  19.954  1.00 15.92 ? 321  GLN A OE1 1 
ATOM   2490 N  NE2 . GLN A 1 321  ? 16.959 50.085  21.384  1.00 14.95 ? 321  GLN A NE2 1 
ATOM   2491 N  N   . TRP A 1 322  ? 21.724 46.323  21.259  1.00 10.99 ? 322  TRP A N   1 
ATOM   2492 C  CA  . TRP A 1 322  ? 22.728 45.513  20.588  1.00 11.60 ? 322  TRP A CA  1 
ATOM   2493 C  C   . TRP A 1 322  ? 22.109 44.314  19.874  1.00 12.42 ? 322  TRP A C   1 
ATOM   2494 O  O   . TRP A 1 322  ? 22.469 43.996  18.725  1.00 11.98 ? 322  TRP A O   1 
ATOM   2495 C  CB  . TRP A 1 322  ? 23.749 45.018  21.599  1.00 11.59 ? 322  TRP A CB  1 
ATOM   2496 C  CG  . TRP A 1 322  ? 24.685 46.065  22.140  1.00 11.99 ? 322  TRP A CG  1 
ATOM   2497 C  CD1 . TRP A 1 322  ? 24.860 47.355  21.712  1.00 10.94 ? 322  TRP A CD1 1 
ATOM   2498 C  CD2 . TRP A 1 322  ? 25.591 45.872  23.240  1.00 11.19 ? 322  TRP A CD2 1 
ATOM   2499 N  NE1 . TRP A 1 322  ? 25.839 47.988  22.496  1.00 12.95 ? 322  TRP A NE1 1 
ATOM   2500 C  CE2 . TRP A 1 322  ? 26.295 47.093  23.428  1.00 11.60 ? 322  TRP A CE2 1 
ATOM   2501 C  CE3 . TRP A 1 322  ? 25.885 44.768  24.092  1.00 12.51 ? 322  TRP A CE3 1 
ATOM   2502 C  CZ2 . TRP A 1 322  ? 27.266 47.263  24.434  1.00 11.92 ? 322  TRP A CZ2 1 
ATOM   2503 C  CZ3 . TRP A 1 322  ? 26.863 44.950  25.107  1.00 12.52 ? 322  TRP A CZ3 1 
ATOM   2504 C  CH2 . TRP A 1 322  ? 27.525 46.170  25.270  1.00 12.15 ? 322  TRP A CH2 1 
ATOM   2505 N  N   . LYS A 1 323  ? 21.168 43.640  20.541  1.00 13.14 ? 323  LYS A N   1 
ATOM   2506 C  CA  . LYS A 1 323  ? 20.584 42.435  19.924  1.00 12.05 ? 323  LYS A CA  1 
ATOM   2507 C  C   . LYS A 1 323  ? 19.717 42.796  18.746  1.00 12.70 ? 323  LYS A C   1 
ATOM   2508 O  O   . LYS A 1 323  ? 19.614 42.024  17.779  1.00 13.31 ? 323  LYS A O   1 
ATOM   2509 C  CB  . LYS A 1 323  ? 19.794 41.617  20.969  1.00 13.98 ? 323  LYS A CB  1 
ATOM   2510 C  CG  . LYS A 1 323  ? 20.772 40.825  21.860  1.00 15.30 ? 323  LYS A CG  1 
ATOM   2511 C  CD  . LYS A 1 323  ? 20.083 40.015  22.936  1.00 17.28 ? 323  LYS A CD  1 
ATOM   2512 C  CE  . LYS A 1 323  ? 21.146 39.157  23.626  1.00 14.97 ? 323  LYS A CE  1 
ATOM   2513 N  NZ  . LYS A 1 323  ? 20.411 38.322  24.640  1.00 23.31 ? 323  LYS A NZ  1 
ATOM   2514 N  N   . LYS A 1 324  ? 19.101 43.955  18.763  1.00 11.47 ? 324  LYS A N   1 
ATOM   2515 C  CA  . LYS A 1 324  ? 18.379 44.437  17.572  1.00 11.41 ? 324  LYS A CA  1 
ATOM   2516 C  C   . LYS A 1 324  ? 19.358 44.724  16.428  1.00 11.62 ? 324  LYS A C   1 
ATOM   2517 O  O   . LYS A 1 324  ? 19.101 44.321  15.299  1.00 12.08 ? 324  LYS A O   1 
ATOM   2518 C  CB  . LYS A 1 324  ? 17.575 45.693  17.916  1.00 12.11 ? 324  LYS A CB  1 
ATOM   2519 C  CG  . LYS A 1 324  ? 16.317 45.332  18.728  1.00 12.41 ? 324  LYS A CG  1 
ATOM   2520 C  CD  . LYS A 1 324  ? 15.634 46.578  19.259  1.00 14.29 ? 324  LYS A CD  1 
ATOM   2521 C  CE  . LYS A 1 324  ? 14.402 46.098  20.060  1.00 14.71 ? 324  LYS A CE  1 
ATOM   2522 N  NZ  . LYS A 1 324  ? 13.814 47.232  20.847  1.00 17.34 ? 324  LYS A NZ  1 
ATOM   2523 N  N   . LYS A 1 325  ? 20.444 45.461  16.719  1.00 11.07 ? 325  LYS A N   1 
ATOM   2524 C  CA  . LYS A 1 325  ? 21.456 45.712  15.664  1.00 10.11 ? 325  LYS A CA  1 
ATOM   2525 C  C   . LYS A 1 325  ? 21.968 44.371  15.102  1.00 10.03 ? 325  LYS A C   1 
ATOM   2526 O  O   . LYS A 1 325  ? 22.152 44.210  13.858  1.00 10.12 ? 325  LYS A O   1 
ATOM   2527 C  CB  . LYS A 1 325  ? 22.635 46.498  16.274  1.00 9.49  ? 325  LYS A CB  1 
ATOM   2528 C  CG  . LYS A 1 325  ? 23.495 47.150  15.113  1.00 9.81  ? 325  LYS A CG  1 
ATOM   2529 C  CD  . LYS A 1 325  ? 24.645 47.970  15.752  1.00 12.09 ? 325  LYS A CD  1 
ATOM   2530 C  CE  . LYS A 1 325  ? 25.389 48.754  14.625  1.00 11.32 ? 325  LYS A CE  1 
ATOM   2531 N  NZ  . LYS A 1 325  ? 26.589 49.347  15.254  1.00 12.05 ? 325  LYS A NZ  1 
ATOM   2532 N  N   . ALA A 1 326  ? 22.209 43.377  15.961  1.00 11.07 ? 326  ALA A N   1 
ATOM   2533 C  CA  . ALA A 1 326  ? 22.748 42.094  15.538  1.00 10.43 ? 326  ALA A CA  1 
ATOM   2534 C  C   . ALA A 1 326  ? 21.824 41.358  14.585  1.00 11.13 ? 326  ALA A C   1 
ATOM   2535 O  O   . ALA A 1 326  ? 22.264 40.537  13.787  1.00 12.81 ? 326  ALA A O   1 
ATOM   2536 C  CB  . ALA A 1 326  ? 23.044 41.200  16.765  1.00 11.82 ? 326  ALA A CB  1 
ATOM   2537 N  N   . GLU A 1 327  ? 20.535 41.634  14.661  1.00 12.03 ? 327  GLU A N   1 
ATOM   2538 C  CA  . GLU A 1 327  ? 19.602 40.972  13.732  1.00 13.01 ? 327  GLU A CA  1 
ATOM   2539 C  C   . GLU A 1 327  ? 19.850 41.334  12.266  1.00 13.12 ? 327  GLU A C   1 
ATOM   2540 O  O   . GLU A 1 327  ? 19.382 40.666  11.363  1.00 15.01 ? 327  GLU A O   1 
ATOM   2541 C  CB  . GLU A 1 327  ? 18.199 41.418  14.051  1.00 16.15 ? 327  GLU A CB  1 
ATOM   2542 C  CG  . GLU A 1 327  ? 17.548 40.654  15.143  1.00 22.20 ? 327  GLU A CG  1 
ATOM   2543 C  CD  . GLU A 1 327  ? 17.510 39.139  14.868  1.00 19.42 ? 327  GLU A CD  1 
ATOM   2544 O  OE1 . GLU A 1 327  ? 16.851 38.654  13.952  1.00 23.31 ? 327  GLU A OE1 1 
ATOM   2545 O  OE2 . GLU A 1 327  ? 18.190 38.429  15.563  1.00 22.72 ? 327  GLU A OE2 1 
ATOM   2546 N  N   . LEU A 1 328  ? 20.542 42.455  12.019  1.00 11.88 ? 328  LEU A N   1 
ATOM   2547 C  CA  . LEU A 1 328  ? 20.812 42.937  10.659  1.00 10.12 ? 328  LEU A CA  1 
ATOM   2548 C  C   . LEU A 1 328  ? 22.041 42.274  10.060  1.00 11.57 ? 328  LEU A C   1 
ATOM   2549 O  O   . LEU A 1 328  ? 22.303 42.523  8.866   1.00 13.26 ? 328  LEU A O   1 
ATOM   2550 C  CB  . LEU A 1 328  ? 21.006 44.450  10.720  1.00 10.69 ? 328  LEU A CB  1 
ATOM   2551 C  CG  . LEU A 1 328  ? 19.884 45.230  11.388  1.00 10.05 ? 328  LEU A CG  1 
ATOM   2552 C  CD1 . LEU A 1 328  ? 20.100 46.712  11.196  1.00 13.48 ? 328  LEU A CD1 1 
ATOM   2553 C  CD2 . LEU A 1 328  ? 18.484 44.842  10.850  1.00 13.75 ? 328  LEU A CD2 1 
ATOM   2554 N  N   . TYR A 1 329  ? 22.753 41.430  10.797  1.00 10.17 ? 329  TYR A N   1 
ATOM   2555 C  CA  . TYR A 1 329  ? 23.979 40.816  10.313  1.00 10.34 ? 329  TYR A CA  1 
ATOM   2556 C  C   . TYR A 1 329  ? 23.957 39.313  10.499  1.00 11.93 ? 329  TYR A C   1 
ATOM   2557 O  O   . TYR A 1 329  ? 23.068 38.796  11.227  1.00 13.60 ? 329  TYR A O   1 
ATOM   2558 C  CB  . TYR A 1 329  ? 25.214 41.427  11.021  1.00 10.41 ? 329  TYR A CB  1 
ATOM   2559 C  CG  . TYR A 1 329  ? 25.419 42.910  10.691  1.00 10.12 ? 329  TYR A CG  1 
ATOM   2560 C  CD1 . TYR A 1 329  ? 24.839 43.907  11.474  1.00 11.01 ? 329  TYR A CD1 1 
ATOM   2561 C  CD2 . TYR A 1 329  ? 26.150 43.289  9.577   1.00 10.69 ? 329  TYR A CD2 1 
ATOM   2562 C  CE1 . TYR A 1 329  ? 24.958 45.276  11.152  1.00 11.87 ? 329  TYR A CE1 1 
ATOM   2563 C  CE2 . TYR A 1 329  ? 26.296 44.650  9.223   1.00 11.73 ? 329  TYR A CE2 1 
ATOM   2564 C  CZ  . TYR A 1 329  ? 25.694 45.611  10.002  1.00 10.56 ? 329  TYR A CZ  1 
ATOM   2565 O  OH  . TYR A 1 329  ? 25.753 46.953  9.664   1.00 12.42 ? 329  TYR A OH  1 
ATOM   2566 N  N   . ARG A 1 330  ? 24.873 38.610  9.883   1.00 11.62 ? 330  ARG A N   1 
ATOM   2567 C  CA  . ARG A 1 330  ? 24.867 37.147  9.862   1.00 11.33 ? 330  ARG A CA  1 
ATOM   2568 C  C   . ARG A 1 330  ? 25.663 36.377  10.894  1.00 12.85 ? 330  ARG A C   1 
ATOM   2569 O  O   . ARG A 1 330  ? 25.441 35.166  11.032  1.00 15.34 ? 330  ARG A O   1 
ATOM   2570 C  CB  . ARG A 1 330  ? 25.276 36.642  8.447   1.00 12.53 ? 330  ARG A CB  1 
ATOM   2571 C  CG  . ARG A 1 330  ? 24.344 37.131  7.329   1.00 12.70 ? 330  ARG A CG  1 
ATOM   2572 C  CD  . ARG A 1 330  ? 24.726 36.550  5.951   1.00 12.20 ? 330  ARG A CD  1 
ATOM   2573 N  NE  . ARG A 1 330  ? 23.769 37.108  4.999   1.00 14.36 ? 330  ARG A NE  1 
ATOM   2574 C  CZ  . ARG A 1 330  ? 23.466 36.587  3.816   1.00 15.54 ? 330  ARG A CZ  1 
ATOM   2575 N  NH1 . ARG A 1 330  ? 24.055 35.474  3.395   1.00 17.28 ? 330  ARG A NH1 1 
ATOM   2576 N  NH2 . ARG A 1 330  ? 22.583 37.241  3.051   1.00 15.30 ? 330  ARG A NH2 1 
ATOM   2577 N  N   . THR A 1 331  ? 26.627 37.002  11.544  1.00 12.52 ? 331  THR A N   1 
ATOM   2578 C  CA  . THR A 1 331  ? 27.401 36.266  12.554  1.00 11.60 ? 331  THR A CA  1 
ATOM   2579 C  C   . THR A 1 331  ? 27.000 36.669  13.968  1.00 12.17 ? 331  THR A C   1 
ATOM   2580 O  O   . THR A 1 331  ? 26.179 37.550  14.176  1.00 14.25 ? 331  THR A O   1 
ATOM   2581 C  CB  . THR A 1 331  ? 28.948 36.494  12.409  1.00 12.63 ? 331  THR A CB  1 
ATOM   2582 O  OG1 . THR A 1 331  ? 29.308 37.802  12.912  1.00 12.21 ? 331  THR A OG1 1 
ATOM   2583 C  CG2 . THR A 1 331  ? 29.394 36.343  10.917  1.00 13.35 ? 331  THR A CG2 1 
ATOM   2584 N  N   . ASN A 1 332  ? 27.621 36.012  14.944  1.00 12.14 ? 332  ASN A N   1 
ATOM   2585 C  CA  . ASN A 1 332  ? 27.387 36.364  16.348  1.00 12.73 ? 332  ASN A CA  1 
ATOM   2586 C  C   . ASN A 1 332  ? 28.468 37.302  16.861  1.00 11.88 ? 332  ASN A C   1 
ATOM   2587 O  O   . ASN A 1 332  ? 28.716 37.340  18.079  1.00 13.22 ? 332  ASN A O   1 
ATOM   2588 C  CB  . ASN A 1 332  ? 27.325 35.097  17.252  1.00 13.89 ? 332  ASN A CB  1 
ATOM   2589 C  CG  . ASN A 1 332  ? 28.674 34.381  17.354  1.00 17.44 ? 332  ASN A CG  1 
ATOM   2590 O  OD1 . ASN A 1 332  ? 29.463 34.392  16.438  1.00 16.78 ? 332  ASN A OD1 1 
ATOM   2591 N  ND2 . ASN A 1 332  ? 28.944 33.723  18.499  1.00 20.07 ? 332  ASN A ND2 1 
ATOM   2592 N  N   . VAL A 1 333  ? 29.079 38.085  15.952  1.00 10.51 ? 333  VAL A N   1 
ATOM   2593 C  CA  . VAL A 1 333  ? 30.112 39.066  16.352  1.00 10.42 ? 333  VAL A CA  1 
ATOM   2594 C  C   . VAL A 1 333  ? 29.565 40.426  15.933  1.00 10.16 ? 333  VAL A C   1 
ATOM   2595 O  O   . VAL A 1 333  ? 29.290 40.628  14.731  1.00 11.33 ? 333  VAL A O   1 
ATOM   2596 C  CB  . VAL A 1 333  ? 31.428 38.790  15.601  1.00 11.45 ? 333  VAL A CB  1 
ATOM   2597 C  CG1 . VAL A 1 333  ? 32.482 39.818  16.018  1.00 13.28 ? 333  VAL A CG1 1 
ATOM   2598 C  CG2 . VAL A 1 333  ? 31.904 37.383  15.878  1.00 15.86 ? 333  VAL A CG2 1 
ATOM   2599 N  N   . LEU A 1 334  ? 29.438 41.382  16.843  1.00 10.18 ? 334  LEU A N   1 
ATOM   2600 C  CA  . LEU A 1 334  ? 28.823 42.661  16.602  1.00 9.13  ? 334  LEU A CA  1 
ATOM   2601 C  C   . LEU A 1 334  ? 29.792 43.821  16.784  1.00 9.52  ? 334  LEU A C   1 
ATOM   2602 O  O   . LEU A 1 334  ? 30.511 43.921  17.784  1.00 11.17 ? 334  LEU A O   1 
ATOM   2603 C  CB  . LEU A 1 334  ? 27.625 42.827  17.589  1.00 10.22 ? 334  LEU A CB  1 
ATOM   2604 C  CG  . LEU A 1 334  ? 26.809 44.136  17.402  1.00 9.79  ? 334  LEU A CG  1 
ATOM   2605 C  CD1 . LEU A 1 334  ? 25.955 44.042  16.097  1.00 11.67 ? 334  LEU A CD1 1 
ATOM   2606 C  CD2 . LEU A 1 334  ? 25.853 44.289  18.619  1.00 12.63 ? 334  LEU A CD2 1 
ATOM   2607 N  N   . LEU A 1 335  ? 29.773 44.736  15.803  1.00 9.63  ? 335  LEU A N   1 
ATOM   2608 C  CA  . LEU A 1 335  ? 30.611 45.941  15.848  1.00 9.56  ? 335  LEU A CA  1 
ATOM   2609 C  C   . LEU A 1 335  ? 29.815 47.108  16.395  1.00 7.37  ? 335  LEU A C   1 
ATOM   2610 O  O   . LEU A 1 335  ? 28.750 47.439  15.861  1.00 10.08 ? 335  LEU A O   1 
ATOM   2611 C  CB  . LEU A 1 335  ? 31.089 46.289  14.405  1.00 9.10  ? 335  LEU A CB  1 
ATOM   2612 C  CG  . LEU A 1 335  ? 31.934 47.582  14.299  1.00 9.34  ? 335  LEU A CG  1 
ATOM   2613 C  CD1 . LEU A 1 335  ? 33.248 47.399  15.042  1.00 11.43 ? 335  LEU A CD1 1 
ATOM   2614 C  CD2 . LEU A 1 335  ? 32.154 47.917  12.846  1.00 12.41 ? 335  LEU A CD2 1 
ATOM   2615 N  N   . ILE A 1 336  ? 30.327 47.748  17.456  1.00 8.64  ? 336  ILE A N   1 
ATOM   2616 C  CA  . ILE A 1 336  ? 29.704 48.932  18.053  1.00 8.98  ? 336  ILE A CA  1 
ATOM   2617 C  C   . ILE A 1 336  ? 30.724 50.065  18.103  1.00 8.15  ? 336  ILE A C   1 
ATOM   2618 O  O   . ILE A 1 336  ? 31.546 50.157  19.014  1.00 9.75  ? 336  ILE A O   1 
ATOM   2619 C  CB  . ILE A 1 336  ? 29.183 48.645  19.501  1.00 9.61  ? 336  ILE A CB  1 
ATOM   2620 C  CG1 . ILE A 1 336  ? 28.125 47.511  19.514  1.00 9.77  ? 336  ILE A CG1 1 
ATOM   2621 C  CG2 . ILE A 1 336  ? 28.592 49.959  20.082  1.00 11.00 ? 336  ILE A CG2 1 
ATOM   2622 C  CD1 . ILE A 1 336  ? 26.825 47.789  18.790  1.00 11.49 ? 336  ILE A CD1 1 
ATOM   2623 N  N   . PRO A 1 337  ? 30.740 50.922  17.070  1.00 9.70  ? 337  PRO A N   1 
ATOM   2624 C  CA  . PRO A 1 337  ? 31.665 52.076  17.116  1.00 9.66  ? 337  PRO A CA  1 
ATOM   2625 C  C   . PRO A 1 337  ? 31.276 52.977  18.296  1.00 9.82  ? 337  PRO A C   1 
ATOM   2626 O  O   . PRO A 1 337  ? 30.068 53.109  18.575  1.00 10.60 ? 337  PRO A O   1 
ATOM   2627 C  CB  . PRO A 1 337  ? 31.394 52.799  15.768  1.00 9.28  ? 337  PRO A CB  1 
ATOM   2628 C  CG  . PRO A 1 337  ? 30.948 51.653  14.850  1.00 9.41  ? 337  PRO A CG  1 
ATOM   2629 C  CD  . PRO A 1 337  ? 29.988 50.879  15.805  1.00 10.43 ? 337  PRO A CD  1 
ATOM   2630 N  N   . LEU A 1 338  ? 32.252 53.638  18.921  1.00 8.93  ? 338  LEU A N   1 
ATOM   2631 C  CA  . LEU A 1 338  ? 31.978 54.556  20.039  1.00 8.17  ? 338  LEU A CA  1 
ATOM   2632 C  C   . LEU A 1 338  ? 32.806 55.831  19.808  1.00 9.31  ? 338  LEU A C   1 
ATOM   2633 O  O   . LEU A 1 338  ? 33.968 55.908  20.211  1.00 9.08  ? 338  LEU A O   1 
ATOM   2634 C  CB  . LEU A 1 338  ? 32.340 53.875  21.375  1.00 9.47  ? 338  LEU A CB  1 
ATOM   2635 C  CG  . LEU A 1 338  ? 31.973 54.778  22.564  1.00 9.66  ? 338  LEU A CG  1 
ATOM   2636 C  CD1 . LEU A 1 338  ? 30.434 54.671  22.859  1.00 11.93 ? 338  LEU A CD1 1 
ATOM   2637 C  CD2 . LEU A 1 338  ? 32.731 54.303  23.823  1.00 13.80 ? 338  LEU A CD2 1 
ATOM   2638 N  N   . GLY A 1 339  ? 32.197 56.818  19.158  1.00 9.07  ? 339  GLY A N   1 
ATOM   2639 C  CA  . GLY A 1 339  ? 32.962 58.022  18.837  1.00 9.34  ? 339  GLY A CA  1 
ATOM   2640 C  C   . GLY A 1 339  ? 32.124 59.004  18.052  1.00 10.75 ? 339  GLY A C   1 
ATOM   2641 O  O   . GLY A 1 339  ? 30.941 58.741  17.751  1.00 10.55 ? 339  GLY A O   1 
ATOM   2642 N  N   . ASP A 1 340  ? 32.757 60.146  17.691  1.00 9.51  ? 340  ASP A N   1 
ATOM   2643 C  CA  . ASP A 1 340  ? 32.118 61.224  16.934  1.00 9.07  ? 340  ASP A CA  1 
ATOM   2644 C  C   . ASP A 1 340  ? 33.273 62.176  16.544  1.00 8.74  ? 340  ASP A C   1 
ATOM   2645 O  O   . ASP A 1 340  ? 34.452 61.886  16.748  1.00 9.84  ? 340  ASP A O   1 
ATOM   2646 C  CB  . ASP A 1 340  ? 31.039 61.874  17.845  1.00 9.69  ? 340  ASP A CB  1 
ATOM   2647 C  CG  . ASP A 1 340  ? 29.918 62.645  17.113  1.00 12.55 ? 340  ASP A CG  1 
ATOM   2648 O  OD1 . ASP A 1 340  ? 30.112 62.978  15.907  1.00 13.11 ? 340  ASP A OD1 1 
ATOM   2649 O  OD2 . ASP A 1 340  ? 28.863 62.901  17.786  1.00 14.30 ? 340  ASP A OD2 1 
ATOM   2650 N  N   . ASN A 1 341  ? 32.855 63.340  16.054  1.00 9.80  ? 341  ASN A N   1 
ATOM   2651 C  CA  . ASN A 1 341  ? 33.821 64.329  15.490  1.00 9.17  ? 341  ASN A CA  1 
ATOM   2652 C  C   . ASN A 1 341  ? 34.696 64.885  16.606  1.00 8.38  ? 341  ASN A C   1 
ATOM   2653 O  O   . ASN A 1 341  ? 34.210 65.352  17.638  1.00 10.13 ? 341  ASN A O   1 
ATOM   2654 C  CB  . ASN A 1 341  ? 33.066 65.483  14.811  1.00 11.55 ? 341  ASN A CB  1 
ATOM   2655 C  CG  . ASN A 1 341  ? 32.310 65.034  13.591  1.00 11.96 ? 341  ASN A CG  1 
ATOM   2656 O  OD1 . ASN A 1 341  ? 32.539 63.925  13.052  1.00 13.03 ? 341  ASN A OD1 1 
ATOM   2657 N  ND2 . ASN A 1 341  ? 31.432 65.928  13.092  1.00 17.51 ? 341  ASN A ND2 1 
ATOM   2658 N  N   . PHE A 1 342  ? 36.008 64.805  16.408  1.00 8.92  ? 342  PHE A N   1 
ATOM   2659 C  CA  . PHE A 1 342  ? 36.968 65.331  17.352  1.00 9.79  ? 342  PHE A CA  1 
ATOM   2660 C  C   . PHE A 1 342  ? 36.689 64.931  18.796  1.00 9.13  ? 342  PHE A C   1 
ATOM   2661 O  O   . PHE A 1 342  ? 36.947 65.724  19.744  1.00 11.76 ? 342  PHE A O   1 
ATOM   2662 C  CB  . PHE A 1 342  ? 37.125 66.876  17.186  1.00 9.09  ? 342  PHE A CB  1 
ATOM   2663 C  CG  . PHE A 1 342  ? 37.692 67.270  15.857  1.00 10.42 ? 342  PHE A CG  1 
ATOM   2664 C  CD1 . PHE A 1 342  ? 36.865 67.742  14.818  1.00 10.20 ? 342  PHE A CD1 1 
ATOM   2665 C  CD2 . PHE A 1 342  ? 39.087 67.186  15.625  1.00 10.02 ? 342  PHE A CD2 1 
ATOM   2666 C  CE1 . PHE A 1 342  ? 37.422 68.144  13.553  1.00 11.73 ? 342  PHE A CE1 1 
ATOM   2667 C  CE2 . PHE A 1 342  ? 39.624 67.583  14.395  1.00 10.31 ? 342  PHE A CE2 1 
ATOM   2668 C  CZ  . PHE A 1 342  ? 38.778 68.068  13.369  1.00 11.03 ? 342  PHE A CZ  1 
ATOM   2669 N  N   . ARG A 1 343  ? 36.290 63.662  18.977  1.00 8.76  ? 343  ARG A N   1 
ATOM   2670 C  CA  . ARG A 1 343  ? 36.090 63.161  20.340  1.00 9.20  ? 343  ARG A CA  1 
ATOM   2671 C  C   . ARG A 1 343  ? 37.396 62.695  20.983  1.00 11.71 ? 343  ARG A C   1 
ATOM   2672 O  O   . ARG A 1 343  ? 38.462 62.628  20.364  1.00 10.24 ? 343  ARG A O   1 
ATOM   2673 C  CB  . ARG A 1 343  ? 35.069 62.006  20.324  1.00 9.79  ? 343  ARG A CB  1 
ATOM   2674 C  CG  . ARG A 1 343  ? 33.626 62.433  20.110  1.00 10.46 ? 343  ARG A CG  1 
ATOM   2675 C  CD  . ARG A 1 343  ? 33.146 63.394  21.239  1.00 10.38 ? 343  ARG A CD  1 
ATOM   2676 N  NE  . ARG A 1 343  ? 31.690 63.650  21.148  1.00 10.16 ? 343  ARG A NE  1 
ATOM   2677 C  CZ  . ARG A 1 343  ? 30.777 62.911  21.791  1.00 10.88 ? 343  ARG A CZ  1 
ATOM   2678 N  NH1 . ARG A 1 343  ? 31.159 61.861  22.529  1.00 10.26 ? 343  ARG A NH1 1 
ATOM   2679 N  NH2 . ARG A 1 343  ? 29.501 63.294  21.695  1.00 11.20 ? 343  ARG A NH2 1 
ATOM   2680 N  N   . PHE A 1 344  ? 37.281 62.384  22.266  1.00 11.47 ? 344  PHE A N   1 
ATOM   2681 C  CA  . PHE A 1 344  ? 38.415 61.917  23.100  1.00 11.03 ? 344  PHE A CA  1 
ATOM   2682 C  C   . PHE A 1 344  ? 39.485 62.956  23.236  1.00 12.24 ? 344  PHE A C   1 
ATOM   2683 O  O   . PHE A 1 344  ? 40.696 62.669  23.206  1.00 15.46 ? 344  PHE A O   1 
ATOM   2684 C  CB  . PHE A 1 344  ? 38.873 60.544  22.587  1.00 11.89 ? 344  PHE A CB  1 
ATOM   2685 C  CG  . PHE A 1 344  ? 37.843 59.483  22.799  1.00 12.42 ? 344  PHE A CG  1 
ATOM   2686 C  CD1 . PHE A 1 344  ? 37.033 59.042  21.769  1.00 12.45 ? 344  PHE A CD1 1 
ATOM   2687 C  CD2 . PHE A 1 344  ? 37.639 58.946  24.090  1.00 15.97 ? 344  PHE A CD2 1 
ATOM   2688 C  CE1 . PHE A 1 344  ? 36.045 58.100  21.978  1.00 13.54 ? 344  PHE A CE1 1 
ATOM   2689 C  CE2 . PHE A 1 344  ? 36.648 57.991  24.298  1.00 15.07 ? 344  PHE A CE2 1 
ATOM   2690 C  CZ  . PHE A 1 344  ? 35.865 57.579  23.253  1.00 12.73 ? 344  PHE A CZ  1 
ATOM   2691 N  N   . LYS A 1 345  ? 39.067 64.193  23.434  1.00 12.41 ? 345  LYS A N   1 
ATOM   2692 C  CA  . LYS A 1 345  ? 39.945 65.313  23.592  1.00 14.08 ? 345  LYS A CA  1 
ATOM   2693 C  C   . LYS A 1 345  ? 40.414 65.610  25.025  1.00 17.22 ? 345  LYS A C   1 
ATOM   2694 O  O   . LYS A 1 345  ? 41.588 65.981  25.199  1.00 23.04 ? 345  LYS A O   1 
ATOM   2695 C  CB  . LYS A 1 345  ? 39.239 66.552  23.076  1.00 17.28 ? 345  LYS A CB  1 
ATOM   2696 C  CG  . LYS A 1 345  ? 40.055 67.743  23.187  1.00 16.19 ? 345  LYS A CG  1 
ATOM   2697 C  CD  . LYS A 1 345  ? 39.353 68.908  22.500  1.00 22.85 ? 345  LYS A CD  1 
ATOM   2698 C  CE  . LYS A 1 345  ? 40.056 70.204  22.764  1.00 22.91 ? 345  LYS A CE  1 
ATOM   2699 N  NZ  . LYS A 1 345  ? 39.249 71.307  22.111  1.00 26.74 ? 345  LYS A NZ  1 
ATOM   2700 N  N   . GLN A 1 346  ? 39.446 65.646  25.930  1.00 15.26 ? 346  GLN A N   1 
ATOM   2701 C  CA  . GLN A 1 346  ? 39.681 65.966  27.353  1.00 16.79 ? 346  GLN A CA  1 
ATOM   2702 C  C   . GLN A 1 346  ? 39.958 64.672  28.145  1.00 15.90 ? 346  GLN A C   1 
ATOM   2703 O  O   . GLN A 1 346  ? 39.317 63.607  27.898  1.00 13.03 ? 346  GLN A O   1 
ATOM   2704 C  CB  . GLN A 1 346  ? 38.416 66.646  27.975  1.00 18.60 ? 346  GLN A CB  1 
ATOM   2705 C  CG  . GLN A 1 346  ? 37.913 68.030  27.381  1.00 25.30 ? 346  GLN A CG  1 
ATOM   2706 C  CD  . GLN A 1 346  ? 36.696 67.874  26.428  1.00 25.42 ? 346  GLN A CD  1 
ATOM   2707 O  OE1 . GLN A 1 346  ? 36.649 66.925  25.614  1.00 21.58 ? 346  GLN A OE1 1 
ATOM   2708 N  NE2 . GLN A 1 346  ? 35.722 68.781  26.519  1.00 25.60 ? 346  GLN A NE2 1 
ATOM   2709 N  N   . ASN A 1 347  ? 40.873 64.726  29.113  1.00 16.34 ? 347  ASN A N   1 
ATOM   2710 C  CA  . ASN A 1 347  ? 41.122 63.566  29.986  1.00 15.43 ? 347  ASN A CA  1 
ATOM   2711 C  C   . ASN A 1 347  ? 39.832 63.141  30.697  1.00 13.54 ? 347  ASN A C   1 
ATOM   2712 O  O   . ASN A 1 347  ? 39.565 61.939  30.792  1.00 14.75 ? 347  ASN A O   1 
ATOM   2713 C  CB  . ASN A 1 347  ? 42.150 63.927  31.088  1.00 18.87 ? 347  ASN A CB  1 
ATOM   2714 C  CG  . ASN A 1 347  ? 43.446 64.144  30.500  1.00 27.56 ? 347  ASN A CG  1 
ATOM   2715 O  OD1 . ASN A 1 347  ? 43.918 63.263  29.807  1.00 27.10 ? 347  ASN A OD1 1 
ATOM   2716 N  ND2 . ASN A 1 347  ? 44.053 65.333  30.702  1.00 31.68 ? 347  ASN A ND2 1 
ATOM   2717 N  N   . THR A 1 348  ? 39.008 64.097  31.123  1.00 12.81 ? 348  THR A N   1 
ATOM   2718 C  CA  . THR A 1 348  ? 37.758 63.785  31.785  1.00 13.65 ? 348  THR A CA  1 
ATOM   2719 C  C   . THR A 1 348  ? 36.808 63.027  30.842  1.00 14.39 ? 348  THR A C   1 
ATOM   2720 O  O   . THR A 1 348  ? 35.947 62.265  31.309  1.00 14.47 ? 348  THR A O   1 
ATOM   2721 C  CB  . THR A 1 348  ? 37.068 65.075  32.293  1.00 16.04 ? 348  THR A CB  1 
ATOM   2722 O  OG1 . THR A 1 348  ? 36.947 66.003  31.201  1.00 19.96 ? 348  THR A OG1 1 
ATOM   2723 C  CG2 . THR A 1 348  ? 37.878 65.708  33.490  1.00 17.37 ? 348  THR A CG2 1 
ATOM   2724 N  N   . GLU A 1 349  ? 36.886 63.273  29.525  1.00 10.73 ? 349  GLU A N   1 
ATOM   2725 C  CA  . GLU A 1 349  ? 36.046 62.536  28.557  1.00 12.24 ? 349  GLU A CA  1 
ATOM   2726 C  C   . GLU A 1 349  ? 36.491 61.086  28.434  1.00 11.00 ? 349  GLU A C   1 
ATOM   2727 O  O   . GLU A 1 349  ? 35.660 60.166  28.417  1.00 10.73 ? 349  GLU A O   1 
ATOM   2728 C  CB  . GLU A 1 349  ? 36.091 63.222  27.176  1.00 12.04 ? 349  GLU A CB  1 
ATOM   2729 C  CG  . GLU A 1 349  ? 35.315 62.471  26.142  1.00 12.31 ? 349  GLU A CG  1 
ATOM   2730 C  CD  . GLU A 1 349  ? 35.537 63.061  24.733  1.00 13.58 ? 349  GLU A CD  1 
ATOM   2731 O  OE1 . GLU A 1 349  ? 35.026 62.440  23.809  1.00 14.03 ? 349  GLU A OE1 1 
ATOM   2732 O  OE2 . GLU A 1 349  ? 36.220 64.099  24.595  1.00 15.36 ? 349  GLU A OE2 1 
ATOM   2733 N  N   . TRP A 1 350  ? 37.795 60.863  28.349  1.00 10.85 ? 350  TRP A N   1 
ATOM   2734 C  CA  . TRP A 1 350  ? 38.316 59.486  28.329  1.00 10.56 ? 350  TRP A CA  1 
ATOM   2735 C  C   . TRP A 1 350  ? 37.795 58.733  29.563  1.00 11.15 ? 350  TRP A C   1 
ATOM   2736 O  O   . TRP A 1 350  ? 37.287 57.610  29.471  1.00 11.96 ? 350  TRP A O   1 
ATOM   2737 C  CB  . TRP A 1 350  ? 39.857 59.442  28.377  1.00 10.00 ? 350  TRP A CB  1 
ATOM   2738 C  CG  . TRP A 1 350  ? 40.477 59.724  27.043  1.00 10.42 ? 350  TRP A CG  1 
ATOM   2739 C  CD1 . TRP A 1 350  ? 40.788 60.926  26.514  1.00 10.56 ? 350  TRP A CD1 1 
ATOM   2740 C  CD2 . TRP A 1 350  ? 40.787 58.742  26.059  1.00 10.58 ? 350  TRP A CD2 1 
ATOM   2741 N  NE1 . TRP A 1 350  ? 41.296 60.770  25.244  1.00 10.37 ? 350  TRP A NE1 1 
ATOM   2742 C  CE2 . TRP A 1 350  ? 41.284 59.441  24.925  1.00 10.77 ? 350  TRP A CE2 1 
ATOM   2743 C  CE3 . TRP A 1 350  ? 40.690 57.358  26.010  1.00 14.05 ? 350  TRP A CE3 1 
ATOM   2744 C  CZ2 . TRP A 1 350  ? 41.680 58.772  23.740  1.00 12.72 ? 350  TRP A CZ2 1 
ATOM   2745 C  CZ3 . TRP A 1 350  ? 41.085 56.706  24.821  1.00 16.77 ? 350  TRP A CZ3 1 
ATOM   2746 C  CH2 . TRP A 1 350  ? 41.561 57.424  23.721  1.00 14.21 ? 350  TRP A CH2 1 
ATOM   2747 N  N   . ASP A 1 351  ? 37.855 59.374  30.743  1.00 11.91 ? 351  ASP A N   1 
ATOM   2748 C  CA  . ASP A 1 351  ? 37.420 58.713  31.971  1.00 13.00 ? 351  ASP A CA  1 
ATOM   2749 C  C   . ASP A 1 351  ? 35.921 58.463  31.962  1.00 11.39 ? 351  ASP A C   1 
ATOM   2750 O  O   . ASP A 1 351  ? 35.480 57.331  32.304  1.00 13.22 ? 351  ASP A O   1 
ATOM   2751 C  CB  . ASP A 1 351  ? 37.735 59.592  33.197  1.00 15.62 ? 351  ASP A CB  1 
ATOM   2752 C  CG  . ASP A 1 351  ? 39.198 59.670  33.518  1.00 20.71 ? 351  ASP A CG  1 
ATOM   2753 O  OD1 . ASP A 1 351  ? 39.953 58.716  33.233  1.00 25.44 ? 351  ASP A OD1 1 
ATOM   2754 O  OD2 . ASP A 1 351  ? 39.579 60.681  34.141  1.00 28.85 ? 351  ASP A OD2 1 
ATOM   2755 N  N   . VAL A 1 352  ? 35.122 59.445  31.582  1.00 12.25 ? 352  VAL A N   1 
ATOM   2756 C  CA  . VAL A 1 352  ? 33.690 59.238  31.666  1.00 12.52 ? 352  VAL A CA  1 
ATOM   2757 C  C   . VAL A 1 352  ? 33.245 58.140  30.700  1.00 13.67 ? 352  VAL A C   1 
ATOM   2758 O  O   . VAL A 1 352  ? 32.370 57.328  31.041  1.00 14.23 ? 352  VAL A O   1 
ATOM   2759 C  CB  . VAL A 1 352  ? 32.927 60.599  31.503  1.00 16.43 ? 352  VAL A CB  1 
ATOM   2760 C  CG1 . VAL A 1 352  ? 32.684 60.965  30.066  1.00 15.11 ? 352  VAL A CG1 1 
ATOM   2761 C  CG2 . VAL A 1 352  ? 31.662 60.586  32.332  1.00 21.29 ? 352  VAL A CG2 1 
ATOM   2762 N  N   . GLN A 1 353  ? 33.814 58.032  29.493  1.00 11.29 ? 353  GLN A N   1 
ATOM   2763 C  CA  . GLN A 1 353  ? 33.378 56.960  28.628  1.00 10.00 ? 353  GLN A CA  1 
ATOM   2764 C  C   . GLN A 1 353  ? 33.925 55.617  29.087  1.00 11.26 ? 353  GLN A C   1 
ATOM   2765 O  O   . GLN A 1 353  ? 33.165 54.620  29.197  1.00 13.00 ? 353  GLN A O   1 
ATOM   2766 C  CB  . GLN A 1 353  ? 33.818 57.202  27.158  1.00 11.14 ? 353  GLN A CB  1 
ATOM   2767 C  CG  . GLN A 1 353  ? 33.299 58.490  26.512  1.00 11.63 ? 353  GLN A CG  1 
ATOM   2768 C  CD  . GLN A 1 353  ? 31.849 58.453  26.070  1.00 11.70 ? 353  GLN A CD  1 
ATOM   2769 O  OE1 . GLN A 1 353  ? 30.996 57.766  26.677  1.00 12.56 ? 353  GLN A OE1 1 
ATOM   2770 N  NE2 . GLN A 1 353  ? 31.518 59.207  25.053  1.00 11.34 ? 353  GLN A NE2 1 
ATOM   2771 N  N   . ARG A 1 354  ? 35.199 55.549  29.412  1.00 10.34 ? 354  ARG A N   1 
ATOM   2772 C  CA  . ARG A 1 354  ? 35.765 54.295  29.804  1.00 11.28 ? 354  ARG A CA  1 
ATOM   2773 C  C   . ARG A 1 354  ? 35.162 53.703  31.091  1.00 12.13 ? 354  ARG A C   1 
ATOM   2774 O  O   . ARG A 1 354  ? 34.824 52.488  31.111  1.00 12.85 ? 354  ARG A O   1 
ATOM   2775 C  CB  . ARG A 1 354  ? 37.283 54.416  30.023  1.00 11.07 ? 354  ARG A CB  1 
ATOM   2776 C  CG  . ARG A 1 354  ? 37.938 53.062  30.497  1.00 11.64 ? 354  ARG A CG  1 
ATOM   2777 C  CD  . ARG A 1 354  ? 39.476 53.219  30.751  1.00 14.52 ? 354  ARG A CD  1 
ATOM   2778 N  NE  . ARG A 1 354  ? 39.782 54.280  31.725  1.00 16.22 ? 354  ARG A NE  1 
ATOM   2779 C  CZ  . ARG A 1 354  ? 39.656 54.182  33.063  1.00 16.91 ? 354  ARG A CZ  1 
ATOM   2780 N  NH1 . ARG A 1 354  ? 39.226 53.061  33.613  1.00 17.61 ? 354  ARG A NH1 1 
ATOM   2781 N  NH2 . ARG A 1 354  ? 39.973 55.198  33.820  1.00 18.65 ? 354  ARG A NH2 1 
ATOM   2782 N  N   . VAL A 1 355  ? 35.028 54.505  32.143  1.00 12.04 ? 355  VAL A N   1 
ATOM   2783 C  CA  . VAL A 1 355  ? 34.576 53.913  33.410  1.00 12.45 ? 355  VAL A CA  1 
ATOM   2784 C  C   . VAL A 1 355  ? 33.128 53.475  33.303  1.00 12.82 ? 355  VAL A C   1 
ATOM   2785 O  O   . VAL A 1 355  ? 32.773 52.402  33.877  1.00 13.76 ? 355  VAL A O   1 
ATOM   2786 C  CB  . VAL A 1 355  ? 34.743 54.963  34.559  1.00 14.41 ? 355  VAL A CB  1 
ATOM   2787 C  CG1 . VAL A 1 355  ? 34.050 54.531  35.866  1.00 21.10 ? 355  VAL A CG1 1 
ATOM   2788 C  CG2 . VAL A 1 355  ? 36.229 55.218  34.815  1.00 16.08 ? 355  VAL A CG2 1 
ATOM   2789 N  N   . ASN A 1 356  ? 32.252 54.247  32.669  1.00 11.47 ? 356  ASN A N   1 
ATOM   2790 C  CA  . ASN A 1 356  ? 30.864 53.830  32.554  1.00 11.65 ? 356  ASN A CA  1 
ATOM   2791 C  C   . ASN A 1 356  ? 30.724 52.565  31.709  1.00 12.98 ? 356  ASN A C   1 
ATOM   2792 O  O   . ASN A 1 356  ? 29.973 51.634  32.081  1.00 12.61 ? 356  ASN A O   1 
ATOM   2793 C  CB  . ASN A 1 356  ? 30.018 54.985  32.052  1.00 12.26 ? 356  ASN A CB  1 
ATOM   2794 C  CG  . ASN A 1 356  ? 29.796 56.014  33.127  1.00 13.81 ? 356  ASN A CG  1 
ATOM   2795 O  OD1 . ASN A 1 356  ? 29.093 55.686  34.116  1.00 14.17 ? 356  ASN A OD1 1 
ATOM   2796 N  ND2 . ASN A 1 356  ? 30.412 57.191  33.066  1.00 13.29 ? 356  ASN A ND2 1 
ATOM   2797 N  N   . TYR A 1 357  ? 31.460 52.457  30.590  1.00 11.19 ? 357  TYR A N   1 
ATOM   2798 C  CA  . TYR A 1 357  ? 31.389 51.242  29.790  1.00 12.78 ? 357  TYR A CA  1 
ATOM   2799 C  C   . TYR A 1 357  ? 31.998 50.090  30.556  1.00 11.69 ? 357  TYR A C   1 
ATOM   2800 O  O   . TYR A 1 357  ? 31.459 48.965  30.472  1.00 12.40 ? 357  TYR A O   1 
ATOM   2801 C  CB  . TYR A 1 357  ? 32.041 51.466  28.370  1.00 11.46 ? 357  TYR A CB  1 
ATOM   2802 C  CG  . TYR A 1 357  ? 31.022 51.981  27.407  1.00 10.93 ? 357  TYR A CG  1 
ATOM   2803 C  CD1 . TYR A 1 357  ? 30.840 53.354  27.238  1.00 10.71 ? 357  TYR A CD1 1 
ATOM   2804 C  CD2 . TYR A 1 357  ? 30.198 51.082  26.687  1.00 11.21 ? 357  TYR A CD2 1 
ATOM   2805 C  CE1 . TYR A 1 357  ? 29.881 53.833  26.384  1.00 10.41 ? 357  TYR A CE1 1 
ATOM   2806 C  CE2 . TYR A 1 357  ? 29.220 51.551  25.853  1.00 11.11 ? 357  TYR A CE2 1 
ATOM   2807 C  CZ  . TYR A 1 357  ? 29.057 52.936  25.701  1.00 11.17 ? 357  TYR A CZ  1 
ATOM   2808 O  OH  . TYR A 1 357  ? 28.062 53.344  24.878  1.00 12.55 ? 357  TYR A OH  1 
ATOM   2809 N  N   . GLU A 1 358  ? 33.091 50.292  31.296  1.00 11.67 ? 358  GLU A N   1 
ATOM   2810 C  CA  . GLU A 1 358  ? 33.631 49.160  32.075  1.00 12.69 ? 358  GLU A CA  1 
ATOM   2811 C  C   . GLU A 1 358  ? 32.599 48.621  33.114  1.00 13.58 ? 358  GLU A C   1 
ATOM   2812 O  O   . GLU A 1 358  ? 32.483 47.413  33.294  1.00 13.51 ? 358  GLU A O   1 
ATOM   2813 C  CB  . GLU A 1 358  ? 34.886 49.545  32.821  1.00 13.77 ? 358  GLU A CB  1 
ATOM   2814 C  CG  . GLU A 1 358  ? 36.233 49.684  32.012  1.00 19.67 ? 358  GLU A CG  1 
ATOM   2815 C  CD  . GLU A 1 358  ? 37.375 50.187  32.930  1.00 19.18 ? 358  GLU A CD  1 
ATOM   2816 O  OE1 . GLU A 1 358  ? 37.160 50.280  34.177  1.00 32.93 ? 358  GLU A OE1 1 
ATOM   2817 O  OE2 . GLU A 1 358  ? 38.495 50.487  32.482  1.00 24.22 ? 358  GLU A OE2 1 
ATOM   2818 N  N   A ARG A 1 359  ? 31.800 49.501  33.707  0.50 11.44 ? 359  ARG A N   1 
ATOM   2819 N  N   B ARG A 1 359  ? 31.800 49.501  33.707  0.50 13.06 ? 359  ARG A N   1 
ATOM   2820 C  CA  A ARG A 1 359  ? 30.808 48.995  34.667  0.50 13.99 ? 359  ARG A CA  1 
ATOM   2821 C  CA  B ARG A 1 359  ? 30.808 48.995  34.667  0.50 15.93 ? 359  ARG A CA  1 
ATOM   2822 C  C   A ARG A 1 359  ? 29.716 48.210  33.910  0.50 13.58 ? 359  ARG A C   1 
ATOM   2823 C  C   B ARG A 1 359  ? 29.716 48.210  33.910  0.50 14.80 ? 359  ARG A C   1 
ATOM   2824 O  O   A ARG A 1 359  ? 29.196 47.185  34.405  0.50 13.52 ? 359  ARG A O   1 
ATOM   2825 O  O   B ARG A 1 359  ? 29.196 47.185  34.405  0.50 14.25 ? 359  ARG A O   1 
ATOM   2826 C  CB  A ARG A 1 359  ? 30.172 50.152  35.413  0.50 11.48 ? 359  ARG A CB  1 
ATOM   2827 C  CB  B ARG A 1 359  ? 30.172 50.152  35.413  0.50 16.55 ? 359  ARG A CB  1 
ATOM   2828 C  CG  A ARG A 1 359  ? 31.082 50.830  36.432  0.50 14.74 ? 359  ARG A CG  1 
ATOM   2829 C  CG  B ARG A 1 359  ? 31.082 50.830  36.432  0.50 21.37 ? 359  ARG A CG  1 
ATOM   2830 C  CD  A ARG A 1 359  ? 30.330 52.066  36.945  0.50 20.90 ? 359  ARG A CD  1 
ATOM   2831 C  CD  B ARG A 1 359  ? 30.330 52.066  36.945  0.50 27.70 ? 359  ARG A CD  1 
ATOM   2832 N  NE  A ARG A 1 359  ? 31.143 52.986  37.766  0.50 22.96 ? 359  ARG A NE  1 
ATOM   2833 N  NE  B ARG A 1 359  ? 30.903 52.675  38.162  0.50 31.71 ? 359  ARG A NE  1 
ATOM   2834 C  CZ  A ARG A 1 359  ? 31.138 54.318  37.607  0.50 25.33 ? 359  ARG A CZ  1 
ATOM   2835 C  CZ  B ARG A 1 359  ? 30.955 52.049  39.347  0.50 33.87 ? 359  ARG A CZ  1 
ATOM   2836 N  NH1 A ARG A 1 359  ? 30.379 54.931  36.649  0.50 16.71 ? 359  ARG A NH1 1 
ATOM   2837 N  NH1 B ARG A 1 359  ? 30.461 50.786  39.522  0.50 34.53 ? 359  ARG A NH1 1 
ATOM   2838 N  NH2 A ARG A 1 359  ? 31.890 55.050  38.430  0.50 31.56 ? 359  ARG A NH2 1 
ATOM   2839 N  NH2 B ARG A 1 359  ? 31.525 52.688  40.370  0.50 35.51 ? 359  ARG A NH2 1 
ATOM   2840 N  N   . LEU A 1 360  ? 29.338 48.657  32.716  1.00 12.25 ? 360  LEU A N   1 
ATOM   2841 C  CA  . LEU A 1 360  ? 28.342 47.936  31.935  1.00 11.60 ? 360  LEU A CA  1 
ATOM   2842 C  C   . LEU A 1 360  ? 28.942 46.578  31.543  1.00 11.70 ? 360  LEU A C   1 
ATOM   2843 O  O   . LEU A 1 360  ? 28.260 45.517  31.696  1.00 13.60 ? 360  LEU A O   1 
ATOM   2844 C  CB  . LEU A 1 360  ? 27.934 48.746  30.696  1.00 13.04 ? 360  LEU A CB  1 
ATOM   2845 C  CG  . LEU A 1 360  ? 27.083 49.969  31.058  1.00 11.76 ? 360  LEU A CG  1 
ATOM   2846 C  CD1 . LEU A 1 360  ? 27.153 50.968  29.908  1.00 15.17 ? 360  LEU A CD1 1 
ATOM   2847 C  CD2 . LEU A 1 360  ? 25.587 49.624  31.266  1.00 14.66 ? 360  LEU A CD2 1 
ATOM   2848 N  N   . PHE A 1 361  ? 30.180 46.484  31.066  1.00 11.57 ? 361  PHE A N   1 
ATOM   2849 C  CA  . PHE A 1 361  ? 30.732 45.202  30.664  1.00 13.05 ? 361  PHE A CA  1 
ATOM   2850 C  C   . PHE A 1 361  ? 30.787 44.235  31.862  1.00 14.71 ? 361  PHE A C   1 
ATOM   2851 O  O   . PHE A 1 361  ? 30.503 43.055  31.712  1.00 14.24 ? 361  PHE A O   1 
ATOM   2852 C  CB  . PHE A 1 361  ? 32.168 45.356  30.141  1.00 11.70 ? 361  PHE A CB  1 
ATOM   2853 C  CG  . PHE A 1 361  ? 32.294 46.193  28.878  1.00 12.98 ? 361  PHE A CG  1 
ATOM   2854 C  CD1 . PHE A 1 361  ? 33.531 46.770  28.601  1.00 11.76 ? 361  PHE A CD1 1 
ATOM   2855 C  CD2 . PHE A 1 361  ? 31.232 46.397  27.993  1.00 11.78 ? 361  PHE A CD2 1 
ATOM   2856 C  CE1 . PHE A 1 361  ? 33.732 47.561  27.421  1.00 12.35 ? 361  PHE A CE1 1 
ATOM   2857 C  CE2 . PHE A 1 361  ? 31.414 47.181  26.818  1.00 12.74 ? 361  PHE A CE2 1 
ATOM   2858 C  CZ  . PHE A 1 361  ? 32.692 47.743  26.581  1.00 12.06 ? 361  PHE A CZ  1 
ATOM   2859 N  N   . GLU A 1 362  ? 31.239 44.718  33.027  1.00 14.99 ? 362  GLU A N   1 
ATOM   2860 C  CA  . GLU A 1 362  ? 31.382 43.822  34.170  1.00 14.12 ? 362  GLU A CA  1 
ATOM   2861 C  C   . GLU A 1 362  ? 29.995 43.259  34.505  1.00 13.08 ? 362  GLU A C   1 
ATOM   2862 O  O   . GLU A 1 362  ? 29.919 42.022  34.739  1.00 16.39 ? 362  GLU A O   1 
ATOM   2863 C  CB  . GLU A 1 362  ? 31.936 44.525  35.407  1.00 17.89 ? 362  GLU A CB  1 
ATOM   2864 C  CG  . GLU A 1 362  ? 32.122 43.401  36.526  1.00 21.42 ? 362  GLU A CG  1 
ATOM   2865 C  CD  . GLU A 1 362  ? 32.596 43.933  37.884  1.00 30.58 ? 362  GLU A CD  1 
ATOM   2866 O  OE1 . GLU A 1 362  ? 33.163 45.038  37.915  1.00 30.21 ? 362  GLU A OE1 1 
ATOM   2867 O  OE2 . GLU A 1 362  ? 32.409 43.230  38.918  1.00 31.51 ? 362  GLU A OE2 1 
ATOM   2868 N  N   . HIS A 1 363  ? 28.943 44.044  34.476  1.00 13.35 ? 363  HIS A N   1 
ATOM   2869 C  CA  . HIS A 1 363  ? 27.621 43.517  34.773  1.00 14.97 ? 363  HIS A CA  1 
ATOM   2870 C  C   . HIS A 1 363  ? 27.122 42.570  33.701  1.00 15.07 ? 363  HIS A C   1 
ATOM   2871 O  O   . HIS A 1 363  ? 26.766 41.402  33.963  1.00 16.73 ? 363  HIS A O   1 
ATOM   2872 C  CB  . HIS A 1 363  ? 26.636 44.645  34.974  1.00 15.74 ? 363  HIS A CB  1 
ATOM   2873 C  CG  . HIS A 1 363  ? 25.236 44.179  35.282  1.00 15.17 ? 363  HIS A CG  1 
ATOM   2874 N  ND1 . HIS A 1 363  ? 24.874 43.650  36.521  1.00 23.82 ? 363  HIS A ND1 1 
ATOM   2875 C  CD2 . HIS A 1 363  ? 24.138 44.107  34.499  1.00 18.80 ? 363  HIS A CD2 1 
ATOM   2876 C  CE1 . HIS A 1 363  ? 23.609 43.259  36.453  1.00 20.43 ? 363  HIS A CE1 1 
ATOM   2877 N  NE2 . HIS A 1 363  ? 23.136 43.522  35.248  1.00 22.25 ? 363  HIS A NE2 1 
ATOM   2878 N  N   . ILE A 1 364  ? 27.131 43.020  32.444  1.00 14.68 ? 364  ILE A N   1 
ATOM   2879 C  CA  . ILE A 1 364  ? 26.637 42.239  31.339  1.00 13.90 ? 364  ILE A CA  1 
ATOM   2880 C  C   . ILE A 1 364  ? 27.354 40.933  31.212  1.00 12.98 ? 364  ILE A C   1 
ATOM   2881 O  O   . ILE A 1 364  ? 26.662 39.862  31.068  1.00 15.20 ? 364  ILE A O   1 
ATOM   2882 C  CB  . ILE A 1 364  ? 26.744 43.040  29.998  1.00 12.57 ? 364  ILE A CB  1 
ATOM   2883 C  CG1 . ILE A 1 364  ? 25.740 44.171  30.052  1.00 13.20 ? 364  ILE A CG1 1 
ATOM   2884 C  CG2 . ILE A 1 364  ? 26.501 42.093  28.802  1.00 14.27 ? 364  ILE A CG2 1 
ATOM   2885 C  CD1 . ILE A 1 364  ? 26.020 45.313  29.026  1.00 14.30 ? 364  ILE A CD1 1 
ATOM   2886 N  N   . ASN A 1 365  ? 28.660 40.924  31.293  1.00 12.94 ? 365  ASN A N   1 
ATOM   2887 C  CA  . ASN A 1 365  ? 29.446 39.704  31.071  1.00 14.25 ? 365  ASN A CA  1 
ATOM   2888 C  C   . ASN A 1 365  ? 29.294 38.660  32.185  1.00 17.65 ? 365  ASN A C   1 
ATOM   2889 O  O   . ASN A 1 365  ? 29.557 37.464  31.974  1.00 17.77 ? 365  ASN A O   1 
ATOM   2890 C  CB  . ASN A 1 365  ? 30.928 40.011  30.857  1.00 13.45 ? 365  ASN A CB  1 
ATOM   2891 C  CG  . ASN A 1 365  ? 31.166 40.853  29.590  1.00 12.70 ? 365  ASN A CG  1 
ATOM   2892 O  OD1 . ASN A 1 365  ? 30.248 41.047  28.762  1.00 14.57 ? 365  ASN A OD1 1 
ATOM   2893 N  ND2 . ASN A 1 365  ? 32.385 41.346  29.463  1.00 13.35 ? 365  ASN A ND2 1 
ATOM   2894 N  N   . SER A 1 366  ? 28.851 39.142  33.352  1.00 18.57 ? 366  SER A N   1 
ATOM   2895 C  CA  . SER A 1 366  ? 28.660 38.244  34.529  1.00 20.90 ? 366  SER A CA  1 
ATOM   2896 C  C   . SER A 1 366  ? 27.227 37.753  34.649  1.00 23.06 ? 366  SER A C   1 
ATOM   2897 O  O   . SER A 1 366  ? 26.970 36.858  35.481  1.00 26.54 ? 366  SER A O   1 
ATOM   2898 C  CB  . SER A 1 366  ? 29.085 38.998  35.817  1.00 22.95 ? 366  SER A CB  1 
ATOM   2899 O  OG  . SER A 1 366  ? 28.088 39.952  36.138  1.00 25.56 ? 366  SER A OG  1 
ATOM   2900 N  N   . GLN A 1 367  ? 26.287 38.303  33.896  1.00 24.37 ? 367  GLN A N   1 
ATOM   2901 C  CA  . GLN A 1 367  ? 24.866 37.933  33.935  1.00 24.77 ? 367  GLN A CA  1 
ATOM   2902 C  C   . GLN A 1 367  ? 24.580 36.933  32.800  1.00 25.95 ? 367  GLN A C   1 
ATOM   2903 O  O   . GLN A 1 367  ? 24.251 37.328  31.672  1.00 22.13 ? 367  GLN A O   1 
ATOM   2904 C  CB  . GLN A 1 367  ? 23.946 39.164  33.738  1.00 27.05 ? 367  GLN A CB  1 
ATOM   2905 C  CG  . GLN A 1 367  ? 23.870 40.128  34.935  1.00 32.35 ? 367  GLN A CG  1 
ATOM   2906 C  CD  . GLN A 1 367  ? 23.327 39.422  36.159  1.00 35.96 ? 367  GLN A CD  1 
ATOM   2907 O  OE1 . GLN A 1 367  ? 22.154 39.069  36.198  1.00 36.74 ? 367  GLN A OE1 1 
ATOM   2908 N  NE2 . GLN A 1 367  ? 24.194 39.187  37.160  1.00 39.85 ? 367  GLN A NE2 1 
ATOM   2909 N  N   . ALA A 1 368  ? 24.650 35.632  33.108  1.00 24.51 ? 368  ALA A N   1 
ATOM   2910 C  CA  . ALA A 1 368  ? 24.420 34.642  32.045  1.00 21.36 ? 368  ALA A CA  1 
ATOM   2911 C  C   . ALA A 1 368  ? 23.171 34.817  31.192  1.00 21.81 ? 368  ALA A C   1 
ATOM   2912 O  O   . ALA A 1 368  ? 23.224 34.511  29.972  1.00 21.47 ? 368  ALA A O   1 
ATOM   2913 C  CB  . ALA A 1 368  ? 24.438 33.204  32.644  1.00 23.74 ? 368  ALA A CB  1 
ATOM   2914 N  N   . HIS A 1 369  ? 22.056 35.293  31.762  1.00 20.41 ? 369  HIS A N   1 
ATOM   2915 C  CA  . HIS A 1 369  ? 20.835 35.432  30.977  1.00 20.04 ? 369  HIS A CA  1 
ATOM   2916 C  C   . HIS A 1 369  ? 20.973 36.322  29.713  1.00 18.11 ? 369  HIS A C   1 
ATOM   2917 O  O   . HIS A 1 369  ? 20.155 36.254  28.816  1.00 20.95 ? 369  HIS A O   1 
ATOM   2918 C  CB  . HIS A 1 369  ? 19.657 35.931  31.870  1.00 23.91 ? 369  HIS A CB  1 
ATOM   2919 C  CG  . HIS A 1 369  ? 19.831 37.321  32.410  1.00 27.22 ? 369  HIS A CG  1 
ATOM   2920 N  ND1 . HIS A 1 369  ? 19.403 38.439  31.727  1.00 29.81 ? 369  HIS A ND1 1 
ATOM   2921 C  CD2 . HIS A 1 369  ? 20.447 37.774  33.526  1.00 29.75 ? 369  HIS A CD2 1 
ATOM   2922 C  CE1 . HIS A 1 369  ? 19.759 39.524  32.395  1.00 25.68 ? 369  HIS A CE1 1 
ATOM   2923 N  NE2 . HIS A 1 369  ? 20.396 39.148  33.490  1.00 29.72 ? 369  HIS A NE2 1 
ATOM   2924 N  N   . PHE A 1 370  ? 21.971 37.208  29.708  1.00 22.07 ? 370  PHE A N   1 
ATOM   2925 C  CA  . PHE A 1 370  ? 22.159 38.054  28.501  1.00 19.40 ? 370  PHE A CA  1 
ATOM   2926 C  C   . PHE A 1 370  ? 22.846 37.277  27.379  1.00 16.15 ? 370  PHE A C   1 
ATOM   2927 O  O   . PHE A 1 370  ? 22.653 37.588  26.218  1.00 16.62 ? 370  PHE A O   1 
ATOM   2928 C  CB  . PHE A 1 370  ? 23.051 39.265  28.784  1.00 22.17 ? 370  PHE A CB  1 
ATOM   2929 C  CG  . PHE A 1 370  ? 22.383 40.360  29.552  1.00 21.06 ? 370  PHE A CG  1 
ATOM   2930 C  CD1 . PHE A 1 370  ? 22.979 40.830  30.685  1.00 22.42 ? 370  PHE A CD1 1 
ATOM   2931 C  CD2 . PHE A 1 370  ? 21.210 40.948  29.104  1.00 20.89 ? 370  PHE A CD2 1 
ATOM   2932 C  CE1 . PHE A 1 370  ? 22.405 41.902  31.387  1.00 23.67 ? 370  PHE A CE1 1 
ATOM   2933 C  CE2 . PHE A 1 370  ? 20.643 42.032  29.803  1.00 26.27 ? 370  PHE A CE2 1 
ATOM   2934 C  CZ  . PHE A 1 370  ? 21.261 42.481  30.933  1.00 22.16 ? 370  PHE A CZ  1 
ATOM   2935 N  N   . ASN A 1 371  ? 23.695 36.340  27.753  1.00 14.53 ? 371  ASN A N   1 
ATOM   2936 C  CA  . ASN A 1 371  ? 24.451 35.536  26.804  1.00 14.17 ? 371  ASN A CA  1 
ATOM   2937 C  C   . ASN A 1 371  ? 25.247 36.447  25.876  1.00 13.40 ? 371  ASN A C   1 
ATOM   2938 O  O   . ASN A 1 371  ? 25.276 36.239  24.657  1.00 14.09 ? 371  ASN A O   1 
ATOM   2939 C  CB  . ASN A 1 371  ? 23.518 34.575  26.002  1.00 16.51 ? 371  ASN A CB  1 
ATOM   2940 C  CG  . ASN A 1 371  ? 22.857 33.507  26.937  1.00 15.44 ? 371  ASN A CG  1 
ATOM   2941 O  OD1 . ASN A 1 371  ? 23.554 32.673  27.508  1.00 20.11 ? 371  ASN A OD1 1 
ATOM   2942 N  ND2 . ASN A 1 371  ? 21.554 33.622  27.114  1.00 20.62 ? 371  ASN A ND2 1 
ATOM   2943 N  N   . VAL A 1 372  ? 25.931 37.395  26.501  1.00 13.49 ? 372  VAL A N   1 
ATOM   2944 C  CA  . VAL A 1 372  ? 26.747 38.374  25.767  1.00 12.33 ? 372  VAL A CA  1 
ATOM   2945 C  C   . VAL A 1 372  ? 28.119 38.451  26.404  1.00 13.72 ? 372  VAL A C   1 
ATOM   2946 O  O   . VAL A 1 372  ? 28.258 38.388  27.653  1.00 14.48 ? 372  VAL A O   1 
ATOM   2947 C  CB  . VAL A 1 372  ? 26.109 39.803  25.878  1.00 13.02 ? 372  VAL A CB  1 
ATOM   2948 C  CG1 . VAL A 1 372  ? 27.124 40.894  25.343  1.00 13.07 ? 372  VAL A CG1 1 
ATOM   2949 C  CG2 . VAL A 1 372  ? 24.803 39.881  25.094  1.00 14.10 ? 372  VAL A CG2 1 
ATOM   2950 N  N   . GLN A 1 373  ? 29.174 38.625  25.583  1.00 13.12 ? 373  GLN A N   1 
ATOM   2951 C  CA  . GLN A 1 373  ? 30.545 38.898  26.066  1.00 12.42 ? 373  GLN A CA  1 
ATOM   2952 C  C   . GLN A 1 373  ? 30.939 40.205  25.342  1.00 12.15 ? 373  GLN A C   1 
ATOM   2953 O  O   . GLN A 1 373  ? 31.149 40.202  24.104  1.00 12.53 ? 373  GLN A O   1 
ATOM   2954 C  CB  . GLN A 1 373  ? 31.496 37.767  25.707  1.00 14.02 ? 373  GLN A CB  1 
ATOM   2955 C  CG  . GLN A 1 373  ? 32.977 38.092  26.040  1.00 15.02 ? 373  GLN A CG  1 
ATOM   2956 C  CD  . GLN A 1 373  ? 33.219 38.400  27.545  1.00 18.52 ? 373  GLN A CD  1 
ATOM   2957 O  OE1 . GLN A 1 373  ? 32.524 37.860  28.435  1.00 20.01 ? 373  GLN A OE1 1 
ATOM   2958 N  NE2 . GLN A 1 373  ? 34.204 39.236  27.830  1.00 18.81 ? 373  GLN A NE2 1 
ATOM   2959 N  N   . ALA A 1 374  ? 31.022 41.309  26.072  1.00 11.10 ? 374  ALA A N   1 
ATOM   2960 C  CA  . ALA A 1 374  ? 31.309 42.624  25.494  1.00 10.62 ? 374  ALA A CA  1 
ATOM   2961 C  C   . ALA A 1 374  ? 32.642 43.146  25.958  1.00 10.84 ? 374  ALA A C   1 
ATOM   2962 O  O   . ALA A 1 374  ? 32.998 42.977  27.148  1.00 11.73 ? 374  ALA A O   1 
ATOM   2963 C  CB  . ALA A 1 374  ? 30.233 43.563  25.889  1.00 11.10 ? 374  ALA A CB  1 
ATOM   2964 N  N   . GLN A 1 375  ? 33.367 43.859  25.090  1.00 11.03 ? 375  GLN A N   1 
ATOM   2965 C  CA  . GLN A 1 375  ? 34.685 44.406  25.461  1.00 11.00 ? 375  GLN A CA  1 
ATOM   2966 C  C   . GLN A 1 375  ? 35.070 45.503  24.483  1.00 10.83 ? 375  GLN A C   1 
ATOM   2967 O  O   . GLN A 1 375  ? 34.471 45.613  23.400  1.00 11.82 ? 375  GLN A O   1 
ATOM   2968 C  CB  . GLN A 1 375  ? 35.763 43.347  25.358  1.00 12.58 ? 375  GLN A CB  1 
ATOM   2969 C  CG  . GLN A 1 375  ? 35.776 42.566  24.052  1.00 16.99 ? 375  GLN A CG  1 
ATOM   2970 C  CD  . GLN A 1 375  ? 34.947 41.250  24.162  1.00 25.35 ? 375  GLN A CD  1 
ATOM   2971 O  OE1 . GLN A 1 375  ? 35.199 40.408  25.061  1.00 26.67 ? 375  GLN A OE1 1 
ATOM   2972 N  NE2 . GLN A 1 375  ? 33.940 41.067  23.265  1.00 22.50 ? 375  GLN A NE2 1 
ATOM   2973 N  N   . PHE A 1 376  ? 36.014 46.331  24.912  1.00 10.54 ? 376  PHE A N   1 
ATOM   2974 C  CA  . PHE A 1 376  ? 36.587 47.294  23.958  1.00 9.77  ? 376  PHE A CA  1 
ATOM   2975 C  C   . PHE A 1 376  ? 37.393 46.476  22.979  1.00 12.29 ? 376  PHE A C   1 
ATOM   2976 O  O   . PHE A 1 376  ? 38.071 45.500  23.330  1.00 12.57 ? 376  PHE A O   1 
ATOM   2977 C  CB  . PHE A 1 376  ? 37.543 48.248  24.677  1.00 10.76 ? 376  PHE A CB  1 
ATOM   2978 C  CG  . PHE A 1 376  ? 36.857 49.178  25.615  1.00 10.78 ? 376  PHE A CG  1 
ATOM   2979 C  CD1 . PHE A 1 376  ? 37.230 49.203  26.968  1.00 11.89 ? 376  PHE A CD1 1 
ATOM   2980 C  CD2 . PHE A 1 376  ? 35.834 50.015  25.175  1.00 11.06 ? 376  PHE A CD2 1 
ATOM   2981 C  CE1 . PHE A 1 376  ? 36.568 50.072  27.870  1.00 12.56 ? 376  PHE A CE1 1 
ATOM   2982 C  CE2 . PHE A 1 376  ? 35.180 50.891  26.138  1.00 13.76 ? 376  PHE A CE2 1 
ATOM   2983 C  CZ  . PHE A 1 376  ? 35.581 50.891  27.459  1.00 14.25 ? 376  PHE A CZ  1 
ATOM   2984 N  N   . GLY A 1 377  ? 37.371 46.930  21.729  1.00 10.60 ? 377  GLY A N   1 
ATOM   2985 C  CA  . GLY A 1 377  ? 38.162 46.242  20.709  1.00 11.16 ? 377  GLY A CA  1 
ATOM   2986 C  C   . GLY A 1 377  ? 38.583 47.223  19.628  1.00 10.52 ? 377  GLY A C   1 
ATOM   2987 O  O   . GLY A 1 377  ? 38.251 48.397  19.661  1.00 10.58 ? 377  GLY A O   1 
ATOM   2988 N  N   . THR A 1 378  ? 39.359 46.677  18.672  1.00 11.80 ? 378  THR A N   1 
ATOM   2989 C  CA  . THR A 1 378  ? 39.786 47.464  17.505  1.00 11.04 ? 378  THR A CA  1 
ATOM   2990 C  C   . THR A 1 378  ? 39.017 46.913  16.303  1.00 10.95 ? 378  THR A C   1 
ATOM   2991 O  O   . THR A 1 378  ? 38.307 45.873  16.329  1.00 11.18 ? 378  THR A O   1 
ATOM   2992 C  CB  . THR A 1 378  ? 41.289 47.367  17.241  1.00 12.14 ? 378  THR A CB  1 
ATOM   2993 O  OG1 . THR A 1 378  ? 41.589 46.007  16.896  1.00 12.85 ? 378  THR A OG1 1 
ATOM   2994 C  CG2 . THR A 1 378  ? 42.117 47.786  18.476  1.00 14.90 ? 378  THR A CG2 1 
ATOM   2995 N  N   . LEU A 1 379  ? 39.161 47.640  15.188  1.00 10.32 ? 379  LEU A N   1 
ATOM   2996 C  CA  . LEU A 1 379  ? 38.502 47.210  13.969  1.00 9.40  ? 379  LEU A CA  1 
ATOM   2997 C  C   . LEU A 1 379  ? 38.990 45.844  13.459  1.00 8.93  ? 379  LEU A C   1 
ATOM   2998 O  O   . LEU A 1 379  ? 38.193 44.993  13.032  1.00 9.93  ? 379  LEU A O   1 
ATOM   2999 C  CB  . LEU A 1 379  ? 38.651 48.323  12.895  1.00 9.86  ? 379  LEU A CB  1 
ATOM   3000 C  CG  . LEU A 1 379  ? 37.893 48.059  11.590  1.00 9.81  ? 379  LEU A CG  1 
ATOM   3001 C  CD1 . LEU A 1 379  ? 36.379 48.044  11.864  1.00 12.56 ? 379  LEU A CD1 1 
ATOM   3002 C  CD2 . LEU A 1 379  ? 38.331 49.147  10.553  1.00 11.51 ? 379  LEU A CD2 1 
ATOM   3003 N  N   . GLN A 1 380  ? 40.305 45.632  13.470  1.00 9.91  ? 380  GLN A N   1 
ATOM   3004 C  CA  . GLN A 1 380  ? 40.841 44.361  13.005  1.00 11.33 ? 380  GLN A CA  1 
ATOM   3005 C  C   . GLN A 1 380  ? 40.358 43.223  13.916  1.00 11.77 ? 380  GLN A C   1 
ATOM   3006 O  O   . GLN A 1 380  ? 40.117 42.118  13.422  1.00 10.31 ? 380  GLN A O   1 
ATOM   3007 C  CB  . GLN A 1 380  ? 42.381 44.400  12.950  1.00 12.85 ? 380  GLN A CB  1 
ATOM   3008 C  CG  . GLN A 1 380  ? 43.020 43.107  12.409  1.00 16.48 ? 380  GLN A CG  1 
ATOM   3009 C  CD  . GLN A 1 380  ? 42.684 42.940  10.975  1.00 18.64 ? 380  GLN A CD  1 
ATOM   3010 O  OE1 . GLN A 1 380  ? 42.805 43.909  10.209  1.00 19.72 ? 380  GLN A OE1 1 
ATOM   3011 N  NE2 . GLN A 1 380  ? 42.204 41.733  10.580  1.00 20.50 ? 380  GLN A NE2 1 
ATOM   3012 N  N   . GLU A 1 381  ? 40.226 43.464  15.218  1.00 10.97 ? 381  GLU A N   1 
ATOM   3013 C  CA  . GLU A 1 381  ? 39.705 42.392  16.085  1.00 10.67 ? 381  GLU A CA  1 
ATOM   3014 C  C   . GLU A 1 381  ? 38.276 42.009  15.668  1.00 9.54  ? 381  GLU A C   1 
ATOM   3015 O  O   . GLU A 1 381  ? 37.966 40.827  15.684  1.00 12.69 ? 381  GLU A O   1 
ATOM   3016 C  CB  . GLU A 1 381  ? 39.685 42.856  17.550  1.00 11.72 ? 381  GLU A CB  1 
ATOM   3017 C  CG  . GLU A 1 381  ? 41.026 42.913  18.328  1.00 16.19 ? 381  GLU A CG  1 
ATOM   3018 C  CD  . GLU A 1 381  ? 40.658 43.273  19.777  1.00 22.75 ? 381  GLU A CD  1 
ATOM   3019 O  OE1 . GLU A 1 381  ? 40.629 44.436  20.098  1.00 21.48 ? 381  GLU A OE1 1 
ATOM   3020 O  OE2 . GLU A 1 381  ? 40.338 42.358  20.617  1.00 29.44 ? 381  GLU A OE2 1 
ATOM   3021 N  N   . TYR A 1 382  ? 37.426 42.988  15.359  1.00 10.31 ? 382  TYR A N   1 
ATOM   3022 C  CA  . TYR A 1 382  ? 36.119 42.664  14.879  1.00 9.63  ? 382  TYR A CA  1 
ATOM   3023 C  C   . TYR A 1 382  ? 36.170 41.765  13.615  1.00 9.83  ? 382  TYR A C   1 
ATOM   3024 O  O   . TYR A 1 382  ? 35.517 40.714  13.539  1.00 9.79  ? 382  TYR A O   1 
ATOM   3025 C  CB  . TYR A 1 382  ? 35.337 43.964  14.528  1.00 10.72 ? 382  TYR A CB  1 
ATOM   3026 C  CG  . TYR A 1 382  ? 34.025 43.715  13.846  1.00 8.87  ? 382  TYR A CG  1 
ATOM   3027 C  CD1 . TYR A 1 382  ? 32.950 43.116  14.516  1.00 10.41 ? 382  TYR A CD1 1 
ATOM   3028 C  CD2 . TYR A 1 382  ? 33.884 43.973  12.466  1.00 9.65  ? 382  TYR A CD2 1 
ATOM   3029 C  CE1 . TYR A 1 382  ? 31.769 42.774  13.839  1.00 10.18 ? 382  TYR A CE1 1 
ATOM   3030 C  CE2 . TYR A 1 382  ? 32.713 43.650  11.794  1.00 10.64 ? 382  TYR A CE2 1 
ATOM   3031 C  CZ  . TYR A 1 382  ? 31.652 43.041  12.496  1.00 9.53  ? 382  TYR A CZ  1 
ATOM   3032 O  OH  . TYR A 1 382  ? 30.447 42.708  11.891  1.00 10.41 ? 382  TYR A OH  1 
ATOM   3033 N  N   . PHE A 1 383  ? 36.912 42.226  12.599  1.00 8.84  ? 383  PHE A N   1 
ATOM   3034 C  CA  . PHE A 1 383  ? 36.920 41.471  11.342  1.00 7.98  ? 383  PHE A CA  1 
ATOM   3035 C  C   . PHE A 1 383  ? 37.566 40.074  11.580  1.00 9.49  ? 383  PHE A C   1 
ATOM   3036 O  O   . PHE A 1 383  ? 37.079 39.101  10.970  1.00 10.23 ? 383  PHE A O   1 
ATOM   3037 C  CB  . PHE A 1 383  ? 37.704 42.226  10.252  1.00 9.50  ? 383  PHE A CB  1 
ATOM   3038 C  CG  . PHE A 1 383  ? 36.950 43.385  9.632   1.00 9.15  ? 383  PHE A CG  1 
ATOM   3039 C  CD1 . PHE A 1 383  ? 37.464 44.672  9.703   1.00 9.39  ? 383  PHE A CD1 1 
ATOM   3040 C  CD2 . PHE A 1 383  ? 35.731 43.177  8.987   1.00 10.45 ? 383  PHE A CD2 1 
ATOM   3041 C  CE1 . PHE A 1 383  ? 36.749 45.743  9.118   1.00 10.12 ? 383  PHE A CE1 1 
ATOM   3042 C  CE2 . PHE A 1 383  ? 35.018 44.258  8.397   1.00 10.79 ? 383  PHE A CE2 1 
ATOM   3043 C  CZ  . PHE A 1 383  ? 35.551 45.550  8.475   1.00 10.24 ? 383  PHE A CZ  1 
ATOM   3044 N  N   . ASP A 1 384  ? 38.615 39.973  12.404  1.00 10.17 ? 384  ASP A N   1 
ATOM   3045 C  CA  . ASP A 1 384  ? 39.171 38.637  12.609  1.00 11.47 ? 384  ASP A CA  1 
ATOM   3046 C  C   . ASP A 1 384  ? 38.110 37.710  13.229  1.00 10.98 ? 384  ASP A C   1 
ATOM   3047 O  O   . ASP A 1 384  ? 37.990 36.533  12.818  1.00 12.26 ? 384  ASP A O   1 
ATOM   3048 C  CB  . ASP A 1 384  ? 40.370 38.712  13.566  1.00 13.76 ? 384  ASP A CB  1 
ATOM   3049 C  CG  . ASP A 1 384  ? 41.575 39.331  12.968  1.00 16.87 ? 384  ASP A CG  1 
ATOM   3050 O  OD1 . ASP A 1 384  ? 41.681 39.473  11.744  1.00 18.24 ? 384  ASP A OD1 1 
ATOM   3051 O  OD2 . ASP A 1 384  ? 42.451 39.674  13.805  1.00 22.69 ? 384  ASP A OD2 1 
ATOM   3052 N  N   . ALA A 1 385  ? 37.327 38.198  14.179  1.00 10.50 ? 385  ALA A N   1 
ATOM   3053 C  CA  . ALA A 1 385  ? 36.300 37.353  14.785  1.00 11.64 ? 385  ALA A CA  1 
ATOM   3054 C  C   . ALA A 1 385  ? 35.185 37.019  13.784  1.00 12.99 ? 385  ALA A C   1 
ATOM   3055 O  O   . ALA A 1 385  ? 34.687 35.870  13.763  1.00 12.59 ? 385  ALA A O   1 
ATOM   3056 C  CB  . ALA A 1 385  ? 35.714 38.081  15.998  1.00 11.89 ? 385  ALA A CB  1 
ATOM   3057 N  N   . VAL A 1 386  ? 34.781 37.977  12.919  1.00 11.22 ? 386  VAL A N   1 
ATOM   3058 C  CA  . VAL A 1 386  ? 33.770 37.656  11.915  1.00 11.73 ? 386  VAL A CA  1 
ATOM   3059 C  C   . VAL A 1 386  ? 34.253 36.528  11.004  1.00 12.61 ? 386  VAL A C   1 
ATOM   3060 O  O   . VAL A 1 386  ? 33.478 35.566  10.705  1.00 13.17 ? 386  VAL A O   1 
ATOM   3061 C  CB  . VAL A 1 386  ? 33.462 38.930  11.049  1.00 10.00 ? 386  VAL A CB  1 
ATOM   3062 C  CG1 . VAL A 1 386  ? 32.678 38.594  9.799   1.00 13.85 ? 386  VAL A CG1 1 
ATOM   3063 C  CG2 . VAL A 1 386  ? 32.725 39.939  11.899  1.00 12.78 ? 386  VAL A CG2 1 
ATOM   3064 N  N   . HIS A 1 387  ? 35.488 36.602  10.543  1.00 11.74 ? 387  HIS A N   1 
ATOM   3065 C  CA  . HIS A 1 387  ? 35.978 35.555  9.644   1.00 12.36 ? 387  HIS A CA  1 
ATOM   3066 C  C   . HIS A 1 387  ? 36.200 34.228  10.376  1.00 14.41 ? 387  HIS A C   1 
ATOM   3067 O  O   . HIS A 1 387  ? 36.124 33.172  9.699   1.00 12.83 ? 387  HIS A O   1 
ATOM   3068 C  CB  . HIS A 1 387  ? 37.218 35.996  8.874   1.00 11.77 ? 387  HIS A CB  1 
ATOM   3069 C  CG  . HIS A 1 387  ? 36.927 37.132  7.939   1.00 12.19 ? 387  HIS A CG  1 
ATOM   3070 N  ND1 . HIS A 1 387  ? 36.017 37.031  6.910   1.00 15.91 ? 387  HIS A ND1 1 
ATOM   3071 C  CD2 . HIS A 1 387  ? 37.380 38.412  7.938   1.00 11.56 ? 387  HIS A CD2 1 
ATOM   3072 C  CE1 . HIS A 1 387  ? 35.932 38.210  6.294   1.00 14.47 ? 387  HIS A CE1 1 
ATOM   3073 N  NE2 . HIS A 1 387  ? 36.752 39.062  6.900   1.00 13.67 ? 387  HIS A NE2 1 
ATOM   3074 N  N   . GLN A 1 388  ? 36.491 34.253  11.683  1.00 13.35 ? 388  GLN A N   1 
ATOM   3075 C  CA  . GLN A 1 388  ? 36.593 32.974  12.447  1.00 13.37 ? 388  GLN A CA  1 
ATOM   3076 C  C   . GLN A 1 388  ? 35.189 32.356  12.418  1.00 15.06 ? 388  GLN A C   1 
ATOM   3077 O  O   . GLN A 1 388  ? 35.030 31.134  12.221  1.00 16.27 ? 388  GLN A O   1 
ATOM   3078 C  CB  . GLN A 1 388  ? 37.054 33.287  13.841  1.00 14.78 ? 388  GLN A CB  1 
ATOM   3079 C  CG  . GLN A 1 388  ? 38.571 33.549  13.839  1.00 21.76 ? 388  GLN A CG  1 
ATOM   3080 C  CD  . GLN A 1 388  ? 39.118 34.304  15.088  1.00 29.32 ? 388  GLN A CD  1 
ATOM   3081 O  OE1 . GLN A 1 388  ? 40.319 34.651  15.155  1.00 33.46 ? 388  GLN A OE1 1 
ATOM   3082 N  NE2 . GLN A 1 388  ? 38.253 34.559  16.066  1.00 31.74 ? 388  GLN A NE2 1 
ATOM   3083 N  N   . ALA A 1 389  ? 34.138 33.141  12.586  1.00 14.51 ? 389  ALA A N   1 
ATOM   3084 C  CA  . ALA A 1 389  ? 32.753 32.627  12.557  1.00 17.60 ? 389  ALA A CA  1 
ATOM   3085 C  C   . ALA A 1 389  ? 32.435 32.062  11.173  1.00 19.74 ? 389  ALA A C   1 
ATOM   3086 O  O   . ALA A 1 389  ? 31.857 30.969  11.053  1.00 20.57 ? 389  ALA A O   1 
ATOM   3087 C  CB  . ALA A 1 389  ? 31.776 33.712  12.930  1.00 15.66 ? 389  ALA A CB  1 
ATOM   3088 N  N   . GLU A 1 390  ? 32.824 32.786  10.111  1.00 17.29 ? 390  GLU A N   1 
ATOM   3089 C  CA  . GLU A 1 390  ? 32.626 32.339  8.720   1.00 18.72 ? 390  GLU A CA  1 
ATOM   3090 C  C   . GLU A 1 390  ? 33.297 30.976  8.501   1.00 19.76 ? 390  GLU A C   1 
ATOM   3091 O  O   . GLU A 1 390  ? 32.679 30.066  7.928   1.00 22.43 ? 390  GLU A O   1 
ATOM   3092 C  CB  . GLU A 1 390  ? 33.240 33.393  7.768   1.00 17.29 ? 390  GLU A CB  1 
ATOM   3093 C  CG  . GLU A 1 390  ? 33.125 33.075  6.269   1.00 19.69 ? 390  GLU A CG  1 
ATOM   3094 C  CD  . GLU A 1 390  ? 33.841 34.119  5.437   1.00 23.53 ? 390  GLU A CD  1 
ATOM   3095 O  OE1 . GLU A 1 390  ? 34.684 34.844  6.027   1.00 23.05 ? 390  GLU A OE1 1 
ATOM   3096 O  OE2 . GLU A 1 390  ? 33.572 34.223  4.222   1.00 24.77 ? 390  GLU A OE2 1 
ATOM   3097 N  N   . ARG A 1 391  ? 34.546 30.827  8.948   1.00 19.70 ? 391  ARG A N   1 
ATOM   3098 C  CA  . ARG A 1 391  ? 35.289 29.576  8.763   1.00 22.16 ? 391  ARG A CA  1 
ATOM   3099 C  C   . ARG A 1 391  ? 34.646 28.463  9.600   1.00 22.42 ? 391  ARG A C   1 
ATOM   3100 O  O   . ARG A 1 391  ? 34.720 27.270  9.207   1.00 28.91 ? 391  ARG A O   1 
ATOM   3101 C  CB  . ARG A 1 391  ? 36.772 29.766  9.136   1.00 21.87 ? 391  ARG A CB  1 
ATOM   3102 C  CG  . ARG A 1 391  ? 37.548 30.600  8.127   1.00 28.17 ? 391  ARG A CG  1 
ATOM   3103 C  CD  . ARG A 1 391  ? 39.040 30.505  8.361   1.00 29.66 ? 391  ARG A CD  1 
ATOM   3104 N  NE  . ARG A 1 391  ? 39.494 31.032  9.652   1.00 35.31 ? 391  ARG A NE  1 
ATOM   3105 C  CZ  . ARG A 1 391  ? 39.700 32.332  9.905   1.00 31.48 ? 391  ARG A CZ  1 
ATOM   3106 N  NH1 . ARG A 1 391  ? 39.489 33.247  8.966   1.00 33.79 ? 391  ARG A NH1 1 
ATOM   3107 N  NH2 . ARG A 1 391  ? 40.143 32.695  11.083  1.00 34.68 ? 391  ARG A NH2 1 
ATOM   3108 N  N   . ALA A 1 392  ? 33.989 28.799  10.695  1.00 23.41 ? 392  ALA A N   1 
ATOM   3109 C  CA  . ALA A 1 392  ? 33.347 27.752  11.512  1.00 25.52 ? 392  ALA A CA  1 
ATOM   3110 C  C   . ALA A 1 392  ? 32.021 27.348  10.833  1.00 27.70 ? 392  ALA A C   1 
ATOM   3111 O  O   . ALA A 1 392  ? 31.266 26.522  11.378  1.00 28.73 ? 392  ALA A O   1 
ATOM   3112 C  CB  . ALA A 1 392  ? 33.084 28.242  12.912  1.00 24.41 ? 392  ALA A CB  1 
ATOM   3113 N  N   . GLY A 1 393  ? 31.728 27.936  9.662   1.00 25.01 ? 393  GLY A N   1 
ATOM   3114 C  CA  . GLY A 1 393  ? 30.511 27.575  8.958   1.00 25.09 ? 393  GLY A CA  1 
ATOM   3115 C  C   . GLY A 1 393  ? 29.286 28.247  9.497   1.00 21.46 ? 393  GLY A C   1 
ATOM   3116 O  O   . GLY A 1 393  ? 28.153 27.869  9.186   1.00 24.25 ? 393  GLY A O   1 
ATOM   3117 N  N   . GLN A 1 394  ? 29.455 29.306  10.280  1.00 22.10 ? 394  GLN A N   1 
ATOM   3118 C  CA  . GLN A 1 394  ? 28.260 29.916  10.778  1.00 24.72 ? 394  GLN A CA  1 
ATOM   3119 C  C   . GLN A 1 394  ? 27.605 30.963  9.902   1.00 21.51 ? 394  GLN A C   1 
ATOM   3120 O  O   . GLN A 1 394  ? 26.456 31.320  10.149  1.00 27.43 ? 394  GLN A O   1 
ATOM   3121 C  CB  . GLN A 1 394  ? 28.455 30.373  12.242  1.00 29.68 ? 394  GLN A CB  1 
ATOM   3122 C  CG  . GLN A 1 394  ? 29.236 31.577  12.492  1.00 32.97 ? 394  GLN A CG  1 
ATOM   3123 C  CD  . GLN A 1 394  ? 28.896 32.180  13.867  1.00 33.27 ? 394  GLN A CD  1 
ATOM   3124 O  OE1 . GLN A 1 394  ? 29.321 31.675  14.936  1.00 30.04 ? 394  GLN A OE1 1 
ATOM   3125 N  NE2 . GLN A 1 394  ? 28.131 33.263  13.842  1.00 19.52 ? 394  GLN A NE2 1 
ATOM   3126 N  N   . ALA A 1 395  ? 28.273 31.402  8.826   1.00 19.06 ? 395  ALA A N   1 
ATOM   3127 C  CA  . ALA A 1 395  ? 27.699 32.370  7.911   1.00 19.51 ? 395  ALA A CA  1 
ATOM   3128 C  C   . ALA A 1 395  ? 28.377 32.285  6.528   1.00 18.49 ? 395  ALA A C   1 
ATOM   3129 O  O   . ALA A 1 395  ? 29.521 31.835  6.421   1.00 18.67 ? 395  ALA A O   1 
ATOM   3130 C  CB  . ALA A 1 395  ? 27.880 33.805  8.524   1.00 23.05 ? 395  ALA A CB  1 
ATOM   3131 N  N   . GLU A 1 396  ? 27.674 32.680  5.475   1.00 20.73 ? 396  GLU A N   1 
ATOM   3132 C  CA  . GLU A 1 396  ? 28.282 32.760  4.149   1.00 19.43 ? 396  GLU A CA  1 
ATOM   3133 C  C   . GLU A 1 396  ? 27.848 34.174  3.748   1.00 17.46 ? 396  GLU A C   1 
ATOM   3134 O  O   . GLU A 1 396  ? 26.730 34.626  4.164   1.00 19.82 ? 396  GLU A O   1 
ATOM   3135 C  CB  . GLU A 1 396  ? 27.689 31.717  3.196   1.00 26.13 ? 396  GLU A CB  1 
ATOM   3136 C  CG  . GLU A 1 396  ? 26.200 31.794  3.083   1.00 36.01 ? 396  GLU A CG  1 
ATOM   3137 C  CD  . GLU A 1 396  ? 25.609 30.497  2.544   1.00 41.87 ? 396  GLU A CD  1 
ATOM   3138 O  OE1 . GLU A 1 396  ? 26.161 29.952  1.557   1.00 44.57 ? 396  GLU A OE1 1 
ATOM   3139 O  OE2 . GLU A 1 396  ? 24.593 30.025  3.111   1.00 47.30 ? 396  GLU A OE2 1 
ATOM   3140 N  N   . PHE A 1 397  ? 28.701 34.855  2.982   1.00 14.46 ? 397  PHE A N   1 
ATOM   3141 C  CA  . PHE A 1 397  ? 28.395 36.217  2.634   1.00 12.06 ? 397  PHE A CA  1 
ATOM   3142 C  C   . PHE A 1 397  ? 28.072 36.393  1.162   1.00 11.57 ? 397  PHE A C   1 
ATOM   3143 O  O   . PHE A 1 397  ? 28.640 35.710  0.312   1.00 14.35 ? 397  PHE A O   1 
ATOM   3144 C  CB  . PHE A 1 397  ? 29.598 37.110  3.026   1.00 13.34 ? 397  PHE A CB  1 
ATOM   3145 C  CG  . PHE A 1 397  ? 29.875 37.142  4.528   1.00 11.59 ? 397  PHE A CG  1 
ATOM   3146 C  CD1 . PHE A 1 397  ? 30.964 36.469  5.053   1.00 13.65 ? 397  PHE A CD1 1 
ATOM   3147 C  CD2 . PHE A 1 397  ? 29.017 37.829  5.372   1.00 11.67 ? 397  PHE A CD2 1 
ATOM   3148 C  CE1 . PHE A 1 397  ? 31.186 36.471  6.465   1.00 14.95 ? 397  PHE A CE1 1 
ATOM   3149 C  CE2 . PHE A 1 397  ? 29.233 37.841  6.736   1.00 13.08 ? 397  PHE A CE2 1 
ATOM   3150 C  CZ  . PHE A 1 397  ? 30.321 37.153  7.263   1.00 12.82 ? 397  PHE A CZ  1 
ATOM   3151 N  N   . PRO A 1 398  ? 27.170 37.303  0.888   1.00 10.15 ? 398  PRO A N   1 
ATOM   3152 C  CA  . PRO A 1 398  ? 26.781 37.601  -0.499  1.00 11.18 ? 398  PRO A CA  1 
ATOM   3153 C  C   . PRO A 1 398  ? 27.860 38.368  -1.263  1.00 10.12 ? 398  PRO A C   1 
ATOM   3154 O  O   . PRO A 1 398  ? 28.726 39.040  -0.654  1.00 10.89 ? 398  PRO A O   1 
ATOM   3155 C  CB  . PRO A 1 398  ? 25.521 38.422  -0.324  1.00 13.34 ? 398  PRO A CB  1 
ATOM   3156 C  CG  . PRO A 1 398  ? 25.806 39.209  0.971   1.00 12.25 ? 398  PRO A CG  1 
ATOM   3157 C  CD  . PRO A 1 398  ? 26.448 38.145  1.839   1.00 12.11 ? 398  PRO A CD  1 
ATOM   3158 N  N   . THR A 1 399  ? 27.835 38.250  -2.548  1.00 10.04 ? 399  THR A N   1 
ATOM   3159 C  CA  . THR A 1 399  ? 28.759 38.960  -3.459  1.00 9.26  ? 399  THR A CA  1 
ATOM   3160 C  C   . THR A 1 399  ? 27.976 40.191  -3.967  1.00 9.82  ? 399  THR A C   1 
ATOM   3161 O  O   . THR A 1 399  ? 26.768 40.181  -4.130  1.00 10.23 ? 399  THR A O   1 
ATOM   3162 C  CB  . THR A 1 399  ? 29.168 38.071  -4.630  1.00 11.19 ? 399  THR A CB  1 
ATOM   3163 O  OG1 . THR A 1 399  ? 27.976 37.645  -5.307  1.00 12.27 ? 399  THR A OG1 1 
ATOM   3164 C  CG2 . THR A 1 399  ? 29.948 36.851  -4.108  1.00 11.81 ? 399  THR A CG2 1 
ATOM   3165 N  N   . LEU A 1 400  ? 28.710 41.293  -4.219  1.00 8.82  ? 400  LEU A N   1 
ATOM   3166 C  CA  . LEU A 1 400  ? 28.092 42.529  -4.656  1.00 7.48  ? 400  LEU A CA  1 
ATOM   3167 C  C   . LEU A 1 400  ? 29.004 43.240  -5.627  1.00 8.51  ? 400  LEU A C   1 
ATOM   3168 O  O   . LEU A 1 400  ? 30.249 43.208  -5.492  1.00 8.84  ? 400  LEU A O   1 
ATOM   3169 C  CB  . LEU A 1 400  ? 27.858 43.430  -3.433  1.00 8.91  ? 400  LEU A CB  1 
ATOM   3170 C  CG  . LEU A 1 400  ? 27.179 44.808  -3.660  1.00 8.28  ? 400  LEU A CG  1 
ATOM   3171 C  CD1 . LEU A 1 400  ? 26.343 45.215  -2.409  1.00 11.52 ? 400  LEU A CD1 1 
ATOM   3172 C  CD2 . LEU A 1 400  ? 28.213 45.878  -3.971  1.00 8.56  ? 400  LEU A CD2 1 
ATOM   3173 N  N   . SER A 1 401  ? 28.402 43.885  -6.640  1.00 8.21  ? 401  SER A N   1 
ATOM   3174 C  CA  . SER A 1 401  ? 29.189 44.821  -7.473  1.00 8.59  ? 401  SER A CA  1 
ATOM   3175 C  C   . SER A 1 401  ? 28.326 46.067  -7.675  1.00 7.68  ? 401  SER A C   1 
ATOM   3176 O  O   . SER A 1 401  ? 27.085 46.038  -7.478  1.00 7.97  ? 401  SER A O   1 
ATOM   3177 C  CB  . SER A 1 401  ? 29.595 44.235  -8.817  1.00 8.81  ? 401  SER A CB  1 
ATOM   3178 O  OG  . SER A 1 401  ? 28.468 44.217  -9.715  1.00 8.83  ? 401  SER A OG  1 
ATOM   3179 N  N   . GLY A 1 402  ? 28.994 47.163  -8.016  1.00 8.08  ? 402  GLY A N   1 
ATOM   3180 C  CA  . GLY A 1 402  ? 28.347 48.448  -8.210  1.00 8.60  ? 402  GLY A CA  1 
ATOM   3181 C  C   . GLY A 1 402  ? 28.948 49.524  -7.354  1.00 7.69  ? 402  GLY A C   1 
ATOM   3182 O  O   . GLY A 1 402  ? 30.027 49.342  -6.746  1.00 9.73  ? 402  GLY A O   1 
ATOM   3183 N  N   . ASP A 1 403  ? 28.319 50.679  -7.311  1.00 7.51  ? 403  ASP A N   1 
ATOM   3184 C  CA  . ASP A 1 403  ? 28.797 51.810  -6.461  1.00 7.89  ? 403  ASP A CA  1 
ATOM   3185 C  C   . ASP A 1 403  ? 27.655 52.259  -5.554  1.00 8.96  ? 403  ASP A C   1 
ATOM   3186 O  O   . ASP A 1 403  ? 26.535 51.689  -5.567  1.00 9.55  ? 403  ASP A O   1 
ATOM   3187 C  CB  . ASP A 1 403  ? 29.305 52.988  -7.312  1.00 8.17  ? 403  ASP A CB  1 
ATOM   3188 C  CG  . ASP A 1 403  ? 28.219 53.715  -8.054  1.00 11.29 ? 403  ASP A CG  1 
ATOM   3189 O  OD1 . ASP A 1 403  ? 27.061 53.256  -8.142  1.00 13.31 ? 403  ASP A OD1 1 
ATOM   3190 O  OD2 . ASP A 1 403  ? 28.569 54.778  -8.566  1.00 13.39 ? 403  ASP A OD2 1 
ATOM   3191 N  N   . PHE A 1 404  ? 27.968 53.259  -4.746  1.00 7.34  ? 404  PHE A N   1 
ATOM   3192 C  CA  . PHE A 1 404  ? 27.036 53.842  -3.790  1.00 7.52  ? 404  PHE A CA  1 
ATOM   3193 C  C   . PHE A 1 404  ? 26.890 55.349  -3.958  1.00 6.81  ? 404  PHE A C   1 
ATOM   3194 O  O   . PHE A 1 404  ? 27.017 56.110  -3.013  1.00 8.05  ? 404  PHE A O   1 
ATOM   3195 C  CB  . PHE A 1 404  ? 27.398 53.450  -2.343  1.00 8.08  ? 404  PHE A CB  1 
ATOM   3196 C  CG  . PHE A 1 404  ? 27.348 51.935  -2.121  1.00 7.29  ? 404  PHE A CG  1 
ATOM   3197 C  CD1 . PHE A 1 404  ? 28.517 51.175  -2.101  1.00 8.13  ? 404  PHE A CD1 1 
ATOM   3198 C  CD2 . PHE A 1 404  ? 26.093 51.296  -2.019  1.00 8.66  ? 404  PHE A CD2 1 
ATOM   3199 C  CE1 . PHE A 1 404  ? 28.439 49.783  -1.975  1.00 9.14  ? 404  PHE A CE1 1 
ATOM   3200 C  CE2 . PHE A 1 404  ? 26.041 49.872  -1.901  1.00 8.92  ? 404  PHE A CE2 1 
ATOM   3201 C  CZ  . PHE A 1 404  ? 27.184 49.142  -1.873  1.00 9.03  ? 404  PHE A CZ  1 
ATOM   3202 N  N   . PHE A 1 405  ? 26.662 55.728  -5.221  1.00 8.72  ? 405  PHE A N   1 
ATOM   3203 C  CA  . PHE A 1 405  ? 26.293 57.127  -5.541  1.00 7.20  ? 405  PHE A CA  1 
ATOM   3204 C  C   . PHE A 1 405  ? 24.932 57.097  -6.214  1.00 8.88  ? 405  PHE A C   1 
ATOM   3205 O  O   . PHE A 1 405  ? 24.610 56.129  -6.897  1.00 10.56 ? 405  PHE A O   1 
ATOM   3206 C  CB  . PHE A 1 405  ? 27.302 57.770  -6.524  1.00 8.76  ? 405  PHE A CB  1 
ATOM   3207 C  CG  . PHE A 1 405  ? 28.721 57.872  -5.967  1.00 8.18  ? 405  PHE A CG  1 
ATOM   3208 C  CD1 . PHE A 1 405  ? 29.759 57.161  -6.572  1.00 8.33  ? 405  PHE A CD1 1 
ATOM   3209 C  CD2 . PHE A 1 405  ? 28.982 58.652  -4.857  1.00 8.88  ? 405  PHE A CD2 1 
ATOM   3210 C  CE1 . PHE A 1 405  ? 31.093 57.256  -6.008  1.00 8.82  ? 405  PHE A CE1 1 
ATOM   3211 C  CE2 . PHE A 1 405  ? 30.295 58.735  -4.323  1.00 7.97  ? 405  PHE A CE2 1 
ATOM   3212 C  CZ  . PHE A 1 405  ? 31.319 58.050  -4.879  1.00 8.33  ? 405  PHE A CZ  1 
ATOM   3213 N  N   . THR A 1 406  ? 24.122 58.135  -6.101  1.00 9.16  ? 406  THR A N   1 
ATOM   3214 C  CA  . THR A 1 406  ? 24.351 59.360  -5.339  1.00 8.19  ? 406  THR A CA  1 
ATOM   3215 C  C   . THR A 1 406  ? 23.702 59.236  -3.983  1.00 9.13  ? 406  THR A C   1 
ATOM   3216 O  O   . THR A 1 406  ? 22.534 58.817  -3.823  1.00 9.94  ? 406  THR A O   1 
ATOM   3217 C  CB  . THR A 1 406  ? 23.820 60.579  -6.128  1.00 8.31  ? 406  THR A CB  1 
ATOM   3218 O  OG1 . THR A 1 406  ? 24.754 60.786  -7.178  1.00 9.71  ? 406  THR A OG1 1 
ATOM   3219 C  CG2 . THR A 1 406  ? 23.691 61.838  -5.286  1.00 9.60  ? 406  THR A CG2 1 
ATOM   3220 N  N   . TYR A 1 407  ? 24.454 59.579  -2.955  1.00 8.19  ? 407  TYR A N   1 
ATOM   3221 C  CA  . TYR A 1 407  ? 24.019 59.478  -1.593  1.00 8.54  ? 407  TYR A CA  1 
ATOM   3222 C  C   . TYR A 1 407  ? 22.913 60.462  -1.229  1.00 9.00  ? 407  TYR A C   1 
ATOM   3223 O  O   . TYR A 1 407  ? 22.952 61.612  -1.676  1.00 9.35  ? 407  TYR A O   1 
ATOM   3224 C  CB  . TYR A 1 407  ? 25.247 59.788  -0.697  1.00 9.23  ? 407  TYR A CB  1 
ATOM   3225 C  CG  . TYR A 1 407  ? 25.027 59.921  0.783   1.00 7.95  ? 407  TYR A CG  1 
ATOM   3226 C  CD1 . TYR A 1 407  ? 24.545 58.853  1.560   1.00 9.72  ? 407  TYR A CD1 1 
ATOM   3227 C  CD2 . TYR A 1 407  ? 25.330 61.098  1.424   1.00 8.58  ? 407  TYR A CD2 1 
ATOM   3228 C  CE1 . TYR A 1 407  ? 24.382 58.971  2.949   1.00 8.81  ? 407  TYR A CE1 1 
ATOM   3229 C  CE2 . TYR A 1 407  ? 25.186 61.233  2.813   1.00 10.00 ? 407  TYR A CE2 1 
ATOM   3230 C  CZ  . TYR A 1 407  ? 24.723 60.145  3.562   1.00 9.15  ? 407  TYR A CZ  1 
ATOM   3231 O  OH  . TYR A 1 407  ? 24.729 60.275  4.935   1.00 10.01 ? 407  TYR A OH  1 
ATOM   3232 N  N   . ALA A 1 408  ? 21.967 60.001  -0.411  1.00 10.27 ? 408  ALA A N   1 
ATOM   3233 C  CA  . ALA A 1 408  ? 20.971 60.892  0.251   1.00 10.22 ? 408  ALA A CA  1 
ATOM   3234 C  C   . ALA A 1 408  ? 20.928 60.417  1.693   1.00 10.14 ? 408  ALA A C   1 
ATOM   3235 O  O   . ALA A 1 408  ? 20.836 59.184  1.957   1.00 10.64 ? 408  ALA A O   1 
ATOM   3236 C  CB  . ALA A 1 408  ? 19.543 60.807  -0.389  1.00 10.93 ? 408  ALA A CB  1 
ATOM   3237 N  N   . ASP A 1 409  ? 21.047 61.355  2.633   1.00 9.98  ? 409  ASP A N   1 
ATOM   3238 C  CA  . ASP A 1 409  ? 20.972 60.975  4.057   1.00 10.81 ? 409  ASP A CA  1 
ATOM   3239 C  C   . ASP A 1 409  ? 19.531 61.045  4.596   1.00 11.17 ? 409  ASP A C   1 
ATOM   3240 O  O   . ASP A 1 409  ? 19.263 60.425  5.643   1.00 12.72 ? 409  ASP A O   1 
ATOM   3241 C  CB  . ASP A 1 409  ? 21.872 61.856  4.949   1.00 10.23 ? 409  ASP A CB  1 
ATOM   3242 C  CG  . ASP A 1 409  ? 21.613 63.366  4.839   1.00 9.05  ? 409  ASP A CG  1 
ATOM   3243 O  OD1 . ASP A 1 409  ? 21.002 63.856  3.865   1.00 10.47 ? 409  ASP A OD1 1 
ATOM   3244 O  OD2 . ASP A 1 409  ? 22.129 64.070  5.752   1.00 11.38 ? 409  ASP A OD2 1 
ATOM   3245 N  N   . ARG A 1 410  ? 18.625 61.748  3.893   1.00 10.07 ? 410  ARG A N   1 
ATOM   3246 C  CA  . ARG A 1 410  ? 17.203 61.843  4.345   1.00 10.75 ? 410  ARG A CA  1 
ATOM   3247 C  C   . ARG A 1 410  ? 16.420 62.496  3.216   1.00 12.22 ? 410  ARG A C   1 
ATOM   3248 O  O   . ARG A 1 410  ? 16.987 63.219  2.342   1.00 12.85 ? 410  ARG A O   1 
ATOM   3249 C  CB  . ARG A 1 410  ? 17.038 62.646  5.636   1.00 12.28 ? 410  ARG A CB  1 
ATOM   3250 C  CG  . ARG A 1 410  ? 17.509 64.116  5.550   1.00 13.88 ? 410  ARG A CG  1 
ATOM   3251 C  CD  . ARG A 1 410  ? 17.490 64.705  6.959   1.00 18.88 ? 410  ARG A CD  1 
ATOM   3252 N  NE  . ARG A 1 410  ? 18.118 66.030  7.085   1.00 17.44 ? 410  ARG A NE  1 
ATOM   3253 C  CZ  . ARG A 1 410  ? 17.535 67.187  6.810   1.00 21.91 ? 410  ARG A CZ  1 
ATOM   3254 N  NH1 . ARG A 1 410  ? 16.270 67.211  6.378   1.00 24.17 ? 410  ARG A NH1 1 
ATOM   3255 N  NH2 . ARG A 1 410  ? 18.230 68.313  6.970   1.00 18.82 ? 410  ARG A NH2 1 
ATOM   3256 N  N   A SER A 1 411  ? 15.124 62.154  3.175   0.50 11.72 ? 411  SER A N   1 
ATOM   3257 N  N   B SER A 1 411  ? 15.124 62.154  3.175   0.50 13.51 ? 411  SER A N   1 
ATOM   3258 C  CA  A SER A 1 411  ? 14.147 62.674  2.193   0.50 11.57 ? 411  SER A CA  1 
ATOM   3259 C  CA  B SER A 1 411  ? 14.147 62.674  2.193   0.50 14.70 ? 411  SER A CA  1 
ATOM   3260 C  C   A SER A 1 411  ? 14.696 62.771  0.790   0.50 11.19 ? 411  SER A C   1 
ATOM   3261 C  C   B SER A 1 411  ? 14.653 62.653  0.771   0.50 14.33 ? 411  SER A C   1 
ATOM   3262 O  O   A SER A 1 411  ? 15.166 61.778  0.238   0.50 10.83 ? 411  SER A O   1 
ATOM   3263 O  O   B SER A 1 411  ? 15.044 61.602  0.267   0.50 18.12 ? 411  SER A O   1 
ATOM   3264 C  CB  A SER A 1 411  ? 13.496 63.978  2.691   0.50 16.46 ? 411  SER A CB  1 
ATOM   3265 C  CB  B SER A 1 411  ? 13.592 64.043  2.630   0.50 18.95 ? 411  SER A CB  1 
ATOM   3266 O  OG  A SER A 1 411  ? 14.419 64.980  2.970   0.50 16.74 ? 411  SER A OG  1 
ATOM   3267 O  OG  B SER A 1 411  ? 12.605 64.531  1.780   0.50 21.50 ? 411  SER A OG  1 
ATOM   3268 N  N   . ASP A 1 412  ? 14.616 63.962  0.183   1.00 11.55 ? 412  ASP A N   1 
ATOM   3269 C  CA  . ASP A 1 412  ? 15.113 64.173  -1.188  1.00 11.48 ? 412  ASP A CA  1 
ATOM   3270 C  C   . ASP A 1 412  ? 16.460 64.946  -1.158  1.00 10.05 ? 412  ASP A C   1 
ATOM   3271 O  O   . ASP A 1 412  ? 16.826 65.535  -2.184  1.00 11.59 ? 412  ASP A O   1 
ATOM   3272 C  CB  . ASP A 1 412  ? 14.080 65.016  -1.985  1.00 12.91 ? 412  ASP A CB  1 
ATOM   3273 C  CG  . ASP A 1 412  ? 13.931 66.440  -1.447  1.00 12.92 ? 412  ASP A CG  1 
ATOM   3274 O  OD1 . ASP A 1 412  ? 14.399 66.779  -0.363  1.00 13.39 ? 412  ASP A OD1 1 
ATOM   3275 O  OD2 . ASP A 1 412  ? 13.277 67.271  -2.155  1.00 15.48 ? 412  ASP A OD2 1 
ATOM   3276 N  N   . ASN A 1 413  ? 17.153 64.903  -0.018  1.00 10.43 ? 413  ASN A N   1 
ATOM   3277 C  CA  . ASN A 1 413  ? 18.407 65.662  0.139   1.00 10.95 ? 413  ASN A CA  1 
ATOM   3278 C  C   . ASN A 1 413  ? 19.597 64.801  -0.425  1.00 10.68 ? 413  ASN A C   1 
ATOM   3279 O  O   . ASN A 1 413  ? 20.283 64.095  0.350   1.00 10.38 ? 413  ASN A O   1 
ATOM   3280 C  CB  . ASN A 1 413  ? 18.670 65.975  1.603   1.00 11.11 ? 413  ASN A CB  1 
ATOM   3281 C  CG  . ASN A 1 413  ? 17.738 67.062  2.215   1.00 11.56 ? 413  ASN A CG  1 
ATOM   3282 O  OD1 . ASN A 1 413  ? 18.006 67.534  3.285   1.00 14.06 ? 413  ASN A OD1 1 
ATOM   3283 N  ND2 . ASN A 1 413  ? 16.657 67.414  1.525   1.00 11.48 ? 413  ASN A ND2 1 
ATOM   3284 N  N   . TYR A 1 414  ? 19.760 64.858  -1.729  1.00 9.78  ? 414  TYR A N   1 
ATOM   3285 C  CA  . TYR A 1 414  ? 20.854 64.146  -2.465  1.00 9.20  ? 414  TYR A CA  1 
ATOM   3286 C  C   . TYR A 1 414  ? 22.086 65.033  -2.510  1.00 9.72  ? 414  TYR A C   1 
ATOM   3287 O  O   . TYR A 1 414  ? 22.003 66.224  -2.839  1.00 10.60 ? 414  TYR A O   1 
ATOM   3288 C  CB  . TYR A 1 414  ? 20.428 63.778  -3.896  1.00 9.66  ? 414  TYR A CB  1 
ATOM   3289 C  CG  . TYR A 1 414  ? 19.412 62.634  -3.930  1.00 9.97  ? 414  TYR A CG  1 
ATOM   3290 C  CD1 . TYR A 1 414  ? 18.056 62.860  -3.697  1.00 10.97 ? 414  TYR A CD1 1 
ATOM   3291 C  CD2 . TYR A 1 414  ? 19.837 61.325  -4.120  1.00 10.90 ? 414  TYR A CD2 1 
ATOM   3292 C  CE1 . TYR A 1 414  ? 17.135 61.785  -3.653  1.00 11.09 ? 414  TYR A CE1 1 
ATOM   3293 C  CE2 . TYR A 1 414  ? 18.933 60.233  -4.087  1.00 11.28 ? 414  TYR A CE2 1 
ATOM   3294 C  CZ  . TYR A 1 414  ? 17.587 60.508  -3.850  1.00 10.63 ? 414  TYR A CZ  1 
ATOM   3295 O  OH  . TYR A 1 414  ? 16.717 59.394  -3.817  1.00 11.06 ? 414  TYR A OH  1 
ATOM   3296 N  N   . TRP A 1 415  ? 23.212 64.388  -2.196  1.00 9.25  ? 415  TRP A N   1 
ATOM   3297 C  CA  . TRP A 1 415  ? 24.487 65.115  -2.076  1.00 9.19  ? 415  TRP A CA  1 
ATOM   3298 C  C   . TRP A 1 415  ? 25.178 65.144  -3.429  1.00 9.33  ? 415  TRP A C   1 
ATOM   3299 O  O   . TRP A 1 415  ? 26.320 64.684  -3.565  1.00 11.44 ? 415  TRP A O   1 
ATOM   3300 C  CB  . TRP A 1 415  ? 25.353 64.425  -1.026  1.00 8.53  ? 415  TRP A CB  1 
ATOM   3301 C  CG  . TRP A 1 415  ? 24.791 64.521  0.378   1.00 8.98  ? 415  TRP A CG  1 
ATOM   3302 C  CD1 . TRP A 1 415  ? 23.443 64.264  0.795   1.00 9.02  ? 415  TRP A CD1 1 
ATOM   3303 C  CD2 . TRP A 1 415  ? 25.526 64.791  1.571   1.00 9.02  ? 415  TRP A CD2 1 
ATOM   3304 N  NE1 . TRP A 1 415  ? 23.388 64.364  2.148   1.00 9.32  ? 415  TRP A NE1 1 
ATOM   3305 C  CE2 . TRP A 1 415  ? 24.634 64.685  2.660   1.00 10.18 ? 415  TRP A CE2 1 
ATOM   3306 C  CE3 . TRP A 1 415  ? 26.896 65.111  1.840   1.00 8.77  ? 415  TRP A CE3 1 
ATOM   3307 C  CZ2 . TRP A 1 415  ? 25.033 64.868  3.983   1.00 9.43  ? 415  TRP A CZ2 1 
ATOM   3308 C  CZ3 . TRP A 1 415  ? 27.296 65.293  3.125   1.00 8.77  ? 415  TRP A CZ3 1 
ATOM   3309 C  CH2 . TRP A 1 415  ? 26.372 65.165  4.213   1.00 9.45  ? 415  TRP A CH2 1 
ATOM   3310 N  N   . SER A 1 416  ? 24.558 65.733  -4.452  1.00 8.58  ? 416  SER A N   1 
ATOM   3311 C  CA  . SER A 1 416  ? 25.204 65.855  -5.736  1.00 8.94  ? 416  SER A CA  1 
ATOM   3312 C  C   . SER A 1 416  ? 25.801 67.265  -5.959  1.00 7.79  ? 416  SER A C   1 
ATOM   3313 O  O   . SER A 1 416  ? 26.463 67.451  -6.963  1.00 8.45  ? 416  SER A O   1 
ATOM   3314 C  CB  . SER A 1 416  ? 24.250 65.438  -6.871  1.00 8.32  ? 416  SER A CB  1 
ATOM   3315 O  OG  . SER A 1 416  ? 22.947 66.015  -6.699  1.00 9.74  ? 416  SER A OG  1 
ATOM   3316 N  N   . GLY A 1 417  ? 25.570 68.203  -5.051  1.00 7.89  ? 417  GLY A N   1 
ATOM   3317 C  CA  . GLY A 1 417  ? 26.164 69.552  -5.220  1.00 9.29  ? 417  GLY A CA  1 
ATOM   3318 C  C   . GLY A 1 417  ? 27.685 69.526  -5.135  1.00 7.31  ? 417  GLY A C   1 
ATOM   3319 O  O   . GLY A 1 417  ? 28.342 70.229  -5.926  1.00 7.93  ? 417  GLY A O   1 
ATOM   3320 N  N   . TYR A 1 418  ? 28.255 68.697  -4.234  1.00 7.26  ? 418  TYR A N   1 
ATOM   3321 C  CA  . TYR A 1 418  ? 29.711 68.706  -4.086  1.00 6.45  ? 418  TYR A CA  1 
ATOM   3322 C  C   . TYR A 1 418  ? 30.457 68.085  -5.254  1.00 7.39  ? 418  TYR A C   1 
ATOM   3323 O  O   . TYR A 1 418  ? 31.697 68.093  -5.270  1.00 8.19  ? 418  TYR A O   1 
ATOM   3324 C  CB  . TYR A 1 418  ? 30.091 68.033  -2.732  1.00 7.68  ? 418  TYR A CB  1 
ATOM   3325 C  CG  . TYR A 1 418  ? 30.212 66.503  -2.781  1.00 7.39  ? 418  TYR A CG  1 
ATOM   3326 C  CD1 . TYR A 1 418  ? 31.447 65.906  -2.949  1.00 7.83  ? 418  TYR A CD1 1 
ATOM   3327 C  CD2 . TYR A 1 418  ? 29.071 65.689  -2.635  1.00 8.45  ? 418  TYR A CD2 1 
ATOM   3328 C  CE1 . TYR A 1 418  ? 31.586 64.530  -2.980  1.00 6.88  ? 418  TYR A CE1 1 
ATOM   3329 C  CE2 . TYR A 1 418  ? 29.190 64.284  -2.653  1.00 8.62  ? 418  TYR A CE2 1 
ATOM   3330 C  CZ  . TYR A 1 418  ? 30.462 63.746  -2.825  1.00 7.19  ? 418  TYR A CZ  1 
ATOM   3331 O  OH  . TYR A 1 418  ? 30.651 62.365  -2.797  1.00 8.41  ? 418  TYR A OH  1 
ATOM   3332 N  N   . TYR A 1 419  ? 29.746 67.492  -6.223  1.00 7.38  ? 419  TYR A N   1 
ATOM   3333 C  CA  . TYR A 1 419  ? 30.414 67.053  -7.455  1.00 7.33  ? 419  TYR A CA  1 
ATOM   3334 C  C   . TYR A 1 419  ? 30.923 68.282  -8.263  1.00 6.60  ? 419  TYR A C   1 
ATOM   3335 O  O   . TYR A 1 419  ? 31.774 68.128  -9.140  1.00 7.55  ? 419  TYR A O   1 
ATOM   3336 C  CB  . TYR A 1 419  ? 29.467 66.239  -8.343  1.00 7.48  ? 419  TYR A CB  1 
ATOM   3337 C  CG  . TYR A 1 419  ? 28.806 65.053  -7.688  1.00 6.68  ? 419  TYR A CG  1 
ATOM   3338 C  CD1 . TYR A 1 419  ? 27.616 64.559  -8.222  1.00 7.17  ? 419  TYR A CD1 1 
ATOM   3339 C  CD2 . TYR A 1 419  ? 29.397 64.377  -6.589  1.00 8.15  ? 419  TYR A CD2 1 
ATOM   3340 C  CE1 . TYR A 1 419  ? 27.008 63.408  -7.673  1.00 7.60  ? 419  TYR A CE1 1 
ATOM   3341 C  CE2 . TYR A 1 419  ? 28.802 63.221  -6.043  1.00 8.41  ? 419  TYR A CE2 1 
ATOM   3342 C  CZ  . TYR A 1 419  ? 27.623 62.761  -6.610  1.00 8.22  ? 419  TYR A CZ  1 
ATOM   3343 O  OH  . TYR A 1 419  ? 27.067 61.599  -6.102  1.00 8.47  ? 419  TYR A OH  1 
ATOM   3344 N  N   . THR A 1 420  ? 30.447 69.490  -7.895  1.00 7.02  ? 420  THR A N   1 
ATOM   3345 C  CA  . THR A 1 420  ? 30.845 70.719  -8.588  1.00 7.82  ? 420  THR A CA  1 
ATOM   3346 C  C   . THR A 1 420  ? 31.371 71.803  -7.692  1.00 7.98  ? 420  THR A C   1 
ATOM   3347 O  O   . THR A 1 420  ? 32.163 72.637  -8.178  1.00 8.87  ? 420  THR A O   1 
ATOM   3348 C  CB  . THR A 1 420  ? 29.603 71.255  -9.405  1.00 7.73  ? 420  THR A CB  1 
ATOM   3349 O  OG1 . THR A 1 420  ? 29.153 70.182  -10.254 1.00 8.89  ? 420  THR A OG1 1 
ATOM   3350 C  CG2 . THR A 1 420  ? 29.913 72.494  -10.261 1.00 10.51 ? 420  THR A CG2 1 
ATOM   3351 N  N   . SER A 1 421  ? 30.991 71.860  -6.420  1.00 7.53  ? 421  SER A N   1 
ATOM   3352 C  CA  . SER A 1 421  ? 31.414 72.944  -5.568  1.00 7.94  ? 421  SER A CA  1 
ATOM   3353 C  C   . SER A 1 421  ? 32.893 73.296  -5.615  1.00 8.04  ? 421  SER A C   1 
ATOM   3354 O  O   . SER A 1 421  ? 33.742 72.398  -5.547  1.00 7.67  ? 421  SER A O   1 
ATOM   3355 C  CB  . SER A 1 421  ? 31.031 72.619  -4.123  1.00 7.19  ? 421  SER A CB  1 
ATOM   3356 O  OG  . SER A 1 421  ? 29.616 72.489  -4.009  1.00 8.66  ? 421  SER A OG  1 
ATOM   3357 N  N   . ARG A 1 422  ? 33.190 74.616  -5.638  1.00 7.59  ? 422  ARG A N   1 
ATOM   3358 C  CA  . ARG A 1 422  ? 34.604 75.118  -5.706  1.00 7.30  ? 422  ARG A CA  1 
ATOM   3359 C  C   . ARG A 1 422  ? 35.337 74.446  -6.905  1.00 8.34  ? 422  ARG A C   1 
ATOM   3360 O  O   . ARG A 1 422  ? 36.380 73.741  -6.764  1.00 7.84  ? 422  ARG A O   1 
ATOM   3361 C  CB  . ARG A 1 422  ? 35.373 74.866  -4.398  1.00 8.18  ? 422  ARG A CB  1 
ATOM   3362 C  CG  . ARG A 1 422  ? 35.084 75.916  -3.283  1.00 8.40  ? 422  ARG A CG  1 
ATOM   3363 C  CD  . ARG A 1 422  ? 33.575 76.055  -2.854  1.00 8.57  ? 422  ARG A CD  1 
ATOM   3364 N  NE  . ARG A 1 422  ? 33.538 77.046  -1.743  1.00 9.04  ? 422  ARG A NE  1 
ATOM   3365 C  CZ  . ARG A 1 422  ? 33.607 76.751  -0.464  1.00 9.62  ? 422  ARG A CZ  1 
ATOM   3366 N  NH1 . ARG A 1 422  ? 33.595 75.493  -0.042  1.00 9.78  ? 422  ARG A NH1 1 
ATOM   3367 N  NH2 . ARG A 1 422  ? 33.876 77.717  0.432   1.00 9.97  ? 422  ARG A NH2 1 
ATOM   3368 N  N   . PRO A 1 423  ? 34.833 74.652  -8.104  1.00 7.43  ? 423  PRO A N   1 
ATOM   3369 C  CA  . PRO A 1 423  ? 35.431 74.025  -9.288  1.00 7.35  ? 423  PRO A CA  1 
ATOM   3370 C  C   . PRO A 1 423  ? 36.821 74.488  -9.632  1.00 7.34  ? 423  PRO A C   1 
ATOM   3371 O  O   . PRO A 1 423  ? 37.560 73.765  -10.310 1.00 7.92  ? 423  PRO A O   1 
ATOM   3372 C  CB  . PRO A 1 423  ? 34.373 74.269  -10.397 1.00 8.45  ? 423  PRO A CB  1 
ATOM   3373 C  CG  . PRO A 1 423  ? 33.800 75.620  -9.996  1.00 8.72  ? 423  PRO A CG  1 
ATOM   3374 C  CD  . PRO A 1 423  ? 33.681 75.516  -8.466  1.00 7.98  ? 423  PRO A CD  1 
ATOM   3375 N  N   . TYR A 1 424  ? 37.208 75.703  -9.207  1.00 8.74  ? 424  TYR A N   1 
ATOM   3376 C  CA  . TYR A 1 424  ? 38.601 76.132  -9.478  1.00 8.04  ? 424  TYR A CA  1 
ATOM   3377 C  C   . TYR A 1 424  ? 39.587 75.136  -8.862  1.00 6.89  ? 424  TYR A C   1 
ATOM   3378 O  O   . TYR A 1 424  ? 40.564 74.741  -9.507  1.00 7.85  ? 424  TYR A O   1 
ATOM   3379 C  CB  . TYR A 1 424  ? 38.834 77.521  -8.853  1.00 8.44  ? 424  TYR A CB  1 
ATOM   3380 C  CG  . TYR A 1 424  ? 40.221 78.066  -9.086  1.00 8.00  ? 424  TYR A CG  1 
ATOM   3381 C  CD1 . TYR A 1 424  ? 40.481 78.825  -10.206 1.00 9.87  ? 424  TYR A CD1 1 
ATOM   3382 C  CD2 . TYR A 1 424  ? 41.259 77.823  -8.198  1.00 8.41  ? 424  TYR A CD2 1 
ATOM   3383 C  CE1 . TYR A 1 424  ? 41.757 79.350  -10.436 1.00 10.90 ? 424  TYR A CE1 1 
ATOM   3384 C  CE2 . TYR A 1 424  ? 42.563 78.340  -8.452  1.00 11.84 ? 424  TYR A CE2 1 
ATOM   3385 C  CZ  . TYR A 1 424  ? 42.760 79.097  -9.573  1.00 11.15 ? 424  TYR A CZ  1 
ATOM   3386 O  OH  . TYR A 1 424  ? 44.012 79.680  -9.852  1.00 15.22 ? 424  TYR A OH  1 
ATOM   3387 N  N   . HIS A 1 425  ? 39.308 74.712  -7.634  1.00 7.54  ? 425  HIS A N   1 
ATOM   3388 C  CA  . HIS A 1 425  ? 40.212 73.790  -6.928  1.00 6.99  ? 425  HIS A CA  1 
ATOM   3389 C  C   . HIS A 1 425  ? 40.119 72.382  -7.406  1.00 7.86  ? 425  HIS A C   1 
ATOM   3390 O  O   . HIS A 1 425  ? 41.105 71.610  -7.353  1.00 7.27  ? 425  HIS A O   1 
ATOM   3391 C  CB  . HIS A 1 425  ? 40.007 73.931  -5.398  1.00 9.07  ? 425  HIS A CB  1 
ATOM   3392 C  CG  . HIS A 1 425  ? 40.004 75.365  -4.974  1.00 8.78  ? 425  HIS A CG  1 
ATOM   3393 N  ND1 . HIS A 1 425  ? 41.141 76.118  -4.680  1.00 13.20 ? 425  HIS A ND1 1 
ATOM   3394 C  CD2 . HIS A 1 425  ? 38.973 76.227  -4.991  1.00 8.12  ? 425  HIS A CD2 1 
ATOM   3395 C  CE1 . HIS A 1 425  ? 40.772 77.392  -4.533  1.00 8.68  ? 425  HIS A CE1 1 
ATOM   3396 N  NE2 . HIS A 1 425  ? 39.470 77.472  -4.718  1.00 12.94 ? 425  HIS A NE2 1 
ATOM   3397 N  N   . LYS A 1 426  ? 38.920 71.991  -7.889  1.00 6.89  ? 426  LYS A N   1 
ATOM   3398 C  CA  . LYS A 1 426  ? 38.769 70.675  -8.538  1.00 7.61  ? 426  LYS A CA  1 
ATOM   3399 C  C   . LYS A 1 426  ? 39.672 70.614  -9.783  1.00 6.66  ? 426  LYS A C   1 
ATOM   3400 O  O   . LYS A 1 426  ? 40.299 69.573  -10.057 1.00 7.68  ? 426  LYS A O   1 
ATOM   3401 C  CB  . LYS A 1 426  ? 37.281 70.485  -8.939  1.00 7.25  ? 426  LYS A CB  1 
ATOM   3402 C  CG  . LYS A 1 426  ? 36.417 70.098  -7.721  1.00 7.26  ? 426  LYS A CG  1 
ATOM   3403 C  CD  . LYS A 1 426  ? 34.889 70.148  -8.072  1.00 8.16  ? 426  LYS A CD  1 
ATOM   3404 C  CE  . LYS A 1 426  ? 34.014 69.227  -7.181  1.00 7.49  ? 426  LYS A CE  1 
ATOM   3405 N  NZ  . LYS A 1 426  ? 34.000 69.668  -5.747  1.00 7.31  ? 426  LYS A NZ  1 
ATOM   3406 N  N   . ARG A 1 427  ? 39.711 71.705  -10.592 1.00 6.32  ? 427  ARG A N   1 
ATOM   3407 C  CA  . ARG A 1 427  ? 40.601 71.717  -11.734 1.00 7.36  ? 427  ARG A CA  1 
ATOM   3408 C  C   . ARG A 1 427  ? 42.078 71.744  -11.288 1.00 8.22  ? 427  ARG A C   1 
ATOM   3409 O  O   . ARG A 1 427  ? 42.896 71.016  -11.861 1.00 7.05  ? 427  ARG A O   1 
ATOM   3410 C  CB  . ARG A 1 427  ? 40.253 72.942  -12.614 1.00 7.53  ? 427  ARG A CB  1 
ATOM   3411 C  CG  . ARG A 1 427  ? 41.209 73.223  -13.741 1.00 9.58  ? 427  ARG A CG  1 
ATOM   3412 C  CD  . ARG A 1 427  ? 41.277 72.076  -14.777 1.00 10.12 ? 427  ARG A CD  1 
ATOM   3413 N  NE  . ARG A 1 427  ? 42.310 72.497  -15.746 1.00 11.34 ? 427  ARG A NE  1 
ATOM   3414 C  CZ  . ARG A 1 427  ? 43.110 71.678  -16.339 1.00 9.95  ? 427  ARG A CZ  1 
ATOM   3415 N  NH1 . ARG A 1 427  ? 43.080 70.365  -16.180 1.00 10.24 ? 427  ARG A NH1 1 
ATOM   3416 N  NH2 . ARG A 1 427  ? 44.078 72.217  -17.126 1.00 11.76 ? 427  ARG A NH2 1 
ATOM   3417 N  N   . MET A 1 428  ? 42.396 72.540  -10.252 1.00 7.31  ? 428  MET A N   1 
ATOM   3418 C  CA  . MET A 1 428  ? 43.782 72.597  -9.753  1.00 7.17  ? 428  MET A CA  1 
ATOM   3419 C  C   . MET A 1 428  ? 44.266 71.196  -9.334  1.00 6.75  ? 428  MET A C   1 
ATOM   3420 O  O   . MET A 1 428  ? 45.436 70.857  -9.555  1.00 7.41  ? 428  MET A O   1 
ATOM   3421 C  CB  . MET A 1 428  ? 43.829 73.558  -8.577  1.00 9.07  ? 428  MET A CB  1 
ATOM   3422 C  CG  . MET A 1 428  ? 45.266 73.950  -8.210  1.00 7.60  ? 428  MET A CG  1 
ATOM   3423 S  SD  . MET A 1 428  ? 45.175 75.273  -6.947  1.00 10.52 ? 428  MET A SD  1 
ATOM   3424 C  CE  . MET A 1 428  ? 46.888 75.787  -6.870  1.00 10.67 ? 428  MET A CE  1 
ATOM   3425 N  N   . ASP A 1 429  ? 43.375 70.385  -8.741  1.00 7.85  ? 429  ASP A N   1 
ATOM   3426 C  CA  . ASP A 1 429  ? 43.708 69.011  -8.361  1.00 7.48  ? 429  ASP A CA  1 
ATOM   3427 C  C   . ASP A 1 429  ? 44.285 68.208  -9.534  1.00 7.33  ? 429  ASP A C   1 
ATOM   3428 O  O   . ASP A 1 429  ? 45.308 67.522  -9.386  1.00 7.04  ? 429  ASP A O   1 
ATOM   3429 C  CB  . ASP A 1 429  ? 42.445 68.300  -7.837  1.00 7.50  ? 429  ASP A CB  1 
ATOM   3430 C  CG  . ASP A 1 429  ? 42.712 66.839  -7.530  1.00 6.60  ? 429  ASP A CG  1 
ATOM   3431 O  OD1 . ASP A 1 429  ? 42.406 65.971  -8.377  1.00 7.87  ? 429  ASP A OD1 1 
ATOM   3432 O  OD2 . ASP A 1 429  ? 43.228 66.601  -6.408  1.00 8.29  ? 429  ASP A OD2 1 
ATOM   3433 N  N   . ARG A 1 430  ? 43.617 68.319  -10.690 1.00 6.31  ? 430  ARG A N   1 
ATOM   3434 C  CA  . ARG A 1 430  ? 44.054 67.562  -11.840 1.00 6.72  ? 430  ARG A CA  1 
ATOM   3435 C  C   . ARG A 1 430  ? 45.367 68.095  -12.403 1.00 6.43  ? 430  ARG A C   1 
ATOM   3436 O  O   . ARG A 1 430  ? 46.213 67.312  -12.906 1.00 7.27  ? 430  ARG A O   1 
ATOM   3437 C  CB  . ARG A 1 430  ? 42.990 67.581  -12.946 1.00 6.81  ? 430  ARG A CB  1 
ATOM   3438 C  CG  . ARG A 1 430  ? 41.762 66.857  -12.548 1.00 7.49  ? 430  ARG A CG  1 
ATOM   3439 C  CD  . ARG A 1 430  ? 41.985 65.394  -12.068 1.00 6.76  ? 430  ARG A CD  1 
ATOM   3440 N  NE  . ARG A 1 430  ? 40.734 64.613  -12.088 1.00 7.95  ? 430  ARG A NE  1 
ATOM   3441 C  CZ  . ARG A 1 430  ? 40.042 64.280  -11.005 1.00 6.90  ? 430  ARG A CZ  1 
ATOM   3442 N  NH1 . ARG A 1 430  ? 40.438 64.612  -9.774  1.00 7.10  ? 430  ARG A NH1 1 
ATOM   3443 N  NH2 . ARG A 1 430  ? 38.903 63.581  -11.143 1.00 8.04  ? 430  ARG A NH2 1 
ATOM   3444 N  N   . VAL A 1 431  ? 45.572 69.407  -12.353 1.00 6.82  ? 431  VAL A N   1 
ATOM   3445 C  CA  . VAL A 1 431  ? 46.862 69.984  -12.812 1.00 7.11  ? 431  VAL A CA  1 
ATOM   3446 C  C   . VAL A 1 431  ? 47.995 69.465  -11.880 1.00 8.31  ? 431  VAL A C   1 
ATOM   3447 O  O   . VAL A 1 431  ? 49.022 68.974  -12.358 1.00 7.38  ? 431  VAL A O   1 
ATOM   3448 C  CB  . VAL A 1 431  ? 46.748 71.515  -12.780 1.00 6.27  ? 431  VAL A CB  1 
ATOM   3449 C  CG1 . VAL A 1 431  ? 48.109 72.126  -13.104 1.00 9.22  ? 431  VAL A CG1 1 
ATOM   3450 C  CG2 . VAL A 1 431  ? 45.715 71.970  -13.839 1.00 9.11  ? 431  VAL A CG2 1 
ATOM   3451 N  N   . LEU A 1 432  ? 47.800 69.595  -10.576 1.00 6.45  ? 432  LEU A N   1 
ATOM   3452 C  CA  . LEU A 1 432  ? 48.822 69.135  -9.643  1.00 6.48  ? 432  LEU A CA  1 
ATOM   3453 C  C   . LEU A 1 432  ? 49.039 67.624  -9.745  1.00 6.79  ? 432  LEU A C   1 
ATOM   3454 O  O   . LEU A 1 432  ? 50.190 67.164  -9.634  1.00 7.36  ? 432  LEU A O   1 
ATOM   3455 C  CB  . LEU A 1 432  ? 48.502 69.607  -8.224  1.00 7.40  ? 432  LEU A CB  1 
ATOM   3456 C  CG  . LEU A 1 432  ? 49.500 69.206  -7.157  1.00 7.71  ? 432  LEU A CG  1 
ATOM   3457 C  CD1 . LEU A 1 432  ? 50.933 69.738  -7.449  1.00 8.08  ? 432  LEU A CD1 1 
ATOM   3458 C  CD2 . LEU A 1 432  ? 49.054 69.840  -5.817  1.00 8.83  ? 432  LEU A CD2 1 
ATOM   3459 N  N   . MET A 1 433  ? 47.985 66.851  -9.981  1.00 6.03  ? 433  MET A N   1 
ATOM   3460 C  CA  . MET A 1 433  ? 48.144 65.411  -10.162 1.00 6.93  ? 433  MET A CA  1 
ATOM   3461 C  C   . MET A 1 433  ? 49.193 65.116  -11.215 1.00 6.84  ? 433  MET A C   1 
ATOM   3462 O  O   . MET A 1 433  ? 50.065 64.266  -11.028 1.00 6.35  ? 433  MET A O   1 
ATOM   3463 C  CB  . MET A 1 433  ? 46.795 64.808  -10.665 1.00 6.87  ? 433  MET A CB  1 
ATOM   3464 C  CG  . MET A 1 433  ? 46.891 63.324  -10.937 1.00 6.97  ? 433  MET A CG  1 
ATOM   3465 S  SD  . MET A 1 433  ? 45.323 62.660  -11.621 1.00 9.57  ? 433  MET A SD  1 
ATOM   3466 C  CE  . MET A 1 433  ? 45.391 63.362  -13.261 1.00 12.12 ? 433  MET A CE  1 
ATOM   3467 N  N   . HIS A 1 434  ? 49.079 65.818  -12.343 1.00 6.20  ? 434  HIS A N   1 
ATOM   3468 C  CA  . HIS A 1 434  ? 49.991 65.585  -13.467 1.00 6.86  ? 434  HIS A CA  1 
ATOM   3469 C  C   . HIS A 1 434  ? 51.396 66.098  -13.132 1.00 6.48  ? 434  HIS A C   1 
ATOM   3470 O  O   . HIS A 1 434  ? 52.388 65.446  -13.504 1.00 7.56  ? 434  HIS A O   1 
ATOM   3471 C  CB  . HIS A 1 434  ? 49.448 66.295  -14.737 1.00 7.58  ? 434  HIS A CB  1 
ATOM   3472 C  CG  . HIS A 1 434  ? 50.442 66.244  -15.848 1.00 6.65  ? 434  HIS A CG  1 
ATOM   3473 N  ND1 . HIS A 1 434  ? 51.264 67.285  -16.248 1.00 11.72 ? 434  HIS A ND1 1 
ATOM   3474 C  CD2 . HIS A 1 434  ? 50.821 65.156  -16.542 1.00 5.83  ? 434  HIS A CD2 1 
ATOM   3475 C  CE1 . HIS A 1 434  ? 52.117 66.823  -17.174 1.00 6.24  ? 434  HIS A CE1 1 
ATOM   3476 N  NE2 . HIS A 1 434  ? 51.865 65.541  -17.350 1.00 11.79 ? 434  HIS A NE2 1 
ATOM   3477 N  N   A TYR A 1 435  ? 51.500 67.275  -12.509 0.50 4.56  ? 435  TYR A N   1 
ATOM   3478 N  N   B TYR A 1 435  ? 51.500 67.275  -12.509 0.50 9.73  ? 435  TYR A N   1 
ATOM   3479 C  CA  A TYR A 1 435  ? 52.832 67.818  -12.194 0.50 3.65  ? 435  TYR A CA  1 
ATOM   3480 C  CA  B TYR A 1 435  ? 52.832 67.818  -12.194 0.50 13.09 ? 435  TYR A CA  1 
ATOM   3481 C  C   A TYR A 1 435  ? 53.563 66.933  -11.185 0.50 1.99  ? 435  TYR A C   1 
ATOM   3482 C  C   B TYR A 1 435  ? 53.426 67.139  -10.960 0.50 14.79 ? 435  TYR A C   1 
ATOM   3483 O  O   A TYR A 1 435  ? 54.793 66.796  -11.276 0.50 1.00  ? 435  TYR A O   1 
ATOM   3484 O  O   B TYR A 1 435  ? 54.656 67.141  -10.798 0.50 20.20 ? 435  TYR A O   1 
ATOM   3485 C  CB  A TYR A 1 435  ? 52.748 69.238  -11.616 0.50 5.49  ? 435  TYR A CB  1 
ATOM   3486 C  CB  B TYR A 1 435  ? 52.786 69.331  -11.935 0.50 16.41 ? 435  TYR A CB  1 
ATOM   3487 C  CG  A TYR A 1 435  ? 52.591 70.414  -12.540 0.50 7.55  ? 435  TYR A CG  1 
ATOM   3488 C  CG  B TYR A 1 435  ? 52.722 70.287  -13.094 0.50 17.49 ? 435  TYR A CG  1 
ATOM   3489 C  CD1 A TYR A 1 435  ? 51.630 70.475  -13.542 0.50 4.95  ? 435  TYR A CD1 1 
ATOM   3490 C  CD1 B TYR A 1 435  ? 53.584 70.226  -14.183 0.50 23.46 ? 435  TYR A CD1 1 
ATOM   3491 C  CD2 A TYR A 1 435  ? 53.368 71.551  -12.310 0.50 10.90 ? 435  TYR A CD2 1 
ATOM   3492 C  CD2 B TYR A 1 435  ? 51.675 71.209  -13.141 0.50 22.27 ? 435  TYR A CD2 1 
ATOM   3493 C  CE1 A TYR A 1 435  ? 51.436 71.578  -14.363 0.50 5.56  ? 435  TYR A CE1 1 
ATOM   3494 C  CE1 B TYR A 1 435  ? 53.499 71.064  -15.286 0.50 25.77 ? 435  TYR A CE1 1 
ATOM   3495 C  CE2 A TYR A 1 435  ? 53.175 72.707  -13.088 0.50 14.08 ? 435  TYR A CE2 1 
ATOM   3496 C  CE2 B TYR A 1 435  ? 51.524 72.048  -14.260 0.50 25.98 ? 435  TYR A CE2 1 
ATOM   3497 C  CZ  A TYR A 1 435  ? 52.208 72.682  -14.113 0.50 10.68 ? 435  TYR A CZ  1 
ATOM   3498 C  CZ  B TYR A 1 435  ? 52.460 71.957  -15.309 0.50 25.81 ? 435  TYR A CZ  1 
ATOM   3499 O  OH  A TYR A 1 435  ? 51.994 73.819  -14.873 0.50 14.56 ? 435  TYR A OH  1 
ATOM   3500 O  OH  B TYR A 1 435  ? 52.311 72.763  -16.425 0.50 22.69 ? 435  TYR A OH  1 
ATOM   3501 N  N   . VAL A 1 436  ? 52.848 66.304  -10.243 1.00 6.52  ? 436  VAL A N   1 
ATOM   3502 C  CA  . VAL A 1 436  ? 53.519 65.398  -9.314  1.00 6.53  ? 436  VAL A CA  1 
ATOM   3503 C  C   . VAL A 1 436  ? 54.040 64.198  -10.106 1.00 7.24  ? 436  VAL A C   1 
ATOM   3504 O  O   . VAL A 1 436  ? 55.201 63.744  -9.936  1.00 7.08  ? 436  VAL A O   1 
ATOM   3505 C  CB  . VAL A 1 436  ? 52.539 64.969  -8.181  1.00 6.62  ? 436  VAL A CB  1 
ATOM   3506 C  CG1 . VAL A 1 436  ? 53.051 63.714  -7.410  1.00 8.06  ? 436  VAL A CG1 1 
ATOM   3507 C  CG2 . VAL A 1 436  ? 52.355 66.135  -7.173  1.00 7.59  ? 436  VAL A CG2 1 
ATOM   3508 N  N   . ARG A 1 437  ? 53.199 63.603  -10.960 1.00 6.81  ? 437  ARG A N   1 
ATOM   3509 C  CA  . ARG A 1 437  ? 53.669 62.472  -11.753 1.00 6.77  ? 437  ARG A CA  1 
ATOM   3510 C  C   . ARG A 1 437  ? 54.884 62.853  -12.570 1.00 6.87  ? 437  ARG A C   1 
ATOM   3511 O  O   . ARG A 1 437  ? 55.880 62.091  -12.639 1.00 7.81  ? 437  ARG A O   1 
ATOM   3512 C  CB  . ARG A 1 437  ? 52.568 61.966  -12.697 1.00 7.91  ? 437  ARG A CB  1 
ATOM   3513 C  CG  . ARG A 1 437  ? 53.077 60.985  -13.751 1.00 7.01  ? 437  ARG A CG  1 
ATOM   3514 C  CD  . ARG A 1 437  ? 51.937 60.523  -14.613 1.00 8.35  ? 437  ARG A CD  1 
ATOM   3515 N  NE  . ARG A 1 437  ? 52.448 59.768  -15.773 1.00 8.06  ? 437  ARG A NE  1 
ATOM   3516 C  CZ  . ARG A 1 437  ? 51.696 58.946  -16.507 1.00 8.26  ? 437  ARG A CZ  1 
ATOM   3517 N  NH1 . ARG A 1 437  ? 50.427 58.734  -16.205 1.00 9.54  ? 437  ARG A NH1 1 
ATOM   3518 N  NH2 . ARG A 1 437  ? 52.225 58.409  -17.598 1.00 9.23  ? 437  ARG A NH2 1 
ATOM   3519 N  N   . ALA A 1 438  ? 54.820 63.993  -13.267 1.00 6.19  ? 438  ALA A N   1 
ATOM   3520 C  CA  . ALA A 1 438  ? 55.926 64.383  -14.151 1.00 7.10  ? 438  ALA A CA  1 
ATOM   3521 C  C   . ALA A 1 438  ? 57.207 64.687  -13.343 1.00 6.74  ? 438  ALA A C   1 
ATOM   3522 O  O   . ALA A 1 438  ? 58.316 64.318  -13.806 1.00 7.92  ? 438  ALA A O   1 
ATOM   3523 C  CB  . ALA A 1 438  ? 55.535 65.612  -14.983 1.00 7.82  ? 438  ALA A CB  1 
ATOM   3524 N  N   . ALA A 1 439  ? 57.083 65.350  -12.176 1.00 7.23  ? 439  ALA A N   1 
ATOM   3525 C  CA  . ALA A 1 439  ? 58.264 65.628  -11.367 1.00 7.25  ? 439  ALA A CA  1 
ATOM   3526 C  C   . ALA A 1 439  ? 58.903 64.349  -10.827 1.00 7.61  ? 439  ALA A C   1 
ATOM   3527 O  O   . ALA A 1 439  ? 60.136 64.209  -10.816 1.00 8.38  ? 439  ALA A O   1 
ATOM   3528 C  CB  . ALA A 1 439  ? 57.912 66.557  -10.247 1.00 8.07  ? 439  ALA A CB  1 
ATOM   3529 N  N   . GLU A 1 440  ? 58.086 63.421  -10.342 1.00 6.61  ? 440  GLU A N   1 
ATOM   3530 C  CA  . GLU A 1 440  ? 58.631 62.166  -9.822  1.00 7.42  ? 440  GLU A CA  1 
ATOM   3531 C  C   . GLU A 1 440  ? 59.277 61.372  -10.963 1.00 7.36  ? 440  GLU A C   1 
ATOM   3532 O  O   . GLU A 1 440  ? 60.337 60.735  -10.778 1.00 8.96  ? 440  GLU A O   1 
ATOM   3533 C  CB  . GLU A 1 440  ? 57.544 61.315  -9.123  1.00 7.83  ? 440  GLU A CB  1 
ATOM   3534 C  CG  . GLU A 1 440  ? 57.003 61.986  -7.857  1.00 8.42  ? 440  GLU A CG  1 
ATOM   3535 C  CD  . GLU A 1 440  ? 56.331 60.985  -6.932  1.00 11.79 ? 440  GLU A CD  1 
ATOM   3536 O  OE1 . GLU A 1 440  ? 55.229 60.475  -7.206  1.00 11.13 ? 440  GLU A OE1 1 
ATOM   3537 O  OE2 . GLU A 1 440  ? 56.971 60.638  -5.918  1.00 12.07 ? 440  GLU A OE2 1 
ATOM   3538 N  N   . MET A 1 441  ? 58.653 61.329  -12.145 1.00 7.10  ? 441  MET A N   1 
ATOM   3539 C  CA  . MET A 1 441  ? 59.213 60.564  -13.263 1.00 7.16  ? 441  MET A CA  1 
ATOM   3540 C  C   . MET A 1 441  ? 60.497 61.203  -13.805 1.00 8.01  ? 441  MET A C   1 
ATOM   3541 O  O   . MET A 1 441  ? 61.545 60.493  -13.937 1.00 8.76  ? 441  MET A O   1 
ATOM   3542 C  CB  . MET A 1 441  ? 58.157 60.458  -14.388 1.00 7.34  ? 441  MET A CB  1 
ATOM   3543 C  CG  . MET A 1 441  ? 58.674 59.699  -15.597 1.00 7.60  ? 441  MET A CG  1 
ATOM   3544 S  SD  . MET A 1 441  ? 57.426 59.447  -16.868 1.00 8.61  ? 441  MET A SD  1 
ATOM   3545 C  CE  . MET A 1 441  ? 56.277 58.263  -16.032 1.00 9.65  ? 441  MET A CE  1 
ATOM   3546 N  N   . LEU A 1 442  ? 60.494 62.503  -14.063 1.00 6.86  ? 442  LEU A N   1 
ATOM   3547 C  CA  . LEU A 1 442  ? 61.713 63.149  -14.603 1.00 7.80  ? 442  LEU A CA  1 
ATOM   3548 C  C   . LEU A 1 442  ? 62.899 63.039  -13.689 1.00 8.73  ? 442  LEU A C   1 
ATOM   3549 O  O   . LEU A 1 442  ? 64.043 62.866  -14.195 1.00 9.38  ? 442  LEU A O   1 
ATOM   3550 C  CB  . LEU A 1 442  ? 61.433 64.632  -14.914 1.00 8.30  ? 442  LEU A CB  1 
ATOM   3551 C  CG  . LEU A 1 442  ? 60.741 64.872  -16.275 1.00 7.06  ? 442  LEU A CG  1 
ATOM   3552 C  CD1 . LEU A 1 442  ? 60.194 66.280  -16.345 1.00 9.94  ? 442  LEU A CD1 1 
ATOM   3553 C  CD2 . LEU A 1 442  ? 61.814 64.698  -17.415 1.00 10.44 ? 442  LEU A CD2 1 
ATOM   3554 N  N   . SER A 1 443  ? 62.678 63.118  -12.377 1.00 7.41  ? 443  SER A N   1 
ATOM   3555 C  CA  . SER A 1 443  ? 63.775 63.074  -11.440 1.00 8.33  ? 443  SER A CA  1 
ATOM   3556 C  C   . SER A 1 443  ? 64.165 61.646  -11.088 1.00 8.65  ? 443  SER A C   1 
ATOM   3557 O  O   . SER A 1 443  ? 65.288 61.474  -10.552 1.00 9.76  ? 443  SER A O   1 
ATOM   3558 C  CB  . SER A 1 443  ? 63.510 63.905  -10.185 1.00 8.50  ? 443  SER A CB  1 
ATOM   3559 O  OG  . SER A 1 443  ? 62.419 63.345  -9.433  1.00 9.21  ? 443  SER A OG  1 
ATOM   3560 N  N   . ALA A 1 444  ? 63.370 60.649  -11.406 1.00 7.50  ? 444  ALA A N   1 
ATOM   3561 C  CA  . ALA A 1 444  ? 63.666 59.256  -11.073 1.00 8.48  ? 444  ALA A CA  1 
ATOM   3562 C  C   . ALA A 1 444  ? 64.826 58.726  -11.881 1.00 9.37  ? 444  ALA A C   1 
ATOM   3563 O  O   . ALA A 1 444  ? 65.469 57.742  -11.445 1.00 10.44 ? 444  ALA A O   1 
ATOM   3564 C  CB  . ALA A 1 444  ? 62.461 58.360  -11.345 1.00 10.06 ? 444  ALA A CB  1 
ATOM   3565 N  N   . TRP A 1 445  ? 65.085 59.256  -13.071 1.00 9.35  ? 445  TRP A N   1 
ATOM   3566 C  CA  . TRP A 1 445  ? 66.156 58.728  -13.935 1.00 10.89 ? 445  TRP A CA  1 
ATOM   3567 C  C   . TRP A 1 445  ? 67.535 58.803  -13.313 1.00 11.07 ? 445  TRP A C   1 
ATOM   3568 O  O   . TRP A 1 445  ? 68.407 58.007  -13.702 1.00 13.34 ? 445  TRP A O   1 
ATOM   3569 C  CB  . TRP A 1 445  ? 66.159 59.481  -15.264 1.00 10.49 ? 445  TRP A CB  1 
ATOM   3570 C  CG  . TRP A 1 445  ? 64.870 59.318  -16.037 1.00 9.21  ? 445  TRP A CG  1 
ATOM   3571 C  CD1 . TRP A 1 445  ? 63.884 60.289  -16.194 1.00 9.42  ? 445  TRP A CD1 1 
ATOM   3572 C  CD2 . TRP A 1 445  ? 64.389 58.136  -16.716 1.00 8.84  ? 445  TRP A CD2 1 
ATOM   3573 N  NE1 . TRP A 1 445  ? 62.853 59.752  -16.905 1.00 9.49  ? 445  TRP A NE1 1 
ATOM   3574 C  CE2 . TRP A 1 445  ? 63.126 58.440  -17.251 1.00 8.12  ? 445  TRP A CE2 1 
ATOM   3575 C  CE3 . TRP A 1 445  ? 64.931 56.846  -16.931 1.00 9.95  ? 445  TRP A CE3 1 
ATOM   3576 C  CZ2 . TRP A 1 445  ? 62.387 57.533  -17.978 1.00 8.85  ? 445  TRP A CZ2 1 
ATOM   3577 C  CZ3 . TRP A 1 445  ? 64.196 55.945  -17.654 1.00 10.40 ? 445  TRP A CZ3 1 
ATOM   3578 C  CH2 . TRP A 1 445  ? 62.923 56.274  -18.177 1.00 9.15  ? 445  TRP A CH2 1 
ATOM   3579 N  N   . HIS A 1 446  ? 67.769 59.756  -12.436 1.00 11.17 ? 446  HIS A N   1 
ATOM   3580 C  CA  . HIS A 1 446  ? 69.072 59.871  -11.799 1.00 12.75 ? 446  HIS A CA  1 
ATOM   3581 C  C   . HIS A 1 446  ? 68.914 59.760  -10.293 1.00 11.59 ? 446  HIS A C   1 
ATOM   3582 O  O   . HIS A 1 446  ? 67.863 59.962  -9.700  1.00 11.64 ? 446  HIS A O   1 
ATOM   3583 C  CB  . HIS A 1 446  ? 69.658 61.268  -12.018 1.00 13.06 ? 446  HIS A CB  1 
ATOM   3584 C  CG  . HIS A 1 446  ? 70.045 61.556  -13.431 1.00 14.80 ? 446  HIS A CG  1 
ATOM   3585 N  ND1 . HIS A 1 446  ? 69.252 62.299  -14.288 1.00 17.71 ? 446  HIS A ND1 1 
ATOM   3586 C  CD2 . HIS A 1 446  ? 71.161 61.229  -14.132 1.00 22.00 ? 446  HIS A CD2 1 
ATOM   3587 C  CE1 . HIS A 1 446  ? 69.862 62.423  -15.452 1.00 24.01 ? 446  HIS A CE1 1 
ATOM   3588 N  NE2 . HIS A 1 446  ? 71.018 61.786  -15.385 1.00 19.48 ? 446  HIS A NE2 1 
ATOM   3589 N  N   . SER A 1 447  ? 70.058 59.489  -9.653  1.00 12.18 ? 447  SER A N   1 
ATOM   3590 C  CA  . SER A 1 447  ? 70.209 59.582  -8.224  1.00 12.18 ? 447  SER A CA  1 
ATOM   3591 C  C   . SER A 1 447  ? 70.666 61.072  -7.970  1.00 13.12 ? 447  SER A C   1 
ATOM   3592 O  O   . SER A 1 447  ? 71.499 61.594  -8.749  1.00 15.73 ? 447  SER A O   1 
ATOM   3593 C  CB  . SER A 1 447  ? 71.297 58.602  -7.843  1.00 16.93 ? 447  SER A CB  1 
ATOM   3594 O  OG  . SER A 1 447  ? 71.280 58.535  -6.454  1.00 23.12 ? 447  SER A OG  1 
ATOM   3595 N  N   . TRP A 1 448  ? 70.151 61.757  -6.957  1.00 11.35 ? 448  TRP A N   1 
ATOM   3596 C  CA  . TRP A 1 448  ? 70.497 63.152  -6.728  1.00 12.41 ? 448  TRP A CA  1 
ATOM   3597 C  C   . TRP A 1 448  ? 71.192 63.350  -5.403  1.00 14.64 ? 448  TRP A C   1 
ATOM   3598 O  O   . TRP A 1 448  ? 70.845 62.733  -4.410  1.00 14.34 ? 448  TRP A O   1 
ATOM   3599 C  CB  . TRP A 1 448  ? 69.231 64.069  -6.744  1.00 12.81 ? 448  TRP A CB  1 
ATOM   3600 C  CG  . TRP A 1 448  ? 68.577 64.079  -8.111  1.00 11.17 ? 448  TRP A CG  1 
ATOM   3601 C  CD1 . TRP A 1 448  ? 67.716 63.150  -8.615  1.00 11.88 ? 448  TRP A CD1 1 
ATOM   3602 C  CD2 . TRP A 1 448  ? 68.745 65.073  -9.124  1.00 9.83  ? 448  TRP A CD2 1 
ATOM   3603 N  NE1 . TRP A 1 448  ? 67.312 63.500  -9.873  1.00 10.95 ? 448  TRP A NE1 1 
ATOM   3604 C  CE2 . TRP A 1 448  ? 67.928 64.680  -10.217 1.00 10.34 ? 448  TRP A CE2 1 
ATOM   3605 C  CE3 . TRP A 1 448  ? 69.506 66.265  -9.213  1.00 11.85 ? 448  TRP A CE3 1 
ATOM   3606 C  CZ2 . TRP A 1 448  ? 67.830 65.437  -11.381 1.00 12.24 ? 448  TRP A CZ2 1 
ATOM   3607 C  CZ3 . TRP A 1 448  ? 69.408 67.024  -10.375 1.00 11.80 ? 448  TRP A CZ3 1 
ATOM   3608 C  CH2 . TRP A 1 448  ? 68.564 66.590  -11.440 1.00 11.57 ? 448  TRP A CH2 1 
ATOM   3609 N  N   . ASP A 1 449  ? 72.160 64.265  -5.390  1.00 15.83 ? 449  ASP A N   1 
ATOM   3610 C  CA  . ASP A 1 449  ? 72.848 64.609  -4.166  1.00 18.61 ? 449  ASP A CA  1 
ATOM   3611 C  C   . ASP A 1 449  ? 71.820 65.251  -3.238  1.00 17.38 ? 449  ASP A C   1 
ATOM   3612 O  O   . ASP A 1 449  ? 70.910 65.937  -3.697  1.00 16.67 ? 449  ASP A O   1 
ATOM   3613 C  CB  . ASP A 1 449  ? 73.975 65.600  -4.491  1.00 22.65 ? 449  ASP A CB  1 
ATOM   3614 C  CG  . ASP A 1 449  ? 74.778 65.970  -3.254  1.00 28.03 ? 449  ASP A CG  1 
ATOM   3615 O  OD1 . ASP A 1 449  ? 74.515 67.036  -2.670  1.00 29.28 ? 449  ASP A OD1 1 
ATOM   3616 O  OD2 . ASP A 1 449  ? 75.647 65.152  -2.853  1.00 36.22 ? 449  ASP A OD2 1 
ATOM   3617 N  N   . GLY A 1 450  ? 71.961 65.060  -1.926  1.00 17.36 ? 450  GLY A N   1 
ATOM   3618 C  CA  . GLY A 1 450  ? 71.034 65.654  -0.978  1.00 18.19 ? 450  GLY A CA  1 
ATOM   3619 C  C   . GLY A 1 450  ? 70.958 67.161  -1.091  1.00 19.76 ? 450  GLY A C   1 
ATOM   3620 O  O   . GLY A 1 450  ? 69.926 67.749  -0.764  1.00 19.68 ? 450  GLY A O   1 
ATOM   3621 N  N   A MET A 1 451  ? 72.040 67.816  -1.523  0.50 18.63 ? 451  MET A N   1 
ATOM   3622 N  N   B MET A 1 451  ? 72.040 67.816  -1.523  0.50 18.57 ? 451  MET A N   1 
ATOM   3623 C  CA  A MET A 1 451  ? 72.003 69.265  -1.635  0.50 20.40 ? 451  MET A CA  1 
ATOM   3624 C  CA  B MET A 1 451  ? 72.003 69.265  -1.635  0.50 20.26 ? 451  MET A CA  1 
ATOM   3625 C  C   A MET A 1 451  ? 71.037 69.774  -2.699  0.50 17.72 ? 451  MET A C   1 
ATOM   3626 C  C   B MET A 1 451  ? 71.037 69.774  -2.699  0.50 17.67 ? 451  MET A C   1 
ATOM   3627 O  O   A MET A 1 451  ? 70.707 70.947  -2.714  0.50 19.13 ? 451  MET A O   1 
ATOM   3628 O  O   B MET A 1 451  ? 70.707 70.947  -2.714  0.50 19.18 ? 451  MET A O   1 
ATOM   3629 C  CB  A MET A 1 451  ? 73.407 69.828  -1.949  0.50 24.64 ? 451  MET A CB  1 
ATOM   3630 C  CB  B MET A 1 451  ? 73.407 69.828  -1.949  0.50 24.14 ? 451  MET A CB  1 
ATOM   3631 C  CG  A MET A 1 451  ? 74.416 69.621  -0.804  0.50 31.09 ? 451  MET A CG  1 
ATOM   3632 C  CG  B MET A 1 451  ? 74.402 69.665  -0.785  0.50 29.98 ? 451  MET A CG  1 
ATOM   3633 S  SD  A MET A 1 451  ? 73.967 70.508  0.779   0.50 39.28 ? 451  MET A SD  1 
ATOM   3634 S  SD  B MET A 1 451  ? 75.986 70.636  -0.994  0.50 38.78 ? 451  MET A SD  1 
ATOM   3635 C  CE  A MET A 1 451  ? 73.204 69.080  1.820   0.50 37.78 ? 451  MET A CE  1 
ATOM   3636 C  CE  B MET A 1 451  ? 76.064 70.844  -2.906  0.50 37.30 ? 451  MET A CE  1 
ATOM   3637 N  N   . ALA A 1 452  ? 70.609 68.900  -3.613  1.00 14.76 ? 452  ALA A N   1 
ATOM   3638 C  CA  . ALA A 1 452  ? 69.677 69.294  -4.674  1.00 15.12 ? 452  ALA A CA  1 
ATOM   3639 C  C   . ALA A 1 452  ? 68.258 69.402  -4.112  1.00 13.04 ? 452  ALA A C   1 
ATOM   3640 O  O   . ALA A 1 452  ? 67.400 69.975  -4.784  1.00 15.80 ? 452  ALA A O   1 
ATOM   3641 C  CB  . ALA A 1 452  ? 69.719 68.284  -5.787  1.00 15.30 ? 452  ALA A CB  1 
ATOM   3642 N  N   . ARG A 1 453  ? 68.004 68.852  -2.923  1.00 12.65 ? 453  ARG A N   1 
ATOM   3643 C  CA  . ARG A 1 453  ? 66.683 68.954  -2.272  1.00 14.50 ? 453  ARG A CA  1 
ATOM   3644 C  C   . ARG A 1 453  ? 65.562 68.377  -3.105  1.00 13.22 ? 453  ARG A C   1 
ATOM   3645 O  O   . ARG A 1 453  ? 64.419 68.843  -2.988  1.00 15.20 ? 453  ARG A O   1 
ATOM   3646 C  CB  . ARG A 1 453  ? 66.391 70.423  -1.911  1.00 16.42 ? 453  ARG A CB  1 
ATOM   3647 C  CG  . ARG A 1 453  ? 67.497 71.041  -1.026  1.00 18.73 ? 453  ARG A CG  1 
ATOM   3648 C  CD  . ARG A 1 453  ? 67.324 72.559  -0.889  1.00 25.88 ? 453  ARG A CD  1 
ATOM   3649 N  NE  . ARG A 1 453  ? 66.159 72.832  -0.067  1.00 24.27 ? 453  ARG A NE  1 
ATOM   3650 C  CZ  . ARG A 1 453  ? 65.670 74.045  0.179   1.00 29.00 ? 453  ARG A CZ  1 
ATOM   3651 N  NH1 . ARG A 1 453  ? 66.245 75.143  -0.346  1.00 27.42 ? 453  ARG A NH1 1 
ATOM   3652 N  NH2 . ARG A 1 453  ? 64.608 74.158  0.957   1.00 27.30 ? 453  ARG A NH2 1 
ATOM   3653 N  N   . ILE A 1 454  ? 65.851 67.362  -3.904  1.00 11.39 ? 454  ILE A N   1 
ATOM   3654 C  CA  . ILE A 1 454  ? 64.837 66.776  -4.756  1.00 10.89 ? 454  ILE A CA  1 
ATOM   3655 C  C   . ILE A 1 454  ? 63.844 66.007  -3.886  1.00 11.52 ? 454  ILE A C   1 
ATOM   3656 O  O   . ILE A 1 454  ? 62.615 66.222  -4.010  1.00 10.81 ? 454  ILE A O   1 
ATOM   3657 C  CB  . ILE A 1 454  ? 65.496 65.820  -5.767  1.00 11.02 ? 454  ILE A CB  1 
ATOM   3658 C  CG1 . ILE A 1 454  ? 66.464 66.580  -6.706  1.00 13.57 ? 454  ILE A CG1 1 
ATOM   3659 C  CG2 . ILE A 1 454  ? 64.403 65.029  -6.535  1.00 12.67 ? 454  ILE A CG2 1 
ATOM   3660 C  CD1 . ILE A 1 454  ? 65.788 67.676  -7.566  1.00 14.54 ? 454  ILE A CD1 1 
ATOM   3661 N  N   . GLU A 1 455  ? 64.301 65.152  -2.998  1.00 11.44 ? 455  GLU A N   1 
ATOM   3662 C  CA  . GLU A 1 455  ? 63.384 64.362  -2.170  1.00 11.51 ? 455  GLU A CA  1 
ATOM   3663 C  C   . GLU A 1 455  ? 62.538 65.270  -1.303  1.00 11.05 ? 455  GLU A C   1 
ATOM   3664 O  O   . GLU A 1 455  ? 61.327 65.012  -1.081  1.00 10.67 ? 455  GLU A O   1 
ATOM   3665 C  CB  . GLU A 1 455  ? 64.154 63.377  -1.258  1.00 13.23 ? 455  GLU A CB  1 
ATOM   3666 C  CG  . GLU A 1 455  ? 64.761 62.187  -1.979  1.00 14.26 ? 455  GLU A CG  1 
ATOM   3667 C  CD  . GLU A 1 455  ? 66.159 62.441  -2.644  1.00 13.74 ? 455  GLU A CD  1 
ATOM   3668 O  OE1 . GLU A 1 455  ? 66.652 63.602  -2.586  1.00 16.61 ? 455  GLU A OE1 1 
ATOM   3669 O  OE2 . GLU A 1 455  ? 66.694 61.453  -3.175  1.00 14.04 ? 455  GLU A OE2 1 
ATOM   3670 N  N   . GLU A 1 456  ? 63.114 66.341  -0.790  1.00 11.91 ? 456  GLU A N   1 
ATOM   3671 C  CA  . GLU A 1 456  ? 62.392 67.254  0.036   1.00 11.11 ? 456  GLU A CA  1 
ATOM   3672 C  C   . GLU A 1 456  ? 61.258 67.892  -0.743  1.00 10.46 ? 456  GLU A C   1 
ATOM   3673 O  O   . GLU A 1 456  ? 60.109 67.994  -0.251  1.00 10.49 ? 456  GLU A O   1 
ATOM   3674 C  CB  . GLU A 1 456  ? 63.379 68.351  0.544   1.00 15.43 ? 456  GLU A CB  1 
ATOM   3675 C  CG  . GLU A 1 456  ? 62.770 69.458  1.291   1.00 16.78 ? 456  GLU A CG  1 
ATOM   3676 C  CD  . GLU A 1 456  ? 63.725 70.638  1.533   1.00 23.70 ? 456  GLU A CD  1 
ATOM   3677 O  OE1 . GLU A 1 456  ? 64.935 70.497  1.275   1.00 24.38 ? 456  GLU A OE1 1 
ATOM   3678 O  OE2 . GLU A 1 456  ? 63.250 71.717  1.982   1.00 25.79 ? 456  GLU A OE2 1 
ATOM   3679 N  N   . ARG A 1 457  ? 61.543 68.376  -1.936  1.00 9.80  ? 457  ARG A N   1 
ATOM   3680 C  CA  . ARG A 1 457  ? 60.463 69.071  -2.698  1.00 10.01 ? 457  ARG A CA  1 
ATOM   3681 C  C   . ARG A 1 457  ? 59.376 68.083  -3.151  1.00 8.44  ? 457  ARG A C   1 
ATOM   3682 O  O   . ARG A 1 457  ? 58.172 68.441  -3.107  1.00 9.36  ? 457  ARG A O   1 
ATOM   3683 C  CB  . ARG A 1 457  ? 61.073 69.837  -3.928  1.00 9.68  ? 457  ARG A CB  1 
ATOM   3684 C  CG  . ARG A 1 457  ? 61.423 71.297  -3.697  1.00 12.86 ? 457  ARG A CG  1 
ATOM   3685 C  CD  . ARG A 1 457  ? 62.312 71.513  -2.560  1.00 16.74 ? 457  ARG A CD  1 
ATOM   3686 N  NE  . ARG A 1 457  ? 62.626 72.951  -2.308  1.00 18.40 ? 457  ARG A NE  1 
ATOM   3687 C  CZ  . ARG A 1 457  ? 63.579 73.686  -2.929  1.00 23.00 ? 457  ARG A CZ  1 
ATOM   3688 N  NH1 . ARG A 1 457  ? 64.394 73.175  -3.895  1.00 19.16 ? 457  ARG A NH1 1 
ATOM   3689 N  NH2 . ARG A 1 457  ? 63.721 74.962  -2.538  1.00 22.63 ? 457  ARG A NH2 1 
ATOM   3690 N  N   . LEU A 1 458  ? 59.774 66.879  -3.523  1.00 8.03  ? 458  LEU A N   1 
ATOM   3691 C  CA  . LEU A 1 458  ? 58.759 65.888  -3.958  1.00 8.42  ? 458  LEU A CA  1 
ATOM   3692 C  C   . LEU A 1 458  ? 57.914 65.452  -2.760  1.00 10.71 ? 458  LEU A C   1 
ATOM   3693 O  O   . LEU A 1 458  ? 56.693 65.252  -2.938  1.00 10.52 ? 458  LEU A O   1 
ATOM   3694 C  CB  . LEU A 1 458  ? 59.464 64.696  -4.564  1.00 9.54  ? 458  LEU A CB  1 
ATOM   3695 C  CG  . LEU A 1 458  ? 60.156 65.021  -5.910  1.00 9.16  ? 458  LEU A CG  1 
ATOM   3696 C  CD1 . LEU A 1 458  ? 60.882 63.749  -6.358  1.00 12.15 ? 458  LEU A CD1 1 
ATOM   3697 C  CD2 . LEU A 1 458  ? 59.045 65.369  -6.994  1.00 10.97 ? 458  LEU A CD2 1 
ATOM   3698 N  N   . GLU A 1 459  ? 58.500 65.320  -1.558  1.00 9.22  ? 459  GLU A N   1 
ATOM   3699 C  CA  . GLU A 1 459  ? 57.678 64.921  -0.412  1.00 8.93  ? 459  GLU A CA  1 
ATOM   3700 C  C   . GLU A 1 459  ? 56.684 66.037  -0.109  1.00 10.00 ? 459  GLU A C   1 
ATOM   3701 O  O   . GLU A 1 459  ? 55.493 65.759  0.176   1.00 9.19  ? 459  GLU A O   1 
ATOM   3702 C  CB  . GLU A 1 459  ? 58.570 64.665  0.808   1.00 11.37 ? 459  GLU A CB  1 
ATOM   3703 C  CG  . GLU A 1 459  ? 57.773 64.458  2.116   1.00 13.51 ? 459  GLU A CG  1 
ATOM   3704 C  CD  . GLU A 1 459  ? 58.648 63.822  3.162   1.00 16.72 ? 459  GLU A CD  1 
ATOM   3705 O  OE1 . GLU A 1 459  ? 59.282 64.598  3.875   1.00 20.98 ? 459  GLU A OE1 1 
ATOM   3706 O  OE2 . GLU A 1 459  ? 58.710 62.568  3.241   1.00 20.42 ? 459  GLU A OE2 1 
ATOM   3707 N  N   . GLN A 1 460  ? 57.099 67.315  -0.174  1.00 8.35  ? 460  GLN A N   1 
ATOM   3708 C  CA  . GLN A 1 460  ? 56.152 68.409  0.055   1.00 9.19  ? 460  GLN A CA  1 
ATOM   3709 C  C   . GLN A 1 460  ? 55.015 68.346  -1.001  1.00 9.81  ? 460  GLN A C   1 
ATOM   3710 O  O   . GLN A 1 460  ? 53.817 68.446  -0.659  1.00 9.97  ? 460  GLN A O   1 
ATOM   3711 C  CB  . GLN A 1 460  ? 56.889 69.744  -0.077  1.00 11.94 ? 460  GLN A CB  1 
ATOM   3712 C  CG  . GLN A 1 460  ? 56.046 70.946  0.087   1.00 17.72 ? 460  GLN A CG  1 
ATOM   3713 C  CD  . GLN A 1 460  ? 56.814 72.238  -0.246  1.00 20.27 ? 460  GLN A CD  1 
ATOM   3714 O  OE1 . GLN A 1 460  ? 56.328 73.314  0.064   1.00 31.41 ? 460  GLN A OE1 1 
ATOM   3715 N  NE2 . GLN A 1 460  ? 57.974 72.124  -0.925  1.00 24.74 ? 460  GLN A NE2 1 
ATOM   3716 N  N   . ALA A 1 461  ? 55.376 68.181  -2.276  1.00 8.17  ? 461  ALA A N   1 
ATOM   3717 C  CA  . ALA A 1 461  ? 54.317 68.141  -3.300  1.00 8.44  ? 461  ALA A CA  1 
ATOM   3718 C  C   . ALA A 1 461  ? 53.375 66.964  -3.091  1.00 8.13  ? 461  ALA A C   1 
ATOM   3719 O  O   . ALA A 1 461  ? 52.133 67.166  -3.203  1.00 8.71  ? 461  ALA A O   1 
ATOM   3720 C  CB  . ALA A 1 461  ? 54.968 68.084  -4.666  1.00 9.30  ? 461  ALA A CB  1 
ATOM   3721 N  N   . ARG A 1 462  ? 53.893 65.776  -2.822  1.00 7.65  ? 462  ARG A N   1 
ATOM   3722 C  CA  . ARG A 1 462  ? 53.001 64.637  -2.608  1.00 7.22  ? 462  ARG A CA  1 
ATOM   3723 C  C   . ARG A 1 462  ? 52.094 64.863  -1.416  1.00 8.27  ? 462  ARG A C   1 
ATOM   3724 O  O   . ARG A 1 462  ? 50.903 64.508  -1.463  1.00 8.33  ? 462  ARG A O   1 
ATOM   3725 C  CB  . ARG A 1 462  ? 53.747 63.324  -2.353  1.00 8.31  ? 462  ARG A CB  1 
ATOM   3726 C  CG  . ARG A 1 462  ? 54.531 62.811  -3.567  1.00 7.87  ? 462  ARG A CG  1 
ATOM   3727 C  CD  . ARG A 1 462  ? 54.987 61.360  -3.295  1.00 9.54  ? 462  ARG A CD  1 
ATOM   3728 N  NE  . ARG A 1 462  ? 55.909 61.266  -2.143  1.00 9.10  ? 462  ARG A NE  1 
ATOM   3729 C  CZ  . ARG A 1 462  ? 57.213 61.411  -2.235  1.00 9.84  ? 462  ARG A CZ  1 
ATOM   3730 N  NH1 . ARG A 1 462  ? 57.800 61.613  -3.402  1.00 11.09 ? 462  ARG A NH1 1 
ATOM   3731 N  NH2 . ARG A 1 462  ? 57.970 61.415  -1.132  1.00 12.69 ? 462  ARG A NH2 1 
ATOM   3732 N  N   . ARG A 1 463  ? 52.600 65.471  -0.355  1.00 8.21  ? 463  ARG A N   1 
ATOM   3733 C  CA  . ARG A 1 463  ? 51.794 65.641  0.860   1.00 8.27  ? 463  ARG A CA  1 
ATOM   3734 C  C   . ARG A 1 463  ? 50.750 66.694  0.676   1.00 8.19  ? 463  ARG A C   1 
ATOM   3735 O  O   . ARG A 1 463  ? 49.632 66.496  1.205   1.00 9.25  ? 463  ARG A O   1 
ATOM   3736 C  CB  . ARG A 1 463  ? 52.702 65.936  2.067   1.00 8.83  ? 463  ARG A CB  1 
ATOM   3737 C  CG  . ARG A 1 463  ? 53.374 64.642  2.504   1.00 9.42  ? 463  ARG A CG  1 
ATOM   3738 C  CD  . ARG A 1 463  ? 54.430 64.828  3.611   1.00 11.18 ? 463  ARG A CD  1 
ATOM   3739 N  NE  . ARG A 1 463  ? 54.934 63.490  3.959   1.00 13.10 ? 463  ARG A NE  1 
ATOM   3740 C  CZ  . ARG A 1 463  ? 55.693 63.243  5.021   1.00 15.16 ? 463  ARG A CZ  1 
ATOM   3741 N  NH1 . ARG A 1 463  ? 56.018 64.259  5.783   1.00 15.92 ? 463  ARG A NH1 1 
ATOM   3742 N  NH2 . ARG A 1 463  ? 56.050 61.978  5.273   1.00 16.54 ? 463  ARG A NH2 1 
ATOM   3743 N  N   . GLU A 1 464  ? 50.993 67.799  -0.034  1.00 7.49  ? 464  GLU A N   1 
ATOM   3744 C  CA  . GLU A 1 464  ? 49.917 68.783  -0.219  1.00 8.66  ? 464  GLU A CA  1 
ATOM   3745 C  C   . GLU A 1 464  ? 48.862 68.263  -1.155  1.00 9.05  ? 464  GLU A C   1 
ATOM   3746 O  O   . GLU A 1 464  ? 47.683 68.528  -0.893  1.00 8.53  ? 464  GLU A O   1 
ATOM   3747 C  CB  . GLU A 1 464  ? 50.427 70.117  -0.762  1.00 10.63 ? 464  GLU A CB  1 
ATOM   3748 C  CG  . GLU A 1 464  ? 51.614 70.773  0.057   1.00 12.39 ? 464  GLU A CG  1 
ATOM   3749 C  CD  . GLU A 1 464  ? 51.299 71.188  1.465   1.00 18.16 ? 464  GLU A CD  1 
ATOM   3750 O  OE1 . GLU A 1 464  ? 50.304 70.771  2.050   1.00 17.27 ? 464  GLU A OE1 1 
ATOM   3751 O  OE2 . GLU A 1 464  ? 52.149 71.948  2.007   1.00 22.73 ? 464  GLU A OE2 1 
ATOM   3752 N  N   . LEU A 1 465  ? 49.234 67.532  -2.206  1.00 7.04  ? 465  LEU A N   1 
ATOM   3753 C  CA  . LEU A 1 465  ? 48.198 66.981  -3.110  1.00 7.36  ? 465  LEU A CA  1 
ATOM   3754 C  C   . LEU A 1 465  ? 47.430 65.907  -2.311  1.00 7.05  ? 465  LEU A C   1 
ATOM   3755 O  O   . LEU A 1 465  ? 46.186 65.803  -2.414  1.00 7.57  ? 465  LEU A O   1 
ATOM   3756 C  CB  . LEU A 1 465  ? 48.864 66.334  -4.340  1.00 7.87  ? 465  LEU A CB  1 
ATOM   3757 C  CG  . LEU A 1 465  ? 47.862 65.679  -5.325  1.00 7.29  ? 465  LEU A CG  1 
ATOM   3758 C  CD1 . LEU A 1 465  ? 46.736 66.655  -5.772  1.00 9.03  ? 465  LEU A CD1 1 
ATOM   3759 C  CD2 . LEU A 1 465  ? 48.634 65.150  -6.530  1.00 8.95  ? 465  LEU A CD2 1 
ATOM   3760 N  N   . SER A 1 466  ? 48.120 65.079  -1.520  1.00 6.88  ? 466  SER A N   1 
ATOM   3761 C  CA  . SER A 1 466  ? 47.443 64.077  -0.705  1.00 6.32  ? 466  SER A CA  1 
ATOM   3762 C  C   . SER A 1 466  ? 46.444 64.674  0.272   1.00 6.82  ? 466  SER A C   1 
ATOM   3763 O  O   . SER A 1 466  ? 45.308 64.149  0.422   1.00 7.37  ? 466  SER A O   1 
ATOM   3764 C  CB  . SER A 1 466  ? 48.459 63.217  0.040   1.00 7.18  ? 466  SER A CB  1 
ATOM   3765 O  OG  . SER A 1 466  ? 49.225 62.408  -0.832  1.00 7.59  ? 466  SER A OG  1 
ATOM   3766 N  N   . LEU A 1 467  ? 46.825 65.761  0.934   1.00 6.61  ? 467  LEU A N   1 
ATOM   3767 C  CA  . LEU A 1 467  ? 45.951 66.412  1.886   1.00 7.15  ? 467  LEU A CA  1 
ATOM   3768 C  C   . LEU A 1 467  ? 44.649 66.843  1.183   1.00 7.01  ? 467  LEU A C   1 
ATOM   3769 O  O   . LEU A 1 467  ? 43.564 66.738  1.765   1.00 7.18  ? 467  LEU A O   1 
ATOM   3770 C  CB  . LEU A 1 467  ? 46.686 67.631  2.478   1.00 8.03  ? 467  LEU A CB  1 
ATOM   3771 C  CG  . LEU A 1 467  ? 45.909 68.252  3.628   1.00 12.37 ? 467  LEU A CG  1 
ATOM   3772 C  CD1 . LEU A 1 467  ? 46.189 67.290  4.918   1.00 16.31 ? 467  LEU A CD1 1 
ATOM   3773 C  CD2 . LEU A 1 467  ? 46.499 69.692  3.891   1.00 13.60 ? 467  LEU A CD2 1 
ATOM   3774 N  N   . PHE A 1 468  ? 44.759 67.354  -0.038  1.00 6.63  ? 468  PHE A N   1 
ATOM   3775 C  CA  . PHE A 1 468  ? 43.580 67.871  -0.754  1.00 6.92  ? 468  PHE A CA  1 
ATOM   3776 C  C   . PHE A 1 468  ? 42.592 66.782  -1.136  1.00 6.19  ? 468  PHE A C   1 
ATOM   3777 O  O   . PHE A 1 468  ? 41.433 67.075  -1.419  1.00 7.81  ? 468  PHE A O   1 
ATOM   3778 C  CB  . PHE A 1 468  ? 43.998 68.688  -1.969  1.00 7.89  ? 468  PHE A CB  1 
ATOM   3779 C  CG  . PHE A 1 468  ? 42.877 69.518  -2.537  1.00 6.63  ? 468  PHE A CG  1 
ATOM   3780 C  CD1 . PHE A 1 468  ? 42.234 70.450  -1.740  1.00 8.48  ? 468  PHE A CD1 1 
ATOM   3781 C  CD2 . PHE A 1 468  ? 42.429 69.354  -3.855  1.00 7.61  ? 468  PHE A CD2 1 
ATOM   3782 C  CE1 . PHE A 1 468  ? 41.165 71.209  -2.215  1.00 7.56  ? 468  PHE A CE1 1 
ATOM   3783 C  CE2 . PHE A 1 468  ? 41.352 70.111  -4.329  1.00 7.53  ? 468  PHE A CE2 1 
ATOM   3784 C  CZ  . PHE A 1 468  ? 40.740 71.021  -3.518  1.00 7.19  ? 468  PHE A CZ  1 
ATOM   3785 N  N   . GLN A 1 469  ? 43.010 65.506  -1.114  1.00 6.23  ? 469  GLN A N   1 
ATOM   3786 C  CA  . GLN A 1 469  ? 42.083 64.413  -1.369  1.00 6.47  ? 469  GLN A CA  1 
ATOM   3787 C  C   . GLN A 1 469  ? 41.067 64.256  -0.236  1.00 6.35  ? 469  GLN A C   1 
ATOM   3788 O  O   . GLN A 1 469  ? 40.082 63.507  -0.428  1.00 6.87  ? 469  GLN A O   1 
ATOM   3789 C  CB  . GLN A 1 469  ? 42.807 63.075  -1.561  1.00 6.98  ? 469  GLN A CB  1 
ATOM   3790 C  CG  . GLN A 1 469  ? 43.892 63.134  -2.669  1.00 6.86  ? 469  GLN A CG  1 
ATOM   3791 C  CD  . GLN A 1 469  ? 43.407 63.823  -3.941  1.00 6.38  ? 469  GLN A CD  1 
ATOM   3792 O  OE1 . GLN A 1 469  ? 44.035 64.852  -4.378  1.00 9.52  ? 469  GLN A OE1 1 
ATOM   3793 N  NE2 . GLN A 1 469  ? 42.368 63.334  -4.531  1.00 5.57  ? 469  GLN A NE2 1 
ATOM   3794 N  N   . HIS A 1 470  ? 41.296 64.890  0.905   1.00 5.95  ? 470  HIS A N   1 
ATOM   3795 C  CA  . HIS A 1 470  ? 40.355 64.842  2.003   1.00 6.01  ? 470  HIS A CA  1 
ATOM   3796 C  C   . HIS A 1 470  ? 38.920 65.117  1.509   1.00 7.58  ? 470  HIS A C   1 
ATOM   3797 O  O   . HIS A 1 470  ? 38.688 65.879  0.578   1.00 7.55  ? 470  HIS A O   1 
ATOM   3798 C  CB  . HIS A 1 470  ? 40.785 65.905  3.054   1.00 7.02  ? 470  HIS A CB  1 
ATOM   3799 C  CG  . HIS A 1 470  ? 39.788 66.062  4.143   1.00 6.70  ? 470  HIS A CG  1 
ATOM   3800 N  ND1 . HIS A 1 470  ? 39.309 67.254  4.649   1.00 10.37 ? 470  HIS A ND1 1 
ATOM   3801 C  CD2 . HIS A 1 470  ? 39.188 65.063  4.838   1.00 6.95  ? 470  HIS A CD2 1 
ATOM   3802 C  CE1 . HIS A 1 470  ? 38.448 66.961  5.630   1.00 6.66  ? 470  HIS A CE1 1 
ATOM   3803 N  NE2 . HIS A 1 470  ? 38.371 65.652  5.755   1.00 13.26 ? 470  HIS A NE2 1 
ATOM   3804 N  N   . HIS A 1 471  ? 37.964 64.481  2.207   1.00 7.31  ? 471  HIS A N   1 
ATOM   3805 C  CA  . HIS A 1 471  ? 36.536 64.628  1.898   1.00 7.92  ? 471  HIS A CA  1 
ATOM   3806 C  C   . HIS A 1 471  ? 35.896 65.996  2.250   1.00 7.19  ? 471  HIS A C   1 
ATOM   3807 O  O   . HIS A 1 471  ? 34.714 66.171  2.020   1.00 8.48  ? 471  HIS A O   1 
ATOM   3808 C  CB  . HIS A 1 471  ? 35.713 63.461  2.482   1.00 7.46  ? 471  HIS A CB  1 
ATOM   3809 C  CG  . HIS A 1 471  ? 35.812 63.359  3.978   1.00 7.32  ? 471  HIS A CG  1 
ATOM   3810 N  ND1 . HIS A 1 471  ? 36.775 62.607  4.656   1.00 8.08  ? 471  HIS A ND1 1 
ATOM   3811 C  CD2 . HIS A 1 471  ? 35.108 63.999  4.955   1.00 7.14  ? 471  HIS A CD2 1 
ATOM   3812 C  CE1 . HIS A 1 471  ? 36.624 62.768  5.970   1.00 9.32  ? 471  HIS A CE1 1 
ATOM   3813 N  NE2 . HIS A 1 471  ? 35.620 63.609  6.183   1.00 6.70  ? 471  HIS A NE2 1 
ATOM   3814 N  N   . ASP A 1 472  ? 36.712 66.992  2.694   1.00 7.93  ? 472  ASP A N   1 
ATOM   3815 C  CA  . ASP A 1 472  ? 36.281 68.397  2.699   1.00 8.09  ? 472  ASP A CA  1 
ATOM   3816 C  C   . ASP A 1 472  ? 37.255 69.249  1.867   1.00 9.28  ? 472  ASP A C   1 
ATOM   3817 O  O   . ASP A 1 472  ? 37.154 70.484  1.889   1.00 9.23  ? 472  ASP A O   1 
ATOM   3818 C  CB  . ASP A 1 472  ? 36.152 68.995  4.118   1.00 8.34  ? 472  ASP A CB  1 
ATOM   3819 C  CG  . ASP A 1 472  ? 35.099 68.283  4.922   1.00 8.00  ? 472  ASP A CG  1 
ATOM   3820 O  OD1 . ASP A 1 472  ? 33.917 68.307  4.471   1.00 8.64  ? 472  ASP A OD1 1 
ATOM   3821 O  OD2 . ASP A 1 472  ? 35.459 67.686  5.962   1.00 9.34  ? 472  ASP A OD2 1 
ATOM   3822 N  N   . GLY A 1 473  ? 38.171 68.634  1.113   1.00 7.67  ? 473  GLY A N   1 
ATOM   3823 C  CA  . GLY A 1 473  ? 39.155 69.370  0.292   1.00 7.44  ? 473  GLY A CA  1 
ATOM   3824 C  C   . GLY A 1 473  ? 38.630 69.456  -1.129  1.00 6.92  ? 473  GLY A C   1 
ATOM   3825 O  O   . GLY A 1 473  ? 37.877 70.388  -1.482  1.00 7.39  ? 473  GLY A O   1 
ATOM   3826 N  N   . ILE A 1 474  ? 38.934 68.418  -1.936  1.00 6.60  ? 474  ILE A N   1 
ATOM   3827 C  CA  . ILE A 1 474  ? 38.515 68.422  -3.327  1.00 7.58  ? 474  ILE A CA  1 
ATOM   3828 C  C   . ILE A 1 474  ? 36.980 68.527  -3.461  1.00 7.59  ? 474  ILE A C   1 
ATOM   3829 O  O   . ILE A 1 474  ? 36.495 69.017  -4.487  1.00 8.32  ? 474  ILE A O   1 
ATOM   3830 C  CB  . ILE A 1 474  ? 39.077 67.151  -4.035  1.00 6.18  ? 474  ILE A CB  1 
ATOM   3831 C  CG1 . ILE A 1 474  ? 38.839 67.239  -5.540  1.00 8.05  ? 474  ILE A CG1 1 
ATOM   3832 C  CG2 . ILE A 1 474  ? 38.508 65.830  -3.417  1.00 8.07  ? 474  ILE A CG2 1 
ATOM   3833 C  CD1 . ILE A 1 474  ? 39.579 66.094  -6.319  1.00 9.18  ? 474  ILE A CD1 1 
ATOM   3834 N  N   . THR A 1 475  ? 36.230 68.101  -2.460  1.00 7.24  ? 475  THR A N   1 
ATOM   3835 C  CA  . THR A 1 475  ? 34.770 68.183  -2.479  1.00 7.44  ? 475  THR A CA  1 
ATOM   3836 C  C   . THR A 1 475  ? 34.247 69.629  -2.477  1.00 7.27  ? 475  THR A C   1 
ATOM   3837 O  O   . THR A 1 475  ? 33.062 69.837  -2.825  1.00 8.04  ? 475  THR A O   1 
ATOM   3838 C  CB  . THR A 1 475  ? 34.215 67.529  -1.218  1.00 7.95  ? 475  THR A CB  1 
ATOM   3839 O  OG1 . THR A 1 475  ? 34.764 68.256  -0.115  1.00 8.12  ? 475  THR A OG1 1 
ATOM   3840 C  CG2 . THR A 1 475  ? 34.582 66.031  -1.083  1.00 8.74  ? 475  THR A CG2 1 
ATOM   3841 N  N   . GLY A 1 476  ? 35.055 70.620  -2.101  1.00 7.11  ? 476  GLY A N   1 
ATOM   3842 C  CA  . GLY A 1 476  ? 34.527 71.976  -2.070  1.00 7.38  ? 476  GLY A CA  1 
ATOM   3843 C  C   . GLY A 1 476  ? 33.540 72.212  -0.929  1.00 7.91  ? 476  GLY A C   1 
ATOM   3844 O  O   . GLY A 1 476  ? 32.648 73.050  -1.088  1.00 8.72  ? 476  GLY A O   1 
ATOM   3845 N  N   . THR A 1 477  ? 33.691 71.500  0.185   1.00 7.17  ? 477  THR A N   1 
ATOM   3846 C  CA  . THR A 1 477  ? 32.801 71.635  1.302   1.00 8.10  ? 477  THR A CA  1 
ATOM   3847 C  C   . THR A 1 477  ? 33.468 72.256  2.527   1.00 8.51  ? 477  THR A C   1 
ATOM   3848 O  O   . THR A 1 477  ? 32.924 72.120  3.647   1.00 10.80 ? 477  THR A O   1 
ATOM   3849 C  CB  . THR A 1 477  ? 32.143 70.279  1.670   1.00 8.06  ? 477  THR A CB  1 
ATOM   3850 O  OG1 . THR A 1 477  ? 33.163 69.298  1.930   1.00 8.94  ? 477  THR A OG1 1 
ATOM   3851 C  CG2 . THR A 1 477  ? 31.290 69.763  0.486   1.00 8.46  ? 477  THR A CG2 1 
ATOM   3852 N  N   . ALA A 1 478  ? 34.569 73.004  2.374   1.00 8.26  ? 478  ALA A N   1 
ATOM   3853 C  CA  . ALA A 1 478  ? 35.217 73.641  3.548   1.00 8.42  ? 478  ALA A CA  1 
ATOM   3854 C  C   . ALA A 1 478  ? 34.897 75.134  3.603   1.00 8.68  ? 478  ALA A C   1 
ATOM   3855 O  O   . ALA A 1 478  ? 34.390 75.744  2.667   1.00 9.36  ? 478  ALA A O   1 
ATOM   3856 C  CB  . ALA A 1 478  ? 36.774 73.431  3.497   1.00 10.18 ? 478  ALA A CB  1 
ATOM   3857 N  N   . LYS A 1 479  ? 35.194 75.740  4.758   1.00 9.21  ? 479  LYS A N   1 
ATOM   3858 C  CA  . LYS A 1 479  ? 34.976 77.202  4.899   1.00 10.56 ? 479  LYS A CA  1 
ATOM   3859 C  C   . LYS A 1 479  ? 35.918 77.936  3.966   1.00 9.49  ? 479  LYS A C   1 
ATOM   3860 O  O   . LYS A 1 479  ? 36.996 77.431  3.600   1.00 9.19  ? 479  LYS A O   1 
ATOM   3861 C  CB  . LYS A 1 479  ? 35.223 77.646  6.353   1.00 11.25 ? 479  LYS A CB  1 
ATOM   3862 C  CG  . LYS A 1 479  ? 34.007 77.312  7.275   1.00 17.96 ? 479  LYS A CG  1 
ATOM   3863 C  CD  . LYS A 1 479  ? 33.848 78.407  8.329   1.00 23.59 ? 479  LYS A CD  1 
ATOM   3864 C  CE  . LYS A 1 479  ? 32.623 78.149  9.231   1.00 22.20 ? 479  LYS A CE  1 
ATOM   3865 N  NZ  . LYS A 1 479  ? 31.295 78.676  8.717   1.00 22.96 ? 479  LYS A NZ  1 
ATOM   3866 N  N   . THR A 1 480  ? 35.535 79.163  3.583   1.00 10.57 ? 480  THR A N   1 
ATOM   3867 C  CA  . THR A 1 480  ? 36.341 79.938  2.668   1.00 10.40 ? 480  THR A CA  1 
ATOM   3868 C  C   . THR A 1 480  ? 37.825 80.036  3.024   1.00 9.86  ? 480  THR A C   1 
ATOM   3869 O  O   . THR A 1 480  ? 38.708 79.826  2.171   1.00 10.65 ? 480  THR A O   1 
ATOM   3870 C  CB  . THR A 1 480  ? 35.767 81.371  2.571   1.00 13.34 ? 480  THR A CB  1 
ATOM   3871 O  OG1 . THR A 1 480  ? 34.434 81.255  2.072   1.00 17.23 ? 480  THR A OG1 1 
ATOM   3872 C  CG2 . THR A 1 480  ? 36.600 82.282  1.625   1.00 16.52 ? 480  THR A CG2 1 
ATOM   3873 N  N   . HIS A 1 481  ? 38.166 80.328  4.287   1.00 10.24 ? 481  HIS A N   1 
ATOM   3874 C  CA  . HIS A 1 481  ? 39.593 80.473  4.600   1.00 9.24  ? 481  HIS A CA  1 
ATOM   3875 C  C   . HIS A 1 481  ? 40.340 79.137  4.573   1.00 10.68 ? 481  HIS A C   1 
ATOM   3876 O  O   . HIS A 1 481  ? 41.548 79.101  4.389   1.00 10.72 ? 481  HIS A O   1 
ATOM   3877 C  CB  . HIS A 1 481  ? 39.791 81.179  5.981   1.00 11.02 ? 481  HIS A CB  1 
ATOM   3878 C  CG  . HIS A 1 481  ? 39.660 80.277  7.173   1.00 10.92 ? 481  HIS A CG  1 
ATOM   3879 N  ND1 . HIS A 1 481  ? 38.447 79.820  7.662   1.00 14.36 ? 481  HIS A ND1 1 
ATOM   3880 C  CD2 . HIS A 1 481  ? 40.612 79.773  7.997   1.00 11.42 ? 481  HIS A CD2 1 
ATOM   3881 C  CE1 . HIS A 1 481  ? 38.667 79.087  8.736   1.00 14.01 ? 481  HIS A CE1 1 
ATOM   3882 N  NE2 . HIS A 1 481  ? 39.971 79.040  8.953   1.00 12.82 ? 481  HIS A NE2 1 
ATOM   3883 N  N   . VAL A 1 482  ? 39.593 78.027  4.707   1.00 10.49 ? 482  VAL A N   1 
ATOM   3884 C  CA  . VAL A 1 482  ? 40.219 76.713  4.606   1.00 9.39  ? 482  VAL A CA  1 
ATOM   3885 C  C   . VAL A 1 482  ? 40.482 76.371  3.144   1.00 8.30  ? 482  VAL A C   1 
ATOM   3886 O  O   . VAL A 1 482  ? 41.549 75.820  2.800   1.00 9.24  ? 482  VAL A O   1 
ATOM   3887 C  CB  . VAL A 1 482  ? 39.296 75.661  5.283   1.00 7.82  ? 482  VAL A CB  1 
ATOM   3888 C  CG1 . VAL A 1 482  ? 39.949 74.241  5.209   1.00 8.98  ? 482  VAL A CG1 1 
ATOM   3889 C  CG2 . VAL A 1 482  ? 39.094 76.025  6.786   1.00 10.19 ? 482  VAL A CG2 1 
ATOM   3890 N  N   . VAL A 1 483  ? 39.545 76.711  2.259   1.00 8.01  ? 483  VAL A N   1 
ATOM   3891 C  CA  . VAL A 1 483  ? 39.788 76.556  0.834   1.00 9.21  ? 483  VAL A CA  1 
ATOM   3892 C  C   . VAL A 1 483  ? 41.037 77.335  0.420   1.00 8.56  ? 483  VAL A C   1 
ATOM   3893 O  O   . VAL A 1 483  ? 41.877 76.841  -0.329  1.00 9.20  ? 483  VAL A O   1 
ATOM   3894 C  CB  . VAL A 1 483  ? 38.550 77.082  0.027   1.00 8.04  ? 483  VAL A CB  1 
ATOM   3895 C  CG1 . VAL A 1 483  ? 38.765 77.054  -1.456  1.00 11.42 ? 483  VAL A CG1 1 
ATOM   3896 C  CG2 . VAL A 1 483  ? 37.339 76.157  0.328   1.00 10.19 ? 483  VAL A CG2 1 
ATOM   3897 N  N   . VAL A 1 484  ? 41.202 78.555  0.982   1.00 9.41  ? 484  VAL A N   1 
ATOM   3898 C  CA  . VAL A 1 484  ? 42.394 79.359  0.656   1.00 11.64 ? 484  VAL A CA  1 
ATOM   3899 C  C   . VAL A 1 484  ? 43.645 78.651  1.139   1.00 10.29 ? 484  VAL A C   1 
ATOM   3900 O  O   . VAL A 1 484  ? 44.661 78.640  0.409   1.00 9.99  ? 484  VAL A O   1 
ATOM   3901 C  CB  . VAL A 1 484  ? 42.265 80.771  1.272   1.00 11.29 ? 484  VAL A CB  1 
ATOM   3902 C  CG1 . VAL A 1 484  ? 43.637 81.524  1.136   1.00 13.92 ? 484  VAL A CG1 1 
ATOM   3903 C  CG2 . VAL A 1 484  ? 41.180 81.558  0.522   1.00 14.61 ? 484  VAL A CG2 1 
ATOM   3904 N  N   . ASP A 1 485  ? 43.603 78.038  2.310   1.00 9.43  ? 485  ASP A N   1 
ATOM   3905 C  CA  . ASP A 1 485  ? 44.754 77.290  2.799   1.00 8.37  ? 485  ASP A CA  1 
ATOM   3906 C  C   . ASP A 1 485  ? 45.115 76.131  1.873   1.00 9.89  ? 485  ASP A C   1 
ATOM   3907 O  O   . ASP A 1 485  ? 46.299 75.897  1.548   1.00 9.49  ? 485  ASP A O   1 
ATOM   3908 C  CB  . ASP A 1 485  ? 44.495 76.766  4.235   1.00 9.52  ? 485  ASP A CB  1 
ATOM   3909 C  CG  . ASP A 1 485  ? 45.731 76.134  4.850   1.00 10.65 ? 485  ASP A CG  1 
ATOM   3910 O  OD1 . ASP A 1 485  ? 45.751 74.954  5.225   1.00 11.74 ? 485  ASP A OD1 1 
ATOM   3911 O  OD2 . ASP A 1 485  ? 46.760 76.873  4.946   1.00 16.85 ? 485  ASP A OD2 1 
ATOM   3912 N  N   . TYR A 1 486  ? 44.118 75.354  1.434   1.00 8.74  ? 486  TYR A N   1 
ATOM   3913 C  CA  . TYR A 1 486  ? 44.409 74.272  0.471   1.00 7.56  ? 486  TYR A CA  1 
ATOM   3914 C  C   . TYR A 1 486  ? 44.992 74.808  -0.829  1.00 8.69  ? 486  TYR A C   1 
ATOM   3915 O  O   . TYR A 1 486  ? 45.930 74.206  -1.359  1.00 9.16  ? 486  TYR A O   1 
ATOM   3916 C  CB  . TYR A 1 486  ? 43.132 73.473  0.133   1.00 8.77  ? 486  TYR A CB  1 
ATOM   3917 C  CG  . TYR A 1 486  ? 42.547 72.626  1.265   1.00 8.35  ? 486  TYR A CG  1 
ATOM   3918 C  CD1 . TYR A 1 486  ? 41.174 72.650  1.495   1.00 8.95  ? 486  TYR A CD1 1 
ATOM   3919 C  CD2 . TYR A 1 486  ? 43.358 71.777  2.042   1.00 10.84 ? 486  TYR A CD2 1 
ATOM   3920 C  CE1 . TYR A 1 486  ? 40.591 71.846  2.487   1.00 9.89  ? 486  TYR A CE1 1 
ATOM   3921 C  CE2 . TYR A 1 486  ? 42.764 70.939  3.052   1.00 10.86 ? 486  TYR A CE2 1 
ATOM   3922 C  CZ  . TYR A 1 486  ? 41.392 71.018  3.226   1.00 8.12  ? 486  TYR A CZ  1 
ATOM   3923 O  OH  . TYR A 1 486  ? 40.781 70.199  4.150   1.00 10.94 ? 486  TYR A OH  1 
ATOM   3924 N  N   . GLU A 1 487  ? 44.461 75.926  -1.318  1.00 8.57  ? 487  GLU A N   1 
ATOM   3925 C  CA  . GLU A 1 487  ? 44.960 76.498  -2.542  1.00 9.61  ? 487  GLU A CA  1 
ATOM   3926 C  C   . GLU A 1 487  ? 46.438 76.925  -2.380  1.00 9.81  ? 487  GLU A C   1 
ATOM   3927 O  O   . GLU A 1 487  ? 47.275 76.680  -3.265  1.00 9.90  ? 487  GLU A O   1 
ATOM   3928 C  CB  . GLU A 1 487  ? 44.139 77.713  -2.946  1.00 10.76 ? 487  GLU A CB  1 
ATOM   3929 C  CG  . GLU A 1 487  ? 44.489 78.260  -4.325  1.00 11.67 ? 487  GLU A CG  1 
ATOM   3930 C  CD  . GLU A 1 487  ? 43.628 79.433  -4.800  1.00 18.47 ? 487  GLU A CD  1 
ATOM   3931 O  OE1 . GLU A 1 487  ? 42.503 79.611  -4.341  1.00 18.97 ? 487  GLU A OE1 1 
ATOM   3932 O  OE2 . GLU A 1 487  ? 44.137 80.185  -5.668  1.00 20.99 ? 487  GLU A OE2 1 
ATOM   3933 N  N   . GLN A 1 488  ? 46.769 77.584  -1.270  1.00 9.43  ? 488  GLN A N   1 
ATOM   3934 C  CA  . GLN A 1 488  ? 48.167 78.037  -1.048  1.00 10.32 ? 488  GLN A CA  1 
ATOM   3935 C  C   . GLN A 1 488  ? 49.072 76.834  -0.941  1.00 10.35 ? 488  GLN A C   1 
ATOM   3936 O  O   . GLN A 1 488  ? 50.192 76.840  -1.490  1.00 10.58 ? 488  GLN A O   1 
ATOM   3937 C  CB  . GLN A 1 488  ? 48.252 78.828  0.281   1.00 14.85 ? 488  GLN A CB  1 
ATOM   3938 C  CG  . GLN A 1 488  ? 47.526 80.171  0.183   1.00 23.99 ? 488  GLN A CG  1 
ATOM   3939 C  CD  . GLN A 1 488  ? 47.654 81.053  1.441   1.00 32.93 ? 488  GLN A CD  1 
ATOM   3940 O  OE1 . GLN A 1 488  ? 47.435 82.262  1.369   1.00 41.49 ? 488  GLN A OE1 1 
ATOM   3941 N  NE2 . GLN A 1 488  ? 47.981 80.455  2.578   1.00 37.95 ? 488  GLN A NE2 1 
ATOM   3942 N  N   . ARG A 1 489  ? 48.660 75.784  -0.251  1.00 8.80  ? 489  ARG A N   1 
ATOM   3943 C  CA  . ARG A 1 489  ? 49.463 74.582  -0.167  1.00 9.63  ? 489  ARG A CA  1 
ATOM   3944 C  C   . ARG A 1 489  ? 49.675 73.988  -1.558  1.00 9.91  ? 489  ARG A C   1 
ATOM   3945 O  O   . ARG A 1 489  ? 50.789 73.602  -1.915  1.00 8.80  ? 489  ARG A O   1 
ATOM   3946 C  CB  . ARG A 1 489  ? 48.742 73.571  0.748   1.00 9.26  ? 489  ARG A CB  1 
ATOM   3947 C  CG  . ARG A 1 489  ? 48.843 73.936  2.179   1.00 8.50  ? 489  ARG A CG  1 
ATOM   3948 C  CD  . ARG A 1 489  ? 47.870 73.026  2.992   1.00 9.81  ? 489  ARG A CD  1 
ATOM   3949 N  NE  . ARG A 1 489  ? 47.951 73.179  4.461   1.00 9.97  ? 489  ARG A NE  1 
ATOM   3950 C  CZ  . ARG A 1 489  ? 48.831 72.524  5.227   1.00 11.83 ? 489  ARG A CZ  1 
ATOM   3951 N  NH1 . ARG A 1 489  ? 49.707 71.674  4.706   1.00 13.99 ? 489  ARG A NH1 1 
ATOM   3952 N  NH2 . ARG A 1 489  ? 48.805 72.764  6.551   1.00 12.82 ? 489  ARG A NH2 1 
ATOM   3953 N  N   . MET A 1 490  ? 48.634 73.907  -2.388  1.00 8.25  ? 490  MET A N   1 
ATOM   3954 C  CA  . MET A 1 490  ? 48.787 73.359  -3.732  1.00 8.34  ? 490  MET A CA  1 
ATOM   3955 C  C   . MET A 1 490  ? 49.661 74.251  -4.612  1.00 8.50  ? 490  MET A C   1 
ATOM   3956 O  O   . MET A 1 490  ? 50.402 73.744  -5.459  1.00 9.28  ? 490  MET A O   1 
ATOM   3957 C  CB  . MET A 1 490  ? 47.447 73.107  -4.413  1.00 8.42  ? 490  MET A CB  1 
ATOM   3958 C  CG  . MET A 1 490  ? 46.726 71.902  -3.769  1.00 9.75  ? 490  MET A CG  1 
ATOM   3959 S  SD  . MET A 1 490  ? 45.376 71.230  -4.857  1.00 12.76 ? 490  MET A SD  1 
ATOM   3960 C  CE  . MET A 1 490  ? 44.119 72.397  -4.462  1.00 13.69 ? 490  MET A CE  1 
ATOM   3961 N  N   . GLN A 1 491  ? 49.612 75.574  -4.427  1.00 8.59  ? 491  GLN A N   1 
ATOM   3962 C  CA  . GLN A 1 491  ? 50.497 76.469  -5.209  1.00 9.16  ? 491  GLN A CA  1 
ATOM   3963 C  C   . GLN A 1 491  ? 51.962 76.216  -4.857  1.00 10.25 ? 491  GLN A C   1 
ATOM   3964 O  O   . GLN A 1 491  ? 52.820 76.144  -5.743  1.00 10.44 ? 491  GLN A O   1 
ATOM   3965 C  CB  . GLN A 1 491  ? 50.194 77.931  -4.883  1.00 12.32 ? 491  GLN A CB  1 
ATOM   3966 C  CG  . GLN A 1 491  ? 50.946 78.866  -5.819  1.00 18.34 ? 491  GLN A CG  1 
ATOM   3967 C  CD  . GLN A 1 491  ? 50.656 78.582  -7.284  1.00 29.41 ? 491  GLN A CD  1 
ATOM   3968 O  OE1 . GLN A 1 491  ? 51.524 78.077  -8.043  1.00 32.19 ? 491  GLN A OE1 1 
ATOM   3969 N  NE2 . GLN A 1 491  ? 49.439 78.868  -7.684  1.00 34.17 ? 491  GLN A NE2 1 
ATOM   3970 N  N   . GLU A 1 492  ? 52.240 76.003  -3.583  1.00 9.59  ? 492  GLU A N   1 
ATOM   3971 C  CA  . GLU A 1 492  ? 53.597 75.698  -3.179  1.00 10.71 ? 492  GLU A CA  1 
ATOM   3972 C  C   . GLU A 1 492  ? 54.004 74.382  -3.770  1.00 10.42 ? 492  GLU A C   1 
ATOM   3973 O  O   . GLU A 1 492  ? 55.153 74.209  -4.214  1.00 10.47 ? 492  GLU A O   1 
ATOM   3974 C  CB  . GLU A 1 492  ? 53.719 75.637  -1.640  1.00 12.49 ? 492  GLU A CB  1 
ATOM   3975 C  CG  . GLU A 1 492  ? 53.626 77.044  -0.949  1.00 19.07 ? 492  GLU A CG  1 
ATOM   3976 C  CD  . GLU A 1 492  ? 54.581 78.106  -1.553  1.00 27.89 ? 492  GLU A CD  1 
ATOM   3977 O  OE1 . GLU A 1 492  ? 54.094 79.188  -1.938  1.00 34.24 ? 492  GLU A OE1 1 
ATOM   3978 O  OE2 . GLU A 1 492  ? 55.825 77.894  -1.650  1.00 32.46 ? 492  GLU A OE2 1 
ATOM   3979 N  N   . ALA A 1 493  ? 53.084 73.412  -3.777  1.00 9.03  ? 493  ALA A N   1 
ATOM   3980 C  CA  . ALA A 1 493  ? 53.405 72.117  -4.372  1.00 8.60  ? 493  ALA A CA  1 
ATOM   3981 C  C   . ALA A 1 493  ? 53.713 72.244  -5.894  1.00 7.86  ? 493  ALA A C   1 
ATOM   3982 O  O   . ALA A 1 493  ? 54.610 71.554  -6.394  1.00 8.42  ? 493  ALA A O   1 
ATOM   3983 C  CB  . ALA A 1 493  ? 52.192 71.124  -4.148  1.00 8.23  ? 493  ALA A CB  1 
ATOM   3984 N  N   . LEU A 1 494  ? 52.922 73.044  -6.620  1.00 8.22  ? 494  LEU A N   1 
ATOM   3985 C  CA  . LEU A 1 494  ? 53.190 73.253  -8.039  1.00 8.44  ? 494  LEU A CA  1 
ATOM   3986 C  C   . LEU A 1 494  ? 54.597 73.844  -8.225  1.00 8.83  ? 494  LEU A C   1 
ATOM   3987 O  O   . LEU A 1 494  ? 55.298 73.420  -9.134  1.00 9.81  ? 494  LEU A O   1 
ATOM   3988 C  CB  . LEU A 1 494  ? 52.125 74.169  -8.672  1.00 10.42 ? 494  LEU A CB  1 
ATOM   3989 C  CG  . LEU A 1 494  ? 50.765 73.516  -8.873  1.00 10.33 ? 494  LEU A CG  1 
ATOM   3990 C  CD1 . LEU A 1 494  ? 49.732 74.625  -9.202  1.00 12.04 ? 494  LEU A CD1 1 
ATOM   3991 C  CD2 . LEU A 1 494  ? 50.838 72.488  -9.983  1.00 10.76 ? 494  LEU A CD2 1 
ATOM   3992 N  N   . LYS A 1 495  ? 54.981 74.803  -7.396  1.00 9.81  ? 495  LYS A N   1 
ATOM   3993 C  CA  . LYS A 1 495  ? 56.330 75.401  -7.506  1.00 8.51  ? 495  LYS A CA  1 
ATOM   3994 C  C   . LYS A 1 495  ? 57.391 74.366  -7.192  1.00 9.87  ? 495  LYS A C   1 
ATOM   3995 O  O   . LYS A 1 495  ? 58.441 74.329  -7.869  1.00 10.21 ? 495  LYS A O   1 
ATOM   3996 C  CB  . LYS A 1 495  ? 56.448 76.610  -6.560  1.00 12.33 ? 495  LYS A CB  1 
ATOM   3997 C  CG  . LYS A 1 495  ? 55.595 77.810  -7.028  1.00 17.20 ? 495  LYS A CG  1 
ATOM   3998 C  CD  . LYS A 1 495  ? 55.821 79.073  -6.167  1.00 26.49 ? 495  LYS A CD  1 
ATOM   3999 C  CE  . LYS A 1 495  ? 55.550 78.796  -4.708  1.00 32.65 ? 495  LYS A CE  1 
ATOM   4000 N  NZ  . LYS A 1 495  ? 55.775 79.998  -3.783  1.00 38.87 ? 495  LYS A NZ  1 
ATOM   4001 N  N   . ALA A 1 496  ? 57.141 73.482  -6.229  1.00 7.99  ? 496  ALA A N   1 
ATOM   4002 C  CA  . ALA A 1 496  ? 58.102 72.459  -5.926  1.00 8.46  ? 496  ALA A CA  1 
ATOM   4003 C  C   . ALA A 1 496  ? 58.276 71.527  -7.135  1.00 9.38  ? 496  ALA A C   1 
ATOM   4004 O  O   . ALA A 1 496  ? 59.397 71.117  -7.508  1.00 9.00  ? 496  ALA A O   1 
ATOM   4005 C  CB  . ALA A 1 496  ? 57.617 71.644  -4.658  1.00 9.11  ? 496  ALA A CB  1 
ATOM   4006 N  N   . CYS A 1 497  ? 57.166 71.128  -7.759  1.00 7.92  ? 497  CYS A N   1 
ATOM   4007 C  CA  . CYS A 1 497  ? 57.229 70.249  -8.931  1.00 8.81  ? 497  CYS A CA  1 
ATOM   4008 C  C   . CYS A 1 497  ? 57.981 70.943  -10.069 1.00 8.86  ? 497  CYS A C   1 
ATOM   4009 O  O   . CYS A 1 497  ? 58.780 70.303  -10.728 1.00 9.06  ? 497  CYS A O   1 
ATOM   4010 C  CB  . CYS A 1 497  ? 55.818 69.832  -9.414  1.00 7.69  ? 497  CYS A CB  1 
ATOM   4011 S  SG  . CYS A 1 497  ? 54.938 68.754  -8.329  1.00 8.93  ? 497  CYS A SG  1 
ATOM   4012 N  N   . GLN A 1 498  ? 57.710 72.210  -10.296 1.00 8.19  ? 498  GLN A N   1 
ATOM   4013 C  CA  . GLN A 1 498  ? 58.413 72.923  -11.379 1.00 9.42  ? 498  GLN A CA  1 
ATOM   4014 C  C   . GLN A 1 498  ? 59.918 72.892  -11.115 1.00 9.34  ? 498  GLN A C   1 
ATOM   4015 O  O   . GLN A 1 498  ? 60.694 72.676  -12.075 1.00 9.77  ? 498  GLN A O   1 
ATOM   4016 C  CB  . GLN A 1 498  ? 57.933 74.376  -11.464 1.00 10.63 ? 498  GLN A CB  1 
ATOM   4017 C  CG  . GLN A 1 498  ? 58.770 75.187  -12.450 1.00 17.76 ? 498  GLN A CG  1 
ATOM   4018 C  CD  . GLN A 1 498  ? 58.326 76.628  -12.550 1.00 20.79 ? 498  GLN A CD  1 
ATOM   4019 O  OE1 . GLN A 1 498  ? 58.233 77.349  -11.490 1.00 25.76 ? 498  GLN A OE1 1 
ATOM   4020 N  NE2 . GLN A 1 498  ? 58.097 77.109  -13.773 1.00 16.96 ? 498  GLN A NE2 1 
ATOM   4021 N  N   . MET A 1 499  ? 60.347 73.168  -9.888  1.00 8.80  ? 499  MET A N   1 
ATOM   4022 C  CA  . MET A 1 499  ? 61.771 73.162  -9.575  1.00 9.20  ? 499  MET A CA  1 
ATOM   4023 C  C   . MET A 1 499  ? 62.398 71.837  -9.888  1.00 9.76  ? 499  MET A C   1 
ATOM   4024 O  O   . MET A 1 499  ? 63.433 71.771  -10.561 1.00 10.21 ? 499  MET A O   1 
ATOM   4025 C  CB  . MET A 1 499  ? 61.948 73.524  -8.109  1.00 10.92 ? 499  MET A CB  1 
ATOM   4026 C  CG  . MET A 1 499  ? 63.394 73.398  -7.600  1.00 13.50 ? 499  MET A CG  1 
ATOM   4027 S  SD  . MET A 1 499  ? 64.691 74.366  -8.425  1.00 19.89 ? 499  MET A SD  1 
ATOM   4028 C  CE  . MET A 1 499  ? 64.011 75.839  -8.016  1.00 18.75 ? 499  MET A CE  1 
ATOM   4029 N  N   . VAL A 1 500  ? 61.768 70.739  -9.442  1.00 7.98  ? 500  VAL A N   1 
ATOM   4030 C  CA  . VAL A 1 500  ? 62.322 69.420  -9.653  1.00 7.73  ? 500  VAL A CA  1 
ATOM   4031 C  C   . VAL A 1 500  ? 62.348 69.109  -11.150 1.00 8.02  ? 500  VAL A C   1 
ATOM   4032 O  O   . VAL A 1 500  ? 63.357 68.557  -11.668 1.00 8.78  ? 500  VAL A O   1 
ATOM   4033 C  CB  . VAL A 1 500  ? 61.518 68.373  -8.880  1.00 8.08  ? 500  VAL A CB  1 
ATOM   4034 C  CG1 . VAL A 1 500  ? 61.956 66.991  -9.299  1.00 9.56  ? 500  VAL A CG1 1 
ATOM   4035 C  CG2 . VAL A 1 500  ? 61.725 68.578  -7.372  1.00 10.37 ? 500  VAL A CG2 1 
ATOM   4036 N  N   . MET A 1 501  ? 61.260 69.393  -11.858 1.00 8.05  ? 501  MET A N   1 
ATOM   4037 C  CA  . MET A 1 501  ? 61.181 69.102  -13.292 1.00 8.63  ? 501  MET A CA  1 
ATOM   4038 C  C   . MET A 1 501  ? 62.272 69.850  -14.052 1.00 9.11  ? 501  MET A C   1 
ATOM   4039 O  O   . MET A 1 501  ? 62.933 69.235  -14.917 1.00 8.78  ? 501  MET A O   1 
ATOM   4040 C  CB  . MET A 1 501  ? 59.814 69.497  -13.844 1.00 10.23 ? 501  MET A CB  1 
ATOM   4041 C  CG  . MET A 1 501  ? 58.691 68.578  -13.331 1.00 9.25  ? 501  MET A CG  1 
ATOM   4042 S  SD  . MET A 1 501  ? 57.009 69.251  -13.555 1.00 14.81 ? 501  MET A SD  1 
ATOM   4043 C  CE  . MET A 1 501  ? 57.042 68.833  -14.884 1.00 12.83 ? 501  MET A CE  1 
ATOM   4044 N  N   . GLN A 1 502  ? 62.455 71.150  -13.804 1.00 9.76  ? 502  GLN A N   1 
ATOM   4045 C  CA  . GLN A 1 502  ? 63.418 71.903  -14.624 1.00 8.57  ? 502  GLN A CA  1 
ATOM   4046 C  C   . GLN A 1 502  ? 64.847 71.518  -14.291 1.00 10.63 ? 502  GLN A C   1 
ATOM   4047 O  O   . GLN A 1 502  ? 65.669 71.442  -15.224 1.00 9.96  ? 502  GLN A O   1 
ATOM   4048 C  CB  . GLN A 1 502  ? 63.130 73.377  -14.528 1.00 11.76 ? 502  GLN A CB  1 
ATOM   4049 C  CG  . GLN A 1 502  ? 63.323 74.044  -13.177 1.00 11.90 ? 502  GLN A CG  1 
ATOM   4050 C  CD  . GLN A 1 502  ? 64.773 74.502  -12.945 1.00 13.25 ? 502  GLN A CD  1 
ATOM   4051 O  OE1 . GLN A 1 502  ? 65.581 74.647  -13.942 1.00 13.05 ? 502  GLN A OE1 1 
ATOM   4052 N  NE2 . GLN A 1 502  ? 65.128 74.758  -11.681 1.00 13.43 ? 502  GLN A NE2 1 
ATOM   4053 N  N   . GLN A 1 503  ? 65.156 71.208  -13.041 1.00 8.74  ? 503  GLN A N   1 
ATOM   4054 C  CA  . GLN A 1 503  ? 66.521 70.700  -12.760 1.00 10.41 ? 503  GLN A CA  1 
ATOM   4055 C  C   . GLN A 1 503  ? 66.710 69.392  -13.476 1.00 9.13  ? 503  GLN A C   1 
ATOM   4056 O  O   . GLN A 1 503  ? 67.820 69.096  -13.981 1.00 10.61 ? 503  GLN A O   1 
ATOM   4057 C  CB  . GLN A 1 503  ? 66.707 70.473  -11.244 1.00 10.71 ? 503  GLN A CB  1 
ATOM   4058 C  CG  . GLN A 1 503  ? 66.864 71.764  -10.414 1.00 12.24 ? 503  GLN A CG  1 
ATOM   4059 C  CD  . GLN A 1 503  ? 68.228 72.433  -10.581 1.00 13.93 ? 503  GLN A CD  1 
ATOM   4060 O  OE1 . GLN A 1 503  ? 69.241 71.778  -10.876 1.00 15.20 ? 503  GLN A OE1 1 
ATOM   4061 N  NE2 . GLN A 1 503  ? 68.262 73.722  -10.326 1.00 15.02 ? 503  GLN A NE2 1 
ATOM   4062 N  N   . SER A 1 504  ? 65.698 68.520  -13.550 1.00 8.17  ? 504  SER A N   1 
ATOM   4063 C  CA  . SER A 1 504  ? 65.864 67.226  -14.181 1.00 9.10  ? 504  SER A CA  1 
ATOM   4064 C  C   . SER A 1 504  ? 66.043 67.377  -15.703 1.00 9.21  ? 504  SER A C   1 
ATOM   4065 O  O   . SER A 1 504  ? 66.873 66.677  -16.292 1.00 9.37  ? 504  SER A O   1 
ATOM   4066 C  CB  . SER A 1 504  ? 64.603 66.336  -13.937 1.00 9.12  ? 504  SER A CB  1 
ATOM   4067 O  OG  . SER A 1 504  ? 64.455 66.063  -12.533 1.00 9.91  ? 504  SER A OG  1 
ATOM   4068 N  N   . VAL A 1 505  ? 65.253 68.227  -16.361 1.00 8.63  ? 505  VAL A N   1 
ATOM   4069 C  CA  . VAL A 1 505  ? 65.420 68.435  -17.803 1.00 9.77  ? 505  VAL A CA  1 
ATOM   4070 C  C   . VAL A 1 505  ? 66.865 68.959  -18.085 1.00 9.62  ? 505  VAL A C   1 
ATOM   4071 O  O   . VAL A 1 505  ? 67.532 68.475  -19.042 1.00 10.67 ? 505  VAL A O   1 
ATOM   4072 C  CB  . VAL A 1 505  ? 64.375 69.473  -18.308 1.00 9.50  ? 505  VAL A CB  1 
ATOM   4073 C  CG1 . VAL A 1 505  ? 64.711 69.915  -19.779 1.00 11.29 ? 505  VAL A CG1 1 
ATOM   4074 C  CG2 . VAL A 1 505  ? 62.967 68.857  -18.224 1.00 11.35 ? 505  VAL A CG2 1 
ATOM   4075 N  N   A TYR A 1 506  ? 67.350 69.871  -17.279 0.50 8.75  ? 506  TYR A N   1 
ATOM   4076 N  N   B TYR A 1 506  ? 67.350 69.871  -17.279 0.50 9.76  ? 506  TYR A N   1 
ATOM   4077 C  CA  A TYR A 1 506  ? 68.680 70.390  -17.545 0.50 9.85  ? 506  TYR A CA  1 
ATOM   4078 C  CA  B TYR A 1 506  ? 68.680 70.390  -17.545 0.50 11.65 ? 506  TYR A CA  1 
ATOM   4079 C  C   A TYR A 1 506  ? 69.710 69.253  -17.452 0.50 11.15 ? 506  TYR A C   1 
ATOM   4080 C  C   B TYR A 1 506  ? 69.710 69.253  -17.452 0.50 12.20 ? 506  TYR A C   1 
ATOM   4081 O  O   A TYR A 1 506  ? 70.629 69.117  -18.294 0.50 11.73 ? 506  TYR A O   1 
ATOM   4082 O  O   B TYR A 1 506  ? 70.629 69.117  -18.294 0.50 12.50 ? 506  TYR A O   1 
ATOM   4083 C  CB  A TYR A 1 506  ? 68.989 71.509  -16.547 0.50 8.44  ? 506  TYR A CB  1 
ATOM   4084 C  CB  B TYR A 1 506  ? 68.989 71.509  -16.547 0.50 12.84 ? 506  TYR A CB  1 
ATOM   4085 C  CG  A TYR A 1 506  ? 70.291 72.185  -16.811 0.50 10.09 ? 506  TYR A CG  1 
ATOM   4086 C  CG  B TYR A 1 506  ? 70.432 71.882  -16.515 0.50 17.12 ? 506  TYR A CG  1 
ATOM   4087 C  CD1 A TYR A 1 506  ? 70.484 72.773  -18.092 0.50 10.06 ? 506  TYR A CD1 1 
ATOM   4088 C  CD1 B TYR A 1 506  ? 71.069 72.170  -17.754 0.50 20.58 ? 506  TYR A CD1 1 
ATOM   4089 C  CD2 A TYR A 1 506  ? 71.294 72.198  -15.879 0.50 9.84  ? 506  TYR A CD2 1 
ATOM   4090 C  CD2 B TYR A 1 506  ? 71.142 71.897  -15.344 0.50 16.69 ? 506  TYR A CD2 1 
ATOM   4091 C  CE1 A TYR A 1 506  ? 71.666 73.366  -18.440 0.50 14.80 ? 506  TYR A CE1 1 
ATOM   4092 C  CE1 B TYR A 1 506  ? 72.402 72.467  -17.824 0.50 22.06 ? 506  TYR A CE1 1 
ATOM   4093 C  CE2 A TYR A 1 506  ? 72.584 72.819  -16.250 0.50 13.01 ? 506  TYR A CE2 1 
ATOM   4094 C  CE2 B TYR A 1 506  ? 72.589 72.198  -15.409 0.50 20.22 ? 506  TYR A CE2 1 
ATOM   4095 C  CZ  A TYR A 1 506  ? 72.682 73.388  -17.543 0.50 9.60  ? 506  TYR A CZ  1 
ATOM   4096 C  CZ  B TYR A 1 506  ? 73.136 72.482  -16.684 0.50 20.83 ? 506  TYR A CZ  1 
ATOM   4097 O  OH  A TYR A 1 506  ? 73.778 74.153  -17.907 0.50 14.18 ? 506  TYR A OH  1 
ATOM   4098 O  OH  B TYR A 1 506  ? 74.430 72.958  -16.818 0.50 18.98 ? 506  TYR A OH  1 
ATOM   4099 N  N   . ARG A 1 507  ? 69.568 68.373  -16.478 1.00 10.21 ? 507  ARG A N   1 
ATOM   4100 C  CA  . ARG A 1 507  ? 70.510 67.274  -16.333 1.00 10.33 ? 507  ARG A CA  1 
ATOM   4101 C  C   . ARG A 1 507  ? 70.360 66.242  -17.439 1.00 10.45 ? 507  ARG A C   1 
ATOM   4102 O  O   . ARG A 1 507  ? 71.372 65.687  -17.931 1.00 11.35 ? 507  ARG A O   1 
ATOM   4103 C  CB  . ARG A 1 507  ? 70.336 66.606  -14.952 1.00 10.90 ? 507  ARG A CB  1 
ATOM   4104 C  CG  . ARG A 1 507  ? 71.485 65.595  -14.660 1.00 12.77 ? 507  ARG A CG  1 
ATOM   4105 C  CD  . ARG A 1 507  ? 71.280 65.102  -13.221 1.00 13.02 ? 507  ARG A CD  1 
ATOM   4106 N  NE  . ARG A 1 507  ? 72.336 64.141  -12.810 1.00 15.95 ? 507  ARG A NE  1 
ATOM   4107 C  CZ  . ARG A 1 507  ? 72.380 63.588  -11.581 1.00 16.43 ? 507  ARG A CZ  1 
ATOM   4108 N  NH1 . ARG A 1 507  ? 71.507 63.895  -10.670 1.00 17.54 ? 507  ARG A NH1 1 
ATOM   4109 N  NH2 . ARG A 1 507  ? 73.228 62.598  -11.308 1.00 18.92 ? 507  ARG A NH2 1 
ATOM   4110 N  N   . LEU A 1 508  ? 69.147 65.958  -17.876 1.00 9.94  ? 508  LEU A N   1 
ATOM   4111 C  CA  . LEU A 1 508  ? 68.915 64.946  -18.887 1.00 9.58  ? 508  LEU A CA  1 
ATOM   4112 C  C   . LEU A 1 508  ? 69.345 65.341  -20.291 1.00 10.34 ? 508  LEU A C   1 
ATOM   4113 O  O   . LEU A 1 508  ? 69.579 64.478  -21.128 1.00 11.68 ? 508  LEU A O   1 
ATOM   4114 C  CB  . LEU A 1 508  ? 67.416 64.565  -18.925 1.00 9.35  ? 508  LEU A CB  1 
ATOM   4115 C  CG  . LEU A 1 508  ? 66.985 63.708  -17.706 1.00 9.29  ? 508  LEU A CG  1 
ATOM   4116 C  CD1 . LEU A 1 508  ? 65.442 63.826  -17.589 1.00 9.84  ? 508  LEU A CD1 1 
ATOM   4117 C  CD2 . LEU A 1 508  ? 67.395 62.267  -17.805 1.00 12.38 ? 508  LEU A CD2 1 
ATOM   4118 N  N   . LEU A 1 509  ? 69.410 66.649  -20.550 1.00 10.50 ? 509  LEU A N   1 
ATOM   4119 C  CA  . LEU A 1 509  ? 69.709 67.180  -21.890 1.00 9.92  ? 509  LEU A CA  1 
ATOM   4120 C  C   . LEU A 1 509  ? 70.979 67.998  -21.982 1.00 11.18 ? 509  LEU A C   1 
ATOM   4121 O  O   . LEU A 1 509  ? 71.127 68.735  -22.970 1.00 12.56 ? 509  LEU A O   1 
ATOM   4122 C  CB  . LEU A 1 509  ? 68.455 67.952  -22.413 1.00 9.54  ? 509  LEU A CB  1 
ATOM   4123 C  CG  . LEU A 1 509  ? 67.244 67.074  -22.702 1.00 10.19 ? 509  LEU A CG  1 
ATOM   4124 C  CD1 . LEU A 1 509  ? 66.098 68.056  -23.127 1.00 10.09 ? 509  LEU A CD1 1 
ATOM   4125 C  CD2 . LEU A 1 509  ? 67.477 66.041  -23.849 1.00 12.41 ? 509  LEU A CD2 1 
ATOM   4126 N  N   . THR A 1 510  ? 71.892 67.875  -21.013 1.00 9.88  ? 510  THR A N   1 
ATOM   4127 C  CA  . THR A 1 510  ? 73.154 68.616  -21.120 1.00 11.57 ? 510  THR A CA  1 
ATOM   4128 C  C   . THR A 1 510  ? 74.297 67.597  -21.146 1.00 12.47 ? 510  THR A C   1 
ATOM   4129 O  O   . THR A 1 510  ? 74.321 66.626  -20.366 1.00 13.08 ? 510  THR A O   1 
ATOM   4130 C  CB  . THR A 1 510  ? 73.326 69.591  -19.964 1.00 11.02 ? 510  THR A CB  1 
ATOM   4131 O  OG1 . THR A 1 510  ? 72.235 70.511  -19.953 1.00 12.35 ? 510  THR A OG1 1 
ATOM   4132 C  CG2 . THR A 1 510  ? 74.650 70.424  -20.085 1.00 11.95 ? 510  THR A CG2 1 
ATOM   4133 N  N   . LYS A 1 511  ? 75.259 67.838  -22.046 1.00 13.78 ? 511  LYS A N   1 
ATOM   4134 C  CA  . LYS A 1 511  ? 76.460 66.951  -22.148 1.00 16.15 ? 511  LYS A CA  1 
ATOM   4135 C  C   . LYS A 1 511  ? 76.978 66.782  -20.747 1.00 13.85 ? 511  LYS A C   1 
ATOM   4136 O  O   . LYS A 1 511  ? 77.260 67.744  -20.029 1.00 13.31 ? 511  LYS A O   1 
ATOM   4137 C  CB  . LYS A 1 511  ? 77.514 67.600  -23.070 1.00 18.93 ? 511  LYS A CB  1 
ATOM   4138 C  CG  . LYS A 1 511  ? 78.770 66.703  -23.127 1.00 25.46 ? 511  LYS A CG  1 
ATOM   4139 C  CD  . LYS A 1 511  ? 79.866 67.117  -24.098 1.00 29.96 ? 511  LYS A CD  1 
ATOM   4140 C  CE  . LYS A 1 511  ? 80.961 66.006  -23.966 1.00 31.98 ? 511  LYS A CE  1 
ATOM   4141 N  NZ  . LYS A 1 511  ? 82.263 66.095  -24.731 1.00 34.40 ? 511  LYS A NZ  1 
ATOM   4142 N  N   . PRO A 1 512  ? 77.211 65.523  -20.322 1.00 16.63 ? 512  PRO A N   1 
ATOM   4143 C  CA  . PRO A 1 512  ? 77.665 65.335  -18.947 1.00 16.32 ? 512  PRO A CA  1 
ATOM   4144 C  C   . PRO A 1 512  ? 78.890 66.067  -18.398 1.00 14.82 ? 512  PRO A C   1 
ATOM   4145 O  O   . PRO A 1 512  ? 78.933 66.493  -17.265 1.00 16.13 ? 512  PRO A O   1 
ATOM   4146 C  CB  . PRO A 1 512  ? 77.828 63.817  -18.837 1.00 21.42 ? 512  PRO A CB  1 
ATOM   4147 C  CG  . PRO A 1 512  ? 76.872 63.293  -19.827 1.00 21.32 ? 512  PRO A CG  1 
ATOM   4148 C  CD  . PRO A 1 512  ? 76.852 64.245  -20.978 1.00 17.82 ? 512  PRO A CD  1 
ATOM   4149 N  N   . SER A 1 513  ? 79.886 66.168  -19.257 1.00 15.70 ? 513  SER A N   1 
ATOM   4150 C  CA  . SER A 1 513  ? 81.134 66.827  -18.806 1.00 15.45 ? 513  SER A CA  1 
ATOM   4151 C  C   . SER A 1 513  ? 81.040 68.346  -18.784 1.00 14.86 ? 513  SER A C   1 
ATOM   4152 O  O   . SER A 1 513  ? 82.000 69.029  -18.394 1.00 16.70 ? 513  SER A O   1 
ATOM   4153 C  CB  . SER A 1 513  ? 82.309 66.374  -19.707 1.00 16.06 ? 513  SER A CB  1 
ATOM   4154 O  OG  . SER A 1 513  ? 82.008 66.710  -21.020 1.00 18.39 ? 513  SER A OG  1 
ATOM   4155 N  N   . ILE A 1 514  ? 79.888 68.885  -19.196 1.00 15.79 ? 514  ILE A N   1 
ATOM   4156 C  CA  . ILE A 1 514  ? 79.602 70.324  -19.218 1.00 15.36 ? 514  ILE A CA  1 
ATOM   4157 C  C   . ILE A 1 514  ? 78.601 70.670  -18.089 1.00 14.76 ? 514  ILE A C   1 
ATOM   4158 O  O   . ILE A 1 514  ? 78.659 71.745  -17.514 1.00 15.15 ? 514  ILE A O   1 
ATOM   4159 C  CB  . ILE A 1 514  ? 78.987 70.733  -20.630 1.00 17.44 ? 514  ILE A CB  1 
ATOM   4160 C  CG1 . ILE A 1 514  ? 80.065 70.589  -21.701 1.00 21.61 ? 514  ILE A CG1 1 
ATOM   4161 C  CG2 . ILE A 1 514  ? 78.337 72.117  -20.559 1.00 20.00 ? 514  ILE A CG2 1 
ATOM   4162 C  CD1 . ILE A 1 514  ? 79.643 71.038  -23.110 1.00 26.63 ? 514  ILE A CD1 1 
ATOM   4163 N  N   . TYR A 1 515  ? 77.722 69.725  -17.746 1.00 13.55 ? 515  TYR A N   1 
ATOM   4164 C  CA  . TYR A 1 515  ? 76.679 69.956  -16.738 1.00 12.74 ? 515  TYR A CA  1 
ATOM   4165 C  C   . TYR A 1 515  ? 77.261 70.511  -15.452 1.00 13.60 ? 515  TYR A C   1 
ATOM   4166 O  O   . TYR A 1 515  ? 78.121 69.875  -14.833 1.00 14.44 ? 515  TYR A O   1 
ATOM   4167 C  CB  . TYR A 1 515  ? 75.996 68.600  -16.532 1.00 13.23 ? 515  TYR A CB  1 
ATOM   4168 C  CG  . TYR A 1 515  ? 75.006 68.553  -15.420 1.00 12.82 ? 515  TYR A CG  1 
ATOM   4169 C  CD1 . TYR A 1 515  ? 73.840 69.286  -15.486 1.00 11.39 ? 515  TYR A CD1 1 
ATOM   4170 C  CD2 . TYR A 1 515  ? 75.222 67.734  -14.316 1.00 14.37 ? 515  TYR A CD2 1 
ATOM   4171 C  CE1 . TYR A 1 515  ? 72.870 69.203  -14.484 1.00 12.07 ? 515  TYR A CE1 1 
ATOM   4172 C  CE2 . TYR A 1 515  ? 74.266 67.649  -13.284 1.00 13.29 ? 515  TYR A CE2 1 
ATOM   4173 C  CZ  . TYR A 1 515  ? 73.100 68.390  -13.406 1.00 13.10 ? 515  TYR A CZ  1 
ATOM   4174 O  OH  . TYR A 1 515  ? 72.153 68.298  -12.401 1.00 13.54 ? 515  TYR A OH  1 
ATOM   4175 N  N   . SER A 1 516  ? 76.786 71.686  -15.023 1.00 13.36 ? 516  SER A N   1 
ATOM   4176 C  CA  . SER A 1 516  ? 77.312 72.326  -13.817 1.00 14.15 ? 516  SER A CA  1 
ATOM   4177 C  C   . SER A 1 516  ? 76.152 72.979  -13.078 1.00 15.24 ? 516  SER A C   1 
ATOM   4178 O  O   . SER A 1 516  ? 75.940 74.206  -13.115 1.00 16.90 ? 516  SER A O   1 
ATOM   4179 C  CB  . SER A 1 516  ? 78.331 73.383  -14.269 1.00 16.76 ? 516  SER A CB  1 
ATOM   4180 O  OG  . SER A 1 516  ? 79.078 73.878  -13.144 1.00 23.21 ? 516  SER A OG  1 
ATOM   4181 N  N   . PRO A 1 517  ? 75.393 72.155  -12.347 1.00 14.73 ? 517  PRO A N   1 
ATOM   4182 C  CA  . PRO A 1 517  ? 74.240 72.699  -11.670 1.00 16.74 ? 517  PRO A CA  1 
ATOM   4183 C  C   . PRO A 1 517  ? 74.336 73.546  -10.456 1.00 17.19 ? 517  PRO A C   1 
ATOM   4184 O  O   . PRO A 1 517  ? 75.195 73.315  -9.622  1.00 21.63 ? 517  PRO A O   1 
ATOM   4185 C  CB  . PRO A 1 517  ? 73.406 71.448  -11.398 1.00 18.76 ? 517  PRO A CB  1 
ATOM   4186 C  CG  . PRO A 1 517  ? 74.466 70.425  -11.076 1.00 18.44 ? 517  PRO A CG  1 
ATOM   4187 C  CD  . PRO A 1 517  ? 75.559 70.711  -12.126 1.00 16.17 ? 517  PRO A CD  1 
ATOM   4188 N  N   . ASP A 1 518  ? 73.508 74.564  -10.415 1.00 18.00 ? 518  ASP A N   1 
ATOM   4189 C  CA  . ASP A 1 518  ? 73.322 75.361  -9.216  1.00 19.07 ? 518  ASP A CA  1 
ATOM   4190 C  C   . ASP A 1 518  ? 71.881 74.882  -8.917  1.00 16.76 ? 518  ASP A C   1 
ATOM   4191 O  O   . ASP A 1 518  ? 70.940 75.201  -9.648  1.00 16.06 ? 518  ASP A O   1 
ATOM   4192 C  CB  . ASP A 1 518  ? 73.324 76.837  -9.554  1.00 21.21 ? 518  ASP A CB  1 
ATOM   4193 C  CG  . ASP A 1 518  ? 72.862 77.706  -8.428  1.00 27.98 ? 518  ASP A CG  1 
ATOM   4194 O  OD1 . ASP A 1 518  ? 72.269 77.216  -7.429  1.00 23.17 ? 518  ASP A OD1 1 
ATOM   4195 O  OD2 . ASP A 1 518  ? 73.054 78.935  -8.575  1.00 29.29 ? 518  ASP A OD2 1 
ATOM   4196 N  N   . PHE A 1 519  ? 71.736 74.146  -7.822  1.00 16.63 ? 519  PHE A N   1 
ATOM   4197 C  CA  . PHE A 1 519  ? 70.436 73.571  -7.441  1.00 17.48 ? 519  PHE A CA  1 
ATOM   4198 C  C   . PHE A 1 519  ? 69.362 74.547  -7.047  1.00 17.44 ? 519  PHE A C   1 
ATOM   4199 O  O   . PHE A 1 519  ? 68.198 74.158  -6.882  1.00 18.52 ? 519  PHE A O   1 
ATOM   4200 C  CB  . PHE A 1 519  ? 70.644 72.494  -6.362  1.00 15.25 ? 519  PHE A CB  1 
ATOM   4201 C  CG  . PHE A 1 519  ? 71.485 71.339  -6.834  1.00 15.14 ? 519  PHE A CG  1 
ATOM   4202 C  CD1 . PHE A 1 519  ? 71.192 70.657  -8.025  1.00 16.37 ? 519  PHE A CD1 1 
ATOM   4203 C  CD2 . PHE A 1 519  ? 72.578 70.930  -6.066  1.00 15.99 ? 519  PHE A CD2 1 
ATOM   4204 C  CE1 . PHE A 1 519  ? 71.950 69.607  -8.458  1.00 14.92 ? 519  PHE A CE1 1 
ATOM   4205 C  CE2 . PHE A 1 519  ? 73.353 69.861  -6.488  1.00 15.68 ? 519  PHE A CE2 1 
ATOM   4206 C  CZ  . PHE A 1 519  ? 73.040 69.187  -7.704  1.00 16.49 ? 519  PHE A CZ  1 
ATOM   4207 N  N   . SER A 1 520  ? 69.695 75.837  -6.934  1.00 17.03 ? 520  SER A N   1 
ATOM   4208 C  CA  . SER A 1 520  ? 68.685 76.854  -6.609  1.00 18.37 ? 520  SER A CA  1 
ATOM   4209 C  C   . SER A 1 520  ? 68.320 77.683  -7.843  1.00 17.45 ? 520  SER A C   1 
ATOM   4210 O  O   . SER A 1 520  ? 67.398 78.481  -7.781  1.00 18.39 ? 520  SER A O   1 
ATOM   4211 C  CB  . SER A 1 520  ? 69.208 77.880  -5.584  1.00 18.67 ? 520  SER A CB  1 
ATOM   4212 O  OG  . SER A 1 520  ? 70.260 78.661  -6.149  1.00 25.69 ? 520  SER A OG  1 
ATOM   4213 N  N   . PHE A 1 521  ? 68.994 77.438  -8.972  1.00 16.97 ? 521  PHE A N   1 
ATOM   4214 C  CA  . PHE A 1 521  ? 68.784 78.235  -10.188 1.00 17.01 ? 521  PHE A CA  1 
ATOM   4215 C  C   . PHE A 1 521  ? 67.672 77.715  -11.086 1.00 14.89 ? 521  PHE A C   1 
ATOM   4216 O  O   . PHE A 1 521  ? 67.456 76.481  -11.136 1.00 17.20 ? 521  PHE A O   1 
ATOM   4217 C  CB  . PHE A 1 521  ? 70.140 78.265  -10.970 1.00 17.81 ? 521  PHE A CB  1 
ATOM   4218 C  CG  . PHE A 1 521  ? 70.155 79.200  -12.151 1.00 18.47 ? 521  PHE A CG  1 
ATOM   4219 C  CD1 . PHE A 1 521  ? 70.305 80.582  -11.946 1.00 22.08 ? 521  PHE A CD1 1 
ATOM   4220 C  CD2 . PHE A 1 521  ? 69.960 78.709  -13.469 1.00 19.90 ? 521  PHE A CD2 1 
ATOM   4221 C  CE1 . PHE A 1 521  ? 70.244 81.470  -13.043 1.00 26.07 ? 521  PHE A CE1 1 
ATOM   4222 C  CE2 . PHE A 1 521  ? 69.897 79.589  -14.559 1.00 20.92 ? 521  PHE A CE2 1 
ATOM   4223 C  CZ  . PHE A 1 521  ? 70.037 80.982  -14.345 1.00 24.08 ? 521  PHE A CZ  1 
ATOM   4224 N  N   . SER A 1 522  ? 66.983 78.608  -11.798 1.00 17.19 ? 522  SER A N   1 
ATOM   4225 C  CA  . SER A 1 522  ? 65.942 78.194  -12.736 1.00 17.06 ? 522  SER A CA  1 
ATOM   4226 C  C   . SER A 1 522  ? 66.500 78.176  -14.149 1.00 14.23 ? 522  SER A C   1 
ATOM   4227 O  O   . SER A 1 522  ? 66.610 79.220  -14.806 1.00 17.89 ? 522  SER A O   1 
ATOM   4228 C  CB  . SER A 1 522  ? 64.734 79.136  -12.696 1.00 21.48 ? 522  SER A CB  1 
ATOM   4229 O  OG  . SER A 1 522  ? 64.070 78.992  -11.436 1.00 30.02 ? 522  SER A OG  1 
ATOM   4230 N  N   . TYR A 1 523  ? 66.893 76.998  -14.591 1.00 11.00 ? 523  TYR A N   1 
ATOM   4231 C  CA  . TYR A 1 523  ? 67.351 76.796  -15.959 1.00 11.05 ? 523  TYR A CA  1 
ATOM   4232 C  C   . TYR A 1 523  ? 66.222 76.866  -16.959 1.00 11.77 ? 523  TYR A C   1 
ATOM   4233 O  O   . TYR A 1 523  ? 66.453 77.290  -18.102 1.00 11.37 ? 523  TYR A O   1 
ATOM   4234 C  CB  . TYR A 1 523  ? 68.030 75.438  -16.085 1.00 12.22 ? 523  TYR A CB  1 
ATOM   4235 C  CG  . TYR A 1 523  ? 69.306 75.369  -15.289 1.00 12.20 ? 523  TYR A CG  1 
ATOM   4236 C  CD1 . TYR A 1 523  ? 69.341 74.814  -14.021 1.00 12.70 ? 523  TYR A CD1 1 
ATOM   4237 C  CD2 . TYR A 1 523  ? 70.504 75.955  -15.806 1.00 13.68 ? 523  TYR A CD2 1 
ATOM   4238 C  CE1 . TYR A 1 523  ? 70.529 74.836  -13.283 1.00 15.22 ? 523  TYR A CE1 1 
ATOM   4239 C  CE2 . TYR A 1 523  ? 71.666 75.998  -15.077 1.00 15.23 ? 523  TYR A CE2 1 
ATOM   4240 C  CZ  . TYR A 1 523  ? 71.671 75.443  -13.821 1.00 18.16 ? 523  TYR A CZ  1 
ATOM   4241 O  OH  . TYR A 1 523  ? 72.793 75.538  -13.009 1.00 17.43 ? 523  TYR A OH  1 
ATOM   4242 N  N   . PHE A 1 524  ? 65.007 76.463  -16.572 1.00 10.50 ? 524  PHE A N   1 
ATOM   4243 C  CA  . PHE A 1 524  ? 63.848 76.518  -17.433 1.00 10.29 ? 524  PHE A CA  1 
ATOM   4244 C  C   . PHE A 1 524  ? 62.687 76.991  -16.603 1.00 11.68 ? 524  PHE A C   1 
ATOM   4245 O  O   . PHE A 1 524  ? 62.632 76.762  -15.395 1.00 12.65 ? 524  PHE A O   1 
ATOM   4246 C  CB  . PHE A 1 524  ? 63.444 75.123  -17.979 1.00 10.92 ? 524  PHE A CB  1 
ATOM   4247 C  CG  . PHE A 1 524  ? 64.482 74.467  -18.851 1.00 9.58  ? 524  PHE A CG  1 
ATOM   4248 C  CD1 . PHE A 1 524  ? 65.489 73.685  -18.285 1.00 10.77 ? 524  PHE A CD1 1 
ATOM   4249 C  CD2 . PHE A 1 524  ? 64.439 74.620  -20.248 1.00 10.48 ? 524  PHE A CD2 1 
ATOM   4250 C  CE1 . PHE A 1 524  ? 66.454 73.070  -19.095 1.00 12.75 ? 524  PHE A CE1 1 
ATOM   4251 C  CE2 . PHE A 1 524  ? 65.387 74.007  -21.062 1.00 10.20 ? 524  PHE A CE2 1 
ATOM   4252 C  CZ  . PHE A 1 524  ? 66.404 73.235  -20.467 1.00 11.87 ? 524  PHE A CZ  1 
ATOM   4253 N  N   . THR A 1 525  ? 61.783 77.638  -17.289 1.00 11.85 ? 525  THR A N   1 
ATOM   4254 C  CA  . THR A 1 525  ? 60.515 77.957  -16.654 1.00 15.26 ? 525  THR A CA  1 
ATOM   4255 C  C   . THR A 1 525  ? 59.448 77.148  -17.395 1.00 12.84 ? 525  THR A C   1 
ATOM   4256 O  O   . THR A 1 525  ? 59.490 76.971  -18.661 1.00 14.16 ? 525  THR A O   1 
ATOM   4257 C  CB  . THR A 1 525  ? 60.179 79.420  -16.692 1.00 19.69 ? 525  THR A CB  1 
ATOM   4258 O  OG1 . THR A 1 525  ? 59.935 79.790  -18.006 1.00 22.28 ? 525  THR A OG1 1 
ATOM   4259 C  CG2 . THR A 1 525  ? 61.381 80.278  -16.239 1.00 20.99 ? 525  THR A CG2 1 
ATOM   4260 N  N   . LEU A 1 526  ? 58.472 76.622  -16.661 1.00 10.91 ? 526  LEU A N   1 
ATOM   4261 C  CA  . LEU A 1 526  ? 57.382 75.901  -17.274 1.00 12.88 ? 526  LEU A CA  1 
ATOM   4262 C  C   . LEU A 1 526  ? 56.430 76.866  -17.950 1.00 11.97 ? 526  LEU A C   1 
ATOM   4263 O  O   . LEU A 1 526  ? 56.250 78.021  -17.500 1.00 16.99 ? 526  LEU A O   1 
ATOM   4264 C  CB  . LEU A 1 526  ? 56.563 75.098  -16.223 1.00 16.32 ? 526  LEU A CB  1 
ATOM   4265 C  CG  . LEU A 1 526  ? 57.021 73.694  -15.788 1.00 19.82 ? 526  LEU A CG  1 
ATOM   4266 C  CD1 . LEU A 1 526  ? 56.127 73.170  -14.620 1.00 24.73 ? 526  LEU A CD1 1 
ATOM   4267 C  CD2 . LEU A 1 526  ? 56.917 72.751  -16.950 1.00 18.19 ? 526  LEU A CD2 1 
ATOM   4268 N  N   . ASP A 1 527  ? 55.831 76.432  -19.036 1.00 10.30 ? 527  ASP A N   1 
ATOM   4269 C  CA  . ASP A 1 527  ? 54.839 77.219  -19.733 1.00 12.11 ? 527  ASP A CA  1 
ATOM   4270 C  C   . ASP A 1 527  ? 53.603 76.329  -19.785 1.00 12.91 ? 527  ASP A C   1 
ATOM   4271 O  O   . ASP A 1 527  ? 53.633 75.235  -20.318 1.00 17.02 ? 527  ASP A O   1 
ATOM   4272 C  CB  . ASP A 1 527  ? 55.298 77.585  -21.163 1.00 12.91 ? 527  ASP A CB  1 
ATOM   4273 C  CG  . ASP A 1 527  ? 54.302 78.484  -21.882 1.00 18.71 ? 527  ASP A CG  1 
ATOM   4274 O  OD1 . ASP A 1 527  ? 54.061 79.600  -21.418 1.00 17.58 ? 527  ASP A OD1 1 
ATOM   4275 O  OD2 . ASP A 1 527  ? 53.737 78.069  -22.914 1.00 20.01 ? 527  ASP A OD2 1 
ATOM   4276 N  N   . ASP A 1 528  ? 52.523 76.764  -19.186 1.00 12.43 ? 528  ASP A N   1 
ATOM   4277 C  CA  . ASP A 1 528  ? 51.298 75.942  -19.186 1.00 10.47 ? 528  ASP A CA  1 
ATOM   4278 C  C   . ASP A 1 528  ? 50.195 76.795  -19.797 1.00 11.89 ? 528  ASP A C   1 
ATOM   4279 O  O   . ASP A 1 528  ? 49.820 77.836  -19.251 1.00 12.43 ? 528  ASP A O   1 
ATOM   4280 C  CB  . ASP A 1 528  ? 50.968 75.536  -17.730 1.00 11.39 ? 528  ASP A CB  1 
ATOM   4281 C  CG  . ASP A 1 528  ? 49.862 74.494  -17.634 1.00 11.82 ? 528  ASP A CG  1 
ATOM   4282 O  OD1 . ASP A 1 528  ? 48.868 74.559  -18.372 1.00 13.72 ? 528  ASP A OD1 1 
ATOM   4283 O  OD2 . ASP A 1 528  ? 50.039 73.570  -16.790 1.00 15.41 ? 528  ASP A OD2 1 
ATOM   4284 N  N   . SER A 1 529  ? 49.673 76.333  -20.929 1.00 12.20 ? 529  SER A N   1 
ATOM   4285 C  CA  . SER A 1 529  ? 48.622 77.085  -21.626 1.00 11.77 ? 529  SER A CA  1 
ATOM   4286 C  C   . SER A 1 529  ? 47.240 76.989  -21.019 1.00 12.22 ? 529  SER A C   1 
ATOM   4287 O  O   . SER A 1 529  ? 46.378 77.760  -21.344 1.00 16.50 ? 529  SER A O   1 
ATOM   4288 C  CB  . SER A 1 529  ? 48.434 76.615  -23.079 1.00 15.79 ? 529  SER A CB  1 
ATOM   4289 O  OG  . SER A 1 529  ? 49.660 76.707  -23.739 1.00 18.12 ? 529  SER A OG  1 
ATOM   4290 N  N   . ARG A 1 530  ? 47.011 76.037  -20.100 1.00 9.96  ? 530  ARG A N   1 
ATOM   4291 C  CA  . ARG A 1 530  ? 45.653 75.831  -19.593 1.00 11.11 ? 530  ARG A CA  1 
ATOM   4292 C  C   . ARG A 1 530  ? 45.523 75.923  -18.113 1.00 12.37 ? 530  ARG A C   1 
ATOM   4293 O  O   . ARG A 1 530  ? 44.493 75.528  -17.555 1.00 17.76 ? 530  ARG A O   1 
ATOM   4294 C  CB  . ARG A 1 530  ? 45.140 74.456  -20.098 1.00 9.82  ? 530  ARG A CB  1 
ATOM   4295 C  CG  . ARG A 1 530  ? 45.136 74.410  -21.666 1.00 11.39 ? 530  ARG A CG  1 
ATOM   4296 C  CD  . ARG A 1 530  ? 44.428 73.191  -22.256 1.00 12.17 ? 530  ARG A CD  1 
ATOM   4297 N  NE  . ARG A 1 530  ? 45.123 71.991  -21.809 1.00 12.60 ? 530  ARG A NE  1 
ATOM   4298 C  CZ  . ARG A 1 530  ? 44.916 70.782  -22.347 1.00 12.75 ? 530  ARG A CZ  1 
ATOM   4299 N  NH1 . ARG A 1 530  ? 44.042 70.633  -23.332 1.00 15.03 ? 530  ARG A NH1 1 
ATOM   4300 N  NH2 . ARG A 1 530  ? 45.573 69.753  -21.866 1.00 15.05 ? 530  ARG A NH2 1 
ATOM   4301 N  N   . TRP A 1 531  ? 46.552 76.366  -17.430 1.00 9.61  ? 531  TRP A N   1 
ATOM   4302 C  CA  . TRP A 1 531  ? 46.420 76.571  -15.969 1.00 9.78  ? 531  TRP A CA  1 
ATOM   4303 C  C   . TRP A 1 531  ? 47.382 77.680  -15.546 1.00 10.09 ? 531  TRP A C   1 
ATOM   4304 O  O   . TRP A 1 531  ? 48.574 77.596  -15.817 1.00 12.76 ? 531  TRP A O   1 
ATOM   4305 C  CB  . TRP A 1 531  ? 46.749 75.317  -15.137 1.00 10.91 ? 531  TRP A CB  1 
ATOM   4306 C  CG  . TRP A 1 531  ? 46.670 75.655  -13.671 1.00 12.68 ? 531  TRP A CG  1 
ATOM   4307 C  CD1 . TRP A 1 531  ? 47.717 76.077  -12.841 1.00 14.52 ? 531  TRP A CD1 1 
ATOM   4308 C  CD2 . TRP A 1 531  ? 45.496 75.757  -12.942 1.00 15.35 ? 531  TRP A CD2 1 
ATOM   4309 N  NE1 . TRP A 1 531  ? 47.203 76.428  -11.636 1.00 17.02 ? 531  TRP A NE1 1 
ATOM   4310 C  CE2 . TRP A 1 531  ? 45.845 76.252  -11.657 1.00 12.00 ? 531  TRP A CE2 1 
ATOM   4311 C  CE3 . TRP A 1 531  ? 44.202 75.490  -13.238 1.00 13.82 ? 531  TRP A CE3 1 
ATOM   4312 C  CZ2 . TRP A 1 531  ? 44.878 76.480  -10.633 1.00 16.22 ? 531  TRP A CZ2 1 
ATOM   4313 C  CZ3 . TRP A 1 531  ? 43.226 75.715  -12.243 1.00 13.65 ? 531  TRP A CZ3 1 
ATOM   4314 C  CH2 . TRP A 1 531  ? 43.580 76.204  -10.947 1.00 17.76 ? 531  TRP A CH2 1 
ATOM   4315 N  N   . PRO A 1 532  ? 46.856 78.702  -14.845 1.00 11.28 ? 532  PRO A N   1 
ATOM   4316 C  CA  . PRO A 1 532  ? 45.458 78.910  -14.446 1.00 11.36 ? 532  PRO A CA  1 
ATOM   4317 C  C   . PRO A 1 532  ? 44.579 79.192  -15.677 1.00 12.68 ? 532  PRO A C   1 
ATOM   4318 O  O   . PRO A 1 532  ? 43.353 79.042  -15.601 1.00 15.29 ? 532  PRO A O   1 
ATOM   4319 C  CB  . PRO A 1 532  ? 45.533 80.121  -13.464 1.00 12.74 ? 532  PRO A CB  1 
ATOM   4320 C  CG  . PRO A 1 532  ? 46.959 79.959  -12.868 1.00 14.96 ? 532  PRO A CG  1 
ATOM   4321 C  CD  . PRO A 1 532  ? 47.768 79.629  -14.122 1.00 13.37 ? 532  PRO A CD  1 
ATOM   4322 N  N   . GLY A 1 533  ? 45.195 79.581  -16.794 1.00 12.95 ? 533  GLY A N   1 
ATOM   4323 C  CA  . GLY A 1 533  ? 44.480 79.792  -18.044 1.00 15.91 ? 533  GLY A CA  1 
ATOM   4324 C  C   . GLY A 1 533  ? 44.260 81.253  -18.414 1.00 19.32 ? 533  GLY A C   1 
ATOM   4325 O  O   . GLY A 1 533  ? 44.268 82.166  -17.564 1.00 17.74 ? 533  GLY A O   1 
ATOM   4326 N  N   . SER A 1 534  ? 44.113 81.422  -19.732 1.00 21.64 ? 534  SER A N   1 
ATOM   4327 C  CA  . SER A 1 534  ? 43.895 82.709  -20.385 1.00 23.10 ? 534  SER A CA  1 
ATOM   4328 C  C   . SER A 1 534  ? 42.629 83.254  -19.745 1.00 21.85 ? 534  SER A C   1 
ATOM   4329 O  O   . SER A 1 534  ? 41.595 82.555  -19.695 1.00 25.19 ? 534  SER A O   1 
ATOM   4330 C  CB  . SER A 1 534  ? 43.689 82.459  -21.885 1.00 30.16 ? 534  SER A CB  1 
ATOM   4331 O  OG  . SER A 1 534  ? 43.565 83.686  -22.579 1.00 36.25 ? 534  SER A OG  1 
ATOM   4332 N  N   . GLY A 1 535  ? 42.693 84.480  -19.224 1.00 24.20 ? 535  GLY A N   1 
ATOM   4333 C  CA  . GLY A 1 535  ? 41.519 85.048  -18.575 1.00 22.49 ? 535  GLY A CA  1 
ATOM   4334 C  C   . GLY A 1 535  ? 41.374 84.761  -17.096 1.00 25.29 ? 535  GLY A C   1 
ATOM   4335 O  O   . GLY A 1 535  ? 40.451 85.266  -16.420 1.00 26.48 ? 535  GLY A O   1 
ATOM   4336 N  N   . VAL A 1 536  ? 42.260 83.908  -16.570 1.00 22.99 ? 536  VAL A N   1 
ATOM   4337 C  CA  . VAL A 1 536  ? 42.229 83.559  -15.163 1.00 20.80 ? 536  VAL A CA  1 
ATOM   4338 C  C   . VAL A 1 536  ? 43.432 84.233  -14.492 1.00 22.65 ? 536  VAL A C   1 
ATOM   4339 O  O   . VAL A 1 536  ? 43.272 84.904  -13.455 1.00 21.07 ? 536  VAL A O   1 
ATOM   4340 C  CB  . VAL A 1 536  ? 42.261 82.017  -15.009 1.00 17.75 ? 536  VAL A CB  1 
ATOM   4341 C  CG1 . VAL A 1 536  ? 42.107 81.606  -13.548 1.00 19.66 ? 536  VAL A CG1 1 
ATOM   4342 C  CG2 . VAL A 1 536  ? 41.045 81.419  -15.762 1.00 22.33 ? 536  VAL A CG2 1 
ATOM   4343 N  N   . GLU A 1 537  ? 44.632 84.028  -15.036 1.00 21.88 ? 537  GLU A N   1 
ATOM   4344 C  CA  . GLU A 1 537  ? 45.822 84.699  -14.496 1.00 24.82 ? 537  GLU A CA  1 
ATOM   4345 C  C   . GLU A 1 537  ? 46.759 84.976  -15.678 1.00 25.62 ? 537  GLU A C   1 
ATOM   4346 O  O   . GLU A 1 537  ? 46.854 84.149  -16.609 1.00 28.23 ? 537  GLU A O   1 
ATOM   4347 C  CB  . GLU A 1 537  ? 46.553 83.815  -13.471 1.00 23.41 ? 537  GLU A CB  1 
ATOM   4348 C  CG  . GLU A 1 537  ? 45.804 83.514  -12.150 1.00 29.48 ? 537  GLU A CG  1 
ATOM   4349 C  CD  . GLU A 1 537  ? 45.438 84.731  -11.323 1.00 38.04 ? 537  GLU A CD  1 
ATOM   4350 O  OE1 . GLU A 1 537  ? 45.997 85.844  -11.537 1.00 38.22 ? 537  GLU A OE1 1 
ATOM   4351 O  OE2 . GLU A 1 537  ? 44.580 84.568  -10.424 1.00 37.31 ? 537  GLU A OE2 1 
ATOM   4352 N  N   A ASP A 1 538  ? 47.440 86.132  -15.697 0.50 28.35 ? 538  ASP A N   1 
ATOM   4353 N  N   B ASP A 1 538  ? 47.440 86.132  -15.697 0.50 28.99 ? 538  ASP A N   1 
ATOM   4354 C  CA  A ASP A 1 538  ? 48.423 86.330  -16.806 0.50 31.87 ? 538  ASP A CA  1 
ATOM   4355 C  CA  B ASP A 1 538  ? 48.423 86.330  -16.806 0.50 32.78 ? 538  ASP A CA  1 
ATOM   4356 C  C   A ASP A 1 538  ? 49.683 85.822  -16.103 0.50 31.72 ? 538  ASP A C   1 
ATOM   4357 C  C   B ASP A 1 538  ? 49.683 85.822  -16.103 0.50 32.28 ? 538  ASP A C   1 
ATOM   4358 O  O   A ASP A 1 538  ? 50.323 86.538  -15.321 0.50 33.95 ? 538  ASP A O   1 
ATOM   4359 O  O   B ASP A 1 538  ? 50.323 86.538  -15.321 0.50 34.38 ? 538  ASP A O   1 
ATOM   4360 C  CB  A ASP A 1 538  ? 48.567 87.820  -17.242 0.50 36.09 ? 538  ASP A CB  1 
ATOM   4361 C  CB  B ASP A 1 538  ? 48.567 87.820  -17.242 0.50 38.30 ? 538  ASP A CB  1 
ATOM   4362 C  CG  A ASP A 1 538  ? 49.000 87.960  -18.744 0.50 39.70 ? 538  ASP A CG  1 
ATOM   4363 C  CG  B ASP A 1 538  ? 48.381 88.007  -18.789 0.50 42.64 ? 538  ASP A CG  1 
ATOM   4364 O  OD1 A ASP A 1 538  ? 49.701 87.040  -19.235 0.50 39.72 ? 538  ASP A OD1 1 
ATOM   4365 O  OD1 B ASP A 1 538  ? 49.136 87.351  -19.549 0.50 44.13 ? 538  ASP A OD1 1 
ATOM   4366 O  OD2 A ASP A 1 538  ? 48.648 88.968  -19.441 0.50 39.30 ? 538  ASP A OD2 1 
ATOM   4367 O  OD2 B ASP A 1 538  ? 47.491 88.791  -19.257 0.50 45.80 ? 538  ASP A OD2 1 
ATOM   4368 N  N   . SER A 1 539  ? 50.023 84.562  -16.344 1.00 29.37 ? 539  SER A N   1 
ATOM   4369 C  CA  . SER A 1 539  ? 51.161 83.932  -15.647 1.00 28.19 ? 539  SER A CA  1 
ATOM   4370 C  C   . SER A 1 539  ? 52.284 83.509  -16.584 1.00 27.12 ? 539  SER A C   1 
ATOM   4371 O  O   . SER A 1 539  ? 53.397 83.233  -16.126 1.00 28.06 ? 539  SER A O   1 
ATOM   4372 C  CB  . SER A 1 539  ? 50.672 82.665  -14.909 1.00 25.28 ? 539  SER A CB  1 
ATOM   4373 O  OG  . SER A 1 539  ? 50.092 81.751  -15.864 1.00 31.10 ? 539  SER A OG  1 
ATOM   4374 N  N   . ARG A 1 540  ? 51.970 83.437  -17.875 1.00 23.12 ? 540  ARG A N   1 
ATOM   4375 C  CA  . ARG A 1 540  ? 52.914 82.932  -18.851 1.00 22.78 ? 540  ARG A CA  1 
ATOM   4376 C  C   . ARG A 1 540  ? 53.939 83.928  -19.275 1.00 21.38 ? 540  ARG A C   1 
ATOM   4377 O  O   . ARG A 1 540  ? 53.651 85.104  -19.404 1.00 26.69 ? 540  ARG A O   1 
ATOM   4378 C  CB  . ARG A 1 540  ? 52.192 82.443  -20.090 1.00 24.20 ? 540  ARG A CB  1 
ATOM   4379 C  CG  . ARG A 1 540  ? 51.253 81.245  -19.813 1.00 19.30 ? 540  ARG A CG  1 
ATOM   4380 C  CD  . ARG A 1 540  ? 50.424 80.911  -21.061 1.00 17.06 ? 540  ARG A CD  1 
ATOM   4381 N  NE  . ARG A 1 540  ? 51.241 80.267  -22.118 1.00 14.54 ? 540  ARG A NE  1 
ATOM   4382 C  CZ  . ARG A 1 540  ? 50.791 79.879  -23.311 1.00 15.02 ? 540  ARG A CZ  1 
ATOM   4383 N  NH1 . ARG A 1 540  ? 49.526 80.037  -23.701 1.00 17.96 ? 540  ARG A NH1 1 
ATOM   4384 N  NH2 . ARG A 1 540  ? 51.638 79.293  -24.135 1.00 16.73 ? 540  ARG A NH2 1 
ATOM   4385 N  N   . THR A 1 541  ? 55.136 83.436  -19.446 1.00 20.13 ? 541  THR A N   1 
ATOM   4386 C  CA  . THR A 1 541  ? 56.156 84.336  -19.891 1.00 21.17 ? 541  THR A CA  1 
ATOM   4387 C  C   . THR A 1 541  ? 56.178 84.387  -21.433 1.00 19.52 ? 541  THR A C   1 
ATOM   4388 O  O   . THR A 1 541  ? 55.934 83.405  -22.133 1.00 24.52 ? 541  THR A O   1 
ATOM   4389 C  CB  . THR A 1 541  ? 57.495 83.862  -19.422 1.00 25.10 ? 541  THR A CB  1 
ATOM   4390 O  OG1 . THR A 1 541  ? 57.824 82.723  -20.187 1.00 30.93 ? 541  THR A OG1 1 
ATOM   4391 C  CG2 . THR A 1 541  ? 57.453 83.453  -17.944 1.00 22.54 ? 541  THR A CG2 1 
ATOM   4392 N  N   . THR A 1 542  ? 56.481 85.566  -21.945 1.00 17.38 ? 542  THR A N   1 
ATOM   4393 C  CA  . THR A 1 542  ? 56.625 85.750  -23.374 1.00 14.52 ? 542  THR A CA  1 
ATOM   4394 C  C   . THR A 1 542  ? 58.087 85.503  -23.704 1.00 12.76 ? 542  THR A C   1 
ATOM   4395 O  O   . THR A 1 542  ? 58.988 85.947  -22.953 1.00 15.60 ? 542  THR A O   1 
ATOM   4396 C  CB  . THR A 1 542  ? 56.285 87.203  -23.766 1.00 15.80 ? 542  THR A CB  1 
ATOM   4397 O  OG1 . THR A 1 542  ? 54.928 87.468  -23.408 1.00 17.81 ? 542  THR A OG1 1 
ATOM   4398 C  CG2 . THR A 1 542  ? 56.450 87.436  -25.250 1.00 15.14 ? 542  THR A CG2 1 
ATOM   4399 N  N   . ILE A 1 543  ? 58.320 84.741  -24.754 1.00 11.41 ? 543  ILE A N   1 
ATOM   4400 C  CA  . ILE A 1 543  ? 59.704 84.536  -25.245 1.00 12.07 ? 543  ILE A CA  1 
ATOM   4401 C  C   . ILE A 1 543  ? 60.048 85.844  -26.035 1.00 11.54 ? 543  ILE A C   1 
ATOM   4402 O  O   . ILE A 1 543  ? 59.402 86.130  -27.060 1.00 13.15 ? 543  ILE A O   1 
ATOM   4403 C  CB  . ILE A 1 543  ? 59.763 83.315  -26.135 1.00 12.60 ? 543  ILE A CB  1 
ATOM   4404 C  CG1 . ILE A 1 543  ? 59.433 82.058  -25.267 1.00 13.56 ? 543  ILE A CG1 1 
ATOM   4405 C  CG2 . ILE A 1 543  ? 61.109 83.223  -26.867 1.00 13.04 ? 543  ILE A CG2 1 
ATOM   4406 C  CD1 . ILE A 1 543  ? 59.325 80.754  -26.065 1.00 12.46 ? 543  ILE A CD1 1 
ATOM   4407 N  N   . ILE A 1 544  ? 60.993 86.593  -25.489 1.00 13.08 ? 544  ILE A N   1 
ATOM   4408 C  CA  . ILE A 1 544  ? 61.384 87.877  -26.067 1.00 12.00 ? 544  ILE A CA  1 
ATOM   4409 C  C   . ILE A 1 544  ? 62.614 87.720  -26.980 1.00 13.61 ? 544  ILE A C   1 
ATOM   4410 O  O   . ILE A 1 544  ? 63.733 87.383  -26.538 1.00 14.69 ? 544  ILE A O   1 
ATOM   4411 C  CB  . ILE A 1 544  ? 61.585 88.908  -24.938 1.00 15.17 ? 544  ILE A CB  1 
ATOM   4412 C  CG1 . ILE A 1 544  ? 60.236 89.053  -24.194 1.00 18.39 ? 544  ILE A CG1 1 
ATOM   4413 C  CG2 . ILE A 1 544  ? 62.044 90.261  -25.549 1.00 18.37 ? 544  ILE A CG2 1 
ATOM   4414 C  CD1 . ILE A 1 544  ? 60.131 90.142  -23.156 1.00 24.23 ? 544  ILE A CD1 1 
ATOM   4415 N  N   . LEU A 1 545  ? 62.342 87.917  -28.268 1.00 12.37 ? 545  LEU A N   1 
ATOM   4416 C  CA  . LEU A 1 545  ? 63.371 87.790  -29.289 1.00 11.86 ? 545  LEU A CA  1 
ATOM   4417 C  C   . LEU A 1 545  ? 63.499 89.144  -29.995 1.00 14.71 ? 545  LEU A C   1 
ATOM   4418 O  O   . LEU A 1 545  ? 62.583 89.963  -30.002 1.00 16.31 ? 545  LEU A O   1 
ATOM   4419 C  CB  . LEU A 1 545  ? 62.971 86.690  -30.295 1.00 11.80 ? 545  LEU A CB  1 
ATOM   4420 C  CG  . LEU A 1 545  ? 62.739 85.268  -29.700 1.00 12.15 ? 545  LEU A CG  1 
ATOM   4421 C  CD1 . LEU A 1 545  ? 62.291 84.305  -30.836 1.00 16.74 ? 545  LEU A CD1 1 
ATOM   4422 C  CD2 . LEU A 1 545  ? 64.048 84.767  -29.082 1.00 13.01 ? 545  LEU A CD2 1 
ATOM   4423 N  N   . GLY A 1 546  ? 64.650 89.388  -30.587 1.00 14.54 ? 546  GLY A N   1 
ATOM   4424 C  CA  . GLY A 1 546  ? 64.835 90.644  -31.307 1.00 15.78 ? 546  GLY A CA  1 
ATOM   4425 C  C   . GLY A 1 546  ? 66.270 90.657  -31.758 1.00 13.80 ? 546  GLY A C   1 
ATOM   4426 O  O   . GLY A 1 546  ? 67.197 90.183  -31.082 1.00 14.68 ? 546  GLY A O   1 
ATOM   4427 N  N   . GLU A 1 547  ? 66.465 91.290  -32.913 1.00 17.05 ? 547  GLU A N   1 
ATOM   4428 C  CA  . GLU A 1 547  ? 67.809 91.403  -33.505 1.00 20.81 ? 547  GLU A CA  1 
ATOM   4429 C  C   . GLU A 1 547  ? 68.827 92.084  -32.568 1.00 22.13 ? 547  GLU A C   1 
ATOM   4430 O  O   . GLU A 1 547  ? 70.020 91.732  -32.525 1.00 23.83 ? 547  GLU A O   1 
ATOM   4431 C  CB  . GLU A 1 547  ? 67.732 92.178  -34.824 1.00 26.57 ? 547  GLU A CB  1 
ATOM   4432 C  CG  . GLU A 1 547  ? 69.086 92.268  -35.543 1.00 39.14 ? 547  GLU A CG  1 
ATOM   4433 C  CD  . GLU A 1 547  ? 69.102 93.311  -36.683 1.00 45.35 ? 547  GLU A CD  1 
ATOM   4434 O  OE1 . GLU A 1 547  ? 68.025 93.895  -36.994 1.00 47.76 ? 547  GLU A OE1 1 
ATOM   4435 O  OE2 . GLU A 1 547  ? 70.202 93.537  -37.263 1.00 49.00 ? 547  GLU A OE2 1 
ATOM   4436 N  N   . ASP A 1 548  ? 68.332 93.018  -31.767 1.00 17.05 ? 548  ASP A N   1 
ATOM   4437 C  CA  . ASP A 1 548  ? 69.194 93.717  -30.836 1.00 19.38 ? 548  ASP A CA  1 
ATOM   4438 C  C   . ASP A 1 548  ? 69.160 93.144  -29.437 1.00 20.96 ? 548  ASP A C   1 
ATOM   4439 O  O   . ASP A 1 548  ? 69.598 93.813  -28.505 1.00 23.42 ? 548  ASP A O   1 
ATOM   4440 C  CB  . ASP A 1 548  ? 68.800 95.195  -30.772 1.00 19.95 ? 548  ASP A CB  1 
ATOM   4441 C  CG  . ASP A 1 548  ? 69.000 95.894  -32.085 1.00 25.25 ? 548  ASP A CG  1 
ATOM   4442 O  OD1 . ASP A 1 548  ? 70.172 95.981  -32.527 1.00 28.88 ? 548  ASP A OD1 1 
ATOM   4443 O  OD2 . ASP A 1 548  ? 68.006 96.356  -32.682 1.00 29.28 ? 548  ASP A OD2 1 
ATOM   4444 N  N   . ILE A 1 549  ? 68.644 91.926  -29.244 1.00 17.12 ? 549  ILE A N   1 
ATOM   4445 C  CA  . ILE A 1 549  ? 68.625 91.377  -27.872 1.00 17.59 ? 549  ILE A CA  1 
ATOM   4446 C  C   . ILE A 1 549  ? 68.870 89.852  -27.818 1.00 19.09 ? 549  ILE A C   1 
ATOM   4447 O  O   . ILE A 1 549  ? 69.703 89.403  -27.024 1.00 18.99 ? 549  ILE A O   1 
ATOM   4448 C  CB  . ILE A 1 549  ? 67.265 91.730  -27.106 1.00 17.73 ? 549  ILE A CB  1 
ATOM   4449 C  CG1 . ILE A 1 549  ? 67.262 91.103  -25.696 1.00 22.60 ? 549  ILE A CG1 1 
ATOM   4450 C  CG2 . ILE A 1 549  ? 66.027 91.251  -27.852 1.00 17.32 ? 549  ILE A CG2 1 
ATOM   4451 C  CD1 . ILE A 1 549  ? 67.972 91.930  -24.698 1.00 29.37 ? 549  ILE A CD1 1 
ATOM   4452 N  N   . LEU A 1 550  ? 68.186 89.093  -28.680 1.00 15.06 ? 550  LEU A N   1 
ATOM   4453 C  CA  . LEU A 1 550  ? 68.311 87.643  -28.597 1.00 14.04 ? 550  LEU A CA  1 
ATOM   4454 C  C   . LEU A 1 550  ? 67.676 87.071  -29.846 1.00 13.53 ? 550  LEU A C   1 
ATOM   4455 O  O   . LEU A 1 550  ? 66.477 87.199  -30.086 1.00 15.34 ? 550  LEU A O   1 
ATOM   4456 C  CB  . LEU A 1 550  ? 67.563 87.145  -27.345 1.00 16.31 ? 550  LEU A CB  1 
ATOM   4457 C  CG  . LEU A 1 550  ? 67.613 85.623  -27.169 1.00 16.14 ? 550  LEU A CG  1 
ATOM   4458 C  CD1 . LEU A 1 550  ? 69.046 85.261  -26.936 1.00 16.86 ? 550  LEU A CD1 1 
ATOM   4459 C  CD2 . LEU A 1 550  ? 66.759 85.167  -26.006 1.00 17.10 ? 550  LEU A CD2 1 
ATOM   4460 N  N   . PRO A 1 551  ? 68.463 86.402  -30.689 1.00 13.49 ? 551  PRO A N   1 
ATOM   4461 C  CA  . PRO A 1 551  ? 67.826 85.896  -31.896 1.00 14.88 ? 551  PRO A CA  1 
ATOM   4462 C  C   . PRO A 1 551  ? 67.002 84.603  -31.800 1.00 13.20 ? 551  PRO A C   1 
ATOM   4463 O  O   . PRO A 1 551  ? 66.159 84.365  -32.666 1.00 14.68 ? 551  PRO A O   1 
ATOM   4464 C  CB  . PRO A 1 551  ? 68.992 85.718  -32.890 1.00 18.28 ? 551  PRO A CB  1 
ATOM   4465 C  CG  . PRO A 1 551  ? 70.119 85.545  -32.121 1.00 21.07 ? 551  PRO A CG  1 
ATOM   4466 C  CD  . PRO A 1 551  ? 69.928 86.397  -30.830 1.00 17.19 ? 551  PRO A CD  1 
ATOM   4467 N  N   . SER A 1 552  ? 67.293 83.781  -30.783 1.00 12.12 ? 552  SER A N   1 
ATOM   4468 C  CA  . SER A 1 552  ? 66.602 82.477  -30.722 1.00 11.51 ? 552  SER A CA  1 
ATOM   4469 C  C   . SER A 1 552  ? 66.507 81.986  -29.283 1.00 10.48 ? 552  SER A C   1 
ATOM   4470 O  O   . SER A 1 552  ? 67.147 82.494  -28.401 1.00 11.80 ? 552  SER A O   1 
ATOM   4471 C  CB  . SER A 1 552  ? 67.313 81.441  -31.569 1.00 12.34 ? 552  SER A CB  1 
ATOM   4472 O  OG  . SER A 1 552  ? 68.541 81.073  -31.011 1.00 15.63 ? 552  SER A OG  1 
ATOM   4473 N  N   . LYS A 1 553  ? 65.608 81.001  -29.123 1.00 11.61 ? 553  LYS A N   1 
ATOM   4474 C  CA  . LYS A 1 553  ? 65.332 80.421  -27.820 1.00 10.12 ? 553  LYS A CA  1 
ATOM   4475 C  C   . LYS A 1 553  ? 65.060 78.896  -27.947 1.00 10.20 ? 553  LYS A C   1 
ATOM   4476 O  O   . LYS A 1 553  ? 64.262 78.471  -28.785 1.00 10.69 ? 553  LYS A O   1 
ATOM   4477 C  CB  . LYS A 1 553  ? 64.033 81.066  -27.250 1.00 11.45 ? 553  LYS A CB  1 
ATOM   4478 C  CG  . LYS A 1 553  ? 63.563 80.518  -25.861 1.00 12.62 ? 553  LYS A CG  1 
ATOM   4479 C  CD  . LYS A 1 553  ? 64.621 80.636  -24.848 1.00 13.02 ? 553  LYS A CD  1 
ATOM   4480 C  CE  . LYS A 1 553  ? 64.808 82.095  -24.393 1.00 13.31 ? 553  LYS A CE  1 
ATOM   4481 N  NZ  . LYS A 1 553  ? 66.048 82.174  -23.473 1.00 15.04 ? 553  LYS A NZ  1 
ATOM   4482 N  N   . HIS A 1 554  ? 65.731 78.133  -27.081 1.00 9.59  ? 554  HIS A N   1 
ATOM   4483 C  CA  . HIS A 1 554  ? 65.431 76.697  -26.953 1.00 9.44  ? 554  HIS A CA  1 
ATOM   4484 C  C   . HIS A 1 554  ? 64.209 76.466  -26.030 1.00 8.49  ? 554  HIS A C   1 
ATOM   4485 O  O   . HIS A 1 554  ? 64.085 77.089  -24.974 1.00 10.46 ? 554  HIS A O   1 
ATOM   4486 C  CB  . HIS A 1 554  ? 66.658 75.943  -26.367 1.00 11.45 ? 554  HIS A CB  1 
ATOM   4487 C  CG  . HIS A 1 554  ? 67.781 75.816  -27.350 1.00 12.97 ? 554  HIS A CG  1 
ATOM   4488 N  ND1 . HIS A 1 554  ? 68.486 74.658  -27.612 1.00 19.88 ? 554  HIS A ND1 1 
ATOM   4489 C  CD2 . HIS A 1 554  ? 68.340 76.778  -28.136 1.00 15.94 ? 554  HIS A CD2 1 
ATOM   4490 C  CE1 . HIS A 1 554  ? 69.442 74.922  -28.493 1.00 14.80 ? 554  HIS A CE1 1 
ATOM   4491 N  NE2 . HIS A 1 554  ? 69.370 76.197  -28.824 1.00 23.87 ? 554  HIS A NE2 1 
ATOM   4492 N  N   . VAL A 1 555  ? 63.355 75.540  -26.477 1.00 8.98  ? 555  VAL A N   1 
ATOM   4493 C  CA  . VAL A 1 555  ? 62.221 75.056  -25.686 1.00 9.79  ? 555  VAL A CA  1 
ATOM   4494 C  C   . VAL A 1 555  ? 62.302 73.532  -25.662 1.00 9.16  ? 555  VAL A C   1 
ATOM   4495 O  O   . VAL A 1 555  ? 62.859 72.904  -26.589 1.00 9.93  ? 555  VAL A O   1 
ATOM   4496 C  CB  . VAL A 1 555  ? 60.877 75.524  -26.225 1.00 9.08  ? 555  VAL A CB  1 
ATOM   4497 C  CG1 . VAL A 1 555  ? 60.819 77.042  -26.151 1.00 10.64 ? 555  VAL A CG1 1 
ATOM   4498 C  CG2 . VAL A 1 555  ? 60.647 75.035  -27.624 1.00 10.84 ? 555  VAL A CG2 1 
ATOM   4499 N  N   . VAL A 1 556  ? 61.764 72.918  -24.600 1.00 8.05  ? 556  VAL A N   1 
ATOM   4500 C  CA  . VAL A 1 556  ? 61.821 71.453  -24.468 1.00 8.63  ? 556  VAL A CA  1 
ATOM   4501 C  C   . VAL A 1 556  ? 60.430 70.949  -24.069 1.00 8.28  ? 556  VAL A C   1 
ATOM   4502 O  O   . VAL A 1 556  ? 59.790 71.542  -23.168 1.00 8.41  ? 556  VAL A O   1 
ATOM   4503 C  CB  . VAL A 1 556  ? 62.832 71.031  -23.354 1.00 8.72  ? 556  VAL A CB  1 
ATOM   4504 C  CG1 . VAL A 1 556  ? 62.776 69.498  -23.131 1.00 8.85  ? 556  VAL A CG1 1 
ATOM   4505 C  CG2 . VAL A 1 556  ? 64.255 71.446  -23.743 1.00 10.54 ? 556  VAL A CG2 1 
ATOM   4506 N  N   . MET A 1 557  ? 60.006 69.866  -24.697 1.00 7.56  ? 557  MET A N   1 
ATOM   4507 C  CA  . MET A 1 557  ? 58.741 69.207  -24.316 1.00 8.50  ? 557  MET A CA  1 
ATOM   4508 C  C   . MET A 1 557  ? 59.016 67.879  -23.646 1.00 8.15  ? 557  MET A C   1 
ATOM   4509 O  O   . MET A 1 557  ? 59.917 67.136  -24.071 1.00 8.63  ? 557  MET A O   1 
ATOM   4510 C  CB  . MET A 1 557  ? 57.843 68.936  -25.526 1.00 8.34  ? 557  MET A CB  1 
ATOM   4511 C  CG  . MET A 1 557  ? 56.843 70.057  -25.820 1.00 9.85  ? 557  MET A CG  1 
ATOM   4512 S  SD  . MET A 1 557  ? 57.514 71.730  -26.009 1.00 10.72 ? 557  MET A SD  1 
ATOM   4513 C  CE  . MET A 1 557  ? 58.567 71.481  -27.477 1.00 13.58 ? 557  MET A CE  1 
ATOM   4514 N  N   . HIS A 1 558  ? 58.242 67.564  -22.595 1.00 7.69  ? 558  HIS A N   1 
ATOM   4515 C  CA  . HIS A 1 558  ? 58.306 66.254  -21.930 1.00 6.40  ? 558  HIS A CA  1 
ATOM   4516 C  C   . HIS A 1 558  ? 57.009 65.507  -22.173 1.00 8.37  ? 558  HIS A C   1 
ATOM   4517 O  O   . HIS A 1 558  ? 55.908 66.109  -22.160 1.00 8.67  ? 558  HIS A O   1 
ATOM   4518 C  CB  . HIS A 1 558  ? 58.489 66.442  -20.443 1.00 8.43  ? 558  HIS A CB  1 
ATOM   4519 C  CG  . HIS A 1 558  ? 58.402 65.161  -19.657 1.00 7.16  ? 558  HIS A CG  1 
ATOM   4520 N  ND1 . HIS A 1 558  ? 57.463 65.006  -18.654 1.00 7.89  ? 558  HIS A ND1 1 
ATOM   4521 C  CD2 . HIS A 1 558  ? 59.144 64.017  -19.664 1.00 7.47  ? 558  HIS A CD2 1 
ATOM   4522 C  CE1 . HIS A 1 558  ? 57.655 63.817  -18.083 1.00 8.05  ? 558  HIS A CE1 1 
ATOM   4523 N  NE2 . HIS A 1 558  ? 58.665 63.190  -18.667 1.00 9.32  ? 558  HIS A NE2 1 
ATOM   4524 N  N   . ASN A 1 559  ? 57.131 64.181  -22.379 1.00 7.21  ? 559  ASN A N   1 
ATOM   4525 C  CA  . ASN A 1 559  ? 55.986 63.327  -22.572 1.00 6.44  ? 559  ASN A CA  1 
ATOM   4526 C  C   . ASN A 1 559  ? 56.004 62.235  -21.502 1.00 6.80  ? 559  ASN A C   1 
ATOM   4527 O  O   . ASN A 1 559  ? 56.760 61.266  -21.630 1.00 8.77  ? 559  ASN A O   1 
ATOM   4528 C  CB  . ASN A 1 559  ? 56.086 62.694  -23.964 1.00 7.78  ? 559  ASN A CB  1 
ATOM   4529 C  CG  . ASN A 1 559  ? 55.048 61.588  -24.174 1.00 8.13  ? 559  ASN A CG  1 
ATOM   4530 O  OD1 . ASN A 1 559  ? 53.945 61.576  -23.601 1.00 9.38  ? 559  ASN A OD1 1 
ATOM   4531 N  ND2 . ASN A 1 559  ? 55.388 60.624  -25.051 1.00 9.28  ? 559  ASN A ND2 1 
ATOM   4532 N  N   . THR A 1 560  ? 55.133 62.340  -20.492 1.00 7.37  ? 560  THR A N   1 
ATOM   4533 C  CA  . THR A 1 560  ? 55.152 61.352  -19.395 1.00 6.99  ? 560  THR A CA  1 
ATOM   4534 C  C   . THR A 1 560  ? 54.558 60.003  -19.820 1.00 8.14  ? 560  THR A C   1 
ATOM   4535 O  O   . THR A 1 560  ? 54.744 59.028  -19.102 1.00 8.03  ? 560  THR A O   1 
ATOM   4536 C  CB  . THR A 1 560  ? 54.393 61.965  -18.205 1.00 6.96  ? 560  THR A CB  1 
ATOM   4537 O  OG1 . THR A 1 560  ? 54.690 61.214  -17.006 1.00 8.10  ? 560  THR A OG1 1 
ATOM   4538 C  CG2 . THR A 1 560  ? 52.877 62.004  -18.371 1.00 8.30  ? 560  THR A CG2 1 
ATOM   4539 N  N   . LEU A 1 561  ? 53.823 59.931  -20.921 1.00 8.27  ? 561  LEU A N   1 
ATOM   4540 C  CA  . LEU A 1 561  ? 53.216 58.649  -21.337 1.00 7.06  ? 561  LEU A CA  1 
ATOM   4541 C  C   . LEU A 1 561  ? 54.230 57.748  -22.018 1.00 7.84  ? 561  LEU A C   1 
ATOM   4542 O  O   . LEU A 1 561  ? 55.135 58.209  -22.727 1.00 8.56  ? 561  LEU A O   1 
ATOM   4543 C  CB  . LEU A 1 561  ? 52.064 58.942  -22.307 1.00 8.88  ? 561  LEU A CB  1 
ATOM   4544 C  CG  . LEU A 1 561  ? 50.964 59.881  -21.753 1.00 8.94  ? 561  LEU A CG  1 
ATOM   4545 C  CD1 . LEU A 1 561  ? 49.847 60.034  -22.842 1.00 11.45 ? 561  LEU A CD1 1 
ATOM   4546 C  CD2 . LEU A 1 561  ? 50.269 59.286  -20.506 1.00 9.68  ? 561  LEU A CD2 1 
ATOM   4547 N  N   . PRO A 1 562  ? 54.085 56.431  -21.850 1.00 8.21  ? 562  PRO A N   1 
ATOM   4548 C  CA  . PRO A 1 562  ? 55.040 55.469  -22.434 1.00 8.10  ? 562  PRO A CA  1 
ATOM   4549 C  C   . PRO A 1 562  ? 54.838 55.104  -23.885 1.00 8.96  ? 562  PRO A C   1 
ATOM   4550 O  O   . PRO A 1 562  ? 55.002 53.943  -24.266 1.00 10.53 ? 562  PRO A O   1 
ATOM   4551 C  CB  . PRO A 1 562  ? 54.883 54.277  -21.487 1.00 9.24  ? 562  PRO A CB  1 
ATOM   4552 C  CG  . PRO A 1 562  ? 53.399 54.273  -21.180 1.00 8.85  ? 562  PRO A CG  1 
ATOM   4553 C  CD  . PRO A 1 562  ? 53.102 55.764  -20.964 1.00 8.45  ? 562  PRO A CD  1 
ATOM   4554 N  N   . HIS A 1 563  ? 54.489 56.071  -24.715 1.00 8.70  ? 563  HIS A N   1 
ATOM   4555 C  CA  . HIS A 1 563  ? 54.436 55.815  -26.158 1.00 9.27  ? 563  HIS A CA  1 
ATOM   4556 C  C   . HIS A 1 563  ? 54.829 57.122  -26.825 1.00 9.64  ? 563  HIS A C   1 
ATOM   4557 O  O   . HIS A 1 563  ? 54.649 58.224  -26.244 1.00 9.51  ? 563  HIS A O   1 
ATOM   4558 C  CB  . HIS A 1 563  ? 53.033 55.349  -26.632 1.00 10.02 ? 563  HIS A CB  1 
ATOM   4559 C  CG  . HIS A 1 563  ? 51.890 56.220  -26.181 1.00 10.23 ? 563  HIS A CG  1 
ATOM   4560 N  ND1 . HIS A 1 563  ? 51.085 55.894  -25.101 1.00 10.55 ? 563  HIS A ND1 1 
ATOM   4561 C  CD2 . HIS A 1 563  ? 51.392 57.390  -26.673 1.00 10.82 ? 563  HIS A CD2 1 
ATOM   4562 C  CE1 . HIS A 1 563  ? 50.134 56.810  -24.960 1.00 11.77 ? 563  HIS A CE1 1 
ATOM   4563 N  NE2 . HIS A 1 563  ? 50.302 57.735  -25.895 1.00 11.60 ? 563  HIS A NE2 1 
ATOM   4564 N  N   . TRP A 1 564  ? 55.343 57.040  -28.043 1.00 9.90  ? 564  TRP A N   1 
ATOM   4565 C  CA  . TRP A 1 564  ? 55.641 58.232  -28.838 1.00 8.71  ? 564  TRP A CA  1 
ATOM   4566 C  C   . TRP A 1 564  ? 54.372 59.058  -28.963 1.00 10.02 ? 564  TRP A C   1 
ATOM   4567 O  O   . TRP A 1 564  ? 53.236 58.546  -29.141 1.00 11.01 ? 564  TRP A O   1 
ATOM   4568 C  CB  . TRP A 1 564  ? 56.091 57.864  -30.285 1.00 11.82 ? 564  TRP A CB  1 
ATOM   4569 C  CG  . TRP A 1 564  ? 57.543 57.445  -30.350 1.00 10.25 ? 564  TRP A CG  1 
ATOM   4570 C  CD1 . TRP A 1 564  ? 58.045 56.146  -30.204 1.00 11.75 ? 564  TRP A CD1 1 
ATOM   4571 C  CD2 . TRP A 1 564  ? 58.683 58.295  -30.505 1.00 11.40 ? 564  TRP A CD2 1 
ATOM   4572 N  NE1 . TRP A 1 564  ? 59.384 56.192  -30.259 1.00 13.34 ? 564  TRP A NE1 1 
ATOM   4573 C  CE2 . TRP A 1 564  ? 59.833 57.478  -30.440 1.00 12.34 ? 564  TRP A CE2 1 
ATOM   4574 C  CE3 . TRP A 1 564  ? 58.838 59.682  -30.697 1.00 14.34 ? 564  TRP A CE3 1 
ATOM   4575 C  CZ2 . TRP A 1 564  ? 61.144 57.996  -30.555 1.00 14.56 ? 564  TRP A CZ2 1 
ATOM   4576 C  CZ3 . TRP A 1 564  ? 60.142 60.210  -30.808 1.00 13.89 ? 564  TRP A CZ3 1 
ATOM   4577 C  CH2 . TRP A 1 564  ? 61.278 59.364  -30.740 1.00 15.83 ? 564  TRP A CH2 1 
ATOM   4578 N  N   . ARG A 1 565  ? 54.514 60.372  -28.868 1.00 9.95  ? 565  ARG A N   1 
ATOM   4579 C  CA  . ARG A 1 565  ? 53.305 61.174  -28.927 1.00 10.37 ? 565  ARG A CA  1 
ATOM   4580 C  C   . ARG A 1 565  ? 53.572 62.472  -29.669 1.00 10.20 ? 565  ARG A C   1 
ATOM   4581 O  O   . ARG A 1 565  ? 54.596 63.126  -29.421 1.00 11.23 ? 565  ARG A O   1 
ATOM   4582 C  CB  . ARG A 1 565  ? 52.790 61.503  -27.477 1.00 11.65 ? 565  ARG A CB  1 
ATOM   4583 C  CG  . ARG A 1 565  ? 51.476 62.342  -27.504 1.00 13.42 ? 565  ARG A CG  1 
ATOM   4584 C  CD  . ARG A 1 565  ? 50.612 62.273  -26.175 1.00 15.05 ? 565  ARG A CD  1 
ATOM   4585 N  NE  . ARG A 1 565  ? 51.398 62.572  -24.991 1.00 15.00 ? 565  ARG A NE  1 
ATOM   4586 C  CZ  . ARG A 1 565  ? 50.898 63.144  -23.902 1.00 11.80 ? 565  ARG A CZ  1 
ATOM   4587 N  NH1 . ARG A 1 565  ? 49.609 63.525  -23.838 1.00 12.25 ? 565  ARG A NH1 1 
ATOM   4588 N  NH2 . ARG A 1 565  ? 51.699 63.278  -22.876 1.00 11.54 ? 565  ARG A NH2 1 
ATOM   4589 N  N   . GLU A 1 566  ? 52.633 62.836  -30.535 1.00 10.92 ? 566  GLU A N   1 
ATOM   4590 C  CA  . GLU A 1 566  ? 52.647 64.184  -31.138 1.00 11.65 ? 566  GLU A CA  1 
ATOM   4591 C  C   . GLU A 1 566  ? 51.498 64.982  -30.537 1.00 11.99 ? 566  GLU A C   1 
ATOM   4592 O  O   . GLU A 1 566  ? 50.407 64.451  -30.261 1.00 13.00 ? 566  GLU A O   1 
ATOM   4593 C  CB  . GLU A 1 566  ? 52.419 64.093  -32.633 1.00 14.37 ? 566  GLU A CB  1 
ATOM   4594 C  CG  . GLU A 1 566  ? 53.530 63.479  -33.352 1.00 14.65 ? 566  GLU A CG  1 
ATOM   4595 C  CD  . GLU A 1 566  ? 53.251 63.426  -34.872 1.00 18.78 ? 566  GLU A CD  1 
ATOM   4596 O  OE1 . GLU A 1 566  ? 52.069 63.231  -35.281 1.00 21.95 ? 566  GLU A OE1 1 
ATOM   4597 O  OE2 . GLU A 1 566  ? 54.230 63.619  -35.610 1.00 22.91 ? 566  GLU A OE2 1 
ATOM   4598 N  N   . GLN A 1 567  ? 51.722 66.278  -30.348 1.00 11.22 ? 567  GLN A N   1 
ATOM   4599 C  CA  . GLN A 1 567  ? 50.681 67.169  -29.832 1.00 10.09 ? 567  GLN A CA  1 
ATOM   4600 C  C   . GLN A 1 567  ? 51.086 68.574  -30.242 1.00 11.14 ? 567  GLN A C   1 
ATOM   4601 O  O   . GLN A 1 567  ? 52.297 68.919  -30.285 1.00 10.13 ? 567  GLN A O   1 
ATOM   4602 C  CB  . GLN A 1 567  ? 50.642 67.115  -28.282 1.00 11.37 ? 567  GLN A CB  1 
ATOM   4603 C  CG  . GLN A 1 567  ? 49.516 67.911  -27.655 1.00 11.49 ? 567  GLN A CG  1 
ATOM   4604 C  CD  . GLN A 1 567  ? 49.896 68.360  -26.254 1.00 13.52 ? 567  GLN A CD  1 
ATOM   4605 O  OE1 . GLN A 1 567  ? 49.906 67.547  -25.315 1.00 12.79 ? 567  GLN A OE1 1 
ATOM   4606 N  NE2 . GLN A 1 567  ? 50.307 69.633  -26.101 1.00 16.94 ? 567  GLN A NE2 1 
ATOM   4607 N  N   . LEU A 1 568  ? 50.086 69.369  -30.601 1.00 11.02 ? 568  LEU A N   1 
ATOM   4608 C  CA  . LEU A 1 568  ? 50.409 70.788  -30.857 1.00 10.60 ? 568  LEU A CA  1 
ATOM   4609 C  C   . LEU A 1 568  ? 50.744 71.473  -29.539 1.00 10.42 ? 568  LEU A C   1 
ATOM   4610 O  O   . LEU A 1 568  ? 50.070 71.225  -28.497 1.00 11.32 ? 568  LEU A O   1 
ATOM   4611 C  CB  . LEU A 1 568  ? 49.239 71.585  -31.478 1.00 12.35 ? 568  LEU A CB  1 
ATOM   4612 C  CG  . LEU A 1 568  ? 48.778 71.104  -32.858 1.00 14.00 ? 568  LEU A CG  1 
ATOM   4613 C  CD1 . LEU A 1 568  ? 47.811 72.168  -33.442 1.00 15.39 ? 568  LEU A CD1 1 
ATOM   4614 C  CD2 . LEU A 1 568  ? 49.955 70.975  -33.799 1.00 16.12 ? 568  LEU A CD2 1 
ATOM   4615 N  N   . VAL A 1 569  ? 51.743 72.315  -29.564 1.00 9.02  ? 569  VAL A N   1 
ATOM   4616 C  CA  . VAL A 1 569  ? 52.134 73.101  -28.412 1.00 9.25  ? 569  VAL A CA  1 
ATOM   4617 C  C   . VAL A 1 569  ? 52.195 74.572  -28.833 1.00 9.41  ? 569  VAL A C   1 
ATOM   4618 O  O   . VAL A 1 569  ? 52.431 74.896  -29.998 1.00 11.07 ? 569  VAL A O   1 
ATOM   4619 C  CB  . VAL A 1 569  ? 53.510 72.670  -27.824 1.00 9.25  ? 569  VAL A CB  1 
ATOM   4620 C  CG1 . VAL A 1 569  ? 53.371 71.270  -27.159 1.00 11.06 ? 569  VAL A CG1 1 
ATOM   4621 C  CG2 . VAL A 1 569  ? 54.639 72.687  -28.895 1.00 11.40 ? 569  VAL A CG2 1 
ATOM   4622 N  N   . ASP A 1 570  ? 51.956 75.455  -27.882 1.00 9.73  ? 570  ASP A N   1 
ATOM   4623 C  CA  . ASP A 1 570  ? 52.014 76.881  -28.220 1.00 9.82  ? 570  ASP A CA  1 
ATOM   4624 C  C   . ASP A 1 570  ? 52.813 77.629  -27.198 1.00 10.93 ? 570  ASP A C   1 
ATOM   4625 O  O   . ASP A 1 570  ? 52.912 77.243  -26.008 1.00 13.16 ? 570  ASP A O   1 
ATOM   4626 C  CB  . ASP A 1 570  ? 50.592 77.478  -28.357 1.00 11.94 ? 570  ASP A CB  1 
ATOM   4627 C  CG  . ASP A 1 570  ? 49.881 77.610  -27.037 1.00 19.59 ? 570  ASP A CG  1 
ATOM   4628 O  OD1 . ASP A 1 570  ? 49.723 76.603  -26.356 1.00 26.61 ? 570  ASP A OD1 1 
ATOM   4629 O  OD2 . ASP A 1 570  ? 49.498 78.709  -26.612 1.00 26.44 ? 570  ASP A OD2 1 
ATOM   4630 N  N   . PHE A 1 571  ? 53.440 78.716  -27.661 1.00 10.30 ? 571  PHE A N   1 
ATOM   4631 C  CA  . PHE A 1 571  ? 54.223 79.603  -26.796 1.00 10.42 ? 571  PHE A CA  1 
ATOM   4632 C  C   . PHE A 1 571  ? 53.870 81.052  -27.185 1.00 9.81  ? 571  PHE A C   1 
ATOM   4633 O  O   . PHE A 1 571  ? 53.552 81.307  -28.339 1.00 12.25 ? 571  PHE A O   1 
ATOM   4634 C  CB  . PHE A 1 571  ? 55.741 79.425  -27.062 1.00 11.06 ? 571  PHE A CB  1 
ATOM   4635 C  CG  . PHE A 1 571  ? 56.282 78.073  -26.643 1.00 9.32  ? 571  PHE A CG  1 
ATOM   4636 C  CD1 . PHE A 1 571  ? 56.254 77.007  -27.500 1.00 9.89  ? 571  PHE A CD1 1 
ATOM   4637 C  CD2 . PHE A 1 571  ? 56.737 77.907  -25.358 1.00 10.90 ? 571  PHE A CD2 1 
ATOM   4638 C  CE1 . PHE A 1 571  ? 56.680 75.727  -27.089 1.00 10.57 ? 571  PHE A CE1 1 
ATOM   4639 C  CE2 . PHE A 1 571  ? 57.162 76.650  -24.913 1.00 11.11 ? 571  PHE A CE2 1 
ATOM   4640 C  CZ  . PHE A 1 571  ? 57.141 75.566  -25.788 1.00 11.36 ? 571  PHE A CZ  1 
ATOM   4641 N  N   . TYR A 1 572  ? 54.001 81.969  -26.241 1.00 9.80  ? 572  TYR A N   1 
ATOM   4642 C  CA  . TYR A 1 572  ? 53.866 83.400  -26.540 1.00 10.17 ? 572  TYR A CA  1 
ATOM   4643 C  C   . TYR A 1 572  ? 55.263 83.887  -26.939 1.00 11.10 ? 572  TYR A C   1 
ATOM   4644 O  O   . TYR A 1 572  ? 56.272 83.569  -26.278 1.00 11.20 ? 572  TYR A O   1 
ATOM   4645 C  CB  . TYR A 1 572  ? 53.453 84.186  -25.299 1.00 11.91 ? 572  TYR A CB  1 
ATOM   4646 C  CG  . TYR A 1 572  ? 52.032 84.020  -24.842 1.00 16.06 ? 572  TYR A CG  1 
ATOM   4647 C  CD1 . TYR A 1 572  ? 51.065 83.437  -25.643 1.00 16.81 ? 572  TYR A CD1 1 
ATOM   4648 C  CD2 . TYR A 1 572  ? 51.651 84.515  -23.593 1.00 23.05 ? 572  TYR A CD2 1 
ATOM   4649 C  CE1 . TYR A 1 572  ? 49.710 83.343  -25.225 1.00 17.69 ? 572  TYR A CE1 1 
ATOM   4650 C  CE2 . TYR A 1 572  ? 50.324 84.437  -23.173 1.00 22.17 ? 572  TYR A CE2 1 
ATOM   4651 C  CZ  . TYR A 1 572  ? 49.366 83.857  -23.991 1.00 20.68 ? 572  TYR A CZ  1 
ATOM   4652 O  OH  . TYR A 1 572  ? 48.038 83.803  -23.577 1.00 21.21 ? 572  TYR A OH  1 
ATOM   4653 N  N   . VAL A 1 573  ? 55.288 84.675  -28.015 1.00 11.33 ? 573  VAL A N   1 
ATOM   4654 C  CA  . VAL A 1 573  ? 56.536 85.252  -28.563 1.00 10.62 ? 573  VAL A CA  1 
ATOM   4655 C  C   . VAL A 1 573  ? 56.297 86.740  -28.823 1.00 10.69 ? 573  VAL A C   1 
ATOM   4656 O  O   . VAL A 1 573  ? 55.171 87.217  -29.077 1.00 12.56 ? 573  VAL A O   1 
ATOM   4657 C  CB  . VAL A 1 573  ? 56.986 84.542  -29.857 1.00 12.02 ? 573  VAL A CB  1 
ATOM   4658 C  CG1 . VAL A 1 573  ? 57.526 83.133  -29.548 1.00 14.83 ? 573  VAL A CG1 1 
ATOM   4659 C  CG2 . VAL A 1 573  ? 55.870 84.457  -30.862 1.00 13.95 ? 573  VAL A CG2 1 
ATOM   4660 N  N   . SER A 1 574  ? 57.402 87.485  -28.810 1.00 11.94 ? 574  SER A N   1 
ATOM   4661 C  CA  . SER A 1 574  ? 57.299 88.968  -28.943 1.00 12.23 ? 574  SER A CA  1 
ATOM   4662 C  C   . SER A 1 574  ? 57.277 89.466  -30.378 1.00 14.32 ? 574  SER A C   1 
ATOM   4663 O  O   . SER A 1 574  ? 57.221 90.716  -30.580 1.00 18.22 ? 574  SER A O   1 
ATOM   4664 C  CB  . SER A 1 574  ? 58.444 89.641  -28.195 1.00 14.73 ? 574  SER A CB  1 
ATOM   4665 O  OG  . SER A 1 574  ? 59.696 89.293  -28.744 1.00 13.55 ? 574  SER A OG  1 
ATOM   4666 N  N   . SER A 1 575  ? 57.309 88.567  -31.356 1.00 14.30 ? 575  SER A N   1 
ATOM   4667 C  CA  . SER A 1 575  ? 57.225 88.917  -32.767 1.00 15.80 ? 575  SER A CA  1 
ATOM   4668 C  C   . SER A 1 575  ? 56.456 87.845  -33.511 1.00 16.10 ? 575  SER A C   1 
ATOM   4669 O  O   . SER A 1 575  ? 56.503 86.668  -33.133 1.00 14.85 ? 575  SER A O   1 
ATOM   4670 C  CB  . SER A 1 575  ? 58.637 88.933  -33.382 1.00 18.13 ? 575  SER A CB  1 
ATOM   4671 O  OG  . SER A 1 575  ? 58.619 88.990  -34.808 1.00 16.75 ? 575  SER A OG  1 
ATOM   4672 N  N   . PRO A 1 576  ? 55.749 88.209  -34.573 1.00 15.72 ? 576  PRO A N   1 
ATOM   4673 C  CA  . PRO A 1 576  ? 55.023 87.204  -35.346 1.00 13.37 ? 576  PRO A CA  1 
ATOM   4674 C  C   . PRO A 1 576  ? 55.953 86.481  -36.349 1.00 13.45 ? 576  PRO A C   1 
ATOM   4675 O  O   . PRO A 1 576  ? 55.586 85.485  -36.980 1.00 15.20 ? 576  PRO A O   1 
ATOM   4676 C  CB  . PRO A 1 576  ? 53.915 88.030  -36.038 1.00 15.64 ? 576  PRO A CB  1 
ATOM   4677 C  CG  . PRO A 1 576  ? 54.614 89.399  -36.219 1.00 20.26 ? 576  PRO A CG  1 
ATOM   4678 C  CD  . PRO A 1 576  ? 55.474 89.595  -35.025 1.00 16.47 ? 576  PRO A CD  1 
ATOM   4679 N  N   . PHE A 1 577  ? 57.164 87.017  -36.543 1.00 13.64 ? 577  PHE A N   1 
ATOM   4680 C  CA  . PHE A 1 577  ? 58.077 86.461  -37.530 1.00 14.71 ? 577  PHE A CA  1 
ATOM   4681 C  C   . PHE A 1 577  ? 59.054 85.512  -36.878 1.00 15.18 ? 577  PHE A C   1 
ATOM   4682 O  O   . PHE A 1 577  ? 60.222 85.813  -36.659 1.00 15.91 ? 577  PHE A O   1 
ATOM   4683 C  CB  . PHE A 1 577  ? 58.797 87.605  -38.260 1.00 15.06 ? 577  PHE A CB  1 
ATOM   4684 C  CG  . PHE A 1 577  ? 57.838 88.598  -38.892 1.00 19.22 ? 577  PHE A CG  1 
ATOM   4685 C  CD1 . PHE A 1 577  ? 58.031 89.977  -38.680 1.00 22.93 ? 577  PHE A CD1 1 
ATOM   4686 C  CD2 . PHE A 1 577  ? 56.822 88.174  -39.720 1.00 17.36 ? 577  PHE A CD2 1 
ATOM   4687 C  CE1 . PHE A 1 577  ? 57.209 90.920  -39.305 1.00 24.17 ? 577  PHE A CE1 1 
ATOM   4688 C  CE2 . PHE A 1 577  ? 55.975 89.120  -40.366 1.00 20.13 ? 577  PHE A CE2 1 
ATOM   4689 C  CZ  . PHE A 1 577  ? 56.199 90.488  -40.137 1.00 24.66 ? 577  PHE A CZ  1 
ATOM   4690 N  N   . VAL A 1 578  ? 58.505 84.339  -36.552 1.00 12.70 ? 578  VAL A N   1 
ATOM   4691 C  CA  . VAL A 1 578  ? 59.281 83.332  -35.834 1.00 14.04 ? 578  VAL A CA  1 
ATOM   4692 C  C   . VAL A 1 578  ? 59.140 82.003  -36.523 1.00 12.66 ? 578  VAL A C   1 
ATOM   4693 O  O   . VAL A 1 578  ? 58.086 81.666  -37.023 1.00 14.20 ? 578  VAL A O   1 
ATOM   4694 C  CB  . VAL A 1 578  ? 58.779 83.245  -34.326 1.00 14.01 ? 578  VAL A CB  1 
ATOM   4695 C  CG1 . VAL A 1 578  ? 59.531 82.067  -33.585 1.00 15.97 ? 578  VAL A CG1 1 
ATOM   4696 C  CG2 . VAL A 1 578  ? 59.047 84.487  -33.619 1.00 15.82 ? 578  VAL A CG2 1 
ATOM   4697 N  N   . SER A 1 579  ? 60.253 81.282  -36.599 1.00 15.34 ? 579  SER A N   1 
ATOM   4698 C  CA  . SER A 1 579  ? 60.173 79.960  -37.179 1.00 15.86 ? 579  SER A CA  1 
ATOM   4699 C  C   . SER A 1 579  ? 60.756 78.937  -36.206 1.00 11.94 ? 579  SER A C   1 
ATOM   4700 O  O   . SER A 1 579  ? 61.523 79.266  -35.306 1.00 13.08 ? 579  SER A O   1 
ATOM   4701 C  CB  . SER A 1 579  ? 60.798 79.901  -38.562 1.00 21.78 ? 579  SER A CB  1 
ATOM   4702 O  OG  . SER A 1 579  ? 62.076 80.393  -38.490 1.00 23.72 ? 579  SER A OG  1 
ATOM   4703 N  N   . VAL A 1 580  ? 60.377 77.703  -36.465 1.00 11.01 ? 580  VAL A N   1 
ATOM   4704 C  CA  . VAL A 1 580  ? 60.723 76.621  -35.558 1.00 10.58 ? 580  VAL A CA  1 
ATOM   4705 C  C   . VAL A 1 580  ? 61.601 75.588  -36.273 1.00 12.46 ? 580  VAL A C   1 
ATOM   4706 O  O   . VAL A 1 580  ? 61.340 75.240  -37.446 1.00 12.98 ? 580  VAL A O   1 
ATOM   4707 C  CB  . VAL A 1 580  ? 59.424 75.920  -35.070 1.00 10.54 ? 580  VAL A CB  1 
ATOM   4708 C  CG1 . VAL A 1 580  ? 59.752 74.795  -34.067 1.00 12.59 ? 580  VAL A CG1 1 
ATOM   4709 C  CG2 . VAL A 1 580  ? 58.491 76.937  -34.407 1.00 12.56 ? 580  VAL A CG2 1 
ATOM   4710 N  N   . THR A 1 581  ? 62.577 75.077  -35.537 1.00 10.43 ? 581  THR A N   1 
ATOM   4711 C  CA  . THR A 1 581  ? 63.440 73.987  -36.010 1.00 12.52 ? 581  THR A CA  1 
ATOM   4712 C  C   . THR A 1 581  ? 63.596 72.974  -34.878 1.00 11.93 ? 581  THR A C   1 
ATOM   4713 O  O   . THR A 1 581  ? 63.397 73.300  -33.696 1.00 12.15 ? 581  THR A O   1 
ATOM   4714 C  CB  . THR A 1 581  ? 64.874 74.475  -36.405 1.00 14.04 ? 581  THR A CB  1 
ATOM   4715 O  OG1 . THR A 1 581  ? 65.374 75.390  -35.424 1.00 16.50 ? 581  THR A OG1 1 
ATOM   4716 C  CG2 . THR A 1 581  ? 64.769 75.284  -37.740 1.00 12.49 ? 581  THR A CG2 1 
ATOM   4717 N  N   . ASP A 1 582  ? 63.930 71.742  -35.244 1.00 13.64 ? 582  ASP A N   1 
ATOM   4718 C  CA  . ASP A 1 582  ? 64.284 70.708  -34.254 1.00 14.02 ? 582  ASP A CA  1 
ATOM   4719 C  C   . ASP A 1 582  ? 65.801 70.857  -34.015 1.00 16.37 ? 582  ASP A C   1 
ATOM   4720 O  O   . ASP A 1 582  ? 66.435 71.740  -34.565 1.00 18.14 ? 582  ASP A O   1 
ATOM   4721 C  CB  . ASP A 1 582  ? 63.817 69.306  -34.676 1.00 19.93 ? 582  ASP A CB  1 
ATOM   4722 C  CG  . ASP A 1 582  ? 64.532 68.741  -35.912 1.00 18.86 ? 582  ASP A CG  1 
ATOM   4723 O  OD1 . ASP A 1 582  ? 63.999 67.722  -36.430 1.00 21.54 ? 582  ASP A OD1 1 
ATOM   4724 O  OD2 . ASP A 1 582  ? 65.571 69.284  -36.317 1.00 16.77 ? 582  ASP A OD2 1 
ATOM   4725 N  N   . LEU A 1 583  ? 66.427 70.050  -33.146 1.00 23.43 ? 583  LEU A N   1 
ATOM   4726 C  CA  . LEU A 1 583  ? 67.839 70.368  -32.942 1.00 24.78 ? 583  LEU A CA  1 
ATOM   4727 C  C   . LEU A 1 583  ? 68.746 69.928  -34.082 1.00 27.52 ? 583  LEU A C   1 
ATOM   4728 O  O   . LEU A 1 583  ? 69.922 70.336  -34.124 1.00 29.97 ? 583  LEU A O   1 
ATOM   4729 C  CB  . LEU A 1 583  ? 68.374 69.857  -31.573 1.00 25.51 ? 583  LEU A CB  1 
ATOM   4730 C  CG  . LEU A 1 583  ? 69.289 70.856  -30.833 1.00 21.97 ? 583  LEU A CG  1 
ATOM   4731 C  CD1 . LEU A 1 583  ? 68.566 72.186  -30.745 1.00 28.21 ? 583  LEU A CD1 1 
ATOM   4732 C  CD2 . LEU A 1 583  ? 69.653 70.418  -29.404 1.00 27.14 ? 583  LEU A CD2 1 
ATOM   4733 N  N   . ALA A 1 584  ? 68.217 69.141  -35.031 1.00 22.46 ? 584  ALA A N   1 
ATOM   4734 C  CA  . ALA A 1 584  ? 69.057 68.824  -36.212 1.00 19.28 ? 584  ALA A CA  1 
ATOM   4735 C  C   . ALA A 1 584  ? 68.821 69.926  -37.223 1.00 16.05 ? 584  ALA A C   1 
ATOM   4736 O  O   . ALA A 1 584  ? 69.219 69.813  -38.402 1.00 17.00 ? 584  ALA A O   1 
ATOM   4737 C  CB  . ALA A 1 584  ? 68.690 67.516  -36.844 1.00 17.20 ? 584  ALA A CB  1 
ATOM   4738 N  N   . ASN A 1 585  ? 68.155 71.007  -36.819 1.00 16.73 ? 585  ASN A N   1 
ATOM   4739 C  CA  . ASN A 1 585  ? 67.914 72.149  -37.688 1.00 16.58 ? 585  ASN A CA  1 
ATOM   4740 C  C   . ASN A 1 585  ? 66.929 71.896  -38.823 1.00 17.99 ? 585  ASN A C   1 
ATOM   4741 O  O   . ASN A 1 585  ? 66.911 72.630  -39.813 1.00 20.36 ? 585  ASN A O   1 
ATOM   4742 C  CB  . ASN A 1 585  ? 69.257 72.668  -38.266 1.00 23.23 ? 585  ASN A CB  1 
ATOM   4743 C  CG  . ASN A 1 585  ? 69.542 74.101  -37.909 1.00 31.69 ? 585  ASN A CG  1 
ATOM   4744 O  OD1 . ASN A 1 585  ? 68.650 74.974  -37.909 1.00 28.56 ? 585  ASN A OD1 1 
ATOM   4745 N  ND2 . ASN A 1 585  ? 70.806 74.372  -37.597 1.00 40.27 ? 585  ASN A ND2 1 
ATOM   4746 N  N   . ASN A 1 586  ? 66.095 70.882  -38.704 1.00 13.82 ? 586  ASN A N   1 
ATOM   4747 C  CA  . ASN A 1 586  ? 65.068 70.554  -39.692 1.00 16.45 ? 586  ASN A CA  1 
ATOM   4748 C  C   . ASN A 1 586  ? 63.897 71.508  -39.402 1.00 17.66 ? 586  ASN A C   1 
ATOM   4749 O  O   . ASN A 1 586  ? 63.469 71.683  -38.234 1.00 15.03 ? 586  ASN A O   1 
ATOM   4750 C  CB  . ASN A 1 586  ? 64.506 69.158  -39.493 1.00 15.92 ? 586  ASN A CB  1 
ATOM   4751 C  CG  . ASN A 1 586  ? 65.550 68.070  -39.603 1.00 19.78 ? 586  ASN A CG  1 
ATOM   4752 O  OD1 . ASN A 1 586  ? 66.413 68.114  -40.486 1.00 20.46 ? 586  ASN A OD1 1 
ATOM   4753 N  ND2 . ASN A 1 586  ? 65.489 67.089  -38.682 1.00 20.11 ? 586  ASN A ND2 1 
ATOM   4754 N  N   . PRO A 1 587  ? 63.392 72.214  -40.414 1.00 16.79 ? 587  PRO A N   1 
ATOM   4755 C  CA  . PRO A 1 587  ? 62.258 73.127  -40.185 1.00 15.73 ? 587  PRO A CA  1 
ATOM   4756 C  C   . PRO A 1 587  ? 61.040 72.341  -39.727 1.00 14.15 ? 587  PRO A C   1 
ATOM   4757 O  O   . PRO A 1 587  ? 60.849 71.164  -40.070 1.00 16.89 ? 587  PRO A O   1 
ATOM   4758 C  CB  . PRO A 1 587  ? 62.041 73.820  -41.536 1.00 18.83 ? 587  PRO A CB  1 
ATOM   4759 C  CG  . PRO A 1 587  ? 63.017 73.236  -42.494 1.00 23.25 ? 587  PRO A CG  1 
ATOM   4760 C  CD  . PRO A 1 587  ? 63.943 72.272  -41.788 1.00 18.98 ? 587  PRO A CD  1 
ATOM   4761 N  N   . VAL A 1 588  ? 60.199 72.992  -38.902 1.00 13.05 ? 588  VAL A N   1 
ATOM   4762 C  CA  . VAL A 1 588  ? 58.988 72.397  -38.389 1.00 12.88 ? 588  VAL A CA  1 
ATOM   4763 C  C   . VAL A 1 588  ? 57.876 73.396  -38.774 1.00 12.19 ? 588  VAL A C   1 
ATOM   4764 O  O   . VAL A 1 588  ? 58.020 74.608  -38.497 1.00 12.48 ? 588  VAL A O   1 
ATOM   4765 C  CB  . VAL A 1 588  ? 59.061 72.256  -36.806 1.00 13.81 ? 588  VAL A CB  1 
ATOM   4766 C  CG1 . VAL A 1 588  ? 57.723 71.866  -36.236 1.00 14.94 ? 588  VAL A CG1 1 
ATOM   4767 C  CG2 . VAL A 1 588  ? 60.213 71.265  -36.421 1.00 14.19 ? 588  VAL A CG2 1 
ATOM   4768 N  N   . GLU A 1 589  ? 56.818 72.914  -39.378 1.00 13.03 ? 589  GLU A N   1 
ATOM   4769 C  CA  . GLU A 1 589  ? 55.723 73.793  -39.777 1.00 12.88 ? 589  GLU A CA  1 
ATOM   4770 C  C   . GLU A 1 589  ? 55.072 74.455  -38.541 1.00 13.04 ? 589  GLU A C   1 
ATOM   4771 O  O   . GLU A 1 589  ? 54.816 73.769  -37.527 1.00 15.15 ? 589  GLU A O   1 
ATOM   4772 C  CB  . GLU A 1 589  ? 54.664 73.001  -40.534 1.00 18.22 ? 589  GLU A CB  1 
ATOM   4773 C  CG  . GLU A 1 589  ? 53.574 73.909  -41.100 1.00 26.82 ? 589  GLU A CG  1 
ATOM   4774 C  CD  . GLU A 1 589  ? 52.460 73.171  -41.825 1.00 33.66 ? 589  GLU A CD  1 
ATOM   4775 O  OE1 . GLU A 1 589  ? 52.661 71.979  -42.138 1.00 38.90 ? 589  GLU A OE1 1 
ATOM   4776 O  OE2 . GLU A 1 589  ? 51.375 73.779  -42.089 1.00 33.49 ? 589  GLU A OE2 1 
ATOM   4777 N  N   . ALA A 1 590  ? 54.777 75.733  -38.589 1.00 12.35 ? 590  ALA A N   1 
ATOM   4778 C  CA  . ALA A 1 590  ? 54.241 76.436  -37.449 1.00 11.83 ? 590  ALA A CA  1 
ATOM   4779 C  C   . ALA A 1 590  ? 53.134 77.368  -37.902 1.00 12.64 ? 590  ALA A C   1 
ATOM   4780 O  O   . ALA A 1 590  ? 53.042 77.707  -39.123 1.00 13.23 ? 590  ALA A O   1 
ATOM   4781 C  CB  . ALA A 1 590  ? 55.318 77.242  -36.775 1.00 12.78 ? 590  ALA A CB  1 
ATOM   4782 N  N   . GLN A 1 591  ? 52.311 77.790  -36.974 1.00 12.15 ? 591  GLN A N   1 
ATOM   4783 C  CA  . GLN A 1 591  ? 51.214 78.726  -37.229 1.00 10.98 ? 591  GLN A CA  1 
ATOM   4784 C  C   . GLN A 1 591  ? 51.300 79.806  -36.170 1.00 12.24 ? 591  GLN A C   1 
ATOM   4785 O  O   . GLN A 1 591  ? 51.531 79.514  -34.977 1.00 13.18 ? 591  GLN A O   1 
ATOM   4786 C  CB  . GLN A 1 591  ? 49.848 78.012  -37.154 1.00 12.07 ? 591  GLN A CB  1 
ATOM   4787 C  CG  . GLN A 1 591  ? 48.669 78.997  -37.132 1.00 12.28 ? 591  GLN A CG  1 
ATOM   4788 C  CD  . GLN A 1 591  ? 47.325 78.290  -36.963 1.00 10.93 ? 591  GLN A CD  1 
ATOM   4789 O  OE1 . GLN A 1 591  ? 47.094 77.202  -37.539 1.00 12.64 ? 591  GLN A OE1 1 
ATOM   4790 N  NE2 . GLN A 1 591  ? 46.445 78.874  -36.165 1.00 12.46 ? 591  GLN A NE2 1 
ATOM   4791 N  N   . VAL A 1 592  ? 51.163 81.086  -36.574 1.00 11.43 ? 592  VAL A N   1 
ATOM   4792 C  CA  . VAL A 1 592  ? 51.106 82.178  -35.612 1.00 11.01 ? 592  VAL A CA  1 
ATOM   4793 C  C   . VAL A 1 592  ? 49.688 82.715  -35.614 1.00 11.46 ? 592  VAL A C   1 
ATOM   4794 O  O   . VAL A 1 592  ? 49.052 82.808  -36.679 1.00 13.10 ? 592  VAL A O   1 
ATOM   4795 C  CB  . VAL A 1 592  ? 52.158 83.285  -35.959 1.00 11.71 ? 592  VAL A CB  1 
ATOM   4796 C  CG1 . VAL A 1 592  ? 51.916 84.565  -35.180 1.00 14.07 ? 592  VAL A CG1 1 
ATOM   4797 C  CG2 . VAL A 1 592  ? 53.599 82.736  -35.619 1.00 12.89 ? 592  VAL A CG2 1 
ATOM   4798 N  N   . SER A 1 593  ? 49.180 82.983  -34.429 1.00 12.23 ? 593  SER A N   1 
ATOM   4799 C  CA  . SER A 1 593  ? 47.818 83.529  -34.209 1.00 13.32 ? 593  SER A CA  1 
ATOM   4800 C  C   . SER A 1 593  ? 47.957 84.645  -33.211 1.00 13.38 ? 593  SER A C   1 
ATOM   4801 O  O   . SER A 1 593  ? 48.957 84.756  -32.474 1.00 14.79 ? 593  SER A O   1 
ATOM   4802 C  CB  . SER A 1 593  ? 46.825 82.481  -33.595 1.00 13.87 ? 593  SER A CB  1 
ATOM   4803 O  OG  . SER A 1 593  ? 46.640 81.317  -34.400 1.00 14.73 ? 593  SER A OG  1 
ATOM   4804 N  N   . PRO A 1 594  ? 46.995 85.543  -33.148 1.00 11.72 ? 594  PRO A N   1 
ATOM   4805 C  CA  . PRO A 1 594  ? 47.096 86.626  -32.156 1.00 12.58 ? 594  PRO A CA  1 
ATOM   4806 C  C   . PRO A 1 594  ? 46.853 86.140  -30.720 1.00 12.07 ? 594  PRO A C   1 
ATOM   4807 O  O   . PRO A 1 594  ? 46.384 84.968  -30.516 1.00 13.04 ? 594  PRO A O   1 
ATOM   4808 C  CB  . PRO A 1 594  ? 45.964 87.606  -32.556 1.00 13.67 ? 594  PRO A CB  1 
ATOM   4809 C  CG  . PRO A 1 594  ? 45.566 87.138  -33.993 1.00 13.46 ? 594  PRO A CG  1 
ATOM   4810 C  CD  . PRO A 1 594  ? 45.780 85.668  -33.985 1.00 13.00 ? 594  PRO A CD  1 
ATOM   4811 N  N   . VAL A 1 595  ? 47.164 86.981  -29.725 1.00 12.32 ? 595  VAL A N   1 
ATOM   4812 C  CA  . VAL A 1 595  ? 46.797 86.649  -28.356 1.00 12.67 ? 595  VAL A CA  1 
ATOM   4813 C  C   . VAL A 1 595  ? 45.530 87.452  -28.098 1.00 12.70 ? 595  VAL A C   1 
ATOM   4814 O  O   . VAL A 1 595  ? 45.543 88.701  -28.144 1.00 14.66 ? 595  VAL A O   1 
ATOM   4815 C  CB  . VAL A 1 595  ? 47.875 87.035  -27.320 1.00 14.44 ? 595  VAL A CB  1 
ATOM   4816 C  CG1 . VAL A 1 595  ? 47.307 86.782  -25.894 1.00 13.71 ? 595  VAL A CG1 1 
ATOM   4817 C  CG2 . VAL A 1 595  ? 49.159 86.211  -27.588 1.00 14.82 ? 595  VAL A CG2 1 
ATOM   4818 N  N   . TRP A 1 596  ? 44.411 86.755  -27.877 1.00 12.29 ? 596  TRP A N   1 
ATOM   4819 C  CA  . TRP A 1 596  ? 43.106 87.370  -27.676 1.00 13.67 ? 596  TRP A CA  1 
ATOM   4820 C  C   . TRP A 1 596  ? 42.694 87.286  -26.234 1.00 16.02 ? 596  TRP A C   1 
ATOM   4821 O  O   . TRP A 1 596  ? 42.824 86.207  -25.624 1.00 17.67 ? 596  TRP A O   1 
ATOM   4822 C  CB  . TRP A 1 596  ? 42.040 86.607  -28.539 1.00 13.21 ? 596  TRP A CB  1 
ATOM   4823 C  CG  . TRP A 1 596  ? 42.192 86.791  -30.008 1.00 11.90 ? 596  TRP A CG  1 
ATOM   4824 C  CD1 . TRP A 1 596  ? 42.578 85.854  -30.948 1.00 11.49 ? 596  TRP A CD1 1 
ATOM   4825 C  CD2 . TRP A 1 596  ? 41.880 87.974  -30.755 1.00 12.16 ? 596  TRP A CD2 1 
ATOM   4826 N  NE1 . TRP A 1 596  ? 42.523 86.398  -32.222 1.00 13.63 ? 596  TRP A NE1 1 
ATOM   4827 C  CE2 . TRP A 1 596  ? 42.095 87.698  -32.115 1.00 13.41 ? 596  TRP A CE2 1 
ATOM   4828 C  CE3 . TRP A 1 596  ? 41.431 89.252  -30.394 1.00 12.14 ? 596  TRP A CE3 1 
ATOM   4829 C  CZ2 . TRP A 1 596  ? 41.880 88.651  -33.105 1.00 14.50 ? 596  TRP A CZ2 1 
ATOM   4830 C  CZ3 . TRP A 1 596  ? 41.223 90.203  -31.392 1.00 14.88 ? 596  TRP A CZ3 1 
ATOM   4831 C  CH2 . TRP A 1 596  ? 41.446 89.890  -32.710 1.00 15.96 ? 596  TRP A CH2 1 
ATOM   4832 N  N   . SER A 1 597  ? 42.254 88.387  -25.657 1.00 15.41 ? 597  SER A N   1 
ATOM   4833 C  CA  . SER A 1 597  ? 41.737 88.343  -24.302 1.00 17.55 ? 597  SER A CA  1 
ATOM   4834 C  C   . SER A 1 597  ? 40.333 88.943  -24.322 1.00 17.34 ? 597  SER A C   1 
ATOM   4835 O  O   . SER A 1 597  ? 40.084 89.951  -25.020 1.00 21.15 ? 597  SER A O   1 
ATOM   4836 C  CB  . SER A 1 597  ? 42.607 89.121  -23.349 1.00 22.17 ? 597  SER A CB  1 
ATOM   4837 O  OG  . SER A 1 597  ? 42.768 90.358  -23.898 1.00 28.35 ? 597  SER A OG  1 
ATOM   4838 N  N   . TRP A 1 598  ? 39.440 88.370  -23.551 1.00 14.51 ? 598  TRP A N   1 
ATOM   4839 C  CA  . TRP A 1 598  ? 38.051 88.827  -23.499 1.00 14.55 ? 598  TRP A CA  1 
ATOM   4840 C  C   . TRP A 1 598  ? 37.803 89.780  -22.327 1.00 15.64 ? 598  TRP A C   1 
ATOM   4841 O  O   . TRP A 1 598  ? 38.230 89.558  -21.199 1.00 19.64 ? 598  TRP A O   1 
ATOM   4842 C  CB  . TRP A 1 598  ? 37.121 87.613  -23.403 1.00 15.21 ? 598  TRP A CB  1 
ATOM   4843 C  CG  . TRP A 1 598  ? 37.084 86.833  -24.714 1.00 12.80 ? 598  TRP A CG  1 
ATOM   4844 C  CD1 . TRP A 1 598  ? 38.013 85.942  -25.169 1.00 13.19 ? 598  TRP A CD1 1 
ATOM   4845 C  CD2 . TRP A 1 598  ? 36.079 86.915  -25.707 1.00 12.72 ? 598  TRP A CD2 1 
ATOM   4846 N  NE1 . TRP A 1 598  ? 37.618 85.448  -26.410 1.00 12.66 ? 598  TRP A NE1 1 
ATOM   4847 C  CE2 . TRP A 1 598  ? 36.440 86.037  -26.754 1.00 12.18 ? 598  TRP A CE2 1 
ATOM   4848 C  CE3 . TRP A 1 598  ? 34.872 87.650  -25.828 1.00 13.51 ? 598  TRP A CE3 1 
ATOM   4849 C  CZ2 . TRP A 1 598  ? 35.665 85.868  -27.887 1.00 13.55 ? 598  TRP A CZ2 1 
ATOM   4850 C  CZ3 . TRP A 1 598  ? 34.093 87.458  -26.980 1.00 12.37 ? 598  TRP A CZ3 1 
ATOM   4851 C  CH2 . TRP A 1 598  ? 34.504 86.579  -27.977 1.00 13.37 ? 598  TRP A CH2 1 
ATOM   4852 N  N   A HIS A 1 599  ? 37.042 90.806  -22.621 0.50 18.15 ? 599  HIS A N   1 
ATOM   4853 N  N   B HIS A 1 599  ? 37.042 90.806  -22.621 0.50 20.72 ? 599  HIS A N   1 
ATOM   4854 C  CA  A HIS A 1 599  ? 36.786 91.831  -21.645 0.50 20.63 ? 599  HIS A CA  1 
ATOM   4855 C  CA  B HIS A 1 599  ? 36.786 91.831  -21.645 0.50 25.07 ? 599  HIS A CA  1 
ATOM   4856 C  C   A HIS A 1 599  ? 35.327 92.096  -21.483 0.50 19.76 ? 599  HIS A C   1 
ATOM   4857 C  C   B HIS A 1 599  ? 35.383 92.332  -21.717 0.50 25.42 ? 599  HIS A C   1 
ATOM   4858 O  O   A HIS A 1 599  ? 34.589 92.164  -22.465 0.50 16.24 ? 599  HIS A O   1 
ATOM   4859 O  O   B HIS A 1 599  ? 34.751 92.281  -22.771 0.50 26.45 ? 599  HIS A O   1 
ATOM   4860 C  CB  A HIS A 1 599  ? 37.498 93.100  -22.093 0.50 24.76 ? 599  HIS A CB  1 
ATOM   4861 C  CB  B HIS A 1 599  ? 37.760 92.975  -21.893 0.50 31.78 ? 599  HIS A CB  1 
ATOM   4862 C  CG  A HIS A 1 599  ? 38.985 92.941  -22.053 0.50 30.79 ? 599  HIS A CG  1 
ATOM   4863 C  CG  B HIS A 1 599  ? 37.093 94.307  -21.754 0.50 35.48 ? 599  HIS A CG  1 
ATOM   4864 N  ND1 A HIS A 1 599  ? 39.663 92.674  -20.875 0.50 33.02 ? 599  HIS A ND1 1 
ATOM   4865 N  ND1 B HIS A 1 599  ? 37.147 95.036  -20.578 0.50 38.85 ? 599  HIS A ND1 1 
ATOM   4866 C  CD2 A HIS A 1 599  ? 39.895 92.811  -23.046 0.50 33.18 ? 599  HIS A CD2 1 
ATOM   4867 C  CD2 B HIS A 1 599  ? 36.537 95.126  -22.677 0.50 38.73 ? 599  HIS A CD2 1 
ATOM   4868 C  CE1 A HIS A 1 599  ? 40.921 92.380  -21.152 0.50 34.40 ? 599  HIS A CE1 1 
ATOM   4869 C  CE1 B HIS A 1 599  ? 36.660 96.245  -20.791 0.50 38.29 ? 599  HIS A CE1 1 
ATOM   4870 N  NE2 A HIS A 1 599  ? 41.087 92.455  -22.461 0.50 32.71 ? 599  HIS A NE2 1 
ATOM   4871 N  NE2 B HIS A 1 599  ? 36.285 96.326  -22.055 0.50 39.35 ? 599  HIS A NE2 1 
ATOM   4872 N  N   . HIS A 1 600  ? 34.920 92.229  -20.237 1.00 24.44 ? 600  HIS A N   1 
ATOM   4873 C  CA  . HIS A 1 600  ? 33.538 92.547  -19.920 1.00 22.75 ? 600  HIS A CA  1 
ATOM   4874 C  C   . HIS A 1 600  ? 33.650 94.039  -19.866 1.00 23.09 ? 600  HIS A C   1 
ATOM   4875 O  O   . HIS A 1 600  ? 34.207 94.612  -18.915 1.00 28.24 ? 600  HIS A O   1 
ATOM   4876 C  CB  . HIS A 1 600  ? 33.195 91.875  -18.594 1.00 27.27 ? 600  HIS A CB  1 
ATOM   4877 C  CG  . HIS A 1 600  ? 33.506 90.413  -18.638 1.00 35.65 ? 600  HIS A CG  1 
ATOM   4878 N  ND1 . HIS A 1 600  ? 34.754 89.952  -19.008 1.00 38.61 ? 600  HIS A ND1 1 
ATOM   4879 C  CD2 . HIS A 1 600  ? 32.704 89.318  -18.585 1.00 39.25 ? 600  HIS A CD2 1 
ATOM   4880 C  CE1 . HIS A 1 600  ? 34.709 88.643  -19.193 1.00 41.59 ? 600  HIS A CE1 1 
ATOM   4881 N  NE2 . HIS A 1 600  ? 33.475 88.232  -18.944 1.00 42.48 ? 600  HIS A NE2 1 
ATOM   4882 N  N   . ASP A 1 601  ? 33.178 94.663  -20.933 1.00 22.82 ? 601  ASP A N   1 
ATOM   4883 C  CA  . ASP A 1 601  ? 33.288 96.085  -21.112 1.00 23.49 ? 601  ASP A CA  1 
ATOM   4884 C  C   . ASP A 1 601  ? 32.148 96.749  -20.322 1.00 25.95 ? 601  ASP A C   1 
ATOM   4885 O  O   . ASP A 1 601  ? 30.993 96.676  -20.737 1.00 23.86 ? 601  ASP A O   1 
ATOM   4886 C  CB  . ASP A 1 601  ? 33.192 96.359  -22.611 1.00 24.42 ? 601  ASP A CB  1 
ATOM   4887 C  CG  . ASP A 1 601  ? 33.553 97.774  -22.993 1.00 30.28 ? 601  ASP A CG  1 
ATOM   4888 O  OD1 . ASP A 1 601  ? 33.311 98.713  -22.191 1.00 28.30 ? 601  ASP A OD1 1 
ATOM   4889 O  OD2 . ASP A 1 601  ? 34.045 97.953  -24.130 1.00 27.92 ? 601  ASP A OD2 1 
ATOM   4890 N  N   . THR A 1 602  ? 32.472 97.357  -19.176 1.00 25.98 ? 602  THR A N   1 
ATOM   4891 C  CA  . THR A 1 602  ? 31.427 97.986  -18.372 1.00 29.26 ? 602  THR A CA  1 
ATOM   4892 C  C   . THR A 1 602  ? 30.886 99.273  -18.960 1.00 28.73 ? 602  THR A C   1 
ATOM   4893 O  O   . THR A 1 602  ? 29.882 99.776  -18.455 1.00 30.16 ? 602  THR A O   1 
ATOM   4894 C  CB  . THR A 1 602  ? 31.868 98.247  -16.921 1.00 30.57 ? 602  THR A CB  1 
ATOM   4895 O  OG1 . THR A 1 602  ? 33.008 99.116  -16.912 1.00 35.17 ? 602  THR A OG1 1 
ATOM   4896 C  CG2 . THR A 1 602  ? 32.194 96.934  -16.218 1.00 33.80 ? 602  THR A CG2 1 
ATOM   4897 N  N   . LEU A 1 603  ? 31.513 99.796  -20.015 1.00 26.13 ? 603  LEU A N   1 
ATOM   4898 C  CA  . LEU A 1 603  ? 31.026 100.993 -20.703 1.00 27.78 ? 603  LEU A CA  1 
ATOM   4899 C  C   . LEU A 1 603  ? 30.003 100.635 -21.797 1.00 26.39 ? 603  LEU A C   1 
ATOM   4900 O  O   . LEU A 1 603  ? 28.879 101.124 -21.773 1.00 23.72 ? 603  LEU A O   1 
ATOM   4901 C  CB  . LEU A 1 603  ? 32.179 101.796 -21.328 1.00 32.71 ? 603  LEU A CB  1 
ATOM   4902 C  CG  . LEU A 1 603  ? 33.002 102.743 -20.439 1.00 37.82 ? 603  LEU A CG  1 
ATOM   4903 C  CD1 . LEU A 1 603  ? 32.045 103.730 -19.720 1.00 39.31 ? 603  LEU A CD1 1 
ATOM   4904 C  CD2 . LEU A 1 603  ? 33.798 101.954 -19.421 1.00 40.40 ? 603  LEU A CD2 1 
ATOM   4905 N  N   . THR A 1 604  ? 30.375 99.766  -22.753 1.00 21.91 ? 604  THR A N   1 
ATOM   4906 C  CA  . THR A 1 604  ? 29.476 99.342  -23.814 1.00 21.10 ? 604  THR A CA  1 
ATOM   4907 C  C   . THR A 1 604  ? 28.510 98.239  -23.366 1.00 17.51 ? 604  THR A C   1 
ATOM   4908 O  O   . THR A 1 604  ? 27.587 97.908  -24.113 1.00 19.05 ? 604  THR A O   1 
ATOM   4909 C  CB  . THR A 1 604  ? 30.247 98.806  -25.052 1.00 23.03 ? 604  THR A CB  1 
ATOM   4910 O  OG1 . THR A 1 604  ? 31.053 97.666  -24.662 1.00 23.51 ? 604  THR A OG1 1 
ATOM   4911 C  CG2 . THR A 1 604  ? 31.165 99.917  -25.631 1.00 23.32 ? 604  THR A CG2 1 
ATOM   4912 N  N   . LYS A 1 605  ? 28.797 97.625  -22.219 1.00 17.60 ? 605  LYS A N   1 
ATOM   4913 C  CA  . LYS A 1 605  ? 27.953 96.528  -21.688 1.00 18.64 ? 605  LYS A CA  1 
ATOM   4914 C  C   . LYS A 1 605  ? 27.965 95.337  -22.666 1.00 21.35 ? 605  LYS A C   1 
ATOM   4915 O  O   . LYS A 1 605  ? 26.932 94.759  -22.993 1.00 21.85 ? 605  LYS A O   1 
ATOM   4916 C  CB  . LYS A 1 605  ? 26.479 96.970  -21.444 1.00 20.62 ? 605  LYS A CB  1 
ATOM   4917 C  CG  . LYS A 1 605  ? 26.370 98.155  -20.517 1.00 20.78 ? 605  LYS A CG  1 
ATOM   4918 C  CD  . LYS A 1 605  ? 26.797 97.758  -19.108 1.00 20.32 ? 605  LYS A CD  1 
ATOM   4919 C  CE  . LYS A 1 605  ? 26.719 98.979  -18.140 1.00 21.02 ? 605  LYS A CE  1 
ATOM   4920 N  NZ  . LYS A 1 605  ? 26.962 98.528  -16.748 1.00 26.70 ? 605  LYS A NZ  1 
ATOM   4921 N  N   . THR A 1 606  ? 29.146 95.012  -23.179 1.00 18.47 ? 606  THR A N   1 
ATOM   4922 C  CA  . THR A 1 606  ? 29.294 93.856  -24.081 1.00 18.59 ? 606  THR A CA  1 
ATOM   4923 C  C   . THR A 1 606  ? 30.540 93.120  -23.647 1.00 15.93 ? 606  THR A C   1 
ATOM   4924 O  O   . THR A 1 606  ? 31.386 93.650  -22.960 1.00 17.23 ? 606  THR A O   1 
ATOM   4925 C  CB  . THR A 1 606  ? 29.486 94.256  -25.562 1.00 20.45 ? 606  THR A CB  1 
ATOM   4926 O  OG1 . THR A 1 606  ? 30.645 95.091  -25.685 1.00 23.65 ? 606  THR A OG1 1 
ATOM   4927 C  CG2 . THR A 1 606  ? 28.236 94.946  -26.116 1.00 20.77 ? 606  THR A CG2 1 
ATOM   4928 N  N   . ILE A 1 607  ? 30.634 91.847  -24.030 1.00 15.91 ? 607  ILE A N   1 
ATOM   4929 C  CA  . ILE A 1 607  ? 31.807 91.019  -23.685 1.00 13.99 ? 607  ILE A CA  1 
ATOM   4930 C  C   . ILE A 1 607  ? 32.483 90.799  -25.037 1.00 13.60 ? 607  ILE A C   1 
ATOM   4931 O  O   . ILE A 1 607  ? 31.918 90.180  -25.967 1.00 13.60 ? 607  ILE A O   1 
ATOM   4932 C  CB  . ILE A 1 607  ? 31.316 89.696  -23.094 1.00 14.56 ? 607  ILE A CB  1 
ATOM   4933 C  CG1 . ILE A 1 607  ? 30.501 89.983  -21.824 1.00 17.06 ? 607  ILE A CG1 1 
ATOM   4934 C  CG2 . ILE A 1 607  ? 32.544 88.813  -22.756 1.00 15.77 ? 607  ILE A CG2 1 
ATOM   4935 C  CD1 . ILE A 1 607  ? 29.632 88.829  -21.361 1.00 21.05 ? 607  ILE A CD1 1 
ATOM   4936 N  N   . HIS A 1 608  ? 33.710 91.305  -25.200 1.00 14.53 ? 608  HIS A N   1 
ATOM   4937 C  CA  . HIS A 1 608  ? 34.321 91.247  -26.542 1.00 16.06 ? 608  HIS A CA  1 
ATOM   4938 C  C   . HIS A 1 608  ? 35.821 91.076  -26.427 1.00 14.89 ? 608  HIS A C   1 
ATOM   4939 O  O   . HIS A 1 608  ? 36.391 91.398  -25.379 1.00 16.75 ? 608  HIS A O   1 
ATOM   4940 C  CB  . HIS A 1 608  ? 33.968 92.505  -27.358 1.00 19.36 ? 608  HIS A CB  1 
ATOM   4941 C  CG  . HIS A 1 608  ? 34.527 93.777  -26.802 1.00 22.29 ? 608  HIS A CG  1 
ATOM   4942 N  ND1 . HIS A 1 608  ? 33.921 94.516  -25.800 1.00 25.59 ? 608  HIS A ND1 1 
ATOM   4943 C  CD2 . HIS A 1 608  ? 35.671 94.440  -27.110 1.00 25.09 ? 608  HIS A CD2 1 
ATOM   4944 C  CE1 . HIS A 1 608  ? 34.662 95.580  -25.523 1.00 25.33 ? 608  HIS A CE1 1 
ATOM   4945 N  NE2 . HIS A 1 608  ? 35.727 95.557  -26.301 1.00 30.13 ? 608  HIS A NE2 1 
ATOM   4946 N  N   . PRO A 1 609  ? 36.465 90.597  -27.474 1.00 14.37 ? 609  PRO A N   1 
ATOM   4947 C  CA  . PRO A 1 609  ? 37.898 90.371  -27.410 1.00 14.68 ? 609  PRO A CA  1 
ATOM   4948 C  C   . PRO A 1 609  ? 38.784 91.499  -27.861 1.00 15.32 ? 609  PRO A C   1 
ATOM   4949 O  O   . PRO A 1 609  ? 38.444 92.241  -28.805 1.00 20.00 ? 609  PRO A O   1 
ATOM   4950 C  CB  . PRO A 1 609  ? 38.083 89.160  -28.314 1.00 16.55 ? 609  PRO A CB  1 
ATOM   4951 C  CG  . PRO A 1 609  ? 37.061 89.401  -29.417 1.00 16.18 ? 609  PRO A CG  1 
ATOM   4952 C  CD  . PRO A 1 609  ? 35.902 90.086  -28.750 1.00 12.66 ? 609  PRO A CD  1 
ATOM   4953 N  N   . GLN A 1 610  ? 39.936 91.550  -27.210 1.00 14.62 ? 610  GLN A N   1 
ATOM   4954 C  CA  . GLN A 1 610  ? 40.952 92.528  -27.532 1.00 17.24 ? 610  GLN A CA  1 
ATOM   4955 C  C   . GLN A 1 610  ? 42.192 91.748  -27.947 1.00 13.91 ? 610  GLN A C   1 
ATOM   4956 O  O   . GLN A 1 610  ? 42.503 90.753  -27.273 1.00 14.76 ? 610  GLN A O   1 
ATOM   4957 C  CB  . GLN A 1 610  ? 41.276 93.382  -26.303 1.00 20.68 ? 610  GLN A CB  1 
ATOM   4958 C  CG  . GLN A 1 610  ? 40.072 94.143  -25.814 1.00 33.15 ? 610  GLN A CG  1 
ATOM   4959 C  CD  . GLN A 1 610  ? 39.805 95.396  -26.625 1.00 39.51 ? 610  GLN A CD  1 
ATOM   4960 O  OE1 . GLN A 1 610  ? 39.238 95.358  -27.739 1.00 42.59 ? 610  GLN A OE1 1 
ATOM   4961 N  NE2 . GLN A 1 610  ? 40.221 96.533  -26.067 1.00 43.58 ? 610  GLN A NE2 1 
ATOM   4962 N  N   . GLY A 1 611  ? 42.869 92.192  -28.992 1.00 14.68 ? 611  GLY A N   1 
ATOM   4963 C  CA  . GLY A 1 611  ? 44.090 91.501  -29.409 1.00 14.79 ? 611  GLY A CA  1 
ATOM   4964 C  C   . GLY A 1 611  ? 45.332 92.266  -28.975 1.00 16.36 ? 611  GLY A C   1 
ATOM   4965 O  O   . GLY A 1 611  ? 45.354 93.496  -28.888 1.00 18.21 ? 611  GLY A O   1 
ATOM   4966 N  N   . SER A 1 612  ? 46.382 91.531  -28.693 1.00 16.80 ? 612  SER A N   1 
ATOM   4967 C  CA  . SER A 1 612  ? 47.653 92.161  -28.318 1.00 17.52 ? 612  SER A CA  1 
ATOM   4968 C  C   . SER A 1 612  ? 48.345 92.667  -29.546 1.00 14.22 ? 612  SER A C   1 
ATOM   4969 O  O   . SER A 1 612  ? 48.273 92.093  -30.613 1.00 18.22 ? 612  SER A O   1 
ATOM   4970 C  CB  . SER A 1 612  ? 48.529 91.092  -27.672 1.00 17.31 ? 612  SER A CB  1 
ATOM   4971 O  OG  . SER A 1 612  ? 49.806 91.652  -27.352 1.00 19.28 ? 612  SER A OG  1 
ATOM   4972 N  N   . THR A 1 613  ? 49.050 93.807  -29.396 1.00 23.18 ? 613  THR A N   1 
ATOM   4973 C  CA  . THR A 1 613  ? 49.786 94.316  -30.540 1.00 23.09 ? 613  THR A CA  1 
ATOM   4974 C  C   . THR A 1 613  ? 51.302 94.091  -30.367 1.00 26.60 ? 613  THR A C   1 
ATOM   4975 O  O   . THR A 1 613  ? 52.107 94.571  -31.192 1.00 28.66 ? 613  THR A O   1 
ATOM   4976 C  CB  . THR A 1 613  ? 49.556 95.818  -30.759 1.00 26.11 ? 613  THR A CB  1 
ATOM   4977 O  OG1 . THR A 1 613  ? 50.044 96.513  -29.607 1.00 22.91 ? 613  THR A OG1 1 
ATOM   4978 C  CG2 . THR A 1 613  ? 48.060 96.112  -30.880 1.00 25.65 ? 613  THR A CG2 1 
ATOM   4979 N  N   . THR A 1 614  ? 51.673 93.321  -29.343 1.00 25.67 ? 614  THR A N   1 
ATOM   4980 C  CA  . THR A 1 614  ? 53.098 93.028  -29.106 1.00 25.59 ? 614  THR A CA  1 
ATOM   4981 C  C   . THR A 1 614  ? 53.428 91.601  -28.618 1.00 26.33 ? 614  THR A C   1 
ATOM   4982 O  O   . THR A 1 614  ? 54.584 91.317  -28.324 1.00 27.15 ? 614  THR A O   1 
ATOM   4983 C  CB  . THR A 1 614  ? 53.622 93.899  -28.068 1.00 25.72 ? 614  THR A CB  1 
ATOM   4984 O  OG1 . THR A 1 614  ? 52.830 93.676  -26.918 1.00 26.30 ? 614  THR A OG1 1 
ATOM   4985 C  CG2 . THR A 1 614  ? 53.631 95.376  -28.517 1.00 28.20 ? 614  THR A CG2 1 
ATOM   4986 N  N   . LYS A 1 615  ? 52.430 90.734  -28.456 1.00 19.45 ? 615  LYS A N   1 
ATOM   4987 C  CA  . LYS A 1 615  ? 52.662 89.345  -28.039 1.00 18.93 ? 615  LYS A CA  1 
ATOM   4988 C  C   . LYS A 1 615  ? 51.847 88.584  -29.071 1.00 17.91 ? 615  LYS A C   1 
ATOM   4989 O  O   . LYS A 1 615  ? 50.739 89.023  -29.408 1.00 17.89 ? 615  LYS A O   1 
ATOM   4990 C  CB  . LYS A 1 615  ? 51.982 88.927  -26.701 1.00 24.82 ? 615  LYS A CB  1 
ATOM   4991 C  CG  . LYS A 1 615  ? 52.444 89.462  -25.377 1.00 30.72 ? 615  LYS A CG  1 
ATOM   4992 C  CD  . LYS A 1 615  ? 52.222 88.425  -24.222 1.00 26.55 ? 615  LYS A CD  1 
ATOM   4993 C  CE  . LYS A 1 615  ? 50.762 88.095  -23.836 1.00 25.05 ? 615  LYS A CE  1 
ATOM   4994 N  NZ  . LYS A 1 615  ? 50.712 88.113  -22.288 1.00 25.30 ? 615  LYS A NZ  1 
ATOM   4995 N  N   . TYR A 1 616  ? 52.347 87.416  -29.502 1.00 14.23 ? 616  TYR A N   1 
ATOM   4996 C  CA  . TYR A 1 616  ? 51.678 86.547  -30.450 1.00 13.86 ? 616  TYR A CA  1 
ATOM   4997 C  C   . TYR A 1 616  ? 51.822 85.120  -29.998 1.00 11.51 ? 616  TYR A C   1 
ATOM   4998 O  O   . TYR A 1 616  ? 52.731 84.820  -29.180 1.00 14.00 ? 616  TYR A O   1 
ATOM   4999 C  CB  . TYR A 1 616  ? 52.331 86.683  -31.839 1.00 13.08 ? 616  TYR A CB  1 
ATOM   5000 C  CG  . TYR A 1 616  ? 52.316 88.126  -32.247 1.00 18.34 ? 616  TYR A CG  1 
ATOM   5001 C  CD1 . TYR A 1 616  ? 53.364 88.981  -31.908 1.00 17.22 ? 616  TYR A CD1 1 
ATOM   5002 C  CD2 . TYR A 1 616  ? 51.153 88.654  -32.859 1.00 19.20 ? 616  TYR A CD2 1 
ATOM   5003 C  CE1 . TYR A 1 616  ? 53.249 90.382  -32.175 1.00 23.65 ? 616  TYR A CE1 1 
ATOM   5004 C  CE2 . TYR A 1 616  ? 51.031 89.991  -33.109 1.00 23.56 ? 616  TYR A CE2 1 
ATOM   5005 C  CZ  . TYR A 1 616  ? 52.069 90.835  -32.775 1.00 23.02 ? 616  TYR A CZ  1 
ATOM   5006 O  OH  . TYR A 1 616  ? 51.907 92.164  -33.150 1.00 28.28 ? 616  TYR A OH  1 
ATOM   5007 N  N   . ARG A 1 617  ? 50.975 84.231  -30.505 1.00 12.64 ? 617  ARG A N   1 
ATOM   5008 C  CA  . ARG A 1 617  ? 51.083 82.799  -30.179 1.00 12.82 ? 617  ARG A CA  1 
ATOM   5009 C  C   . ARG A 1 617  ? 51.704 82.053  -31.347 1.00 13.46 ? 617  ARG A C   1 
ATOM   5010 O  O   . ARG A 1 617  ? 51.222 82.190  -32.500 1.00 14.95 ? 617  ARG A O   1 
ATOM   5011 C  CB  . ARG A 1 617  ? 49.714 82.167  -29.983 1.00 16.53 ? 617  ARG A CB  1 
ATOM   5012 C  CG  . ARG A 1 617  ? 49.015 82.487  -28.698 1.00 20.13 ? 617  ARG A CG  1 
ATOM   5013 C  CD  . ARG A 1 617  ? 47.594 81.846  -28.657 1.00 21.46 ? 617  ARG A CD  1 
ATOM   5014 N  NE  . ARG A 1 617  ? 47.593 80.378  -28.640 1.00 18.08 ? 617  ARG A NE  1 
ATOM   5015 C  CZ  . ARG A 1 617  ? 46.864 79.612  -29.460 1.00 19.95 ? 617  ARG A CZ  1 
ATOM   5016 N  NH1 . ARG A 1 617  ? 46.043 80.131  -30.393 1.00 18.07 ? 617  ARG A NH1 1 
ATOM   5017 N  NH2 . ARG A 1 617  ? 46.982 78.291  -29.399 1.00 18.78 ? 617  ARG A NH2 1 
ATOM   5018 N  N   . ILE A 1 618  ? 52.734 81.235  -31.102 1.00 11.37 ? 618  ILE A N   1 
ATOM   5019 C  CA  . ILE A 1 618  ? 53.255 80.384  -32.146 1.00 12.65 ? 618  ILE A CA  1 
ATOM   5020 C  C   . ILE A 1 618  ? 52.883 78.952  -31.763 1.00 10.30 ? 618  ILE A C   1 
ATOM   5021 O  O   . ILE A 1 618  ? 53.022 78.552  -30.584 1.00 12.45 ? 618  ILE A O   1 
ATOM   5022 C  CB  . ILE A 1 618  ? 54.704 80.565  -32.372 1.00 12.19 ? 618  ILE A CB  1 
ATOM   5023 C  CG1 . ILE A 1 618  ? 55.081 79.739  -33.617 1.00 16.47 ? 618  ILE A CG1 1 
ATOM   5024 C  CG2 . ILE A 1 618  ? 55.558 80.236  -31.136 1.00 14.73 ? 618  ILE A CG2 1 
ATOM   5025 C  CD1 . ILE A 1 618  ? 56.355 80.144  -34.273 1.00 15.46 ? 618  ILE A CD1 1 
ATOM   5026 N  N   . ILE A 1 619  ? 52.433 78.179  -32.720 1.00 10.78 ? 619  ILE A N   1 
ATOM   5027 C  CA  . ILE A 1 619  ? 51.911 76.831  -32.493 1.00 10.56 ? 619  ILE A CA  1 
ATOM   5028 C  C   . ILE A 1 619  ? 52.618 75.859  -33.427 1.00 11.60 ? 619  ILE A C   1 
ATOM   5029 O  O   . ILE A 1 619  ? 52.802 76.173  -34.641 1.00 11.58 ? 619  ILE A O   1 
ATOM   5030 C  CB  . ILE A 1 619  ? 50.384 76.839  -32.883 1.00 13.84 ? 619  ILE A CB  1 
ATOM   5031 C  CG1 . ILE A 1 619  ? 49.677 77.882  -32.042 1.00 14.55 ? 619  ILE A CG1 1 
ATOM   5032 C  CG2 . ILE A 1 619  ? 49.758 75.462  -32.802 1.00 16.39 ? 619  ILE A CG2 1 
ATOM   5033 C  CD1 . ILE A 1 619  ? 48.465 78.563  -32.802 1.00 17.90 ? 619  ILE A CD1 1 
ATOM   5034 N  N   . PHE A 1 620  ? 53.027 74.688  -32.966 1.00 10.19 ? 620  PHE A N   1 
ATOM   5035 C  CA  . PHE A 1 620  ? 53.656 73.728  -33.867 1.00 9.98  ? 620  PHE A CA  1 
ATOM   5036 C  C   . PHE A 1 620  ? 53.467 72.344  -33.263 1.00 10.32 ? 620  PHE A C   1 
ATOM   5037 O  O   . PHE A 1 620  ? 53.154 72.236  -32.052 1.00 10.72 ? 620  PHE A O   1 
ATOM   5038 C  CB  . PHE A 1 620  ? 55.150 74.021  -34.078 1.00 10.22 ? 620  PHE A CB  1 
ATOM   5039 C  CG  . PHE A 1 620  ? 55.993 73.936  -32.825 1.00 9.23  ? 620  PHE A CG  1 
ATOM   5040 C  CD1 . PHE A 1 620  ? 56.647 72.737  -32.497 1.00 11.86 ? 620  PHE A CD1 1 
ATOM   5041 C  CD2 . PHE A 1 620  ? 56.190 75.064  -32.028 1.00 10.72 ? 620  PHE A CD2 1 
ATOM   5042 C  CE1 . PHE A 1 620  ? 57.505 72.661  -31.369 1.00 11.54 ? 620  PHE A CE1 1 
ATOM   5043 C  CE2 . PHE A 1 620  ? 57.057 74.992  -30.893 1.00 11.58 ? 620  PHE A CE2 1 
ATOM   5044 C  CZ  . PHE A 1 620  ? 57.687 73.780  -30.598 1.00 11.94 ? 620  PHE A CZ  1 
ATOM   5045 N  N   . LYS A 1 621  ? 53.664 71.317  -34.079 1.00 9.90  ? 621  LYS A N   1 
ATOM   5046 C  CA  . LYS A 1 621  ? 53.524 69.965  -33.608 1.00 10.49 ? 621  LYS A CA  1 
ATOM   5047 C  C   . LYS A 1 621  ? 54.819 69.455  -33.024 1.00 12.05 ? 621  LYS A C   1 
ATOM   5048 O  O   . LYS A 1 621  ? 55.862 69.417  -33.694 1.00 14.17 ? 621  LYS A O   1 
ATOM   5049 C  CB  . LYS A 1 621  ? 53.055 69.110  -34.801 1.00 11.73 ? 621  LYS A CB  1 
ATOM   5050 C  CG  . LYS A 1 621  ? 52.775 67.644  -34.399 1.00 13.93 ? 621  LYS A CG  1 
ATOM   5051 C  CD  . LYS A 1 621  ? 51.982 66.942  -35.545 1.00 19.18 ? 621  LYS A CD  1 
ATOM   5052 C  CE  . LYS A 1 621  ? 52.653 66.988  -36.865 1.00 23.35 ? 621  LYS A CE  1 
ATOM   5053 N  NZ  . LYS A 1 621  ? 51.792 66.250  -37.894 1.00 26.68 ? 621  LYS A NZ  1 
ATOM   5054 N  N   . ALA A 1 622  ? 54.782 69.120  -31.729 1.00 11.20 ? 622  ALA A N   1 
ATOM   5055 C  CA  . ALA A 1 622  ? 55.975 68.502  -31.104 1.00 10.57 ? 622  ALA A CA  1 
ATOM   5056 C  C   . ALA A 1 622  ? 55.820 66.985  -31.144 1.00 10.53 ? 622  ALA A C   1 
ATOM   5057 O  O   . ALA A 1 622  ? 54.709 66.462  -31.022 1.00 14.71 ? 622  ALA A O   1 
ATOM   5058 C  CB  . ALA A 1 622  ? 56.122 68.945  -29.633 1.00 11.72 ? 622  ALA A CB  1 
ATOM   5059 N  N   . ARG A 1 623  ? 56.937 66.304  -31.360 1.00 10.26 ? 623  ARG A N   1 
ATOM   5060 C  CA  . ARG A 1 623  ? 56.943 64.814  -31.391 1.00 10.42 ? 623  ARG A CA  1 
ATOM   5061 C  C   . ARG A 1 623  ? 57.961 64.402  -30.359 1.00 9.40  ? 623  ARG A C   1 
ATOM   5062 O  O   . ARG A 1 623  ? 59.128 64.775  -30.420 1.00 11.30 ? 623  ARG A O   1 
ATOM   5063 C  CB  . ARG A 1 623  ? 57.326 64.292  -32.793 1.00 13.40 ? 623  ARG A CB  1 
ATOM   5064 C  CG  . ARG A 1 623  ? 57.346 62.772  -32.811 1.00 14.82 ? 623  ARG A CG  1 
ATOM   5065 C  CD  . ARG A 1 623  ? 57.406 62.213  -34.292 1.00 17.61 ? 623  ARG A CD  1 
ATOM   5066 N  NE  . ARG A 1 623  ? 57.597 60.753  -34.291 1.00 18.47 ? 623  ARG A NE  1 
ATOM   5067 C  CZ  . ARG A 1 623  ? 58.801 60.184  -34.211 1.00 20.26 ? 623  ARG A CZ  1 
ATOM   5068 N  NH1 . ARG A 1 623  ? 59.903 60.902  -34.156 1.00 22.11 ? 623  ARG A NH1 1 
ATOM   5069 N  NH2 . ARG A 1 623  ? 58.881 58.863  -34.084 1.00 22.18 ? 623  ARG A NH2 1 
ATOM   5070 N  N   . VAL A 1 624  ? 57.486 63.631  -29.379 1.00 9.62  ? 624  VAL A N   1 
ATOM   5071 C  CA  . VAL A 1 624  ? 58.283 63.350  -28.182 1.00 9.52  ? 624  VAL A CA  1 
ATOM   5072 C  C   . VAL A 1 624  ? 58.353 61.864  -27.880 1.00 8.92  ? 624  VAL A C   1 
ATOM   5073 O  O   . VAL A 1 624  ? 57.316 61.185  -27.969 1.00 9.15  ? 624  VAL A O   1 
ATOM   5074 C  CB  . VAL A 1 624  ? 57.644 64.119  -26.977 1.00 9.43  ? 624  VAL A CB  1 
ATOM   5075 C  CG1 . VAL A 1 624  ? 58.659 64.082  -25.783 1.00 9.80  ? 624  VAL A CG1 1 
ATOM   5076 C  CG2 . VAL A 1 624  ? 57.301 65.602  -27.397 1.00 10.69 ? 624  VAL A CG2 1 
ATOM   5077 N  N   . PRO A 1 625  ? 59.568 61.374  -27.513 1.00 9.00  ? 625  PRO A N   1 
ATOM   5078 C  CA  . PRO A 1 625  ? 59.684 59.927  -27.253 1.00 9.24  ? 625  PRO A CA  1 
ATOM   5079 C  C   . PRO A 1 625  ? 58.866 59.464  -26.037 1.00 8.99  ? 625  PRO A C   1 
ATOM   5080 O  O   . PRO A 1 625  ? 58.438 60.284  -25.187 1.00 8.83  ? 625  PRO A O   1 
ATOM   5081 C  CB  . PRO A 1 625  ? 61.167 59.730  -26.915 1.00 11.12 ? 625  PRO A CB  1 
ATOM   5082 C  CG  . PRO A 1 625  ? 61.897 60.945  -27.529 1.00 11.25 ? 625  PRO A CG  1 
ATOM   5083 C  CD  . PRO A 1 625  ? 60.870 62.063  -27.398 1.00 9.61  ? 625  PRO A CD  1 
ATOM   5084 N  N   . PRO A 1 626  ? 58.658 58.165  -25.898 1.00 9.03  ? 626  PRO A N   1 
ATOM   5085 C  CA  . PRO A 1 626  ? 57.933 57.614  -24.724 1.00 8.06  ? 626  PRO A CA  1 
ATOM   5086 C  C   . PRO A 1 626  ? 58.733 58.049  -23.463 1.00 7.79  ? 626  PRO A C   1 
ATOM   5087 O  O   . PRO A 1 626  ? 59.956 57.872  -23.385 1.00 8.95  ? 626  PRO A O   1 
ATOM   5088 C  CB  . PRO A 1 626  ? 58.118 56.100  -24.893 1.00 8.31  ? 626  PRO A CB  1 
ATOM   5089 C  CG  . PRO A 1 626  ? 58.373 55.917  -26.401 1.00 9.09  ? 626  PRO A CG  1 
ATOM   5090 C  CD  . PRO A 1 626  ? 59.247 57.103  -26.758 1.00 9.71  ? 626  PRO A CD  1 
ATOM   5091 N  N   . MET A 1 627  ? 58.027 58.604  -22.463 1.00 7.59  ? 627  MET A N   1 
ATOM   5092 C  CA  . MET A 1 627  ? 58.666 59.023  -21.183 1.00 7.49  ? 627  MET A CA  1 
ATOM   5093 C  C   . MET A 1 627  ? 59.931 59.787  -21.449 1.00 7.64  ? 627  MET A C   1 
ATOM   5094 O  O   . MET A 1 627  ? 60.965 59.630  -20.772 1.00 8.80  ? 627  MET A O   1 
ATOM   5095 C  CB  . MET A 1 627  ? 58.980 57.791  -20.300 1.00 8.34  ? 627  MET A CB  1 
ATOM   5096 C  CG  . MET A 1 627  ? 57.645 57.069  -19.904 1.00 8.77  ? 627  MET A CG  1 
ATOM   5097 S  SD  . MET A 1 627  ? 57.872 55.383  -19.240 1.00 11.26 ? 627  MET A SD  1 
ATOM   5098 C  CE  . MET A 1 627  ? 58.714 55.704  -17.783 1.00 12.11 ? 627  MET A CE  1 
ATOM   5099 N  N   . GLY A 1 628  ? 59.825 60.683  -22.442 1.00 8.99  ? 628  GLY A N   1 
ATOM   5100 C  CA  . GLY A 1 628  ? 61.018 61.360  -22.951 1.00 10.36 ? 628  GLY A CA  1 
ATOM   5101 C  C   . GLY A 1 628  ? 60.946 62.850  -23.158 1.00 7.76  ? 628  GLY A C   1 
ATOM   5102 O  O   . GLY A 1 628  ? 59.970 63.507  -22.716 1.00 8.36  ? 628  GLY A O   1 
ATOM   5103 N  N   . LEU A 1 629  ? 61.986 63.392  -23.796 1.00 8.37  ? 629  LEU A N   1 
ATOM   5104 C  CA  . LEU A 1 629  ? 62.114 64.864  -24.005 1.00 8.91  ? 629  LEU A CA  1 
ATOM   5105 C  C   . LEU A 1 629  ? 62.502 65.148  -25.423 1.00 9.29  ? 629  LEU A C   1 
ATOM   5106 O  O   . LEU A 1 629  ? 63.257 64.351  -26.063 1.00 9.51  ? 629  LEU A O   1 
ATOM   5107 C  CB  . LEU A 1 629  ? 63.199 65.454  -23.093 1.00 8.88  ? 629  LEU A CB  1 
ATOM   5108 C  CG  . LEU A 1 629  ? 62.963 65.300  -21.597 1.00 8.98  ? 629  LEU A CG  1 
ATOM   5109 C  CD1 . LEU A 1 629  ? 64.225 65.521  -20.792 1.00 9.66  ? 629  LEU A CD1 1 
ATOM   5110 C  CD2 . LEU A 1 629  ? 61.899 66.321  -21.147 1.00 9.23  ? 629  LEU A CD2 1 
ATOM   5111 N  N   . ALA A 1 630  ? 62.041 66.282  -25.935 1.00 9.03  ? 630  ALA A N   1 
ATOM   5112 C  CA  . ALA A 1 630  ? 62.425 66.705  -27.315 1.00 9.15  ? 630  ALA A CA  1 
ATOM   5113 C  C   . ALA A 1 630  ? 62.664 68.212  -27.297 1.00 9.18  ? 630  ALA A C   1 
ATOM   5114 O  O   . ALA A 1 630  ? 61.847 68.972  -26.753 1.00 10.00 ? 630  ALA A O   1 
ATOM   5115 C  CB  . ALA A 1 630  ? 61.339 66.338  -28.321 1.00 11.18 ? 630  ALA A CB  1 
ATOM   5116 N  N   . THR A 1 631  ? 63.774 68.639  -27.894 1.00 9.93  ? 631  THR A N   1 
ATOM   5117 C  CA  . THR A 1 631  ? 64.169 70.077  -27.919 1.00 10.80 ? 631  THR A CA  1 
ATOM   5118 C  C   . THR A 1 631  ? 63.908 70.738  -29.271 1.00 10.15 ? 631  THR A C   1 
ATOM   5119 O  O   . THR A 1 631  ? 64.135 70.107  -30.313 1.00 11.45 ? 631  THR A O   1 
ATOM   5120 C  CB  . THR A 1 631  ? 65.688 70.158  -27.648 1.00 10.97 ? 631  THR A CB  1 
ATOM   5121 O  OG1 . THR A 1 631  ? 65.960 69.460  -26.424 1.00 11.03 ? 631  THR A OG1 1 
ATOM   5122 C  CG2 . THR A 1 631  ? 66.200 71.616  -27.482 1.00 13.62 ? 631  THR A CG2 1 
ATOM   5123 N  N   . TYR A 1 632  ? 63.387 71.951  -29.231 1.00 9.83  ? 632  TYR A N   1 
ATOM   5124 C  CA  . TYR A 1 632  ? 63.139 72.747  -30.462 1.00 8.88  ? 632  TYR A CA  1 
ATOM   5125 C  C   . TYR A 1 632  ? 63.723 74.130  -30.220 1.00 9.86  ? 632  TYR A C   1 
ATOM   5126 O  O   . TYR A 1 632  ? 64.046 74.536  -29.115 1.00 9.94  ? 632  TYR A O   1 
ATOM   5127 C  CB  . TYR A 1 632  ? 61.640 72.851  -30.791 1.00 11.16 ? 632  TYR A CB  1 
ATOM   5128 C  CG  . TYR A 1 632  ? 60.997 71.534  -31.123 1.00 9.99  ? 632  TYR A CG  1 
ATOM   5129 C  CD1 . TYR A 1 632  ? 60.610 70.619  -30.120 1.00 10.62 ? 632  TYR A CD1 1 
ATOM   5130 C  CD2 . TYR A 1 632  ? 60.790 71.162  -32.469 1.00 11.09 ? 632  TYR A CD2 1 
ATOM   5131 C  CE1 . TYR A 1 632  ? 60.056 69.399  -30.472 1.00 11.58 ? 632  TYR A CE1 1 
ATOM   5132 C  CE2 . TYR A 1 632  ? 60.240 69.936  -32.829 1.00 12.27 ? 632  TYR A CE2 1 
ATOM   5133 C  CZ  . TYR A 1 632  ? 59.881 69.058  -31.812 1.00 12.27 ? 632  TYR A CZ  1 
ATOM   5134 O  OH  . TYR A 1 632  ? 59.331 67.813  -32.146 1.00 14.53 ? 632  TYR A OH  1 
ATOM   5135 N  N   . VAL A 1 633  ? 63.852 74.840  -31.344 1.00 9.83  ? 633  VAL A N   1 
ATOM   5136 C  CA  . VAL A 1 633  ? 64.412 76.188  -31.318 1.00 10.47 ? 633  VAL A CA  1 
ATOM   5137 C  C   . VAL A 1 633  ? 63.470 77.149  -32.056 1.00 9.89  ? 633  VAL A C   1 
ATOM   5138 O  O   . VAL A 1 633  ? 62.980 76.831  -33.146 1.00 11.38 ? 633  VAL A O   1 
ATOM   5139 C  CB  . VAL A 1 633  ? 65.815 76.225  -32.033 1.00 11.73 ? 633  VAL A CB  1 
ATOM   5140 C  CG1 . VAL A 1 633  ? 66.406 77.623  -31.956 1.00 14.66 ? 633  VAL A CG1 1 
ATOM   5141 C  CG2 . VAL A 1 633  ? 66.749 75.196  -31.405 1.00 14.23 ? 633  VAL A CG2 1 
ATOM   5142 N  N   . LEU A 1 634  ? 63.226 78.285  -31.437 1.00 9.90  ? 634  LEU A N   1 
ATOM   5143 C  CA  . LEU A 1 634  ? 62.374 79.349  -32.028 1.00 10.67 ? 634  LEU A CA  1 
ATOM   5144 C  C   . LEU A 1 634  ? 63.348 80.459  -32.407 1.00 11.58 ? 634  LEU A C   1 
ATOM   5145 O  O   . LEU A 1 634  ? 64.116 80.929  -31.571 1.00 12.20 ? 634  LEU A O   1 
ATOM   5146 C  CB  . LEU A 1 634  ? 61.354 79.901  -31.012 1.00 12.73 ? 634  LEU A CB  1 
ATOM   5147 C  CG  . LEU A 1 634  ? 60.477 78.898  -30.263 1.00 20.53 ? 634  LEU A CG  1 
ATOM   5148 C  CD1 . LEU A 1 634  ? 59.335 79.676  -29.570 1.00 17.50 ? 634  LEU A CD1 1 
ATOM   5149 C  CD2 . LEU A 1 634  ? 59.973 77.797  -31.091 1.00 22.48 ? 634  LEU A CD2 1 
ATOM   5150 N  N   . THR A 1 635  ? 63.274 80.885  -33.689 1.00 12.47 ? 635  THR A N   1 
ATOM   5151 C  CA  . THR A 1 635  ? 64.222 81.907  -34.195 1.00 11.44 ? 635  THR A CA  1 
ATOM   5152 C  C   . THR A 1 635  ? 63.457 83.061  -34.854 1.00 12.89 ? 635  THR A C   1 
ATOM   5153 O  O   . THR A 1 635  ? 62.508 82.851  -35.608 1.00 13.60 ? 635  THR A O   1 
ATOM   5154 C  CB  . THR A 1 635  ? 65.148 81.262  -35.269 1.00 12.99 ? 635  THR A CB  1 
ATOM   5155 O  OG1 . THR A 1 635  ? 65.838 80.137  -34.670 1.00 14.60 ? 635  THR A OG1 1 
ATOM   5156 C  CG2 . THR A 1 635  ? 66.224 82.271  -35.739 1.00 14.05 ? 635  THR A CG2 1 
ATOM   5157 N  N   . ILE A 1 636  ? 63.902 84.275  -34.545 1.00 14.77 ? 636  ILE A N   1 
ATOM   5158 C  CA  . ILE A 1 636  ? 63.211 85.432  -35.148 1.00 15.96 ? 636  ILE A CA  1 
ATOM   5159 C  C   . ILE A 1 636  ? 63.821 85.766  -36.528 1.00 17.06 ? 636  ILE A C   1 
ATOM   5160 O  O   . ILE A 1 636  ? 64.959 85.392  -36.819 1.00 16.16 ? 636  ILE A O   1 
ATOM   5161 C  CB  . ILE A 1 636  ? 63.321 86.626  -34.234 1.00 15.48 ? 636  ILE A CB  1 
ATOM   5162 C  CG1 . ILE A 1 636  ? 62.355 87.747  -34.681 1.00 15.30 ? 636  ILE A CG1 1 
ATOM   5163 C  CG2 . ILE A 1 636  ? 64.764 87.151  -34.217 1.00 16.59 ? 636  ILE A CG2 1 
ATOM   5164 C  CD1 . ILE A 1 636  ? 62.324 88.949  -33.736 1.00 19.29 ? 636  ILE A CD1 1 
ATOM   5165 N  N   . SER A 1 637  ? 62.989 86.328  -37.409 1.00 17.74 ? 637  SER A N   1 
ATOM   5166 C  CA  . SER A 1 637  ? 63.500 86.800  -38.715 1.00 20.05 ? 637  SER A CA  1 
ATOM   5167 C  C   . SER A 1 637  ? 62.848 88.163  -38.937 1.00 22.65 ? 637  SER A C   1 
ATOM   5168 O  O   . SER A 1 637  ? 61.944 88.560  -38.217 1.00 21.03 ? 637  SER A O   1 
ATOM   5169 C  CB  . SER A 1 637  ? 63.181 85.813  -39.861 1.00 25.36 ? 637  SER A CB  1 
ATOM   5170 O  OG  . SER A 1 637  ? 61.803 85.548  -39.988 1.00 32.35 ? 637  SER A OG  1 
ATOM   5171 N  N   . ASP A 1 638  ? 63.346 88.896  -39.933 1.00 26.62 ? 638  ASP A N   1 
ATOM   5172 C  CA  . ASP A 1 638  ? 62.802 90.237  -40.185 1.00 29.84 ? 638  ASP A CA  1 
ATOM   5173 C  C   . ASP A 1 638  ? 61.471 90.207  -40.947 1.00 28.87 ? 638  ASP A C   1 
ATOM   5174 O  O   . ASP A 1 638  ? 60.721 91.183  -40.910 1.00 34.27 ? 638  ASP A O   1 
ATOM   5175 C  CB  . ASP A 1 638  ? 63.830 91.091  -40.937 1.00 35.79 ? 638  ASP A CB  1 
ATOM   5176 C  CG  . ASP A 1 638  ? 63.769 90.871  -42.430 1.00 44.50 ? 638  ASP A CG  1 
ATOM   5177 O  OD1 . ASP A 1 638  ? 63.797 89.684  -42.855 1.00 49.24 ? 638  ASP A OD1 1 
ATOM   5178 O  OD2 . ASP A 1 638  ? 63.689 91.879  -43.188 1.00 48.98 ? 638  ASP A OD2 1 
ATOM   5179 N  N   . SER A 1 639  ? 61.149 89.081  -41.596 1.00 24.78 ? 639  SER A N   1 
ATOM   5180 C  CA  . SER A 1 639  ? 59.914 88.977  -42.352 1.00 26.34 ? 639  SER A CA  1 
ATOM   5181 C  C   . SER A 1 639  ? 59.306 87.587  -42.249 1.00 25.40 ? 639  SER A C   1 
ATOM   5182 O  O   . SER A 1 639  ? 59.880 86.700  -41.591 1.00 22.92 ? 639  SER A O   1 
ATOM   5183 C  CB  . SER A 1 639  ? 60.162 89.331  -43.830 1.00 24.14 ? 639  SER A CB  1 
ATOM   5184 O  OG  . SER A 1 639  ? 60.983 88.358  -44.456 1.00 32.58 ? 639  SER A OG  1 
ATOM   5185 N  N   . LYS A 1 640  ? 58.153 87.401  -42.874 1.00 23.41 ? 640  LYS A N   1 
ATOM   5186 C  CA  . LYS A 1 640  ? 57.469 86.109  -42.845 1.00 24.68 ? 640  LYS A CA  1 
ATOM   5187 C  C   . LYS A 1 640  ? 58.394 84.947  -43.198 1.00 23.11 ? 640  LYS A C   1 
ATOM   5188 O  O   . LYS A 1 640  ? 58.949 84.856  -44.298 1.00 23.25 ? 640  LYS A O   1 
ATOM   5189 C  CB  . LYS A 1 640  ? 56.257 86.089  -43.783 1.00 27.29 ? 640  LYS A CB  1 
ATOM   5190 C  CG  . LYS A 1 640  ? 55.006 86.833  -43.293 1.00 35.72 ? 640  LYS A CG  1 
ATOM   5191 C  CD  . LYS A 1 640  ? 53.789 86.568  -44.221 1.00 38.28 ? 640  LYS A CD  1 
ATOM   5192 C  CE  . LYS A 1 640  ? 54.019 87.096  -45.631 1.00 42.58 ? 640  LYS A CE  1 
ATOM   5193 N  NZ  . LYS A 1 640  ? 52.979 88.095  -46.035 1.00 46.09 ? 640  LYS A NZ  1 
ATOM   5194 N  N   . PRO A 1 641  ? 58.566 84.008  -42.255 1.00 21.37 ? 641  PRO A N   1 
ATOM   5195 C  CA  . PRO A 1 641  ? 59.410 82.835  -42.446 1.00 20.79 ? 641  PRO A CA  1 
ATOM   5196 C  C   . PRO A 1 641  ? 58.752 81.850  -43.406 1.00 19.55 ? 641  PRO A C   1 
ATOM   5197 O  O   . PRO A 1 641  ? 57.529 81.699  -43.445 1.00 19.37 ? 641  PRO A O   1 
ATOM   5198 C  CB  . PRO A 1 641  ? 59.480 82.210  -41.029 1.00 23.24 ? 641  PRO A CB  1 
ATOM   5199 C  CG  . PRO A 1 641  ? 59.114 83.270  -40.127 1.00 20.71 ? 641  PRO A CG  1 
ATOM   5200 C  CD  . PRO A 1 641  ? 58.099 84.091  -40.855 1.00 20.90 ? 641  PRO A CD  1 
ATOM   5201 N  N   . GLU A 1 642  ? 59.556 81.109  -44.142 1.00 19.11 ? 642  GLU A N   1 
ATOM   5202 C  CA  . GLU A 1 642  ? 58.998 80.134  -45.064 1.00 19.07 ? 642  GLU A CA  1 
ATOM   5203 C  C   . GLU A 1 642  ? 58.045 79.060  -44.517 1.00 19.73 ? 642  GLU A C   1 
ATOM   5204 O  O   . GLU A 1 642  ? 57.062 78.683  -45.148 1.00 22.57 ? 642  GLU A O   1 
ATOM   5205 C  CB  . GLU A 1 642  ? 60.140 79.405  -45.802 1.00 22.84 ? 642  GLU A CB  1 
ATOM   5206 C  CG  . GLU A 1 642  ? 59.686 78.315  -46.745 1.00 28.43 ? 642  GLU A CG  1 
ATOM   5207 C  CD  . GLU A 1 642  ? 60.866 77.690  -47.484 1.00 36.14 ? 642  GLU A CD  1 
ATOM   5208 O  OE1 . GLU A 1 642  ? 60.647 76.653  -48.160 1.00 42.06 ? 642  GLU A OE1 1 
ATOM   5209 O  OE2 . GLU A 1 642  ? 62.001 78.234  -47.376 1.00 37.33 ? 642  GLU A OE2 1 
ATOM   5210 N  N   . HIS A 1 643  ? 58.336 78.564  -43.316 1.00 17.57 ? 643  HIS A N   1 
ATOM   5211 C  CA  . HIS A 1 643  ? 57.530 77.463  -42.761 1.00 17.47 ? 643  HIS A CA  1 
ATOM   5212 C  C   . HIS A 1 643  ? 56.560 77.882  -41.667 1.00 15.47 ? 643  HIS A C   1 
ATOM   5213 O  O   . HIS A 1 643  ? 56.110 77.011  -40.895 1.00 15.59 ? 643  HIS A O   1 
ATOM   5214 C  CB  . HIS A 1 643  ? 58.464 76.362  -42.232 1.00 18.29 ? 643  HIS A CB  1 
ATOM   5215 C  CG  . HIS A 1 643  ? 59.327 75.751  -43.295 1.00 18.97 ? 643  HIS A CG  1 
ATOM   5216 N  ND1 . HIS A 1 643  ? 58.882 74.736  -44.110 1.00 27.08 ? 643  HIS A ND1 1 
ATOM   5217 C  CD2 . HIS A 1 643  ? 60.574 76.061  -43.716 1.00 22.20 ? 643  HIS A CD2 1 
ATOM   5218 C  CE1 . HIS A 1 643  ? 59.823 74.445  -45.001 1.00 22.74 ? 643  HIS A CE1 1 
ATOM   5219 N  NE2 . HIS A 1 643  ? 60.854 75.239  -44.781 1.00 22.11 ? 643  HIS A NE2 1 
ATOM   5220 N  N   . THR A 1 644  ? 56.238 79.165  -41.589 1.00 13.20 ? 644  THR A N   1 
ATOM   5221 C  CA  . THR A 1 644  ? 55.266 79.653  -40.623 1.00 14.29 ? 644  THR A CA  1 
ATOM   5222 C  C   . THR A 1 644  ? 54.097 80.293  -41.380 1.00 15.99 ? 644  THR A C   1 
ATOM   5223 O  O   . THR A 1 644  ? 54.339 81.126  -42.286 1.00 17.77 ? 644  THR A O   1 
ATOM   5224 C  CB  . THR A 1 644  ? 55.933 80.634  -39.675 1.00 13.85 ? 644  THR A CB  1 
ATOM   5225 O  OG1 . THR A 1 644  ? 56.985 79.936  -38.964 1.00 14.93 ? 644  THR A OG1 1 
ATOM   5226 C  CG2 . THR A 1 644  ? 54.947 81.245  -38.636 1.00 13.71 ? 644  THR A CG2 1 
ATOM   5227 N  N   . SER A 1 645  ? 52.861 79.935  -41.044 1.00 13.89 ? 645  SER A N   1 
ATOM   5228 C  CA  . SER A 1 645  ? 51.666 80.512  -41.652 1.00 13.70 ? 645  SER A CA  1 
ATOM   5229 C  C   . SER A 1 645  ? 50.961 81.350  -40.592 1.00 13.03 ? 645  SER A C   1 
ATOM   5230 O  O   . SER A 1 645  ? 51.286 81.285  -39.400 1.00 13.75 ? 645  SER A O   1 
ATOM   5231 C  CB  . SER A 1 645  ? 50.737 79.433  -42.199 1.00 14.54 ? 645  SER A CB  1 
ATOM   5232 O  OG  . SER A 1 645  ? 50.222 78.659  -41.103 1.00 15.36 ? 645  SER A OG  1 
ATOM   5233 N  N   . TYR A 1 646  ? 50.015 82.183  -41.008 1.00 12.97 ? 646  TYR A N   1 
ATOM   5234 C  CA  . TYR A 1 646  ? 49.306 83.076  -40.123 1.00 11.49 ? 646  TYR A CA  1 
ATOM   5235 C  C   . TYR A 1 646  ? 47.810 82.861  -40.206 1.00 12.83 ? 646  TYR A C   1 
ATOM   5236 O  O   . TYR A 1 646  ? 47.267 82.827  -41.300 1.00 16.47 ? 646  TYR A O   1 
ATOM   5237 C  CB  . TYR A 1 646  ? 49.612 84.538  -40.527 1.00 14.05 ? 646  TYR A CB  1 
ATOM   5238 C  CG  . TYR A 1 646  ? 51.085 84.798  -40.291 1.00 13.03 ? 646  TYR A CG  1 
ATOM   5239 C  CD1 . TYR A 1 646  ? 52.016 84.537  -41.284 1.00 15.23 ? 646  TYR A CD1 1 
ATOM   5240 C  CD2 . TYR A 1 646  ? 51.549 85.165  -39.036 1.00 11.99 ? 646  TYR A CD2 1 
ATOM   5241 C  CE1 . TYR A 1 646  ? 53.415 84.636  -41.047 1.00 16.86 ? 646  TYR A CE1 1 
ATOM   5242 C  CE2 . TYR A 1 646  ? 52.956 85.281  -38.781 1.00 16.01 ? 646  TYR A CE2 1 
ATOM   5243 C  CZ  . TYR A 1 646  ? 53.855 85.002  -39.811 1.00 16.49 ? 646  TYR A CZ  1 
ATOM   5244 O  OH  . TYR A 1 646  ? 55.220 85.063  -39.583 1.00 19.28 ? 646  TYR A OH  1 
ATOM   5245 N  N   . ALA A 1 647  ? 47.139 82.775  -39.051 1.00 12.18 ? 647  ALA A N   1 
ATOM   5246 C  CA  . ALA A 1 647  ? 45.715 82.551  -39.033 1.00 12.05 ? 647  ALA A CA  1 
ATOM   5247 C  C   . ALA A 1 647  ? 44.939 83.798  -39.486 1.00 12.71 ? 647  ALA A C   1 
ATOM   5248 O  O   . ALA A 1 647  ? 45.354 84.912  -39.301 1.00 13.46 ? 647  ALA A O   1 
ATOM   5249 C  CB  . ALA A 1 647  ? 45.267 82.174  -37.584 1.00 13.29 ? 647  ALA A CB  1 
ATOM   5250 N  N   . SER A 1 648  ? 43.791 83.534  -40.073 1.00 12.78 ? 648  SER A N   1 
ATOM   5251 C  CA  . SER A 1 648  ? 42.883 84.653  -40.338 1.00 12.68 ? 648  SER A CA  1 
ATOM   5252 C  C   . SER A 1 648  ? 41.999 84.800  -39.121 1.00 12.61 ? 648  SER A C   1 
ATOM   5253 O  O   . SER A 1 648  ? 41.826 83.843  -38.312 1.00 12.46 ? 648  SER A O   1 
ATOM   5254 C  CB  . SER A 1 648  ? 42.031 84.348  -41.568 1.00 15.09 ? 648  SER A CB  1 
ATOM   5255 O  OG  . SER A 1 648  ? 41.213 83.215  -41.369 1.00 20.04 ? 648  SER A OG  1 
ATOM   5256 N  N   . ASN A 1 649  ? 41.368 85.952  -38.933 1.00 11.77 ? 649  ASN A N   1 
ATOM   5257 C  CA  . ASN A 1 649  ? 40.508 86.228  -37.783 1.00 11.47 ? 649  ASN A CA  1 
ATOM   5258 C  C   . ASN A 1 649  ? 39.305 86.996  -38.251 1.00 11.73 ? 649  ASN A C   1 
ATOM   5259 O  O   . ASN A 1 649  ? 39.468 88.011  -39.016 1.00 12.74 ? 649  ASN A O   1 
ATOM   5260 C  CB  . ASN A 1 649  ? 41.240 87.035  -36.716 1.00 11.79 ? 649  ASN A CB  1 
ATOM   5261 C  CG  . ASN A 1 649  ? 42.475 86.296  -36.147 1.00 12.36 ? 649  ASN A CG  1 
ATOM   5262 O  OD1 . ASN A 1 649  ? 42.340 85.511  -35.176 1.00 13.00 ? 649  ASN A OD1 1 
ATOM   5263 N  ND2 . ASN A 1 649  ? 43.661 86.480  -36.753 1.00 13.14 ? 649  ASN A ND2 1 
ATOM   5264 N  N   . LEU A 1 650  ? 38.142 86.581  -37.805 1.00 12.50 ? 650  LEU A N   1 
ATOM   5265 C  CA  . LEU A 1 650  ? 36.850 87.172  -38.190 1.00 11.07 ? 650  LEU A CA  1 
ATOM   5266 C  C   . LEU A 1 650  ? 36.042 87.442  -36.949 1.00 11.31 ? 650  LEU A C   1 
ATOM   5267 O  O   . LEU A 1 650  ? 35.783 86.507  -36.168 1.00 12.84 ? 650  LEU A O   1 
ATOM   5268 C  CB  . LEU A 1 650  ? 36.128 86.191  -39.135 1.00 12.23 ? 650  LEU A CB  1 
ATOM   5269 C  CG  . LEU A 1 650  ? 34.675 86.565  -39.458 1.00 11.97 ? 650  LEU A CG  1 
ATOM   5270 C  CD1 . LEU A 1 650  ? 34.626 87.862  -40.343 1.00 13.52 ? 650  LEU A CD1 1 
ATOM   5271 C  CD2 . LEU A 1 650  ? 34.026 85.413  -40.242 1.00 16.33 ? 650  LEU A CD2 1 
ATOM   5272 N  N   . LEU A 1 651  ? 35.690 88.681  -36.668 1.00 12.90 ? 651  LEU A N   1 
ATOM   5273 C  CA  . LEU A 1 651  ? 34.903 89.074  -35.530 1.00 12.18 ? 651  LEU A CA  1 
ATOM   5274 C  C   . LEU A 1 651  ? 33.452 89.320  -35.978 1.00 13.46 ? 651  LEU A C   1 
ATOM   5275 O  O   . LEU A 1 651  ? 33.194 90.219  -36.818 1.00 15.59 ? 651  LEU A O   1 
ATOM   5276 C  CB  . LEU A 1 651  ? 35.532 90.326  -34.921 1.00 15.89 ? 651  LEU A CB  1 
ATOM   5277 C  CG  . LEU A 1 651  ? 35.174 90.667  -33.455 1.00 22.18 ? 651  LEU A CG  1 
ATOM   5278 C  CD1 . LEU A 1 651  ? 33.832 91.275  -33.349 1.00 28.44 ? 651  LEU A CD1 1 
ATOM   5279 C  CD2 . LEU A 1 651  ? 35.263 89.449  -32.618 1.00 19.47 ? 651  LEU A CD2 1 
ATOM   5280 N  N   . LEU A 1 652  ? 32.509 88.521  -35.511 1.00 13.11 ? 652  LEU A N   1 
ATOM   5281 C  CA  . LEU A 1 652  ? 31.118 88.598  -35.886 1.00 13.32 ? 652  LEU A CA  1 
ATOM   5282 C  C   . LEU A 1 652  ? 30.352 89.289  -34.791 1.00 16.16 ? 652  LEU A C   1 
ATOM   5283 O  O   . LEU A 1 652  ? 30.245 88.810  -33.632 1.00 15.54 ? 652  LEU A O   1 
ATOM   5284 C  CB  . LEU A 1 652  ? 30.574 87.200  -36.175 1.00 13.79 ? 652  LEU A CB  1 
ATOM   5285 C  CG  . LEU A 1 652  ? 31.351 86.498  -37.285 1.00 14.25 ? 652  LEU A CG  1 
ATOM   5286 C  CD1 . LEU A 1 652  ? 30.815 85.071  -37.482 1.00 15.54 ? 652  LEU A CD1 1 
ATOM   5287 C  CD2 . LEU A 1 652  ? 31.235 87.284  -38.648 1.00 15.77 ? 652  LEU A CD2 1 
ATOM   5288 N  N   . ARG A 1 653  ? 29.786 90.454  -35.126 1.00 15.70 ? 653  ARG A N   1 
ATOM   5289 C  CA  . ARG A 1 653  ? 29.038 91.239  -34.170 1.00 17.95 ? 653  ARG A CA  1 
ATOM   5290 C  C   . ARG A 1 653  ? 28.440 92.436  -34.911 1.00 18.38 ? 653  ARG A C   1 
ATOM   5291 O  O   . ARG A 1 653  ? 28.959 92.852  -35.921 1.00 19.93 ? 653  ARG A O   1 
ATOM   5292 C  CB  . ARG A 1 653  ? 29.953 91.747  -33.054 1.00 18.49 ? 653  ARG A CB  1 
ATOM   5293 C  CG  . ARG A 1 653  ? 30.934 92.757  -33.470 1.00 20.65 ? 653  ARG A CG  1 
ATOM   5294 C  CD  . ARG A 1 653  ? 30.583 93.899  -32.638 1.00 33.08 ? 653  ARG A CD  1 
ATOM   5295 N  NE  . ARG A 1 653  ? 31.479 93.985  -31.520 1.00 27.75 ? 653  ARG A NE  1 
ATOM   5296 C  CZ  . ARG A 1 653  ? 31.208 94.573  -30.352 1.00 31.30 ? 653  ARG A CZ  1 
ATOM   5297 N  NH1 . ARG A 1 653  ? 30.032 95.123  -30.094 1.00 35.81 ? 653  ARG A NH1 1 
ATOM   5298 N  NH2 . ARG A 1 653  ? 32.175 94.696  -29.466 1.00 36.97 ? 653  ARG A NH2 1 
ATOM   5299 N  N   . LYS A 1 654  ? 27.349 92.962  -34.397 1.00 22.12 ? 654  LYS A N   1 
ATOM   5300 C  CA  . LYS A 1 654  ? 26.834 94.176  -35.023 1.00 25.78 ? 654  LYS A CA  1 
ATOM   5301 C  C   . LYS A 1 654  ? 27.664 95.325  -34.376 1.00 26.17 ? 654  LYS A C   1 
ATOM   5302 O  O   . LYS A 1 654  ? 28.154 95.201  -33.259 1.00 28.53 ? 654  LYS A O   1 
ATOM   5303 C  CB  . LYS A 1 654  ? 25.361 94.368  -34.665 1.00 28.99 ? 654  LYS A CB  1 
ATOM   5304 C  CG  . LYS A 1 654  ? 24.438 93.240  -35.119 1.00 33.35 ? 654  LYS A CG  1 
ATOM   5305 C  CD  . LYS A 1 654  ? 23.266 93.785  -35.910 1.00 40.46 ? 654  LYS A CD  1 
ATOM   5306 C  CE  . LYS A 1 654  ? 23.755 94.525  -37.154 1.00 41.72 ? 654  LYS A CE  1 
ATOM   5307 N  NZ  . LYS A 1 654  ? 22.631 95.148  -37.937 1.00 46.02 ? 654  LYS A NZ  1 
ATOM   5308 N  N   . ASN A 1 655  ? 27.807 96.444  -35.054 1.00 28.22 ? 655  ASN A N   1 
ATOM   5309 C  CA  . ASN A 1 655  ? 28.537 97.559  -34.424 1.00 28.85 ? 655  ASN A CA  1 
ATOM   5310 C  C   . ASN A 1 655  ? 30.005 97.241  -34.043 1.00 25.00 ? 655  ASN A C   1 
ATOM   5311 O  O   . ASN A 1 655  ? 30.432 97.440  -32.915 1.00 27.89 ? 655  ASN A O   1 
ATOM   5312 C  CB  . ASN A 1 655  ? 27.785 97.993  -33.157 1.00 29.74 ? 655  ASN A CB  1 
ATOM   5313 C  CG  . ASN A 1 655  ? 28.283 99.316  -32.602 1.00 38.10 ? 655  ASN A CG  1 
ATOM   5314 O  OD1 . ASN A 1 655  ? 28.131 99.597  -31.399 1.00 36.13 ? 655  ASN A OD1 1 
ATOM   5315 N  ND2 . ASN A 1 655  ? 28.864 100.158 -33.479 1.00 34.78 ? 655  ASN A ND2 1 
ATOM   5316 N  N   . PRO A 1 656  ? 30.796 96.760  -34.997 1.00 21.40 ? 656  PRO A N   1 
ATOM   5317 C  CA  . PRO A 1 656  ? 32.200 96.445  -34.693 1.00 19.45 ? 656  PRO A CA  1 
ATOM   5318 C  C   . PRO A 1 656  ? 33.054 97.701  -34.705 1.00 19.23 ? 656  PRO A C   1 
ATOM   5319 O  O   . PRO A 1 656  ? 32.704 98.749  -35.279 1.00 18.79 ? 656  PRO A O   1 
ATOM   5320 C  CB  . PRO A 1 656  ? 32.605 95.542  -35.845 1.00 19.04 ? 656  PRO A CB  1 
ATOM   5321 C  CG  . PRO A 1 656  ? 31.805 96.190  -37.004 1.00 17.91 ? 656  PRO A CG  1 
ATOM   5322 C  CD  . PRO A 1 656  ? 30.450 96.359  -36.372 1.00 20.35 ? 656  PRO A CD  1 
ATOM   5323 N  N   . THR A 1 657  ? 34.188 97.586  -34.031 1.00 18.98 ? 657  THR A N   1 
ATOM   5324 C  CA  . THR A 1 657  ? 35.170 98.643  -34.044 1.00 18.47 ? 657  THR A CA  1 
ATOM   5325 C  C   . THR A 1 657  ? 36.466 97.923  -34.442 1.00 19.79 ? 657  THR A C   1 
ATOM   5326 O  O   . THR A 1 657  ? 36.606 96.682  -34.298 1.00 21.35 ? 657  THR A O   1 
ATOM   5327 C  CB  . THR A 1 657  ? 35.328 99.302  -32.669 1.00 22.31 ? 657  THR A CB  1 
ATOM   5328 O  OG1 . THR A 1 657  ? 35.400 98.287  -31.660 1.00 25.81 ? 657  THR A OG1 1 
ATOM   5329 C  CG2 . THR A 1 657  ? 34.129 100.217 -32.356 1.00 23.38 ? 657  THR A CG2 1 
ATOM   5330 N  N   . SER A 1 658  ? 37.437 98.684  -34.891 1.00 17.04 ? 658  SER A N   1 
ATOM   5331 C  CA  . SER A 1 658  ? 38.699 98.157  -35.381 1.00 18.37 ? 658  SER A CA  1 
ATOM   5332 C  C   . SER A 1 658  ? 39.454 97.348  -34.316 1.00 18.45 ? 658  SER A C   1 
ATOM   5333 O  O   . SER A 1 658  ? 39.252 97.527  -33.111 1.00 20.81 ? 658  SER A O   1 
ATOM   5334 C  CB  . SER A 1 658  ? 39.542 99.321  -35.831 1.00 22.55 ? 658  SER A CB  1 
ATOM   5335 O  OG  . SER A 1 658  ? 39.913 100.049 -34.664 1.00 24.52 ? 658  SER A OG  1 
ATOM   5336 N  N   . LEU A 1 659  ? 40.324 96.445  -34.792 1.00 17.72 ? 659  LEU A N   1 
ATOM   5337 C  CA  . LEU A 1 659  ? 41.120 95.568  -33.880 1.00 20.05 ? 659  LEU A CA  1 
ATOM   5338 C  C   . LEU A 1 659  ? 42.530 95.422  -34.501 1.00 20.11 ? 659  LEU A C   1 
ATOM   5339 O  O   . LEU A 1 659  ? 42.825 94.441  -35.202 1.00 20.51 ? 659  LEU A O   1 
ATOM   5340 C  CB  . LEU A 1 659  ? 40.475 94.156  -33.787 1.00 22.22 ? 659  LEU A CB  1 
ATOM   5341 C  CG  . LEU A 1 659  ? 39.168 94.005  -32.987 1.00 22.94 ? 659  LEU A CG  1 
ATOM   5342 C  CD1 . LEU A 1 659  ? 38.506 92.617  -33.211 1.00 24.84 ? 659  LEU A CD1 1 
ATOM   5343 C  CD2 . LEU A 1 659  ? 39.448 94.179  -31.553 1.00 23.18 ? 659  LEU A CD2 1 
ATOM   5344 N  N   . PRO A 1 660  ? 43.393 96.426  -34.308 1.00 20.54 ? 660  PRO A N   1 
ATOM   5345 C  CA  . PRO A 1 660  ? 44.763 96.398  -34.843 1.00 20.61 ? 660  PRO A CA  1 
ATOM   5346 C  C   . PRO A 1 660  ? 45.580 95.318  -34.095 1.00 17.96 ? 660  PRO A C   1 
ATOM   5347 O  O   . PRO A 1 660  ? 45.328 95.046  -32.914 1.00 20.01 ? 660  PRO A O   1 
ATOM   5348 C  CB  . PRO A 1 660  ? 45.266 97.823  -34.597 1.00 22.79 ? 660  PRO A CB  1 
ATOM   5349 C  CG  . PRO A 1 660  ? 44.574 98.229  -33.349 1.00 23.10 ? 660  PRO A CG  1 
ATOM   5350 C  CD  . PRO A 1 660  ? 43.131 97.641  -33.522 1.00 21.55 ? 660  PRO A CD  1 
ATOM   5351 N  N   . LEU A 1 661  ? 46.533 94.733  -34.794 1.00 20.80 ? 661  LEU A N   1 
ATOM   5352 C  CA  . LEU A 1 661  ? 47.312 93.642  -34.164 1.00 19.55 ? 661  LEU A CA  1 
ATOM   5353 C  C   . LEU A 1 661  ? 48.849 93.850  -34.320 1.00 24.30 ? 661  LEU A C   1 
ATOM   5354 O  O   . LEU A 1 661  ? 49.608 92.871  -34.423 1.00 19.82 ? 661  LEU A O   1 
ATOM   5355 C  CB  . LEU A 1 661  ? 46.871 92.338  -34.840 1.00 20.36 ? 661  LEU A CB  1 
ATOM   5356 C  CG  . LEU A 1 661  ? 45.421 91.890  -34.597 1.00 15.41 ? 661  LEU A CG  1 
ATOM   5357 C  CD1 . LEU A 1 661  ? 45.191 90.594  -35.396 1.00 15.98 ? 661  LEU A CD1 1 
ATOM   5358 C  CD2 . LEU A 1 661  ? 45.213 91.657  -33.078 1.00 19.08 ? 661  LEU A CD2 1 
ATOM   5359 N  N   . GLY A 1 662  ? 49.308 95.106  -34.378 1.00 23.31 ? 662  GLY A N   1 
ATOM   5360 C  CA  . GLY A 1 662  ? 50.750 95.359  -34.541 1.00 22.37 ? 662  GLY A CA  1 
ATOM   5361 C  C   . GLY A 1 662  ? 51.321 94.782  -35.819 1.00 22.28 ? 662  GLY A C   1 
ATOM   5362 O  O   . GLY A 1 662  ? 50.747 94.925  -36.906 1.00 25.83 ? 662  GLY A O   1 
ATOM   5363 N  N   . GLN A 1 663  ? 52.427 94.024  -35.681 1.00 22.90 ? 663  GLN A N   1 
ATOM   5364 C  CA  . GLN A 1 663  ? 53.083 93.432  -36.841 1.00 24.72 ? 663  GLN A CA  1 
ATOM   5365 C  C   . GLN A 1 663  ? 52.402 92.214  -37.455 1.00 18.45 ? 663  GLN A C   1 
ATOM   5366 O  O   . GLN A 1 663  ? 52.795 91.733  -38.525 1.00 24.26 ? 663  GLN A O   1 
ATOM   5367 C  CB  . GLN A 1 663  ? 54.522 93.044  -36.489 1.00 28.59 ? 663  GLN A CB  1 
ATOM   5368 C  CG  . GLN A 1 663  ? 55.262 93.949  -35.476 1.00 35.10 ? 663  GLN A CG  1 
ATOM   5369 C  CD  . GLN A 1 663  ? 56.565 93.256  -35.039 1.00 35.79 ? 663  GLN A CD  1 
ATOM   5370 O  OE1 . GLN A 1 663  ? 57.433 92.972  -35.895 1.00 32.90 ? 663  GLN A OE1 1 
ATOM   5371 N  NE2 . GLN A 1 663  ? 56.688 92.937  -33.727 1.00 34.26 ? 663  GLN A NE2 1 
ATOM   5372 N  N   . TYR A 1 664  ? 51.343 91.735  -36.808 1.00 23.78 ? 664  TYR A N   1 
ATOM   5373 C  CA  . TYR A 1 664  ? 50.629 90.567  -37.320 1.00 22.29 ? 664  TYR A CA  1 
ATOM   5374 C  C   . TYR A 1 664  ? 50.288 90.854  -38.785 1.00 19.90 ? 664  TYR A C   1 
ATOM   5375 O  O   . TYR A 1 664  ? 49.626 91.873  -39.082 1.00 24.19 ? 664  TYR A O   1 
ATOM   5376 C  CB  . TYR A 1 664  ? 49.407 90.338  -36.420 1.00 21.59 ? 664  TYR A CB  1 
ATOM   5377 C  CG  . TYR A 1 664  ? 48.786 88.991  -36.641 1.00 17.02 ? 664  TYR A CG  1 
ATOM   5378 C  CD1 . TYR A 1 664  ? 49.327 87.816  -36.049 1.00 15.37 ? 664  TYR A CD1 1 
ATOM   5379 C  CD2 . TYR A 1 664  ? 47.677 88.866  -37.458 1.00 14.74 ? 664  TYR A CD2 1 
ATOM   5380 C  CE1 . TYR A 1 664  ? 48.766 86.602  -36.285 1.00 14.22 ? 664  TYR A CE1 1 
ATOM   5381 C  CE2 . TYR A 1 664  ? 47.087 87.624  -37.700 1.00 16.57 ? 664  TYR A CE2 1 
ATOM   5382 C  CZ  . TYR A 1 664  ? 47.652 86.488  -37.094 1.00 13.76 ? 664  TYR A CZ  1 
ATOM   5383 O  OH  . TYR A 1 664  ? 47.009 85.285  -37.296 1.00 13.85 ? 664  TYR A OH  1 
ATOM   5384 N  N   . PRO A 1 665  ? 50.656 89.963  -39.717 1.00 23.65 ? 665  PRO A N   1 
ATOM   5385 C  CA  . PRO A 1 665  ? 50.413 90.179  -41.148 1.00 23.55 ? 665  PRO A CA  1 
ATOM   5386 C  C   . PRO A 1 665  ? 49.056 90.051  -41.831 1.00 25.43 ? 665  PRO A C   1 
ATOM   5387 O  O   . PRO A 1 665  ? 48.939 90.295  -43.031 1.00 27.99 ? 665  PRO A O   1 
ATOM   5388 C  CB  . PRO A 1 665  ? 51.471 89.273  -41.803 1.00 24.46 ? 665  PRO A CB  1 
ATOM   5389 C  CG  . PRO A 1 665  ? 51.524 88.113  -40.841 1.00 23.45 ? 665  PRO A CG  1 
ATOM   5390 C  CD  . PRO A 1 665  ? 51.523 88.781  -39.503 1.00 20.80 ? 665  PRO A CD  1 
ATOM   5391 N  N   A GLU A 1 666  ? 48.019 89.688  -41.096 0.50 22.42 ? 666  GLU A N   1 
ATOM   5392 N  N   B GLU A 1 666  ? 48.055 89.660  -41.119 0.50 23.20 ? 666  GLU A N   1 
ATOM   5393 C  CA  A GLU A 1 666  ? 46.696 89.524  -41.717 0.50 21.55 ? 666  GLU A CA  1 
ATOM   5394 C  CA  B GLU A 1 666  ? 46.717 89.544  -41.686 0.50 22.73 ? 666  GLU A CA  1 
ATOM   5395 C  C   A GLU A 1 666  ? 45.780 90.415  -40.927 0.50 20.32 ? 666  GLU A C   1 
ATOM   5396 C  C   B GLU A 1 666  ? 45.723 90.423  -40.935 0.50 21.62 ? 666  GLU A C   1 
ATOM   5397 O  O   A GLU A 1 666  ? 45.736 90.338  -39.695 0.50 18.90 ? 666  GLU A O   1 
ATOM   5398 O  O   B GLU A 1 666  ? 45.736 90.338  -39.695 0.50 20.06 ? 666  GLU A O   1 
ATOM   5399 C  CB  A GLU A 1 666  ? 46.230 88.074  -41.580 0.50 23.41 ? 666  GLU A CB  1 
ATOM   5400 C  CB  B GLU A 1 666  ? 46.255 88.086  -41.674 0.50 24.78 ? 666  GLU A CB  1 
ATOM   5401 C  CG  A GLU A 1 666  ? 44.724 87.838  -41.747 0.50 30.44 ? 666  GLU A CG  1 
ATOM   5402 C  CG  B GLU A 1 666  ? 47.004 87.190  -42.647 0.50 31.09 ? 666  GLU A CG  1 
ATOM   5403 C  CD  A GLU A 1 666  ? 44.355 87.061  -43.028 0.50 30.76 ? 666  GLU A CD  1 
ATOM   5404 C  CD  B GLU A 1 666  ? 46.633 87.460  -44.092 0.50 31.25 ? 666  GLU A CD  1 
ATOM   5405 O  OE1 A GLU A 1 666  ? 45.272 86.636  -43.768 0.50 36.81 ? 666  GLU A OE1 1 
ATOM   5406 O  OE1 B GLU A 1 666  ? 45.431 87.653  -44.371 0.50 34.77 ? 666  GLU A OE1 1 
ATOM   5407 O  OE2 A GLU A 1 666  ? 43.155 86.875  -43.312 0.50 29.15 ? 666  GLU A OE2 1 
ATOM   5408 O  OE2 B GLU A 1 666  ? 47.545 87.478  -44.946 0.50 37.32 ? 666  GLU A OE2 1 
ATOM   5409 N  N   . ASP A 1 667  ? 45.042 91.275  -41.643 1.00 18.90 ? 667  ASP A N   1 
ATOM   5410 C  CA  . ASP A 1 667  ? 44.102 92.175  -40.962 1.00 19.18 ? 667  ASP A CA  1 
ATOM   5411 C  C   . ASP A 1 667  ? 42.806 91.417  -40.485 1.00 12.03 ? 667  ASP A C   1 
ATOM   5412 O  O   . ASP A 1 667  ? 42.305 90.590  -41.208 1.00 15.77 ? 667  ASP A O   1 
ATOM   5413 C  CB  . ASP A 1 667  ? 43.593 93.270  -41.947 1.00 20.70 ? 667  ASP A CB  1 
ATOM   5414 C  CG  . ASP A 1 667  ? 44.685 94.250  -42.368 1.00 28.03 ? 667  ASP A CG  1 
ATOM   5415 O  OD1 . ASP A 1 667  ? 45.681 94.427  -41.613 1.00 31.51 ? 667  ASP A OD1 1 
ATOM   5416 O  OD2 . ASP A 1 667  ? 44.520 94.882  -43.441 1.00 30.30 ? 667  ASP A OD2 1 
ATOM   5417 N  N   . VAL A 1 668  ? 42.349 91.773  -39.330 1.00 13.30 ? 668  VAL A N   1 
ATOM   5418 C  CA  . VAL A 1 668  ? 41.087 91.212  -38.813 1.00 14.85 ? 668  VAL A CA  1 
ATOM   5419 C  C   . VAL A 1 668  ? 39.924 91.590  -39.726 1.00 14.96 ? 668  VAL A C   1 
ATOM   5420 O  O   . VAL A 1 668  ? 39.892 92.757  -40.204 1.00 15.33 ? 668  VAL A O   1 
ATOM   5421 C  CB  . VAL A 1 668  ? 40.781 91.701  -37.386 1.00 16.41 ? 668  VAL A CB  1 
ATOM   5422 C  CG1 . VAL A 1 668  ? 39.418 91.106  -36.897 1.00 15.74 ? 668  VAL A CG1 1 
ATOM   5423 C  CG2 . VAL A 1 668  ? 41.935 91.258  -36.409 1.00 17.22 ? 668  VAL A CG2 1 
ATOM   5424 N  N   A LYS A 1 669  ? 39.028 90.661  -40.013 0.50 13.13 ? 669  LYS A N   1 
ATOM   5425 N  N   B LYS A 1 669  ? 39.028 90.661  -40.013 0.50 13.42 ? 669  LYS A N   1 
ATOM   5426 C  CA  A LYS A 1 669  ? 37.817 90.897  -40.833 0.50 13.49 ? 669  LYS A CA  1 
ATOM   5427 C  CA  B LYS A 1 669  ? 37.817 90.897  -40.833 0.50 13.92 ? 669  LYS A CA  1 
ATOM   5428 C  C   A LYS A 1 669  ? 36.633 90.971  -39.878 0.50 13.69 ? 669  LYS A C   1 
ATOM   5429 C  C   B LYS A 1 669  ? 36.633 90.971  -39.878 0.50 14.15 ? 669  LYS A C   1 
ATOM   5430 O  O   A LYS A 1 669  ? 36.666 90.386  -38.740 0.50 12.85 ? 669  LYS A O   1 
ATOM   5431 O  O   B LYS A 1 669  ? 36.666 90.386  -38.740 0.50 13.57 ? 669  LYS A O   1 
ATOM   5432 C  CB  A LYS A 1 669  ? 37.639 89.770  -41.810 0.50 18.08 ? 669  LYS A CB  1 
ATOM   5433 C  CB  B LYS A 1 669  ? 37.639 89.770  -41.810 0.50 18.60 ? 669  LYS A CB  1 
ATOM   5434 C  CG  A LYS A 1 669  ? 38.799 89.583  -42.790 0.50 26.00 ? 669  LYS A CG  1 
ATOM   5435 C  CG  B LYS A 1 669  ? 38.799 89.583  -42.790 0.50 26.56 ? 669  LYS A CG  1 
ATOM   5436 C  CD  A LYS A 1 669  ? 39.115 90.881  -43.540 0.50 30.36 ? 669  LYS A CD  1 
ATOM   5437 C  CD  B LYS A 1 669  ? 39.115 90.881  -43.540 0.50 30.92 ? 669  LYS A CD  1 
ATOM   5438 C  CE  A LYS A 1 669  ? 40.171 90.641  -44.644 0.50 32.94 ? 669  LYS A CE  1 
ATOM   5439 N  NZ  A LYS A 1 669  ? 41.486 90.213  -44.025 0.50 32.15 ? 669  LYS A NZ  1 
ATOM   5440 N  NZ  B LYS A 1 669  ? 39.493 90.481  -45.990 0.50 33.62 ? 669  LYS A NZ  1 
ATOM   5441 N  N   . PHE A 1 670  ? 35.538 91.593  -40.321 1.00 13.84 ? 670  PHE A N   1 
ATOM   5442 C  CA  . PHE A 1 670  ? 34.346 91.797  -39.511 1.00 13.53 ? 670  PHE A CA  1 
ATOM   5443 C  C   . PHE A 1 670  ? 33.107 91.388  -40.292 1.00 15.25 ? 670  PHE A C   1 
ATOM   5444 O  O   . PHE A 1 670  ? 33.124 91.312  -41.516 1.00 15.75 ? 670  PHE A O   1 
ATOM   5445 C  CB  . PHE A 1 670  ? 34.192 93.296  -39.051 1.00 14.63 ? 670  PHE A CB  1 
ATOM   5446 C  CG  . PHE A 1 670  ? 35.355 93.795  -38.254 1.00 13.40 ? 670  PHE A CG  1 
ATOM   5447 C  CD1 . PHE A 1 670  ? 36.489 94.267  -38.931 1.00 17.11 ? 670  PHE A CD1 1 
ATOM   5448 C  CD2 . PHE A 1 670  ? 35.389 93.711  -36.868 1.00 17.23 ? 670  PHE A CD2 1 
ATOM   5449 C  CE1 . PHE A 1 670  ? 37.660 94.636  -38.227 1.00 17.10 ? 670  PHE A CE1 1 
ATOM   5450 C  CE2 . PHE A 1 670  ? 36.541 94.080  -36.155 1.00 18.09 ? 670  PHE A CE2 1 
ATOM   5451 C  CZ  . PHE A 1 670  ? 37.691 94.545  -36.858 1.00 17.24 ? 670  PHE A CZ  1 
ATOM   5452 N  N   . GLY A 1 671  ? 32.034 91.067  -39.586 1.00 14.64 ? 671  GLY A N   1 
ATOM   5453 C  CA  . GLY A 1 671  ? 30.785 90.710  -40.259 1.00 13.36 ? 671  GLY A CA  1 
ATOM   5454 C  C   . GLY A 1 671  ? 29.668 90.640  -39.252 1.00 14.30 ? 671  GLY A C   1 
ATOM   5455 O  O   . GLY A 1 671  ? 29.871 90.621  -38.039 1.00 13.34 ? 671  GLY A O   1 
ATOM   5456 N  N   . ASP A 1 672  ? 28.445 90.654  -39.758 1.00 15.01 ? 672  ASP A N   1 
ATOM   5457 C  CA  . ASP A 1 672  ? 27.311 90.503  -38.874 1.00 14.89 ? 672  ASP A CA  1 
ATOM   5458 C  C   . ASP A 1 672  ? 27.242 88.989  -38.432 1.00 14.29 ? 672  ASP A C   1 
ATOM   5459 O  O   . ASP A 1 672  ? 27.752 88.113  -39.142 1.00 15.45 ? 672  ASP A O   1 
ATOM   5460 C  CB  . ASP A 1 672  ? 25.994 90.761  -39.627 1.00 18.38 ? 672  ASP A CB  1 
ATOM   5461 C  CG  . ASP A 1 672  ? 25.675 92.245  -39.806 1.00 23.15 ? 672  ASP A CG  1 
ATOM   5462 O  OD1 . ASP A 1 672  ? 26.353 93.098  -39.223 1.00 26.35 ? 672  ASP A OD1 1 
ATOM   5463 O  OD2 . ASP A 1 672  ? 24.679 92.517  -40.543 1.00 29.51 ? 672  ASP A OD2 1 
ATOM   5464 N  N   . PRO A 1 673  ? 26.672 88.716  -37.230 1.00 14.59 ? 673  PRO A N   1 
ATOM   5465 C  CA  . PRO A 1 673  ? 26.558 87.304  -36.807 1.00 16.37 ? 673  PRO A CA  1 
ATOM   5466 C  C   . PRO A 1 673  ? 25.963 86.457  -37.928 1.00 18.00 ? 673  PRO A C   1 
ATOM   5467 O  O   . PRO A 1 673  ? 25.054 86.908  -38.640 1.00 18.16 ? 673  PRO A O   1 
ATOM   5468 C  CB  . PRO A 1 673  ? 25.603 87.387  -35.628 1.00 17.53 ? 673  PRO A CB  1 
ATOM   5469 C  CG  . PRO A 1 673  ? 26.017 88.680  -34.963 1.00 20.56 ? 673  PRO A CG  1 
ATOM   5470 C  CD  . PRO A 1 673  ? 26.095 89.611  -36.200 1.00 16.56 ? 673  PRO A CD  1 
ATOM   5471 N  N   . ARG A 1 674  ? 26.473 85.245  -38.077 1.00 16.36 ? 674  ARG A N   1 
ATOM   5472 C  CA  . ARG A 1 674  ? 25.993 84.307  -39.122 1.00 14.45 ? 674  ARG A CA  1 
ATOM   5473 C  C   . ARG A 1 674  ? 26.470 82.906  -38.764 1.00 15.07 ? 674  ARG A C   1 
ATOM   5474 O  O   . ARG A 1 674  ? 27.434 82.751  -37.993 1.00 15.36 ? 674  ARG A O   1 
ATOM   5475 C  CB  . ARG A 1 674  ? 26.570 84.661  -40.522 1.00 16.00 ? 674  ARG A CB  1 
ATOM   5476 C  CG  . ARG A 1 674  ? 28.094 84.604  -40.653 1.00 18.39 ? 674  ARG A CG  1 
ATOM   5477 C  CD  . ARG A 1 674  ? 28.480 84.744  -42.124 1.00 19.72 ? 674  ARG A CD  1 
ATOM   5478 N  NE  . ARG A 1 674  ? 29.854 84.431  -42.465 1.00 24.81 ? 674  ARG A NE  1 
ATOM   5479 C  CZ  . ARG A 1 674  ? 30.824 85.322  -42.619 1.00 25.68 ? 674  ARG A CZ  1 
ATOM   5480 N  NH1 . ARG A 1 674  ? 30.595 86.642  -42.438 1.00 26.63 ? 674  ARG A NH1 1 
ATOM   5481 N  NH2 . ARG A 1 674  ? 32.029 84.863  -43.018 1.00 27.34 ? 674  ARG A NH2 1 
ATOM   5482 N  N   . GLU A 1 675  ? 25.827 81.894  -39.311 1.00 16.25 ? 675  GLU A N   1 
ATOM   5483 C  CA  . GLU A 1 675  ? 26.336 80.542  -39.131 1.00 14.83 ? 675  GLU A CA  1 
ATOM   5484 C  C   . GLU A 1 675  ? 27.686 80.344  -39.862 1.00 16.72 ? 675  GLU A C   1 
ATOM   5485 O  O   . GLU A 1 675  ? 27.986 80.964  -40.920 1.00 19.12 ? 675  GLU A O   1 
ATOM   5486 C  CB  . GLU A 1 675  ? 25.311 79.532  -39.641 1.00 18.96 ? 675  GLU A CB  1 
ATOM   5487 C  CG  . GLU A 1 675  ? 24.053 79.668  -38.877 1.00 19.54 ? 675  GLU A CG  1 
ATOM   5488 C  CD  . GLU A 1 675  ? 23.176 78.431  -38.880 1.00 30.73 ? 675  GLU A CD  1 
ATOM   5489 O  OE1 . GLU A 1 675  ? 23.327 77.618  -39.830 1.00 33.56 ? 675  GLU A OE1 1 
ATOM   5490 O  OE2 . GLU A 1 675  ? 22.341 78.297  -37.923 1.00 34.55 ? 675  GLU A OE2 1 
ATOM   5491 N  N   . ILE A 1 676  ? 28.545 79.487  -39.311 1.00 15.97 ? 676  ILE A N   1 
ATOM   5492 C  CA  . ILE A 1 676  ? 29.785 79.220  -39.960 1.00 18.08 ? 676  ILE A CA  1 
ATOM   5493 C  C   . ILE A 1 676  ? 30.171 77.751  -39.810 1.00 15.47 ? 676  ILE A C   1 
ATOM   5494 O  O   . ILE A 1 676  ? 29.652 77.053  -38.908 1.00 16.94 ? 676  ILE A O   1 
ATOM   5495 C  CB  . ILE A 1 676  ? 30.908 80.073  -39.462 1.00 22.88 ? 676  ILE A CB  1 
ATOM   5496 C  CG1 . ILE A 1 676  ? 31.079 79.844  -38.006 1.00 19.18 ? 676  ILE A CG1 1 
ATOM   5497 C  CG2 . ILE A 1 676  ? 30.716 81.582  -39.795 1.00 27.90 ? 676  ILE A CG2 1 
ATOM   5498 C  CD1 . ILE A 1 676  ? 32.502 79.359  -37.805 1.00 27.76 ? 676  ILE A CD1 1 
ATOM   5499 N  N   A SER A 1 677  ? 31.049 77.306  -40.676 0.50 14.06 ? 677  SER A N   1 
ATOM   5500 N  N   B SER A 1 677  ? 31.049 77.306  -40.676 0.50 14.06 ? 677  SER A N   1 
ATOM   5501 C  CA  A SER A 1 677  ? 31.550 75.943  -40.714 0.50 17.75 ? 677  SER A CA  1 
ATOM   5502 C  CA  B SER A 1 677  ? 31.550 75.943  -40.714 0.50 17.64 ? 677  SER A CA  1 
ATOM   5503 C  C   A SER A 1 677  ? 33.061 75.978  -40.818 0.50 17.77 ? 677  SER A C   1 
ATOM   5504 C  C   B SER A 1 677  ? 33.061 75.978  -40.818 0.50 17.75 ? 677  SER A C   1 
ATOM   5505 O  O   A SER A 1 677  ? 33.639 76.820  -41.505 0.50 18.69 ? 677  SER A O   1 
ATOM   5506 O  O   B SER A 1 677  ? 33.639 76.820  -41.505 0.50 18.70 ? 677  SER A O   1 
ATOM   5507 C  CB  A SER A 1 677  ? 30.938 75.238  -41.954 0.50 19.96 ? 677  SER A CB  1 
ATOM   5508 C  CB  B SER A 1 677  ? 30.938 75.238  -41.954 0.50 19.67 ? 677  SER A CB  1 
ATOM   5509 O  OG  A SER A 1 677  ? 31.465 73.956  -42.147 0.50 23.51 ? 677  SER A OG  1 
ATOM   5510 O  OG  B SER A 1 677  ? 29.641 74.772  -41.711 0.50 23.81 ? 677  SER A OG  1 
ATOM   5511 N  N   . LEU A 1 678  ? 33.744 75.036  -40.156 1.00 14.99 ? 678  LEU A N   1 
ATOM   5512 C  CA  . LEU A 1 678  ? 35.191 74.981  -40.173 1.00 15.53 ? 678  LEU A CA  1 
ATOM   5513 C  C   . LEU A 1 678  ? 35.619 73.523  -40.267 1.00 14.77 ? 678  LEU A C   1 
ATOM   5514 O  O   . LEU A 1 678  ? 34.873 72.634  -39.747 1.00 15.78 ? 678  LEU A O   1 
ATOM   5515 C  CB  . LEU A 1 678  ? 35.772 75.536  -38.861 1.00 17.13 ? 678  LEU A CB  1 
ATOM   5516 C  CG  . LEU A 1 678  ? 35.731 77.032  -38.659 1.00 16.82 ? 678  LEU A CG  1 
ATOM   5517 C  CD1 . LEU A 1 678  ? 36.056 77.294  -37.197 1.00 19.18 ? 678  LEU A CD1 1 
ATOM   5518 C  CD2 . LEU A 1 678  ? 36.790 77.702  -39.517 1.00 24.71 ? 678  LEU A CD2 1 
ATOM   5519 N  N   . ARG A 1 679  ? 36.779 73.321  -40.851 1.00 14.00 ? 679  ARG A N   1 
ATOM   5520 C  CA  . ARG A 1 679  ? 37.397 72.011  -40.947 1.00 15.55 ? 679  ARG A CA  1 
ATOM   5521 C  C   . ARG A 1 679  ? 38.913 72.189  -40.886 1.00 17.85 ? 679  ARG A C   1 
ATOM   5522 O  O   . ARG A 1 679  ? 39.489 72.961  -41.681 1.00 19.10 ? 679  ARG A O   1 
ATOM   5523 C  CB  . ARG A 1 679  ? 37.023 71.330  -42.270 1.00 19.46 ? 679  ARG A CB  1 
ATOM   5524 C  CG  . ARG A 1 679  ? 37.506 69.868  -42.315 1.00 21.07 ? 679  ARG A CG  1 
ATOM   5525 C  CD  . ARG A 1 679  ? 37.321 69.249  -43.706 1.00 25.46 ? 679  ARG A CD  1 
ATOM   5526 N  NE  . ARG A 1 679  ? 37.618 67.831  -43.574 1.00 31.16 ? 679  ARG A NE  1 
ATOM   5527 C  CZ  . ARG A 1 679  ? 37.696 66.957  -44.569 1.00 36.05 ? 679  ARG A CZ  1 
ATOM   5528 N  NH1 . ARG A 1 679  ? 37.492 67.334  -45.832 1.00 38.55 ? 679  ARG A NH1 1 
ATOM   5529 N  NH2 . ARG A 1 679  ? 37.991 65.697  -44.277 1.00 37.18 ? 679  ARG A NH2 1 
ATOM   5530 N  N   . VAL A 1 680  ? 39.596 71.501  -39.958 1.00 14.97 ? 680  VAL A N   1 
ATOM   5531 C  CA  . VAL A 1 680  ? 41.044 71.521  -39.892 1.00 15.14 ? 680  VAL A CA  1 
ATOM   5532 C  C   . VAL A 1 680  ? 41.579 70.169  -40.359 1.00 18.30 ? 680  VAL A C   1 
ATOM   5533 O  O   . VAL A 1 680  ? 41.035 69.129  -39.968 1.00 17.09 ? 680  VAL A O   1 
ATOM   5534 C  CB  . VAL A 1 680  ? 41.564 71.789  -38.461 1.00 14.49 ? 680  VAL A CB  1 
ATOM   5535 C  CG1 . VAL A 1 680  ? 43.058 71.608  -38.386 1.00 16.79 ? 680  VAL A CG1 1 
ATOM   5536 C  CG2 . VAL A 1 680  ? 41.112 73.228  -38.047 1.00 13.74 ? 680  VAL A CG2 1 
ATOM   5537 N  N   . GLY A 1 681  ? 42.602 70.202  -41.219 1.00 18.38 ? 681  GLY A N   1 
ATOM   5538 C  CA  . GLY A 1 681  ? 43.160 68.947  -41.752 1.00 24.22 ? 681  GLY A CA  1 
ATOM   5539 C  C   . GLY A 1 681  ? 42.089 68.080  -42.441 1.00 24.00 ? 681  GLY A C   1 
ATOM   5540 O  O   . GLY A 1 681  ? 41.216 68.583  -43.169 1.00 25.23 ? 681  GLY A O   1 
ATOM   5541 N  N   . ASN A 1 682  ? 42.150 66.771  -42.174 1.00 30.36 ? 682  ASN A N   1 
ATOM   5542 C  CA  . ASN A 1 682  ? 41.171 65.839  -42.755 1.00 32.11 ? 682  ASN A CA  1 
ATOM   5543 C  C   . ASN A 1 682  ? 40.192 65.495  -41.680 1.00 33.90 ? 682  ASN A C   1 
ATOM   5544 O  O   . ASN A 1 682  ? 39.442 64.529  -41.801 1.00 37.42 ? 682  ASN A O   1 
ATOM   5545 C  CB  . ASN A 1 682  ? 41.827 64.537  -43.196 1.00 35.75 ? 682  ASN A CB  1 
ATOM   5546 C  CG  . ASN A 1 682  ? 42.898 64.756  -44.202 1.00 39.09 ? 682  ASN A CG  1 
ATOM   5547 O  OD1 . ASN A 1 682  ? 42.680 65.415  -45.229 1.00 45.54 ? 682  ASN A OD1 1 
ATOM   5548 N  ND2 . ASN A 1 682  ? 44.079 64.213  -43.928 1.00 43.79 ? 682  ASN A ND2 1 
ATOM   5549 N  N   . GLY A 1 683  ? 40.188 66.298  -40.628 1.00 30.83 ? 683  GLY A N   1 
ATOM   5550 C  CA  . GLY A 1 683  ? 39.342 66.000  -39.496 1.00 28.04 ? 683  GLY A CA  1 
ATOM   5551 C  C   . GLY A 1 683  ? 37.885 66.275  -39.730 1.00 23.81 ? 683  GLY A C   1 
ATOM   5552 O  O   . GLY A 1 683  ? 37.464 66.495  -40.868 1.00 23.76 ? 683  GLY A O   1 
ATOM   5553 N  N   . PRO A 1 684  ? 37.097 66.322  -38.663 1.00 18.52 ? 684  PRO A N   1 
ATOM   5554 C  CA  . PRO A 1 684  ? 35.659 66.578  -38.827 1.00 18.09 ? 684  PRO A CA  1 
ATOM   5555 C  C   . PRO A 1 684  ? 35.338 68.018  -39.258 1.00 15.62 ? 684  PRO A C   1 
ATOM   5556 O  O   . PRO A 1 684  ? 36.154 68.899  -39.097 1.00 15.71 ? 684  PRO A O   1 
ATOM   5557 C  CB  . PRO A 1 684  ? 35.105 66.267  -37.437 1.00 18.74 ? 684  PRO A CB  1 
ATOM   5558 C  CG  . PRO A 1 684  ? 36.268 66.703  -36.509 1.00 20.83 ? 684  PRO A CG  1 
ATOM   5559 C  CD  . PRO A 1 684  ? 37.454 66.125  -37.238 1.00 20.32 ? 684  PRO A CD  1 
ATOM   5560 N  N   . THR A 1 685  ? 34.152 68.211  -39.818 1.00 15.79 ? 685  THR A N   1 
ATOM   5561 C  CA  . THR A 1 685  ? 33.694 69.563  -40.206 1.00 15.79 ? 685  THR A CA  1 
ATOM   5562 C  C   . THR A 1 685  ? 32.672 69.908  -39.157 1.00 15.30 ? 685  THR A C   1 
ATOM   5563 O  O   . THR A 1 685  ? 31.741 69.161  -38.942 1.00 16.53 ? 685  THR A O   1 
ATOM   5564 C  CB  . THR A 1 685  ? 33.059 69.573  -41.609 1.00 16.90 ? 685  THR A CB  1 
ATOM   5565 O  OG1 . THR A 1 685  ? 34.074 69.250  -42.541 1.00 19.75 ? 685  THR A OG1 1 
ATOM   5566 C  CG2 . THR A 1 685  ? 32.459 70.961  -41.923 1.00 19.36 ? 685  THR A CG2 1 
ATOM   5567 N  N   . LEU A 1 686  ? 32.839 71.052  -38.486 1.00 12.09 ? 686  LEU A N   1 
ATOM   5568 C  CA  . LEU A 1 686  ? 31.943 71.466  -37.434 1.00 13.79 ? 686  LEU A CA  1 
ATOM   5569 C  C   . LEU A 1 686  ? 31.114 72.686  -37.884 1.00 11.51 ? 686  LEU A C   1 
ATOM   5570 O  O   . LEU A 1 686  ? 31.736 73.640  -38.496 1.00 13.44 ? 686  LEU A O   1 
ATOM   5571 C  CB  . LEU A 1 686  ? 32.746 71.870  -36.182 1.00 11.96 ? 686  LEU A CB  1 
ATOM   5572 C  CG  . LEU A 1 686  ? 33.682 70.819  -35.558 1.00 18.63 ? 686  LEU A CG  1 
ATOM   5573 C  CD1 . LEU A 1 686  ? 33.945 71.212  -34.090 1.00 16.99 ? 686  LEU A CD1 1 
ATOM   5574 C  CD2 . LEU A 1 686  ? 33.210 69.439  -35.649 1.00 18.43 ? 686  LEU A CD2 1 
ATOM   5575 N  N   . ALA A 1 687  ? 29.825 72.703  -37.618 1.00 12.47 ? 687  ALA A N   1 
ATOM   5576 C  CA  . ALA A 1 687  ? 29.013 73.859  -37.982 1.00 13.59 ? 687  ALA A CA  1 
ATOM   5577 C  C   . ALA A 1 687  ? 28.576 74.532  -36.692 1.00 14.77 ? 687  ALA A C   1 
ATOM   5578 O  O   . ALA A 1 687  ? 28.277 73.836  -35.688 1.00 13.86 ? 687  ALA A O   1 
ATOM   5579 C  CB  . ALA A 1 687  ? 27.758 73.370  -38.799 1.00 12.98 ? 687  ALA A CB  1 
ATOM   5580 N  N   . PHE A 1 688  ? 28.497 75.874  -36.688 1.00 13.08 ? 688  PHE A N   1 
ATOM   5581 C  CA  . PHE A 1 688  ? 28.139 76.639  -35.545 1.00 11.19 ? 688  PHE A CA  1 
ATOM   5582 C  C   . PHE A 1 688  ? 26.961 77.545  -35.806 1.00 12.03 ? 688  PHE A C   1 
ATOM   5583 O  O   . PHE A 1 688  ? 26.831 78.050  -36.954 1.00 14.85 ? 688  PHE A O   1 
ATOM   5584 C  CB  . PHE A 1 688  ? 29.322 77.521  -35.089 1.00 13.14 ? 688  PHE A CB  1 
ATOM   5585 C  CG  . PHE A 1 688  ? 30.565 76.720  -34.753 1.00 10.80 ? 688  PHE A CG  1 
ATOM   5586 C  CD1 . PHE A 1 688  ? 31.401 76.246  -35.732 1.00 11.70 ? 688  PHE A CD1 1 
ATOM   5587 C  CD2 . PHE A 1 688  ? 30.847 76.422  -33.419 1.00 10.97 ? 688  PHE A CD2 1 
ATOM   5588 C  CE1 . PHE A 1 688  ? 32.526 75.474  -35.430 1.00 11.25 ? 688  PHE A CE1 1 
ATOM   5589 C  CE2 . PHE A 1 688  ? 31.966 75.658  -33.126 1.00 10.98 ? 688  PHE A CE2 1 
ATOM   5590 C  CZ  . PHE A 1 688  ? 32.799 75.190  -34.079 1.00 11.37 ? 688  PHE A CZ  1 
ATOM   5591 N  N   . SER A 1 689  ? 26.166 77.817  -34.816 1.00 12.77 ? 689  SER A N   1 
ATOM   5592 C  CA  . SER A 1 689  ? 25.039 78.748  -34.924 1.00 13.55 ? 689  SER A CA  1 
ATOM   5593 C  C   . SER A 1 689  ? 25.613 80.185  -34.954 1.00 14.90 ? 689  SER A C   1 
ATOM   5594 O  O   . SER A 1 689  ? 26.804 80.438  -34.704 1.00 13.82 ? 689  SER A O   1 
ATOM   5595 C  CB  . SER A 1 689  ? 24.137 78.623  -33.705 1.00 14.20 ? 689  SER A CB  1 
ATOM   5596 O  OG  . SER A 1 689  ? 24.767 79.176  -32.556 1.00 16.15 ? 689  SER A OG  1 
ATOM   5597 N  N   . GLU A 1 690  ? 24.733 81.141  -35.239 1.00 14.16 ? 690  GLU A N   1 
ATOM   5598 C  CA  . GLU A 1 690  ? 25.165 82.538  -35.229 1.00 13.36 ? 690  GLU A CA  1 
ATOM   5599 C  C   . GLU A 1 690  ? 25.540 83.001  -33.829 1.00 16.06 ? 690  GLU A C   1 
ATOM   5600 O  O   . GLU A 1 690  ? 26.101 84.090  -33.652 1.00 14.02 ? 690  GLU A O   1 
ATOM   5601 C  CB  . GLU A 1 690  ? 24.079 83.435  -35.835 1.00 18.25 ? 690  GLU A CB  1 
ATOM   5602 C  CG  . GLU A 1 690  ? 22.945 83.753  -34.967 1.00 21.13 ? 690  GLU A CG  1 
ATOM   5603 C  CD  . GLU A 1 690  ? 22.115 84.865  -35.621 1.00 29.19 ? 690  GLU A CD  1 
ATOM   5604 O  OE1 . GLU A 1 690  ? 21.576 84.568  -36.704 1.00 31.89 ? 690  GLU A OE1 1 
ATOM   5605 O  OE2 . GLU A 1 690  ? 22.019 86.013  -35.081 1.00 33.76 ? 690  GLU A OE2 1 
ATOM   5606 N  N   . GLN A 1 691  ? 25.214 82.190  -32.812 1.00 15.40 ? 691  GLN A N   1 
ATOM   5607 C  CA  . GLN A 1 691  ? 25.627 82.523  -31.437 1.00 14.94 ? 691  GLN A CA  1 
ATOM   5608 C  C   . GLN A 1 691  ? 26.978 81.867  -31.080 1.00 10.97 ? 691  GLN A C   1 
ATOM   5609 O  O   . GLN A 1 691  ? 27.397 81.962  -29.905 1.00 16.40 ? 691  GLN A O   1 
ATOM   5610 C  CB  . GLN A 1 691  ? 24.586 82.144  -30.375 1.00 17.31 ? 691  GLN A CB  1 
ATOM   5611 C  CG  . GLN A 1 691  ? 23.331 82.965  -30.466 1.00 23.33 ? 691  GLN A CG  1 
ATOM   5612 C  CD  . GLN A 1 691  ? 22.230 82.045  -30.545 1.00 34.15 ? 691  GLN A CD  1 
ATOM   5613 O  OE1 . GLN A 1 691  ? 21.747 81.543  -29.519 1.00 31.18 ? 691  GLN A OE1 1 
ATOM   5614 N  NE2 . GLN A 1 691  ? 21.834 81.725  -31.774 1.00 34.85 ? 691  GLN A NE2 1 
ATOM   5615 N  N   . GLY A 1 692  ? 27.656 81.266  -32.028 1.00 11.43 ? 692  GLY A N   1 
ATOM   5616 C  CA  . GLY A 1 692  ? 28.984 80.701  -31.759 1.00 12.73 ? 692  GLY A CA  1 
ATOM   5617 C  C   . GLY A 1 692  ? 28.967 79.350  -31.082 1.00 12.21 ? 692  GLY A C   1 
ATOM   5618 O  O   . GLY A 1 692  ? 30.009 78.931  -30.585 1.00 13.99 ? 692  GLY A O   1 
ATOM   5619 N  N   . LEU A 1 693  ? 27.823 78.661  -31.099 1.00 12.36 ? 693  LEU A N   1 
ATOM   5620 C  CA  . LEU A 1 693  ? 27.676 77.336  -30.432 1.00 12.11 ? 693  LEU A CA  1 
ATOM   5621 C  C   . LEU A 1 693  ? 27.583 76.250  -31.414 1.00 12.30 ? 693  LEU A C   1 
ATOM   5622 O  O   . LEU A 1 693  ? 26.868 76.375  -32.454 1.00 12.89 ? 693  LEU A O   1 
ATOM   5623 C  CB  . LEU A 1 693  ? 26.437 77.346  -29.537 1.00 13.90 ? 693  LEU A CB  1 
ATOM   5624 C  CG  . LEU A 1 693  ? 26.562 78.324  -28.368 1.00 16.40 ? 693  LEU A CG  1 
ATOM   5625 C  CD1 . LEU A 1 693  ? 25.136 78.662  -27.940 1.00 20.87 ? 693  LEU A CD1 1 
ATOM   5626 C  CD2 . LEU A 1 693  ? 27.382 77.741  -27.232 1.00 19.30 ? 693  LEU A CD2 1 
ATOM   5627 N  N   . LEU A 1 694  ? 28.253 75.125  -31.151 1.00 11.96 ? 694  LEU A N   1 
ATOM   5628 C  CA  . LEU A 1 694  ? 28.205 73.992  -32.048 1.00 11.46 ? 694  LEU A CA  1 
ATOM   5629 C  C   . LEU A 1 694  ? 26.756 73.593  -32.333 1.00 11.08 ? 694  LEU A C   1 
ATOM   5630 O  O   . LEU A 1 694  ? 25.896 73.598  -31.441 1.00 12.05 ? 694  LEU A O   1 
ATOM   5631 C  CB  . LEU A 1 694  ? 28.935 72.792  -31.365 1.00 12.59 ? 694  LEU A CB  1 
ATOM   5632 C  CG  . LEU A 1 694  ? 29.108 71.557  -32.231 1.00 12.55 ? 694  LEU A CG  1 
ATOM   5633 C  CD1 . LEU A 1 694  ? 30.032 71.810  -33.344 1.00 13.45 ? 694  LEU A CD1 1 
ATOM   5634 C  CD2 . LEU A 1 694  ? 29.607 70.371  -31.356 1.00 14.08 ? 694  LEU A CD2 1 
ATOM   5635 N  N   . LYS A 1 695  ? 26.510 73.237  -33.603 1.00 11.95 ? 695  LYS A N   1 
ATOM   5636 C  CA  . LYS A 1 695  ? 25.186 72.726  -33.982 1.00 13.16 ? 695  LYS A CA  1 
ATOM   5637 C  C   . LYS A 1 695  ? 25.323 71.392  -34.692 1.00 12.19 ? 695  LYS A C   1 
ATOM   5638 O  O   . LYS A 1 695  ? 24.337 70.618  -34.640 1.00 14.85 ? 695  LYS A O   1 
ATOM   5639 C  CB  . LYS A 1 695  ? 24.354 73.727  -34.845 1.00 17.36 ? 695  LYS A CB  1 
ATOM   5640 C  CG  . LYS A 1 695  ? 24.958 74.167  -36.130 1.00 19.91 ? 695  LYS A CG  1 
ATOM   5641 C  CD  . LYS A 1 695  ? 23.972 75.166  -36.831 1.00 24.04 ? 695  LYS A CD  1 
ATOM   5642 C  CE  . LYS A 1 695  ? 23.003 74.431  -37.756 1.00 33.30 ? 695  LYS A CE  1 
ATOM   5643 N  NZ  . LYS A 1 695  ? 21.978 75.373  -38.384 1.00 34.80 ? 695  LYS A NZ  1 
ATOM   5644 N  N   . SER A 1 696  ? 26.435 71.053  -35.308 1.00 12.60 ? 696  SER A N   1 
ATOM   5645 C  CA  . SER A 1 696  ? 26.571 69.742  -35.957 1.00 13.81 ? 696  SER A CA  1 
ATOM   5646 C  C   . SER A 1 696  ? 28.019 69.358  -36.159 1.00 13.78 ? 696  SER A C   1 
ATOM   5647 O  O   . SER A 1 696  ? 28.919 70.230  -36.224 1.00 13.52 ? 696  SER A O   1 
ATOM   5648 C  CB  . SER A 1 696  ? 25.770 69.708  -37.309 1.00 15.45 ? 696  SER A CB  1 
ATOM   5649 O  OG  . SER A 1 696  ? 26.400 70.472  -38.330 1.00 17.61 ? 696  SER A OG  1 
ATOM   5650 N  N   . ILE A 1 697  ? 28.290 68.046  -36.346 1.00 13.84 ? 697  ILE A N   1 
ATOM   5651 C  CA  . ILE A 1 697  ? 29.575 67.469  -36.600 1.00 13.27 ? 697  ILE A CA  1 
ATOM   5652 C  C   . ILE A 1 697  ? 29.447 66.526  -37.791 1.00 15.98 ? 697  ILE A C   1 
ATOM   5653 O  O   . ILE A 1 697  ? 28.582 65.624  -37.770 1.00 17.29 ? 697  ILE A O   1 
ATOM   5654 C  CB  . ILE A 1 697  ? 30.119 66.634  -35.382 1.00 14.21 ? 697  ILE A CB  1 
ATOM   5655 C  CG1 . ILE A 1 697  ? 30.253 67.574  -34.172 1.00 13.24 ? 697  ILE A CG1 1 
ATOM   5656 C  CG2 . ILE A 1 697  ? 31.477 66.038  -35.697 1.00 14.47 ? 697  ILE A CG2 1 
ATOM   5657 C  CD1 . ILE A 1 697  ? 30.759 66.811  -32.880 1.00 13.00 ? 697  ILE A CD1 1 
ATOM   5658 N  N   . GLN A 1 698  ? 30.307 66.687  -38.775 1.00 14.93 ? 698  GLN A N   1 
ATOM   5659 C  CA  . GLN A 1 698  ? 30.291 65.807  -39.937 1.00 16.41 ? 698  GLN A CA  1 
ATOM   5660 C  C   . GLN A 1 698  ? 31.613 65.105  -39.889 1.00 15.40 ? 698  GLN A C   1 
ATOM   5661 O  O   . GLN A 1 698  ? 32.666 65.708  -40.037 1.00 16.31 ? 698  GLN A O   1 
ATOM   5662 C  CB  . GLN A 1 698  ? 30.162 66.654  -41.224 1.00 17.72 ? 698  GLN A CB  1 
ATOM   5663 C  CG  . GLN A 1 698  ? 30.320 65.685  -42.435 1.00 22.92 ? 698  GLN A CG  1 
ATOM   5664 C  CD  . GLN A 1 698  ? 30.309 66.411  -43.744 1.00 24.05 ? 698  GLN A CD  1 
ATOM   5665 O  OE1 . GLN A 1 698  ? 29.413 66.182  -44.589 1.00 29.61 ? 698  GLN A OE1 1 
ATOM   5666 N  NE2 . GLN A 1 698  ? 31.272 67.288  -43.933 1.00 24.69 ? 698  GLN A NE2 1 
ATOM   5667 N  N   . LEU A 1 699  ? 31.604 63.784  -39.692 1.00 17.27 ? 699  LEU A N   1 
ATOM   5668 C  CA  . LEU A 1 699  ? 32.882 63.108  -39.529 1.00 20.18 ? 699  LEU A CA  1 
ATOM   5669 C  C   . LEU A 1 699  ? 33.838 63.036  -40.733 1.00 24.98 ? 699  LEU A C   1 
ATOM   5670 O  O   . LEU A 1 699  ? 35.034 63.234  -40.576 1.00 25.94 ? 699  LEU A O   1 
ATOM   5671 C  CB  . LEU A 1 699  ? 32.649 61.690  -38.924 1.00 23.46 ? 699  LEU A CB  1 
ATOM   5672 C  CG  . LEU A 1 699  ? 32.028 61.647  -37.513 1.00 20.78 ? 699  LEU A CG  1 
ATOM   5673 C  CD1 . LEU A 1 699  ? 31.888 60.201  -37.072 1.00 23.31 ? 699  LEU A CD1 1 
ATOM   5674 C  CD2 . LEU A 1 699  ? 32.924 62.428  -36.532 1.00 18.91 ? 699  LEU A CD2 1 
ATOM   5675 N  N   . THR A 1 700  ? 33.292 62.821  -41.927 1.00 28.09 ? 700  THR A N   1 
ATOM   5676 C  CA  . THR A 1 700  ? 34.121 62.736  -43.129 1.00 32.96 ? 700  THR A CA  1 
ATOM   5677 C  C   . THR A 1 700  ? 33.417 63.498  -44.251 1.00 32.72 ? 700  THR A C   1 
ATOM   5678 O  O   . THR A 1 700  ? 32.272 63.896  -44.095 1.00 31.98 ? 700  THR A O   1 
ATOM   5679 C  CB  . THR A 1 700  ? 34.336 61.253  -43.554 1.00 32.92 ? 700  THR A CB  1 
ATOM   5680 O  OG1 . THR A 1 700  ? 33.060 60.627  -43.732 1.00 35.02 ? 700  THR A OG1 1 
ATOM   5681 C  CG2 . THR A 1 700  ? 35.139 60.495  -42.488 1.00 34.87 ? 700  THR A CG2 1 
ATOM   5682 N  N   . GLN A 1 701  ? 34.122 63.726  -45.363 1.00 37.70 ? 701  GLN A N   1 
ATOM   5683 C  CA  . GLN A 1 701  ? 33.564 64.451  -46.517 1.00 40.51 ? 701  GLN A CA  1 
ATOM   5684 C  C   . GLN A 1 701  ? 32.198 63.919  -46.929 1.00 41.46 ? 701  GLN A C   1 
ATOM   5685 O  O   . GLN A 1 701  ? 31.245 64.682  -47.128 1.00 43.20 ? 701  GLN A O   1 
ATOM   5686 C  CB  . GLN A 1 701  ? 34.499 64.339  -47.734 1.00 42.70 ? 701  GLN A CB  1 
ATOM   5687 C  CG  . GLN A 1 701  ? 35.672 65.301  -47.770 1.00 44.54 ? 701  GLN A CG  1 
ATOM   5688 C  CD  . GLN A 1 701  ? 35.247 66.749  -48.029 1.00 46.69 ? 701  GLN A CD  1 
ATOM   5689 O  OE1 . GLN A 1 701  ? 36.068 67.599  -48.423 1.00 45.44 ? 701  GLN A OE1 1 
ATOM   5690 N  NE2 . GLN A 1 701  ? 33.957 67.043  -47.794 1.00 47.37 ? 701  GLN A NE2 1 
ATOM   5691 N  N   . ASP A 1 702  ? 32.117 62.600  -47.039 1.00 42.32 ? 702  ASP A N   1 
ATOM   5692 C  CA  . ASP A 1 702  ? 30.907 61.911  -47.458 1.00 44.78 ? 702  ASP A CA  1 
ATOM   5693 C  C   . ASP A 1 702  ? 29.794 61.811  -46.417 1.00 44.36 ? 702  ASP A C   1 
ATOM   5694 O  O   . ASP A 1 702  ? 28.595 61.978  -46.737 1.00 43.79 ? 702  ASP A O   1 
ATOM   5695 C  CB  . ASP A 1 702  ? 31.285 60.500  -47.947 1.00 47.39 ? 702  ASP A CB  1 
ATOM   5696 C  CG  . ASP A 1 702  ? 32.291 60.526  -49.113 1.00 51.25 ? 702  ASP A CG  1 
ATOM   5697 O  OD1 . ASP A 1 702  ? 32.859 59.444  -49.436 1.00 53.70 ? 702  ASP A OD1 1 
ATOM   5698 O  OD2 . ASP A 1 702  ? 32.508 61.621  -49.711 1.00 51.02 ? 702  ASP A OD2 1 
ATOM   5699 N  N   . SER A 1 703  ? 30.188 61.580  -45.164 1.00 41.29 ? 703  SER A N   1 
ATOM   5700 C  CA  . SER A 1 703  ? 29.227 61.403  -44.084 1.00 36.67 ? 703  SER A CA  1 
ATOM   5701 C  C   . SER A 1 703  ? 28.276 62.568  -43.828 1.00 33.76 ? 703  SER A C   1 
ATOM   5702 O  O   . SER A 1 703  ? 28.490 63.679  -44.319 1.00 35.23 ? 703  SER A O   1 
ATOM   5703 C  CB  . SER A 1 703  ? 29.976 61.049  -42.796 1.00 37.59 ? 703  SER A CB  1 
ATOM   5704 O  OG  . SER A 1 703  ? 30.674 62.173  -42.271 1.00 33.47 ? 703  SER A OG  1 
ATOM   5705 N  N   . PRO A 1 704  ? 27.191 62.316  -43.067 1.00 33.48 ? 704  PRO A N   1 
ATOM   5706 C  CA  . PRO A 1 704  ? 26.140 63.256  -42.671 1.00 30.96 ? 704  PRO A CA  1 
ATOM   5707 C  C   . PRO A 1 704  ? 26.467 64.300  -41.564 1.00 30.01 ? 704  PRO A C   1 
ATOM   5708 O  O   . PRO A 1 704  ? 27.345 64.084  -40.716 1.00 28.39 ? 704  PRO A O   1 
ATOM   5709 C  CB  . PRO A 1 704  ? 24.979 62.353  -42.267 1.00 35.34 ? 704  PRO A CB  1 
ATOM   5710 C  CG  . PRO A 1 704  ? 25.581 61.080  -41.936 1.00 31.73 ? 704  PRO A CG  1 
ATOM   5711 C  CD  . PRO A 1 704  ? 26.844 60.925  -42.705 1.00 34.01 ? 704  PRO A CD  1 
ATOM   5712 N  N   . HIS A 1 705  ? 25.776 65.442  -41.609 1.00 26.58 ? 705  HIS A N   1 
ATOM   5713 C  CA  . HIS A 1 705  ? 26.005 66.468  -40.568 1.00 24.71 ? 705  HIS A CA  1 
ATOM   5714 C  C   . HIS A 1 705  ? 25.154 66.066  -39.356 1.00 23.88 ? 705  HIS A C   1 
ATOM   5715 O  O   . HIS A 1 705  ? 23.986 66.374  -39.264 1.00 23.63 ? 705  HIS A O   1 
ATOM   5716 C  CB  . HIS A 1 705  ? 25.596 67.866  -41.088 1.00 28.14 ? 705  HIS A CB  1 
ATOM   5717 C  CG  . HIS A 1 705  ? 26.456 68.352  -42.210 1.00 31.24 ? 705  HIS A CG  1 
ATOM   5718 N  ND1 . HIS A 1 705  ? 27.636 69.032  -42.001 1.00 29.58 ? 705  HIS A ND1 1 
ATOM   5719 C  CD2 . HIS A 1 705  ? 26.395 68.116  -43.545 1.00 33.08 ? 705  HIS A CD2 1 
ATOM   5720 C  CE1 . HIS A 1 705  ? 28.277 69.178  -43.148 1.00 34.17 ? 705  HIS A CE1 1 
ATOM   5721 N  NE2 . HIS A 1 705  ? 27.544 68.630  -44.105 1.00 35.30 ? 705  HIS A NE2 1 
ATOM   5722 N  N   . VAL A 1 706  ? 25.776 65.401  -38.373 1.00 19.73 ? 706  VAL A N   1 
ATOM   5723 C  CA  . VAL A 1 706  ? 25.039 64.953  -37.194 1.00 18.34 ? 706  VAL A CA  1 
ATOM   5724 C  C   . VAL A 1 706  ? 24.681 66.054  -36.210 1.00 17.46 ? 706  VAL A C   1 
ATOM   5725 O  O   . VAL A 1 706  ? 25.587 66.760  -35.776 1.00 16.50 ? 706  VAL A O   1 
ATOM   5726 C  CB  . VAL A 1 706  ? 25.901 63.872  -36.437 1.00 18.12 ? 706  VAL A CB  1 
ATOM   5727 C  CG1 . VAL A 1 706  ? 25.130 63.392  -35.231 1.00 16.62 ? 706  VAL A CG1 1 
ATOM   5728 C  CG2 . VAL A 1 706  ? 26.308 62.745  -37.414 1.00 18.13 ? 706  VAL A CG2 1 
ATOM   5729 N  N   . PRO A 1 707  ? 23.421 66.239  -35.819 1.00 16.25 ? 707  PRO A N   1 
ATOM   5730 C  CA  . PRO A 1 707  ? 23.075 67.291  -34.869 1.00 18.94 ? 707  PRO A CA  1 
ATOM   5731 C  C   . PRO A 1 707  ? 23.727 67.038  -33.512 1.00 17.97 ? 707  PRO A C   1 
ATOM   5732 O  O   . PRO A 1 707  ? 23.577 65.970  -32.903 1.00 17.84 ? 707  PRO A O   1 
ATOM   5733 C  CB  . PRO A 1 707  ? 21.560 67.215  -34.762 1.00 19.16 ? 707  PRO A CB  1 
ATOM   5734 C  CG  . PRO A 1 707  ? 21.132 66.613  -36.111 1.00 22.66 ? 707  PRO A CG  1 
ATOM   5735 C  CD  . PRO A 1 707  ? 22.188 65.571  -36.345 1.00 17.42 ? 707  PRO A CD  1 
ATOM   5736 N  N   . VAL A 1 708  ? 24.480 68.045  -33.055 1.00 16.29 ? 708  VAL A N   1 
ATOM   5737 C  CA  . VAL A 1 708  ? 25.158 67.999  -31.738 1.00 14.16 ? 708  VAL A CA  1 
ATOM   5738 C  C   . VAL A 1 708  ? 25.127 69.484  -31.327 1.00 12.56 ? 708  VAL A C   1 
ATOM   5739 O  O   . VAL A 1 708  ? 25.887 70.318  -31.937 1.00 13.35 ? 708  VAL A O   1 
ATOM   5740 C  CB  . VAL A 1 708  ? 26.597 67.469  -31.878 1.00 13.61 ? 708  VAL A CB  1 
ATOM   5741 C  CG1 . VAL A 1 708  ? 27.309 67.514  -30.445 1.00 14.28 ? 708  VAL A CG1 1 
ATOM   5742 C  CG2 . VAL A 1 708  ? 26.607 66.012  -32.430 1.00 18.52 ? 708  VAL A CG2 1 
ATOM   5743 N  N   A HIS A 1 709  ? 24.280 69.842  -30.407 0.50 12.28 ? 709  HIS A N   1 
ATOM   5744 N  N   B HIS A 1 709  ? 24.280 69.842  -30.407 0.50 12.92 ? 709  HIS A N   1 
ATOM   5745 C  CA  A HIS A 1 709  ? 24.137 71.249  -30.060 0.50 13.38 ? 709  HIS A CA  1 
ATOM   5746 C  CA  B HIS A 1 709  ? 24.137 71.249  -30.060 0.50 14.38 ? 709  HIS A CA  1 
ATOM   5747 C  C   A HIS A 1 709  ? 24.546 71.562  -28.629 0.50 13.78 ? 709  HIS A C   1 
ATOM   5748 C  C   B HIS A 1 709  ? 24.546 71.562  -28.629 0.50 14.39 ? 709  HIS A C   1 
ATOM   5749 O  O   A HIS A 1 709  ? 24.070 70.912  -27.684 0.50 14.39 ? 709  HIS A O   1 
ATOM   5750 O  O   B HIS A 1 709  ? 24.077 70.906  -27.685 0.50 14.85 ? 709  HIS A O   1 
ATOM   5751 C  CB  A HIS A 1 709  ? 22.671 71.655  -30.218 0.50 16.17 ? 709  HIS A CB  1 
ATOM   5752 C  CB  B HIS A 1 709  ? 22.671 71.655  -30.218 0.50 17.70 ? 709  HIS A CB  1 
ATOM   5753 C  CG  A HIS A 1 709  ? 22.147 71.593  -31.620 0.50 19.54 ? 709  HIS A CG  1 
ATOM   5754 C  CG  B HIS A 1 709  ? 22.414 73.129  -30.152 0.50 22.93 ? 709  HIS A CG  1 
ATOM   5755 N  ND1 A HIS A 1 709  ? 21.709 72.710  -32.299 0.50 23.06 ? 709  HIS A ND1 1 
ATOM   5756 N  ND1 B HIS A 1 709  ? 21.344 73.667  -29.470 0.50 25.56 ? 709  HIS A ND1 1 
ATOM   5757 C  CD2 A HIS A 1 709  ? 22.029 70.555  -32.484 0.50 22.14 ? 709  HIS A CD2 1 
ATOM   5758 C  CD2 B HIS A 1 709  ? 23.112 74.180  -30.650 0.50 24.71 ? 709  HIS A CD2 1 
ATOM   5759 C  CE1 A HIS A 1 709  ? 21.349 72.365  -33.525 0.50 24.06 ? 709  HIS A CE1 1 
ATOM   5760 C  CE1 B HIS A 1 709  ? 21.395 74.988  -29.544 0.50 27.53 ? 709  HIS A CE1 1 
ATOM   5761 N  NE2 A HIS A 1 709  ? 21.543 71.062  -33.663 0.50 14.01 ? 709  HIS A NE2 1 
ATOM   5762 N  NE2 B HIS A 1 709  ? 22.466 75.322  -30.248 0.50 27.26 ? 709  HIS A NE2 1 
ATOM   5763 N  N   . PHE A 1 710  ? 25.431 72.531  -28.456 1.00 12.17 ? 710  PHE A N   1 
ATOM   5764 C  CA  . PHE A 1 710  ? 25.783 72.995  -27.131 1.00 11.62 ? 710  PHE A CA  1 
ATOM   5765 C  C   . PHE A 1 710  ? 24.783 74.077  -26.692 1.00 13.53 ? 710  PHE A C   1 
ATOM   5766 O  O   . PHE A 1 710  ? 24.388 74.960  -27.535 1.00 13.38 ? 710  PHE A O   1 
ATOM   5767 C  CB  . PHE A 1 710  ? 27.194 73.616  -27.071 1.00 12.80 ? 710  PHE A CB  1 
ATOM   5768 C  CG  . PHE A 1 710  ? 28.303 72.648  -26.666 1.00 12.90 ? 710  PHE A CG  1 
ATOM   5769 C  CD1 . PHE A 1 710  ? 29.408 72.463  -27.484 1.00 14.16 ? 710  PHE A CD1 1 
ATOM   5770 C  CD2 . PHE A 1 710  ? 28.250 71.945  -25.457 1.00 14.15 ? 710  PHE A CD2 1 
ATOM   5771 C  CE1 . PHE A 1 710  ? 30.470 71.562  -27.066 1.00 14.00 ? 710  PHE A CE1 1 
ATOM   5772 C  CE2 . PHE A 1 710  ? 29.263 71.070  -25.061 1.00 14.66 ? 710  PHE A CE2 1 
ATOM   5773 C  CZ  . PHE A 1 710  ? 30.348 70.892  -25.850 1.00 14.03 ? 710  PHE A CZ  1 
ATOM   5774 N  N   . LYS A 1 711  ? 24.376 74.067  -25.444 1.00 10.92 ? 711  LYS A N   1 
ATOM   5775 C  CA  . LYS A 1 711  ? 23.467 75.023  -24.868 1.00 13.77 ? 711  LYS A CA  1 
ATOM   5776 C  C   . LYS A 1 711  ? 23.827 75.261  -23.428 1.00 12.46 ? 711  LYS A C   1 
ATOM   5777 O  O   . LYS A 1 711  ? 24.169 74.282  -22.719 1.00 15.42 ? 711  LYS A O   1 
ATOM   5778 C  CB  . LYS A 1 711  ? 22.029 74.460  -24.927 1.00 15.68 ? 711  LYS A CB  1 
ATOM   5779 C  CG  . LYS A 1 711  ? 20.965 75.435  -24.415 1.00 20.01 ? 711  LYS A CG  1 
ATOM   5780 C  CD  . LYS A 1 711  ? 19.534 74.867  -24.533 1.00 25.83 ? 711  LYS A CD  1 
ATOM   5781 C  CE  . LYS A 1 711  ? 19.130 74.750  -26.013 1.00 24.25 ? 711  LYS A CE  1 
ATOM   5782 N  NZ  . LYS A 1 711  ? 17.775 74.108  -26.107 1.00 28.68 ? 711  LYS A NZ  1 
ATOM   5783 N  N   . PHE A 1 712  ? 23.720 76.490  -22.927 1.00 10.91 ? 712  PHE A N   1 
ATOM   5784 C  CA  . PHE A 1 712  ? 23.949 76.808  -21.552 1.00 11.25 ? 712  PHE A CA  1 
ATOM   5785 C  C   . PHE A 1 712  ? 22.662 77.134  -20.862 1.00 10.39 ? 712  PHE A C   1 
ATOM   5786 O  O   . PHE A 1 712  ? 21.814 77.888  -21.430 1.00 12.70 ? 712  PHE A O   1 
ATOM   5787 C  CB  . PHE A 1 712  ? 24.973 77.977  -21.384 1.00 12.51 ? 712  PHE A CB  1 
ATOM   5788 C  CG  . PHE A 1 712  ? 26.389 77.568  -21.736 1.00 12.18 ? 712  PHE A CG  1 
ATOM   5789 C  CD1 . PHE A 1 712  ? 26.865 77.583  -23.069 1.00 12.36 ? 712  PHE A CD1 1 
ATOM   5790 C  CD2 . PHE A 1 712  ? 27.229 77.103  -20.697 1.00 12.58 ? 712  PHE A CD2 1 
ATOM   5791 C  CE1 . PHE A 1 712  ? 28.161 77.151  -23.377 1.00 11.36 ? 712  PHE A CE1 1 
ATOM   5792 C  CE2 . PHE A 1 712  ? 28.505 76.678  -20.980 1.00 12.23 ? 712  PHE A CE2 1 
ATOM   5793 C  CZ  . PHE A 1 712  ? 28.988 76.693  -22.290 1.00 11.75 ? 712  PHE A CZ  1 
ATOM   5794 N  N   . LEU A 1 713  ? 22.435 76.598  -19.702 1.00 10.10 ? 713  LEU A N   1 
ATOM   5795 C  CA  . LEU A 1 713  ? 21.215 76.793  -18.923 1.00 11.20 ? 713  LEU A CA  1 
ATOM   5796 C  C   . LEU A 1 713  ? 21.519 77.078  -17.474 1.00 11.65 ? 713  LEU A C   1 
ATOM   5797 O  O   . LEU A 1 713  ? 22.720 76.994  -17.045 1.00 11.76 ? 713  LEU A O   1 
ATOM   5798 C  CB  . LEU A 1 713  ? 20.295 75.542  -19.010 1.00 11.15 ? 713  LEU A CB  1 
ATOM   5799 C  CG  . LEU A 1 713  ? 19.951 75.129  -20.439 1.00 12.09 ? 713  LEU A CG  1 
ATOM   5800 C  CD1 . LEU A 1 713  ? 20.791 73.954  -20.935 1.00 13.86 ? 713  LEU A CD1 1 
ATOM   5801 C  CD2 . LEU A 1 713  ? 18.469 74.683  -20.532 1.00 13.90 ? 713  LEU A CD2 1 
ATOM   5802 N  N   . LYS A 1 714  ? 20.531 77.456  -16.685 1.00 11.02 ? 714  LYS A N   1 
ATOM   5803 C  CA  . LYS A 1 714  ? 20.726 77.722  -15.290 1.00 12.56 ? 714  LYS A CA  1 
ATOM   5804 C  C   . LYS A 1 714  ? 19.695 77.066  -14.419 1.00 13.70 ? 714  LYS A C   1 
ATOM   5805 O  O   . LYS A 1 714  ? 18.496 77.021  -14.778 1.00 14.72 ? 714  LYS A O   1 
ATOM   5806 C  CB  . LYS A 1 714  ? 20.706 79.233  -14.968 1.00 18.40 ? 714  LYS A CB  1 
ATOM   5807 C  CG  . LYS A 1 714  ? 19.731 80.048  -15.707 1.00 28.32 ? 714  LYS A CG  1 
ATOM   5808 C  CD  . LYS A 1 714  ? 19.981 81.567  -15.390 1.00 32.66 ? 714  LYS A CD  1 
ATOM   5809 C  CE  . LYS A 1 714  ? 21.471 81.983  -15.536 1.00 39.05 ? 714  LYS A CE  1 
ATOM   5810 N  NZ  . LYS A 1 714  ? 21.704 83.472  -15.474 1.00 39.35 ? 714  LYS A NZ  1 
ATOM   5811 N  N   . TYR A 1 715  ? 20.159 76.520  -13.295 1.00 11.24 ? 715  TYR A N   1 
ATOM   5812 C  CA  . TYR A 1 715  ? 19.285 76.003  -12.288 1.00 10.83 ? 715  TYR A CA  1 
ATOM   5813 C  C   . TYR A 1 715  ? 19.236 77.059  -11.195 1.00 13.88 ? 715  TYR A C   1 
ATOM   5814 O  O   . TYR A 1 715  ? 20.215 77.781  -10.945 1.00 13.76 ? 715  TYR A O   1 
ATOM   5815 C  CB  . TYR A 1 715  ? 19.831 74.705  -11.633 1.00 11.26 ? 715  TYR A CB  1 
ATOM   5816 C  CG  . TYR A 1 715  ? 19.760 73.525  -12.512 1.00 10.25 ? 715  TYR A CG  1 
ATOM   5817 C  CD1 . TYR A 1 715  ? 20.862 73.078  -13.257 1.00 10.79 ? 715  TYR A CD1 1 
ATOM   5818 C  CD2 . TYR A 1 715  ? 18.569 72.781  -12.592 1.00 11.13 ? 715  TYR A CD2 1 
ATOM   5819 C  CE1 . TYR A 1 715  ? 20.804 71.927  -14.041 1.00 11.02 ? 715  TYR A CE1 1 
ATOM   5820 C  CE2 . TYR A 1 715  ? 18.483 71.622  -13.370 1.00 11.06 ? 715  TYR A CE2 1 
ATOM   5821 C  CZ  . TYR A 1 715  ? 19.598 71.168  -14.099 1.00 9.85  ? 715  TYR A CZ  1 
ATOM   5822 O  OH  . TYR A 1 715  ? 19.499 70.020  -14.834 1.00 11.67 ? 715  TYR A OH  1 
ATOM   5823 N  N   . GLY A 1 716  ? 18.133 77.138  -10.461 1.00 11.87 ? 716  GLY A N   1 
ATOM   5824 C  CA  . GLY A 1 716  ? 17.952 78.068  -9.354  1.00 12.27 ? 716  GLY A CA  1 
ATOM   5825 C  C   . GLY A 1 716  ? 17.825 77.290  -8.030  1.00 13.63 ? 716  GLY A C   1 
ATOM   5826 O  O   . GLY A 1 716  ? 18.123 76.051  -7.972  1.00 15.85 ? 716  GLY A O   1 
ATOM   5827 N  N   . VAL A 1 717  ? 17.339 77.949  -6.995  1.00 13.39 ? 717  VAL A N   1 
ATOM   5828 C  CA  . VAL A 1 717  ? 17.206 77.389  -5.662  1.00 14.63 ? 717  VAL A CA  1 
ATOM   5829 C  C   . VAL A 1 717  ? 15.743 77.541  -5.230  1.00 16.02 ? 717  VAL A C   1 
ATOM   5830 O  O   . VAL A 1 717  ? 15.077 78.501  -5.648  1.00 18.17 ? 717  VAL A O   1 
ATOM   5831 C  CB  . VAL A 1 717  ? 18.125 78.156  -4.701  1.00 15.32 ? 717  VAL A CB  1 
ATOM   5832 C  CG1 . VAL A 1 717  ? 17.919 77.763  -3.278  1.00 20.05 ? 717  VAL A CG1 1 
ATOM   5833 C  CG2 . VAL A 1 717  ? 19.586 77.910  -5.083  1.00 14.95 ? 717  VAL A CG2 1 
ATOM   5834 N  N   . ARG A 1 718  ? 15.265 76.655  -4.383  1.00 13.65 ? 718  ARG A N   1 
ATOM   5835 C  CA  . ARG A 1 718  ? 13.862 76.675  -3.917  1.00 15.21 ? 718  ARG A CA  1 
ATOM   5836 C  C   . ARG A 1 718  ? 13.603 77.846  -3.027  1.00 18.98 ? 718  ARG A C   1 
ATOM   5837 O  O   . ARG A 1 718  ? 14.435 78.201  -2.227  1.00 21.91 ? 718  ARG A O   1 
ATOM   5838 C  CB  . ARG A 1 718  ? 13.528 75.363  -3.209  1.00 15.00 ? 718  ARG A CB  1 
ATOM   5839 C  CG  . ARG A 1 718  ? 13.599 74.237  -4.198  1.00 13.73 ? 718  ARG A CG  1 
ATOM   5840 C  CD  . ARG A 1 718  ? 13.597 72.863  -3.484  1.00 15.87 ? 718  ARG A CD  1 
ATOM   5841 N  NE  . ARG A 1 718  ? 13.824 71.861  -4.489  1.00 15.13 ? 718  ARG A NE  1 
ATOM   5842 C  CZ  . ARG A 1 718  ? 13.807 70.550  -4.245  1.00 16.22 ? 718  ARG A CZ  1 
ATOM   5843 N  NH1 . ARG A 1 718  ? 13.535 70.096  -3.020  1.00 15.26 ? 718  ARG A NH1 1 
ATOM   5844 N  NH2 . ARG A 1 718  ? 14.144 69.720  -5.216  1.00 17.95 ? 718  ARG A NH2 1 
ATOM   5845 N  N   . SER A 1 719  ? 12.411 78.442  -3.154  1.00 20.50 ? 719  SER A N   1 
ATOM   5846 C  CA  . SER A 1 719  ? 12.078 79.607  -2.323  1.00 26.17 ? 719  SER A CA  1 
ATOM   5847 C  C   . SER A 1 719  ? 11.467 79.243  -0.976  1.00 30.01 ? 719  SER A C   1 
ATOM   5848 O  O   . SER A 1 719  ? 11.344 80.082  -0.102  1.00 33.64 ? 719  SER A O   1 
ATOM   5849 C  CB  . SER A 1 719  ? 11.154 80.561  -3.093  1.00 24.49 ? 719  SER A CB  1 
ATOM   5850 O  OG  . SER A 1 719  ? 10.017 79.862  -3.495  1.00 29.85 ? 719  SER A OG  1 
ATOM   5851 N  N   . HIS A 1 720  ? 11.048 77.997  -0.835  1.00 32.15 ? 720  HIS A N   1 
ATOM   5852 C  CA  . HIS A 1 720  ? 10.544 77.495  0.430   1.00 34.80 ? 720  HIS A CA  1 
ATOM   5853 C  C   . HIS A 1 720  ? 11.091 76.051  0.485   1.00 34.26 ? 720  HIS A C   1 
ATOM   5854 O  O   . HIS A 1 720  ? 11.455 75.458  -0.541  1.00 34.39 ? 720  HIS A O   1 
ATOM   5855 C  CB  . HIS A 1 720  ? 9.010  77.562  0.478   1.00 37.53 ? 720  HIS A CB  1 
ATOM   5856 C  CG  . HIS A 1 720  ? 8.334  76.767  -0.591  1.00 40.71 ? 720  HIS A CG  1 
ATOM   5857 N  ND1 . HIS A 1 720  ? 8.041  75.425  -0.447  1.00 43.49 ? 720  HIS A ND1 1 
ATOM   5858 C  CD2 . HIS A 1 720  ? 7.939  77.113  -1.842  1.00 43.31 ? 720  HIS A CD2 1 
ATOM   5859 C  CE1 . HIS A 1 720  ? 7.498  74.978  -1.567  1.00 45.27 ? 720  HIS A CE1 1 
ATOM   5860 N  NE2 . HIS A 1 720  ? 7.427  75.981  -2.429  1.00 44.27 ? 720  HIS A NE2 1 
ATOM   5861 N  N   . GLY A 1 721  ? 11.185 75.488  1.675   1.00 31.85 ? 721  GLY A N   1 
ATOM   5862 C  CA  . GLY A 1 721  ? 11.750 74.162  1.737   1.00 28.47 ? 721  GLY A CA  1 
ATOM   5863 C  C   . GLY A 1 721  ? 13.276 74.227  1.813   1.00 26.70 ? 721  GLY A C   1 
ATOM   5864 O  O   . GLY A 1 721  ? 13.905 75.273  2.067   1.00 23.07 ? 721  GLY A O   1 
ATOM   5865 N  N   . ASP A 1 722  ? 13.882 73.090  1.518   1.00 21.12 ? 722  ASP A N   1 
ATOM   5866 C  CA  . ASP A 1 722  ? 15.327 72.991  1.688   1.00 18.92 ? 722  ASP A CA  1 
ATOM   5867 C  C   . ASP A 1 722  ? 16.095 73.664  0.582   1.00 15.74 ? 722  ASP A C   1 
ATOM   5868 O  O   . ASP A 1 722  ? 15.751 73.574  -0.570  1.00 16.91 ? 722  ASP A O   1 
ATOM   5869 C  CB  . ASP A 1 722  ? 15.717 71.522  1.777   1.00 16.84 ? 722  ASP A CB  1 
ATOM   5870 C  CG  . ASP A 1 722  ? 15.159 70.803  3.047   1.00 18.49 ? 722  ASP A CG  1 
ATOM   5871 O  OD1 . ASP A 1 722  ? 14.965 69.556  2.931   1.00 19.14 ? 722  ASP A OD1 1 
ATOM   5872 O  OD2 . ASP A 1 722  ? 14.955 71.434  4.152   1.00 20.29 ? 722  ASP A OD2 1 
ATOM   5873 N  N   . ARG A 1 723  ? 17.189 74.313  0.990   1.00 15.00 ? 723  ARG A N   1 
ATOM   5874 C  CA  . ARG A 1 723  ? 18.040 75.026  0.048   1.00 14.34 ? 723  ARG A CA  1 
ATOM   5875 C  C   . ARG A 1 723  ? 19.339 74.318  -0.325  1.00 14.00 ? 723  ARG A C   1 
ATOM   5876 O  O   . ARG A 1 723  ? 19.956 73.654  0.508   1.00 13.86 ? 723  ARG A O   1 
ATOM   5877 C  CB  . ARG A 1 723  ? 18.427 76.374  0.643   1.00 16.58 ? 723  ARG A CB  1 
ATOM   5878 C  CG  . ARG A 1 723  ? 17.197 77.170  1.101   1.00 24.52 ? 723  ARG A CG  1 
ATOM   5879 C  CD  . ARG A 1 723  ? 17.502 78.626  1.327   1.00 33.35 ? 723  ARG A CD  1 
ATOM   5880 N  NE  . ARG A 1 723  ? 16.240 79.285  1.599   1.00 39.68 ? 723  ARG A NE  1 
ATOM   5881 C  CZ  . ARG A 1 723  ? 16.110 80.521  2.061   1.00 41.68 ? 723  ARG A CZ  1 
ATOM   5882 N  NH1 . ARG A 1 723  ? 17.189 81.270  2.311   1.00 41.99 ? 723  ARG A NH1 1 
ATOM   5883 N  NH2 . ARG A 1 723  ? 14.887 80.993  2.289   1.00 39.20 ? 723  ARG A NH2 1 
ATOM   5884 N  N   . SER A 1 724  ? 19.693 74.465  -1.601  1.00 11.90 ? 724  SER A N   1 
ATOM   5885 C  CA  . SER A 1 724  ? 20.953 73.952  -2.110  1.00 11.10 ? 724  SER A CA  1 
ATOM   5886 C  C   . SER A 1 724  ? 22.060 74.657  -1.337  1.00 12.37 ? 724  SER A C   1 
ATOM   5887 O  O   . SER A 1 724  ? 21.950 75.844  -0.972  1.00 15.23 ? 724  SER A O   1 
ATOM   5888 C  CB  . SER A 1 724  ? 21.124 74.327  -3.577  1.00 12.33 ? 724  SER A CB  1 
ATOM   5889 O  OG  . SER A 1 724  ? 20.087 73.680  -4.281  1.00 12.29 ? 724  SER A OG  1 
ATOM   5890 N  N   . GLY A 1 725  ? 23.189 73.949  -1.147  1.00 10.40 ? 725  GLY A N   1 
ATOM   5891 C  CA  . GLY A 1 725  ? 24.359 74.531  -0.485  1.00 10.05 ? 725  GLY A CA  1 
ATOM   5892 C  C   . GLY A 1 725  ? 25.592 73.772  -1.042  1.00 9.02  ? 725  GLY A C   1 
ATOM   5893 O  O   . GLY A 1 725  ? 25.544 73.164  -2.126  1.00 9.88  ? 725  GLY A O   1 
ATOM   5894 N  N   . ALA A 1 726  ? 26.716 73.868  -0.341  1.00 9.02  ? 726  ALA A N   1 
ATOM   5895 C  CA  . ALA A 1 726  ? 27.931 73.205  -0.830  1.00 8.79  ? 726  ALA A CA  1 
ATOM   5896 C  C   . ALA A 1 726  ? 27.796 71.709  -1.058  1.00 8.93  ? 726  ALA A C   1 
ATOM   5897 O  O   . ALA A 1 726  ? 28.453 71.141  -1.944  1.00 8.86  ? 726  ALA A O   1 
ATOM   5898 C  CB  . ALA A 1 726  ? 29.122 73.446  0.115   1.00 10.46 ? 726  ALA A CB  1 
ATOM   5899 N  N   . TYR A 1 727  ? 26.969 71.058  -0.259  1.00 8.95  ? 727  TYR A N   1 
ATOM   5900 C  CA  . TYR A 1 727  ? 26.779 69.593  -0.392  1.00 8.24  ? 727  TYR A CA  1 
ATOM   5901 C  C   . TYR A 1 727  ? 25.612 69.181  -1.308  1.00 8.27  ? 727  TYR A C   1 
ATOM   5902 O  O   . TYR A 1 727  ? 25.723 68.344  -2.170  1.00 8.81  ? 727  TYR A O   1 
ATOM   5903 C  CB  . TYR A 1 727  ? 26.502 68.962  0.972   1.00 9.50  ? 727  TYR A CB  1 
ATOM   5904 C  CG  . TYR A 1 727  ? 27.555 69.263  2.032   1.00 9.29  ? 727  TYR A CG  1 
ATOM   5905 C  CD1 . TYR A 1 727  ? 27.481 70.432  2.796   1.00 10.37 ? 727  TYR A CD1 1 
ATOM   5906 C  CD2 . TYR A 1 727  ? 28.608 68.362  2.294   1.00 9.78  ? 727  TYR A CD2 1 
ATOM   5907 C  CE1 . TYR A 1 727  ? 28.426 70.675  3.802   1.00 9.27  ? 727  TYR A CE1 1 
ATOM   5908 C  CE2 . TYR A 1 727  ? 29.554 68.622  3.296   1.00 8.98  ? 727  TYR A CE2 1 
ATOM   5909 C  CZ  . TYR A 1 727  ? 29.457 69.755  4.038   1.00 9.63  ? 727  TYR A CZ  1 
ATOM   5910 O  OH  . TYR A 1 727  ? 30.282 70.003  5.121   1.00 10.46 ? 727  TYR A OH  1 
ATOM   5911 N  N   . LEU A 1 728  ? 24.469 69.827  -1.009  1.00 9.72  ? 728  LEU A N   1 
ATOM   5912 C  CA  . LEU A 1 728  ? 23.186 69.451  -1.635  1.00 9.33  ? 728  LEU A CA  1 
ATOM   5913 C  C   . LEU A 1 728  ? 22.820 70.204  -2.885  1.00 9.43  ? 728  LEU A C   1 
ATOM   5914 O  O   . LEU A 1 728  ? 23.002 71.423  -2.949  1.00 10.58 ? 728  LEU A O   1 
ATOM   5915 C  CB  . LEU A 1 728  ? 21.996 69.681  -0.636  1.00 10.66 ? 728  LEU A CB  1 
ATOM   5916 C  CG  . LEU A 1 728  ? 22.161 69.050  0.750   1.00 9.78  ? 728  LEU A CG  1 
ATOM   5917 C  CD1 . LEU A 1 728  ? 20.837 69.267  1.563   1.00 12.18 ? 728  LEU A CD1 1 
ATOM   5918 C  CD2 . LEU A 1 728  ? 22.490 67.576  0.700   1.00 13.11 ? 728  LEU A CD2 1 
ATOM   5919 N  N   . PHE A 1 729  ? 22.283 69.490  -3.872  1.00 9.59  ? 729  PHE A N   1 
ATOM   5920 C  CA  . PHE A 1 729  ? 21.737 70.095  -5.082  1.00 10.41 ? 729  PHE A CA  1 
ATOM   5921 C  C   . PHE A 1 729  ? 20.198 69.883  -4.979  1.00 11.22 ? 729  PHE A C   1 
ATOM   5922 O  O   . PHE A 1 729  ? 19.715 68.741  -5.070  1.00 10.71 ? 729  PHE A O   1 
ATOM   5923 C  CB  . PHE A 1 729  ? 22.298 69.332  -6.288  1.00 10.24 ? 729  PHE A CB  1 
ATOM   5924 C  CG  . PHE A 1 729  ? 21.759 69.795  -7.646  1.00 9.34  ? 729  PHE A CG  1 
ATOM   5925 C  CD1 . PHE A 1 729  ? 21.657 68.901  -8.680  1.00 9.91  ? 729  PHE A CD1 1 
ATOM   5926 C  CD2 . PHE A 1 729  ? 21.441 71.154  -7.901  1.00 10.21 ? 729  PHE A CD2 1 
ATOM   5927 C  CE1 . PHE A 1 729  ? 21.257 69.285  -9.932  1.00 9.25  ? 729  PHE A CE1 1 
ATOM   5928 C  CE2 . PHE A 1 729  ? 21.026 71.560  -9.181  1.00 9.26  ? 729  PHE A CE2 1 
ATOM   5929 C  CZ  . PHE A 1 729  ? 20.934 70.632  -10.181 1.00 10.43 ? 729  PHE A CZ  1 
ATOM   5930 N  N   . LEU A 1 730  ? 19.486 71.000  -4.794  1.00 10.69 ? 730  LEU A N   1 
ATOM   5931 C  CA  . LEU A 1 730  ? 17.999 70.975  -4.616  1.00 12.94 ? 730  LEU A CA  1 
ATOM   5932 C  C   . LEU A 1 730  ? 17.420 71.987  -5.592  1.00 10.38 ? 730  LEU A C   1 
ATOM   5933 O  O   . LEU A 1 730  ? 16.961 73.073  -5.184  1.00 12.06 ? 730  LEU A O   1 
ATOM   5934 C  CB  . LEU A 1 730  ? 17.644 71.327  -3.159  1.00 12.64 ? 730  LEU A CB  1 
ATOM   5935 C  CG  . LEU A 1 730  ? 18.073 70.230  -2.160  1.00 12.77 ? 730  LEU A CG  1 
ATOM   5936 C  CD1 . LEU A 1 730  ? 18.082 70.772  -0.748  1.00 15.13 ? 730  LEU A CD1 1 
ATOM   5937 C  CD2 . LEU A 1 730  ? 17.093 69.051  -2.252  1.00 16.02 ? 730  LEU A CD2 1 
ATOM   5938 N  N   . PRO A 1 731  ? 17.458 71.663  -6.878  1.00 11.62 ? 731  PRO A N   1 
ATOM   5939 C  CA  . PRO A 1 731  ? 16.948 72.619  -7.869  1.00 12.50 ? 731  PRO A CA  1 
ATOM   5940 C  C   . PRO A 1 731  ? 15.482 72.924  -7.774  1.00 12.87 ? 731  PRO A C   1 
ATOM   5941 O  O   . PRO A 1 731  ? 14.686 72.103  -7.314  1.00 13.38 ? 731  PRO A O   1 
ATOM   5942 C  CB  . PRO A 1 731  ? 17.294 71.942  -9.193  1.00 13.17 ? 731  PRO A CB  1 
ATOM   5943 C  CG  . PRO A 1 731  ? 17.197 70.471  -8.887  1.00 13.40 ? 731  PRO A CG  1 
ATOM   5944 C  CD  . PRO A 1 731  ? 17.771 70.366  -7.500  1.00 11.67 ? 731  PRO A CD  1 
ATOM   5945 N  N   . ASN A 1 732  ? 15.147 74.127  -8.234  1.00 13.79 ? 732  ASN A N   1 
ATOM   5946 C  CA  . ASN A 1 732  ? 13.705 74.531  -8.289  1.00 14.64 ? 732  ASN A CA  1 
ATOM   5947 C  C   . ASN A 1 732  ? 13.211 74.173  -9.679  1.00 15.76 ? 732  ASN A C   1 
ATOM   5948 O  O   . ASN A 1 732  ? 12.775 75.040  -10.458 1.00 19.83 ? 732  ASN A O   1 
ATOM   5949 C  CB  . ASN A 1 732  ? 13.565 76.026  -7.966  1.00 18.61 ? 732  ASN A CB  1 
ATOM   5950 C  CG  . ASN A 1 732  ? 14.268 76.905  -8.940  1.00 19.69 ? 732  ASN A CG  1 
ATOM   5951 O  OD1 . ASN A 1 732  ? 15.253 76.546  -9.555  1.00 21.01 ? 732  ASN A OD1 1 
ATOM   5952 N  ND2 . ASN A 1 732  ? 13.729 78.134  -9.119  1.00 23.96 ? 732  ASN A ND2 1 
ATOM   5953 N  N   . GLY A 1 733  ? 13.289 72.905  -10.028 1.00 14.61 ? 733  GLY A N   1 
ATOM   5954 C  CA  . GLY A 1 733  ? 12.838 72.420  -11.321 1.00 15.88 ? 733  GLY A CA  1 
ATOM   5955 C  C   . GLY A 1 733  ? 13.908 72.348  -12.413 1.00 14.38 ? 733  GLY A C   1 
ATOM   5956 O  O   . GLY A 1 733  ? 15.093 72.708  -12.146 1.00 13.98 ? 733  GLY A O   1 
ATOM   5957 N  N   . PRO A 1 734  ? 13.581 71.866  -13.603 1.00 13.23 ? 734  PRO A N   1 
ATOM   5958 C  CA  . PRO A 1 734  ? 14.522 71.774  -14.716 1.00 13.19 ? 734  PRO A CA  1 
ATOM   5959 C  C   . PRO A 1 734  ? 15.132 73.145  -15.012 1.00 14.03 ? 734  PRO A C   1 
ATOM   5960 O  O   . PRO A 1 734  ? 14.545 74.216  -14.773 1.00 14.22 ? 734  PRO A O   1 
ATOM   5961 C  CB  . PRO A 1 734  ? 13.673 71.297  -15.880 1.00 15.76 ? 734  PRO A CB  1 
ATOM   5962 C  CG  . PRO A 1 734  ? 12.535 70.526  -15.171 1.00 20.47 ? 734  PRO A CG  1 
ATOM   5963 C  CD  . PRO A 1 734  ? 12.258 71.290  -13.942 1.00 15.72 ? 734  PRO A CD  1 
ATOM   5964 N  N   . ALA A 1 735  ? 16.328 73.086  -15.594 1.00 13.20 ? 735  ALA A N   1 
ATOM   5965 C  CA  . ALA A 1 735  ? 17.066 74.299  -15.942 1.00 13.05 ? 735  ALA A CA  1 
ATOM   5966 C  C   . ALA A 1 735  ? 16.380 75.137  -17.033 1.00 13.51 ? 735  ALA A C   1 
ATOM   5967 O  O   . ALA A 1 735  ? 15.666 74.618  -17.874 1.00 15.83 ? 735  ALA A O   1 
ATOM   5968 C  CB  . ALA A 1 735  ? 18.513 73.882  -16.338 1.00 12.89 ? 735  ALA A CB  1 
ATOM   5969 N  N   . SER A 1 736  ? 16.640 76.433  -16.942 1.00 14.62 ? 736  SER A N   1 
ATOM   5970 C  CA  . SER A 1 736  ? 16.086 77.428  -17.881 1.00 14.88 ? 736  SER A CA  1 
ATOM   5971 C  C   . SER A 1 736  ? 17.217 77.914  -18.731 1.00 15.53 ? 736  SER A C   1 
ATOM   5972 O  O   . SER A 1 736  ? 18.313 78.146  -18.234 1.00 15.28 ? 736  SER A O   1 
ATOM   5973 C  CB  . SER A 1 736  ? 15.508 78.588  -17.089 1.00 16.83 ? 736  SER A CB  1 
ATOM   5974 O  OG  . SER A 1 736  ? 14.546 78.155  -16.150 1.00 28.68 ? 736  SER A OG  1 
ATOM   5975 N  N   . PRO A 1 737  ? 16.983 78.164  -20.027 1.00 17.33 ? 737  PRO A N   1 
ATOM   5976 C  CA  . PRO A 1 737  ? 18.082 78.635  -20.910 1.00 19.44 ? 737  PRO A CA  1 
ATOM   5977 C  C   . PRO A 1 737  ? 18.676 79.979  -20.470 1.00 18.18 ? 737  PRO A C   1 
ATOM   5978 O  O   . PRO A 1 737  ? 17.939 80.864  -19.987 1.00 20.71 ? 737  PRO A O   1 
ATOM   5979 C  CB  . PRO A 1 737  ? 17.419 78.782  -22.291 1.00 24.24 ? 737  PRO A CB  1 
ATOM   5980 C  CG  . PRO A 1 737  ? 16.219 77.823  -22.212 1.00 22.91 ? 737  PRO A CG  1 
ATOM   5981 C  CD  . PRO A 1 737  ? 15.722 77.989  -20.776 1.00 19.42 ? 737  PRO A CD  1 
ATOM   5982 N  N   . VAL A 1 738  ? 20.014 80.115  -20.529 1.00 16.28 ? 738  VAL A N   1 
ATOM   5983 C  CA  . VAL A 1 738  ? 20.639 81.435  -20.254 1.00 15.73 ? 738  VAL A CA  1 
ATOM   5984 C  C   . VAL A 1 738  ? 20.222 82.330  -21.451 1.00 16.96 ? 738  VAL A C   1 
ATOM   5985 O  O   . VAL A 1 738  ? 20.294 81.912  -22.598 1.00 17.96 ? 738  VAL A O   1 
ATOM   5986 C  CB  . VAL A 1 738  ? 22.185 81.295  -20.202 1.00 16.24 ? 738  VAL A CB  1 
ATOM   5987 C  CG1 . VAL A 1 738  ? 22.868 82.730  -20.189 1.00 16.91 ? 738  VAL A CG1 1 
ATOM   5988 C  CG2 . VAL A 1 738  ? 22.596 80.458  -18.945 1.00 15.56 ? 738  VAL A CG2 1 
ATOM   5989 N  N   . GLU A 1 739  ? 19.767 83.539  -21.154 1.00 19.78 ? 739  GLU A N   1 
ATOM   5990 C  CA  . GLU A 1 739  ? 19.391 84.468  -22.233 1.00 20.29 ? 739  GLU A CA  1 
ATOM   5991 C  C   . GLU A 1 739  ? 20.724 84.997  -22.804 1.00 16.62 ? 739  GLU A C   1 
ATOM   5992 O  O   . GLU A 1 739  ? 21.500 85.645  -22.105 1.00 19.32 ? 739  GLU A O   1 
ATOM   5993 C  CB  . GLU A 1 739  ? 18.592 85.619  -21.644 1.00 23.22 ? 739  GLU A CB  1 
ATOM   5994 C  CG  . GLU A 1 739  ? 17.161 85.240  -21.355 1.00 32.04 ? 739  GLU A CG  1 
ATOM   5995 C  CD  . GLU A 1 739  ? 16.222 86.454  -21.209 1.00 41.27 ? 739  GLU A CD  1 
ATOM   5996 O  OE1 . GLU A 1 739  ? 14.999 86.235  -20.999 1.00 43.45 ? 739  GLU A OE1 1 
ATOM   5997 O  OE2 . GLU A 1 739  ? 16.697 87.610  -21.310 1.00 44.37 ? 739  GLU A OE2 1 
ATOM   5998 N  N   . LEU A 1 740  ? 20.966 84.724  -24.069 1.00 18.39 ? 740  LEU A N   1 
ATOM   5999 C  CA  . LEU A 1 740  ? 22.265 85.068  -24.679 1.00 19.81 ? 740  LEU A CA  1 
ATOM   6000 C  C   . LEU A 1 740  ? 22.443 86.444  -25.287 1.00 22.95 ? 740  LEU A C   1 
ATOM   6001 O  O   . LEU A 1 740  ? 23.580 86.873  -25.420 1.00 24.77 ? 740  LEU A O   1 
ATOM   6002 C  CB  . LEU A 1 740  ? 22.620 84.028  -25.736 1.00 22.54 ? 740  LEU A CB  1 
ATOM   6003 C  CG  . LEU A 1 740  ? 22.632 82.567  -25.249 1.00 20.25 ? 740  LEU A CG  1 
ATOM   6004 C  CD1 . LEU A 1 740  ? 23.037 81.667  -26.393 1.00 19.04 ? 740  LEU A CD1 1 
ATOM   6005 C  CD2 . LEU A 1 740  ? 23.595 82.399  -24.018 1.00 20.44 ? 740  LEU A CD2 1 
ATOM   6006 N  N   . GLY A 1 741  ? 21.337 87.123  -25.634 1.00 24.04 ? 741  GLY A N   1 
ATOM   6007 C  CA  . GLY A 1 741  ? 21.464 88.431  -26.278 1.00 23.21 ? 741  GLY A CA  1 
ATOM   6008 C  C   . GLY A 1 741  ? 22.037 88.203  -27.686 1.00 22.26 ? 741  GLY A C   1 
ATOM   6009 O  O   . GLY A 1 741  ? 21.696 87.219  -28.326 1.00 24.03 ? 741  GLY A O   1 
ATOM   6010 N  N   . GLN A 1 742  ? 22.874 89.113  -28.207 1.00 23.60 ? 742  GLN A N   1 
ATOM   6011 C  CA  . GLN A 1 742  ? 23.502 88.887  -29.536 1.00 19.96 ? 742  GLN A CA  1 
ATOM   6012 C  C   . GLN A 1 742  ? 25.007 88.872  -29.199 1.00 20.37 ? 742  GLN A C   1 
ATOM   6013 O  O   . GLN A 1 742  ? 25.721 89.858  -29.345 1.00 21.33 ? 742  GLN A O   1 
ATOM   6014 C  CB  . GLN A 1 742  ? 23.192 90.050  -30.497 1.00 28.58 ? 742  GLN A CB  1 
ATOM   6015 C  CG  . GLN A 1 742  ? 23.618 89.739  -31.936 1.00 34.84 ? 742  GLN A CG  1 
ATOM   6016 C  CD  . GLN A 1 742  ? 23.079 90.742  -32.975 1.00 43.03 ? 742  GLN A CD  1 
ATOM   6017 O  OE1 . GLN A 1 742  ? 22.819 90.367  -34.117 1.00 43.83 ? 742  GLN A OE1 1 
ATOM   6018 N  NE2 . GLN A 1 742  ? 22.925 92.019  -32.578 1.00 45.49 ? 742  GLN A NE2 1 
ATOM   6019 N  N   . PRO A 1 743  ? 25.507 87.719  -28.768 1.00 16.52 ? 743  PRO A N   1 
ATOM   6020 C  CA  . PRO A 1 743  ? 26.935 87.676  -28.385 1.00 13.73 ? 743  PRO A CA  1 
ATOM   6021 C  C   . PRO A 1 743  ? 27.959 87.874  -29.489 1.00 15.03 ? 743  PRO A C   1 
ATOM   6022 O  O   . PRO A 1 743  ? 27.715 87.638  -30.679 1.00 16.96 ? 743  PRO A O   1 
ATOM   6023 C  CB  . PRO A 1 743  ? 27.057 86.332  -27.692 1.00 16.32 ? 743  PRO A CB  1 
ATOM   6024 C  CG  . PRO A 1 743  ? 26.061 85.476  -28.415 1.00 15.62 ? 743  PRO A CG  1 
ATOM   6025 C  CD  . PRO A 1 743  ? 24.862 86.387  -28.736 1.00 14.79 ? 743  PRO A CD  1 
ATOM   6026 N  N   . VAL A 1 744  ? 29.118 88.360  -29.065 1.00 12.01 ? 744  VAL A N   1 
ATOM   6027 C  CA  . VAL A 1 744  ? 30.253 88.580  -29.977 1.00 11.45 ? 744  VAL A CA  1 
ATOM   6028 C  C   . VAL A 1 744  ? 30.961 87.241  -30.197 1.00 10.60 ? 744  VAL A C   1 
ATOM   6029 O  O   . VAL A 1 744  ? 31.280 86.540  -29.212 1.00 12.19 ? 744  VAL A O   1 
ATOM   6030 C  CB  . VAL A 1 744  ? 31.219 89.596  -29.359 1.00 11.72 ? 744  VAL A CB  1 
ATOM   6031 C  CG1 . VAL A 1 744  ? 32.435 89.783  -30.250 1.00 13.53 ? 744  VAL A CG1 1 
ATOM   6032 C  CG2 . VAL A 1 744  ? 30.476 90.958  -29.161 1.00 15.65 ? 744  VAL A CG2 1 
ATOM   6033 N  N   . VAL A 1 745  ? 31.184 86.880  -31.423 1.00 10.99 ? 745  VAL A N   1 
ATOM   6034 C  CA  . VAL A 1 745  ? 31.815 85.622  -31.814 1.00 10.92 ? 745  VAL A CA  1 
ATOM   6035 C  C   . VAL A 1 745  ? 33.094 85.855  -32.547 1.00 10.90 ? 745  VAL A C   1 
ATOM   6036 O  O   . VAL A 1 745  ? 33.118 86.631  -33.538 1.00 12.73 ? 745  VAL A O   1 
ATOM   6037 C  CB  . VAL A 1 745  ? 30.851 84.808  -32.736 1.00 10.26 ? 745  VAL A CB  1 
ATOM   6038 C  CG1 . VAL A 1 745  ? 31.467 83.490  -33.163 1.00 12.17 ? 745  VAL A CG1 1 
ATOM   6039 C  CG2 . VAL A 1 745  ? 29.522 84.562  -32.018 1.00 10.95 ? 745  VAL A CG2 1 
ATOM   6040 N  N   . LEU A 1 746  ? 34.190 85.197  -32.165 1.00 10.28 ? 746  LEU A N   1 
ATOM   6041 C  CA  . LEU A 1 746  ? 35.457 85.347  -32.815 1.00 10.06 ? 746  LEU A CA  1 
ATOM   6042 C  C   . LEU A 1 746  ? 35.867 84.061  -33.490 1.00 10.52 ? 746  LEU A C   1 
ATOM   6043 O  O   . LEU A 1 746  ? 35.928 82.989  -32.801 1.00 10.25 ? 746  LEU A O   1 
ATOM   6044 C  CB  . LEU A 1 746  ? 36.482 85.728  -31.739 1.00 11.91 ? 746  LEU A CB  1 
ATOM   6045 C  CG  . LEU A 1 746  ? 37.956 85.694  -32.198 1.00 13.41 ? 746  LEU A CG  1 
ATOM   6046 C  CD1 . LEU A 1 746  ? 38.235 86.810  -33.259 1.00 15.93 ? 746  LEU A CD1 1 
ATOM   6047 C  CD2 . LEU A 1 746  ? 38.859 85.873  -30.949 1.00 16.81 ? 746  LEU A CD2 1 
ATOM   6048 N  N   . VAL A 1 747  ? 36.155 84.082  -34.759 1.00 10.12 ? 747  VAL A N   1 
ATOM   6049 C  CA  . VAL A 1 747  ? 36.567 82.913  -35.515 1.00 9.76  ? 747  VAL A CA  1 
ATOM   6050 C  C   . VAL A 1 747  ? 38.005 83.033  -35.948 1.00 11.39 ? 747  VAL A C   1 
ATOM   6051 O  O   . VAL A 1 747  ? 38.358 84.000  -36.658 1.00 13.37 ? 747  VAL A O   1 
ATOM   6052 C  CB  . VAL A 1 747  ? 35.661 82.749  -36.768 1.00 11.05 ? 747  VAL A CB  1 
ATOM   6053 C  CG1 . VAL A 1 747  ? 36.026 81.455  -37.508 1.00 12.15 ? 747  VAL A CG1 1 
ATOM   6054 C  CG2 . VAL A 1 747  ? 34.179 82.751  -36.345 1.00 11.94 ? 747  VAL A CG2 1 
ATOM   6055 N  N   . THR A 1 748  ? 38.875 82.113  -35.559 1.00 10.89 ? 748  THR A N   1 
ATOM   6056 C  CA  . THR A 1 748  ? 40.244 82.123  -35.999 1.00 12.26 ? 748  THR A CA  1 
ATOM   6057 C  C   . THR A 1 748  ? 40.453 80.924  -36.866 1.00 12.09 ? 748  THR A C   1 
ATOM   6058 O  O   . THR A 1 748  ? 40.106 79.797  -36.424 1.00 13.54 ? 748  THR A O   1 
ATOM   6059 C  CB  . THR A 1 748  ? 41.146 82.150  -34.751 1.00 13.26 ? 748  THR A CB  1 
ATOM   6060 O  OG1 . THR A 1 748  ? 40.924 83.378  -34.035 1.00 14.95 ? 748  THR A OG1 1 
ATOM   6061 C  CG2 . THR A 1 748  ? 42.598 82.091  -35.147 1.00 14.83 ? 748  THR A CG2 1 
ATOM   6062 N  N   . LYS A 1 749  ? 40.971 81.095  -38.087 1.00 11.75 ? 749  LYS A N   1 
ATOM   6063 C  CA  . LYS A 1 749  ? 41.142 79.969  -39.003 1.00 11.89 ? 749  LYS A CA  1 
ATOM   6064 C  C   . LYS A 1 749  ? 42.558 79.825  -39.401 1.00 13.18 ? 749  LYS A C   1 
ATOM   6065 O  O   . LYS A 1 749  ? 43.170 80.744  -39.985 1.00 12.68 ? 749  LYS A O   1 
ATOM   6066 C  CB  . LYS A 1 749  ? 40.284 80.175  -40.248 1.00 14.20 ? 749  LYS A CB  1 
ATOM   6067 C  CG  . LYS A 1 749  ? 40.424 79.049  -41.255 1.00 18.90 ? 749  LYS A CG  1 
ATOM   6068 C  CD  . LYS A 1 749  ? 39.466 79.267  -42.450 1.00 22.50 ? 749  LYS A CD  1 
ATOM   6069 C  CE  . LYS A 1 749  ? 39.808 78.352  -43.607 1.00 28.76 ? 749  LYS A CE  1 
ATOM   6070 N  NZ  . LYS A 1 749  ? 38.960 78.837  -44.778 1.00 37.97 ? 749  LYS A NZ  1 
ATOM   6071 N  N   . GLY A 1 750  ? 43.127 78.658  -39.090 1.00 11.65 ? 750  GLY A N   1 
ATOM   6072 C  CA  . GLY A 1 750  ? 44.522 78.416  -39.406 1.00 14.13 ? 750  GLY A CA  1 
ATOM   6073 C  C   . GLY A 1 750  ? 44.740 77.040  -39.972 1.00 12.07 ? 750  GLY A C   1 
ATOM   6074 O  O   . GLY A 1 750  ? 43.824 76.180  -39.870 1.00 15.10 ? 750  GLY A O   1 
ATOM   6075 N  N   . LYS A 1 751  ? 45.940 76.840  -40.532 1.00 13.53 ? 751  LYS A N   1 
ATOM   6076 C  CA  . LYS A 1 751  ? 46.225 75.535  -41.109 1.00 13.56 ? 751  LYS A CA  1 
ATOM   6077 C  C   . LYS A 1 751  ? 46.361 74.445  -40.048 1.00 12.77 ? 751  LYS A C   1 
ATOM   6078 O  O   . LYS A 1 751  ? 45.983 73.301  -40.312 1.00 14.16 ? 751  LYS A O   1 
ATOM   6079 C  CB  . LYS A 1 751  ? 47.490 75.601  -41.962 1.00 18.01 ? 751  LYS A CB  1 
ATOM   6080 C  CG  . LYS A 1 751  ? 47.811 74.248  -42.558 1.00 28.01 ? 751  LYS A CG  1 
ATOM   6081 C  CD  . LYS A 1 751  ? 48.425 74.313  -43.962 1.00 34.34 ? 751  LYS A CD  1 
ATOM   6082 C  CE  . LYS A 1 751  ? 48.796 72.896  -44.430 1.00 37.54 ? 751  LYS A CE  1 
ATOM   6083 N  NZ  . LYS A 1 751  ? 47.629 71.924  -44.341 1.00 44.01 ? 751  LYS A NZ  1 
ATOM   6084 N  N   . LEU A 1 752  ? 46.934 74.788  -38.897 1.00 12.21 ? 752  LEU A N   1 
ATOM   6085 C  CA  . LEU A 1 752  ? 47.147 73.808  -37.796 1.00 10.89 ? 752  LEU A CA  1 
ATOM   6086 C  C   . LEU A 1 752  ? 46.065 73.845  -36.729 1.00 12.34 ? 752  LEU A C   1 
ATOM   6087 O  O   . LEU A 1 752  ? 45.760 72.823  -36.123 1.00 12.48 ? 752  LEU A O   1 
ATOM   6088 C  CB  . LEU A 1 752  ? 48.488 74.058  -37.091 1.00 12.49 ? 752  LEU A CB  1 
ATOM   6089 C  CG  . LEU A 1 752  ? 49.685 73.998  -38.057 1.00 15.60 ? 752  LEU A CG  1 
ATOM   6090 C  CD1 . LEU A 1 752  ? 50.965 74.122  -37.233 1.00 16.06 ? 752  LEU A CD1 1 
ATOM   6091 C  CD2 . LEU A 1 752  ? 49.640 72.784  -38.954 1.00 19.35 ? 752  LEU A CD2 1 
ATOM   6092 N  N   . GLU A 1 753  ? 45.433 74.993  -36.504 1.00 11.66 ? 753  GLU A N   1 
ATOM   6093 C  CA  . GLU A 1 753  ? 44.468 75.134  -35.444 1.00 12.83 ? 753  GLU A CA  1 
ATOM   6094 C  C   . GLU A 1 753  ? 43.468 76.236  -35.804 1.00 12.87 ? 753  GLU A C   1 
ATOM   6095 O  O   . GLU A 1 753  ? 43.883 77.353  -36.218 1.00 13.43 ? 753  GLU A O   1 
ATOM   6096 C  CB  . GLU A 1 753  ? 45.208 75.513  -34.121 1.00 12.18 ? 753  GLU A CB  1 
ATOM   6097 C  CG  . GLU A 1 753  ? 44.256 75.704  -32.917 1.00 13.59 ? 753  GLU A CG  1 
ATOM   6098 C  CD  . GLU A 1 753  ? 44.965 76.134  -31.645 1.00 19.51 ? 753  GLU A CD  1 
ATOM   6099 O  OE1 . GLU A 1 753  ? 45.228 77.347  -31.501 1.00 26.12 ? 753  GLU A OE1 1 
ATOM   6100 O  OE2 . GLU A 1 753  ? 45.232 75.241  -30.813 1.00 25.68 ? 753  GLU A OE2 1 
ATOM   6101 N  N   . SER A 1 754  ? 42.209 75.949  -35.627 1.00 10.84 ? 754  SER A N   1 
ATOM   6102 C  CA  . SER A 1 754  ? 41.134 76.909  -35.822 1.00 10.18 ? 754  SER A CA  1 
ATOM   6103 C  C   . SER A 1 754  ? 40.271 76.919  -34.583 1.00 9.86  ? 754  SER A C   1 
ATOM   6104 O  O   . SER A 1 754  ? 40.281 75.980  -33.747 1.00 11.56 ? 754  SER A O   1 
ATOM   6105 C  CB  . SER A 1 754  ? 40.289 76.534  -37.015 1.00 12.17 ? 754  SER A CB  1 
ATOM   6106 O  OG  . SER A 1 754  ? 41.072 76.692  -38.193 1.00 12.23 ? 754  SER A OG  1 
ATOM   6107 N  N   . SER A 1 755  ? 39.487 77.970  -34.360 1.00 9.96  ? 755  SER A N   1 
ATOM   6108 C  CA  . SER A 1 755  ? 38.625 78.021  -33.208 1.00 11.26 ? 755  SER A CA  1 
ATOM   6109 C  C   . SER A 1 755  ? 37.472 78.978  -33.348 1.00 10.21 ? 755  SER A C   1 
ATOM   6110 O  O   . SER A 1 755  ? 37.547 79.961  -34.171 1.00 11.17 ? 755  SER A O   1 
ATOM   6111 C  CB  . SER A 1 755  ? 39.426 78.406  -31.961 1.00 16.08 ? 755  SER A CB  1 
ATOM   6112 O  OG  . SER A 1 755  ? 39.930 79.707  -32.103 1.00 17.15 ? 755  SER A OG  1 
ATOM   6113 N  N   . VAL A 1 756  ? 36.417 78.764  -32.599 1.00 9.18  ? 756  VAL A N   1 
ATOM   6114 C  CA  . VAL A 1 756  ? 35.293 79.674  -32.511 1.00 10.15 ? 756  VAL A CA  1 
ATOM   6115 C  C   . VAL A 1 756  ? 35.126 79.994  -31.026 1.00 9.85  ? 756  VAL A C   1 
ATOM   6116 O  O   . VAL A 1 756  ? 34.953 79.039  -30.193 1.00 11.37 ? 756  VAL A O   1 
ATOM   6117 C  CB  . VAL A 1 756  ? 33.990 79.046  -33.071 1.00 10.64 ? 756  VAL A CB  1 
ATOM   6118 C  CG1 . VAL A 1 756  ? 32.775 79.974  -32.805 1.00 11.43 ? 756  VAL A CG1 1 
ATOM   6119 C  CG2 . VAL A 1 756  ? 34.199 78.721  -34.540 1.00 13.21 ? 756  VAL A CG2 1 
ATOM   6120 N  N   . SER A 1 757  ? 35.101 81.262  -30.632 1.00 9.51  ? 757  SER A N   1 
ATOM   6121 C  CA  . SER A 1 757  ? 34.959 81.636  -29.241 1.00 9.22  ? 757  SER A CA  1 
ATOM   6122 C  C   . SER A 1 757  ? 33.832 82.607  -29.122 1.00 10.58 ? 757  SER A C   1 
ATOM   6123 O  O   . SER A 1 757  ? 33.712 83.490  -30.001 1.00 12.86 ? 757  SER A O   1 
ATOM   6124 C  CB  . SER A 1 757  ? 36.262 82.328  -28.738 1.00 11.54 ? 757  SER A CB  1 
ATOM   6125 O  OG  . SER A 1 757  ? 37.393 81.452  -28.905 1.00 14.86 ? 757  SER A OG  1 
ATOM   6126 N  N   . VAL A 1 758  ? 33.035 82.543  -28.083 1.00 10.09 ? 758  VAL A N   1 
ATOM   6127 C  CA  . VAL A 1 758  ? 31.907 83.468  -27.927 1.00 10.22 ? 758  VAL A CA  1 
ATOM   6128 C  C   . VAL A 1 758  ? 31.802 83.915  -26.493 1.00 10.83 ? 758  VAL A C   1 
ATOM   6129 O  O   . VAL A 1 758  ? 31.970 83.107  -25.535 1.00 10.82 ? 758  VAL A O   1 
ATOM   6130 C  CB  . VAL A 1 758  ? 30.628 82.819  -28.458 1.00 11.11 ? 758  VAL A CB  1 
ATOM   6131 C  CG1 . VAL A 1 758  ? 30.317 81.463  -27.770 1.00 12.16 ? 758  VAL A CG1 1 
ATOM   6132 C  CG2 . VAL A 1 758  ? 29.485 83.769  -28.254 1.00 12.49 ? 758  VAL A CG2 1 
ATOM   6133 N  N   . GLY A 1 759  ? 31.557 85.211  -26.294 1.00 10.72 ? 759  GLY A N   1 
ATOM   6134 C  CA  . GLY A 1 759  ? 31.423 85.771  -24.965 1.00 10.91 ? 759  GLY A CA  1 
ATOM   6135 C  C   . GLY A 1 759  ? 29.992 85.734  -24.507 1.00 13.00 ? 759  GLY A C   1 
ATOM   6136 O  O   . GLY A 1 759  ? 29.145 86.596  -24.835 1.00 13.01 ? 759  GLY A O   1 
ATOM   6137 N  N   . LEU A 1 760  ? 29.622 84.717  -23.771 1.00 12.77 ? 760  LEU A N   1 
ATOM   6138 C  CA  . LEU A 1 760  ? 28.259 84.562  -23.240 1.00 12.12 ? 760  LEU A CA  1 
ATOM   6139 C  C   . LEU A 1 760  ? 28.173 85.057  -21.841 1.00 11.83 ? 760  LEU A C   1 
ATOM   6140 O  O   . LEU A 1 760  ? 29.221 85.247  -21.168 1.00 14.37 ? 760  LEU A O   1 
ATOM   6141 C  CB  . LEU A 1 760  ? 27.889 83.036  -23.235 1.00 13.96 ? 760  LEU A CB  1 
ATOM   6142 C  CG  . LEU A 1 760  ? 28.065 82.335  -24.571 1.00 13.97 ? 760  LEU A CG  1 
ATOM   6143 C  CD1 . LEU A 1 760  ? 27.783 80.831  -24.383 1.00 16.95 ? 760  LEU A CD1 1 
ATOM   6144 C  CD2 . LEU A 1 760  ? 27.111 82.907  -25.673 1.00 18.55 ? 760  LEU A CD2 1 
ATOM   6145 N  N   . PRO A 1 761  ? 26.979 85.280  -21.301 1.00 14.47 ? 761  PRO A N   1 
ATOM   6146 C  CA  . PRO A 1 761  ? 26.926 85.738  -19.899 1.00 15.27 ? 761  PRO A CA  1 
ATOM   6147 C  C   . PRO A 1 761  ? 27.492 84.582  -19.019 1.00 15.48 ? 761  PRO A C   1 
ATOM   6148 O  O   . PRO A 1 761  ? 27.050 83.404  -19.105 1.00 17.34 ? 761  PRO A O   1 
ATOM   6149 C  CB  . PRO A 1 761  ? 25.422 85.972  -19.638 1.00 17.18 ? 761  PRO A CB  1 
ATOM   6150 C  CG  . PRO A 1 761  ? 24.870 86.205  -21.012 1.00 17.37 ? 761  PRO A CG  1 
ATOM   6151 C  CD  . PRO A 1 761  ? 25.642 85.294  -21.928 1.00 17.53 ? 761  PRO A CD  1 
ATOM   6152 N  N   . SER A 1 762  ? 28.481 84.959  -18.222 1.00 13.81 ? 762  SER A N   1 
ATOM   6153 C  CA  . SER A 1 762  ? 29.213 84.097  -17.297 1.00 12.88 ? 762  SER A CA  1 
ATOM   6154 C  C   . SER A 1 762  ? 30.152 83.112  -17.946 1.00 11.96 ? 762  SER A C   1 
ATOM   6155 O  O   . SER A 1 762  ? 30.824 82.394  -17.180 1.00 12.48 ? 762  SER A O   1 
ATOM   6156 C  CB  . SER A 1 762  ? 28.290 83.258  -16.409 1.00 16.39 ? 762  SER A CB  1 
ATOM   6157 O  OG  . SER A 1 762  ? 27.393 84.048  -15.677 1.00 19.32 ? 762  SER A OG  1 
ATOM   6158 N  N   . VAL A 1 763  ? 30.218 82.993  -19.255 1.00 11.53 ? 763  VAL A N   1 
ATOM   6159 C  CA  . VAL A 1 763  ? 31.120 82.016  -19.848 1.00 10.45 ? 763  VAL A CA  1 
ATOM   6160 C  C   . VAL A 1 763  ? 31.711 82.448  -21.158 1.00 11.41 ? 763  VAL A C   1 
ATOM   6161 O  O   . VAL A 1 763  ? 30.953 82.805  -22.073 1.00 12.46 ? 763  VAL A O   1 
ATOM   6162 C  CB  . VAL A 1 763  ? 30.374 80.669  -20.133 1.00 14.39 ? 763  VAL A CB  1 
ATOM   6163 C  CG1 . VAL A 1 763  ? 31.342 79.633  -20.676 1.00 13.15 ? 763  VAL A CG1 1 
ATOM   6164 C  CG2 . VAL A 1 763  ? 29.661 80.139  -18.935 1.00 15.65 ? 763  VAL A CG2 1 
ATOM   6165 N  N   . VAL A 1 764  ? 33.038 82.440  -21.305 1.00 9.51  ? 764  VAL A N   1 
ATOM   6166 C  CA  . VAL A 1 764  ? 33.608 82.626  -22.631 1.00 9.20  ? 764  VAL A CA  1 
ATOM   6167 C  C   . VAL A 1 764  ? 33.782 81.154  -23.074 1.00 10.38 ? 764  VAL A C   1 
ATOM   6168 O  O   . VAL A 1 764  ? 34.608 80.386  -22.495 1.00 9.74  ? 764  VAL A O   1 
ATOM   6169 C  CB  . VAL A 1 764  ? 34.976 83.368  -22.643 1.00 10.16 ? 764  VAL A CB  1 
ATOM   6170 C  CG1 . VAL A 1 764  ? 35.539 83.474  -24.096 1.00 12.43 ? 764  VAL A CG1 1 
ATOM   6171 C  CG2 . VAL A 1 764  ? 34.732 84.765  -22.035 1.00 12.49 ? 764  VAL A CG2 1 
ATOM   6172 N  N   . HIS A 1 765  ? 33.036 80.762  -24.090 1.00 9.19  ? 765  HIS A N   1 
ATOM   6173 C  CA  . HIS A 1 765  ? 32.948 79.361  -24.573 1.00 9.19  ? 765  HIS A CA  1 
ATOM   6174 C  C   . HIS A 1 765  ? 33.792 79.240  -25.821 1.00 10.70 ? 765  HIS A C   1 
ATOM   6175 O  O   . HIS A 1 765  ? 33.617 80.064  -26.760 1.00 10.84 ? 765  HIS A O   1 
ATOM   6176 C  CB  . HIS A 1 765  ? 31.475 79.036  -24.895 1.00 10.12 ? 765  HIS A CB  1 
ATOM   6177 C  CG  . HIS A 1 765  ? 31.261 77.683  -25.460 1.00 9.00  ? 765  HIS A CG  1 
ATOM   6178 N  ND1 . HIS A 1 765  ? 30.738 77.400  -26.713 1.00 13.99 ? 765  HIS A ND1 1 
ATOM   6179 C  CD2 . HIS A 1 765  ? 31.472 76.476  -24.874 1.00 7.20  ? 765  HIS A CD2 1 
ATOM   6180 C  CE1 . HIS A 1 765  ? 30.644 76.081  -26.875 1.00 8.04  ? 765  HIS A CE1 1 
ATOM   6181 N  NE2 . HIS A 1 765  ? 31.093 75.500  -25.764 1.00 13.67 ? 765  HIS A NE2 1 
ATOM   6182 N  N   A GLN A 1 766  ? 34.679 78.273  -25.921 0.50 9.35  ? 766  GLN A N   1 
ATOM   6183 N  N   B GLN A 1 766  ? 34.679 78.273  -25.921 0.50 9.52  ? 766  GLN A N   1 
ATOM   6184 C  CA  A GLN A 1 766  ? 35.585 78.136  -27.038 0.50 10.20 ? 766  GLN A CA  1 
ATOM   6185 C  CA  B GLN A 1 766  ? 35.585 78.136  -27.038 0.50 10.15 ? 766  GLN A CA  1 
ATOM   6186 C  C   A GLN A 1 766  ? 35.619 76.721  -27.550 0.50 10.14 ? 766  GLN A C   1 
ATOM   6187 C  C   B GLN A 1 766  ? 35.619 76.721  -27.550 0.50 10.33 ? 766  GLN A C   1 
ATOM   6188 O  O   A GLN A 1 766  ? 35.752 75.768  -26.768 0.50 10.83 ? 766  GLN A O   1 
ATOM   6189 O  O   B GLN A 1 766  ? 35.752 75.768  -26.768 0.50 11.05 ? 766  GLN A O   1 
ATOM   6190 C  CB  A GLN A 1 766  ? 37.040 78.528  -26.631 0.50 10.92 ? 766  GLN A CB  1 
ATOM   6191 C  CB  B GLN A 1 766  ? 37.040 78.528  -26.631 0.50 10.30 ? 766  GLN A CB  1 
ATOM   6192 C  CG  A GLN A 1 766  ? 37.165 79.856  -25.865 0.50 13.19 ? 766  GLN A CG  1 
ATOM   6193 C  CG  B GLN A 1 766  ? 38.094 78.349  -27.737 0.50 11.59 ? 766  GLN A CG  1 
ATOM   6194 C  CD  A GLN A 1 766  ? 38.201 79.838  -24.667 0.50 18.39 ? 766  GLN A CD  1 
ATOM   6195 C  CD  B GLN A 1 766  ? 39.537 78.895  -27.375 0.50 16.17 ? 766  GLN A CD  1 
ATOM   6196 O  OE1 A GLN A 1 766  ? 39.378 79.492  -24.894 0.50 14.43 ? 766  GLN A OE1 1 
ATOM   6197 O  OE1 B GLN A 1 766  ? 40.303 79.230  -28.300 0.50 16.75 ? 766  GLN A OE1 1 
ATOM   6198 N  NE2 A GLN A 1 766  ? 37.747 80.200  -23.380 0.50 11.73 ? 766  GLN A NE2 1 
ATOM   6199 N  NE2 B GLN A 1 766  ? 39.907 78.966  -26.014 0.50 17.99 ? 766  GLN A NE2 1 
ATOM   6200 N  N   . THR A 1 767  ? 35.507 76.564  -28.857 1.00 8.80  ? 767  THR A N   1 
ATOM   6201 C  CA  . THR A 1 767  ? 35.642 75.286  -29.537 1.00 9.63  ? 767  THR A CA  1 
ATOM   6202 C  C   . THR A 1 767  ? 36.891 75.318  -30.373 1.00 9.63  ? 767  THR A C   1 
ATOM   6203 O  O   . THR A 1 767  ? 36.971 76.203  -31.274 1.00 11.72 ? 767  THR A O   1 
ATOM   6204 C  CB  . THR A 1 767  ? 34.428 74.979  -30.411 1.00 10.20 ? 767  THR A CB  1 
ATOM   6205 O  OG1 . THR A 1 767  ? 33.253 75.070  -29.635 1.00 13.01 ? 767  THR A OG1 1 
ATOM   6206 C  CG2 . THR A 1 767  ? 34.553 73.589  -31.018 1.00 11.68 ? 767  THR A CG2 1 
ATOM   6207 N  N   . ILE A 1 768  ? 37.888 74.477  -30.126 1.00 9.90  ? 768  ILE A N   1 
ATOM   6208 C  CA  . ILE A 1 768  ? 39.166 74.456  -30.789 1.00 9.71  ? 768  ILE A CA  1 
ATOM   6209 C  C   . ILE A 1 768  ? 39.337 73.214  -31.616 1.00 11.15 ? 768  ILE A C   1 
ATOM   6210 O  O   . ILE A 1 768  ? 39.053 72.099  -31.110 1.00 11.31 ? 768  ILE A O   1 
ATOM   6211 C  CB  . ILE A 1 768  ? 40.279 74.597  -29.746 1.00 10.36 ? 768  ILE A CB  1 
ATOM   6212 C  CG1 . ILE A 1 768  ? 40.066 75.852  -28.893 1.00 13.16 ? 768  ILE A CG1 1 
ATOM   6213 C  CG2 . ILE A 1 768  ? 41.612 74.666  -30.444 1.00 13.79 ? 768  ILE A CG2 1 
ATOM   6214 C  CD1 . ILE A 1 768  ? 40.999 75.847  -27.593 1.00 14.87 ? 768  ILE A CD1 1 
ATOM   6215 N  N   A MET A 1 769  ? 39.817 73.361  -32.830 0.50 11.12 ? 769  MET A N   1 
ATOM   6216 N  N   B MET A 1 769  ? 39.817 73.361  -32.830 0.50 10.89 ? 769  MET A N   1 
ATOM   6217 C  CA  A MET A 1 769  ? 39.960 72.262  -33.798 0.50 11.41 ? 769  MET A CA  1 
ATOM   6218 C  CA  B MET A 1 769  ? 39.960 72.262  -33.798 0.50 10.78 ? 769  MET A CA  1 
ATOM   6219 C  C   A MET A 1 769  ? 41.388 72.139  -34.207 0.50 12.19 ? 769  MET A C   1 
ATOM   6220 C  C   B MET A 1 769  ? 41.388 72.139  -34.207 0.50 11.95 ? 769  MET A C   1 
ATOM   6221 O  O   A MET A 1 769  ? 42.008 73.097  -34.686 0.50 11.92 ? 769  MET A O   1 
ATOM   6222 O  O   B MET A 1 769  ? 42.008 73.097  -34.686 0.50 11.81 ? 769  MET A O   1 
ATOM   6223 C  CB  A MET A 1 769  ? 39.104 72.563  -35.034 0.50 14.29 ? 769  MET A CB  1 
ATOM   6224 C  CB  B MET A 1 769  ? 39.104 72.563  -35.034 0.50 13.06 ? 769  MET A CB  1 
ATOM   6225 C  CG  A MET A 1 769  ? 37.662 72.565  -34.668 0.50 14.96 ? 769  MET A CG  1 
ATOM   6226 C  CG  B MET A 1 769  ? 37.662 72.565  -34.668 0.50 11.03 ? 769  MET A CG  1 
ATOM   6227 S  SD  A MET A 1 769  ? 36.606 73.290  -35.921 0.50 22.20 ? 769  MET A SD  1 
ATOM   6228 S  SD  B MET A 1 769  ? 36.606 73.290  -35.921 0.50 14.83 ? 769  MET A SD  1 
ATOM   6229 C  CE  A MET A 1 769  ? 36.573 75.052  -35.127 0.50 21.85 ? 769  MET A CE  1 
ATOM   6230 C  CE  B MET A 1 769  ? 36.940 71.923  -37.246 0.50 14.54 ? 769  MET A CE  1 
ATOM   6231 N  N   . ARG A 1 770  ? 41.939 70.939  -34.092 1.00 12.27 ? 770  ARG A N   1 
ATOM   6232 C  CA  . ARG A 1 770  ? 43.286 70.664  -34.488 1.00 11.87 ? 770  ARG A CA  1 
ATOM   6233 C  C   . ARG A 1 770  ? 43.399 69.489  -35.436 1.00 13.95 ? 770  ARG A C   1 
ATOM   6234 O  O   . ARG A 1 770  ? 44.520 69.006  -35.665 1.00 18.19 ? 770  ARG A O   1 
ATOM   6235 C  CB  . ARG A 1 770  ? 44.198 70.477  -33.281 1.00 13.05 ? 770  ARG A CB  1 
ATOM   6236 C  CG  . ARG A 1 770  ? 44.264 71.715  -32.406 1.00 16.27 ? 770  ARG A CG  1 
ATOM   6237 C  CD  . ARG A 1 770  ? 45.106 71.449  -31.166 1.00 19.18 ? 770  ARG A CD  1 
ATOM   6238 N  NE  . ARG A 1 770  ? 45.159 72.602  -30.303 1.00 24.89 ? 770  ARG A NE  1 
ATOM   6239 C  CZ  . ARG A 1 770  ? 44.522 72.663  -29.141 1.00 27.15 ? 770  ARG A CZ  1 
ATOM   6240 N  NH1 . ARG A 1 770  ? 43.783 71.633  -28.739 1.00 30.89 ? 770  ARG A NH1 1 
ATOM   6241 N  NH2 . ARG A 1 770  ? 44.672 73.724  -28.352 1.00 34.58 ? 770  ARG A NH2 1 
ATOM   6242 N  N   . GLY A 1 771  ? 42.258 69.045  -35.925 1.00 13.95 ? 771  GLY A N   1 
ATOM   6243 C  CA  . GLY A 1 771  ? 42.295 67.967  -36.883 1.00 17.42 ? 771  GLY A CA  1 
ATOM   6244 C  C   . GLY A 1 771  ? 41.662 66.697  -36.413 1.00 19.62 ? 771  GLY A C   1 
ATOM   6245 O  O   . GLY A 1 771  ? 41.485 65.797  -37.246 1.00 20.64 ? 771  GLY A O   1 
ATOM   6246 N  N   . GLY A 1 772  ? 41.326 66.607  -35.120 1.00 16.69 ? 772  GLY A N   1 
ATOM   6247 C  CA  . GLY A 1 772  ? 40.672 65.412  -34.549 1.00 19.18 ? 772  GLY A CA  1 
ATOM   6248 C  C   . GLY A 1 772  ? 39.452 65.903  -33.761 1.00 17.24 ? 772  GLY A C   1 
ATOM   6249 O  O   . GLY A 1 772  ? 38.857 66.940  -34.088 1.00 14.64 ? 772  GLY A O   1 
ATOM   6250 N  N   . ALA A 1 773  ? 39.025 65.166  -32.730 1.00 14.03 ? 773  ALA A N   1 
ATOM   6251 C  CA  . ALA A 1 773  ? 37.912 65.634  -31.910 1.00 12.94 ? 773  ALA A CA  1 
ATOM   6252 C  C   . ALA A 1 773  ? 38.218 67.030  -31.351 1.00 11.79 ? 773  ALA A C   1 
ATOM   6253 O  O   . ALA A 1 773  ? 39.348 67.312  -30.931 1.00 11.39 ? 773  ALA A O   1 
ATOM   6254 C  CB  . ALA A 1 773  ? 37.659 64.695  -30.761 1.00 14.04 ? 773  ALA A CB  1 
ATOM   6255 N  N   . PRO A 1 774  ? 37.234 67.903  -31.341 1.00 10.08 ? 774  PRO A N   1 
ATOM   6256 C  CA  . PRO A 1 774  ? 37.508 69.267  -30.821 1.00 10.35 ? 774  PRO A CA  1 
ATOM   6257 C  C   . PRO A 1 774  ? 37.815 69.293  -29.324 1.00 9.17  ? 774  PRO A C   1 
ATOM   6258 O  O   . PRO A 1 774  ? 37.458 68.359  -28.560 1.00 10.10 ? 774  PRO A O   1 
ATOM   6259 C  CB  . PRO A 1 774  ? 36.188 70.028  -31.088 1.00 12.05 ? 774  PRO A CB  1 
ATOM   6260 C  CG  . PRO A 1 774  ? 35.168 68.983  -31.212 1.00 16.43 ? 774  PRO A CG  1 
ATOM   6261 C  CD  . PRO A 1 774  ? 35.864 67.753  -31.855 1.00 10.84 ? 774  PRO A CD  1 
ATOM   6262 N  N   . GLU A 1 775  ? 38.435 70.370  -28.906 1.00 10.26 ? 775  GLU A N   1 
ATOM   6263 C  CA  . GLU A 1 775  ? 38.689 70.660  -27.520 1.00 9.42  ? 775  GLU A CA  1 
ATOM   6264 C  C   . GLU A 1 775  ? 37.736 71.782  -27.172 1.00 8.99  ? 775  GLU A C   1 
ATOM   6265 O  O   . GLU A 1 775  ? 37.522 72.731  -28.004 1.00 11.63 ? 775  GLU A O   1 
ATOM   6266 C  CB  . GLU A 1 775  ? 40.119 71.114  -27.309 1.00 10.14 ? 775  GLU A CB  1 
ATOM   6267 C  CG  . GLU A 1 775  ? 40.425 71.587  -25.801 1.00 11.90 ? 775  GLU A CG  1 
ATOM   6268 C  CD  . GLU A 1 775  ? 41.856 71.996  -25.547 1.00 18.23 ? 775  GLU A CD  1 
ATOM   6269 O  OE1 . GLU A 1 775  ? 42.722 71.856  -26.421 1.00 27.56 ? 775  GLU A OE1 1 
ATOM   6270 O  OE2 . GLU A 1 775  ? 42.149 72.496  -24.434 1.00 17.02 ? 775  GLU A OE2 1 
ATOM   6271 N  N   . ILE A 1 776  ? 37.068 71.727  -26.061 1.00 8.68  ? 776  ILE A N   1 
ATOM   6272 C  CA  . ILE A 1 776  ? 36.186 72.779  -25.591 1.00 9.63  ? 776  ILE A CA  1 
ATOM   6273 C  C   . ILE A 1 776  ? 36.833 73.422  -24.381 1.00 9.40  ? 776  ILE A C   1 
ATOM   6274 O  O   . ILE A 1 776  ? 37.324 72.692  -23.475 1.00 9.52  ? 776  ILE A O   1 
ATOM   6275 C  CB  . ILE A 1 776  ? 34.788 72.229  -25.160 1.00 10.04 ? 776  ILE A CB  1 
ATOM   6276 C  CG1 . ILE A 1 776  ? 34.176 71.310  -26.241 1.00 14.16 ? 776  ILE A CG1 1 
ATOM   6277 C  CG2 . ILE A 1 776  ? 33.907 73.384  -24.744 1.00 12.10 ? 776  ILE A CG2 1 
ATOM   6278 C  CD1 . ILE A 1 776  ? 34.073 71.864  -27.680 1.00 16.16 ? 776  ILE A CD1 1 
ATOM   6279 N  N   . ARG A 1 777  ? 36.884 74.739  -24.325 1.00 9.41  ? 777  ARG A N   1 
ATOM   6280 C  CA  . ARG A 1 777  ? 37.351 75.447  -23.110 1.00 9.75  ? 777  ARG A CA  1 
ATOM   6281 C  C   . ARG A 1 777  ? 36.288 76.432  -22.662 1.00 9.64  ? 777  ARG A C   1 
ATOM   6282 O  O   . ARG A 1 777  ? 35.774 77.219  -23.520 1.00 10.63 ? 777  ARG A O   1 
ATOM   6283 C  CB  . ARG A 1 777  ? 38.674 76.197  -23.339 1.00 10.74 ? 777  ARG A CB  1 
ATOM   6284 C  CG  . ARG A 1 777  ? 39.811 75.310  -23.730 1.00 10.19 ? 777  ARG A CG  1 
ATOM   6285 C  CD  . ARG A 1 777  ? 41.100 76.091  -23.870 1.00 11.54 ? 777  ARG A CD  1 
ATOM   6286 N  NE  . ARG A 1 777  ? 42.166 75.214  -24.344 1.00 13.27 ? 777  ARG A NE  1 
ATOM   6287 C  CZ  . ARG A 1 777  ? 43.361 75.648  -24.766 1.00 14.95 ? 777  ARG A CZ  1 
ATOM   6288 N  NH1 . ARG A 1 777  ? 43.621 76.978  -24.702 1.00 19.28 ? 777  ARG A NH1 1 
ATOM   6289 N  NH2 . ARG A 1 777  ? 44.259 74.835  -25.343 1.00 16.65 ? 777  ARG A NH2 1 
ATOM   6290 N  N   . ASN A 1 778  ? 35.900 76.432  -21.412 1.00 8.75  ? 778  ASN A N   1 
ATOM   6291 C  CA  . ASN A 1 778  ? 34.989 77.405  -20.896 1.00 8.74  ? 778  ASN A CA  1 
ATOM   6292 C  C   . ASN A 1 778  ? 35.680 78.234  -19.822 1.00 8.16  ? 778  ASN A C   1 
ATOM   6293 O  O   . ASN A 1 778  ? 36.124 77.671  -18.782 1.00 8.45  ? 778  ASN A O   1 
ATOM   6294 C  CB  . ASN A 1 778  ? 33.767 76.749  -20.217 1.00 10.45 ? 778  ASN A CB  1 
ATOM   6295 C  CG  . ASN A 1 778  ? 32.819 76.078  -21.191 1.00 10.24 ? 778  ASN A CG  1 
ATOM   6296 O  OD1 . ASN A 1 778  ? 32.758 76.457  -22.370 1.00 10.96 ? 778  ASN A OD1 1 
ATOM   6297 N  ND2 . ASN A 1 778  ? 32.050 75.117  -20.675 1.00 10.69 ? 778  ASN A ND2 1 
ATOM   6298 N  N   . LEU A 1 779  ? 35.717 79.563  -20.008 1.00 8.60  ? 779  LEU A N   1 
ATOM   6299 C  CA  . LEU A 1 779  ? 36.244 80.441  -18.930 1.00 8.62  ? 779  LEU A CA  1 
ATOM   6300 C  C   . LEU A 1 779  ? 34.998 80.847  -18.180 1.00 8.28  ? 779  LEU A C   1 
ATOM   6301 O  O   . LEU A 1 779  ? 34.155 81.659  -18.700 1.00 10.21 ? 779  LEU A O   1 
ATOM   6302 C  CB  . LEU A 1 779  ? 37.017 81.632  -19.540 1.00 10.76 ? 779  LEU A CB  1 
ATOM   6303 C  CG  . LEU A 1 779  ? 37.531 82.613  -18.471 1.00 13.14 ? 779  LEU A CG  1 
ATOM   6304 C  CD1 . LEU A 1 779  ? 38.598 82.019  -17.612 1.00 16.88 ? 779  LEU A CD1 1 
ATOM   6305 C  CD2 . LEU A 1 779  ? 38.036 83.865  -19.302 1.00 20.46 ? 779  LEU A CD2 1 
ATOM   6306 N  N   . VAL A 1 780  ? 34.826 80.252  -17.000 1.00 9.21  ? 780  VAL A N   1 
ATOM   6307 C  CA  . VAL A 1 780  ? 33.587 80.441  -16.262 1.00 10.30 ? 780  VAL A CA  1 
ATOM   6308 C  C   . VAL A 1 780  ? 33.711 81.439  -15.134 1.00 9.01  ? 780  VAL A C   1 
ATOM   6309 O  O   . VAL A 1 780  ? 34.502 81.225  -14.229 1.00 10.91 ? 780  VAL A O   1 
ATOM   6310 C  CB  . VAL A 1 780  ? 33.080 79.046  -15.688 1.00 9.44  ? 780  VAL A CB  1 
ATOM   6311 C  CG1 . VAL A 1 780  ? 31.739 79.204  -14.958 1.00 11.55 ? 780  VAL A CG1 1 
ATOM   6312 C  CG2 . VAL A 1 780  ? 32.969 78.034  -16.827 1.00 10.12 ? 780  VAL A CG2 1 
ATOM   6313 N  N   . ASP A 1 781  ? 32.953 82.533  -15.222 1.00 10.03 ? 781  ASP A N   1 
ATOM   6314 C  CA  . ASP A 1 781  ? 32.932 83.547  -14.156 1.00 11.33 ? 781  ASP A CA  1 
ATOM   6315 C  C   . ASP A 1 781  ? 31.501 83.859  -13.794 1.00 11.83 ? 781  ASP A C   1 
ATOM   6316 O  O   . ASP A 1 781  ? 30.817 84.706  -14.470 1.00 12.18 ? 781  ASP A O   1 
ATOM   6317 C  CB  . ASP A 1 781  ? 33.634 84.814  -14.634 1.00 14.61 ? 781  ASP A CB  1 
ATOM   6318 C  CG  . ASP A 1 781  ? 33.687 85.864  -13.553 1.00 16.24 ? 781  ASP A CG  1 
ATOM   6319 O  OD1 . ASP A 1 781  ? 34.211 86.965  -13.877 1.00 21.68 ? 781  ASP A OD1 1 
ATOM   6320 O  OD2 . ASP A 1 781  ? 33.245 85.662  -12.399 1.00 15.44 ? 781  ASP A OD2 1 
ATOM   6321 N  N   . ILE A 1 782  ? 30.976 83.158  -12.807 1.00 11.22 ? 782  ILE A N   1 
ATOM   6322 C  CA  . ILE A 1 782  ? 29.570 83.288  -12.403 1.00 12.62 ? 782  ILE A CA  1 
ATOM   6323 C  C   . ILE A 1 782  ? 29.327 84.646  -11.756 1.00 15.87 ? 782  ILE A C   1 
ATOM   6324 O  O   . ILE A 1 782  ? 28.153 85.055  -11.545 1.00 17.90 ? 782  ILE A O   1 
ATOM   6325 C  CB  . ILE A 1 782  ? 29.230 82.070  -11.529 1.00 13.70 ? 782  ILE A CB  1 
ATOM   6326 C  CG1 . ILE A 1 782  ? 27.731 81.918  -11.338 1.00 15.99 ? 782  ILE A CG1 1 
ATOM   6327 C  CG2 . ILE A 1 782  ? 29.975 82.224  -10.151 1.00 16.19 ? 782  ILE A CG2 1 
ATOM   6328 C  CD1 . ILE A 1 782  ? 27.453 80.458  -10.841 1.00 15.90 ? 782  ILE A CD1 1 
ATOM   6329 N  N   . GLY A 1 783  ? 30.388 85.379  -11.424 1.00 15.99 ? 783  GLY A N   1 
ATOM   6330 C  CA  . GLY A 1 783  ? 30.186 86.777  -10.987 1.00 16.11 ? 783  GLY A CA  1 
ATOM   6331 C  C   . GLY A 1 783  ? 29.361 86.912  -9.745  1.00 17.56 ? 783  GLY A C   1 
ATOM   6332 O  O   . GLY A 1 783  ? 29.591 86.174  -8.762  1.00 21.24 ? 783  GLY A O   1 
ATOM   6333 N  N   . SER A 1 784  ? 28.369 87.791  -9.769  1.00 22.03 ? 784  SER A N   1 
ATOM   6334 C  CA  . SER A 1 784  ? 27.553 87.948  -8.571  1.00 22.52 ? 784  SER A CA  1 
ATOM   6335 C  C   . SER A 1 784  ? 26.163 87.318  -8.717  1.00 23.03 ? 784  SER A C   1 
ATOM   6336 O  O   . SER A 1 784  ? 25.203 87.729  -8.011  1.00 23.27 ? 784  SER A O   1 
ATOM   6337 C  CB  . SER A 1 784  ? 27.413 89.431  -8.204  1.00 26.71 ? 784  SER A CB  1 
ATOM   6338 O  OG  . SER A 1 784  ? 26.708 90.120  -9.218  1.00 34.16 ? 784  SER A OG  1 
ATOM   6339 N  N   . LEU A 1 785  ? 26.022 86.337  -9.606  1.00 21.18 ? 785  LEU A N   1 
ATOM   6340 C  CA  . LEU A 1 785  ? 24.714 85.704  -9.793  1.00 19.81 ? 785  LEU A CA  1 
ATOM   6341 C  C   . LEU A 1 785  ? 24.370 84.757  -8.633  1.00 23.41 ? 785  LEU A C   1 
ATOM   6342 O  O   . LEU A 1 785  ? 24.635 83.508  -8.675  1.00 22.72 ? 785  LEU A O   1 
ATOM   6343 C  CB  . LEU A 1 785  ? 24.693 84.932  -11.118 1.00 19.19 ? 785  LEU A CB  1 
ATOM   6344 C  CG  . LEU A 1 785  ? 24.932 85.727  -12.420 1.00 20.09 ? 785  LEU A CG  1 
ATOM   6345 C  CD1 . LEU A 1 785  ? 24.950 84.826  -13.593 1.00 24.88 ? 785  LEU A CD1 1 
ATOM   6346 C  CD2 . LEU A 1 785  ? 23.841 86.794  -12.587 1.00 22.30 ? 785  LEU A CD2 1 
ATOM   6347 N  N   . ASP A 1 786  ? 23.700 85.279  -7.612  1.00 23.00 ? 786  ASP A N   1 
ATOM   6348 C  CA  . ASP A 1 786  ? 23.398 84.434  -6.467  1.00 21.58 ? 786  ASP A CA  1 
ATOM   6349 C  C   . ASP A 1 786  ? 22.311 83.386  -6.796  1.00 14.57 ? 786  ASP A C   1 
ATOM   6350 O  O   . ASP A 1 786  ? 21.481 83.518  -7.694  1.00 18.06 ? 786  ASP A O   1 
ATOM   6351 C  CB  . ASP A 1 786  ? 22.922 85.248  -5.245  1.00 24.82 ? 786  ASP A CB  1 
ATOM   6352 C  CG  . ASP A 1 786  ? 24.054 85.918  -4.458  1.00 28.96 ? 786  ASP A CG  1 
ATOM   6353 O  OD1 . ASP A 1 786  ? 23.751 86.257  -3.296  1.00 32.84 ? 786  ASP A OD1 1 
ATOM   6354 O  OD2 . ASP A 1 786  ? 25.205 86.125  -4.945  1.00 27.31 ? 786  ASP A OD2 1 
ATOM   6355 N  N   . ASN A 1 787  ? 22.455 82.297  -6.077  1.00 15.96 ? 787  ASN A N   1 
ATOM   6356 C  CA  . ASN A 1 787  ? 21.542 81.169  -6.189  1.00 13.72 ? 787  ASN A CA  1 
ATOM   6357 C  C   . ASN A 1 787  ? 21.354 80.690  -7.592  1.00 14.97 ? 787  ASN A C   1 
ATOM   6358 O  O   . ASN A 1 787  ? 20.250 80.487  -8.084  1.00 15.43 ? 787  ASN A O   1 
ATOM   6359 C  CB  . ASN A 1 787  ? 20.206 81.518  -5.488  1.00 13.57 ? 787  ASN A CB  1 
ATOM   6360 C  CG  . ASN A 1 787  ? 20.387 81.665  -4.001  1.00 20.83 ? 787  ASN A CG  1 
ATOM   6361 O  OD1 . ASN A 1 787  ? 21.159 80.922  -3.373  1.00 20.94 ? 787  ASN A OD1 1 
ATOM   6362 N  ND2 . ASN A 1 787  ? 19.657 82.619  -3.403  1.00 28.51 ? 787  ASN A ND2 1 
ATOM   6363 N  N   . THR A 1 788  ? 22.470 80.460  -8.249  1.00 12.14 ? 788  THR A N   1 
ATOM   6364 C  CA  . THR A 1 788  ? 22.474 80.044  -9.636  1.00 13.01 ? 788  THR A CA  1 
ATOM   6365 C  C   . THR A 1 788  ? 23.507 78.914  -9.856  1.00 11.18 ? 788  THR A C   1 
ATOM   6366 O  O   . THR A 1 788  ? 24.614 79.012  -9.286  1.00 11.87 ? 788  THR A O   1 
ATOM   6367 C  CB  . THR A 1 788  ? 22.940 81.241  -10.555 1.00 15.02 ? 788  THR A CB  1 
ATOM   6368 O  OG1 . THR A 1 788  ? 21.970 82.319  -10.422 1.00 16.64 ? 788  THR A OG1 1 
ATOM   6369 C  CG2 . THR A 1 788  ? 22.948 80.829  -12.022 1.00 17.79 ? 788  THR A CG2 1 
ATOM   6370 N  N   . GLU A 1 789  ? 23.146 77.913  -10.637 1.00 10.24 ? 789  GLU A N   1 
ATOM   6371 C  CA  . GLU A 1 789  ? 24.110 76.874  -11.029 1.00 9.30  ? 789  GLU A CA  1 
ATOM   6372 C  C   . GLU A 1 789  ? 24.083 76.898  -12.543 1.00 9.56  ? 789  GLU A C   1 
ATOM   6373 O  O   . GLU A 1 789  ? 23.000 76.807  -13.179 1.00 12.77 ? 789  GLU A O   1 
ATOM   6374 C  CB  . GLU A 1 789  ? 23.719 75.477  -10.474 1.00 9.75  ? 789  GLU A CB  1 
ATOM   6375 C  CG  . GLU A 1 789  ? 23.302 75.511  -9.057  1.00 10.93 ? 789  GLU A CG  1 
ATOM   6376 C  CD  . GLU A 1 789  ? 23.500 74.227  -8.267  1.00 10.50 ? 789  GLU A CD  1 
ATOM   6377 O  OE1 . GLU A 1 789  ? 24.342 73.377  -8.762  1.00 11.46 ? 789  GLU A OE1 1 
ATOM   6378 O  OE2 . GLU A 1 789  ? 22.876 74.059  -7.215  1.00 11.37 ? 789  GLU A OE2 1 
ATOM   6379 N  N   . ILE A 1 790  ? 25.222 77.040  -13.197 1.00 8.54  ? 790  ILE A N   1 
ATOM   6380 C  CA  . ILE A 1 790  ? 25.331 77.093  -14.635 1.00 10.16 ? 790  ILE A CA  1 
ATOM   6381 C  C   . ILE A 1 790  ? 25.688 75.728  -15.177 1.00 9.73  ? 790  ILE A C   1 
ATOM   6382 O  O   . ILE A 1 790  ? 26.686 75.125  -14.743 1.00 10.28 ? 790  ILE A O   1 
ATOM   6383 C  CB  . ILE A 1 790  ? 26.425 78.099  -15.103 1.00 11.44 ? 790  ILE A CB  1 
ATOM   6384 C  CG1 . ILE A 1 790  ? 26.005 79.522  -14.692 1.00 15.96 ? 790  ILE A CG1 1 
ATOM   6385 C  CG2 . ILE A 1 790  ? 26.627 78.036  -16.608 1.00 13.03 ? 790  ILE A CG2 1 
ATOM   6386 C  CD1 . ILE A 1 790  ? 27.204 80.495  -14.783 1.00 23.12 ? 790  ILE A CD1 1 
ATOM   6387 N  N   . VAL A 1 791  ? 24.896 75.208  -16.093 1.00 10.61 ? 791  VAL A N   1 
ATOM   6388 C  CA  . VAL A 1 791  ? 25.119 73.917  -16.723 1.00 9.99  ? 791  VAL A CA  1 
ATOM   6389 C  C   . VAL A 1 791  ? 25.367 74.018  -18.186 1.00 10.29 ? 791  VAL A C   1 
ATOM   6390 O  O   . VAL A 1 791  ? 24.776 74.907  -18.897 1.00 10.40 ? 791  VAL A O   1 
ATOM   6391 C  CB  . VAL A 1 791  ? 23.908 72.970  -16.422 1.00 10.82 ? 791  VAL A CB  1 
ATOM   6392 C  CG1 . VAL A 1 791  ? 22.640 73.457  -17.220 1.00 13.98 ? 791  VAL A CG1 1 
ATOM   6393 C  CG2 . VAL A 1 791  ? 24.246 71.521  -16.769 1.00 12.58 ? 791  VAL A CG2 1 
ATOM   6394 N  N   . MET A 1 792  ? 26.258 73.215  -18.704 1.00 9.22  ? 792  MET A N   1 
ATOM   6395 C  CA  . MET A 1 792  ? 26.541 73.088  -20.128 1.00 8.62  ? 792  MET A CA  1 
ATOM   6396 C  C   . MET A 1 792  ? 25.870 71.786  -20.594 1.00 9.80  ? 792  MET A C   1 
ATOM   6397 O  O   . MET A 1 792  ? 26.208 70.685  -20.094 1.00 10.59 ? 792  MET A O   1 
ATOM   6398 C  CB  . MET A 1 792  ? 28.054 73.057  -20.437 1.00 10.25 ? 792  MET A CB  1 
ATOM   6399 C  CG  . MET A 1 792  ? 28.321 72.892  -21.916 1.00 10.41 ? 792  MET A CG  1 
ATOM   6400 S  SD  . MET A 1 792  ? 30.094 72.950  -22.300 1.00 10.98 ? 792  MET A SD  1 
ATOM   6401 C  CE  . MET A 1 792  ? 30.723 71.453  -21.526 1.00 12.78 ? 792  MET A CE  1 
ATOM   6402 N  N   . ARG A 1 793  ? 24.919 71.856  -21.528 1.00 9.97  ? 793  ARG A N   1 
ATOM   6403 C  CA  . ARG A 1 793  ? 24.220 70.686  -22.052 1.00 9.73  ? 793  ARG A CA  1 
ATOM   6404 C  C   . ARG A 1 793  ? 24.526 70.477  -23.504 1.00 9.71  ? 793  ARG A C   1 
ATOM   6405 O  O   . ARG A 1 793  ? 24.723 71.441  -24.284 1.00 10.61 ? 793  ARG A O   1 
ATOM   6406 C  CB  . ARG A 1 793  ? 22.715 70.931  -21.850 1.00 10.81 ? 793  ARG A CB  1 
ATOM   6407 C  CG  . ARG A 1 793  ? 21.856 69.710  -22.326 1.00 10.92 ? 793  ARG A CG  1 
ATOM   6408 C  CD  . ARG A 1 793  ? 20.337 69.946  -22.050 1.00 12.37 ? 793  ARG A CD  1 
ATOM   6409 N  NE  . ARG A 1 793  ? 20.090 69.995  -20.622 1.00 11.88 ? 793  ARG A NE  1 
ATOM   6410 C  CZ  . ARG A 1 793  ? 19.036 70.558  -20.038 1.00 12.38 ? 793  ARG A CZ  1 
ATOM   6411 N  NH1 . ARG A 1 793  ? 18.087 71.140  -20.814 1.00 14.66 ? 793  ARG A NH1 1 
ATOM   6412 N  NH2 . ARG A 1 793  ? 18.909 70.601  -18.741 1.00 12.32 ? 793  ARG A NH2 1 
ATOM   6413 N  N   . LEU A 1 794  ? 24.623 69.222  -23.915 1.00 9.58  ? 794  LEU A N   1 
ATOM   6414 C  CA  . LEU A 1 794  ? 24.728 68.737  -25.310 1.00 10.20 ? 794  LEU A CA  1 
ATOM   6415 C  C   . LEU A 1 794  ? 23.399 68.050  -25.668 1.00 10.75 ? 794  LEU A C   1 
ATOM   6416 O  O   . LEU A 1 794  ? 22.910 67.188  -24.932 1.00 11.22 ? 794  LEU A O   1 
ATOM   6417 C  CB  . LEU A 1 794  ? 25.846 67.720  -25.481 1.00 12.33 ? 794  LEU A CB  1 
ATOM   6418 C  CG  . LEU A 1 794  ? 27.179 68.424  -25.516 1.00 10.81 ? 794  LEU A CG  1 
ATOM   6419 C  CD1 . LEU A 1 794  ? 28.319 67.466  -25.086 1.00 14.38 ? 794  LEU A CD1 1 
ATOM   6420 C  CD2 . LEU A 1 794  ? 27.438 68.855  -26.955 1.00 16.29 ? 794  LEU A CD2 1 
ATOM   6421 N  N   . GLU A 1 795  ? 22.809 68.483  -26.794 1.00 12.02 ? 795  GLU A N   1 
ATOM   6422 C  CA  . GLU A 1 795  ? 21.537 67.925  -27.298 1.00 12.41 ? 795  GLU A CA  1 
ATOM   6423 C  C   . GLU A 1 795  ? 21.849 67.231  -28.608 1.00 13.11 ? 795  GLU A C   1 
ATOM   6424 O  O   . GLU A 1 795  ? 22.399 67.803  -29.556 1.00 13.88 ? 795  GLU A O   1 
ATOM   6425 C  CB  . GLU A 1 795  ? 20.481 69.044  -27.493 1.00 14.54 ? 795  GLU A CB  1 
ATOM   6426 C  CG  . GLU A 1 795  ? 20.075 69.728  -26.231 1.00 17.93 ? 795  GLU A CG  1 
ATOM   6427 C  CD  . GLU A 1 795  ? 19.193 71.000  -26.416 1.00 20.38 ? 795  GLU A CD  1 
ATOM   6428 O  OE1 . GLU A 1 795  ? 19.197 71.607  -27.526 1.00 26.84 ? 795  GLU A OE1 1 
ATOM   6429 O  OE2 . GLU A 1 795  ? 18.541 71.440  -25.450 1.00 25.66 ? 795  GLU A OE2 1 
ATOM   6430 N  N   . THR A 1 796  ? 21.488 65.931  -28.686 1.00 13.13 ? 796  THR A N   1 
ATOM   6431 C  CA  . THR A 1 796  ? 21.668 65.139  -29.857 1.00 11.87 ? 796  THR A CA  1 
ATOM   6432 C  C   . THR A 1 796  ? 20.359 64.347  -30.125 1.00 11.24 ? 796  THR A C   1 
ATOM   6433 O  O   . THR A 1 796  ? 19.433 64.420  -29.321 1.00 17.26 ? 796  THR A O   1 
ATOM   6434 C  CB  . THR A 1 796  ? 22.863 64.095  -29.734 1.00 11.92 ? 796  THR A CB  1 
ATOM   6435 O  OG1 . THR A 1 796  ? 22.433 62.933  -28.984 1.00 11.77 ? 796  THR A OG1 1 
ATOM   6436 C  CG2 . THR A 1 796  ? 24.050 64.746  -29.025 1.00 13.61 ? 796  THR A CG2 1 
ATOM   6437 N  N   A HIS A 1 797  ? 20.383 63.644  -31.210 0.50 12.24 ? 797  HIS A N   1 
ATOM   6438 N  N   B HIS A 1 797  ? 20.363 63.649  -31.216 0.50 19.00 ? 797  HIS A N   1 
ATOM   6439 C  CA  A HIS A 1 797  ? 19.148 62.818  -31.454 0.50 10.17 ? 797  HIS A CA  1 
ATOM   6440 C  CA  B HIS A 1 797  ? 19.182 62.823  -31.446 0.50 22.85 ? 797  HIS A CA  1 
ATOM   6441 C  C   A HIS A 1 797  ? 19.518 61.363  -31.216 0.50 14.10 ? 797  HIS A C   1 
ATOM   6442 C  C   B HIS A 1 797  ? 19.514 61.350  -31.255 0.50 21.50 ? 797  HIS A C   1 
ATOM   6443 O  O   A HIS A 1 797  ? 18.679 60.525  -31.540 0.50 15.81 ? 797  HIS A O   1 
ATOM   6444 O  O   B HIS A 1 797  ? 18.687 60.525  -31.581 0.50 22.02 ? 797  HIS A O   1 
ATOM   6445 C  CB  A HIS A 1 797  ? 18.527 63.179  -32.867 0.50 10.44 ? 797  HIS A CB  1 
ATOM   6446 C  CB  B HIS A 1 797  ? 18.638 63.016  -32.877 0.50 33.53 ? 797  HIS A CB  1 
ATOM   6447 C  CG  A HIS A 1 797  ? 18.068 64.623  -32.967 0.50 4.64  ? 797  HIS A CG  1 
ATOM   6448 C  CG  B HIS A 1 797  ? 18.606 64.492  -33.344 0.50 41.76 ? 797  HIS A CG  1 
ATOM   6449 N  ND1 A HIS A 1 797  ? 17.761 65.278  -34.156 0.50 7.19  ? 797  HIS A ND1 1 
ATOM   6450 N  ND1 B HIS A 1 797  ? 19.417 64.972  -34.350 0.50 47.35 ? 797  HIS A ND1 1 
ATOM   6451 C  CD2 A HIS A 1 797  ? 17.838 65.529  -31.977 0.50 9.46  ? 797  HIS A CD2 1 
ATOM   6452 C  CD2 B HIS A 1 797  ? 17.864 65.544  -32.924 0.50 46.73 ? 797  HIS A CD2 1 
ATOM   6453 C  CE1 A HIS A 1 797  ? 17.357 66.498  -33.890 0.50 11.07 ? 797  HIS A CE1 1 
ATOM   6454 C  CE1 B HIS A 1 797  ? 19.174 66.259  -34.531 0.50 49.53 ? 797  HIS A CE1 1 
ATOM   6455 N  NE2 A HIS A 1 797  ? 17.387 66.687  -32.580 0.50 12.17 ? 797  HIS A NE2 1 
ATOM   6456 N  NE2 B HIS A 1 797  ? 18.236 66.630  -33.678 0.50 49.33 ? 797  HIS A NE2 1 
ATOM   6457 N  N   . ILE A 1 798  ? 20.709 61.036  -30.606 1.00 15.96 ? 798  ILE A N   1 
ATOM   6458 C  CA  . ILE A 1 798  ? 21.143 59.654  -30.258 1.00 14.34 ? 798  ILE A CA  1 
ATOM   6459 C  C   . ILE A 1 798  ? 20.041 59.045  -29.376 1.00 12.02 ? 798  ILE A C   1 
ATOM   6460 O  O   . ILE A 1 798  ? 19.545 59.633  -28.457 1.00 14.02 ? 798  ILE A O   1 
ATOM   6461 C  CB  . ILE A 1 798  ? 22.496 59.696  -29.481 1.00 12.94 ? 798  ILE A CB  1 
ATOM   6462 C  CG1 . ILE A 1 798  ? 23.596 60.174  -30.409 1.00 14.07 ? 798  ILE A CG1 1 
ATOM   6463 C  CG2 . ILE A 1 798  ? 22.848 58.240  -28.942 1.00 15.45 ? 798  ILE A CG2 1 
ATOM   6464 C  CD1 . ILE A 1 798  ? 25.004 60.432  -29.660 1.00 14.40 ? 798  ILE A CD1 1 
ATOM   6465 N  N   . ASP A 1 799  ? 19.618 57.814  -29.765 1.00 14.49 ? 799  ASP A N   1 
ATOM   6466 C  CA  . ASP A 1 799  ? 18.545 57.159  -29.057 1.00 12.67 ? 799  ASP A CA  1 
ATOM   6467 C  C   . ASP A 1 799  ? 19.048 56.357  -27.841 1.00 13.41 ? 799  ASP A C   1 
ATOM   6468 O  O   . ASP A 1 799  ? 19.066 55.120  -27.805 1.00 12.98 ? 799  ASP A O   1 
ATOM   6469 C  CB  . ASP A 1 799  ? 17.761 56.247  -30.042 1.00 16.49 ? 799  ASP A CB  1 
ATOM   6470 C  CG  . ASP A 1 799  ? 16.467 55.723  -29.442 1.00 18.53 ? 799  ASP A CG  1 
ATOM   6471 O  OD1 . ASP A 1 799  ? 16.000 54.714  -30.001 1.00 25.32 ? 799  ASP A OD1 1 
ATOM   6472 O  OD2 . ASP A 1 799  ? 15.962 56.196  -28.400 1.00 24.44 ? 799  ASP A OD2 1 
ATOM   6473 N  N   . SER A 1 800  ? 19.502 57.130  -26.856 1.00 12.82 ? 800  SER A N   1 
ATOM   6474 C  CA  . SER A 1 800  ? 20.063 56.539  -25.649 1.00 11.73 ? 800  SER A CA  1 
ATOM   6475 C  C   . SER A 1 800  ? 19.018 56.135  -24.659 1.00 12.26 ? 800  SER A C   1 
ATOM   6476 O  O   . SER A 1 800  ? 19.326 55.333  -23.734 1.00 11.99 ? 800  SER A O   1 
ATOM   6477 C  CB  . SER A 1 800  ? 21.052 57.570  -25.001 1.00 12.81 ? 800  SER A CB  1 
ATOM   6478 O  OG  . SER A 1 800  ? 20.445 58.796  -24.709 1.00 11.57 ? 800  SER A OG  1 
ATOM   6479 N  N   . GLY A 1 801  ? 17.787 56.652  -24.733 1.00 11.47 ? 801  GLY A N   1 
ATOM   6480 C  CA  . GLY A 1 801  ? 16.770 56.278  -23.800 1.00 11.91 ? 801  GLY A CA  1 
ATOM   6481 C  C   . GLY A 1 801  ? 17.055 56.804  -22.434 1.00 12.52 ? 801  GLY A C   1 
ATOM   6482 O  O   . GLY A 1 801  ? 17.148 58.014  -22.270 1.00 13.79 ? 801  GLY A O   1 
ATOM   6483 N  N   . ASP A 1 802  ? 17.136 55.906  -21.457 1.00 11.28 ? 802  ASP A N   1 
ATOM   6484 C  CA  . ASP A 1 802  ? 17.431 56.291  -20.095 1.00 10.98 ? 802  ASP A CA  1 
ATOM   6485 C  C   . ASP A 1 802  ? 18.847 55.841  -19.672 1.00 10.52 ? 802  ASP A C   1 
ATOM   6486 O  O   . ASP A 1 802  ? 19.132 55.881  -18.458 1.00 11.79 ? 802  ASP A O   1 
ATOM   6487 C  CB  . ASP A 1 802  ? 16.354 55.671  -19.157 1.00 13.12 ? 802  ASP A CB  1 
ATOM   6488 C  CG  . ASP A 1 802  ? 16.238 54.141  -19.271 1.00 12.35 ? 802  ASP A CG  1 
ATOM   6489 O  OD1 . ASP A 1 802  ? 15.293 53.644  -18.584 1.00 18.02 ? 802  ASP A OD1 1 
ATOM   6490 O  OD2 . ASP A 1 802  ? 17.016 53.483  -19.980 1.00 15.73 ? 802  ASP A OD2 1 
ATOM   6491 N  N   . ILE A 1 803  ? 19.685 55.440  -20.591 1.00 8.80  ? 803  ILE A N   1 
ATOM   6492 C  CA  . ILE A 1 803  ? 21.020 54.945  -20.232 1.00 9.42  ? 803  ILE A CA  1 
ATOM   6493 C  C   . ILE A 1 803  ? 22.101 55.983  -20.559 1.00 9.39  ? 803  ILE A C   1 
ATOM   6494 O  O   . ILE A 1 803  ? 22.072 56.661  -21.580 1.00 9.33  ? 803  ILE A O   1 
ATOM   6495 C  CB  . ILE A 1 803  ? 21.318 53.677  -21.039 1.00 9.03  ? 803  ILE A CB  1 
ATOM   6496 C  CG1 . ILE A 1 803  ? 20.273 52.577  -20.657 1.00 11.31 ? 803  ILE A CG1 1 
ATOM   6497 C  CG2 . ILE A 1 803  ? 22.736 53.145  -20.793 1.00 11.27 ? 803  ILE A CG2 1 
ATOM   6498 C  CD1 . ILE A 1 803  ? 20.215 52.279  -19.172 1.00 13.06 ? 803  ILE A CD1 1 
ATOM   6499 N  N   . PHE A 1 804  ? 23.095 56.072  -19.658 1.00 9.59  ? 804  PHE A N   1 
ATOM   6500 C  CA  . PHE A 1 804  ? 24.295 56.876  -19.899 1.00 9.34  ? 804  PHE A CA  1 
ATOM   6501 C  C   . PHE A 1 804  ? 25.426 56.250  -19.078 1.00 8.83  ? 804  PHE A C   1 
ATOM   6502 O  O   . PHE A 1 804  ? 25.174 55.385  -18.267 1.00 10.29 ? 804  PHE A O   1 
ATOM   6503 C  CB  . PHE A 1 804  ? 24.063 58.387  -19.563 1.00 8.33  ? 804  PHE A CB  1 
ATOM   6504 C  CG  . PHE A 1 804  ? 23.652 58.694  -18.138 1.00 8.30  ? 804  PHE A CG  1 
ATOM   6505 C  CD1 . PHE A 1 804  ? 24.569 59.324  -17.264 1.00 8.23  ? 804  PHE A CD1 1 
ATOM   6506 C  CD2 . PHE A 1 804  ? 22.372 58.504  -17.667 1.00 9.01  ? 804  PHE A CD2 1 
ATOM   6507 C  CE1 . PHE A 1 804  ? 24.186 59.727  -16.025 1.00 8.27  ? 804  PHE A CE1 1 
ATOM   6508 C  CE2 . PHE A 1 804  ? 21.985 58.906  -16.426 1.00 9.64  ? 804  PHE A CE2 1 
ATOM   6509 C  CZ  . PHE A 1 804  ? 22.903 59.548  -15.563 1.00 9.84  ? 804  PHE A CZ  1 
ATOM   6510 N  N   . TYR A 1 805  ? 26.630 56.702  -19.330 1.00 8.53  ? 805  TYR A N   1 
ATOM   6511 C  CA  . TYR A 1 805  ? 27.807 56.129  -18.649 1.00 8.36  ? 805  TYR A CA  1 
ATOM   6512 C  C   . TYR A 1 805  ? 28.633 57.262  -18.074 1.00 7.49  ? 805  TYR A C   1 
ATOM   6513 O  O   . TYR A 1 805  ? 28.786 58.304  -18.748 1.00 9.06  ? 805  TYR A O   1 
ATOM   6514 C  CB  . TYR A 1 805  ? 28.661 55.365  -19.635 1.00 8.42  ? 805  TYR A CB  1 
ATOM   6515 C  CG  . TYR A 1 805  ? 27.996 54.119  -20.209 1.00 8.20  ? 805  TYR A CG  1 
ATOM   6516 C  CD1 . TYR A 1 805  ? 26.989 54.238  -21.228 1.00 10.73 ? 805  TYR A CD1 1 
ATOM   6517 C  CD2 . TYR A 1 805  ? 28.312 52.859  -19.717 1.00 9.24  ? 805  TYR A CD2 1 
ATOM   6518 C  CE1 . TYR A 1 805  ? 26.344 53.103  -21.703 1.00 10.68 ? 805  TYR A CE1 1 
ATOM   6519 C  CE2 . TYR A 1 805  ? 27.651 51.704  -20.219 1.00 9.56  ? 805  TYR A CE2 1 
ATOM   6520 C  CZ  . TYR A 1 805  ? 26.686 51.887  -21.189 1.00 11.12 ? 805  TYR A CZ  1 
ATOM   6521 O  OH  . TYR A 1 805  ? 26.042 50.758  -21.708 1.00 12.52 ? 805  TYR A OH  1 
ATOM   6522 N  N   . THR A 1 806  ? 29.120 57.062  -16.853 1.00 8.53  ? 806  THR A N   1 
ATOM   6523 C  CA  . THR A 1 806  ? 29.996 58.072  -16.209 1.00 6.94  ? 806  THR A CA  1 
ATOM   6524 C  C   . THR A 1 806  ? 31.174 57.304  -15.634 1.00 8.80  ? 806  THR A C   1 
ATOM   6525 O  O   . THR A 1 806  ? 31.116 56.081  -15.410 1.00 9.18  ? 806  THR A O   1 
ATOM   6526 C  CB  . THR A 1 806  ? 29.274 58.852  -15.133 1.00 8.60  ? 806  THR A CB  1 
ATOM   6527 O  OG1 . THR A 1 806  ? 28.901 57.960  -14.093 1.00 8.64  ? 806  THR A OG1 1 
ATOM   6528 C  CG2 . THR A 1 806  ? 28.003 59.528  -15.663 1.00 8.62  ? 806  THR A CG2 1 
ATOM   6529 N  N   . ASP A 1 807  ? 32.306 57.962  -15.430 1.00 7.49  ? 807  ASP A N   1 
ATOM   6530 C  CA  . ASP A 1 807  ? 33.425 57.255  -14.828 1.00 8.80  ? 807  ASP A CA  1 
ATOM   6531 C  C   . ASP A 1 807  ? 33.481 57.329  -13.328 1.00 7.13  ? 807  ASP A C   1 
ATOM   6532 O  O   . ASP A 1 807  ? 32.842 58.143  -12.668 1.00 7.72  ? 807  ASP A O   1 
ATOM   6533 C  CB  . ASP A 1 807  ? 34.743 57.704  -15.434 1.00 10.65 ? 807  ASP A CB  1 
ATOM   6534 C  CG  . ASP A 1 807  ? 35.165 58.998  -14.957 1.00 10.17 ? 807  ASP A CG  1 
ATOM   6535 O  OD1 . ASP A 1 807  ? 36.341 59.059  -14.433 1.00 12.16 ? 807  ASP A OD1 1 
ATOM   6536 O  OD2 . ASP A 1 807  ? 34.412 59.993  -15.044 1.00 11.47 ? 807  ASP A OD2 1 
ATOM   6537 N  N   . LEU A 1 808  ? 34.241 56.396  -12.774 1.00 7.30  ? 808  LEU A N   1 
ATOM   6538 C  CA  . LEU A 1 808  ? 34.545 56.361  -11.328 1.00 6.58  ? 808  LEU A CA  1 
ATOM   6539 C  C   . LEU A 1 808  ? 36.038 56.586  -11.162 1.00 6.57  ? 808  LEU A C   1 
ATOM   6540 O  O   . LEU A 1 808  ? 36.848 55.774  -11.618 1.00 7.31  ? 808  LEU A O   1 
ATOM   6541 C  CB  . LEU A 1 808  ? 34.162 55.024  -10.702 1.00 7.94  ? 808  LEU A CB  1 
ATOM   6542 C  CG  . LEU A 1 808  ? 32.621 54.913  -10.589 1.00 8.96  ? 808  LEU A CG  1 
ATOM   6543 C  CD1 . LEU A 1 808  ? 32.277 53.411  -10.384 1.00 9.37  ? 808  LEU A CD1 1 
ATOM   6544 C  CD2 . LEU A 1 808  ? 32.035 55.751  -9.439  1.00 10.18 ? 808  LEU A CD2 1 
ATOM   6545 N  N   . ASN A 1 809  ? 36.377 57.754  -10.608 1.00 6.45  ? 809  ASN A N   1 
ATOM   6546 C  CA  . ASN A 1 809  ? 37.793 58.080  -10.263 1.00 6.32  ? 809  ASN A CA  1 
ATOM   6547 C  C   . ASN A 1 809  ? 38.761 57.972  -11.422 1.00 6.84  ? 809  ASN A C   1 
ATOM   6548 O  O   . ASN A 1 809  ? 39.965 57.708  -11.226 1.00 7.34  ? 809  ASN A O   1 
ATOM   6549 C  CB  . ASN A 1 809  ? 38.286 57.165  -9.102  1.00 6.20  ? 809  ASN A CB  1 
ATOM   6550 C  CG  . ASN A 1 809  ? 37.265 57.123  -8.012  1.00 6.34  ? 809  ASN A CG  1 
ATOM   6551 O  OD1 . ASN A 1 809  ? 37.250 58.048  -7.094  1.00 10.21 ? 809  ASN A OD1 1 
ATOM   6552 N  ND2 . ASN A 1 809  ? 36.400 56.180  -8.027  1.00 5.01  ? 809  ASN A ND2 1 
ATOM   6553 N  N   . GLY A 1 810  ? 38.319 58.186  -12.673 1.00 6.70  ? 810  GLY A N   1 
ATOM   6554 C  CA  . GLY A 1 810  ? 39.255 58.090  -13.786 1.00 7.78  ? 810  GLY A CA  1 
ATOM   6555 C  C   . GLY A 1 810  ? 39.686 56.674  -14.083 1.00 8.58  ? 810  GLY A C   1 
ATOM   6556 O  O   . GLY A 1 810  ? 40.647 56.469  -14.887 1.00 10.54 ? 810  GLY A O   1 
ATOM   6557 N  N   . LEU A 1 811  ? 39.067 55.681  -13.467 1.00 7.49  ? 811  LEU A N   1 
ATOM   6558 C  CA  . LEU A 1 811  ? 39.519 54.278  -13.578 1.00 8.36  ? 811  LEU A CA  1 
ATOM   6559 C  C   . LEU A 1 811  ? 38.615 53.362  -14.432 1.00 9.48  ? 811  LEU A C   1 
ATOM   6560 O  O   . LEU A 1 811  ? 39.146 52.483  -15.107 1.00 12.38 ? 811  LEU A O   1 
ATOM   6561 C  CB  . LEU A 1 811  ? 39.607 53.683  -12.139 1.00 9.54  ? 811  LEU A CB  1 
ATOM   6562 C  CG  . LEU A 1 811  ? 40.046 52.218  -11.989 1.00 11.06 ? 811  LEU A CG  1 
ATOM   6563 C  CD1 . LEU A 1 811  ? 41.479 52.061  -12.506 1.00 13.22 ? 811  LEU A CD1 1 
ATOM   6564 C  CD2 . LEU A 1 811  ? 39.939 51.731  -10.528 1.00 13.08 ? 811  LEU A CD2 1 
ATOM   6565 N  N   . GLN A 1 812  ? 37.309 53.599  -14.424 1.00 7.47  ? 812  GLN A N   1 
ATOM   6566 C  CA  . GLN A 1 812  ? 36.354 52.686  -15.064 1.00 8.08  ? 812  GLN A CA  1 
ATOM   6567 C  C   . GLN A 1 812  ? 35.117 53.456  -15.385 1.00 7.92  ? 812  GLN A C   1 
ATOM   6568 O  O   . GLN A 1 812  ? 34.828 54.492  -14.730 1.00 9.75  ? 812  GLN A O   1 
ATOM   6569 C  CB  . GLN A 1 812  ? 36.008 51.554  -14.057 1.00 9.11  ? 812  GLN A CB  1 
ATOM   6570 C  CG  . GLN A 1 812  ? 35.430 52.071  -12.743 1.00 12.02 ? 812  GLN A CG  1 
ATOM   6571 C  CD  . GLN A 1 812  ? 35.144 50.945  -11.752 1.00 12.60 ? 812  GLN A CD  1 
ATOM   6572 O  OE1 . GLN A 1 812  ? 34.187 50.199  -11.907 1.00 13.07 ? 812  GLN A OE1 1 
ATOM   6573 N  NE2 . GLN A 1 812  ? 35.980 50.855  -10.706 1.00 14.03 ? 812  GLN A NE2 1 
ATOM   6574 N  N   . PHE A 1 813  ? 34.340 52.982  -16.360 1.00 8.19  ? 813  PHE A N   1 
ATOM   6575 C  CA  . PHE A 1 813  ? 33.043 53.599  -16.727 1.00 6.99  ? 813  PHE A CA  1 
ATOM   6576 C  C   . PHE A 1 813  ? 31.950 52.699  -16.281 1.00 8.03  ? 813  PHE A C   1 
ATOM   6577 O  O   . PHE A 1 813  ? 31.979 51.463  -16.600 1.00 10.92 ? 813  PHE A O   1 
ATOM   6578 C  CB  . PHE A 1 813  ? 33.008 53.883  -18.220 1.00 7.59  ? 813  PHE A CB  1 
ATOM   6579 C  CG  . PHE A 1 813  ? 33.784 55.112  -18.605 1.00 7.83  ? 813  PHE A CG  1 
ATOM   6580 C  CD1 . PHE A 1 813  ? 35.156 55.064  -18.695 1.00 8.53  ? 813  PHE A CD1 1 
ATOM   6581 C  CD2 . PHE A 1 813  ? 33.064 56.326  -18.796 1.00 8.75  ? 813  PHE A CD2 1 
ATOM   6582 C  CE1 . PHE A 1 813  ? 35.844 56.266  -18.959 1.00 10.27 ? 813  PHE A CE1 1 
ATOM   6583 C  CE2 . PHE A 1 813  ? 33.736 57.487  -19.070 1.00 10.84 ? 813  PHE A CE2 1 
ATOM   6584 C  CZ  . PHE A 1 813  ? 35.116 57.446  -19.147 1.00 10.07 ? 813  PHE A CZ  1 
ATOM   6585 N  N   . ILE A 1 814  ? 30.982 53.259  -15.603 1.00 7.70  ? 814  ILE A N   1 
ATOM   6586 C  CA  . ILE A 1 814  ? 29.902 52.460  -15.077 1.00 8.11  ? 814  ILE A CA  1 
ATOM   6587 C  C   . ILE A 1 814  ? 28.599 52.894  -15.741 1.00 8.53  ? 814  ILE A C   1 
ATOM   6588 O  O   . ILE A 1 814  ? 28.334 54.091  -16.004 1.00 7.93  ? 814  ILE A O   1 
ATOM   6589 C  CB  . ILE A 1 814  ? 29.874 52.629  -13.527 1.00 7.76  ? 814  ILE A CB  1 
ATOM   6590 C  CG1 . ILE A 1 814  ? 28.800 51.693  -12.910 1.00 8.81  ? 814  ILE A CG1 1 
ATOM   6591 C  CG2 . ILE A 1 814  ? 29.587 54.083  -13.098 1.00 8.73  ? 814  ILE A CG2 1 
ATOM   6592 C  CD1 . ILE A 1 814  ? 28.968 51.527  -11.353 1.00 8.99  ? 814  ILE A CD1 1 
ATOM   6593 N  N   . LYS A 1 815  ? 27.721 51.915  -16.015 1.00 7.76  ? 815  LYS A N   1 
ATOM   6594 C  CA  . LYS A 1 815  ? 26.408 52.211  -16.611 1.00 8.41  ? 815  LYS A CA  1 
ATOM   6595 C  C   . LYS A 1 815  ? 25.494 52.817  -15.576 1.00 8.20  ? 815  LYS A C   1 
ATOM   6596 O  O   . LYS A 1 815  ? 25.359 52.352  -14.441 1.00 8.75  ? 815  LYS A O   1 
ATOM   6597 C  CB  . LYS A 1 815  ? 25.823 50.891  -17.138 1.00 9.57  ? 815  LYS A CB  1 
ATOM   6598 C  CG  . LYS A 1 815  ? 24.493 51.053  -17.942 1.00 10.26 ? 815  LYS A CG  1 
ATOM   6599 C  CD  . LYS A 1 815  ? 24.052 49.617  -18.418 1.00 13.93 ? 815  LYS A CD  1 
ATOM   6600 C  CE  . LYS A 1 815  ? 22.909 49.678  -19.380 1.00 20.27 ? 815  LYS A CE  1 
ATOM   6601 N  NZ  . LYS A 1 815  ? 22.691 48.215  -19.794 1.00 23.34 ? 815  LYS A NZ  1 
ATOM   6602 N  N   . ARG A 1 816  ? 24.824 53.895  -15.988 1.00 8.50  ? 816  ARG A N   1 
ATOM   6603 C  CA  . ARG A 1 816  ? 23.821 54.592  -15.229 1.00 8.14  ? 816  ARG A CA  1 
ATOM   6604 C  C   . ARG A 1 816  ? 22.477 54.458  -15.934 1.00 9.00  ? 816  ARG A C   1 
ATOM   6605 O  O   . ARG A 1 816  ? 22.413 54.424  -17.149 1.00 8.77  ? 816  ARG A O   1 
ATOM   6606 C  CB  . ARG A 1 816  ? 24.118 56.118  -15.135 1.00 9.24  ? 816  ARG A CB  1 
ATOM   6607 C  CG  . ARG A 1 816  ? 25.579 56.482  -14.577 1.00 8.61  ? 816  ARG A CG  1 
ATOM   6608 C  CD  . ARG A 1 816  ? 25.735 55.868  -13.208 1.00 9.38  ? 816  ARG A CD  1 
ATOM   6609 N  NE  . ARG A 1 816  ? 26.954 56.447  -12.582 1.00 8.80  ? 816  ARG A NE  1 
ATOM   6610 C  CZ  . ARG A 1 816  ? 27.345 56.052  -11.373 1.00 8.87  ? 816  ARG A CZ  1 
ATOM   6611 N  NH1 . ARG A 1 816  ? 26.659 55.109  -10.726 1.00 8.33  ? 816  ARG A NH1 1 
ATOM   6612 N  NH2 . ARG A 1 816  ? 28.389 56.622  -10.764 1.00 9.22  ? 816  ARG A NH2 1 
ATOM   6613 N  N   . ARG A 1 817  ? 21.449 54.468  -15.103 1.00 8.72  ? 817  ARG A N   1 
ATOM   6614 C  CA  . ARG A 1 817  ? 20.085 54.485  -15.665 1.00 8.64  ? 817  ARG A CA  1 
ATOM   6615 C  C   . ARG A 1 817  ? 19.360 55.627  -14.968 1.00 8.83  ? 817  ARG A C   1 
ATOM   6616 O  O   . ARG A 1 817  ? 19.231 55.671  -13.742 1.00 10.54 ? 817  ARG A O   1 
ATOM   6617 C  CB  . ARG A 1 817  ? 19.356 53.119  -15.453 1.00 10.26 ? 817  ARG A CB  1 
ATOM   6618 C  CG  . ARG A 1 817  ? 17.884 53.174  -15.954 1.00 12.07 ? 817  ARG A CG  1 
ATOM   6619 C  CD  . ARG A 1 817  ? 17.152 51.799  -15.709 1.00 12.94 ? 817  ARG A CD  1 
ATOM   6620 N  NE  . ARG A 1 817  ? 17.744 50.754  -16.506 1.00 13.22 ? 817  ARG A NE  1 
ATOM   6621 C  CZ  . ARG A 1 817  ? 18.483 49.744  -16.095 1.00 14.54 ? 817  ARG A CZ  1 
ATOM   6622 N  NH1 . ARG A 1 817  ? 18.789 49.597  -14.825 1.00 13.74 ? 817  ARG A NH1 1 
ATOM   6623 N  NH2 . ARG A 1 817  ? 18.913 48.847  -16.981 1.00 18.05 ? 817  ARG A NH2 1 
ATOM   6624 N  N   . ARG A 1 818  ? 18.904 56.586  -15.813 1.00 9.04  ? 818  ARG A N   1 
ATOM   6625 C  CA  . ARG A 1 818  ? 18.094 57.671  -15.306 1.00 10.99 ? 818  ARG A CA  1 
ATOM   6626 C  C   . ARG A 1 818  ? 16.778 57.083  -14.750 1.00 11.14 ? 818  ARG A C   1 
ATOM   6627 O  O   . ARG A 1 818  ? 16.153 56.269  -15.461 1.00 13.12 ? 818  ARG A O   1 
ATOM   6628 C  CB  . ARG A 1 818  ? 17.764 58.632  -16.491 1.00 10.30 ? 818  ARG A CB  1 
ATOM   6629 C  CG  . ARG A 1 818  ? 17.015 59.876  -16.013 1.00 12.42 ? 818  ARG A CG  1 
ATOM   6630 C  CD  . ARG A 1 818  ? 16.434 60.680  -17.194 1.00 11.88 ? 818  ARG A CD  1 
ATOM   6631 N  NE  . ARG A 1 818  ? 15.137 60.052  -17.514 1.00 17.99 ? 818  ARG A NE  1 
ATOM   6632 C  CZ  . ARG A 1 818  ? 14.810 59.461  -18.681 1.00 18.15 ? 818  ARG A CZ  1 
ATOM   6633 N  NH1 . ARG A 1 818  ? 15.641 59.381  -19.715 1.00 15.32 ? 818  ARG A NH1 1 
ATOM   6634 N  NH2 . ARG A 1 818  ? 13.583 58.911  -18.784 1.00 18.97 ? 818  ARG A NH2 1 
ATOM   6635 N  N   . LEU A 1 819  ? 16.387 57.488  -13.562 1.00 11.43 ? 819  LEU A N   1 
ATOM   6636 C  CA  . LEU A 1 819  ? 15.146 56.959  -12.905 1.00 12.71 ? 819  LEU A CA  1 
ATOM   6637 C  C   . LEU A 1 819  ? 14.191 58.107  -12.625 1.00 11.05 ? 819  LEU A C   1 
ATOM   6638 O  O   . LEU A 1 819  ? 14.436 58.963  -11.799 1.00 12.02 ? 819  LEU A O   1 
ATOM   6639 C  CB  . LEU A 1 819  ? 15.485 56.255  -11.586 1.00 12.50 ? 819  LEU A CB  1 
ATOM   6640 C  CG  . LEU A 1 819  ? 16.450 55.032  -11.725 1.00 13.14 ? 819  LEU A CG  1 
ATOM   6641 C  CD1 . LEU A 1 819  ? 16.930 54.552  -10.321 1.00 15.80 ? 819  LEU A CD1 1 
ATOM   6642 C  CD2 . LEU A 1 819  ? 15.818 53.884  -12.505 1.00 14.46 ? 819  LEU A CD2 1 
ATOM   6643 N  N   . ASP A 1 820  ? 13.073 58.064  -13.354 1.00 14.07 ? 820  ASP A N   1 
ATOM   6644 C  CA  . ASP A 1 820  ? 12.108 59.126  -13.163 1.00 14.71 ? 820  ASP A CA  1 
ATOM   6645 C  C   . ASP A 1 820  ? 11.369 58.971  -11.836 1.00 12.80 ? 820  ASP A C   1 
ATOM   6646 O  O   . ASP A 1 820  ? 10.755 59.932  -11.359 1.00 15.49 ? 820  ASP A O   1 
ATOM   6647 C  CB  . ASP A 1 820  ? 11.160 59.213  -14.374 1.00 17.21 ? 820  ASP A CB  1 
ATOM   6648 C  CG  . ASP A 1 820  ? 11.905 59.542  -15.662 1.00 21.95 ? 820  ASP A CG  1 
ATOM   6649 O  OD1 . ASP A 1 820  ? 12.986 60.200  -15.636 1.00 20.80 ? 820  ASP A OD1 1 
ATOM   6650 O  OD2 . ASP A 1 820  ? 11.414 59.157  -16.728 1.00 24.33 ? 820  ASP A OD2 1 
ATOM   6651 N  N   . LYS A 1 821  ? 11.561 57.832  -11.147 1.00 13.38 ? 821  LYS A N   1 
ATOM   6652 C  CA  . LYS A 1 821  ? 10.947 57.691  -9.827  1.00 13.84 ? 821  LYS A CA  1 
ATOM   6653 C  C   . LYS A 1 821  ? 11.789 58.438  -8.763  1.00 15.93 ? 821  LYS A C   1 
ATOM   6654 O  O   . LYS A 1 821  ? 11.329 58.604  -7.636  1.00 16.90 ? 821  LYS A O   1 
ATOM   6655 C  CB  . LYS A 1 821  ? 10.814 56.203  -9.444  1.00 12.47 ? 821  LYS A CB  1 
ATOM   6656 C  CG  . LYS A 1 821  ? 12.153 55.496  -9.173  1.00 13.56 ? 821  LYS A CG  1 
ATOM   6657 C  CD  . LYS A 1 821  ? 11.972 54.013  -9.019  1.00 13.53 ? 821  LYS A CD  1 
ATOM   6658 C  CE  . LYS A 1 821  ? 13.334 53.303  -8.986  1.00 15.95 ? 821  LYS A CE  1 
ATOM   6659 N  NZ  . LYS A 1 821  ? 13.242 51.821  -9.187  1.00 16.00 ? 821  LYS A NZ  1 
ATOM   6660 N  N   . LEU A 1 822  ? 12.987 58.932  -9.168  1.00 13.50 ? 822  LEU A N   1 
ATOM   6661 C  CA  . LEU A 1 822  ? 13.815 59.742  -8.221  1.00 12.02 ? 822  LEU A CA  1 
ATOM   6662 C  C   . LEU A 1 822  ? 13.855 61.183  -8.755  1.00 13.59 ? 822  LEU A C   1 
ATOM   6663 O  O   . LEU A 1 822  ? 13.679 61.411  -9.949  1.00 14.33 ? 822  LEU A O   1 
ATOM   6664 C  CB  . LEU A 1 822  ? 15.241 59.213  -8.192  1.00 13.81 ? 822  LEU A CB  1 
ATOM   6665 C  CG  . LEU A 1 822  ? 15.395 57.746  -7.719  1.00 14.88 ? 822  LEU A CG  1 
ATOM   6666 C  CD1 . LEU A 1 822  ? 16.868 57.379  -7.721  1.00 17.77 ? 822  LEU A CD1 1 
ATOM   6667 C  CD2 . LEU A 1 822  ? 14.708 57.496  -6.399  1.00 15.15 ? 822  LEU A CD2 1 
ATOM   6668 N  N   . PRO A 1 823  ? 14.077 62.138  -7.870  1.00 12.67 ? 823  PRO A N   1 
ATOM   6669 C  CA  . PRO A 1 823  ? 14.138 63.551  -8.280  1.00 12.13 ? 823  PRO A CA  1 
ATOM   6670 C  C   . PRO A 1 823  ? 15.354 63.846  -9.129  1.00 13.09 ? 823  PRO A C   1 
ATOM   6671 O  O   . PRO A 1 823  ? 16.348 63.064  -9.184  1.00 11.80 ? 823  PRO A O   1 
ATOM   6672 C  CB  . PRO A 1 823  ? 14.104 64.318  -6.961  1.00 13.45 ? 823  PRO A CB  1 
ATOM   6673 C  CG  . PRO A 1 823  ? 14.762 63.409  -5.983  1.00 16.39 ? 823  PRO A CG  1 
ATOM   6674 C  CD  . PRO A 1 823  ? 14.252 61.984  -6.412  1.00 13.58 ? 823  PRO A CD  1 
ATOM   6675 N  N   . LEU A 1 824  ? 15.307 64.967  -9.848  1.00 12.65 ? 824  LEU A N   1 
ATOM   6676 C  CA  . LEU A 1 824  ? 16.359 65.350  -10.746 1.00 12.92 ? 824  LEU A CA  1 
ATOM   6677 C  C   . LEU A 1 824  ? 17.787 65.227  -10.112 1.00 10.94 ? 824  LEU A C   1 
ATOM   6678 O  O   . LEU A 1 824  ? 18.694 64.660  -10.757 1.00 11.43 ? 824  LEU A O   1 
ATOM   6679 C  CB  . LEU A 1 824  ? 16.067 66.806  -11.217 1.00 12.42 ? 824  LEU A CB  1 
ATOM   6680 C  CG  . LEU A 1 824  ? 16.854 67.405  -12.345 1.00 12.17 ? 824  LEU A CG  1 
ATOM   6681 C  CD1 . LEU A 1 824  ? 16.068 68.665  -12.848 1.00 13.43 ? 824  LEU A CD1 1 
ATOM   6682 C  CD2 . LEU A 1 824  ? 18.306 67.830  -11.902 1.00 12.51 ? 824  LEU A CD2 1 
ATOM   6683 N  N   . GLN A 1 825  ? 17.948 65.747  -8.905  1.00 10.03 ? 825  GLN A N   1 
ATOM   6684 C  CA  . GLN A 1 825  ? 19.276 65.748  -8.269  1.00 10.04 ? 825  GLN A CA  1 
ATOM   6685 C  C   . GLN A 1 825  ? 19.797 64.375  -7.973  1.00 11.27 ? 825  GLN A C   1 
ATOM   6686 O  O   . GLN A 1 825  ? 21.050 64.220  -7.823  1.00 10.59 ? 825  GLN A O   1 
ATOM   6687 C  CB  . GLN A 1 825  ? 19.268 66.640  -7.040  1.00 11.13 ? 825  GLN A CB  1 
ATOM   6688 C  CG  . GLN A 1 825  ? 18.317 66.118  -5.908  1.00 9.68  ? 825  GLN A CG  1 
ATOM   6689 C  CD  . GLN A 1 825  ? 16.852 66.624  -5.995  1.00 12.64 ? 825  GLN A CD  1 
ATOM   6690 O  OE1 . GLN A 1 825  ? 16.403 67.102  -7.059  1.00 12.79 ? 825  GLN A OE1 1 
ATOM   6691 N  NE2 . GLN A 1 825  ? 16.121 66.504  -4.865  1.00 11.56 ? 825  GLN A NE2 1 
ATOM   6692 N  N   . ALA A 1 826  ? 18.926 63.348  -7.869  1.00 10.09 ? 826  ALA A N   1 
ATOM   6693 C  CA  . ALA A 1 826  ? 19.384 61.964  -7.625  1.00 9.72  ? 826  ALA A CA  1 
ATOM   6694 C  C   . ALA A 1 826  ? 19.959 61.403  -8.894  1.00 9.32  ? 826  ALA A C   1 
ATOM   6695 O  O   . ALA A 1 826  ? 20.718 60.404  -8.868  1.00 11.22 ? 826  ALA A O   1 
ATOM   6696 C  CB  . ALA A 1 826  ? 18.169 61.098  -7.168  1.00 10.66 ? 826  ALA A CB  1 
ATOM   6697 N  N   . ASN A 1 827  ? 19.622 61.979  -10.060 1.00 9.43  ? 827  ASN A N   1 
ATOM   6698 C  CA  . ASN A 1 827  ? 20.123 61.489  -11.356 1.00 9.20  ? 827  ASN A CA  1 
ATOM   6699 C  C   . ASN A 1 827  ? 21.447 62.112  -11.796 1.00 7.97  ? 827  ASN A C   1 
ATOM   6700 O  O   . ASN A 1 827  ? 21.944 61.801  -12.843 1.00 9.82  ? 827  ASN A O   1 
ATOM   6701 C  CB  . ASN A 1 827  ? 19.006 61.611  -12.433 1.00 10.36 ? 827  ASN A CB  1 
ATOM   6702 C  CG  . ASN A 1 827  ? 17.897 60.590  -12.173 1.00 11.70 ? 827  ASN A CG  1 
ATOM   6703 O  OD1 . ASN A 1 827  ? 18.112 59.403  -12.270 1.00 12.28 ? 827  ASN A OD1 1 
ATOM   6704 N  ND2 . ASN A 1 827  ? 16.706 61.072  -11.805 1.00 15.12 ? 827  ASN A ND2 1 
ATOM   6705 N  N   . TYR A 1 828  ? 21.927 63.000  -10.926 1.00 9.44  ? 828  TYR A N   1 
ATOM   6706 C  CA  . TYR A 1 828  ? 23.259 63.593  -11.119 1.00 8.60  ? 828  TYR A CA  1 
ATOM   6707 C  C   . TYR A 1 828  ? 24.323 62.653  -10.466 1.00 7.76  ? 828  TYR A C   1 
ATOM   6708 O  O   . TYR A 1 828  ? 24.082 62.101  -9.381  1.00 9.66  ? 828  TYR A O   1 
ATOM   6709 C  CB  . TYR A 1 828  ? 23.368 64.975  -10.426 1.00 8.06  ? 828  TYR A CB  1 
ATOM   6710 C  CG  . TYR A 1 828  ? 23.317 66.099  -11.396 1.00 8.90  ? 828  TYR A CG  1 
ATOM   6711 C  CD1 . TYR A 1 828  ? 22.273 66.306  -12.271 1.00 9.56  ? 828  TYR A CD1 1 
ATOM   6712 C  CD2 . TYR A 1 828  ? 24.390 66.960  -11.483 1.00 9.62  ? 828  TYR A CD2 1 
ATOM   6713 C  CE1 . TYR A 1 828  ? 22.305 67.342  -13.214 1.00 11.16 ? 828  TYR A CE1 1 
ATOM   6714 C  CE2 . TYR A 1 828  ? 24.445 67.982  -12.407 1.00 11.67 ? 828  TYR A CE2 1 
ATOM   6715 C  CZ  . TYR A 1 828  ? 23.411 68.165  -13.270 1.00 9.10  ? 828  TYR A CZ  1 
ATOM   6716 O  OH  . TYR A 1 828  ? 23.540 69.157  -14.231 1.00 11.90 ? 828  TYR A OH  1 
ATOM   6717 N  N   . TYR A 1 829  ? 25.431 62.451  -11.180 1.00 7.86  ? 829  TYR A N   1 
ATOM   6718 C  CA  . TYR A 1 829  ? 26.542 61.609  -10.746 1.00 8.19  ? 829  TYR A CA  1 
ATOM   6719 C  C   . TYR A 1 829  ? 27.844 62.346  -10.923 1.00 8.60  ? 829  TYR A C   1 
ATOM   6720 O  O   . TYR A 1 829  ? 27.948 63.338  -11.625 1.00 8.45  ? 829  TYR A O   1 
ATOM   6721 C  CB  . TYR A 1 829  ? 26.572 60.328  -11.621 1.00 8.52  ? 829  TYR A CB  1 
ATOM   6722 C  CG  . TYR A 1 829  ? 25.388 59.414  -11.363 1.00 8.80  ? 829  TYR A CG  1 
ATOM   6723 C  CD1 . TYR A 1 829  ? 24.224 59.478  -12.154 1.00 9.20  ? 829  TYR A CD1 1 
ATOM   6724 C  CD2 . TYR A 1 829  ? 25.404 58.534  -10.293 1.00 8.37  ? 829  TYR A CD2 1 
ATOM   6725 C  CE1 . TYR A 1 829  ? 23.139 58.674  -11.850 1.00 10.03 ? 829  TYR A CE1 1 
ATOM   6726 C  CE2 . TYR A 1 829  ? 24.286 57.709  -9.982  1.00 9.66  ? 829  TYR A CE2 1 
ATOM   6727 C  CZ  . TYR A 1 829  ? 23.193 57.804  -10.772 1.00 8.80  ? 829  TYR A CZ  1 
ATOM   6728 O  OH  . TYR A 1 829  ? 22.123 56.974  -10.442 1.00 10.83 ? 829  TYR A OH  1 
ATOM   6729 N  N   . PRO A 1 830  ? 28.890 61.841  -10.227 1.00 7.97  ? 830  PRO A N   1 
ATOM   6730 C  CA  . PRO A 1 830  ? 30.184 62.506  -10.417 1.00 8.54  ? 830  PRO A CA  1 
ATOM   6731 C  C   . PRO A 1 830  ? 30.681 62.231  -11.837 1.00 8.58  ? 830  PRO A C   1 
ATOM   6732 O  O   . PRO A 1 830  ? 30.461 61.141  -12.411 1.00 9.42  ? 830  PRO A O   1 
ATOM   6733 C  CB  . PRO A 1 830  ? 31.119 61.800  -9.403  1.00 12.22 ? 830  PRO A CB  1 
ATOM   6734 C  CG  . PRO A 1 830  ? 30.226 60.896  -8.539  1.00 11.19 ? 830  PRO A CG  1 
ATOM   6735 C  CD  . PRO A 1 830  ? 28.915 60.696  -9.286  1.00 7.99  ? 830  PRO A CD  1 
ATOM   6736 N  N   . ILE A 1 831  ? 31.307 63.248  -12.453 1.00 7.40  ? 831  ILE A N   1 
ATOM   6737 C  CA  . ILE A 1 831  ? 31.946 63.083  -13.769 1.00 8.57  ? 831  ILE A CA  1 
ATOM   6738 C  C   . ILE A 1 831  ? 33.403 63.393  -13.503 1.00 8.19  ? 831  ILE A C   1 
ATOM   6739 O  O   . ILE A 1 831  ? 33.893 64.482  -13.834 1.00 8.69  ? 831  ILE A O   1 
ATOM   6740 C  CB  . ILE A 1 831  ? 31.375 64.035  -14.877 1.00 7.46  ? 831  ILE A CB  1 
ATOM   6741 C  CG1 . ILE A 1 831  ? 29.832 64.088  -14.880 1.00 8.07  ? 831  ILE A CG1 1 
ATOM   6742 C  CG2 . ILE A 1 831  ? 31.951 63.572  -16.217 1.00 8.76  ? 831  ILE A CG2 1 
ATOM   6743 C  CD1 . ILE A 1 831  ? 29.089 62.748  -15.101 1.00 7.41  ? 831  ILE A CD1 1 
ATOM   6744 N  N   . PRO A 1 832  ? 34.137 62.428  -12.921 1.00 7.76  ? 832  PRO A N   1 
ATOM   6745 C  CA  . PRO A 1 832  ? 35.531 62.737  -12.604 1.00 8.57  ? 832  PRO A CA  1 
ATOM   6746 C  C   . PRO A 1 832  ? 36.399 62.871  -13.794 1.00 8.70  ? 832  PRO A C   1 
ATOM   6747 O  O   . PRO A 1 832  ? 37.401 63.622  -13.675 1.00 12.53 ? 832  PRO A O   1 
ATOM   6748 C  CB  . PRO A 1 832  ? 35.969 61.624  -11.590 1.00 8.21  ? 832  PRO A CB  1 
ATOM   6749 C  CG  . PRO A 1 832  ? 34.922 60.565  -11.766 1.00 10.13 ? 832  PRO A CG  1 
ATOM   6750 C  CD  . PRO A 1 832  ? 33.661 61.208  -12.236 1.00 9.16  ? 832  PRO A CD  1 
ATOM   6751 N  N   . SER A 1 833  ? 36.104 62.218  -14.917 1.00 7.83  ? 833  SER A N   1 
ATOM   6752 C  CA  . SER A 1 833  ? 36.948 62.354  -16.109 1.00 8.23  ? 833  SER A CA  1 
ATOM   6753 C  C   . SER A 1 833  ? 36.163 62.185  -17.437 1.00 8.10  ? 833  SER A C   1 
ATOM   6754 O  O   . SER A 1 833  ? 36.696 62.515  -18.484 1.00 7.64  ? 833  SER A O   1 
ATOM   6755 C  CB  . SER A 1 833  ? 38.151 61.419  -16.118 1.00 11.99 ? 833  SER A CB  1 
ATOM   6756 O  OG  . SER A 1 833  ? 37.807 60.124  -16.373 1.00 13.20 ? 833  SER A OG  1 
ATOM   6757 N  N   . GLY A 1 834  ? 34.933 61.655  -17.412 1.00 7.72  ? 834  GLY A N   1 
ATOM   6758 C  CA  . GLY A 1 834  ? 34.220 61.557  -18.682 1.00 8.59  ? 834  GLY A CA  1 
ATOM   6759 C  C   . GLY A 1 834  ? 32.858 60.925  -18.536 1.00 7.09  ? 834  GLY A C   1 
ATOM   6760 O  O   . GLY A 1 834  ? 32.496 60.335  -17.505 1.00 8.54  ? 834  GLY A O   1 
ATOM   6761 N  N   . MET A 1 835  ? 32.077 61.094  -19.615 1.00 7.65  ? 835  MET A N   1 
ATOM   6762 C  CA  . MET A 1 835  ? 30.705 60.548  -19.655 1.00 7.97  ? 835  MET A CA  1 
ATOM   6763 C  C   . MET A 1 835  ? 30.372 60.332  -21.114 1.00 7.43  ? 835  MET A C   1 
ATOM   6764 O  O   . MET A 1 835  ? 30.944 60.953  -22.027 1.00 8.45  ? 835  MET A O   1 
ATOM   6765 C  CB  . MET A 1 835  ? 29.709 61.519  -19.023 1.00 7.80  ? 835  MET A CB  1 
ATOM   6766 C  CG  . MET A 1 835  ? 29.621 62.890  -19.777 1.00 10.31 ? 835  MET A CG  1 
ATOM   6767 S  SD  . MET A 1 835  ? 28.737 64.176  -18.868 1.00 12.69 ? 835  MET A SD  1 
ATOM   6768 C  CE  . MET A 1 835  ? 27.350 63.444  -18.426 1.00 13.32 ? 835  MET A CE  1 
ATOM   6769 N  N   . PHE A 1 836  ? 29.422 59.410  -21.368 1.00 8.00  ? 836  PHE A N   1 
ATOM   6770 C  CA  . PHE A 1 836  ? 28.994 59.191  -22.766 1.00 8.23  ? 836  PHE A CA  1 
ATOM   6771 C  C   . PHE A 1 836  ? 27.599 58.624  -22.803 1.00 8.60  ? 836  PHE A C   1 
ATOM   6772 O  O   . PHE A 1 836  ? 27.058 58.084  -21.835 1.00 8.79  ? 836  PHE A O   1 
ATOM   6773 C  CB  . PHE A 1 836  ? 29.980 58.318  -23.570 1.00 8.30  ? 836  PHE A CB  1 
ATOM   6774 C  CG  . PHE A 1 836  ? 30.173 56.872  -23.120 1.00 8.73  ? 836  PHE A CG  1 
ATOM   6775 C  CD1 . PHE A 1 836  ? 29.323 55.824  -23.590 1.00 9.72  ? 836  PHE A CD1 1 
ATOM   6776 C  CD2 . PHE A 1 836  ? 31.271 56.534  -22.321 1.00 9.20  ? 836  PHE A CD2 1 
ATOM   6777 C  CE1 . PHE A 1 836  ? 29.590 54.487  -23.259 1.00 11.77 ? 836  PHE A CE1 1 
ATOM   6778 C  CE2 . PHE A 1 836  ? 31.528 55.159  -21.998 1.00 10.59 ? 836  PHE A CE2 1 
ATOM   6779 C  CZ  . PHE A 1 836  ? 30.709 54.142  -22.469 1.00 10.82 ? 836  PHE A CZ  1 
ATOM   6780 N  N   . ILE A 1 837  ? 26.984 58.846  -23.987 1.00 8.19  ? 837  ILE A N   1 
ATOM   6781 C  CA  . ILE A 1 837  ? 25.689 58.229  -24.356 1.00 9.99  ? 837  ILE A CA  1 
ATOM   6782 C  C   . ILE A 1 837  ? 25.889 57.586  -25.708 1.00 8.95  ? 837  ILE A C   1 
ATOM   6783 O  O   . ILE A 1 837  ? 26.758 57.978  -26.518 1.00 9.69  ? 837  ILE A O   1 
ATOM   6784 C  CB  . ILE A 1 837  ? 24.538 59.250  -24.409 1.00 9.65  ? 837  ILE A CB  1 
ATOM   6785 C  CG1 . ILE A 1 837  ? 24.932 60.470  -25.236 1.00 10.99 ? 837  ILE A CG1 1 
ATOM   6786 C  CG2 . ILE A 1 837  ? 24.073 59.587  -23.083 1.00 10.66 ? 837  ILE A CG2 1 
ATOM   6787 C  CD1 . ILE A 1 837  ? 23.689 61.343  -25.691 1.00 11.55 ? 837  ILE A CD1 1 
ATOM   6788 N  N   . GLU A 1 838  ? 25.084 56.530  -25.938 1.00 9.85  ? 838  GLU A N   1 
ATOM   6789 C  CA  . GLU A 1 838  ? 25.154 55.829  -27.207 1.00 10.20 ? 838  GLU A CA  1 
ATOM   6790 C  C   . GLU A 1 838  ? 23.853 55.084  -27.525 1.00 9.28  ? 838  GLU A C   1 
ATOM   6791 O  O   . GLU A 1 838  ? 22.987 54.864  -26.682 1.00 10.80 ? 838  GLU A O   1 
ATOM   6792 C  CB  . GLU A 1 838  ? 26.290 54.795  -27.235 1.00 10.80 ? 838  GLU A CB  1 
ATOM   6793 C  CG  . GLU A 1 838  ? 26.089 53.654  -26.214 1.00 12.05 ? 838  GLU A CG  1 
ATOM   6794 C  CD  . GLU A 1 838  ? 27.221 52.647  -26.183 1.00 14.44 ? 838  GLU A CD  1 
ATOM   6795 O  OE1 . GLU A 1 838  ? 27.025 51.646  -25.455 1.00 16.82 ? 838  GLU A OE1 1 
ATOM   6796 O  OE2 . GLU A 1 838  ? 28.235 52.767  -26.842 1.00 16.21 ? 838  GLU A OE2 1 
ATOM   6797 N  N   . ASP A 1 839  ? 23.758 54.802  -28.830 1.00 11.36 ? 839  ASP A N   1 
ATOM   6798 C  CA  . ASP A 1 839  ? 22.680 53.894  -29.284 1.00 10.69 ? 839  ASP A CA  1 
ATOM   6799 C  C   . ASP A 1 839  ? 23.376 52.811  -30.081 1.00 11.93 ? 839  ASP A C   1 
ATOM   6800 O  O   . ASP A 1 839  ? 24.565 52.579  -29.964 1.00 13.65 ? 839  ASP A O   1 
ATOM   6801 C  CB  . ASP A 1 839  ? 21.562 54.608  -30.055 1.00 11.82 ? 839  ASP A CB  1 
ATOM   6802 C  CG  . ASP A 1 839  ? 22.036 55.335  -31.312 1.00 12.10 ? 839  ASP A CG  1 
ATOM   6803 O  OD1 . ASP A 1 839  ? 23.066 54.967  -31.891 1.00 13.44 ? 839  ASP A OD1 1 
ATOM   6804 O  OD2 . ASP A 1 839  ? 21.248 56.283  -31.703 1.00 16.41 ? 839  ASP A OD2 1 
ATOM   6805 N  N   . ALA A 1 840  ? 22.615 52.088  -30.918 1.00 13.58 ? 840  ALA A N   1 
ATOM   6806 C  CA  . ALA A 1 840  ? 23.253 51.056  -31.685 1.00 15.68 ? 840  ALA A CA  1 
ATOM   6807 C  C   . ALA A 1 840  ? 24.347 51.510  -32.629 1.00 14.58 ? 840  ALA A C   1 
ATOM   6808 O  O   . ALA A 1 840  ? 25.303 50.771  -32.894 1.00 15.93 ? 840  ALA A O   1 
ATOM   6809 C  CB  . ALA A 1 840  ? 22.195 50.256  -32.512 1.00 17.87 ? 840  ALA A CB  1 
ATOM   6810 N  N   . ASN A 1 841  ? 24.257 52.747  -33.108 1.00 12.62 ? 841  ASN A N   1 
ATOM   6811 C  CA  . ASN A 1 841  ? 25.173 53.225  -34.110 1.00 12.66 ? 841  ASN A CA  1 
ATOM   6812 C  C   . ASN A 1 841  ? 26.146 54.337  -33.787 1.00 10.29 ? 841  ASN A C   1 
ATOM   6813 O  O   . ASN A 1 841  ? 27.188 54.432  -34.417 1.00 12.92 ? 841  ASN A O   1 
ATOM   6814 C  CB  . ASN A 1 841  ? 24.332 53.651  -35.363 1.00 13.50 ? 841  ASN A CB  1 
ATOM   6815 C  CG  . ASN A 1 841  ? 23.577 52.464  -35.958 1.00 17.91 ? 841  ASN A CG  1 
ATOM   6816 O  OD1 . ASN A 1 841  ? 24.155 51.396  -36.136 1.00 19.98 ? 841  ASN A OD1 1 
ATOM   6817 N  ND2 . ASN A 1 841  ? 22.307 52.651  -36.217 1.00 21.96 ? 841  ASN A ND2 1 
ATOM   6818 N  N   . THR A 1 842  ? 25.728 55.145  -32.833 1.00 10.93 ? 842  THR A N   1 
ATOM   6819 C  CA  . THR A 1 842  ? 26.463 56.398  -32.564 1.00 10.94 ? 842  THR A CA  1 
ATOM   6820 C  C   . THR A 1 842  ? 26.693 56.552  -31.069 1.00 9.98  ? 842  THR A C   1 
ATOM   6821 O  O   . THR A 1 842  ? 25.808 56.278  -30.256 1.00 12.13 ? 842  THR A O   1 
ATOM   6822 C  CB  . THR A 1 842  ? 25.617 57.619  -33.051 1.00 10.90 ? 842  THR A CB  1 
ATOM   6823 O  OG1 . THR A 1 842  ? 25.250 57.414  -34.442 1.00 14.91 ? 842  THR A OG1 1 
ATOM   6824 C  CG2 . THR A 1 842  ? 26.419 58.879  -33.058 1.00 14.50 ? 842  THR A CG2 1 
ATOM   6825 N  N   . ARG A 1 843  ? 27.849 57.144  -30.785 1.00 10.56 ? 843  ARG A N   1 
ATOM   6826 C  CA  . ARG A 1 843  ? 28.224 57.467  -29.396 1.00 9.93  ? 843  ARG A CA  1 
ATOM   6827 C  C   . ARG A 1 843  ? 28.768 58.925  -29.347 1.00 9.06  ? 843  ARG A C   1 
ATOM   6828 O  O   . ARG A 1 843  ? 29.462 59.363  -30.265 1.00 10.11 ? 843  ARG A O   1 
ATOM   6829 C  CB  . ARG A 1 843  ? 29.331 56.543  -28.878 1.00 10.06 ? 843  ARG A CB  1 
ATOM   6830 C  CG  . ARG A 1 843  ? 29.717 56.830  -27.376 1.00 9.69  ? 843  ARG A CG  1 
ATOM   6831 C  CD  . ARG A 1 843  ? 30.889 55.998  -26.946 1.00 9.35  ? 843  ARG A CD  1 
ATOM   6832 N  NE  . ARG A 1 843  ? 30.510 54.595  -26.681 1.00 10.50 ? 843  ARG A NE  1 
ATOM   6833 C  CZ  . ARG A 1 843  ? 31.350 53.748  -26.104 1.00 11.70 ? 843  ARG A CZ  1 
ATOM   6834 N  NH1 . ARG A 1 843  ? 32.586 54.091  -25.755 1.00 11.72 ? 843  ARG A NH1 1 
ATOM   6835 N  NH2 . ARG A 1 843  ? 30.908 52.511  -25.775 1.00 12.29 ? 843  ARG A NH2 1 
ATOM   6836 N  N   . LEU A 1 844  ? 28.406 59.627  -28.279 1.00 8.93  ? 844  LEU A N   1 
ATOM   6837 C  CA  . LEU A 1 844  ? 28.986 60.980  -28.010 1.00 8.49  ? 844  LEU A CA  1 
ATOM   6838 C  C   . LEU A 1 844  ? 29.635 60.880  -26.601 1.00 8.52  ? 844  LEU A C   1 
ATOM   6839 O  O   . LEU A 1 844  ? 28.979 60.530  -25.629 1.00 9.23  ? 844  LEU A O   1 
ATOM   6840 C  CB  . LEU A 1 844  ? 27.908 62.046  -27.980 1.00 9.57  ? 844  LEU A CB  1 
ATOM   6841 C  CG  . LEU A 1 844  ? 28.541 63.471  -27.879 1.00 10.63 ? 844  LEU A CG  1 
ATOM   6842 C  CD1 . LEU A 1 844  ? 29.442 63.795  -29.083 1.00 12.92 ? 844  LEU A CD1 1 
ATOM   6843 C  CD2 . LEU A 1 844  ? 27.459 64.474  -27.744 1.00 12.95 ? 844  LEU A CD2 1 
ATOM   6844 N  N   . THR A 1 845  ? 30.951 61.119  -26.592 1.00 9.14  ? 845  THR A N   1 
ATOM   6845 C  CA  . THR A 1 845  ? 31.717 61.060  -25.309 1.00 9.05  ? 845  THR A CA  1 
ATOM   6846 C  C   . THR A 1 845  ? 32.262 62.476  -25.013 1.00 8.25  ? 845  THR A C   1 
ATOM   6847 O  O   . THR A 1 845  ? 32.862 63.102  -25.891 1.00 9.09  ? 845  THR A O   1 
ATOM   6848 C  CB  . THR A 1 845  ? 32.923 60.110  -25.416 1.00 8.12  ? 845  THR A CB  1 
ATOM   6849 O  OG1 . THR A 1 845  ? 32.460 58.790  -25.816 1.00 9.72  ? 845  THR A OG1 1 
ATOM   6850 C  CG2 . THR A 1 845  ? 33.649 59.920  -24.067 1.00 9.66  ? 845  THR A CG2 1 
ATOM   6851 N  N   . LEU A 1 846  ? 32.066 62.920  -23.786 1.00 8.16  ? 846  LEU A N   1 
ATOM   6852 C  CA  . LEU A 1 846  ? 32.630 64.193  -23.338 1.00 8.07  ? 846  LEU A CA  1 
ATOM   6853 C  C   . LEU A 1 846  ? 33.686 63.842  -22.267 1.00 7.20  ? 846  LEU A C   1 
ATOM   6854 O  O   . LEU A 1 846  ? 33.313 63.246  -21.206 1.00 8.00  ? 846  LEU A O   1 
ATOM   6855 C  CB  . LEU A 1 846  ? 31.540 65.068  -22.758 1.00 9.43  ? 846  LEU A CB  1 
ATOM   6856 C  CG  . LEU A 1 846  ? 32.028 66.422  -22.230 1.00 9.21  ? 846  LEU A CG  1 
ATOM   6857 C  CD1 . LEU A 1 846  ? 32.454 67.331  -23.404 1.00 10.84 ? 846  LEU A CD1 1 
ATOM   6858 C  CD2 . LEU A 1 846  ? 30.919 67.097  -21.396 1.00 14.75 ? 846  LEU A CD2 1 
ATOM   6859 N  N   . LEU A 1 847  ? 34.950 64.145  -22.541 1.00 8.36  ? 847  LEU A N   1 
ATOM   6860 C  CA  . LEU A 1 847  ? 36.068 63.901  -21.585 1.00 7.46  ? 847  LEU A CA  1 
ATOM   6861 C  C   . LEU A 1 847  ? 36.317 65.211  -20.870 1.00 7.57  ? 847  LEU A C   1 
ATOM   6862 O  O   . LEU A 1 847  ? 36.223 66.295  -21.505 1.00 7.72  ? 847  LEU A O   1 
ATOM   6863 C  CB  . LEU A 1 847  ? 37.330 63.450  -22.287 1.00 8.35  ? 847  LEU A CB  1 
ATOM   6864 C  CG  . LEU A 1 847  ? 37.315 62.089  -22.979 1.00 8.20  ? 847  LEU A CG  1 
ATOM   6865 C  CD1 . LEU A 1 847  ? 36.662 60.987  -22.123 1.00 8.98  ? 847  LEU A CD1 1 
ATOM   6866 C  CD2 . LEU A 1 847  ? 36.598 62.187  -24.363 1.00 10.33 ? 847  LEU A CD2 1 
ATOM   6867 N  N   . THR A 1 848  ? 36.659 65.145  -19.569 1.00 7.81  ? 848  THR A N   1 
ATOM   6868 C  CA  . THR A 1 848  ? 36.886 66.377  -18.783 1.00 7.70  ? 848  THR A CA  1 
ATOM   6869 C  C   . THR A 1 848  ? 38.288 66.466  -18.176 1.00 8.48  ? 848  THR A C   1 
ATOM   6870 O  O   . THR A 1 848  ? 38.982 65.438  -17.923 1.00 9.64  ? 848  THR A O   1 
ATOM   6871 C  CB  . THR A 1 848  ? 35.927 66.485  -17.637 1.00 9.81  ? 848  THR A CB  1 
ATOM   6872 O  OG1 . THR A 1 848  ? 36.388 65.585  -16.572 1.00 13.81 ? 848  THR A OG1 1 
ATOM   6873 C  CG2 . THR A 1 848  ? 34.535 66.195  -17.997 1.00 12.65 ? 848  THR A CG2 1 
ATOM   6874 N  N   . GLY A 1 849  ? 38.762 67.709  -18.037 1.00 7.10  ? 849  GLY A N   1 
ATOM   6875 C  CA  . GLY A 1 849  ? 40.019 67.947  -17.376 1.00 7.55  ? 849  GLY A CA  1 
ATOM   6876 C  C   . GLY A 1 849  ? 39.849 68.289  -15.904 1.00 7.43  ? 849  GLY A C   1 
ATOM   6877 O  O   . GLY A 1 849  ? 40.810 68.714  -15.240 1.00 7.60  ? 849  GLY A O   1 
ATOM   6878 N  N   . GLN A 1 850  ? 38.668 68.113  -15.357 1.00 6.92  ? 850  GLN A N   1 
ATOM   6879 C  CA  . GLN A 1 850  ? 38.365 68.410  -13.971 1.00 7.22  ? 850  GLN A CA  1 
ATOM   6880 C  C   . GLN A 1 850  ? 37.084 67.666  -13.583 1.00 6.83  ? 850  GLN A C   1 
ATOM   6881 O  O   . GLN A 1 850  ? 36.196 67.467  -14.435 1.00 7.99  ? 850  GLN A O   1 
ATOM   6882 C  CB  . GLN A 1 850  ? 38.160 69.962  -13.785 1.00 7.83  ? 850  GLN A CB  1 
ATOM   6883 C  CG  . GLN A 1 850  ? 36.992 70.552  -14.705 1.00 7.49  ? 850  GLN A CG  1 
ATOM   6884 C  CD  . GLN A 1 850  ? 37.359 70.660  -16.161 1.00 7.97  ? 850  GLN A CD  1 
ATOM   6885 O  OE1 . GLN A 1 850  ? 38.480 71.073  -16.538 1.00 8.73  ? 850  GLN A OE1 1 
ATOM   6886 N  NE2 . GLN A 1 850  ? 36.421 70.307  -17.042 1.00 7.75  ? 850  GLN A NE2 1 
ATOM   6887 N  N   . PRO A 1 851  ? 36.939 67.277  -12.317 1.00 6.13  ? 851  PRO A N   1 
ATOM   6888 C  CA  . PRO A 1 851  ? 35.707 66.580  -11.885 1.00 6.43  ? 851  PRO A CA  1 
ATOM   6889 C  C   . PRO A 1 851  ? 34.600 67.598  -11.689 1.00 6.74  ? 851  PRO A C   1 
ATOM   6890 O  O   . PRO A 1 851  ? 34.777 68.640  -11.024 1.00 7.85  ? 851  PRO A O   1 
ATOM   6891 C  CB  . PRO A 1 851  ? 36.116 65.894  -10.566 1.00 7.46  ? 851  PRO A CB  1 
ATOM   6892 C  CG  . PRO A 1 851  ? 37.230 66.833  -10.005 1.00 6.47  ? 851  PRO A CG  1 
ATOM   6893 C  CD  . PRO A 1 851  ? 37.961 67.338  -11.248 1.00 6.24  ? 851  PRO A CD  1 
ATOM   6894 N  N   . LEU A 1 852  ? 33.422 67.266  -12.239 1.00 7.54  ? 852  LEU A N   1 
ATOM   6895 C  CA  . LEU A 1 852  ? 32.226 68.100  -12.141 1.00 8.84  ? 852  LEU A CA  1 
ATOM   6896 C  C   . LEU A 1 852  ? 30.997 67.199  -12.047 1.00 9.49  ? 852  LEU A C   1 
ATOM   6897 O  O   . LEU A 1 852  ? 31.127 65.992  -12.297 1.00 14.43 ? 852  LEU A O   1 
ATOM   6898 C  CB  . LEU A 1 852  ? 32.092 68.982  -13.394 1.00 8.73  ? 852  LEU A CB  1 
ATOM   6899 C  CG  . LEU A 1 852  ? 33.263 70.008  -13.549 1.00 7.40  ? 852  LEU A CG  1 
ATOM   6900 C  CD1 . LEU A 1 852  ? 33.243 70.611  -14.985 1.00 9.37  ? 852  LEU A CD1 1 
ATOM   6901 C  CD2 . LEU A 1 852  ? 33.185 71.118  -12.553 1.00 9.21  ? 852  LEU A CD2 1 
ATOM   6902 N  N   . GLY A 1 853  ? 29.843 67.691  -11.689 1.00 7.41  ? 853  GLY A N   1 
ATOM   6903 C  CA  . GLY A 1 853  ? 28.647 66.833  -11.670 1.00 8.32  ? 853  GLY A CA  1 
ATOM   6904 C  C   . GLY A 1 853  ? 27.905 66.847  -12.963 1.00 8.40  ? 853  GLY A C   1 
ATOM   6905 O  O   . GLY A 1 853  ? 27.924 67.838  -13.721 1.00 8.21  ? 853  GLY A O   1 
ATOM   6906 N  N   . GLY A 1 854  ? 27.232 65.753  -13.289 1.00 7.25  ? 854  GLY A N   1 
ATOM   6907 C  CA  . GLY A 1 854  ? 26.522 65.727  -14.556 1.00 9.38  ? 854  GLY A CA  1 
ATOM   6908 C  C   . GLY A 1 854  ? 25.498 64.615  -14.643 1.00 7.27  ? 854  GLY A C   1 
ATOM   6909 O  O   . GLY A 1 854  ? 25.344 63.785  -13.738 1.00 8.50  ? 854  GLY A O   1 
ATOM   6910 N  N   . SER A 1 855  ? 24.808 64.596  -15.795 1.00 9.11  ? 855  SER A N   1 
ATOM   6911 C  CA  . SER A 1 855  ? 23.748 63.596  -15.995 1.00 9.52  ? 855  SER A CA  1 
ATOM   6912 C  C   . SER A 1 855  ? 23.358 63.578  -17.450 1.00 9.41  ? 855  SER A C   1 
ATOM   6913 O  O   . SER A 1 855  ? 23.913 64.238  -18.329 1.00 9.69  ? 855  SER A O   1 
ATOM   6914 C  CB  . SER A 1 855  ? 22.524 64.056  -15.201 1.00 10.27 ? 855  SER A CB  1 
ATOM   6915 O  OG  . SER A 1 855  ? 21.489 63.051  -15.166 1.00 11.13 ? 855  SER A OG  1 
ATOM   6916 N  N   . SER A 1 856  ? 22.349 62.710  -17.698 1.00 10.25 ? 856  SER A N   1 
ATOM   6917 C  CA  . SER A 1 856  ? 21.642 62.678  -19.026 1.00 9.84  ? 856  SER A CA  1 
ATOM   6918 C  C   . SER A 1 856  ? 20.167 62.667  -18.611 1.00 11.12 ? 856  SER A C   1 
ATOM   6919 O  O   . SER A 1 856  ? 19.646 61.605  -18.216 1.00 12.30 ? 856  SER A O   1 
ATOM   6920 C  CB  . SER A 1 856  ? 22.027 61.419  -19.791 1.00 9.72  ? 856  SER A CB  1 
ATOM   6921 O  OG  . SER A 1 856  ? 21.146 61.332  -20.956 1.00 10.87 ? 856  SER A OG  1 
ATOM   6922 N  N   . LEU A 1 857  ? 19.494 63.836  -18.608 1.00 11.33 ? 857  LEU A N   1 
ATOM   6923 C  CA  . LEU A 1 857  ? 18.132 63.936  -18.118 1.00 11.85 ? 857  LEU A CA  1 
ATOM   6924 C  C   . LEU A 1 857  ? 17.060 63.612  -19.161 1.00 12.11 ? 857  LEU A C   1 
ATOM   6925 O  O   . LEU A 1 857  ? 15.872 63.592  -18.792 1.00 12.38 ? 857  LEU A O   1 
ATOM   6926 C  CB  . LEU A 1 857  ? 17.903 65.345  -17.512 1.00 12.04 ? 857  LEU A CB  1 
ATOM   6927 C  CG  . LEU A 1 857  ? 18.747 65.611  -16.273 1.00 12.08 ? 857  LEU A CG  1 
ATOM   6928 C  CD1 . LEU A 1 857  ? 18.558 67.111  -15.832 1.00 13.42 ? 857  LEU A CD1 1 
ATOM   6929 C  CD2 . LEU A 1 857  ? 18.390 64.634  -15.119 1.00 14.74 ? 857  LEU A CD2 1 
ATOM   6930 N  N   . ALA A 1 858  ? 17.487 63.347  -20.345 1.00 10.30 ? 858  ALA A N   1 
ATOM   6931 C  CA  . ALA A 1 858  ? 16.570 62.945  -21.439 1.00 9.99  ? 858  ALA A CA  1 
ATOM   6932 C  C   . ALA A 1 858  ? 17.369 62.273  -22.491 1.00 13.29 ? 858  ALA A C   1 
ATOM   6933 O  O   . ALA A 1 858  ? 18.591 62.492  -22.644 1.00 11.10 ? 858  ALA A O   1 
ATOM   6934 C  CB  . ALA A 1 858  ? 15.811 64.191  -22.073 1.00 13.95 ? 858  ALA A CB  1 
ATOM   6935 N  N   . SER A 1 859  ? 16.743 61.399  -23.285 1.00 12.11 ? 859  SER A N   1 
ATOM   6936 C  CA  . SER A 1 859  ? 17.391 60.668  -24.321 1.00 11.59 ? 859  SER A CA  1 
ATOM   6937 C  C   . SER A 1 859  ? 18.127 61.609  -25.248 1.00 9.51  ? 859  SER A C   1 
ATOM   6938 O  O   . SER A 1 859  ? 17.553 62.683  -25.601 1.00 12.95 ? 859  SER A O   1 
ATOM   6939 C  CB  . SER A 1 859  ? 16.310 59.845  -25.107 1.00 12.45 ? 859  SER A CB  1 
ATOM   6940 O  OG  . SER A 1 859  ? 16.836 59.074  -26.082 1.00 13.74 ? 859  SER A OG  1 
ATOM   6941 N  N   . GLY A 1 860  ? 19.344 61.259  -25.619 1.00 11.17 ? 860  GLY A N   1 
ATOM   6942 C  CA  . GLY A 1 860  ? 20.142 62.087  -26.505 1.00 11.12 ? 860  GLY A CA  1 
ATOM   6943 C  C   . GLY A 1 860  ? 20.889 63.248  -25.833 1.00 9.90  ? 860  GLY A C   1 
ATOM   6944 O  O   . GLY A 1 860  ? 21.634 63.924  -26.554 1.00 11.43 ? 860  GLY A O   1 
ATOM   6945 N  N   . GLU A 1 861  ? 20.700 63.449  -24.539 1.00 9.73  ? 861  GLU A N   1 
ATOM   6946 C  CA  . GLU A 1 861  ? 21.392 64.569  -23.869 1.00 11.03 ? 861  GLU A CA  1 
ATOM   6947 C  C   . GLU A 1 861  ? 22.530 64.166  -22.951 1.00 11.68 ? 861  GLU A C   1 
ATOM   6948 O  O   . GLU A 1 861  ? 22.591 63.051  -22.419 1.00 11.53 ? 861  GLU A O   1 
ATOM   6949 C  CB  . GLU A 1 861  ? 20.462 65.345  -22.996 1.00 12.57 ? 861  GLU A CB  1 
ATOM   6950 C  CG  . GLU A 1 861  ? 19.349 66.007  -23.736 1.00 14.75 ? 861  GLU A CG  1 
ATOM   6951 C  CD  . GLU A 1 861  ? 18.423 66.832  -22.819 1.00 17.99 ? 861  GLU A CD  1 
ATOM   6952 O  OE1 . GLU A 1 861  ? 18.540 66.895  -21.562 1.00 16.89 ? 861  GLU A OE1 1 
ATOM   6953 O  OE2 . GLU A 1 861  ? 17.453 67.482  -23.362 1.00 19.93 ? 861  GLU A OE2 1 
ATOM   6954 N  N   . LEU A 1 862  ? 23.458 65.086  -22.799 1.00 10.95 ? 862  LEU A N   1 
ATOM   6955 C  CA  . LEU A 1 862  ? 24.510 64.979  -21.754 1.00 11.27 ? 862  LEU A CA  1 
ATOM   6956 C  C   . LEU A 1 862  ? 24.523 66.370  -21.129 1.00 9.72  ? 862  LEU A C   1 
ATOM   6957 O  O   . LEU A 1 862  ? 24.329 67.386  -21.854 1.00 10.16 ? 862  LEU A O   1 
ATOM   6958 C  CB  . LEU A 1 862  ? 25.916 64.705  -22.366 1.00 11.72 ? 862  LEU A CB  1 
ATOM   6959 C  CG  . LEU A 1 862  ? 26.255 63.364  -23.009 1.00 11.62 ? 862  LEU A CG  1 
ATOM   6960 C  CD1 . LEU A 1 862  ? 27.612 63.424  -23.670 1.00 11.94 ? 862  LEU A CD1 1 
ATOM   6961 C  CD2 . LEU A 1 862  ? 26.175 62.266  -21.948 1.00 11.93 ? 862  LEU A CD2 1 
ATOM   6962 N  N   . GLU A 1 863  ? 24.791 66.487  -19.839 1.00 8.89  ? 863  GLU A N   1 
ATOM   6963 C  CA  . GLU A 1 863  ? 24.993 67.814  -19.274 1.00 8.63  ? 863  GLU A CA  1 
ATOM   6964 C  C   . GLU A 1 863  ? 25.988 67.727  -18.137 1.00 9.08  ? 863  GLU A C   1 
ATOM   6965 O  O   . GLU A 1 863  ? 26.102 66.699  -17.452 1.00 8.27  ? 863  GLU A O   1 
ATOM   6966 C  CB  . GLU A 1 863  ? 23.694 68.477  -18.823 1.00 10.20 ? 863  GLU A CB  1 
ATOM   6967 C  CG  . GLU A 1 863  ? 23.061 67.863  -17.584 1.00 10.55 ? 863  GLU A CG  1 
ATOM   6968 C  CD  . GLU A 1 863  ? 21.772 68.602  -17.173 1.00 11.00 ? 863  GLU A CD  1 
ATOM   6969 O  OE1 . GLU A 1 863  ? 21.619 69.128  -16.064 1.00 11.48 ? 863  GLU A OE1 1 
ATOM   6970 O  OE2 . GLU A 1 863  ? 20.886 68.638  -18.079 1.00 13.18 ? 863  GLU A OE2 1 
ATOM   6971 N  N   . ILE A 1 864  ? 26.692 68.838  -17.948 1.00 9.29  ? 864  ILE A N   1 
ATOM   6972 C  CA  . ILE A 1 864  ? 27.732 68.881  -16.877 1.00 9.05  ? 864  ILE A CA  1 
ATOM   6973 C  C   . ILE A 1 864  ? 27.739 70.297  -16.262 1.00 8.19  ? 864  ILE A C   1 
ATOM   6974 O  O   . ILE A 1 864  ? 27.760 71.312  -17.014 1.00 8.30  ? 864  ILE A O   1 
ATOM   6975 C  CB  . ILE A 1 864  ? 29.098 68.439  -17.497 1.00 9.58  ? 864  ILE A CB  1 
ATOM   6976 C  CG1 . ILE A 1 864  ? 30.178 68.378  -16.414 1.00 11.45 ? 864  ILE A CG1 1 
ATOM   6977 C  CG2 . ILE A 1 864  ? 29.471 69.336  -18.646 1.00 12.29 ? 864  ILE A CG2 1 
ATOM   6978 C  CD1 . ILE A 1 864  ? 31.352 67.480  -16.909 1.00 11.29 ? 864  ILE A CD1 1 
ATOM   6979 N  N   . MET A 1 865  ? 27.692 70.363  -14.947 1.00 8.40  ? 865  MET A N   1 
ATOM   6980 C  CA  . MET A 1 865  ? 27.663 71.627  -14.243 1.00 8.59  ? 865  MET A CA  1 
ATOM   6981 C  C   . MET A 1 865  ? 29.018 72.311  -14.296 1.00 8.71  ? 865  MET A C   1 
ATOM   6982 O  O   . MET A 1 865  ? 30.078 71.674  -14.115 1.00 10.21 ? 865  MET A O   1 
ATOM   6983 C  CB  . MET A 1 865  ? 27.216 71.363  -12.812 1.00 8.81  ? 865  MET A CB  1 
ATOM   6984 C  CG  . MET A 1 865  ? 26.587 72.613  -12.136 1.00 8.97  ? 865  MET A CG  1 
ATOM   6985 S  SD  . MET A 1 865  ? 24.961 73.021  -12.869 1.00 11.45 ? 865  MET A SD  1 
ATOM   6986 C  CE  . MET A 1 865  ? 23.959 71.807  -11.955 1.00 12.21 ? 865  MET A CE  1 
ATOM   6987 N  N   . GLN A 1 866  ? 28.997 73.644  -14.460 1.00 9.24  ? 866  GLN A N   1 
ATOM   6988 C  CA  . GLN A 1 866  ? 30.225 74.429  -14.596 1.00 8.31  ? 866  GLN A CA  1 
ATOM   6989 C  C   . GLN A 1 866  ? 30.603 75.115  -13.301 1.00 8.06  ? 866  GLN A C   1 
ATOM   6990 O  O   . GLN A 1 866  ? 31.790 75.182  -12.933 1.00 9.00  ? 866  GLN A O   1 
ATOM   6991 C  CB  . GLN A 1 866  ? 30.040 75.487  -15.720 1.00 9.59  ? 866  GLN A CB  1 
ATOM   6992 C  CG  . GLN A 1 866  ? 29.712 74.862  -17.089 1.00 9.21  ? 866  GLN A CG  1 
ATOM   6993 C  CD  . GLN A 1 866  ? 30.735 73.866  -17.503 1.00 9.20  ? 866  GLN A CD  1 
ATOM   6994 O  OE1 . GLN A 1 866  ? 31.874 74.218  -17.847 1.00 10.77 ? 866  GLN A OE1 1 
ATOM   6995 N  NE2 . GLN A 1 866  ? 30.358 72.587  -17.480 1.00 10.09 ? 866  GLN A NE2 1 
ATOM   6996 N  N   . ASP A 1 867  ? 29.625 75.751  -12.640 1.00 9.52  ? 867  ASP A N   1 
ATOM   6997 C  CA  . ASP A 1 867  ? 29.876 76.384  -11.327 1.00 9.21  ? 867  ASP A CA  1 
ATOM   6998 C  C   . ASP A 1 867  ? 28.548 76.623  -10.658 1.00 8.49  ? 867  ASP A C   1 
ATOM   6999 O  O   . ASP A 1 867  ? 27.462 76.517  -11.341 1.00 9.12  ? 867  ASP A O   1 
ATOM   7000 C  CB  . ASP A 1 867  ? 30.702 77.698  -11.450 1.00 9.16  ? 867  ASP A CB  1 
ATOM   7001 C  CG  . ASP A 1 867  ? 31.387 78.072  -10.135 1.00 9.23  ? 867  ASP A CG  1 
ATOM   7002 O  OD1 . ASP A 1 867  ? 31.239 77.425  -9.082  1.00 9.48  ? 867  ASP A OD1 1 
ATOM   7003 O  OD2 . ASP A 1 867  ? 32.105 79.101  -10.191 1.00 11.27 ? 867  ASP A OD2 1 
ATOM   7004 N  N   . ARG A 1 868  ? 28.582 76.915  -9.393  1.00 9.05  ? 868  ARG A N   1 
ATOM   7005 C  CA  . ARG A 1 868  ? 27.370 77.123  -8.620  1.00 9.36  ? 868  ARG A CA  1 
ATOM   7006 C  C   . ARG A 1 868  ? 27.703 78.132  -7.524  1.00 10.12 ? 868  ARG A C   1 
ATOM   7007 O  O   . ARG A 1 868  ? 28.742 78.057  -6.881  1.00 10.77 ? 868  ARG A O   1 
ATOM   7008 C  CB  . ARG A 1 868  ? 26.857 75.768  -8.024  1.00 8.97  ? 868  ARG A CB  1 
ATOM   7009 C  CG  . ARG A 1 868  ? 27.833 75.025  -7.148  1.00 9.41  ? 868  ARG A CG  1 
ATOM   7010 C  CD  . ARG A 1 868  ? 27.580 73.480  -7.180  1.00 9.78  ? 868  ARG A CD  1 
ATOM   7011 N  NE  . ARG A 1 868  ? 26.200 73.163  -6.751  1.00 9.32  ? 868  ARG A NE  1 
ATOM   7012 C  CZ  . ARG A 1 868  ? 25.860 72.884  -5.513  1.00 9.11  ? 868  ARG A CZ  1 
ATOM   7013 N  NH1 . ARG A 1 868  ? 26.755 72.799  -4.512  1.00 8.99  ? 868  ARG A NH1 1 
ATOM   7014 N  NH2 . ARG A 1 868  ? 24.550 72.752  -5.238  1.00 11.01 ? 868  ARG A NH2 1 
ATOM   7015 N  N   . ARG A 1 869  ? 26.769 79.089  -7.316  1.00 10.36 ? 869  ARG A N   1 
ATOM   7016 C  CA  . ARG A 1 869  ? 26.927 80.162  -6.318  1.00 10.46 ? 869  ARG A CA  1 
ATOM   7017 C  C   . ARG A 1 869  ? 25.642 80.149  -5.527  1.00 12.17 ? 869  ARG A C   1 
ATOM   7018 O  O   . ARG A 1 869  ? 24.555 80.353  -6.096  1.00 12.46 ? 869  ARG A O   1 
ATOM   7019 C  CB  . ARG A 1 869  ? 27.194 81.476  -7.062  1.00 11.75 ? 869  ARG A CB  1 
ATOM   7020 C  CG  . ARG A 1 869  ? 27.367 82.638  -6.112  1.00 11.49 ? 869  ARG A CG  1 
ATOM   7021 C  CD  . ARG A 1 869  ? 27.695 83.894  -6.907  1.00 15.26 ? 869  ARG A CD  1 
ATOM   7022 N  NE  . ARG A 1 869  ? 27.822 85.081  -6.034  1.00 17.54 ? 869  ARG A NE  1 
ATOM   7023 C  CZ  . ARG A 1 869  ? 28.932 85.428  -5.412  1.00 15.99 ? 869  ARG A CZ  1 
ATOM   7024 N  NH1 . ARG A 1 869  ? 30.017 84.720  -5.545  1.00 15.75 ? 869  ARG A NH1 1 
ATOM   7025 N  NH2 . ARG A 1 869  ? 28.945 86.529  -4.625  1.00 19.63 ? 869  ARG A NH2 1 
ATOM   7026 N  N   . LEU A 1 870  ? 25.782 79.866  -4.249  1.00 12.72 ? 870  LEU A N   1 
ATOM   7027 C  CA  . LEU A 1 870  ? 24.635 79.640  -3.346  1.00 12.71 ? 870  LEU A CA  1 
ATOM   7028 C  C   . LEU A 1 870  ? 24.730 80.489  -2.109  1.00 14.21 ? 870  LEU A C   1 
ATOM   7029 O  O   . LEU A 1 870  ? 25.674 80.428  -1.373  1.00 14.72 ? 870  LEU A O   1 
ATOM   7030 C  CB  . LEU A 1 870  ? 24.626 78.167  -2.949  1.00 13.01 ? 870  LEU A CB  1 
ATOM   7031 C  CG  . LEU A 1 870  ? 24.599 77.302  -4.221  1.00 18.69 ? 870  LEU A CG  1 
ATOM   7032 C  CD1 . LEU A 1 870  ? 25.119 75.977  -3.860  1.00 18.97 ? 870  LEU A CD1 1 
ATOM   7033 C  CD2 . LEU A 1 870  ? 23.266 77.275  -4.966  1.00 15.33 ? 870  LEU A CD2 1 
ATOM   7034 N  N   . ALA A 1 871  ? 23.637 81.206  -1.838  1.00 14.60 ? 871  ALA A N   1 
ATOM   7035 C  CA  . ALA A 1 871  ? 23.658 82.108  -0.685  1.00 17.00 ? 871  ALA A CA  1 
ATOM   7036 C  C   . ALA A 1 871  ? 23.379 81.433  0.665   1.00 19.42 ? 871  ALA A C   1 
ATOM   7037 O  O   . ALA A 1 871  ? 23.783 81.939  1.709   1.00 22.48 ? 871  ALA A O   1 
ATOM   7038 C  CB  . ALA A 1 871  ? 22.617 83.233  -0.931  1.00 18.70 ? 871  ALA A CB  1 
ATOM   7039 N  N   . SER A 1 872  ? 22.738 80.280  0.630   1.00 17.08 ? 872  SER A N   1 
ATOM   7040 C  CA  . SER A 1 872  ? 22.339 79.593  1.858   1.00 17.72 ? 872  SER A CA  1 
ATOM   7041 C  C   . SER A 1 872  ? 23.195 78.427  2.278   1.00 15.14 ? 872  SER A C   1 
ATOM   7042 O  O   . SER A 1 872  ? 23.841 77.801  1.428   1.00 17.14 ? 872  SER A O   1 
ATOM   7043 C  CB  . SER A 1 872  ? 20.897 79.068  1.663   1.00 20.64 ? 872  SER A CB  1 
ATOM   7044 O  OG  . SER A 1 872  ? 19.984 80.146  1.474   1.00 25.93 ? 872  SER A OG  1 
ATOM   7045 N  N   . ASP A 1 873  ? 23.222 78.171  3.580   1.00 15.83 ? 873  ASP A N   1 
ATOM   7046 C  CA  . ASP A 1 873  ? 23.885 76.989  4.151   1.00 16.48 ? 873  ASP A CA  1 
ATOM   7047 C  C   . ASP A 1 873  ? 22.844 75.846  3.979   1.00 16.21 ? 873  ASP A C   1 
ATOM   7048 O  O   . ASP A 1 873  ? 21.614 76.084  4.022   1.00 17.30 ? 873  ASP A O   1 
ATOM   7049 C  CB  . ASP A 1 873  ? 24.176 77.211  5.642   1.00 16.23 ? 873  ASP A CB  1 
ATOM   7050 C  CG  . ASP A 1 873  ? 24.642 75.936  6.335   1.00 16.47 ? 873  ASP A CG  1 
ATOM   7051 O  OD1 . ASP A 1 873  ? 23.894 75.383  7.177   1.00 20.02 ? 873  ASP A OD1 1 
ATOM   7052 O  OD2 . ASP A 1 873  ? 25.752 75.456  5.961   1.00 18.27 ? 873  ASP A OD2 1 
ATOM   7053 N  N   . ASP A 1 874  ? 23.331 74.610  3.805   1.00 14.46 ? 874  ASP A N   1 
ATOM   7054 C  CA  . ASP A 1 874  ? 22.462 73.443  3.594   1.00 11.71 ? 874  ASP A CA  1 
ATOM   7055 C  C   . ASP A 1 874  ? 22.411 72.498  4.783   1.00 13.03 ? 874  ASP A C   1 
ATOM   7056 O  O   . ASP A 1 874  ? 22.180 71.285  4.617   1.00 14.24 ? 874  ASP A O   1 
ATOM   7057 C  CB  . ASP A 1 874  ? 22.803 72.706  2.286   1.00 10.79 ? 874  ASP A CB  1 
ATOM   7058 C  CG  . ASP A 1 874  ? 24.283 72.379  2.156   1.00 10.32 ? 874  ASP A CG  1 
ATOM   7059 O  OD1 . ASP A 1 874  ? 25.073 72.706  3.106   1.00 13.53 ? 874  ASP A OD1 1 
ATOM   7060 O  OD2 . ASP A 1 874  ? 24.609 71.810  1.095   1.00 11.68 ? 874  ASP A OD2 1 
ATOM   7061 N  N   . GLU A 1 875  ? 22.670 73.031  5.974   1.00 13.36 ? 875  GLU A N   1 
ATOM   7062 C  CA  . GLU A 1 875  ? 22.453 72.295  7.221   1.00 15.45 ? 875  GLU A CA  1 
ATOM   7063 C  C   . GLU A 1 875  ? 23.215 71.029  7.437   1.00 15.15 ? 875  GLU A C   1 
ATOM   7064 O  O   . GLU A 1 875  ? 22.716 70.099  8.091   1.00 15.58 ? 875  GLU A O   1 
ATOM   7065 C  CB  . GLU A 1 875  ? 20.941 71.968  7.405   1.00 20.75 ? 875  GLU A CB  1 
ATOM   7066 C  CG  . GLU A 1 875  ? 20.022 73.159  7.139   1.00 27.02 ? 875  GLU A CG  1 
ATOM   7067 C  CD  . GLU A 1 875  ? 18.790 73.119  8.002   1.00 35.16 ? 875  GLU A CD  1 
ATOM   7068 O  OE1 . GLU A 1 875  ? 18.914 73.328  9.234   1.00 43.55 ? 875  GLU A OE1 1 
ATOM   7069 O  OE2 . GLU A 1 875  ? 17.700 72.871  7.461   1.00 39.85 ? 875  GLU A OE2 1 
ATOM   7070 N  N   . ARG A 1 876  ? 24.418 70.956  6.875   1.00 12.97 ? 876  ARG A N   1 
ATOM   7071 C  CA  . ARG A 1 876  ? 25.301 69.787  7.085   1.00 13.60 ? 876  ARG A CA  1 
ATOM   7072 C  C   . ARG A 1 876  ? 26.572 70.126  7.883   1.00 15.39 ? 876  ARG A C   1 
ATOM   7073 O  O   . ARG A 1 876  ? 27.538 69.341  7.885   1.00 17.47 ? 876  ARG A O   1 
ATOM   7074 C  CB  . ARG A 1 876  ? 25.670 69.099  5.761   1.00 13.72 ? 876  ARG A CB  1 
ATOM   7075 C  CG  . ARG A 1 876  ? 24.437 68.576  5.018   1.00 11.87 ? 876  ARG A CG  1 
ATOM   7076 C  CD  . ARG A 1 876  ? 23.637 67.622  5.906   1.00 12.44 ? 876  ARG A CD  1 
ATOM   7077 N  NE  . ARG A 1 876  ? 22.544 66.907  5.215   1.00 11.87 ? 876  ARG A NE  1 
ATOM   7078 C  CZ  . ARG A 1 876  ? 21.347 67.444  4.908   1.00 12.55 ? 876  ARG A CZ  1 
ATOM   7079 N  NH1 . ARG A 1 876  ? 21.099 68.736  5.183   1.00 11.91 ? 876  ARG A NH1 1 
ATOM   7080 N  NH2 . ARG A 1 876  ? 20.383 66.658  4.400   1.00 12.13 ? 876  ARG A NH2 1 
ATOM   7081 N  N   . GLY A 1 877  ? 26.564 71.277  8.520   1.00 17.39 ? 877  GLY A N   1 
ATOM   7082 C  CA  . GLY A 1 877  ? 27.734 71.633  9.346   1.00 17.58 ? 877  GLY A CA  1 
ATOM   7083 C  C   . GLY A 1 877  ? 28.687 72.688  8.840   1.00 16.63 ? 877  GLY A C   1 
ATOM   7084 O  O   . GLY A 1 877  ? 29.474 73.240  9.646   1.00 19.32 ? 877  GLY A O   1 
ATOM   7085 N  N   . LEU A 1 878  ? 28.606 73.058  7.563   1.00 15.10 ? 878  LEU A N   1 
ATOM   7086 C  CA  . LEU A 1 878  ? 29.546 74.060  7.047   1.00 16.05 ? 878  LEU A CA  1 
ATOM   7087 C  C   . LEU A 1 878  ? 29.271 75.486  7.545   1.00 15.27 ? 878  LEU A C   1 
ATOM   7088 O  O   . LEU A 1 878  ? 30.233 76.253  7.789   1.00 16.75 ? 878  LEU A O   1 
ATOM   7089 C  CB  . LEU A 1 878  ? 29.535 73.982  5.510   1.00 13.27 ? 878  LEU A CB  1 
ATOM   7090 C  CG  . LEU A 1 878  ? 30.324 75.052  4.762   1.00 13.39 ? 878  LEU A CG  1 
ATOM   7091 C  CD1 . LEU A 1 878  ? 31.831 75.026  5.218   1.00 12.58 ? 878  LEU A CD1 1 
ATOM   7092 C  CD2 . LEU A 1 878  ? 30.207 74.788  3.237   1.00 15.13 ? 878  LEU A CD2 1 
ATOM   7093 N  N   . GLY A 1 879  ? 27.983 75.843  7.698   1.00 15.81 ? 879  GLY A N   1 
ATOM   7094 C  CA  . GLY A 1 879  ? 27.629 77.152  8.228   1.00 17.99 ? 879  GLY A CA  1 
ATOM   7095 C  C   . GLY A 1 879  ? 27.859 78.347  7.314   1.00 19.86 ? 879  GLY A C   1 
ATOM   7096 O  O   . GLY A 1 879  ? 28.039 79.465  7.766   1.00 21.14 ? 879  GLY A O   1 
ATOM   7097 N  N   . GLN A 1 880  ? 27.904 78.103  6.013   1.00 16.78 ? 880  GLN A N   1 
ATOM   7098 C  CA  . GLN A 1 880  ? 28.008 79.205  5.066   1.00 14.99 ? 880  GLN A CA  1 
ATOM   7099 C  C   . GLN A 1 880  ? 27.517 78.658  3.724   1.00 14.73 ? 880  GLN A C   1 
ATOM   7100 O  O   . GLN A 1 880  ? 27.444 77.429  3.552   1.00 16.17 ? 880  GLN A O   1 
ATOM   7101 C  CB  . GLN A 1 880  ? 29.461 79.719  4.928   1.00 14.28 ? 880  GLN A CB  1 
ATOM   7102 C  CG  . GLN A 1 880  ? 30.494 78.671  4.407   1.00 16.31 ? 880  GLN A CG  1 
ATOM   7103 C  CD  . GLN A 1 880  ? 31.760 79.334  3.812   1.00 15.39 ? 880  GLN A CD  1 
ATOM   7104 O  OE1 . GLN A 1 880  ? 31.835 79.600  2.606   1.00 20.00 ? 880  GLN A OE1 1 
ATOM   7105 N  NE2 . GLN A 1 880  ? 32.706 79.586  4.633   1.00 12.77 ? 880  GLN A NE2 1 
ATOM   7106 N  N   . GLY A 1 881  ? 27.195 79.559  2.804   1.00 17.39 ? 881  GLY A N   1 
ATOM   7107 C  CA  . GLY A 1 881  ? 26.872 79.166  1.433   1.00 18.12 ? 881  GLY A CA  1 
ATOM   7108 C  C   . GLY A 1 881  ? 28.184 79.089  0.626   1.00 17.54 ? 881  GLY A C   1 
ATOM   7109 O  O   . GLY A 1 881  ? 29.313 78.920  1.185   1.00 18.05 ? 881  GLY A O   1 
ATOM   7110 N  N   . VAL A 1 882  ? 28.036 79.198  -0.691  1.00 14.53 ? 882  VAL A N   1 
ATOM   7111 C  CA  . VAL A 1 882  ? 29.207 79.141  -1.569  1.00 12.38 ? 882  VAL A CA  1 
ATOM   7112 C  C   . VAL A 1 882  ? 29.135 80.457  -2.335  1.00 12.02 ? 882  VAL A C   1 
ATOM   7113 O  O   . VAL A 1 882  ? 28.400 80.628  -3.310  1.00 12.92 ? 882  VAL A O   1 
ATOM   7114 C  CB  . VAL A 1 882  ? 29.128 77.940  -2.484  1.00 13.08 ? 882  VAL A CB  1 
ATOM   7115 C  CG1 . VAL A 1 882  ? 30.227 77.975  -3.513  1.00 13.33 ? 882  VAL A CG1 1 
ATOM   7116 C  CG2 . VAL A 1 882  ? 29.272 76.680  -1.635  1.00 14.38 ? 882  VAL A CG2 1 
ATOM   7117 N  N   . LEU A 1 883  ? 29.924 81.419  -1.844  1.00 12.99 ? 883  LEU A N   1 
ATOM   7118 C  CA  . LEU A 1 883  ? 29.911 82.783  -2.436  1.00 14.52 ? 883  LEU A CA  1 
ATOM   7119 C  C   . LEU A 1 883  ? 31.330 83.278  -2.753  1.00 17.23 ? 883  LEU A C   1 
ATOM   7120 O  O   . LEU A 1 883  ? 31.532 84.490  -2.933  1.00 20.22 ? 883  LEU A O   1 
ATOM   7121 C  CB  . LEU A 1 883  ? 29.226 83.794  -1.461  1.00 15.92 ? 883  LEU A CB  1 
ATOM   7122 C  CG  . LEU A 1 883  ? 27.741 83.516  -1.201  1.00 14.33 ? 883  LEU A CG  1 
ATOM   7123 C  CD1 . LEU A 1 883  ? 27.157 84.500  -0.124  1.00 17.53 ? 883  LEU A CD1 1 
ATOM   7124 C  CD2 . LEU A 1 883  ? 26.976 83.720  -2.544  1.00 16.98 ? 883  LEU A CD2 1 
ATOM   7125 N  N   . ASP A 1 884  ? 32.305 82.375  -2.805  1.00 12.44 ? 884  ASP A N   1 
ATOM   7126 C  CA  . ASP A 1 884  ? 33.722 82.655  -3.057  1.00 11.50 ? 884  ASP A CA  1 
ATOM   7127 C  C   . ASP A 1 884  ? 34.200 82.177  -4.426  1.00 11.49 ? 884  ASP A C   1 
ATOM   7128 O  O   . ASP A 1 884  ? 35.386 81.922  -4.631  1.00 13.26 ? 884  ASP A O   1 
ATOM   7129 C  CB  . ASP A 1 884  ? 34.597 82.029  -1.944  1.00 14.29 ? 884  ASP A CB  1 
ATOM   7130 C  CG  . ASP A 1 884  ? 34.374 80.488  -1.766  1.00 15.10 ? 884  ASP A CG  1 
ATOM   7131 O  OD1 . ASP A 1 884  ? 35.087 79.938  -0.872  1.00 17.43 ? 884  ASP A OD1 1 
ATOM   7132 O  OD2 . ASP A 1 884  ? 33.535 79.854  -2.474  1.00 13.61 ? 884  ASP A OD2 1 
ATOM   7133 N  N   . ASN A 1 885  ? 33.260 82.147  -5.374  1.00 11.24 ? 885  ASN A N   1 
ATOM   7134 C  CA  . ASN A 1 885  ? 33.583 81.761  -6.734  1.00 11.91 ? 885  ASN A CA  1 
ATOM   7135 C  C   . ASN A 1 885  ? 34.649 82.630  -7.347  1.00 12.47 ? 885  ASN A C   1 
ATOM   7136 O  O   . ASN A 1 885  ? 34.783 83.823  -7.034  1.00 13.22 ? 885  ASN A O   1 
ATOM   7137 C  CB  . ASN A 1 885  ? 32.326 81.884  -7.623  1.00 10.74 ? 885  ASN A CB  1 
ATOM   7138 C  CG  . ASN A 1 885  ? 31.154 81.168  -7.041  1.00 11.77 ? 885  ASN A CG  1 
ATOM   7139 O  OD1 . ASN A 1 885  ? 30.831 80.010  -7.468  1.00 14.22 ? 885  ASN A OD1 1 
ATOM   7140 N  ND2 . ASN A 1 885  ? 30.472 81.786  -6.126  1.00 11.14 ? 885  ASN A ND2 1 
ATOM   7141 N  N   . LYS A 1 886  ? 35.444 82.040  -8.222  1.00 11.57 ? 886  LYS A N   1 
ATOM   7142 C  CA  . LYS A 1 886  ? 36.445 82.789  -8.967  1.00 13.84 ? 886  LYS A CA  1 
ATOM   7143 C  C   . LYS A 1 886  ? 36.516 82.209  -10.374 1.00 11.65 ? 886  LYS A C   1 
ATOM   7144 O  O   . LYS A 1 886  ? 36.146 81.045  -10.624 1.00 12.47 ? 886  LYS A O   1 
ATOM   7145 C  CB  . LYS A 1 886  ? 37.795 82.723  -8.236  1.00 18.89 ? 886  LYS A CB  1 
ATOM   7146 C  CG  . LYS A 1 886  ? 38.342 81.323  -8.073  1.00 17.90 ? 886  LYS A CG  1 
ATOM   7147 C  CD  . LYS A 1 886  ? 39.383 81.143  -6.904  1.00 22.90 ? 886  LYS A CD  1 
ATOM   7148 C  CE  . LYS A 1 886  ? 40.711 81.656  -7.392  1.00 20.88 ? 886  LYS A CE  1 
ATOM   7149 N  NZ  . LYS A 1 886  ? 41.888 81.749  -6.477  1.00 21.94 ? 886  LYS A NZ  1 
ATOM   7150 N  N   . PRO A 1 887  ? 37.015 82.972  -11.337 1.00 10.23 ? 887  PRO A N   1 
ATOM   7151 C  CA  . PRO A 1 887  ? 37.120 82.495  -12.711 1.00 9.98  ? 887  PRO A CA  1 
ATOM   7152 C  C   . PRO A 1 887  ? 37.898 81.217  -12.800 1.00 10.18 ? 887  PRO A C   1 
ATOM   7153 O  O   . PRO A 1 887  ? 38.965 81.088  -12.185 1.00 10.93 ? 887  PRO A O   1 
ATOM   7154 C  CB  . PRO A 1 887  ? 37.868 83.638  -13.424 1.00 12.20 ? 887  PRO A CB  1 
ATOM   7155 C  CG  . PRO A 1 887  ? 37.357 84.885  -12.623 1.00 12.55 ? 887  PRO A CG  1 
ATOM   7156 C  CD  . PRO A 1 887  ? 37.372 84.413  -11.214 1.00 12.59 ? 887  PRO A CD  1 
ATOM   7157 N  N   . VAL A 1 888  ? 37.385 80.249  -13.556 1.00 8.87  ? 888  VAL A N   1 
ATOM   7158 C  CA  . VAL A 1 888  ? 38.071 78.968  -13.775 1.00 8.66  ? 888  VAL A CA  1 
ATOM   7159 C  C   . VAL A 1 888  ? 38.011 78.610  -15.233 1.00 8.50  ? 888  VAL A C   1 
ATOM   7160 O  O   . VAL A 1 888  ? 36.963 78.859  -15.902 1.00 9.76  ? 888  VAL A O   1 
ATOM   7161 C  CB  . VAL A 1 888  ? 37.446 77.819  -12.872 1.00 9.86  ? 888  VAL A CB  1 
ATOM   7162 C  CG1 . VAL A 1 888  ? 35.901 77.718  -13.070 1.00 10.12 ? 888  VAL A CG1 1 
ATOM   7163 C  CG2 . VAL A 1 888  ? 38.121 76.507  -13.137 1.00 10.33 ? 888  VAL A CG2 1 
ATOM   7164 N  N   . LEU A 1 889  ? 39.072 78.032  -15.779 1.00 7.38  ? 889  LEU A N   1 
ATOM   7165 C  CA  . LEU A 1 889  ? 39.081 77.561  -17.151 1.00 8.57  ? 889  LEU A CA  1 
ATOM   7166 C  C   . LEU A 1 889  ? 38.881 76.036  -17.173 1.00 8.39  ? 889  LEU A C   1 
ATOM   7167 O  O   . LEU A 1 889  ? 39.775 75.251  -16.866 1.00 10.82 ? 889  LEU A O   1 
ATOM   7168 C  CB  . LEU A 1 889  ? 40.419 77.915  -17.819 1.00 9.76  ? 889  LEU A CB  1 
ATOM   7169 C  CG  . LEU A 1 889  ? 40.425 77.490  -19.325 1.00 10.15 ? 889  LEU A CG  1 
ATOM   7170 C  CD1 . LEU A 1 889  ? 39.521 78.452  -20.160 1.00 12.19 ? 889  LEU A CD1 1 
ATOM   7171 C  CD2 . LEU A 1 889  ? 41.880 77.528  -19.833 1.00 15.18 ? 889  LEU A CD2 1 
ATOM   7172 N  N   . HIS A 1 890  ? 37.663 75.619  -17.490 1.00 7.20  ? 890  HIS A N   1 
ATOM   7173 C  CA  . HIS A 1 890  ? 37.337 74.184  -17.632 1.00 7.37  ? 890  HIS A CA  1 
ATOM   7174 C  C   . HIS A 1 890  ? 37.718 73.718  -19.009 1.00 7.55  ? 890  HIS A C   1 
ATOM   7175 O  O   . HIS A 1 890  ? 37.490 74.449  -20.016 1.00 9.17  ? 890  HIS A O   1 
ATOM   7176 C  CB  . HIS A 1 890  ? 35.827 73.943  -17.413 1.00 7.89  ? 890  HIS A CB  1 
ATOM   7177 C  CG  . HIS A 1 890  ? 35.402 74.120  -16.006 1.00 8.57  ? 890  HIS A CG  1 
ATOM   7178 N  ND1 . HIS A 1 890  ? 36.220 73.775  -14.928 1.00 11.16 ? 890  HIS A ND1 1 
ATOM   7179 C  CD2 . HIS A 1 890  ? 34.229 74.539  -15.485 1.00 9.14  ? 890  HIS A CD2 1 
ATOM   7180 C  CE1 . HIS A 1 890  ? 35.541 73.979  -13.817 1.00 11.04 ? 890  HIS A CE1 1 
ATOM   7181 N  NE2 . HIS A 1 890  ? 34.332 74.431  -14.120 1.00 9.42  ? 890  HIS A NE2 1 
ATOM   7182 N  N   . ILE A 1 891  ? 38.254 72.509  -19.125 1.00 7.38  ? 891  ILE A N   1 
ATOM   7183 C  CA  . ILE A 1 891  ? 38.658 71.973  -20.420 1.00 6.46  ? 891  ILE A CA  1 
ATOM   7184 C  C   . ILE A 1 891  ? 38.008 70.615  -20.703 1.00 6.93  ? 891  ILE A C   1 
ATOM   7185 O  O   . ILE A 1 891  ? 37.726 69.843  -19.739 1.00 7.43  ? 891  ILE A O   1 
ATOM   7186 C  CB  . ILE A 1 891  ? 40.197 71.919  -20.547 1.00 7.91  ? 891  ILE A CB  1 
ATOM   7187 C  CG1 . ILE A 1 891  ? 40.785 70.896  -19.561 1.00 9.05  ? 891  ILE A CG1 1 
ATOM   7188 C  CG2 . ILE A 1 891  ? 40.750 73.373  -20.334 1.00 10.66 ? 891  ILE A CG2 1 
ATOM   7189 C  CD1 . ILE A 1 891  ? 42.322 70.757  -19.791 1.00 9.93  ? 891  ILE A CD1 1 
ATOM   7190 N  N   . TYR A 1 892  ? 37.780 70.325  -21.962 1.00 7.12  ? 892  TYR A N   1 
ATOM   7191 C  CA  . TYR A 1 892  ? 37.100 69.106  -22.417 1.00 5.97  ? 892  TYR A CA  1 
ATOM   7192 C  C   . TYR A 1 892  ? 37.517 68.684  -23.769 1.00 6.90  ? 892  TYR A C   1 
ATOM   7193 O  O   . TYR A 1 892  ? 38.125 69.456  -24.538 1.00 8.13  ? 892  TYR A O   1 
ATOM   7194 C  CB  . TYR A 1 892  ? 35.558 69.336  -22.518 1.00 7.33  ? 892  TYR A CB  1 
ATOM   7195 C  CG  . TYR A 1 892  ? 34.898 70.007  -21.361 1.00 6.51  ? 892  TYR A CG  1 
ATOM   7196 C  CD1 . TYR A 1 892  ? 34.861 71.397  -21.235 1.00 7.52  ? 892  TYR A CD1 1 
ATOM   7197 C  CD2 . TYR A 1 892  ? 34.323 69.231  -20.329 1.00 7.77  ? 892  TYR A CD2 1 
ATOM   7198 C  CE1 . TYR A 1 892  ? 34.257 71.988  -20.151 1.00 8.24  ? 892  TYR A CE1 1 
ATOM   7199 C  CE2 . TYR A 1 892  ? 33.747 69.798  -19.239 1.00 7.73  ? 892  TYR A CE2 1 
ATOM   7200 C  CZ  . TYR A 1 892  ? 33.715 71.191  -19.141 1.00 7.37  ? 892  TYR A CZ  1 
ATOM   7201 O  OH  . TYR A 1 892  ? 33.112 71.742  -18.034 1.00 8.92  ? 892  TYR A OH  1 
ATOM   7202 N  N   . ARG A 1 893  ? 37.224 67.407  -24.096 1.00 7.16  ? 893  ARG A N   1 
ATOM   7203 C  CA  . ARG A 1 893  ? 37.334 66.962  -25.505 1.00 7.90  ? 893  ARG A CA  1 
ATOM   7204 C  C   . ARG A 1 893  ? 35.958 66.328  -25.788 1.00 8.02  ? 893  ARG A C   1 
ATOM   7205 O  O   . ARG A 1 893  ? 35.349 65.711  -24.937 1.00 9.36  ? 893  ARG A O   1 
ATOM   7206 C  CB  . ARG A 1 893  ? 38.404 65.908  -25.741 1.00 7.75  ? 893  ARG A CB  1 
ATOM   7207 C  CG  . ARG A 1 893  ? 39.843 66.403  -25.585 1.00 9.12  ? 893  ARG A CG  1 
ATOM   7208 C  CD  . ARG A 1 893  ? 40.284 67.420  -26.665 1.00 9.02  ? 893  ARG A CD  1 
ATOM   7209 N  NE  . ARG A 1 893  ? 40.335 66.857  -28.025 1.00 10.17 ? 893  ARG A NE  1 
ATOM   7210 C  CZ  . ARG A 1 893  ? 41.271 66.033  -28.490 1.00 8.81  ? 893  ARG A CZ  1 
ATOM   7211 N  NH1 . ARG A 1 893  ? 42.291 65.602  -27.727 1.00 11.50 ? 893  ARG A NH1 1 
ATOM   7212 N  NH2 . ARG A 1 893  ? 41.233 65.590  -29.756 1.00 12.93 ? 893  ARG A NH2 1 
ATOM   7213 N  N   . LEU A 1 894  ? 35.477 66.550  -27.026 1.00 8.21  ? 894  LEU A N   1 
ATOM   7214 C  CA  . LEU A 1 894  ? 34.133 66.082  -27.468 1.00 9.94  ? 894  LEU A CA  1 
ATOM   7215 C  C   . LEU A 1 894  ? 34.324 65.134  -28.632 1.00 9.35  ? 894  LEU A C   1 
ATOM   7216 O  O   . LEU A 1 894  ? 34.764 65.556  -29.715 1.00 10.21 ? 894  LEU A O   1 
ATOM   7217 C  CB  . LEU A 1 894  ? 33.287 67.295  -27.876 1.00 10.92 ? 894  LEU A CB  1 
ATOM   7218 C  CG  . LEU A 1 894  ? 31.839 66.889  -28.277 1.00 11.67 ? 894  LEU A CG  1 
ATOM   7219 C  CD1 . LEU A 1 894  ? 31.088 66.334  -27.104 1.00 14.86 ? 894  LEU A CD1 1 
ATOM   7220 C  CD2 . LEU A 1 894  ? 31.111 68.134  -28.805 1.00 14.01 ? 894  LEU A CD2 1 
ATOM   7221 N  N   . VAL A 1 895  ? 34.034 63.841  -28.404 1.00 9.42  ? 895  VAL A N   1 
ATOM   7222 C  CA  . VAL A 1 895  ? 34.263 62.803  -29.384 1.00 9.86  ? 895  VAL A CA  1 
ATOM   7223 C  C   . VAL A 1 895  ? 32.957 62.157  -29.854 1.00 11.27 ? 895  VAL A C   1 
ATOM   7224 O  O   . VAL A 1 895  ? 32.264 61.437  -29.093 1.00 10.58 ? 895  VAL A O   1 
ATOM   7225 C  CB  . VAL A 1 895  ? 35.163 61.704  -28.732 1.00 10.57 ? 895  VAL A CB  1 
ATOM   7226 C  CG1 . VAL A 1 895  ? 35.494 60.674  -29.770 1.00 13.80 ? 895  VAL A CG1 1 
ATOM   7227 C  CG2 . VAL A 1 895  ? 36.427 62.350  -28.130 1.00 12.98 ? 895  VAL A CG2 1 
ATOM   7228 N  N   . LEU A 1 896  ? 32.611 62.431  -31.112 1.00 11.05 ? 896  LEU A N   1 
ATOM   7229 C  CA  . LEU A 1 896  ? 31.425 61.810  -31.755 1.00 10.89 ? 896  LEU A CA  1 
ATOM   7230 C  C   . LEU A 1 896  ? 32.014 60.688  -32.606 1.00 12.22 ? 896  LEU A C   1 
ATOM   7231 O  O   . LEU A 1 896  ? 32.972 60.864  -33.346 1.00 12.62 ? 896  LEU A O   1 
ATOM   7232 C  CB  . LEU A 1 896  ? 30.697 62.818  -32.658 1.00 11.36 ? 896  LEU A CB  1 
ATOM   7233 C  CG  . LEU A 1 896  ? 29.575 62.123  -33.470 1.00 12.50 ? 896  LEU A CG  1 
ATOM   7234 C  CD1 . LEU A 1 896  ? 28.429 61.862  -32.585 1.00 15.00 ? 896  LEU A CD1 1 
ATOM   7235 C  CD2 . LEU A 1 896  ? 29.100 63.110  -34.589 1.00 15.35 ? 896  LEU A CD2 1 
ATOM   7236 N  N   . GLU A 1 897  ? 31.446 59.481  -32.447 1.00 11.76 ? 897  GLU A N   1 
ATOM   7237 C  CA  . GLU A 1 897  ? 31.962 58.322  -33.190 1.00 12.33 ? 897  GLU A CA  1 
ATOM   7238 C  C   . GLU A 1 897  ? 30.849 57.351  -33.587 1.00 11.94 ? 897  GLU A C   1 
ATOM   7239 O  O   . GLU A 1 897  ? 29.819 57.271  -32.918 1.00 12.67 ? 897  GLU A O   1 
ATOM   7240 C  CB  . GLU A 1 897  ? 32.924 57.528  -32.316 1.00 15.79 ? 897  GLU A CB  1 
ATOM   7241 C  CG  . GLU A 1 897  ? 34.004 58.250  -31.546 1.00 20.44 ? 897  GLU A CG  1 
ATOM   7242 C  CD  . GLU A 1 897  ? 34.674 57.329  -30.435 1.00 14.08 ? 897  GLU A CD  1 
ATOM   7243 O  OE1 . GLU A 1 897  ? 34.031 57.069  -29.356 1.00 20.85 ? 897  GLU A OE1 1 
ATOM   7244 O  OE2 . GLU A 1 897  ? 35.838 56.997  -30.731 1.00 23.59 ? 897  GLU A OE2 1 
ATOM   7245 N  N   A LYS A 1 898  ? 31.141 56.574  -34.636 0.50 12.42 ? 898  LYS A N   1 
ATOM   7246 N  N   B LYS A 1 898  ? 31.141 56.574  -34.636 0.50 12.56 ? 898  LYS A N   1 
ATOM   7247 C  CA  A LYS A 1 898  ? 30.246 55.474  -35.046 0.50 13.41 ? 898  LYS A CA  1 
ATOM   7248 C  CA  B LYS A 1 898  ? 30.246 55.474  -35.046 0.50 13.54 ? 898  LYS A CA  1 
ATOM   7249 C  C   A LYS A 1 898  ? 30.726 54.270  -34.242 0.50 15.34 ? 898  LYS A C   1 
ATOM   7250 C  C   B LYS A 1 898  ? 30.726 54.270  -34.242 0.50 15.45 ? 898  LYS A C   1 
ATOM   7251 O  O   A LYS A 1 898  ? 31.931 53.980  -34.177 0.50 20.39 ? 898  LYS A O   1 
ATOM   7252 O  O   B LYS A 1 898  ? 31.931 53.980  -34.177 0.50 20.49 ? 898  LYS A O   1 
ATOM   7253 C  CB  A LYS A 1 898  ? 30.425 55.201  -36.524 0.50 15.91 ? 898  LYS A CB  1 
ATOM   7254 C  CB  B LYS A 1 898  ? 30.425 55.201  -36.524 0.50 16.20 ? 898  LYS A CB  1 
ATOM   7255 C  CG  A LYS A 1 898  ? 29.949 56.319  -37.416 0.50 20.06 ? 898  LYS A CG  1 
ATOM   7256 C  CG  B LYS A 1 898  ? 29.949 56.319  -37.416 0.50 20.29 ? 898  LYS A CG  1 
ATOM   7257 C  CD  A LYS A 1 898  ? 28.513 56.827  -37.113 0.50 25.76 ? 898  LYS A CD  1 
ATOM   7258 C  CD  B LYS A 1 898  ? 28.513 56.827  -37.113 0.50 25.78 ? 898  LYS A CD  1 
ATOM   7259 C  CE  A LYS A 1 898  ? 27.388 55.730  -37.111 0.50 28.76 ? 898  LYS A CE  1 
ATOM   7260 C  CE  B LYS A 1 898  ? 27.372 55.753  -37.225 0.50 28.76 ? 898  LYS A CE  1 
ATOM   7261 N  NZ  A LYS A 1 898  ? 27.155 55.148  -38.458 0.50 33.16 ? 898  LYS A NZ  1 
ATOM   7262 N  NZ  B LYS A 1 898  ? 27.829 54.500  -37.880 0.50 32.96 ? 898  LYS A NZ  1 
ATOM   7263 N  N   . VAL A 1 899  ? 29.787 53.570  -33.618 1.00 13.74 ? 899  VAL A N   1 
ATOM   7264 C  CA  . VAL A 1 899  ? 30.114 52.424  -32.800 1.00 14.29 ? 899  VAL A CA  1 
ATOM   7265 C  C   . VAL A 1 899  ? 29.390 51.139  -33.225 1.00 15.60 ? 899  VAL A C   1 
ATOM   7266 O  O   . VAL A 1 899  ? 29.434 50.117  -32.557 1.00 13.67 ? 899  VAL A O   1 
ATOM   7267 C  CB  . VAL A 1 899  ? 29.821 52.712  -31.304 1.00 13.93 ? 899  VAL A CB  1 
ATOM   7268 C  CG1 . VAL A 1 899  ? 30.846 53.758  -30.761 1.00 17.30 ? 899  VAL A CG1 1 
ATOM   7269 C  CG2 . VAL A 1 899  ? 28.416 53.200  -31.124 1.00 13.68 ? 899  VAL A CG2 1 
ATOM   7270 N  N   . ASN A 1 900  ? 28.736 51.196  -34.377 1.00 15.02 ? 900  ASN A N   1 
ATOM   7271 C  CA  . ASN A 1 900  ? 27.995 50.004  -34.840 1.00 16.08 ? 900  ASN A CA  1 
ATOM   7272 C  C   . ASN A 1 900  ? 28.906 48.767  -35.076 1.00 14.26 ? 900  ASN A C   1 
ATOM   7273 O  O   . ASN A 1 900  ? 28.411 47.630  -35.046 1.00 19.44 ? 900  ASN A O   1 
ATOM   7274 C  CB  . ASN A 1 900  ? 27.220 50.336  -36.157 1.00 16.89 ? 900  ASN A CB  1 
ATOM   7275 C  CG  . ASN A 1 900  ? 28.107 50.880  -37.221 1.00 19.87 ? 900  ASN A CG  1 
ATOM   7276 O  OD1 . ASN A 1 900  ? 28.740 51.937  -37.093 1.00 26.68 ? 900  ASN A OD1 1 
ATOM   7277 N  ND2 . ASN A 1 900  ? 28.209 50.122  -38.328 1.00 24.17 ? 900  ASN A ND2 1 
ATOM   7278 N  N   . ASN A 1 901  ? 30.179 48.969  -35.330 1.00 12.34 ? 901  ASN A N   1 
ATOM   7279 C  CA  . ASN A 1 901  ? 31.128 47.876  -35.546 1.00 14.98 ? 901  ASN A CA  1 
ATOM   7280 C  C   . ASN A 1 901  ? 31.888 47.474  -34.288 1.00 14.34 ? 901  ASN A C   1 
ATOM   7281 O  O   . ASN A 1 901  ? 32.656 46.536  -34.345 1.00 15.68 ? 901  ASN A O   1 
ATOM   7282 C  CB  . ASN A 1 901  ? 32.149 48.289  -36.624 1.00 17.97 ? 901  ASN A CB  1 
ATOM   7283 C  CG  . ASN A 1 901  ? 31.573 48.273  -38.005 1.00 24.68 ? 901  ASN A CG  1 
ATOM   7284 O  OD1 . ASN A 1 901  ? 31.930 49.125  -38.832 1.00 29.94 ? 901  ASN A OD1 1 
ATOM   7285 N  ND2 . ASN A 1 901  ? 30.711 47.311  -38.289 1.00 23.90 ? 901  ASN A ND2 1 
ATOM   7286 N  N   . CYS A 1 902  ? 31.684 48.186  -33.194 1.00 14.31 ? 902  CYS A N   1 
ATOM   7287 C  CA  . CYS A 1 902  ? 32.429 47.877  -31.977 1.00 15.32 ? 902  CYS A CA  1 
ATOM   7288 C  C   . CYS A 1 902  ? 31.889 46.677  -31.214 1.00 12.62 ? 902  CYS A C   1 
ATOM   7289 O  O   . CYS A 1 902  ? 30.655 46.523  -31.070 1.00 15.85 ? 902  CYS A O   1 
ATOM   7290 C  CB  . CYS A 1 902  ? 32.391 49.046  -31.012 1.00 15.39 ? 902  CYS A CB  1 
ATOM   7291 S  SG  . CYS A 1 902  ? 33.144 50.580  -31.618 1.00 18.17 ? 902  CYS A SG  1 
ATOM   7292 N  N   . VAL A 1 903  ? 32.813 45.888  -30.678 1.00 12.48 ? 903  VAL A N   1 
ATOM   7293 C  CA  . VAL A 1 903  ? 32.393 44.747  -29.813 1.00 13.45 ? 903  VAL A CA  1 
ATOM   7294 C  C   . VAL A 1 903  ? 32.110 45.321  -28.415 1.00 14.27 ? 903  VAL A C   1 
ATOM   7295 O  O   . VAL A 1 903  ? 33.028 45.691  -27.658 1.00 15.14 ? 903  VAL A O   1 
ATOM   7296 C  CB  . VAL A 1 903  ? 33.487 43.683  -29.771 1.00 12.93 ? 903  VAL A CB  1 
ATOM   7297 C  CG1 . VAL A 1 903  ? 33.117 42.532  -28.782 1.00 14.89 ? 903  VAL A CG1 1 
ATOM   7298 C  CG2 . VAL A 1 903  ? 33.628 43.131  -31.196 1.00 15.34 ? 903  VAL A CG2 1 
ATOM   7299 N  N   . ARG A 1 904  ? 30.856 45.458  -28.071 1.00 13.48 ? 904  ARG A N   1 
ATOM   7300 C  CA  . ARG A 1 904  ? 30.484 46.053  -26.796 1.00 13.54 ? 904  ARG A CA  1 
ATOM   7301 C  C   . ARG A 1 904  ? 29.920 45.002  -25.841 1.00 13.62 ? 904  ARG A C   1 
ATOM   7302 O  O   . ARG A 1 904  ? 29.545 43.883  -26.253 1.00 13.67 ? 904  ARG A O   1 
ATOM   7303 C  CB  . ARG A 1 904  ? 29.388 47.102  -27.026 1.00 13.80 ? 904  ARG A CB  1 
ATOM   7304 C  CG  . ARG A 1 904  ? 29.950 48.337  -27.677 1.00 16.33 ? 904  ARG A CG  1 
ATOM   7305 C  CD  . ARG A 1 904  ? 28.858 49.359  -27.924 1.00 20.63 ? 904  ARG A CD  1 
ATOM   7306 N  NE  . ARG A 1 904  ? 28.152 49.012  -29.136 1.00 18.71 ? 904  ARG A NE  1 
ATOM   7307 C  CZ  . ARG A 1 904  ? 27.202 49.787  -29.649 1.00 19.51 ? 904  ARG A CZ  1 
ATOM   7308 N  NH1 . ARG A 1 904  ? 26.850 50.934  -29.061 1.00 20.18 ? 904  ARG A NH1 1 
ATOM   7309 N  NH2 . ARG A 1 904  ? 26.596 49.383  -30.757 1.00 20.11 ? 904  ARG A NH2 1 
ATOM   7310 N  N   . PRO A 1 905  ? 29.877 45.324  -24.538 1.00 11.25 ? 905  PRO A N   1 
ATOM   7311 C  CA  . PRO A 1 905  ? 29.303 44.378  -23.573 1.00 12.41 ? 905  PRO A CA  1 
ATOM   7312 C  C   . PRO A 1 905  ? 27.815 44.162  -23.908 1.00 12.30 ? 905  PRO A C   1 
ATOM   7313 O  O   . PRO A 1 905  ? 27.175 44.987  -24.588 1.00 12.98 ? 905  PRO A O   1 
ATOM   7314 C  CB  . PRO A 1 905  ? 29.406 45.134  -22.236 1.00 12.36 ? 905  PRO A CB  1 
ATOM   7315 C  CG  . PRO A 1 905  ? 30.570 46.098  -22.453 1.00 11.73 ? 905  PRO A CG  1 
ATOM   7316 C  CD  . PRO A 1 905  ? 30.373 46.570  -23.883 1.00 11.51 ? 905  PRO A CD  1 
ATOM   7317 N  N   . SER A 1 906  ? 27.259 43.049  -23.433 1.00 12.99 ? 906  SER A N   1 
ATOM   7318 C  CA  . SER A 1 906  ? 25.830 42.799  -23.616 1.00 14.92 ? 906  SER A CA  1 
ATOM   7319 C  C   . SER A 1 906  ? 24.991 43.788  -22.852 1.00 14.88 ? 906  SER A C   1 
ATOM   7320 O  O   . SER A 1 906  ? 25.498 44.543  -21.987 1.00 14.81 ? 906  SER A O   1 
ATOM   7321 C  CB  . SER A 1 906  ? 25.499 41.404  -23.142 1.00 21.44 ? 906  SER A CB  1 
ATOM   7322 O  OG  . SER A 1 906  ? 25.159 41.494  -21.789 1.00 24.76 ? 906  SER A OG  1 
ATOM   7323 N  N   . LYS A 1 907  ? 23.696 43.819  -23.134 1.00 15.54 ? 907  LYS A N   1 
ATOM   7324 C  CA  . LYS A 1 907  ? 22.820 44.769  -22.488 1.00 18.53 ? 907  LYS A CA  1 
ATOM   7325 C  C   . LYS A 1 907  ? 22.743 44.571  -20.981 1.00 16.77 ? 907  LYS A C   1 
ATOM   7326 O  O   . LYS A 1 907  ? 22.351 45.501  -20.281 1.00 22.11 ? 907  LYS A O   1 
ATOM   7327 C  CB  . LYS A 1 907  ? 21.418 44.705  -23.133 1.00 23.96 ? 907  LYS A CB  1 
ATOM   7328 C  CG  . LYS A 1 907  ? 20.640 43.451  -22.809 1.00 31.14 ? 907  LYS A CG  1 
ATOM   7329 C  CD  . LYS A 1 907  ? 19.251 43.483  -23.495 1.00 37.16 ? 907  LYS A CD  1 
ATOM   7330 C  CE  . LYS A 1 907  ? 18.171 44.080  -22.581 1.00 39.27 ? 907  LYS A CE  1 
ATOM   7331 N  NZ  . LYS A 1 907  ? 17.821 43.160  -21.436 1.00 42.67 ? 907  LYS A NZ  1 
ATOM   7332 N  N   . LEU A 1 908  ? 23.130 43.415  -20.468 1.00 15.14 ? 908  LEU A N   1 
ATOM   7333 C  CA  . LEU A 1 908  ? 23.040 43.208  -19.021 1.00 17.06 ? 908  LEU A CA  1 
ATOM   7334 C  C   . LEU A 1 908  ? 24.350 43.501  -18.277 1.00 15.10 ? 908  LEU A C   1 
ATOM   7335 O  O   . LEU A 1 908  ? 24.401 43.424  -17.044 1.00 17.05 ? 908  LEU A O   1 
ATOM   7336 C  CB  . LEU A 1 908  ? 22.586 41.767  -18.700 1.00 21.11 ? 908  LEU A CB  1 
ATOM   7337 C  CG  . LEU A 1 908  ? 21.188 41.338  -19.209 1.00 22.97 ? 908  LEU A CG  1 
ATOM   7338 C  CD1 . LEU A 1 908  ? 20.918 39.882  -18.808 1.00 23.88 ? 908  LEU A CD1 1 
ATOM   7339 C  CD2 . LEU A 1 908  ? 20.080 42.257  -18.626 1.00 23.36 ? 908  LEU A CD2 1 
ATOM   7340 N  N   . HIS A 1 909  ? 25.406 43.843  -19.010 1.00 14.18 ? 909  HIS A N   1 
ATOM   7341 C  CA  . HIS A 1 909  ? 26.708 44.112  -18.358 1.00 12.25 ? 909  HIS A CA  1 
ATOM   7342 C  C   . HIS A 1 909  ? 26.662 45.502  -17.705 1.00 12.60 ? 909  HIS A C   1 
ATOM   7343 O  O   . HIS A 1 909  ? 26.232 46.453  -18.310 1.00 12.72 ? 909  HIS A O   1 
ATOM   7344 C  CB  . HIS A 1 909  ? 27.788 44.043  -19.399 1.00 12.25 ? 909  HIS A CB  1 
ATOM   7345 C  CG  . HIS A 1 909  ? 29.161 43.818  -18.843 1.00 10.23 ? 909  HIS A CG  1 
ATOM   7346 N  ND1 . HIS A 1 909  ? 29.849 44.792  -18.118 1.00 11.89 ? 909  HIS A ND1 1 
ATOM   7347 C  CD2 . HIS A 1 909  ? 29.974 42.741  -18.922 1.00 11.31 ? 909  HIS A CD2 1 
ATOM   7348 C  CE1 . HIS A 1 909  ? 31.034 44.300  -17.790 1.00 11.89 ? 909  HIS A CE1 1 
ATOM   7349 N  NE2 . HIS A 1 909  ? 31.139 43.059  -18.276 1.00 12.87 ? 909  HIS A NE2 1 
ATOM   7350 N  N   . PRO A 1 910  ? 27.149 45.635  -16.492 1.00 9.81  ? 910  PRO A N   1 
ATOM   7351 C  CA  . PRO A 1 910  ? 27.129 46.957  -15.796 1.00 9.57  ? 910  PRO A CA  1 
ATOM   7352 C  C   . PRO A 1 910  ? 28.214 47.939  -16.197 1.00 7.82  ? 910  PRO A C   1 
ATOM   7353 O  O   . PRO A 1 910  ? 28.171 49.047  -15.644 1.00 9.48  ? 910  PRO A O   1 
ATOM   7354 C  CB  . PRO A 1 910  ? 27.201 46.626  -14.308 1.00 10.87 ? 910  PRO A CB  1 
ATOM   7355 C  CG  . PRO A 1 910  ? 27.471 45.123  -14.218 1.00 12.89 ? 910  PRO A CG  1 
ATOM   7356 C  CD  . PRO A 1 910  ? 27.565 44.525  -15.588 1.00 11.32 ? 910  PRO A CD  1 
ATOM   7357 N  N   . ALA A 1 911  ? 29.175 47.559  -17.015 1.00 8.90  ? 911  ALA A N   1 
ATOM   7358 C  CA  . ALA A 1 911  ? 30.260 48.492  -17.412 1.00 9.21  ? 911  ALA A CA  1 
ATOM   7359 C  C   . ALA A 1 911  ? 30.150 48.949  -18.821 1.00 10.39 ? 911  ALA A C   1 
ATOM   7360 O  O   . ALA A 1 911  ? 29.423 48.336  -19.644 1.00 11.13 ? 911  ALA A O   1 
ATOM   7361 C  CB  . ALA A 1 911  ? 31.617 47.812  -17.287 1.00 10.23 ? 911  ALA A CB  1 
ATOM   7362 N  N   . GLY A 1 912  ? 30.903 49.991  -19.152 1.00 9.78  ? 912  GLY A N   1 
ATOM   7363 C  CA  . GLY A 1 912  ? 31.107 50.446  -20.510 1.00 11.80 ? 912  GLY A CA  1 
ATOM   7364 C  C   . GLY A 1 912  ? 32.605 50.715  -20.679 1.00 9.76  ? 912  GLY A C   1 
ATOM   7365 O  O   . GLY A 1 912  ? 33.352 50.829  -19.663 1.00 9.97  ? 912  GLY A O   1 
ATOM   7366 N  N   . TYR A 1 913  ? 33.076 50.865  -21.902 1.00 9.27  ? 913  TYR A N   1 
ATOM   7367 C  CA  . TYR A 1 913  ? 34.498 51.076  -22.193 1.00 9.38  ? 913  TYR A CA  1 
ATOM   7368 C  C   . TYR A 1 913  ? 34.662 52.111  -23.274 1.00 9.95  ? 913  TYR A C   1 
ATOM   7369 O  O   . TYR A 1 913  ? 33.835 52.166  -24.216 1.00 10.83 ? 913  TYR A O   1 
ATOM   7370 C  CB  . TYR A 1 913  ? 35.172 49.758  -22.672 1.00 9.24  ? 913  TYR A CB  1 
ATOM   7371 C  CG  . TYR A 1 913  ? 35.121 48.695  -21.585 1.00 8.22  ? 913  TYR A CG  1 
ATOM   7372 C  CD1 . TYR A 1 913  ? 34.126 47.736  -21.584 1.00 9.49  ? 913  TYR A CD1 1 
ATOM   7373 C  CD2 . TYR A 1 913  ? 36.005 48.752  -20.519 1.00 9.61  ? 913  TYR A CD2 1 
ATOM   7374 C  CE1 . TYR A 1 913  ? 34.033 46.834  -20.493 1.00 11.22 ? 913  TYR A CE1 1 
ATOM   7375 C  CE2 . TYR A 1 913  ? 35.928 47.887  -19.451 1.00 9.16  ? 913  TYR A CE2 1 
ATOM   7376 C  CZ  . TYR A 1 913  ? 34.937 46.926  -19.443 1.00 10.12 ? 913  TYR A CZ  1 
ATOM   7377 O  OH  . TYR A 1 913  ? 34.831 46.051  -18.368 1.00 10.98 ? 913  TYR A OH  1 
ATOM   7378 N  N   . LEU A 1 914  ? 35.744 52.862  -23.189 1.00 8.88  ? 914  LEU A N   1 
ATOM   7379 C  CA  . LEU A 1 914  ? 36.041 53.865  -24.194 1.00 8.86  ? 914  LEU A CA  1 
ATOM   7380 C  C   . LEU A 1 914  ? 36.618 53.260  -25.432 1.00 10.76 ? 914  LEU A C   1 
ATOM   7381 O  O   . LEU A 1 914  ? 37.164 52.141  -25.443 1.00 10.20 ? 914  LEU A O   1 
ATOM   7382 C  CB  . LEU A 1 914  ? 37.125 54.841  -23.630 1.00 9.58  ? 914  LEU A CB  1 
ATOM   7383 C  CG  . LEU A 1 914  ? 36.687 55.739  -22.458 1.00 10.01 ? 914  LEU A CG  1 
ATOM   7384 C  CD1 . LEU A 1 914  ? 37.800 56.762  -22.175 1.00 11.30 ? 914  LEU A CD1 1 
ATOM   7385 C  CD2 . LEU A 1 914  ? 35.326 56.455  -22.749 1.00 9.47  ? 914  LEU A CD2 1 
ATOM   7386 N  N   . THR A 1 915  ? 36.539 54.044  -26.512 1.00 11.09 ? 915  THR A N   1 
ATOM   7387 C  CA  . THR A 1 915  ? 37.263 53.720  -27.731 1.00 10.10 ? 915  THR A CA  1 
ATOM   7388 C  C   . THR A 1 915  ? 38.705 54.286  -27.618 1.00 10.72 ? 915  THR A C   1 
ATOM   7389 O  O   . THR A 1 915  ? 39.022 55.122  -26.707 1.00 11.12 ? 915  THR A O   1 
ATOM   7390 C  CB  . THR A 1 915  ? 36.631 54.441  -28.924 1.00 11.80 ? 915  THR A CB  1 
ATOM   7391 O  OG1 . THR A 1 915  ? 36.657 55.872  -28.631 1.00 14.27 ? 915  THR A OG1 1 
ATOM   7392 C  CG2 . THR A 1 915  ? 35.222 53.964  -29.248 1.00 13.80 ? 915  THR A CG2 1 
ATOM   7393 N  N   A SER A 1 916  ? 39.609 53.886  -28.508 0.50 10.55 ? 916  SER A N   1 
ATOM   7394 N  N   B SER A 1 916  ? 39.609 53.886  -28.508 0.50 12.31 ? 916  SER A N   1 
ATOM   7395 C  CA  A SER A 1 916  ? 40.936 54.418  -28.556 0.50 10.14 ? 916  SER A CA  1 
ATOM   7396 C  CA  B SER A 1 916  ? 40.936 54.418  -28.556 0.50 13.37 ? 916  SER A CA  1 
ATOM   7397 C  C   A SER A 1 916  ? 40.939 55.943  -28.659 0.50 11.42 ? 916  SER A C   1 
ATOM   7398 C  C   B SER A 1 916  ? 40.939 55.943  -28.659 0.50 13.04 ? 916  SER A C   1 
ATOM   7399 O  O   A SER A 1 916  ? 41.665 56.629  -27.911 0.50 10.33 ? 916  SER A O   1 
ATOM   7400 O  O   B SER A 1 916  ? 41.665 56.629  -27.911 0.50 11.37 ? 916  SER A O   1 
ATOM   7401 C  CB  A SER A 1 916  ? 41.669 53.846  -29.799 0.50 10.75 ? 916  SER A CB  1 
ATOM   7402 C  CB  B SER A 1 916  ? 41.669 53.846  -29.799 0.50 16.98 ? 916  SER A CB  1 
ATOM   7403 O  OG  A SER A 1 916  ? 42.867 54.560  -30.031 0.50 11.93 ? 916  SER A OG  1 
ATOM   7404 O  OG  B SER A 1 916  ? 42.112 52.528  -29.541 0.50 25.73 ? 916  SER A OG  1 
ATOM   7405 N  N   . ALA A 1 917  ? 40.116 56.517  -29.523 1.00 10.29 ? 917  ALA A N   1 
ATOM   7406 C  CA  . ALA A 1 917  ? 40.196 57.979  -29.690 1.00 10.88 ? 917  ALA A CA  1 
ATOM   7407 C  C   . ALA A 1 917  ? 39.733 58.677  -28.415 1.00 9.95  ? 917  ALA A C   1 
ATOM   7408 O  O   . ALA A 1 917  ? 40.272 59.753  -28.042 1.00 10.43 ? 917  ALA A O   1 
ATOM   7409 C  CB  . ALA A 1 917  ? 39.312 58.450  -30.855 1.00 12.46 ? 917  ALA A CB  1 
ATOM   7410 N  N   . ALA A 1 918  ? 38.717 58.130  -27.744 1.00 8.94  ? 918  ALA A N   1 
ATOM   7411 C  CA  . ALA A 1 918  ? 38.246 58.808  -26.502 1.00 9.91  ? 918  ALA A CA  1 
ATOM   7412 C  C   . ALA A 1 918  ? 39.284 58.687  -25.398 1.00 8.47  ? 918  ALA A C   1 
ATOM   7413 O  O   . ALA A 1 918  ? 39.496 59.637  -24.620 1.00 9.16  ? 918  ALA A O   1 
ATOM   7414 C  CB  . ALA A 1 918  ? 36.897 58.263  -26.076 1.00 10.40 ? 918  ALA A CB  1 
ATOM   7415 N  N   . HIS A 1 919  ? 39.919 57.537  -25.271 1.00 8.53  ? 919  HIS A N   1 
ATOM   7416 C  CA  . HIS A 1 919  ? 40.950 57.394  -24.257 1.00 7.99  ? 919  HIS A CA  1 
ATOM   7417 C  C   . HIS A 1 919  ? 42.123 58.330  -24.534 1.00 8.83  ? 919  HIS A C   1 
ATOM   7418 O  O   . HIS A 1 919  ? 42.626 59.001  -23.597 1.00 8.43  ? 919  HIS A O   1 
ATOM   7419 C  CB  . HIS A 1 919  ? 41.411 55.914  -24.283 1.00 10.22 ? 919  HIS A CB  1 
ATOM   7420 C  CG  . HIS A 1 919  ? 42.519 55.638  -23.323 1.00 10.89 ? 919  HIS A CG  1 
ATOM   7421 N  ND1 . HIS A 1 919  ? 43.773 55.227  -23.722 1.00 14.98 ? 919  HIS A ND1 1 
ATOM   7422 C  CD2 . HIS A 1 919  ? 42.555 55.759  -21.981 1.00 10.93 ? 919  HIS A CD2 1 
ATOM   7423 C  CE1 . HIS A 1 919  ? 44.556 55.110  -22.656 1.00 13.72 ? 919  HIS A CE1 1 
ATOM   7424 N  NE2 . HIS A 1 919  ? 43.857 55.423  -21.598 1.00 13.72 ? 919  HIS A NE2 1 
ATOM   7425 N  N   . LYS A 1 920  ? 42.617 58.402  -25.765 1.00 9.24  ? 920  LYS A N   1 
ATOM   7426 C  CA  . LYS A 1 920  ? 43.691 59.336  -26.073 1.00 9.67  ? 920  LYS A CA  1 
ATOM   7427 C  C   . LYS A 1 920  ? 43.236 60.770  -25.804 1.00 8.03  ? 920  LYS A C   1 
ATOM   7428 O  O   . LYS A 1 920  ? 44.024 61.603  -25.314 1.00 9.01  ? 920  LYS A O   1 
ATOM   7429 C  CB  . LYS A 1 920  ? 44.161 59.198  -27.521 1.00 11.82 ? 920  LYS A CB  1 
ATOM   7430 C  CG  . LYS A 1 920  ? 45.025 57.929  -27.642 1.00 14.93 ? 920  LYS A CG  1 
ATOM   7431 C  CD  . LYS A 1 920  ? 45.816 57.891  -28.935 1.00 16.89 ? 920  LYS A CD  1 
ATOM   7432 C  CE  . LYS A 1 920  ? 46.678 56.687  -29.029 1.00 15.95 ? 920  LYS A CE  1 
ATOM   7433 N  NZ  . LYS A 1 920  ? 47.900 56.747  -28.134 1.00 16.54 ? 920  LYS A NZ  1 
ATOM   7434 N  N   . ALA A 1 921  ? 41.973 61.108  -26.085 1.00 8.21  ? 921  ALA A N   1 
ATOM   7435 C  CA  . ALA A 1 921  ? 41.510 62.467  -25.814 1.00 8.74  ? 921  ALA A CA  1 
ATOM   7436 C  C   . ALA A 1 921  ? 41.538 62.716  -24.288 1.00 8.21  ? 921  ALA A C   1 
ATOM   7437 O  O   . ALA A 1 921  ? 41.892 63.829  -23.838 1.00 8.72  ? 921  ALA A O   1 
ATOM   7438 C  CB  . ALA A 1 921  ? 40.067 62.633  -26.377 1.00 8.60  ? 921  ALA A CB  1 
ATOM   7439 N  N   . SER A 1 922  ? 41.153 61.717  -23.474 1.00 7.84  ? 922  SER A N   1 
ATOM   7440 C  CA  . SER A 1 922  ? 41.247 61.910  -22.019 1.00 7.23  ? 922  SER A CA  1 
ATOM   7441 C  C   . SER A 1 922  ? 42.716 62.120  -21.598 1.00 8.75  ? 922  SER A C   1 
ATOM   7442 O  O   . SER A 1 922  ? 43.001 63.027  -20.804 1.00 9.09  ? 922  SER A O   1 
ATOM   7443 C  CB  . SER A 1 922  ? 40.660 60.706  -21.320 1.00 7.91  ? 922  SER A CB  1 
ATOM   7444 O  OG  . SER A 1 922  ? 40.821 60.859  -19.907 1.00 8.07  ? 922  SER A OG  1 
ATOM   7445 N  N   . GLN A 1 923  ? 43.624 61.347  -22.152 1.00 8.50  ? 923  GLN A N   1 
ATOM   7446 C  CA  . GLN A 1 923  ? 45.051 61.540  -21.811 1.00 8.55  ? 923  GLN A CA  1 
ATOM   7447 C  C   . GLN A 1 923  ? 45.542 62.916  -22.255 1.00 8.42  ? 923  GLN A C   1 
ATOM   7448 O  O   . GLN A 1 923  ? 46.423 63.496  -21.583 1.00 9.13  ? 923  GLN A O   1 
ATOM   7449 C  CB  . GLN A 1 923  ? 45.895 60.438  -22.457 1.00 8.21  ? 923  GLN A CB  1 
ATOM   7450 C  CG  . GLN A 1 923  ? 45.596 59.056  -21.918 1.00 8.18  ? 923  GLN A CG  1 
ATOM   7451 C  CD  . GLN A 1 923  ? 46.549 58.024  -22.513 1.00 9.92  ? 923  GLN A CD  1 
ATOM   7452 O  OE1 . GLN A 1 923  ? 46.706 57.942  -23.753 1.00 11.59 ? 923  GLN A OE1 1 
ATOM   7453 N  NE2 . GLN A 1 923  ? 47.164 57.200  -21.661 1.00 9.94  ? 923  GLN A NE2 1 
ATOM   7454 N  N   . SER A 1 924  ? 45.004 63.495  -23.335 1.00 8.48  ? 924  SER A N   1 
ATOM   7455 C  CA  . SER A 1 924  ? 45.450 64.815  -23.787 1.00 9.08  ? 924  SER A CA  1 
ATOM   7456 C  C   . SER A 1 924  ? 45.048 65.900  -22.782 1.00 9.22  ? 924  SER A C   1 
ATOM   7457 O  O   . SER A 1 924  ? 45.665 66.978  -22.763 1.00 11.31 ? 924  SER A O   1 
ATOM   7458 C  CB  . SER A 1 924  ? 44.833 65.167  -25.170 1.00 10.24 ? 924  SER A CB  1 
ATOM   7459 O  OG  . SER A 1 924  ? 43.451 65.583  -25.100 1.00 11.87 ? 924  SER A OG  1 
ATOM   7460 N  N   . LEU A 1 925  ? 43.978 65.665  -22.019 1.00 8.67  ? 925  LEU A N   1 
ATOM   7461 C  CA  . LEU A 1 925  ? 43.514 66.602  -21.001 1.00 8.10  ? 925  LEU A CA  1 
ATOM   7462 C  C   . LEU A 1 925  ? 44.256 66.415  -19.690 1.00 9.08  ? 925  LEU A C   1 
ATOM   7463 O  O   . LEU A 1 925  ? 44.635 67.384  -19.044 1.00 10.50 ? 925  LEU A O   1 
ATOM   7464 C  CB  . LEU A 1 925  ? 41.990 66.423  -20.719 1.00 7.87  ? 925  LEU A CB  1 
ATOM   7465 C  CG  . LEU A 1 925  ? 41.108 66.687  -21.966 1.00 7.96  ? 925  LEU A CG  1 
ATOM   7466 C  CD1 . LEU A 1 925  ? 39.665 66.302  -21.594 1.00 10.74 ? 925  LEU A CD1 1 
ATOM   7467 C  CD2 . LEU A 1 925  ? 41.223 68.189  -22.394 1.00 11.19 ? 925  LEU A CD2 1 
ATOM   7468 N  N   . LEU A 1 926  ? 44.424 65.171  -19.251 1.00 7.37  ? 926  LEU A N   1 
ATOM   7469 C  CA  . LEU A 1 926  ? 45.001 64.909  -17.930 1.00 7.66  ? 926  LEU A CA  1 
ATOM   7470 C  C   . LEU A 1 926  ? 46.504 64.885  -17.914 1.00 8.25  ? 926  LEU A C   1 
ATOM   7471 O  O   . LEU A 1 926  ? 47.095 65.277  -16.870 1.00 9.30  ? 926  LEU A O   1 
ATOM   7472 C  CB  . LEU A 1 926  ? 44.446 63.600  -17.365 1.00 10.24 ? 926  LEU A CB  1 
ATOM   7473 C  CG  . LEU A 1 926  ? 42.909 63.664  -17.141 1.00 10.78 ? 926  LEU A CG  1 
ATOM   7474 C  CD1 . LEU A 1 926  ? 42.423 62.271  -16.564 1.00 13.76 ? 926  LEU A CD1 1 
ATOM   7475 C  CD2 . LEU A 1 926  ? 42.594 64.828  -16.140 1.00 14.68 ? 926  LEU A CD2 1 
ATOM   7476 N  N   . ASP A 1 927  ? 47.124 64.385  -18.961 1.00 8.14  ? 927  ASP A N   1 
ATOM   7477 C  CA  . ASP A 1 927  ? 48.592 64.305  -18.996 1.00 8.53  ? 927  ASP A CA  1 
ATOM   7478 C  C   . ASP A 1 927  ? 49.153 64.835  -20.308 1.00 8.94  ? 927  ASP A C   1 
ATOM   7479 O  O   . ASP A 1 927  ? 49.711 64.119  -21.106 1.00 8.18  ? 927  ASP A O   1 
ATOM   7480 C  CB  . ASP A 1 927  ? 49.017 62.858  -18.754 1.00 9.15  ? 927  ASP A CB  1 
ATOM   7481 C  CG  . ASP A 1 927  ? 48.749 62.420  -17.305 1.00 9.11  ? 927  ASP A CG  1 
ATOM   7482 O  OD1 . ASP A 1 927  ? 49.456 62.823  -16.322 1.00 9.80  ? 927  ASP A OD1 1 
ATOM   7483 O  OD2 . ASP A 1 927  ? 47.740 61.729  -17.149 1.00 10.92 ? 927  ASP A OD2 1 
ATOM   7484 N  N   . PRO A 1 928  ? 48.974 66.149  -20.528 1.00 8.92  ? 928  PRO A N   1 
ATOM   7485 C  CA  . PRO A 1 928  ? 49.477 66.781  -21.766 1.00 8.40  ? 928  PRO A CA  1 
ATOM   7486 C  C   . PRO A 1 928  ? 51.020 66.795  -21.770 1.00 8.47  ? 928  PRO A C   1 
ATOM   7487 O  O   . PRO A 1 928  ? 51.678 66.496  -20.761 1.00 8.74  ? 928  PRO A O   1 
ATOM   7488 C  CB  . PRO A 1 928  ? 48.975 68.235  -21.657 1.00 10.54 ? 928  PRO A CB  1 
ATOM   7489 C  CG  . PRO A 1 928  ? 48.958 68.502  -20.191 1.00 12.36 ? 928  PRO A CG  1 
ATOM   7490 C  CD  . PRO A 1 928  ? 48.396 67.152  -19.592 1.00 10.03 ? 928  PRO A CD  1 
ATOM   7491 N  N   . LEU A 1 929  ? 51.623 67.161  -22.897 1.00 8.69  ? 929  LEU A N   1 
ATOM   7492 C  CA  . LEU A 1 929  ? 53.045 67.416  -22.884 1.00 7.80  ? 929  LEU A CA  1 
ATOM   7493 C  C   . LEU A 1 929  ? 53.368 68.572  -21.945 1.00 8.10  ? 929  LEU A C   1 
ATOM   7494 O  O   . LEU A 1 929  ? 52.598 69.528  -21.849 1.00 11.23 ? 929  LEU A O   1 
ATOM   7495 C  CB  . LEU A 1 929  ? 53.543 67.825  -24.300 1.00 9.55  ? 929  LEU A CB  1 
ATOM   7496 C  CG  . LEU A 1 929  ? 53.364 66.796  -25.418 1.00 9.21  ? 929  LEU A CG  1 
ATOM   7497 C  CD1 . LEU A 1 929  ? 53.969 67.388  -26.724 1.00 10.46 ? 929  LEU A CD1 1 
ATOM   7498 C  CD2 . LEU A 1 929  ? 54.069 65.449  -25.071 1.00 9.12  ? 929  LEU A CD2 1 
ATOM   7499 N  N   . ASP A 1 930  ? 54.484 68.512  -21.246 1.00 8.02  ? 930  ASP A N   1 
ATOM   7500 C  CA  . ASP A 1 930  ? 54.976 69.626  -20.435 1.00 7.90  ? 930  ASP A CA  1 
ATOM   7501 C  C   . ASP A 1 930  ? 55.884 70.478  -21.320 1.00 9.14  ? 930  ASP A C   1 
ATOM   7502 O  O   . ASP A 1 930  ? 56.672 69.906  -22.147 1.00 10.45 ? 930  ASP A O   1 
ATOM   7503 C  CB  . ASP A 1 930  ? 55.741 69.082  -19.217 1.00 8.48  ? 930  ASP A CB  1 
ATOM   7504 C  CG  . ASP A 1 930  ? 54.944 68.056  -18.506 1.00 11.18 ? 930  ASP A CG  1 
ATOM   7505 O  OD1 . ASP A 1 930  ? 53.877 68.495  -18.014 1.00 13.79 ? 930  ASP A OD1 1 
ATOM   7506 O  OD2 . ASP A 1 930  ? 55.307 66.849  -18.461 1.00 11.14 ? 930  ASP A OD2 1 
ATOM   7507 N  N   . LYS A 1 931  ? 55.889 71.790  -21.099 1.00 9.43  ? 931  LYS A N   1 
ATOM   7508 C  CA  . LYS A 1 931  ? 56.679 72.702  -21.935 1.00 8.93  ? 931  LYS A CA  1 
ATOM   7509 C  C   . LYS A 1 931  ? 57.621 73.505  -21.080 1.00 9.63  ? 931  LYS A C   1 
ATOM   7510 O  O   . LYS A 1 931  ? 57.210 74.111  -20.076 1.00 11.16 ? 931  LYS A O   1 
ATOM   7511 C  CB  . LYS A 1 931  ? 55.717 73.666  -22.662 1.00 10.19 ? 931  LYS A CB  1 
ATOM   7512 C  CG  . LYS A 1 931  ? 54.713 72.952  -23.617 1.00 12.71 ? 931  LYS A CG  1 
ATOM   7513 C  CD  . LYS A 1 931  ? 53.843 74.003  -24.305 1.00 16.85 ? 931  LYS A CD  1 
ATOM   7514 C  CE  . LYS A 1 931  ? 52.832 74.543  -23.323 1.00 22.09 ? 931  LYS A CE  1 
ATOM   7515 N  NZ  . LYS A 1 931  ? 52.349 75.805  -23.803 1.00 18.68 ? 931  LYS A NZ  1 
ATOM   7516 N  N   . PHE A 1 932  ? 58.898 73.566  -21.466 1.00 8.38  ? 932  PHE A N   1 
ATOM   7517 C  CA  . PHE A 1 932  ? 59.936 74.267  -20.727 1.00 7.88  ? 932  PHE A CA  1 
ATOM   7518 C  C   . PHE A 1 932  ? 60.609 75.285  -21.632 1.00 8.70  ? 932  PHE A C   1 
ATOM   7519 O  O   . PHE A 1 932  ? 60.937 74.964  -22.764 1.00 10.28 ? 932  PHE A O   1 
ATOM   7520 C  CB  . PHE A 1 932  ? 61.003 73.283  -20.256 1.00 9.30  ? 932  PHE A CB  1 
ATOM   7521 C  CG  . PHE A 1 932  ? 60.465 72.182  -19.368 1.00 9.53  ? 932  PHE A CG  1 
ATOM   7522 C  CD1 . PHE A 1 932  ? 59.862 71.026  -19.889 1.00 9.89  ? 932  PHE A CD1 1 
ATOM   7523 C  CD2 . PHE A 1 932  ? 60.590 72.309  -17.997 1.00 12.14 ? 932  PHE A CD2 1 
ATOM   7524 C  CE1 . PHE A 1 932  ? 59.387 69.971  -19.032 1.00 9.72  ? 932  PHE A CE1 1 
ATOM   7525 C  CE2 . PHE A 1 932  ? 60.138 71.290  -17.143 1.00 12.65 ? 932  PHE A CE2 1 
ATOM   7526 C  CZ  . PHE A 1 932  ? 59.543 70.138  -17.670 1.00 12.09 ? 932  PHE A CZ  1 
ATOM   7527 N  N   . ILE A 1 933  ? 60.824 76.485  -21.114 1.00 9.48  ? 933  ILE A N   1 
ATOM   7528 C  CA  . ILE A 1 933  ? 61.479 77.551  -21.883 1.00 9.54  ? 933  ILE A CA  1 
ATOM   7529 C  C   . ILE A 1 933  ? 62.843 77.803  -21.223 1.00 9.42  ? 933  ILE A C   1 
ATOM   7530 O  O   . ILE A 1 933  ? 62.903 78.076  -20.003 1.00 10.01 ? 933  ILE A O   1 
ATOM   7531 C  CB  . ILE A 1 933  ? 60.679 78.874  -21.817 1.00 9.27  ? 933  ILE A CB  1 
ATOM   7532 C  CG1 . ILE A 1 933  ? 59.270 78.686  -22.398 1.00 10.09 ? 933  ILE A CG1 1 
ATOM   7533 C  CG2 . ILE A 1 933  ? 61.464 79.981  -22.583 1.00 10.32 ? 933  ILE A CG2 1 
ATOM   7534 C  CD1 . ILE A 1 933  ? 58.387 79.874  -22.105 1.00 11.76 ? 933  ILE A CD1 1 
ATOM   7535 N  N   . PHE A 1 934  ? 63.960 77.667  -21.983 1.00 9.12  ? 934  PHE A N   1 
ATOM   7536 C  CA  . PHE A 1 934  ? 65.284 77.871  -21.370 1.00 10.00 ? 934  PHE A CA  1 
ATOM   7537 C  C   . PHE A 1 934  ? 65.406 79.341  -20.902 1.00 11.14 ? 934  PHE A C   1 
ATOM   7538 O  O   . PHE A 1 934  ? 65.103 80.257  -21.656 1.00 11.51 ? 934  PHE A O   1 
ATOM   7539 C  CB  . PHE A 1 934  ? 66.390 77.499  -22.375 1.00 11.78 ? 934  PHE A CB  1 
ATOM   7540 C  CG  . PHE A 1 934  ? 67.755 77.531  -21.762 1.00 11.20 ? 934  PHE A CG  1 
ATOM   7541 C  CD1 . PHE A 1 934  ? 68.155 76.535  -20.882 1.00 12.40 ? 934  PHE A CD1 1 
ATOM   7542 C  CD2 . PHE A 1 934  ? 68.619 78.599  -22.022 1.00 14.29 ? 934  PHE A CD2 1 
ATOM   7543 C  CE1 . PHE A 1 934  ? 69.403 76.581  -20.247 1.00 17.14 ? 934  PHE A CE1 1 
ATOM   7544 C  CE2 . PHE A 1 934  ? 69.842 78.679  -21.420 1.00 16.49 ? 934  PHE A CE2 1 
ATOM   7545 C  CZ  . PHE A 1 934  ? 70.262 77.682  -20.522 1.00 19.19 ? 934  PHE A CZ  1 
ATOM   7546 N  N   . ALA A 1 935  ? 65.839 79.553  -19.666 1.00 10.55 ? 935  ALA A N   1 
ATOM   7547 C  CA  . ALA A 1 935  ? 65.804 80.895  -19.111 1.00 11.70 ? 935  ALA A CA  1 
ATOM   7548 C  C   . ALA A 1 935  ? 66.938 81.834  -19.577 1.00 17.83 ? 935  ALA A C   1 
ATOM   7549 O  O   . ALA A 1 935  ? 66.680 83.040  -19.892 1.00 21.92 ? 935  ALA A O   1 
ATOM   7550 C  CB  . ALA A 1 935  ? 65.799 80.803  -17.610 1.00 15.70 ? 935  ALA A CB  1 
ATOM   7551 N  N   . GLU A 1 936  ? 68.141 81.307  -19.715 1.00 14.14 ? 936  GLU A N   1 
ATOM   7552 C  CA  . GLU A 1 936  ? 69.313 82.133  -20.053 1.00 16.14 ? 936  GLU A CA  1 
ATOM   7553 C  C   . GLU A 1 936  ? 69.420 82.323  -21.546 1.00 15.50 ? 936  GLU A C   1 
ATOM   7554 O  O   . GLU A 1 936  ? 68.669 81.752  -22.334 1.00 15.22 ? 936  GLU A O   1 
ATOM   7555 C  CB  . GLU A 1 936  ? 70.599 81.445  -19.528 1.00 20.97 ? 936  GLU A CB  1 
ATOM   7556 C  CG  . GLU A 1 936  ? 70.749 81.189  -17.986 1.00 25.85 ? 936  GLU A CG  1 
ATOM   7557 C  CD  . GLU A 1 936  ? 71.856 80.100  -17.677 1.00 31.21 ? 936  GLU A CD  1 
ATOM   7558 O  OE1 . GLU A 1 936  ? 71.634 78.870  -17.899 1.00 27.65 ? 936  GLU A OE1 1 
ATOM   7559 O  OE2 . GLU A 1 936  ? 72.980 80.458  -17.240 1.00 33.51 ? 936  GLU A OE2 1 
ATOM   7560 N  N   . ASN A 1 937  ? 70.399 83.119  -21.982 1.00 15.89 ? 937  ASN A N   1 
ATOM   7561 C  CA  . ASN A 1 937  ? 70.529 83.351  -23.408 1.00 15.57 ? 937  ASN A CA  1 
ATOM   7562 C  C   . ASN A 1 937  ? 71.075 82.186  -24.197 1.00 13.10 ? 937  ASN A C   1 
ATOM   7563 O  O   . ASN A 1 937  ? 70.661 81.977  -25.342 1.00 14.83 ? 937  ASN A O   1 
ATOM   7564 C  CB  . ASN A 1 937  ? 71.430 84.573  -23.667 1.00 17.22 ? 937  ASN A CB  1 
ATOM   7565 C  CG  . ASN A 1 937  ? 70.751 85.877  -23.250 1.00 20.46 ? 937  ASN A CG  1 
ATOM   7566 O  OD1 . ASN A 1 937  ? 69.505 85.945  -23.150 1.00 18.88 ? 937  ASN A OD1 1 
ATOM   7567 N  ND2 . ASN A 1 937  ? 71.556 86.908  -23.007 1.00 24.31 ? 937  ASN A ND2 1 
ATOM   7568 N  N   . GLU A 1 938  ? 72.009 81.438  -23.602 1.00 14.79 ? 938  GLU A N   1 
ATOM   7569 C  CA  . GLU A 1 938  ? 72.630 80.342  -24.321 1.00 17.17 ? 938  GLU A CA  1 
ATOM   7570 C  C   . GLU A 1 938  ? 72.725 79.088  -23.459 1.00 13.88 ? 938  GLU A C   1 
ATOM   7571 O  O   . GLU A 1 938  ? 73.124 79.166  -22.342 1.00 16.75 ? 938  GLU A O   1 
ATOM   7572 C  CB  . GLU A 1 938  ? 74.057 80.732  -24.786 1.00 20.14 ? 938  GLU A CB  1 
ATOM   7573 C  CG  . GLU A 1 938  ? 74.706 79.548  -25.515 1.00 26.47 ? 938  GLU A CG  1 
ATOM   7574 C  CD  . GLU A 1 938  ? 76.026 79.842  -26.207 1.00 34.34 ? 938  GLU A CD  1 
ATOM   7575 O  OE1 . GLU A 1 938  ? 76.808 80.679  -25.708 1.00 34.91 ? 938  GLU A OE1 1 
ATOM   7576 O  OE2 . GLU A 1 938  ? 76.277 79.188  -27.251 1.00 36.33 ? 938  GLU A OE2 1 
ATOM   7577 N  N   . TRP A 1 939  ? 72.340 77.953  -24.044 1.00 16.02 ? 939  TRP A N   1 
ATOM   7578 C  CA  . TRP A 1 939  ? 72.406 76.653  -23.324 1.00 13.83 ? 939  TRP A CA  1 
ATOM   7579 C  C   . TRP A 1 939  ? 73.603 75.855  -23.875 1.00 15.96 ? 939  TRP A C   1 
ATOM   7580 O  O   . TRP A 1 939  ? 73.518 75.227  -24.923 1.00 18.57 ? 939  TRP A O   1 
ATOM   7581 C  CB  . TRP A 1 939  ? 71.076 75.916  -23.572 1.00 14.02 ? 939  TRP A CB  1 
ATOM   7582 C  CG  . TRP A 1 939  ? 70.956 74.585  -22.905 1.00 12.23 ? 939  TRP A CG  1 
ATOM   7583 C  CD1 . TRP A 1 939  ? 71.841 73.963  -22.075 1.00 13.01 ? 939  TRP A CD1 1 
ATOM   7584 C  CD2 . TRP A 1 939  ? 69.866 73.702  -23.108 1.00 12.17 ? 939  TRP A CD2 1 
ATOM   7585 N  NE1 . TRP A 1 939  ? 71.354 72.693  -21.750 1.00 12.49 ? 939  TRP A NE1 1 
ATOM   7586 C  CE2 . TRP A 1 939  ? 70.138 72.518  -22.365 1.00 11.08 ? 939  TRP A CE2 1 
ATOM   7587 C  CE3 . TRP A 1 939  ? 68.687 73.789  -23.845 1.00 11.91 ? 939  TRP A CE3 1 
ATOM   7588 C  CZ2 . TRP A 1 939  ? 69.255 71.427  -22.351 1.00 11.19 ? 939  TRP A CZ2 1 
ATOM   7589 C  CZ3 . TRP A 1 939  ? 67.794 72.721  -23.843 1.00 10.88 ? 939  TRP A CZ3 1 
ATOM   7590 C  CH2 . TRP A 1 939  ? 68.090 71.545  -23.096 1.00 11.92 ? 939  TRP A CH2 1 
ATOM   7591 N  N   . ILE A 1 940  ? 74.717 75.917  -23.152 1.00 19.67 ? 940  ILE A N   1 
ATOM   7592 C  CA  . ILE A 1 940  ? 75.912 75.194  -23.609 1.00 21.65 ? 940  ILE A CA  1 
ATOM   7593 C  C   . ILE A 1 940  ? 75.767 73.669  -23.369 1.00 16.25 ? 940  ILE A C   1 
ATOM   7594 O  O   . ILE A 1 940  ? 75.354 73.250  -22.283 1.00 17.19 ? 940  ILE A O   1 
ATOM   7595 C  CB  . ILE A 1 940  ? 77.165 75.734  -22.867 1.00 24.15 ? 940  ILE A CB  1 
ATOM   7596 C  CG1 . ILE A 1 940  ? 77.291 77.243  -23.127 1.00 26.44 ? 940  ILE A CG1 1 
ATOM   7597 C  CG2 . ILE A 1 940  ? 78.446 74.996  -23.345 1.00 24.33 ? 940  ILE A CG2 1 
ATOM   7598 C  CD1 . ILE A 1 940  ? 78.608 77.819  -22.681 1.00 31.41 ? 940  ILE A CD1 1 
ATOM   7599 N  N   . GLY A 1 941  ? 76.050 72.874  -24.385 1.00 17.44 ? 941  GLY A N   1 
ATOM   7600 C  CA  . GLY A 1 941  ? 75.983 71.419  -24.189 1.00 16.18 ? 941  GLY A CA  1 
ATOM   7601 C  C   . GLY A 1 941  ? 74.586 70.857  -24.396 1.00 17.17 ? 941  GLY A C   1 
ATOM   7602 O  O   . GLY A 1 941  ? 74.364 69.694  -24.074 1.00 15.73 ? 941  GLY A O   1 
ATOM   7603 N  N   . ALA A 1 942  ? 73.663 71.648  -24.965 1.00 14.93 ? 942  ALA A N   1 
ATOM   7604 C  CA  . ALA A 1 942  ? 72.278 71.182  -25.163 1.00 13.71 ? 942  ALA A CA  1 
ATOM   7605 C  C   . ALA A 1 942  ? 72.206 69.984  -26.083 1.00 16.94 ? 942  ALA A C   1 
ATOM   7606 O  O   . ALA A 1 942  ? 72.916 69.922  -27.080 1.00 19.15 ? 942  ALA A O   1 
ATOM   7607 C  CB  . ALA A 1 942  ? 71.447 72.307  -25.718 1.00 16.65 ? 942  ALA A CB  1 
ATOM   7608 N  N   . GLN A 1 943  ? 71.322 69.036  -25.778 1.00 14.03 ? 943  GLN A N   1 
ATOM   7609 C  CA  . GLN A 1 943  ? 71.082 67.866  -26.564 1.00 15.65 ? 943  GLN A CA  1 
ATOM   7610 C  C   . GLN A 1 943  ? 69.649 67.881  -27.099 1.00 11.73 ? 943  GLN A C   1 
ATOM   7611 O  O   . GLN A 1 943  ? 68.734 68.516  -26.475 1.00 15.19 ? 943  GLN A O   1 
ATOM   7612 C  CB  . GLN A 1 943  ? 71.305 66.610  -25.716 1.00 15.95 ? 943  GLN A CB  1 
ATOM   7613 C  CG  . GLN A 1 943  ? 72.719 66.534  -25.196 1.00 21.54 ? 943  GLN A CG  1 
ATOM   7614 C  CD  . GLN A 1 943  ? 72.926 65.313  -24.309 1.00 24.10 ? 943  GLN A CD  1 
ATOM   7615 O  OE1 . GLN A 1 943  ? 71.986 64.871  -23.619 1.00 28.70 ? 943  GLN A OE1 1 
ATOM   7616 N  NE2 . GLN A 1 943  ? 74.152 64.776  -24.302 1.00 25.70 ? 943  GLN A NE2 1 
ATOM   7617 N  N   . GLY A 1 944  ? 69.400 67.188  -28.178 1.00 12.79 ? 944  GLY A N   1 
ATOM   7618 C  CA  . GLY A 1 944  ? 68.129 67.261  -28.822 1.00 14.09 ? 944  GLY A CA  1 
ATOM   7619 C  C   . GLY A 1 944  ? 67.020 66.366  -28.360 1.00 14.19 ? 944  GLY A C   1 
ATOM   7620 O  O   . GLY A 1 944  ? 65.871 66.646  -28.630 1.00 14.61 ? 944  GLY A O   1 
ATOM   7621 N  N   . GLN A 1 945  ? 67.351 65.295  -27.665 1.00 12.65 ? 945  GLN A N   1 
ATOM   7622 C  CA  . GLN A 1 945  ? 66.314 64.335  -27.301 1.00 13.36 ? 945  GLN A CA  1 
ATOM   7623 C  C   . GLN A 1 945  ? 66.780 63.470  -26.161 1.00 12.85 ? 945  GLN A C   1 
ATOM   7624 O  O   . GLN A 1 945  ? 67.985 63.259  -25.980 1.00 14.19 ? 945  GLN A O   1 
ATOM   7625 C  CB  . GLN A 1 945  ? 66.086 63.428  -28.489 1.00 14.37 ? 945  GLN A CB  1 
ATOM   7626 C  CG  . GLN A 1 945  ? 64.877 62.512  -28.463 1.00 18.33 ? 945  GLN A CG  1 
ATOM   7627 C  CD  . GLN A 1 945  ? 64.851 61.575  -29.686 1.00 19.99 ? 945  GLN A CD  1 
ATOM   7628 O  OE1 . GLN A 1 945  ? 64.013 61.720  -30.562 1.00 25.24 ? 945  GLN A OE1 1 
ATOM   7629 N  NE2 . GLN A 1 945  ? 65.763 60.633  -29.725 1.00 23.52 ? 945  GLN A NE2 1 
ATOM   7630 N  N   . PHE A 1 946  ? 65.804 62.987  -25.385 1.00 10.26 ? 946  PHE A N   1 
ATOM   7631 C  CA  . PHE A 1 946  ? 66.056 61.990  -24.322 1.00 9.82  ? 946  PHE A CA  1 
ATOM   7632 C  C   . PHE A 1 946  ? 64.963 60.961  -24.439 1.00 10.52 ? 946  PHE A C   1 
ATOM   7633 O  O   . PHE A 1 946  ? 63.789 61.280  -24.658 1.00 10.84 ? 946  PHE A O   1 
ATOM   7634 C  CB  . PHE A 1 946  ? 66.064 62.601  -22.914 1.00 10.78 ? 946  PHE A CB  1 
ATOM   7635 C  CG  . PHE A 1 946  ? 65.950 61.582  -21.814 1.00 11.24 ? 946  PHE A CG  1 
ATOM   7636 C  CD1 . PHE A 1 946  ? 66.974 60.739  -21.502 1.00 12.37 ? 946  PHE A CD1 1 
ATOM   7637 C  CD2 . PHE A 1 946  ? 64.736 61.460  -21.126 1.00 11.13 ? 946  PHE A CD2 1 
ATOM   7638 C  CE1 . PHE A 1 946  ? 66.818 59.723  -20.489 1.00 12.54 ? 946  PHE A CE1 1 
ATOM   7639 C  CE2 . PHE A 1 946  ? 64.561 60.448  -20.128 1.00 11.76 ? 946  PHE A CE2 1 
ATOM   7640 C  CZ  . PHE A 1 946  ? 65.591 59.593  -19.826 1.00 11.89 ? 946  PHE A CZ  1 
ATOM   7641 N  N   . GLY A 1 947  ? 65.310 59.666  -24.333 1.00 10.99 ? 947  GLY A N   1 
ATOM   7642 C  CA  . GLY A 1 947  ? 64.301 58.626  -24.371 1.00 12.24 ? 947  GLY A CA  1 
ATOM   7643 C  C   . GLY A 1 947  ? 63.982 58.020  -25.710 1.00 11.86 ? 947  GLY A C   1 
ATOM   7644 O  O   . GLY A 1 947  ? 63.067 57.248  -25.818 1.00 12.87 ? 947  GLY A O   1 
ATOM   7645 N  N   . GLY A 1 948  ? 64.772 58.351  -26.766 1.00 13.67 ? 948  GLY A N   1 
ATOM   7646 C  CA  . GLY A 1 948  ? 64.505 57.794  -28.080 1.00 13.74 ? 948  GLY A CA  1 
ATOM   7647 C  C   . GLY A 1 948  ? 64.544 56.273  -28.109 1.00 14.31 ? 948  GLY A C   1 
ATOM   7648 O  O   . GLY A 1 948  ? 63.911 55.686  -29.000 1.00 19.24 ? 948  GLY A O   1 
ATOM   7649 N  N   . ASP A 1 949  ? 65.257 55.651  -27.171 1.00 15.80 ? 949  ASP A N   1 
ATOM   7650 C  CA  . ASP A 1 949  ? 65.318 54.193  -27.094 1.00 18.47 ? 949  ASP A CA  1 
ATOM   7651 C  C   . ASP A 1 949  ? 64.346 53.577  -26.087 1.00 18.94 ? 949  ASP A C   1 
ATOM   7652 O  O   . ASP A 1 949  ? 64.392 52.346  -25.803 1.00 19.45 ? 949  ASP A O   1 
ATOM   7653 C  CB  . ASP A 1 949  ? 66.758 53.733  -26.736 1.00 20.04 ? 949  ASP A CB  1 
ATOM   7654 C  CG  . ASP A 1 949  ? 67.259 54.295  -25.419 1.00 27.95 ? 949  ASP A CG  1 
ATOM   7655 O  OD1 . ASP A 1 949  ? 66.637 55.208  -24.775 1.00 28.34 ? 949  ASP A OD1 1 
ATOM   7656 O  OD2 . ASP A 1 949  ? 68.339 53.816  -24.981 1.00 32.84 ? 949  ASP A OD2 1 
ATOM   7657 N  N   . HIS A 1 950  ? 63.465 54.406  -25.503 1.00 15.44 ? 950  HIS A N   1 
ATOM   7658 C  CA  . HIS A 1 950  ? 62.481 53.844  -24.561 1.00 12.69 ? 950  HIS A CA  1 
ATOM   7659 C  C   . HIS A 1 950  ? 61.388 53.090  -25.370 1.00 12.55 ? 950  HIS A C   1 
ATOM   7660 O  O   . HIS A 1 950  ? 60.966 53.518  -26.428 1.00 14.24 ? 950  HIS A O   1 
ATOM   7661 C  CB  . HIS A 1 950  ? 61.765 54.930  -23.800 1.00 11.82 ? 950  HIS A CB  1 
ATOM   7662 C  CG  . HIS A 1 950  ? 62.604 55.731  -22.857 1.00 11.98 ? 950  HIS A CG  1 
ATOM   7663 N  ND1 . HIS A 1 950  ? 63.875 55.432  -22.371 1.00 14.18 ? 950  HIS A ND1 1 
ATOM   7664 C  CD2 . HIS A 1 950  ? 62.231 56.862  -22.231 1.00 8.14  ? 950  HIS A CD2 1 
ATOM   7665 C  CE1 . HIS A 1 950  ? 64.229 56.366  -21.496 1.00 10.38 ? 950  HIS A CE1 1 
ATOM   7666 N  NE2 . HIS A 1 950  ? 63.233 57.244  -21.408 1.00 14.25 ? 950  HIS A NE2 1 
ATOM   7667 N  N   . PRO A 1 951  ? 60.933 51.939  -24.904 1.00 13.49 ? 951  PRO A N   1 
ATOM   7668 C  CA  . PRO A 1 951  ? 59.910 51.194  -25.623 1.00 13.37 ? 951  PRO A CA  1 
ATOM   7669 C  C   . PRO A 1 951  ? 58.619 51.990  -25.786 1.00 12.76 ? 951  PRO A C   1 
ATOM   7670 O  O   . PRO A 1 951  ? 58.178 52.684  -24.803 1.00 13.08 ? 951  PRO A O   1 
ATOM   7671 C  CB  . PRO A 1 951  ? 59.647 49.961  -24.736 1.00 16.51 ? 951  PRO A CB  1 
ATOM   7672 C  CG  . PRO A 1 951  ? 60.899 49.760  -24.048 1.00 19.65 ? 951  PRO A CG  1 
ATOM   7673 C  CD  . PRO A 1 951  ? 61.439 51.201  -23.738 1.00 16.57 ? 951  PRO A CD  1 
ATOM   7674 N  N   . SER A 1 952  ? 57.969 51.877  -26.921 1.00 12.38 ? 952  SER A N   1 
ATOM   7675 C  CA  . SER A 1 952  ? 56.705 52.586  -27.151 1.00 11.99 ? 952  SER A CA  1 
ATOM   7676 C  C   . SER A 1 952  ? 55.637 51.533  -26.948 1.00 12.71 ? 952  SER A C   1 
ATOM   7677 O  O   . SER A 1 952  ? 55.377 50.691  -27.838 1.00 13.79 ? 952  SER A O   1 
ATOM   7678 C  CB  . SER A 1 952  ? 56.675 53.172  -28.581 1.00 11.90 ? 952  SER A CB  1 
ATOM   7679 O  OG  . SER A 1 952  ? 55.635 54.124  -28.694 1.00 13.06 ? 952  SER A OG  1 
ATOM   7680 N  N   . ALA A 1 953  ? 54.994 51.560  -25.778 1.00 12.28 ? 953  ALA A N   1 
ATOM   7681 C  CA  . ALA A 1 953  ? 54.025 50.528  -25.363 1.00 11.06 ? 953  ALA A CA  1 
ATOM   7682 C  C   . ALA A 1 953  ? 52.665 50.614  -25.991 1.00 11.09 ? 953  ALA A C   1 
ATOM   7683 O  O   . ALA A 1 953  ? 52.253 51.687  -26.457 1.00 11.15 ? 953  ALA A O   1 
ATOM   7684 C  CB  . ALA A 1 953  ? 53.875 50.584  -23.813 1.00 13.56 ? 953  ALA A CB  1 
ATOM   7685 N  N   . ARG A 1 954  ? 51.951 49.502  -26.029 1.00 10.87 ? 954  ARG A N   1 
ATOM   7686 C  CA  . ARG A 1 954  ? 50.609 49.497  -26.559 1.00 11.80 ? 954  ARG A CA  1 
ATOM   7687 C  C   . ARG A 1 954  ? 49.789 50.656  -25.923 1.00 10.08 ? 954  ARG A C   1 
ATOM   7688 O  O   . ARG A 1 954  ? 49.884 50.953  -24.710 1.00 10.52 ? 954  ARG A O   1 
ATOM   7689 C  CB  . ARG A 1 954  ? 49.946 48.147  -26.320 1.00 13.56 ? 954  ARG A CB  1 
ATOM   7690 C  CG  . ARG A 1 954  ? 48.709 47.967  -27.258 1.00 20.35 ? 954  ARG A CG  1 
ATOM   7691 C  CD  . ARG A 1 954  ? 48.231 46.517  -27.443 1.00 21.87 ? 954  ARG A CD  1 
ATOM   7692 N  NE  . ARG A 1 954  ? 47.212 46.243  -26.447 1.00 23.70 ? 954  ARG A NE  1 
ATOM   7693 C  CZ  . ARG A 1 954  ? 46.567 45.097  -26.315 1.00 30.45 ? 954  ARG A CZ  1 
ATOM   7694 N  NH1 . ARG A 1 954  ? 46.833 44.074  -27.142 1.00 32.77 ? 954  ARG A NH1 1 
ATOM   7695 N  NH2 . ARG A 1 954  ? 45.659 44.972  -25.363 1.00 26.98 ? 954  ARG A NH2 1 
ATOM   7696 N  N   . GLU A 1 955  ? 48.867 51.206  -26.699 1.00 10.63 ? 955  GLU A N   1 
ATOM   7697 C  CA  . GLU A 1 955  ? 48.140 52.427  -26.304 1.00 11.64 ? 955  GLU A CA  1 
ATOM   7698 C  C   . GLU A 1 955  ? 47.308 52.302  -25.033 1.00 10.38 ? 955  GLU A C   1 
ATOM   7699 O  O   . GLU A 1 955  ? 46.995 53.311  -24.406 1.00 11.50 ? 955  GLU A O   1 
ATOM   7700 C  CB  . GLU A 1 955  ? 47.237 52.881  -27.472 1.00 13.60 ? 955  GLU A CB  1 
ATOM   7701 C  CG  . GLU A 1 955  ? 46.163 51.883  -27.827 1.00 14.19 ? 955  GLU A CG  1 
ATOM   7702 C  CD  . GLU A 1 955  ? 45.230 52.381  -28.869 1.00 20.05 ? 955  GLU A CD  1 
ATOM   7703 O  OE1 . GLU A 1 955  ? 45.075 53.606  -29.029 1.00 24.99 ? 955  GLU A OE1 1 
ATOM   7704 O  OE2 . GLU A 1 955  ? 44.594 51.543  -29.555 1.00 20.88 ? 955  GLU A OE2 1 
ATOM   7705 N  N   . ASP A 1 956  ? 46.878 51.071  -24.693 1.00 9.25  ? 956  ASP A N   1 
ATOM   7706 C  CA  . ASP A 1 956  ? 46.088 50.908  -23.477 1.00 9.98  ? 956  ASP A CA  1 
ATOM   7707 C  C   . ASP A 1 956  ? 46.898 50.803  -22.216 1.00 8.44  ? 956  ASP A C   1 
ATOM   7708 O  O   . ASP A 1 956  ? 46.307 50.738  -21.127 1.00 11.56 ? 956  ASP A O   1 
ATOM   7709 C  CB  . ASP A 1 956  ? 45.086 49.714  -23.630 1.00 11.56 ? 956  ASP A CB  1 
ATOM   7710 C  CG  . ASP A 1 956  ? 45.737 48.409  -23.989 1.00 12.91 ? 956  ASP A CG  1 
ATOM   7711 O  OD1 . ASP A 1 956  ? 46.936 48.362  -24.190 1.00 15.49 ? 956  ASP A OD1 1 
ATOM   7712 O  OD2 . ASP A 1 956  ? 44.967 47.400  -24.038 1.00 14.86 ? 956  ASP A OD2 1 
ATOM   7713 N  N   . LEU A 1 957  ? 48.208 50.796  -22.333 1.00 8.96  ? 957  LEU A N   1 
ATOM   7714 C  CA  . LEU A 1 957  ? 49.077 50.661  -21.144 1.00 9.10  ? 957  LEU A CA  1 
ATOM   7715 C  C   . LEU A 1 957  ? 49.640 52.014  -20.708 1.00 9.81  ? 957  LEU A C   1 
ATOM   7716 O  O   . LEU A 1 957  ? 50.066 52.827  -21.564 1.00 11.65 ? 957  LEU A O   1 
ATOM   7717 C  CB  . LEU A 1 957  ? 50.267 49.728  -21.499 1.00 11.38 ? 957  LEU A CB  1 
ATOM   7718 C  CG  . LEU A 1 957  ? 51.132 49.198  -20.340 1.00 14.52 ? 957  LEU A CG  1 
ATOM   7719 C  CD1 . LEU A 1 957  ? 50.250 48.319  -19.421 1.00 18.09 ? 957  LEU A CD1 1 
ATOM   7720 C  CD2 . LEU A 1 957  ? 52.255 48.307  -20.883 1.00 16.79 ? 957  LEU A CD2 1 
ATOM   7721 N  N   . ASP A 1 958  ? 49.682 52.243  -19.407 1.00 8.49  ? 958  ASP A N   1 
ATOM   7722 C  CA  . ASP A 1 958  ? 50.301 53.457  -18.891 1.00 7.94  ? 958  ASP A CA  1 
ATOM   7723 C  C   . ASP A 1 958  ? 51.213 53.150  -17.733 1.00 8.02  ? 958  ASP A C   1 
ATOM   7724 O  O   . ASP A 1 958  ? 50.980 52.184  -16.962 1.00 9.58  ? 958  ASP A O   1 
ATOM   7725 C  CB  . ASP A 1 958  ? 49.210 54.453  -18.441 1.00 9.88  ? 958  ASP A CB  1 
ATOM   7726 C  CG  . ASP A 1 958  ? 49.749 55.870  -18.226 1.00 8.55  ? 958  ASP A CG  1 
ATOM   7727 O  OD1 . ASP A 1 958  ? 50.866 56.195  -18.689 1.00 9.86  ? 958  ASP A OD1 1 
ATOM   7728 O  OD2 . ASP A 1 958  ? 49.043 56.667  -17.547 1.00 10.33 ? 958  ASP A OD2 1 
ATOM   7729 N  N   . VAL A 1 959  ? 52.284 53.933  -17.620 1.00 7.91  ? 959  VAL A N   1 
ATOM   7730 C  CA  . VAL A 1 959  ? 53.149 53.910  -16.433 1.00 7.85  ? 959  VAL A CA  1 
ATOM   7731 C  C   . VAL A 1 959  ? 52.592 55.042  -15.585 1.00 8.09  ? 959  VAL A C   1 
ATOM   7732 O  O   . VAL A 1 959  ? 53.008 56.205  -15.707 1.00 8.80  ? 959  VAL A O   1 
ATOM   7733 C  CB  . VAL A 1 959  ? 54.605 54.166  -16.804 1.00 8.85  ? 959  VAL A CB  1 
ATOM   7734 C  CG1 . VAL A 1 959  ? 55.480 54.310  -15.503 1.00 9.42  ? 959  VAL A CG1 1 
ATOM   7735 C  CG2 . VAL A 1 959  ? 55.139 52.984  -17.650 1.00 9.94  ? 959  VAL A CG2 1 
ATOM   7736 N  N   . SER A 1 960  ? 51.630 54.703  -14.738 1.00 8.16  ? 960  SER A N   1 
ATOM   7737 C  CA  . SER A 1 960  ? 50.928 55.682  -13.907 1.00 8.40  ? 960  SER A CA  1 
ATOM   7738 C  C   . SER A 1 960  ? 51.850 56.393  -12.948 1.00 8.97  ? 960  SER A C   1 
ATOM   7739 O  O   . SER A 1 960  ? 51.677 57.599  -12.664 1.00 10.02 ? 960  SER A O   1 
ATOM   7740 C  CB  . SER A 1 960  ? 49.806 54.988  -13.110 1.00 9.41  ? 960  SER A CB  1 
ATOM   7741 O  OG  . SER A 1 960  ? 48.999 54.184  -13.983 1.00 11.76 ? 960  SER A OG  1 
ATOM   7742 N  N   . VAL A 1 961  ? 52.818 55.646  -12.405 1.00 8.33  ? 961  VAL A N   1 
ATOM   7743 C  CA  . VAL A 1 961  ? 53.815 56.150  -11.465 1.00 9.07  ? 961  VAL A CA  1 
ATOM   7744 C  C   . VAL A 1 961  ? 55.174 55.590  -11.783 1.00 8.44  ? 961  VAL A C   1 
ATOM   7745 O  O   . VAL A 1 961  ? 55.333 54.383  -12.030 1.00 8.01  ? 961  VAL A O   1 
ATOM   7746 C  CB  . VAL A 1 961  ? 53.505 55.685  -10.010 1.00 9.00  ? 961  VAL A CB  1 
ATOM   7747 C  CG1 . VAL A 1 961  ? 54.619 56.163  -9.025  1.00 10.66 ? 961  VAL A CG1 1 
ATOM   7748 C  CG2 . VAL A 1 961  ? 52.143 56.250  -9.534  1.00 10.46 ? 961  VAL A CG2 1 
ATOM   7749 N  N   . MET A 1 962  ? 56.172 56.485  -11.770 1.00 8.09  ? 962  MET A N   1 
ATOM   7750 C  CA  . MET A 1 962  ? 57.579 56.053  -11.778 1.00 7.77  ? 962  MET A CA  1 
ATOM   7751 C  C   . MET A 1 962  ? 58.178 56.882  -10.638 1.00 7.89  ? 962  MET A C   1 
ATOM   7752 O  O   . MET A 1 962  ? 58.127 58.130  -10.618 1.00 9.33  ? 962  MET A O   1 
ATOM   7753 C  CB  . MET A 1 962  ? 58.267 56.376  -13.093 1.00 8.86  ? 962  MET A CB  1 
ATOM   7754 C  CG  . MET A 1 962  ? 59.795 56.080  -13.015 1.00 8.90  ? 962  MET A CG  1 
ATOM   7755 S  SD  . MET A 1 962  ? 60.513 56.352  -14.642 1.00 10.64 ? 962  MET A SD  1 
ATOM   7756 C  CE  . MET A 1 962  ? 62.272 55.896  -14.366 1.00 11.10 ? 962  MET A CE  1 
ATOM   7757 N  N   . ARG A 1 963  ? 58.733 56.197  -9.621  1.00 8.02  ? 963  ARG A N   1 
ATOM   7758 C  CA  . ARG A 1 963  ? 59.272 56.868  -8.453  1.00 7.71  ? 963  ARG A CA  1 
ATOM   7759 C  C   . ARG A 1 963  ? 60.533 56.186  -7.945  1.00 8.30  ? 963  ARG A C   1 
ATOM   7760 O  O   . ARG A 1 963  ? 60.472 54.996  -7.557  1.00 8.54  ? 963  ARG A O   1 
ATOM   7761 C  CB  . ARG A 1 963  ? 58.201 56.825  -7.318  1.00 8.58  ? 963  ARG A CB  1 
ATOM   7762 C  CG  . ARG A 1 963  ? 58.636 57.479  -5.985  1.00 8.94  ? 963  ARG A CG  1 
ATOM   7763 C  CD  . ARG A 1 963  ? 57.581 57.284  -4.851  1.00 11.19 ? 963  ARG A CD  1 
ATOM   7764 N  NE  . ARG A 1 963  ? 56.348 57.998  -5.227  1.00 10.36 ? 963  ARG A NE  1 
ATOM   7765 C  CZ  . ARG A 1 963  ? 55.120 57.475  -5.171  1.00 9.34  ? 963  ARG A CZ  1 
ATOM   7766 N  NH1 . ARG A 1 963  ? 54.884 56.262  -4.655  1.00 9.40  ? 963  ARG A NH1 1 
ATOM   7767 N  NH2 . ARG A 1 963  ? 54.136 58.144  -5.818  1.00 9.86  ? 963  ARG A NH2 1 
ATOM   7768 N  N   . ARG A 1 964  ? 61.635 56.937  -7.820  1.00 8.97  ? 964  ARG A N   1 
ATOM   7769 C  CA  . ARG A 1 964  ? 62.833 56.314  -7.184  1.00 9.24  ? 964  ARG A CA  1 
ATOM   7770 C  C   . ARG A 1 964  ? 62.523 56.265  -5.678  1.00 8.54  ? 964  ARG A C   1 
ATOM   7771 O  O   . ARG A 1 964  ? 62.090 57.245  -5.087  1.00 9.56  ? 964  ARG A O   1 
ATOM   7772 C  CB  . ARG A 1 964  ? 64.037 57.178  -7.502  1.00 8.63  ? 964  ARG A CB  1 
ATOM   7773 C  CG  . ARG A 1 964  ? 65.312 56.511  -6.875  1.00 10.25 ? 964  ARG A CG  1 
ATOM   7774 C  CD  . ARG A 1 964  ? 66.584 57.181  -7.383  1.00 10.92 ? 964  ARG A CD  1 
ATOM   7775 N  NE  . ARG A 1 964  ? 66.801 57.020  -8.821  1.00 11.30 ? 964  ARG A NE  1 
ATOM   7776 C  CZ  . ARG A 1 964  ? 67.666 56.222  -9.393  1.00 10.90 ? 964  ARG A CZ  1 
ATOM   7777 N  NH1 . ARG A 1 964  ? 68.440 55.436  -8.643  1.00 15.18 ? 964  ARG A NH1 1 
ATOM   7778 N  NH2 . ARG A 1 964  ? 67.808 56.212  -10.703 1.00 14.00 ? 964  ARG A NH2 1 
ATOM   7779 N  N   . LEU A 1 965  ? 62.769 55.091  -5.098  1.00 9.38  ? 965  LEU A N   1 
ATOM   7780 C  CA  . LEU A 1 965  ? 62.404 54.842  -3.701  1.00 8.85  ? 965  LEU A CA  1 
ATOM   7781 C  C   . LEU A 1 965  ? 63.564 54.985  -2.722  1.00 10.24 ? 965  LEU A C   1 
ATOM   7782 O  O   . LEU A 1 965  ? 63.321 54.906  -1.506  1.00 11.54 ? 965  LEU A O   1 
ATOM   7783 C  CB  . LEU A 1 965  ? 61.866 53.440  -3.587  1.00 9.93  ? 965  LEU A CB  1 
ATOM   7784 C  CG  . LEU A 1 965  ? 60.641 53.175  -4.484  1.00 9.56  ? 965  LEU A CG  1 
ATOM   7785 C  CD1 . LEU A 1 965  ? 60.203 51.700  -4.379  1.00 11.12 ? 965  LEU A CD1 1 
ATOM   7786 C  CD2 . LEU A 1 965  ? 59.457 54.071  -4.061  1.00 13.79 ? 965  LEU A CD2 1 
ATOM   7787 N  N   . THR A 1 966  ? 64.792 55.141  -3.249  1.00 10.50 ? 966  THR A N   1 
ATOM   7788 C  CA  . THR A 1 966  ? 65.998 55.241  -2.401  1.00 10.66 ? 966  THR A CA  1 
ATOM   7789 C  C   . THR A 1 966  ? 66.676 56.555  -2.585  1.00 10.15 ? 966  THR A C   1 
ATOM   7790 O  O   . THR A 1 966  ? 66.662 57.092  -3.708  1.00 11.08 ? 966  THR A O   1 
ATOM   7791 C  CB  . THR A 1 966  ? 66.993 54.144  -2.806  1.00 12.39 ? 966  THR A CB  1 
ATOM   7792 O  OG1 . THR A 1 966  ? 67.048 54.021  -4.229  1.00 11.71 ? 966  THR A OG1 1 
ATOM   7793 C  CG2 . THR A 1 966  ? 66.551 52.766  -2.260  1.00 11.99 ? 966  THR A CG2 1 
ATOM   7794 N  N   . LYS A 1 967  ? 67.358 57.010  -1.540  1.00 11.41 ? 967  LYS A N   1 
ATOM   7795 C  CA  . LYS A 1 967  ? 68.170 58.233  -1.590  1.00 11.54 ? 967  LYS A CA  1 
ATOM   7796 C  C   . LYS A 1 967  ? 69.590 57.795  -2.118  1.00 12.17 ? 967  LYS A C   1 
ATOM   7797 O  O   . LYS A 1 967  ? 69.891 56.602  -2.265  1.00 12.42 ? 967  LYS A O   1 
ATOM   7798 C  CB  . LYS A 1 967  ? 68.280 58.871  -0.200  1.00 14.57 ? 967  LYS A CB  1 
ATOM   7799 C  CG  . LYS A 1 967  ? 66.918 59.499  0.243   1.00 19.27 ? 967  LYS A CG  1 
ATOM   7800 C  CD  . LYS A 1 967  ? 67.037 60.420  1.492   1.00 22.04 ? 967  LYS A CD  1 
ATOM   7801 C  CE  . LYS A 1 967  ? 65.681 61.048  1.807   1.00 29.80 ? 967  LYS A CE  1 
ATOM   7802 N  NZ  . LYS A 1 967  ? 65.408 60.961  3.262   1.00 39.61 ? 967  LYS A NZ  1 
ATOM   7803 N  N   . SER A 1 968  ? 70.423 58.798  -2.416  1.00 13.00 ? 968  SER A N   1 
ATOM   7804 C  CA  . SER A 1 968  ? 71.699 58.498  -3.084  1.00 13.72 ? 968  SER A CA  1 
ATOM   7805 C  C   . SER A 1 968  ? 72.688 57.677  -2.271  1.00 14.73 ? 968  SER A C   1 
ATOM   7806 O  O   . SER A 1 968  ? 73.512 56.984  -2.908  1.00 17.91 ? 968  SER A O   1 
ATOM   7807 C  CB  . SER A 1 968  ? 72.362 59.792  -3.572  1.00 16.79 ? 968  SER A CB  1 
ATOM   7808 O  OG  . SER A 1 968  ? 72.587 60.649  -2.516  1.00 22.58 ? 968  SER A OG  1 
ATOM   7809 N  N   . SER A 1 969  ? 72.545 57.684  -0.952  1.00 16.08 ? 969  SER A N   1 
ATOM   7810 C  CA  . SER A 1 969  ? 73.473 56.894  -0.100  1.00 17.38 ? 969  SER A CA  1 
ATOM   7811 C  C   . SER A 1 969  ? 73.224 55.377  -0.129  1.00 18.29 ? 969  SER A C   1 
ATOM   7812 O  O   . SER A 1 969  ? 74.062 54.620  0.362   1.00 18.54 ? 969  SER A O   1 
ATOM   7813 C  CB  . SER A 1 969  ? 73.427 57.436  1.322   1.00 21.97 ? 969  SER A CB  1 
ATOM   7814 O  OG  . SER A 1 969  ? 72.113 57.302  1.802   1.00 32.56 ? 969  SER A OG  1 
ATOM   7815 N  N   . ALA A 1 970  ? 72.102 54.887  -0.674  1.00 13.93 ? 970  ALA A N   1 
ATOM   7816 C  CA  . ALA A 1 970  ? 71.837 53.463  -0.753  1.00 13.33 ? 970  ALA A CA  1 
ATOM   7817 C  C   . ALA A 1 970  ? 72.655 52.753  -1.807  1.00 16.39 ? 970  ALA A C   1 
ATOM   7818 O  O   . ALA A 1 970  ? 72.641 53.105  -3.010  1.00 15.49 ? 970  ALA A O   1 
ATOM   7819 C  CB  . ALA A 1 970  ? 70.328 53.187  -1.004  1.00 16.11 ? 970  ALA A CB  1 
ATOM   7820 N  N   A LYS A 1 971  ? 73.431 51.744  -1.356  0.50 16.75 ? 971  LYS A N   1 
ATOM   7821 N  N   B LYS A 1 971  ? 73.431 51.744  -1.356  0.50 17.09 ? 971  LYS A N   1 
ATOM   7822 C  CA  A LYS A 1 971  ? 74.225 50.962  -2.304  0.50 18.03 ? 971  LYS A CA  1 
ATOM   7823 C  CA  B LYS A 1 971  ? 74.225 50.962  -2.304  0.50 18.49 ? 971  LYS A CA  1 
ATOM   7824 C  C   A LYS A 1 971  ? 73.336 50.342  -3.388  0.50 17.30 ? 971  LYS A C   1 
ATOM   7825 C  C   B LYS A 1 971  ? 73.336 50.342  -3.388  0.50 17.65 ? 971  LYS A C   1 
ATOM   7826 O  O   A LYS A 1 971  ? 73.719 50.306  -4.553  0.50 20.02 ? 971  LYS A O   1 
ATOM   7827 O  O   B LYS A 1 971  ? 73.719 50.306  -4.553  0.50 20.34 ? 971  LYS A O   1 
ATOM   7828 C  CB  A LYS A 1 971  ? 74.975 49.846  -1.539  0.50 20.83 ? 971  LYS A CB  1 
ATOM   7829 C  CB  B LYS A 1 971  ? 74.975 49.846  -1.539  0.50 21.73 ? 971  LYS A CB  1 
ATOM   7830 C  CG  A LYS A 1 971  ? 75.836 48.943  -2.409  0.50 26.53 ? 971  LYS A CG  1 
ATOM   7831 C  CG  B LYS A 1 971  ? 75.766 48.890  -2.418  0.50 27.63 ? 971  LYS A CG  1 
ATOM   7832 C  CD  A LYS A 1 971  ? 76.891 48.218  -1.517  0.50 29.92 ? 971  LYS A CD  1 
ATOM   7833 C  CD  B LYS A 1 971  ? 76.899 48.228  -1.574  0.50 31.49 ? 971  LYS A CD  1 
ATOM   7834 C  CE  A LYS A 1 971  ? 77.599 47.096  -2.297  0.50 32.33 ? 971  LYS A CE  1 
ATOM   7835 C  CE  B LYS A 1 971  ? 76.911 48.776  -0.136  0.50 34.08 ? 971  LYS A CE  1 
ATOM   7836 N  NZ  A LYS A 1 971  ? 78.139 47.507  -3.637  0.50 33.43 ? 971  LYS A NZ  1 
ATOM   7837 N  NZ  B LYS A 1 971  ? 77.358 50.205  -0.013  0.50 37.35 ? 971  LYS A NZ  1 
ATOM   7838 N  N   . THR A 1 972  ? 72.175 49.806  -2.984  1.00 17.75 ? 972  THR A N   1 
ATOM   7839 C  CA  . THR A 1 972  ? 71.251 49.224  -3.940  1.00 16.61 ? 972  THR A CA  1 
ATOM   7840 C  C   . THR A 1 972  ? 70.100 50.229  -4.203  1.00 13.70 ? 972  THR A C   1 
ATOM   7841 O  O   . THR A 1 972  ? 69.309 50.501  -3.311  1.00 15.54 ? 972  THR A O   1 
ATOM   7842 C  CB  . THR A 1 972  ? 70.667 47.882  -3.468  1.00 18.96 ? 972  THR A CB  1 
ATOM   7843 O  OG1 . THR A 1 972  ? 71.753 46.959  -3.231  1.00 22.02 ? 972  THR A OG1 1 
ATOM   7844 C  CG2 . THR A 1 972  ? 69.823 47.237  -4.575  1.00 17.92 ? 972  THR A CG2 1 
ATOM   7845 N  N   . GLN A 1 973  ? 70.085 50.829  -5.396  1.00 12.04 ? 973  GLN A N   1 
ATOM   7846 C  CA  . GLN A 1 973  ? 68.998 51.771  -5.748  1.00 12.63 ? 973  GLN A CA  1 
ATOM   7847 C  C   . GLN A 1 973  ? 67.754 50.963  -6.091  1.00 12.76 ? 973  GLN A C   1 
ATOM   7848 O  O   . GLN A 1 973  ? 67.815 49.903  -6.674  1.00 13.21 ? 973  GLN A O   1 
ATOM   7849 C  CB  . GLN A 1 973  ? 69.450 52.638  -6.917  1.00 12.20 ? 973  GLN A CB  1 
ATOM   7850 C  CG  . GLN A 1 973  ? 70.562 53.619  -6.465  1.00 11.37 ? 973  GLN A CG  1 
ATOM   7851 C  CD  . GLN A 1 973  ? 70.124 54.643  -5.453  1.00 12.43 ? 973  GLN A CD  1 
ATOM   7852 O  OE1 . GLN A 1 973  ? 70.752 54.853  -4.360  1.00 14.00 ? 973  GLN A OE1 1 
ATOM   7853 N  NE2 . GLN A 1 973  ? 69.044 55.344  -5.786  1.00 10.41 ? 973  GLN A NE2 1 
ATOM   7854 N  N   . ARG A 1 974  ? 66.598 51.558  -5.784  1.00 12.78 ? 974  ARG A N   1 
ATOM   7855 C  CA  . ARG A 1 974  ? 65.309 50.935  -6.086  1.00 12.20 ? 974  ARG A CA  1 
ATOM   7856 C  C   . ARG A 1 974  ? 64.380 51.934  -6.751  1.00 9.80  ? 974  ARG A C   1 
ATOM   7857 O  O   . ARG A 1 974  ? 64.297 53.083  -6.280  1.00 10.50 ? 974  ARG A O   1 
ATOM   7858 C  CB  . ARG A 1 974  ? 64.625 50.436  -4.819  1.00 11.79 ? 974  ARG A CB  1 
ATOM   7859 C  CG  . ARG A 1 974  ? 65.462 49.316  -4.092  1.00 13.77 ? 974  ARG A CG  1 
ATOM   7860 C  CD  . ARG A 1 974  ? 64.955 49.034  -2.657  1.00 16.39 ? 974  ARG A CD  1 
ATOM   7861 N  NE  . ARG A 1 974  ? 63.700 48.310  -2.706  1.00 23.10 ? 974  ARG A NE  1 
ATOM   7862 C  CZ  . ARG A 1 974  ? 62.548 48.727  -2.198  1.00 20.03 ? 974  ARG A CZ  1 
ATOM   7863 N  NH1 . ARG A 1 974  ? 62.423 49.878  -1.567  1.00 21.59 ? 974  ARG A NH1 1 
ATOM   7864 N  NH2 . ARG A 1 974  ? 61.500 47.944  -2.354  1.00 19.04 ? 974  ARG A NH2 1 
ATOM   7865 N  N   . VAL A 1 975  ? 63.723 51.491  -7.809  1.00 9.86  ? 975  VAL A N   1 
ATOM   7866 C  CA  . VAL A 1 975  ? 62.759 52.352  -8.528  1.00 11.29 ? 975  VAL A CA  1 
ATOM   7867 C  C   . VAL A 1 975  ? 61.461 51.595  -8.629  1.00 10.72 ? 975  VAL A C   1 
ATOM   7868 O  O   . VAL A 1 975  ? 61.415 50.421  -9.081  1.00 10.74 ? 975  VAL A O   1 
ATOM   7869 C  CB  . VAL A 1 975  ? 63.279 52.711  -9.964  1.00 11.41 ? 975  VAL A CB  1 
ATOM   7870 C  CG1 . VAL A 1 975  ? 62.323 53.730  -10.636 1.00 11.09 ? 975  VAL A CG1 1 
ATOM   7871 C  CG2 . VAL A 1 975  ? 64.620 53.469  -9.836  1.00 13.46 ? 975  VAL A CG2 1 
ATOM   7872 N  N   . GLY A 1 976  ? 60.392 52.299  -8.235  1.00 9.91  ? 976  GLY A N   1 
ATOM   7873 C  CA  . GLY A 1 976  ? 59.051 51.717  -8.257  1.00 9.67  ? 976  GLY A CA  1 
ATOM   7874 C  C   . GLY A 1 976  ? 58.229 52.216  -9.436  1.00 7.44  ? 976  GLY A C   1 
ATOM   7875 O  O   . GLY A 1 976  ? 58.284 53.409  -9.846  1.00 9.09  ? 976  GLY A O   1 
ATOM   7876 N  N   . TYR A 1 977  ? 57.471 51.306  -9.990  1.00 8.55  ? 977  TYR A N   1 
ATOM   7877 C  CA  . TYR A 1 977  ? 56.570 51.618  -11.109 1.00 8.26  ? 977  TYR A CA  1 
ATOM   7878 C  C   . TYR A 1 977  ? 55.155 51.084  -10.844 1.00 8.28  ? 977  TYR A C   1 
ATOM   7879 O  O   . TYR A 1 977  ? 54.994 49.952  -10.342 1.00 9.21  ? 977  TYR A O   1 
ATOM   7880 C  CB  . TYR A 1 977  ? 57.012 50.886  -12.393 1.00 9.03  ? 977  TYR A CB  1 
ATOM   7881 C  CG  . TYR A 1 977  ? 58.415 51.245  -12.805 1.00 8.54  ? 977  TYR A CG  1 
ATOM   7882 C  CD1 . TYR A 1 977  ? 59.519 50.522  -12.333 1.00 10.11 ? 977  TYR A CD1 1 
ATOM   7883 C  CD2 . TYR A 1 977  ? 58.632 52.318  -13.672 1.00 10.07 ? 977  TYR A CD2 1 
ATOM   7884 C  CE1 . TYR A 1 977  ? 60.816 50.886  -12.746 1.00 11.24 ? 977  TYR A CE1 1 
ATOM   7885 C  CE2 . TYR A 1 977  ? 59.892 52.683  -14.086 1.00 11.31 ? 977  TYR A CE2 1 
ATOM   7886 C  CZ  . TYR A 1 977  ? 60.966 51.969  -13.615 1.00 10.38 ? 977  TYR A CZ  1 
ATOM   7887 O  OH  . TYR A 1 977  ? 62.237 52.383  -14.040 1.00 11.73 ? 977  TYR A OH  1 
ATOM   7888 N  N   . VAL A 1 978  ? 54.132 51.901  -11.154 1.00 7.39  ? 978  VAL A N   1 
ATOM   7889 C  CA  . VAL A 1 978  ? 52.753 51.390  -11.137 1.00 7.48  ? 978  VAL A CA  1 
ATOM   7890 C  C   . VAL A 1 978  ? 52.327 51.363  -12.613 1.00 8.13  ? 978  VAL A C   1 
ATOM   7891 O  O   . VAL A 1 978  ? 52.394 52.398  -13.293 1.00 9.34  ? 978  VAL A O   1 
ATOM   7892 C  CB  . VAL A 1 978  ? 51.779 52.274  -10.333 1.00 8.12  ? 978  VAL A CB  1 
ATOM   7893 C  CG1 . VAL A 1 978  ? 50.324 51.741  -10.508 1.00 9.58  ? 978  VAL A CG1 1 
ATOM   7894 C  CG2 . VAL A 1 978  ? 52.174 52.246  -8.826  1.00 9.38  ? 978  VAL A CG2 1 
ATOM   7895 N  N   A LEU A 1 979  ? 51.912 50.189  -13.085 0.50 7.42  ? 979  LEU A N   1 
ATOM   7896 N  N   B LEU A 1 979  ? 51.912 50.189  -13.085 0.50 8.89  ? 979  LEU A N   1 
ATOM   7897 C  CA  A LEU A 1 979  ? 51.500 49.966  -14.467 0.50 9.29  ? 979  LEU A CA  1 
ATOM   7898 C  CA  B LEU A 1 979  ? 51.500 49.966  -14.467 0.50 11.28 ? 979  LEU A CA  1 
ATOM   7899 C  C   A LEU A 1 979  ? 50.025 49.707  -14.488 0.50 8.53  ? 979  LEU A C   1 
ATOM   7900 C  C   B LEU A 1 979  ? 50.025 49.707  -14.488 0.50 10.34 ? 979  LEU A C   1 
ATOM   7901 O  O   A LEU A 1 979  ? 49.517 48.814  -13.765 0.50 11.85 ? 979  LEU A O   1 
ATOM   7902 O  O   B LEU A 1 979  ? 49.517 48.814  -13.765 0.50 12.68 ? 979  LEU A O   1 
ATOM   7903 C  CB  A LEU A 1 979  ? 52.168 48.716  -15.027 0.50 11.76 ? 979  LEU A CB  1 
ATOM   7904 C  CB  B LEU A 1 979  ? 52.168 48.716  -15.027 0.50 16.99 ? 979  LEU A CB  1 
ATOM   7905 C  CG  A LEU A 1 979  ? 53.249 48.542  -16.101 0.50 22.12 ? 979  LEU A CG  1 
ATOM   7906 C  CG  B LEU A 1 979  ? 53.187 48.535  -16.159 0.50 27.15 ? 979  LEU A CG  1 
ATOM   7907 C  CD1 A LEU A 1 979  ? 53.119 47.140  -16.756 0.50 15.94 ? 979  LEU A CD1 1 
ATOM   7908 C  CD1 B LEU A 1 979  ? 54.209 49.704  -16.139 0.50 27.85 ? 979  LEU A CD1 1 
ATOM   7909 C  CD2 A LEU A 1 979  ? 53.095 49.570  -17.148 0.50 13.72 ? 979  LEU A CD2 1 
ATOM   7910 C  CD2 B LEU A 1 979  ? 53.917 47.264  -15.987 0.50 27.37 ? 979  LEU A CD2 1 
ATOM   7911 N  N   . HIS A 1 980  ? 49.313 50.463  -15.295 1.00 8.70  ? 980  HIS A N   1 
ATOM   7912 C  CA  . HIS A 1 980  ? 47.860 50.305  -15.427 1.00 9.57  ? 980  HIS A CA  1 
ATOM   7913 C  C   . HIS A 1 980  ? 47.485 50.011  -16.881 1.00 9.65  ? 980  HIS A C   1 
ATOM   7914 O  O   . HIS A 1 980  ? 47.936 50.736  -17.773 1.00 11.46 ? 980  HIS A O   1 
ATOM   7915 C  CB  . HIS A 1 980  ? 47.058 51.585  -15.015 1.00 10.25 ? 980  HIS A CB  1 
ATOM   7916 C  CG  . HIS A 1 980  ? 45.575 51.363  -15.109 1.00 10.27 ? 980  HIS A CG  1 
ATOM   7917 N  ND1 . HIS A 1 980  ? 44.699 51.952  -16.012 1.00 14.02 ? 980  HIS A ND1 1 
ATOM   7918 C  CD2 . HIS A 1 980  ? 44.840 50.487  -14.408 1.00 7.90  ? 980  HIS A CD2 1 
ATOM   7919 C  CE1 . HIS A 1 980  ? 43.485 51.435  -15.840 1.00 8.41  ? 980  HIS A CE1 1 
ATOM   7920 N  NE2 . HIS A 1 980  ? 43.557 50.532  -14.884 1.00 14.22 ? 980  HIS A NE2 1 
ATOM   7921 N  N   . ARG A 1 981  ? 46.678 48.977  -17.116 1.00 8.49  ? 981  ARG A N   1 
ATOM   7922 C  CA  . ARG A 1 981  ? 46.148 48.780  -18.471 1.00 9.22  ? 981  ARG A CA  1 
ATOM   7923 C  C   . ARG A 1 981  ? 44.665 48.978  -18.419 1.00 7.92  ? 981  ARG A C   1 
ATOM   7924 O  O   . ARG A 1 981  ? 43.990 48.316  -17.617 1.00 9.86  ? 981  ARG A O   1 
ATOM   7925 C  CB  . ARG A 1 981  ? 46.445 47.386  -19.034 1.00 11.49 ? 981  ARG A CB  1 
ATOM   7926 C  CG  . ARG A 1 981  ? 46.207 47.356  -20.621 1.00 13.92 ? 981  ARG A CG  1 
ATOM   7927 C  CD  . ARG A 1 981  ? 46.220 45.968  -21.351 1.00 20.46 ? 981  ARG A CD  1 
ATOM   7928 N  NE  . ARG A 1 981  ? 47.465 45.287  -21.134 1.00 22.81 ? 981  ARG A NE  1 
ATOM   7929 C  CZ  . ARG A 1 981  ? 48.500 45.321  -21.988 1.00 21.32 ? 981  ARG A CZ  1 
ATOM   7930 N  NH1 . ARG A 1 981  ? 48.440 46.038  -23.134 1.00 19.67 ? 981  ARG A NH1 1 
ATOM   7931 N  NH2 . ARG A 1 981  ? 49.582 44.568  -21.719 1.00 21.17 ? 981  ARG A NH2 1 
ATOM   7932 N  N   . THR A 1 982  ? 44.176 49.877  -19.261 1.00 9.46  ? 982  THR A N   1 
ATOM   7933 C  CA  . THR A 1 982  ? 42.717 50.085  -19.345 1.00 9.72  ? 982  THR A CA  1 
ATOM   7934 C  C   . THR A 1 982  ? 42.206 49.059  -20.374 1.00 10.32 ? 982  THR A C   1 
ATOM   7935 O  O   . THR A 1 982  ? 42.932 48.119  -20.732 1.00 12.63 ? 982  THR A O   1 
ATOM   7936 C  CB  . THR A 1 982  ? 42.416 51.534  -19.787 1.00 9.73  ? 982  THR A CB  1 
ATOM   7937 O  OG1 . THR A 1 982  ? 41.033 51.790  -19.637 1.00 11.47 ? 982  THR A OG1 1 
ATOM   7938 C  CG2 . THR A 1 982  ? 42.889 51.845  -21.227 1.00 11.40 ? 982  THR A CG2 1 
ATOM   7939 N  N   . ASN A 1 983  ? 40.941 49.153  -20.708 1.00 9.00  ? 983  ASN A N   1 
ATOM   7940 C  CA  . ASN A 1 983  ? 40.369 48.248  -21.740 1.00 9.47  ? 983  ASN A CA  1 
ATOM   7941 C  C   . ASN A 1 983  ? 39.633 49.135  -22.755 1.00 9.82  ? 983  ASN A C   1 
ATOM   7942 O  O   . ASN A 1 983  ? 38.722 49.882  -22.384 1.00 11.48 ? 983  ASN A O   1 
ATOM   7943 C  CB  . ASN A 1 983  ? 39.374 47.239  -21.130 1.00 9.30  ? 983  ASN A CB  1 
ATOM   7944 C  CG  . ASN A 1 983  ? 38.862 46.265  -22.184 1.00 9.01  ? 983  ASN A CG  1 
ATOM   7945 O  OD1 . ASN A 1 983  ? 39.606 45.375  -22.578 1.00 12.17 ? 983  ASN A OD1 1 
ATOM   7946 N  ND2 . ASN A 1 983  ? 37.654 46.505  -22.664 1.00 11.09 ? 983  ASN A ND2 1 
ATOM   7947 N  N   . LEU A 1 984  ? 40.079 49.016  -23.987 1.00 9.94  ? 984  LEU A N   1 
ATOM   7948 C  CA  . LEU A 1 984  ? 39.508 49.790  -25.082 1.00 9.78  ? 984  LEU A CA  1 
ATOM   7949 C  C   . LEU A 1 984  ? 38.679 48.899  -25.988 1.00 11.85 ? 984  LEU A C   1 
ATOM   7950 O  O   . LEU A 1 984  ? 38.995 47.732  -26.205 1.00 13.75 ? 984  LEU A O   1 
ATOM   7951 C  CB  . LEU A 1 984  ? 40.634 50.430  -25.905 1.00 11.60 ? 984  LEU A CB  1 
ATOM   7952 C  CG  . LEU A 1 984  ? 41.585 51.311  -25.054 1.00 12.38 ? 984  LEU A CG  1 
ATOM   7953 C  CD1 . LEU A 1 984  ? 42.744 51.797  -25.975 1.00 14.21 ? 984  LEU A CD1 1 
ATOM   7954 C  CD2 . LEU A 1 984  ? 40.837 52.485  -24.424 1.00 13.09 ? 984  LEU A CD2 1 
ATOM   7955 N  N   . MET A 1 985  ? 37.622 49.460  -26.539 1.00 12.35 ? 985  MET A N   1 
ATOM   7956 C  CA  . MET A 1 985  ? 36.790 48.622  -27.433 1.00 15.88 ? 985  MET A CA  1 
ATOM   7957 C  C   . MET A 1 985  ? 37.468 48.263  -28.714 1.00 19.44 ? 985  MET A C   1 
ATOM   7958 O  O   . MET A 1 985  ? 38.236 49.033  -29.298 1.00 17.05 ? 985  MET A O   1 
ATOM   7959 C  CB  . MET A 1 985  ? 35.518 49.350  -27.786 1.00 17.57 ? 985  MET A CB  1 
ATOM   7960 C  CG  . MET A 1 985  ? 34.603 49.450  -26.605 1.00 19.05 ? 985  MET A CG  1 
ATOM   7961 S  SD  . MET A 1 985  ? 32.899 49.600  -27.093 1.00 21.74 ? 985  MET A SD  1 
ATOM   7962 C  CE  . MET A 1 985  ? 33.004 51.138  -27.887 1.00 19.84 ? 985  MET A CE  1 
ATOM   7963 N  N   . GLN A 1 986  ? 37.163 47.050  -29.159 1.00 19.02 ? 986  GLN A N   1 
ATOM   7964 C  CA  . GLN A 1 986  ? 37.671 46.563  -30.455 1.00 18.08 ? 986  GLN A CA  1 
ATOM   7965 C  C   . GLN A 1 986  ? 36.643 47.045  -31.466 1.00 17.57 ? 986  GLN A C   1 
ATOM   7966 O  O   . GLN A 1 986  ? 35.469 46.658  -31.354 1.00 17.23 ? 986  GLN A O   1 
ATOM   7967 C  CB  . GLN A 1 986  ? 37.685 45.022  -30.467 1.00 22.31 ? 986  GLN A CB  1 
ATOM   7968 C  CG  . GLN A 1 986  ? 38.751 44.335  -29.586 1.00 28.13 ? 986  GLN A CG  1 
ATOM   7969 C  CD  . GLN A 1 986  ? 40.159 44.622  -30.072 1.00 34.31 ? 986  GLN A CD  1 
ATOM   7970 O  OE1 . GLN A 1 986  ? 41.068 44.812  -29.260 1.00 42.17 ? 986  GLN A OE1 1 
ATOM   7971 N  NE2 . GLN A 1 986  ? 40.362 44.651  -31.408 1.00 35.81 ? 986  GLN A NE2 1 
ATOM   7972 N  N   . CYS A 1 987  ? 37.059 47.898  -32.414 1.00 18.19 ? 987  CYS A N   1 
ATOM   7973 C  CA  . CYS A 1 987  ? 36.108 48.397  -33.399 1.00 19.20 ? 987  CYS A CA  1 
ATOM   7974 C  C   . CYS A 1 987  ? 36.559 48.183  -34.833 1.00 22.49 ? 987  CYS A C   1 
ATOM   7975 O  O   . CYS A 1 987  ? 35.997 48.823  -35.742 1.00 24.64 ? 987  CYS A O   1 
ATOM   7976 C  CB  . CYS A 1 987  ? 35.795 49.877  -33.164 1.00 20.36 ? 987  CYS A CB  1 
ATOM   7977 S  SG  . CYS A 1 987  ? 35.187 50.291  -31.472 1.00 22.55 ? 987  CYS A SG  1 
ATOM   7978 N  N   . GLY A 1 988  ? 37.532 47.296  -35.041 1.00 19.81 ? 988  GLY A N   1 
ATOM   7979 C  CA  . GLY A 1 988  ? 37.947 47.032  -36.413 1.00 26.32 ? 988  GLY A CA  1 
ATOM   7980 C  C   . GLY A 1 988  ? 39.188 47.714  -36.912 1.00 30.41 ? 988  GLY A C   1 
ATOM   7981 O  O   . GLY A 1 988  ? 39.503 47.633  -38.121 1.00 30.21 ? 988  GLY A O   1 
ATOM   7982 N  N   . THR A 1 989  ? 39.901 48.396  -36.025 1.00 29.26 ? 989  THR A N   1 
ATOM   7983 C  CA  . THR A 1 989  ? 41.126 49.038  -36.459 1.00 30.44 ? 989  THR A CA  1 
ATOM   7984 C  C   . THR A 1 989  ? 42.247 48.066  -36.227 1.00 34.25 ? 989  THR A C   1 
ATOM   7985 O  O   . THR A 1 989  ? 42.496 47.651  -35.094 1.00 33.11 ? 989  THR A O   1 
ATOM   7986 C  CB  . THR A 1 989  ? 41.382 50.295  -35.678 1.00 31.10 ? 989  THR A CB  1 
ATOM   7987 O  OG1 . THR A 1 989  ? 40.246 51.147  -35.827 1.00 32.85 ? 989  THR A OG1 1 
ATOM   7988 C  CG2 . THR A 1 989  ? 42.615 51.007  -36.214 1.00 32.83 ? 989  THR A CG2 1 
ATOM   7989 N  N   . PRO A 1 990  ? 42.945 47.675  -37.310 1.00 34.05 ? 990  PRO A N   1 
ATOM   7990 C  CA  . PRO A 1 990  ? 44.042 46.726  -37.123 1.00 36.00 ? 990  PRO A CA  1 
ATOM   7991 C  C   . PRO A 1 990  ? 45.065 47.186  -36.072 1.00 39.32 ? 990  PRO A C   1 
ATOM   7992 O  O   . PRO A 1 990  ? 45.658 46.327  -35.406 1.00 41.59 ? 990  PRO A O   1 
ATOM   7993 C  CB  . PRO A 1 990  ? 44.657 46.623  -38.521 1.00 36.87 ? 990  PRO A CB  1 
ATOM   7994 C  CG  . PRO A 1 990  ? 43.520 46.903  -39.442 1.00 34.72 ? 990  PRO A CG  1 
ATOM   7995 C  CD  . PRO A 1 990  ? 42.800 48.058  -38.728 1.00 35.61 ? 990  PRO A CD  1 
ATOM   7996 N  N   . GLU A 1 991  ? 45.235 48.502  -35.867 1.00 41.13 ? 991  GLU A N   1 
ATOM   7997 C  CA  . GLU A 1 991  ? 46.246 49.028  -34.909 1.00 46.41 ? 991  GLU A CA  1 
ATOM   7998 C  C   . GLU A 1 991  ? 47.247 47.918  -34.482 1.00 47.64 ? 991  GLU A C   1 
ATOM   7999 O  O   . GLU A 1 991  ? 46.902 46.967  -33.752 1.00 50.18 ? 991  GLU A O   1 
ATOM   8000 C  CB  . GLU A 1 991  ? 45.573 49.732  -33.688 1.00 46.76 ? 991  GLU A CB  1 
ATOM   8001 C  CG  . GLU A 1 991  ? 44.894 51.083  -34.101 1.00 48.33 ? 991  GLU A CG  1 
ATOM   8002 C  CD  . GLU A 1 991  ? 44.164 51.886  -32.980 1.00 50.56 ? 991  GLU A CD  1 
ATOM   8003 O  OE1 . GLU A 1 991  ? 43.398 51.306  -32.157 1.00 45.43 ? 991  GLU A OE1 1 
ATOM   8004 O  OE2 . GLU A 1 991  ? 44.335 53.138  -32.964 1.00 49.17 ? 991  GLU A OE2 1 
ATOM   8005 N  N   . GLU A 1 992  ? 48.487 48.040  -34.952 1.00 46.60 ? 992  GLU A N   1 
ATOM   8006 C  CA  . GLU A 1 992  ? 49.484 47.003  -34.702 1.00 47.42 ? 992  GLU A CA  1 
ATOM   8007 C  C   . GLU A 1 992  ? 50.806 47.322  -33.966 1.00 44.47 ? 992  GLU A C   1 
ATOM   8008 O  O   . GLU A 1 992  ? 50.792 47.789  -32.853 1.00 43.28 ? 992  GLU A O   1 
ATOM   8009 C  CB  . GLU A 1 992  ? 49.792 46.343  -36.051 1.00 49.57 ? 992  GLU A CB  1 
ATOM   8010 C  CG  . GLU A 1 992  ? 48.522 45.866  -36.806 1.00 50.69 ? 992  GLU A CG  1 
ATOM   8011 C  CD  . GLU A 1 992  ? 47.827 44.688  -36.121 1.00 51.35 ? 992  GLU A CD  1 
ATOM   8012 O  OE1 . GLU A 1 992  ? 46.959 44.032  -36.755 1.00 53.07 ? 992  GLU A OE1 1 
ATOM   8013 O  OE2 . GLU A 1 992  ? 48.143 44.409  -34.941 1.00 52.78 ? 992  GLU A OE2 1 
ATOM   8014 N  N   . HIS A 1 993  ? 51.936 47.046  -34.614 1.00 42.52 ? 993  HIS A N   1 
ATOM   8015 C  CA  . HIS A 1 993  ? 53.309 47.249  -34.076 1.00 42.11 ? 993  HIS A CA  1 
ATOM   8016 C  C   . HIS A 1 993  ? 53.670 48.171  -32.885 1.00 39.58 ? 993  HIS A C   1 
ATOM   8017 O  O   . HIS A 1 993  ? 53.812 49.409  -33.028 1.00 39.66 ? 993  HIS A O   1 
ATOM   8018 C  CB  . HIS A 1 993  ? 54.271 47.616  -35.233 1.00 42.87 ? 993  HIS A CB  1 
ATOM   8019 C  CG  . HIS A 1 993  ? 53.903 48.881  -35.936 1.00 43.90 ? 993  HIS A CG  1 
ATOM   8020 N  ND1 . HIS A 1 993  ? 52.767 48.996  -36.714 1.00 47.46 ? 993  HIS A ND1 1 
ATOM   8021 C  CD2 . HIS A 1 993  ? 54.464 50.113  -35.905 1.00 44.58 ? 993  HIS A CD2 1 
ATOM   8022 C  CE1 . HIS A 1 993  ? 52.641 50.248  -37.126 1.00 47.73 ? 993  HIS A CE1 1 
ATOM   8023 N  NE2 . HIS A 1 993  ? 53.657 50.946  -36.649 1.00 47.27 ? 993  HIS A NE2 1 
ATOM   8024 N  N   . THR A 1 994  ? 53.843 47.551  -31.713 1.00 36.35 ? 994  THR A N   1 
ATOM   8025 C  CA  . THR A 1 994  ? 54.284 48.265  -30.515 1.00 29.12 ? 994  THR A CA  1 
ATOM   8026 C  C   . THR A 1 994  ? 55.290 47.343  -29.827 1.00 28.32 ? 994  THR A C   1 
ATOM   8027 O  O   . THR A 1 994  ? 55.354 46.147  -30.107 1.00 30.84 ? 994  THR A O   1 
ATOM   8028 C  CB  . THR A 1 994  ? 53.132 48.578  -29.554 1.00 25.41 ? 994  THR A CB  1 
ATOM   8029 O  OG1 . THR A 1 994  ? 52.459 47.366  -29.203 1.00 27.06 ? 994  THR A OG1 1 
ATOM   8030 C  CG2 . THR A 1 994  ? 52.133 49.507  -30.225 1.00 23.40 ? 994  THR A CG2 1 
ATOM   8031 N  N   . GLN A 1 995  ? 56.058 47.869  -28.886 1.00 23.23 ? 995  GLN A N   1 
ATOM   8032 C  CA  . GLN A 1 995  ? 57.050 47.048  -28.237 1.00 22.32 ? 995  GLN A CA  1 
ATOM   8033 C  C   . GLN A 1 995  ? 56.608 46.717  -26.842 1.00 19.42 ? 995  GLN A C   1 
ATOM   8034 O  O   . GLN A 1 995  ? 55.928 47.504  -26.175 1.00 19.82 ? 995  GLN A O   1 
ATOM   8035 C  CB  . GLN A 1 995  ? 58.355 47.820  -28.137 1.00 20.67 ? 995  GLN A CB  1 
ATOM   8036 C  CG  . GLN A 1 995  ? 58.812 48.289  -29.501 1.00 27.32 ? 995  GLN A CG  1 
ATOM   8037 C  CD  . GLN A 1 995  ? 59.676 49.516  -29.418 1.00 33.09 ? 995  GLN A CD  1 
ATOM   8038 O  OE1 . GLN A 1 995  ? 59.181 50.649  -29.276 1.00 23.54 ? 995  GLN A OE1 1 
ATOM   8039 N  NE2 . GLN A 1 995  ? 60.988 49.304  -29.484 1.00 36.77 ? 995  GLN A NE2 1 
ATOM   8040 N  N   . LYS A 1 996  ? 57.064 45.572  -26.376 1.00 17.70 ? 996  LYS A N   1 
ATOM   8041 C  CA  . LYS A 1 996  ? 56.795 45.144  -25.016 1.00 18.34 ? 996  LYS A CA  1 
ATOM   8042 C  C   . LYS A 1 996  ? 57.504 46.116  -24.075 1.00 16.37 ? 996  LYS A C   1 
ATOM   8043 O  O   . LYS A 1 996  ? 58.666 46.494  -24.281 1.00 18.08 ? 996  LYS A O   1 
ATOM   8044 C  CB  . LYS A 1 996  ? 57.356 43.699  -24.823 1.00 21.28 ? 996  LYS A CB  1 
ATOM   8045 C  CG  . LYS A 1 996  ? 57.099 43.088  -23.454 1.00 26.23 ? 996  LYS A CG  1 
ATOM   8046 C  CD  . LYS A 1 996  ? 57.641 41.606  -23.450 1.00 29.34 ? 996  LYS A CD  1 
ATOM   8047 C  CE  . LYS A 1 996  ? 57.574 40.966  -22.051 1.00 34.64 ? 996  LYS A CE  1 
ATOM   8048 N  NZ  . LYS A 1 996  ? 57.733 39.491  -22.210 1.00 41.42 ? 996  LYS A NZ  1 
ATOM   8049 N  N   . LEU A 1 997  ? 56.792 46.523  -23.031 1.00 16.19 ? 997  LEU A N   1 
ATOM   8050 C  CA  . LEU A 1 997  ? 57.401 47.414  -22.056 1.00 16.01 ? 997  LEU A CA  1 
ATOM   8051 C  C   . LEU A 1 997  ? 57.739 46.602  -20.804 1.00 13.60 ? 997  LEU A C   1 
ATOM   8052 O  O   . LEU A 1 997  ? 56.825 46.058  -20.160 1.00 16.50 ? 997  LEU A O   1 
ATOM   8053 C  CB  . LEU A 1 997  ? 56.391 48.503  -21.695 1.00 17.29 ? 997  LEU A CB  1 
ATOM   8054 C  CG  . LEU A 1 997  ? 56.817 49.356  -20.493 1.00 18.01 ? 997  LEU A CG  1 
ATOM   8055 C  CD1 . LEU A 1 997  ? 58.069 50.099  -20.809 1.00 20.41 ? 997  LEU A CD1 1 
ATOM   8056 C  CD2 . LEU A 1 997  ? 55.706 50.336  -20.178 1.00 21.67 ? 997  LEU A CD2 1 
ATOM   8057 N  N   . ASP A 1 998  ? 59.027 46.545  -20.506 1.00 14.23 ? 998  ASP A N   1 
ATOM   8058 C  CA  . ASP A 1 998  ? 59.511 45.893  -19.293 1.00 15.84 ? 998  ASP A CA  1 
ATOM   8059 C  C   . ASP A 1 998  ? 60.097 47.008  -18.437 1.00 14.04 ? 998  ASP A C   1 
ATOM   8060 O  O   . ASP A 1 998  ? 61.213 47.480  -18.640 1.00 14.39 ? 998  ASP A O   1 
ATOM   8061 C  CB  . ASP A 1 998  ? 60.577 44.830  -19.635 1.00 16.50 ? 998  ASP A CB  1 
ATOM   8062 C  CG  . ASP A 1 998  ? 61.249 44.292  -18.407 1.00 20.04 ? 998  ASP A CG  1 
ATOM   8063 O  OD1 . ASP A 1 998  ? 62.289 43.626  -18.586 1.00 18.77 ? 998  ASP A OD1 1 
ATOM   8064 O  OD2 . ASP A 1 998  ? 60.763 44.529  -17.267 1.00 17.42 ? 998  ASP A OD2 1 
ATOM   8065 N  N   . VAL A 1 999  ? 59.319 47.446  -17.451 1.00 14.11 ? 999  VAL A N   1 
ATOM   8066 C  CA  . VAL A 1 999  ? 59.810 48.562  -16.651 1.00 12.67 ? 999  VAL A CA  1 
ATOM   8067 C  C   . VAL A 1 999  ? 61.055 48.256  -15.868 1.00 13.46 ? 999  VAL A C   1 
ATOM   8068 O  O   . VAL A 1 999  ? 61.822 49.170  -15.540 1.00 13.93 ? 999  VAL A O   1 
ATOM   8069 C  CB  . VAL A 1 999  ? 58.722 49.137  -15.667 1.00 12.70 ? 999  VAL A CB  1 
ATOM   8070 C  CG1 . VAL A 1 999  ? 57.617 49.732  -16.513 1.00 14.31 ? 999  VAL A CG1 1 
ATOM   8071 C  CG2 . VAL A 1 999  ? 58.150 48.070  -14.744 1.00 15.38 ? 999  VAL A CG2 1 
ATOM   8072 N  N   . CYS A 1 1000 ? 61.305 46.966  -15.580 1.00 13.27 ? 1000 CYS A N   1 
ATOM   8073 C  CA  . CYS A 1 1000 ? 62.468 46.641  -14.806 1.00 14.97 ? 1000 CYS A CA  1 
ATOM   8074 C  C   . CYS A 1 1000 ? 63.796 46.847  -15.546 1.00 14.84 ? 1000 CYS A C   1 
ATOM   8075 O  O   . CYS A 1 1000 ? 64.837 46.921  -14.897 1.00 16.92 ? 1000 CYS A O   1 
ATOM   8076 C  CB  . CYS A 1 1000 ? 62.326 45.228  -14.267 1.00 15.61 ? 1000 CYS A CB  1 
ATOM   8077 S  SG  . CYS A 1 1000 ? 61.427 45.269  -12.636 1.00 20.69 ? 1000 CYS A SG  1 
ATOM   8078 N  N   . HIS A 1 1001 ? 63.723 47.015  -16.878 1.00 15.37 ? 1001 HIS A N   1 
ATOM   8079 C  CA  . HIS A 1 1001 ? 64.928 47.269  -17.668 1.00 15.40 ? 1001 HIS A CA  1 
ATOM   8080 C  C   . HIS A 1 1001 ? 65.022 48.705  -18.201 1.00 17.69 ? 1001 HIS A C   1 
ATOM   8081 O  O   . HIS A 1 1001 ? 65.836 49.006  -19.060 1.00 19.55 ? 1001 HIS A O   1 
ATOM   8082 C  CB  . HIS A 1 1001 ? 65.059 46.231  -18.786 1.00 18.10 ? 1001 HIS A CB  1 
ATOM   8083 C  CG  . HIS A 1 1001 ? 65.648 44.924  -18.334 1.00 17.81 ? 1001 HIS A CG  1 
ATOM   8084 N  ND1 . HIS A 1 1001 ? 64.877 43.891  -17.854 1.00 19.32 ? 1001 HIS A ND1 1 
ATOM   8085 C  CD2 . HIS A 1 1001 ? 66.937 44.517  -18.213 1.00 22.27 ? 1001 HIS A CD2 1 
ATOM   8086 C  CE1 . HIS A 1 1001 ? 65.657 42.899  -17.448 1.00 18.90 ? 1001 HIS A CE1 1 
ATOM   8087 N  NE2 . HIS A 1 1001 ? 66.917 43.251  -17.656 1.00 20.21 ? 1001 HIS A NE2 1 
ATOM   8088 N  N   . LEU A 1 1002 ? 64.199 49.622  -17.690 1.00 15.29 ? 1002 LEU A N   1 
ATOM   8089 C  CA  . LEU A 1 1002 ? 64.286 51.017  -18.127 1.00 13.20 ? 1002 LEU A CA  1 
ATOM   8090 C  C   . LEU A 1 1002 ? 65.546 51.668  -17.583 1.00 16.54 ? 1002 LEU A C   1 
ATOM   8091 O  O   . LEU A 1 1002 ? 66.053 52.614  -18.202 1.00 19.72 ? 1002 LEU A O   1 
ATOM   8092 C  CB  . LEU A 1 1002 ? 63.077 51.847  -17.642 1.00 15.94 ? 1002 LEU A CB  1 
ATOM   8093 C  CG  . LEU A 1 1002 ? 61.826 51.608  -18.440 1.00 14.16 ? 1002 LEU A CG  1 
ATOM   8094 C  CD1 . LEU A 1 1002 ? 60.659 52.300  -17.752 1.00 14.59 ? 1002 LEU A CD1 1 
ATOM   8095 C  CD2 . LEU A 1 1002 ? 61.982 52.178  -19.864 1.00 18.45 ? 1002 LEU A CD2 1 
ATOM   8096 N  N   . LEU A 1 1003 ? 66.038 51.250  -16.424 1.00 16.91 ? 1003 LEU A N   1 
ATOM   8097 C  CA  . LEU A 1 1003 ? 67.277 51.787  -15.855 1.00 17.20 ? 1003 LEU A CA  1 
ATOM   8098 C  C   . LEU A 1 1003 ? 68.308 50.665  -15.992 1.00 18.61 ? 1003 LEU A C   1 
ATOM   8099 O  O   . LEU A 1 1003 ? 67.987 49.479  -15.872 1.00 18.56 ? 1003 LEU A O   1 
ATOM   8100 C  CB  . LEU A 1 1003 ? 67.102 52.198  -14.389 1.00 16.48 ? 1003 LEU A CB  1 
ATOM   8101 C  CG  . LEU A 1 1003 ? 66.415 53.573  -14.326 1.00 23.47 ? 1003 LEU A CG  1 
ATOM   8102 C  CD1 . LEU A 1 1003 ? 65.780 53.721  -12.959 1.00 25.87 ? 1003 LEU A CD1 1 
ATOM   8103 C  CD2 . LEU A 1 1003 ? 67.427 54.712  -14.623 1.00 24.19 ? 1003 LEU A CD2 1 
ATOM   8104 N  N   . PRO A 1 1004 ? 69.562 51.041  -16.195 1.00 19.11 ? 1004 PRO A N   1 
ATOM   8105 C  CA  . PRO A 1 1004 ? 70.576 50.001  -16.363 1.00 16.72 ? 1004 PRO A CA  1 
ATOM   8106 C  C   . PRO A 1 1004 ? 71.009 49.315  -15.097 1.00 17.45 ? 1004 PRO A C   1 
ATOM   8107 O  O   . PRO A 1 1004 ? 70.638 49.687  -13.950 1.00 17.04 ? 1004 PRO A O   1 
ATOM   8108 C  CB  . PRO A 1 1004 ? 71.732 50.763  -17.025 1.00 19.96 ? 1004 PRO A CB  1 
ATOM   8109 C  CG  . PRO A 1 1004 ? 71.645 52.112  -16.373 1.00 20.97 ? 1004 PRO A CG  1 
ATOM   8110 C  CD  . PRO A 1 1004 ? 70.131 52.392  -16.311 1.00 20.41 ? 1004 PRO A CD  1 
ATOM   8111 N  N   . ASN A 1 1005 ? 71.800 48.262  -15.316 1.00 18.91 ? 1005 ASN A N   1 
ATOM   8112 C  CA  . ASN A 1 1005 ? 72.383 47.500  -14.206 1.00 19.33 ? 1005 ASN A CA  1 
ATOM   8113 C  C   . ASN A 1 1005 ? 71.331 46.905  -13.252 1.00 18.64 ? 1005 ASN A C   1 
ATOM   8114 O  O   . ASN A 1 1005 ? 71.514 46.943  -12.048 1.00 18.48 ? 1005 ASN A O   1 
ATOM   8115 C  CB  . ASN A 1 1005 ? 73.333 48.385  -13.399 1.00 22.31 ? 1005 ASN A CB  1 
ATOM   8116 C  CG  . ASN A 1 1005 ? 74.324 49.139  -14.286 1.00 27.47 ? 1005 ASN A CG  1 
ATOM   8117 O  OD1 . ASN A 1 1005 ? 74.377 50.397  -14.286 1.00 32.20 ? 1005 ASN A OD1 1 
ATOM   8118 N  ND2 . ASN A 1 1005 ? 75.089 48.391  -15.052 1.00 26.30 ? 1005 ASN A ND2 1 
ATOM   8119 N  N   . VAL A 1 1006 ? 70.281 46.324  -13.803 1.00 17.90 ? 1006 VAL A N   1 
ATOM   8120 C  CA  . VAL A 1 1006 ? 69.233 45.744  -12.966 1.00 18.61 ? 1006 VAL A CA  1 
ATOM   8121 C  C   . VAL A 1 1006 ? 69.783 44.448  -12.304 1.00 19.05 ? 1006 VAL A C   1 
ATOM   8122 O  O   . VAL A 1 1006 ? 70.357 43.611  -12.975 1.00 23.30 ? 1006 VAL A O   1 
ATOM   8123 C  CB  . VAL A 1 1006 ? 67.884 45.498  -13.782 1.00 17.65 ? 1006 VAL A CB  1 
ATOM   8124 C  CG1 . VAL A 1 1006 ? 67.985 44.442  -14.791 1.00 20.94 ? 1006 VAL A CG1 1 
ATOM   8125 C  CG2 . VAL A 1 1006 ? 66.780 45.083  -12.823 1.00 16.57 ? 1006 VAL A CG2 1 
ATOM   8126 N  N   . ALA A 1 1007 ? 69.561 44.319  -11.005 1.00 16.91 ? 1007 ALA A N   1 
ATOM   8127 C  CA  . ALA A 1 1007 ? 70.010 43.183  -10.183 1.00 18.32 ? 1007 ALA A CA  1 
ATOM   8128 C  C   . ALA A 1 1007 ? 68.811 42.336  -9.737  1.00 20.87 ? 1007 ALA A C   1 
ATOM   8129 O  O   . ALA A 1 1007 ? 68.954 41.130  -9.453  1.00 21.76 ? 1007 ALA A O   1 
ATOM   8130 C  CB  . ALA A 1 1007 ? 70.787 43.724  -8.939  1.00 19.71 ? 1007 ALA A CB  1 
ATOM   8131 N  N   . ARG A 1 1008 ? 67.606 42.936  -9.665  1.00 18.71 ? 1008 ARG A N   1 
ATOM   8132 C  CA  . ARG A 1 1008 ? 66.427 42.187  -9.206  1.00 16.26 ? 1008 ARG A CA  1 
ATOM   8133 C  C   . ARG A 1 1008 ? 65.176 42.939  -9.660  1.00 14.31 ? 1008 ARG A C   1 
ATOM   8134 O  O   . ARG A 1 1008 ? 65.223 44.191  -9.785  1.00 16.10 ? 1008 ARG A O   1 
ATOM   8135 C  CB  . ARG A 1 1008 ? 66.441 42.153  -7.683  1.00 17.03 ? 1008 ARG A CB  1 
ATOM   8136 C  CG  . ARG A 1 1008 ? 65.442 41.212  -7.044  1.00 22.40 ? 1008 ARG A CG  1 
ATOM   8137 C  CD  . ARG A 1 1008 ? 65.512 41.370  -5.501  1.00 23.97 ? 1008 ARG A CD  1 
ATOM   8138 N  NE  . ARG A 1 1008 ? 64.755 40.328  -4.786  1.00 35.00 ? 1008 ARG A NE  1 
ATOM   8139 C  CZ  . ARG A 1 1008 ? 65.114 39.034  -4.709  1.00 38.49 ? 1008 ARG A CZ  1 
ATOM   8140 N  NH1 . ARG A 1 1008 ? 66.237 38.583  -5.291  1.00 40.34 ? 1008 ARG A NH1 1 
ATOM   8141 N  NH2 . ARG A 1 1008 ? 64.331 38.172  -4.062  1.00 35.87 ? 1008 ARG A NH2 1 
ATOM   8142 N  N   . CYS A 1 1009 ? 64.105 42.192  -9.890  1.00 14.72 ? 1009 CYS A N   1 
ATOM   8143 C  CA  . CYS A 1 1009 ? 62.800 42.819  -10.262 1.00 15.15 ? 1009 CYS A CA  1 
ATOM   8144 C  C   . CYS A 1 1009 ? 61.772 42.101  -9.399  1.00 15.30 ? 1009 CYS A C   1 
ATOM   8145 O  O   . CYS A 1 1009 ? 61.706 40.842  -9.389  1.00 14.99 ? 1009 CYS A O   1 
ATOM   8146 C  CB  . CYS A 1 1009 ? 62.499 42.600  -11.720 1.00 15.00 ? 1009 CYS A CB  1 
ATOM   8147 S  SG  . CYS A 1 1009 ? 60.938 43.331  -12.385 1.00 19.67 ? 1009 CYS A SG  1 
ATOM   8148 N  N   A GLU A 1 1010 ? 60.948 42.865  -8.681  0.50 12.86 ? 1010 GLU A N   1 
ATOM   8149 N  N   B GLU A 1 1010 ? 60.948 42.865  -8.681  0.50 13.87 ? 1010 GLU A N   1 
ATOM   8150 C  CA  A GLU A 1 1010 ? 59.941 42.279  -7.824  0.50 12.00 ? 1010 GLU A CA  1 
ATOM   8151 C  CA  B GLU A 1 1010 ? 59.941 42.279  -7.824  0.50 13.60 ? 1010 GLU A CA  1 
ATOM   8152 C  C   A GLU A 1 1010 ? 58.559 42.870  -8.092  0.50 11.77 ? 1010 GLU A C   1 
ATOM   8153 C  C   B GLU A 1 1010 ? 58.559 42.870  -8.092  0.50 12.96 ? 1010 GLU A C   1 
ATOM   8154 O  O   A GLU A 1 1010 ? 58.426 44.069  -8.376  0.50 13.10 ? 1010 GLU A O   1 
ATOM   8155 O  O   B GLU A 1 1010 ? 58.426 44.069  -8.376  0.50 13.85 ? 1010 GLU A O   1 
ATOM   8156 C  CB  A GLU A 1 1010 ? 60.275 42.554  -6.348  0.50 14.59 ? 1010 GLU A CB  1 
ATOM   8157 C  CB  B GLU A 1 1010 ? 60.275 42.554  -6.348  0.50 17.72 ? 1010 GLU A CB  1 
ATOM   8158 C  CG  A GLU A 1 1010 ? 61.535 41.755  -5.874  0.50 17.70 ? 1010 GLU A CG  1 
ATOM   8159 C  CG  B GLU A 1 1010 ? 61.517 41.733  -5.866  0.50 24.16 ? 1010 GLU A CG  1 
ATOM   8160 C  CD  A GLU A 1 1010 ? 62.350 42.362  -4.720  0.50 19.98 ? 1010 GLU A CD  1 
ATOM   8161 C  CD  B GLU A 1 1010 ? 61.237 40.482  -5.016  0.50 27.20 ? 1010 GLU A CD  1 
ATOM   8162 O  OE1 A GLU A 1 1010 ? 62.791 43.534  -4.780  0.50 19.15 ? 1010 GLU A OE1 1 
ATOM   8163 O  OE1 B GLU A 1 1010 ? 60.103 40.266  -4.530  0.50 31.86 ? 1010 GLU A OE1 1 
ATOM   8164 O  OE2 A GLU A 1 1010 ? 62.596 41.613  -3.735  0.50 23.65 ? 1010 GLU A OE2 1 
ATOM   8165 O  OE2 B GLU A 1 1010 ? 62.211 39.711  -4.791  0.50 33.27 ? 1010 GLU A OE2 1 
ATOM   8166 N  N   . ARG A 1 1011 ? 57.556 42.036  -8.064  1.00 11.35 ? 1011 ARG A N   1 
ATOM   8167 C  CA  . ARG A 1 1011 ? 56.169 42.565  -8.084  1.00 9.70  ? 1011 ARG A CA  1 
ATOM   8168 C  C   . ARG A 1 1011 ? 55.842 42.901  -6.615  1.00 11.48 ? 1011 ARG A C   1 
ATOM   8169 O  O   . ARG A 1 1011 ? 56.153 42.111  -5.694  1.00 12.59 ? 1011 ARG A O   1 
ATOM   8170 C  CB  . ARG A 1 1011 ? 55.172 41.542  -8.590  1.00 12.08 ? 1011 ARG A CB  1 
ATOM   8171 C  CG  . ARG A 1 1011 ? 53.766 42.199  -8.813  1.00 15.22 ? 1011 ARG A CG  1 
ATOM   8172 C  CD  . ARG A 1 1011 ? 52.866 41.329  -9.629  1.00 21.49 ? 1011 ARG A CD  1 
ATOM   8173 N  NE  . ARG A 1 1011 ? 52.589 40.142  -8.845  1.00 23.41 ? 1011 ARG A NE  1 
ATOM   8174 C  CZ  . ARG A 1 1011 ? 51.632 40.034  -7.915  1.00 28.39 ? 1011 ARG A CZ  1 
ATOM   8175 N  NH1 . ARG A 1 1011 ? 50.833 41.066  -7.639  1.00 32.01 ? 1011 ARG A NH1 1 
ATOM   8176 N  NH2 . ARG A 1 1011 ? 51.462 38.879  -7.264  1.00 28.42 ? 1011 ARG A NH2 1 
ATOM   8177 N  N   . THR A 1 1012 ? 55.222 44.048  -6.355  1.00 9.68  ? 1012 THR A N   1 
ATOM   8178 C  CA  . THR A 1 1012 ? 54.909 44.477  -5.006  1.00 8.92  ? 1012 THR A CA  1 
ATOM   8179 C  C   . THR A 1 1012 ? 53.429 44.914  -4.930  1.00 9.94  ? 1012 THR A C   1 
ATOM   8180 O  O   . THR A 1 1012 ? 52.733 45.068  -5.940  1.00 10.14 ? 1012 THR A O   1 
ATOM   8181 C  CB  . THR A 1 1012 ? 55.758 45.731  -4.595  1.00 10.61 ? 1012 THR A CB  1 
ATOM   8182 O  OG1 . THR A 1 1012 ? 55.428 46.850  -5.452  1.00 10.85 ? 1012 THR A OG1 1 
ATOM   8183 C  CG2 . THR A 1 1012 ? 57.231 45.465  -4.779  1.00 11.51 ? 1012 THR A CG2 1 
ATOM   8184 N  N   . THR A 1 1013 ? 52.991 45.150  -3.719  1.00 9.13  ? 1013 THR A N   1 
ATOM   8185 C  CA  . THR A 1 1013 ? 51.699 45.788  -3.517  1.00 9.97  ? 1013 THR A CA  1 
ATOM   8186 C  C   . THR A 1 1013 ? 51.829 47.194  -4.145  1.00 9.08  ? 1013 THR A C   1 
ATOM   8187 O  O   . THR A 1 1013 ? 52.921 47.762  -4.378  1.00 8.68  ? 1013 THR A O   1 
ATOM   8188 C  CB  . THR A 1 1013 ? 51.397 45.934  -2.045  1.00 9.26  ? 1013 THR A CB  1 
ATOM   8189 O  OG1 . THR A 1 1013 ? 52.578 46.393  -1.355  1.00 9.57  ? 1013 THR A OG1 1 
ATOM   8190 C  CG2 . THR A 1 1013 ? 50.919 44.551  -1.469  1.00 11.53 ? 1013 THR A CG2 1 
ATOM   8191 N  N   . LEU A 1 1014 ? 50.670 47.852  -4.387  1.00 8.12  ? 1014 LEU A N   1 
ATOM   8192 C  CA  . LEU A 1 1014 ? 50.684 49.170  -5.096  1.00 7.77  ? 1014 LEU A CA  1 
ATOM   8193 C  C   . LEU A 1 1014 ? 51.341 50.292  -4.364  1.00 6.51  ? 1014 LEU A C   1 
ATOM   8194 O  O   . LEU A 1 1014 ? 51.721 51.287  -4.981  1.00 8.25  ? 1014 LEU A O   1 
ATOM   8195 C  CB  . LEU A 1 1014 ? 49.259 49.603  -5.508  1.00 7.77  ? 1014 LEU A CB  1 
ATOM   8196 C  CG  . LEU A 1 1014 ? 48.520 48.621  -6.420  1.00 8.35  ? 1014 LEU A CG  1 
ATOM   8197 C  CD1 . LEU A 1 1014 ? 47.182 49.334  -6.824  1.00 9.61  ? 1014 LEU A CD1 1 
ATOM   8198 C  CD2 . LEU A 1 1014 ? 49.310 48.228  -7.661  1.00 10.08 ? 1014 LEU A CD2 1 
ATOM   8199 N  N   . THR A 1 1015 ? 51.510 50.150  -3.057  1.00 7.69  ? 1015 THR A N   1 
ATOM   8200 C  CA  . THR A 1 1015 ? 52.191 51.129  -2.212  1.00 8.36  ? 1015 THR A CA  1 
ATOM   8201 C  C   . THR A 1 1015 ? 53.708 50.878  -2.167  1.00 7.34  ? 1015 THR A C   1 
ATOM   8202 O  O   . THR A 1 1015 ? 54.414 51.660  -1.511  1.00 8.86  ? 1015 THR A O   1 
ATOM   8203 C  CB  . THR A 1 1015 ? 51.675 51.027  -0.791  1.00 8.62  ? 1015 THR A CB  1 
ATOM   8204 O  OG1 . THR A 1 1015 ? 51.850 49.640  -0.425  1.00 8.73  ? 1015 THR A OG1 1 
ATOM   8205 C  CG2 . THR A 1 1015 ? 50.166 51.389  -0.672  1.00 9.99  ? 1015 THR A CG2 1 
ATOM   8206 N  N   . PHE A 1 1016 ? 54.154 49.812  -2.836  1.00 8.57  ? 1016 PHE A N   1 
ATOM   8207 C  CA  . PHE A 1 1016 ? 55.582 49.360  -2.878  1.00 8.75  ? 1016 PHE A CA  1 
ATOM   8208 C  C   . PHE A 1 1016 ? 56.034 48.813  -1.546  1.00 10.22 ? 1016 PHE A C   1 
ATOM   8209 O  O   . PHE A 1 1016 ? 57.228 48.503  -1.430  1.00 11.69 ? 1016 PHE A O   1 
ATOM   8210 C  CB  . PHE A 1 1016 ? 56.543 50.487  -3.317  1.00 9.17  ? 1016 PHE A CB  1 
ATOM   8211 C  CG  . PHE A 1 1016 ? 56.177 51.125  -4.626  1.00 7.97  ? 1016 PHE A CG  1 
ATOM   8212 C  CD1 . PHE A 1 1016 ? 55.973 52.522  -4.694  1.00 9.39  ? 1016 PHE A CD1 1 
ATOM   8213 C  CD2 . PHE A 1 1016 ? 56.069 50.361  -5.792  1.00 9.26  ? 1016 PHE A CD2 1 
ATOM   8214 C  CE1 . PHE A 1 1016 ? 55.680 53.104  -5.942  1.00 8.78  ? 1016 PHE A CE1 1 
ATOM   8215 C  CE2 . PHE A 1 1016 ? 55.769 50.995  -7.019  1.00 10.20 ? 1016 PHE A CE2 1 
ATOM   8216 C  CZ  . PHE A 1 1016 ? 55.586 52.333  -7.080  1.00 10.03 ? 1016 PHE A CZ  1 
ATOM   8217 N  N   . LEU A 1 1017 ? 55.129 48.584  -0.578  1.00 8.84  ? 1017 LEU A N   1 
ATOM   8218 C  CA  . LEU A 1 1017 ? 55.582 48.203  0.780   1.00 10.57 ? 1017 LEU A CA  1 
ATOM   8219 C  C   . LEU A 1 1017 ? 55.751 46.722  1.011   1.00 11.47 ? 1017 LEU A C   1 
ATOM   8220 O  O   . LEU A 1 1017 ? 56.343 46.372  2.045   1.00 15.17 ? 1017 LEU A O   1 
ATOM   8221 C  CB  . LEU A 1 1017 ? 54.616 48.829  1.806   1.00 9.99  ? 1017 LEU A CB  1 
ATOM   8222 C  CG  . LEU A 1 1017 ? 54.631 50.364  1.749   1.00 9.47  ? 1017 LEU A CG  1 
ATOM   8223 C  CD1 . LEU A 1 1017 ? 53.599 50.882  2.715   1.00 10.92 ? 1017 LEU A CD1 1 
ATOM   8224 C  CD2 . LEU A 1 1017 ? 55.978 50.975  2.098   1.00 12.86 ? 1017 LEU A CD2 1 
ATOM   8225 N  N   . GLN A 1 1018 ? 55.281 45.841  0.152   1.00 10.73 ? 1018 GLN A N   1 
ATOM   8226 C  CA  . GLN A 1 1018 ? 55.462 44.403  0.391   1.00 11.64 ? 1018 GLN A CA  1 
ATOM   8227 C  C   . GLN A 1 1018 ? 55.813 43.745  -0.929  1.00 12.67 ? 1018 GLN A C   1 
ATOM   8228 O  O   . GLN A 1 1018 ? 55.160 44.012  -1.963  1.00 12.19 ? 1018 GLN A O   1 
ATOM   8229 C  CB  . GLN A 1 1018 ? 54.172 43.779  0.952   1.00 12.71 ? 1018 GLN A CB  1 
ATOM   8230 C  CG  . GLN A 1 1018 ? 54.417 42.264  1.268   1.00 17.26 ? 1018 GLN A CG  1 
ATOM   8231 C  CD  . GLN A 1 1018 ? 53.176 41.454  1.547   1.00 26.81 ? 1018 GLN A CD  1 
ATOM   8232 O  OE1 . GLN A 1 1018 ? 53.249 40.202  1.695   1.00 28.04 ? 1018 GLN A OE1 1 
ATOM   8233 N  NE2 . GLN A 1 1018 ? 52.029 42.117  1.599   1.00 21.53 ? 1018 GLN A NE2 1 
ATOM   8234 N  N   . ASN A 1 1019 ? 56.852 42.899  -0.923  1.00 12.72 ? 1019 ASN A N   1 
ATOM   8235 C  CA  . ASN A 1 1019 ? 57.259 42.154  -2.109  1.00 13.47 ? 1019 ASN A CA  1 
ATOM   8236 C  C   . ASN A 1 1019 ? 56.343 40.947  -2.244  1.00 15.65 ? 1019 ASN A C   1 
ATOM   8237 O  O   . ASN A 1 1019 ? 56.167 40.171  -1.263  1.00 18.47 ? 1019 ASN A O   1 
ATOM   8238 C  CB  . ASN A 1 1019 ? 58.715 41.699  -1.982  1.00 15.39 ? 1019 ASN A CB  1 
ATOM   8239 C  CG  . ASN A 1 1019 ? 59.673 42.884  -1.899  1.00 17.99 ? 1019 ASN A CG  1 
ATOM   8240 O  OD1 . ASN A 1 1019 ? 59.422 43.966  -2.508  1.00 17.48 ? 1019 ASN A OD1 1 
ATOM   8241 N  ND2 . ASN A 1 1019 ? 60.795 42.726  -1.156  1.00 22.78 ? 1019 ASN A ND2 1 
ATOM   8242 N  N   . LEU A 1 1020 ? 55.769 40.741  -3.412  1.00 14.75 ? 1020 LEU A N   1 
ATOM   8243 C  CA  . LEU A 1 1020 ? 54.843 39.652  -3.661  1.00 16.85 ? 1020 LEU A CA  1 
ATOM   8244 C  C   . LEU A 1 1020 ? 55.434 38.559  -4.538  1.00 16.51 ? 1020 LEU A C   1 
ATOM   8245 O  O   . LEU A 1 1020 ? 54.991 37.391  -4.434  1.00 18.76 ? 1020 LEU A O   1 
ATOM   8246 C  CB  . LEU A 1 1020 ? 53.553 40.167  -4.332  1.00 17.41 ? 1020 LEU A CB  1 
ATOM   8247 C  CG  . LEU A 1 1020 ? 52.837 41.229  -3.482  1.00 15.43 ? 1020 LEU A CG  1 
ATOM   8248 C  CD1 . LEU A 1 1020 ? 51.675 41.768  -4.311  1.00 19.08 ? 1020 LEU A CD1 1 
ATOM   8249 C  CD2 . LEU A 1 1020 ? 52.289 40.655  -2.157  1.00 19.15 ? 1020 LEU A CD2 1 
ATOM   8250 N  N   . GLU A 1 1021 ? 56.392 38.894  -5.383  1.00 15.61 ? 1021 GLU A N   1 
ATOM   8251 C  CA  . GLU A 1 1021 ? 56.967 37.909  -6.315  1.00 18.66 ? 1021 GLU A CA  1 
ATOM   8252 C  C   . GLU A 1 1021 ? 58.315 38.325  -6.799  1.00 18.66 ? 1021 GLU A C   1 
ATOM   8253 O  O   . GLU A 1 1021 ? 58.537 39.476  -7.168  1.00 18.17 ? 1021 GLU A O   1 
ATOM   8254 C  CB  . GLU A 1 1021 ? 56.027 37.723  -7.516  1.00 21.49 ? 1021 GLU A CB  1 
ATOM   8255 C  CG  . GLU A 1 1021 ? 56.477 36.606  -8.472  1.00 28.47 ? 1021 GLU A CG  1 
ATOM   8256 C  CD  . GLU A 1 1021 ? 55.575 36.452  -9.680  1.00 35.29 ? 1021 GLU A CD  1 
ATOM   8257 O  OE1 . GLU A 1 1021 ? 55.903 35.577  -10.524 1.00 38.86 ? 1021 GLU A OE1 1 
ATOM   8258 O  OE2 . GLU A 1 1021 ? 54.573 37.204  -9.784  1.00 33.44 ? 1021 GLU A OE2 1 
ATOM   8259 N  N   . HIS A 1 1022 ? 59.254 37.381  -6.835  1.00 20.48 ? 1022 HIS A N   1 
ATOM   8260 C  CA  . HIS A 1 1022 ? 60.598 37.636  -7.314  1.00 20.10 ? 1022 HIS A CA  1 
ATOM   8261 C  C   . HIS A 1 1022 ? 60.498 37.217  -8.774  1.00 21.89 ? 1022 HIS A C   1 
ATOM   8262 O  O   . HIS A 1 1022 ? 60.123 36.076  -9.093  1.00 23.51 ? 1022 HIS A O   1 
ATOM   8263 C  CB  . HIS A 1 1022 ? 61.558 36.752  -6.521  1.00 22.96 ? 1022 HIS A CB  1 
ATOM   8264 C  CG  . HIS A 1 1022 ? 62.983 36.944  -6.901  1.00 30.11 ? 1022 HIS A CG  1 
ATOM   8265 N  ND1 . HIS A 1 1022 ? 63.936 35.972  -6.687  1.00 33.98 ? 1022 HIS A ND1 1 
ATOM   8266 C  CD2 . HIS A 1 1022 ? 63.620 37.970  -7.523  1.00 32.75 ? 1022 HIS A CD2 1 
ATOM   8267 C  CE1 . HIS A 1 1022 ? 65.096 36.381  -7.178  1.00 36.05 ? 1022 HIS A CE1 1 
ATOM   8268 N  NE2 . HIS A 1 1022 ? 64.932 37.589  -7.692  1.00 36.36 ? 1022 HIS A NE2 1 
ATOM   8269 N  N   . LEU A 1 1023 ? 60.829 38.119  -9.684  1.00 16.72 ? 1023 LEU A N   1 
ATOM   8270 C  CA  . LEU A 1 1023 ? 60.579 37.860  -11.075 1.00 20.31 ? 1023 LEU A CA  1 
ATOM   8271 C  C   . LEU A 1 1023 ? 61.721 37.294  -11.884 1.00 18.81 ? 1023 LEU A C   1 
ATOM   8272 O  O   . LEU A 1 1023 ? 62.814 37.870  -11.919 1.00 20.01 ? 1023 LEU A O   1 
ATOM   8273 C  CB  . LEU A 1 1023 ? 60.090 39.158  -11.725 1.00 19.59 ? 1023 LEU A CB  1 
ATOM   8274 C  CG  . LEU A 1 1023 ? 58.752 39.637  -11.150 1.00 19.25 ? 1023 LEU A CG  1 
ATOM   8275 C  CD1 . LEU A 1 1023 ? 58.519 41.099  -11.449 1.00 19.98 ? 1023 LEU A CD1 1 
ATOM   8276 C  CD2 . LEU A 1 1023 ? 57.634 38.761  -11.745 1.00 22.43 ? 1023 LEU A CD2 1 
ATOM   8277 N  N   . ASP A 1 1024 ? 61.428 36.222  -12.604 1.00 26.00 ? 1024 ASP A N   1 
ATOM   8278 C  CA  . ASP A 1 1024 ? 62.475 35.617  -13.396 1.00 27.47 ? 1024 ASP A CA  1 
ATOM   8279 C  C   . ASP A 1 1024 ? 62.958 36.449  -14.534 1.00 26.47 ? 1024 ASP A C   1 
ATOM   8280 O  O   . ASP A 1 1024 ? 62.185 37.144  -15.229 1.00 26.46 ? 1024 ASP A O   1 
ATOM   8281 C  CB  . ASP A 1 1024 ? 62.048 34.232  -13.853 1.00 34.70 ? 1024 ASP A CB  1 
ATOM   8282 C  CG  . ASP A 1 1024 ? 62.508 33.175  -12.868 1.00 42.59 ? 1024 ASP A CG  1 
ATOM   8283 O  OD1 . ASP A 1 1024 ? 62.147 33.308  -11.667 1.00 45.55 ? 1024 ASP A OD1 1 
ATOM   8284 O  OD2 . ASP A 1 1024 ? 63.253 32.242  -13.280 1.00 48.48 ? 1024 ASP A OD2 1 
ATOM   8285 N  N   . GLY A 1 1025 ? 64.269 36.395  -14.684 1.00 23.24 ? 1025 GLY A N   1 
ATOM   8286 C  CA  . GLY A 1 1025 ? 64.953 37.111  -15.732 1.00 23.08 ? 1025 GLY A CA  1 
ATOM   8287 C  C   . GLY A 1 1025 ? 64.942 38.594  -15.459 1.00 21.76 ? 1025 GLY A C   1 
ATOM   8288 O  O   . GLY A 1 1025 ? 65.389 39.351  -16.299 1.00 23.22 ? 1025 GLY A O   1 
ATOM   8289 N  N   A MET A 1 1026 ? 64.486 38.998  -14.264 0.50 20.18 ? 1026 MET A N   1 
ATOM   8290 N  N   B MET A 1 1026 ? 64.486 38.998  -14.264 0.50 21.00 ? 1026 MET A N   1 
ATOM   8291 C  CA  A MET A 1 1026 ? 64.396 40.420  -13.907 0.50 20.67 ? 1026 MET A CA  1 
ATOM   8292 C  CA  B MET A 1 1026 ? 64.396 40.420  -13.907 0.50 21.88 ? 1026 MET A CA  1 
ATOM   8293 C  C   A MET A 1 1026 ? 63.444 41.136  -14.855 0.50 18.88 ? 1026 MET A C   1 
ATOM   8294 C  C   B MET A 1 1026 ? 63.444 41.136  -14.855 0.50 19.66 ? 1026 MET A C   1 
ATOM   8295 O  O   A MET A 1 1026 ? 63.622 42.335  -15.100 0.50 21.34 ? 1026 MET A O   1 
ATOM   8296 O  O   B MET A 1 1026 ? 63.622 42.335  -15.100 0.50 21.91 ? 1026 MET A O   1 
ATOM   8297 C  CB  A MET A 1 1026 ? 65.773 41.080  -13.945 0.50 20.48 ? 1026 MET A CB  1 
ATOM   8298 C  CB  B MET A 1 1026 ? 65.773 41.080  -13.945 0.50 23.28 ? 1026 MET A CB  1 
ATOM   8299 C  CG  A MET A 1 1026 ? 66.676 40.438  -12.901 0.50 23.24 ? 1026 MET A CG  1 
ATOM   8300 C  CG  B MET A 1 1026 ? 66.676 40.438  -12.901 0.50 27.58 ? 1026 MET A CG  1 
ATOM   8301 S  SD  A MET A 1 1026 ? 68.380 40.998  -12.915 0.50 23.23 ? 1026 MET A SD  1 
ATOM   8302 S  SD  B MET A 1 1026 ? 67.962 39.371  -13.554 0.50 32.55 ? 1026 MET A SD  1 
ATOM   8303 C  CE  A MET A 1 1026 ? 68.881 40.525  -14.640 0.50 25.58 ? 1026 MET A CE  1 
ATOM   8304 C  CE  B MET A 1 1026 ? 69.090 40.628  -14.326 0.50 31.87 ? 1026 MET A CE  1 
ATOM   8305 N  N   . VAL A 1 1027 ? 62.440 40.425  -15.349 1.00 18.25 ? 1027 VAL A N   1 
ATOM   8306 C  CA  . VAL A 1 1027 ? 61.493 40.986  -16.296 1.00 20.18 ? 1027 VAL A CA  1 
ATOM   8307 C  C   . VAL A 1 1027 ? 60.148 41.202  -15.662 1.00 19.75 ? 1027 VAL A C   1 
ATOM   8308 O  O   . VAL A 1 1027 ? 59.566 40.299  -15.057 1.00 21.19 ? 1027 VAL A O   1 
ATOM   8309 C  CB  . VAL A 1 1027 ? 61.307 40.074  -17.521 1.00 16.80 ? 1027 VAL A CB  1 
ATOM   8310 C  CG1 . VAL A 1 1027 ? 60.190 40.625  -18.423 1.00 19.83 ? 1027 VAL A CG1 1 
ATOM   8311 C  CG2 . VAL A 1 1027 ? 62.600 40.046  -18.331 1.00 21.27 ? 1027 VAL A CG2 1 
ATOM   8312 N  N   . ALA A 1 1028 ? 59.616 42.408  -15.848 1.00 18.84 ? 1028 ALA A N   1 
ATOM   8313 C  CA  . ALA A 1 1028 ? 58.287 42.753  -15.276 1.00 20.52 ? 1028 ALA A CA  1 
ATOM   8314 C  C   . ALA A 1 1028 ? 57.299 42.578  -16.354 1.00 21.25 ? 1028 ALA A C   1 
ATOM   8315 O  O   . ALA A 1 1028 ? 57.317 43.337  -17.350 1.00 22.02 ? 1028 ALA A O   1 
ATOM   8316 C  CB  . ALA A 1 1028 ? 58.256 44.219  -14.804 1.00 19.03 ? 1028 ALA A CB  1 
ATOM   8317 N  N   . PRO A 1 1029 ? 56.400 41.611  -16.200 1.00 18.20 ? 1029 PRO A N   1 
ATOM   8318 C  CA  . PRO A 1 1029 ? 55.378 41.368  -17.232 1.00 20.64 ? 1029 PRO A CA  1 
ATOM   8319 C  C   . PRO A 1 1029 ? 54.385 42.526  -17.352 1.00 19.43 ? 1029 PRO A C   1 
ATOM   8320 O  O   . PRO A 1 1029 ? 54.189 43.293  -16.416 1.00 24.46 ? 1029 PRO A O   1 
ATOM   8321 C  CB  . PRO A 1 1029 ? 54.637 40.134  -16.723 1.00 20.61 ? 1029 PRO A CB  1 
ATOM   8322 C  CG  . PRO A 1 1029 ? 55.535 39.535  -15.650 1.00 23.83 ? 1029 PRO A CG  1 
ATOM   8323 C  CD  . PRO A 1 1029 ? 56.273 40.696  -15.051 1.00 18.80 ? 1029 PRO A CD  1 
ATOM   8324 N  N   . GLU A 1 1030 ? 53.760 42.649  -18.497 1.00 19.73 ? 1030 GLU A N   1 
ATOM   8325 C  CA  . GLU A 1 1030 ? 52.730 43.666  -18.638 1.00 20.34 ? 1030 GLU A CA  1 
ATOM   8326 C  C   . GLU A 1 1030 ? 51.461 43.089  -17.975 1.00 21.31 ? 1030 GLU A C   1 
ATOM   8327 O  O   . GLU A 1 1030 ? 51.293 41.846  -17.754 1.00 24.66 ? 1030 GLU A O   1 
ATOM   8328 C  CB  . GLU A 1 1030 ? 52.478 43.984  -20.122 1.00 21.58 ? 1030 GLU A CB  1 
ATOM   8329 C  CG  . GLU A 1 1030 ? 53.695 44.579  -20.885 1.00 20.04 ? 1030 GLU A CG  1 
ATOM   8330 C  CD  . GLU A 1 1030 ? 53.310 44.953  -22.317 1.00 21.81 ? 1030 GLU A CD  1 
ATOM   8331 O  OE1 . GLU A 1 1030 ? 52.285 44.399  -22.812 1.00 25.71 ? 1030 GLU A OE1 1 
ATOM   8332 O  OE2 . GLU A 1 1030 ? 54.055 45.779  -22.927 1.00 19.46 ? 1030 GLU A OE2 1 
ATOM   8333 N  N   . VAL A 1 1031 ? 50.541 43.971  -17.677 1.00 18.29 ? 1031 VAL A N   1 
ATOM   8334 C  CA  . VAL A 1 1031 ? 49.346 43.554  -16.969 1.00 15.62 ? 1031 VAL A CA  1 
ATOM   8335 C  C   . VAL A 1 1031 ? 48.175 43.361  -17.891 1.00 14.97 ? 1031 VAL A C   1 
ATOM   8336 O  O   . VAL A 1 1031 ? 48.208 43.828  -19.026 1.00 17.00 ? 1031 VAL A O   1 
ATOM   8337 C  CB  . VAL A 1 1031 ? 48.986 44.595  -15.866 1.00 18.81 ? 1031 VAL A CB  1 
ATOM   8338 C  CG1 . VAL A 1 1031 ? 50.166 44.673  -14.887 1.00 22.51 ? 1031 VAL A CG1 1 
ATOM   8339 C  CG2 . VAL A 1 1031 ? 48.653 45.942  -16.438 1.00 18.27 ? 1031 VAL A CG2 1 
ATOM   8340 N  N   . CYS A 1 1032 ? 47.147 42.676  -17.415 1.00 13.30 ? 1032 CYS A N   1 
ATOM   8341 C  CA  . CYS A 1 1032 ? 45.909 42.417  -18.167 1.00 14.28 ? 1032 CYS A CA  1 
ATOM   8342 C  C   . CYS A 1 1032 ? 44.975 43.639  -18.210 1.00 13.01 ? 1032 CYS A C   1 
ATOM   8343 O  O   . CYS A 1 1032 ? 45.079 44.542  -17.401 1.00 11.05 ? 1032 CYS A O   1 
ATOM   8344 C  CB  . CYS A 1 1032 ? 45.110 41.314  -17.462 1.00 13.78 ? 1032 CYS A CB  1 
ATOM   8345 S  SG  . CYS A 1 1032 ? 45.943 39.688  -17.624 1.00 23.13 ? 1032 CYS A SG  1 
ATOM   8346 N  N   . PRO A 1 1033 ? 44.029 43.677  -19.164 1.00 11.39 ? 1033 PRO A N   1 
ATOM   8347 C  CA  . PRO A 1 1033 ? 43.063 44.797  -19.236 1.00 10.59 ? 1033 PRO A CA  1 
ATOM   8348 C  C   . PRO A 1 1033 ? 42.343 44.934  -17.880 1.00 10.04 ? 1033 PRO A C   1 
ATOM   8349 O  O   . PRO A 1 1033 ? 41.825 43.975  -17.288 1.00 10.45 ? 1033 PRO A O   1 
ATOM   8350 C  CB  . PRO A 1 1033 ? 42.060 44.385  -20.358 1.00 11.60 ? 1033 PRO A CB  1 
ATOM   8351 C  CG  . PRO A 1 1033 ? 42.953 43.496  -21.245 1.00 13.46 ? 1033 PRO A CG  1 
ATOM   8352 C  CD  . PRO A 1 1033 ? 43.784 42.680  -20.241 1.00 13.48 ? 1033 PRO A CD  1 
ATOM   8353 N  N   . MET A 1 1034 ? 42.235 46.197  -17.468 1.00 9.50  ? 1034 MET A N   1 
ATOM   8354 C  CA  . MET A 1 1034 ? 41.628 46.667  -16.217 1.00 10.66 ? 1034 MET A CA  1 
ATOM   8355 C  C   . MET A 1 1034 ? 42.432 46.314  -14.969 1.00 11.86 ? 1034 MET A C   1 
ATOM   8356 O  O   . MET A 1 1034 ? 41.969 46.630  -13.870 1.00 16.49 ? 1034 MET A O   1 
ATOM   8357 C  CB  . MET A 1 1034 ? 40.133 46.200  -16.065 1.00 9.35  ? 1034 MET A CB  1 
ATOM   8358 C  CG  . MET A 1 1034 ? 39.269 46.750  -17.203 1.00 11.07 ? 1034 MET A CG  1 
ATOM   8359 S  SD  . MET A 1 1034 ? 39.310 48.538  -17.431 1.00 13.10 ? 1034 MET A SD  1 
ATOM   8360 C  CE  . MET A 1 1034 ? 38.429 49.127  -15.895 1.00 14.65 ? 1034 MET A CE  1 
ATOM   8361 N  N   . GLU A 1 1035 ? 43.623 45.802  -15.134 1.00 9.62  ? 1035 GLU A N   1 
ATOM   8362 C  CA  . GLU A 1 1035 ? 44.466 45.474  -13.972 1.00 10.39 ? 1035 GLU A CA  1 
ATOM   8363 C  C   . GLU A 1 1035 ? 45.544 46.545  -13.791 1.00 9.79  ? 1035 GLU A C   1 
ATOM   8364 O  O   . GLU A 1 1035 ? 45.880 47.299  -14.709 1.00 10.45 ? 1035 GLU A O   1 
ATOM   8365 C  CB  . GLU A 1 1035 ? 45.071 44.083  -14.155 1.00 15.06 ? 1035 GLU A CB  1 
ATOM   8366 C  CG  . GLU A 1 1035 ? 43.963 42.948  -14.059 1.00 22.96 ? 1035 GLU A CG  1 
ATOM   8367 C  CD  . GLU A 1 1035 ? 43.307 42.758  -12.655 1.00 29.17 ? 1035 GLU A CD  1 
ATOM   8368 O  OE1 . GLU A 1 1035 ? 43.311 43.674  -11.819 1.00 32.84 ? 1035 GLU A OE1 1 
ATOM   8369 O  OE2 . GLU A 1 1035 ? 42.742 41.675  -12.394 1.00 34.52 ? 1035 GLU A OE2 1 
ATOM   8370 N  N   . THR A 1 1036 ? 46.029 46.612  -12.555 1.00 9.13  ? 1036 THR A N   1 
ATOM   8371 C  CA  . THR A 1 1036 ? 47.076 47.543  -12.154 1.00 10.24 ? 1036 THR A CA  1 
ATOM   8372 C  C   . THR A 1 1036 ? 48.064 46.724  -11.339 1.00 10.06 ? 1036 THR A C   1 
ATOM   8373 O  O   . THR A 1 1036 ? 47.624 45.944  -10.450 1.00 11.37 ? 1036 THR A O   1 
ATOM   8374 C  CB  . THR A 1 1036 ? 46.482 48.665  -11.278 1.00 10.63 ? 1036 THR A CB  1 
ATOM   8375 O  OG1 . THR A 1 1036 ? 45.417 49.281  -12.000 1.00 11.31 ? 1036 THR A OG1 1 
ATOM   8376 C  CG2 . THR A 1 1036 ? 47.520 49.721  -10.923 1.00 10.97 ? 1036 THR A CG2 1 
ATOM   8377 N  N   . ALA A 1 1037 ? 49.370 46.832  -11.606 1.00 9.12  ? 1037 ALA A N   1 
ATOM   8378 C  CA  . ALA A 1 1037 ? 50.385 46.109  -10.849 1.00 10.39 ? 1037 ALA A CA  1 
ATOM   8379 C  C   . ALA A 1 1037 ? 51.513 47.046  -10.531 1.00 8.54  ? 1037 ALA A C   1 
ATOM   8380 O  O   . ALA A 1 1037 ? 51.634 48.115  -11.156 1.00 11.28 ? 1037 ALA A O   1 
ATOM   8381 C  CB  . ALA A 1 1037 ? 50.935 44.919  -11.693 1.00 13.28 ? 1037 ALA A CB  1 
ATOM   8382 N  N   . ALA A 1 1038 ? 52.305 46.709  -9.531  1.00 8.87  ? 1038 ALA A N   1 
ATOM   8383 C  CA  . ALA A 1 1038 ? 53.447 47.513  -9.175  1.00 9.40  ? 1038 ALA A CA  1 
ATOM   8384 C  C   . ALA A 1 1038 ? 54.667 46.637  -9.210  1.00 9.09  ? 1038 ALA A C   1 
ATOM   8385 O  O   . ALA A 1 1038 ? 54.610 45.443  -8.857  1.00 9.91  ? 1038 ALA A O   1 
ATOM   8386 C  CB  . ALA A 1 1038 ? 53.268 48.133  -7.805  1.00 10.23 ? 1038 ALA A CB  1 
ATOM   8387 N  N   . TYR A 1 1039 ? 55.751 47.270  -9.640  1.00 9.98  ? 1039 TYR A N   1 
ATOM   8388 C  CA  . TYR A 1 1039 ? 57.026 46.562  -9.716  1.00 10.52 ? 1039 TYR A CA  1 
ATOM   8389 C  C   . TYR A 1 1039 ? 58.115 47.431  -9.161  1.00 11.34 ? 1039 TYR A C   1 
ATOM   8390 O  O   . TYR A 1 1039 ? 58.055 48.666  -9.297  1.00 11.98 ? 1039 TYR A O   1 
ATOM   8391 C  CB  . TYR A 1 1039 ? 57.381 46.225  -11.166 1.00 10.75 ? 1039 TYR A CB  1 
ATOM   8392 C  CG  . TYR A 1 1039 ? 56.407 45.347  -11.879 1.00 10.52 ? 1039 TYR A CG  1 
ATOM   8393 C  CD1 . TYR A 1 1039 ? 55.475 45.880  -12.779 1.00 12.81 ? 1039 TYR A CD1 1 
ATOM   8394 C  CD2 . TYR A 1 1039 ? 56.392 43.961  -11.625 1.00 12.29 ? 1039 TYR A CD2 1 
ATOM   8395 C  CE1 . TYR A 1 1039 ? 54.541 45.033  -13.437 1.00 16.09 ? 1039 TYR A CE1 1 
ATOM   8396 C  CE2 . TYR A 1 1039 ? 55.468 43.147  -12.239 1.00 14.34 ? 1039 TYR A CE2 1 
ATOM   8397 C  CZ  . TYR A 1 1039 ? 54.559 43.704  -13.144 1.00 16.24 ? 1039 TYR A CZ  1 
ATOM   8398 O  OH  . TYR A 1 1039 ? 53.710 42.900  -13.858 1.00 19.49 ? 1039 TYR A OH  1 
ATOM   8399 N  N   . VAL A 1 1040 ? 59.129 46.813  -8.548  1.00 11.34 ? 1040 VAL A N   1 
ATOM   8400 C  CA  . VAL A 1 1040 ? 60.280 47.567  -8.071  1.00 11.49 ? 1040 VAL A CA  1 
ATOM   8401 C  C   . VAL A 1 1040 ? 61.538 46.928  -8.677  1.00 12.77 ? 1040 VAL A C   1 
ATOM   8402 O  O   . VAL A 1 1040 ? 61.754 45.686  -8.533  1.00 13.65 ? 1040 VAL A O   1 
ATOM   8403 C  CB  . VAL A 1 1040 ? 60.399 47.545  -6.537  1.00 12.08 ? 1040 VAL A CB  1 
ATOM   8404 C  CG1 . VAL A 1 1040 ? 61.774 48.224  -6.088  1.00 11.88 ? 1040 VAL A CG1 1 
ATOM   8405 C  CG2 . VAL A 1 1040 ? 59.202 48.294  -5.948  1.00 12.34 ? 1040 VAL A CG2 1 
ATOM   8406 N  N   . SER A 1 1041 ? 62.348 47.732  -9.382  1.00 10.73 ? 1041 SER A N   1 
ATOM   8407 C  CA  . SER A 1 1041 ? 63.617 47.233  -9.907  1.00 12.27 ? 1041 SER A CA  1 
ATOM   8408 C  C   . SER A 1 1041 ? 64.729 47.701  -8.959  1.00 12.16 ? 1041 SER A C   1 
ATOM   8409 O  O   . SER A 1 1041 ? 64.705 48.815  -8.425  1.00 12.68 ? 1041 SER A O   1 
ATOM   8410 C  CB  . SER A 1 1041 ? 63.859 47.738  -11.347 1.00 13.44 ? 1041 SER A CB  1 
ATOM   8411 O  OG  . SER A 1 1041 ? 63.890 49.158  -11.413 1.00 13.70 ? 1041 SER A OG  1 
ATOM   8412 N  N   . SER A 1 1042 ? 65.721 46.813  -8.753  1.00 13.21 ? 1042 SER A N   1 
ATOM   8413 C  CA  . SER A 1 1042 ? 66.876 47.103  -7.862  1.00 13.81 ? 1042 SER A CA  1 
ATOM   8414 C  C   . SER A 1 1042 ? 68.107 47.135  -8.773  1.00 12.67 ? 1042 SER A C   1 
ATOM   8415 O  O   . SER A 1 1042 ? 68.188 46.361  -9.728  1.00 16.10 ? 1042 SER A O   1 
ATOM   8416 C  CB  . SER A 1 1042 ? 67.043 45.987  -6.797  1.00 13.03 ? 1042 SER A CB  1 
ATOM   8417 O  OG  . SER A 1 1042 ? 65.906 45.960  -5.935  1.00 15.52 ? 1042 SER A OG  1 
ATOM   8418 N  N   . HIS A 1 1043 ? 69.003 48.087  -8.514  1.00 14.81 ? 1043 HIS A N   1 
ATOM   8419 C  CA  . HIS A 1 1043 ? 70.142 48.347  -9.404  1.00 15.53 ? 1043 HIS A CA  1 
ATOM   8420 C  C   . HIS A 1 1043 ? 71.369 48.474  -8.555  1.00 17.61 ? 1043 HIS A C   1 
ATOM   8421 O  O   . HIS A 1 1043 ? 71.392 49.141  -7.509  1.00 16.36 ? 1043 HIS A O   1 
ATOM   8422 C  CB  . HIS A 1 1043 ? 69.893 49.641  -10.220 1.00 15.94 ? 1043 HIS A CB  1 
ATOM   8423 C  CG  . HIS A 1 1043 ? 68.576 49.652  -10.942 1.00 14.66 ? 1043 HIS A CG  1 
ATOM   8424 N  ND1 . HIS A 1 1043 ? 68.439 49.196  -12.231 1.00 15.42 ? 1043 HIS A ND1 1 
ATOM   8425 C  CD2 . HIS A 1 1043 ? 67.308 49.913  -10.498 1.00 12.84 ? 1043 HIS A CD2 1 
ATOM   8426 C  CE1 . HIS A 1 1043 ? 67.154 49.172  -12.558 1.00 14.33 ? 1043 HIS A CE1 1 
ATOM   8427 N  NE2 . HIS A 1 1043 ? 66.452 49.598  -11.510 1.00 13.44 ? 1043 HIS A NE2 1 
ATOM   8428 N  N   . SER A 1 1044 ? 72.407 47.811  -9.074  1.00 20.57 ? 1044 SER A N   1 
ATOM   8429 C  CA  . SER A 1 1044 ? 73.661 47.738  -8.371  1.00 28.97 ? 1044 SER A CA  1 
ATOM   8430 C  C   . SER A 1 1044 ? 74.568 48.895  -8.663  1.00 32.44 ? 1044 SER A C   1 
ATOM   8431 O  O   . SER A 1 1044 ? 74.182 49.781  -9.460  1.00 33.17 ? 1044 SER A O   1 
ATOM   8432 C  CB  . SER A 1 1044 ? 74.358 46.398  -8.693  1.00 30.39 ? 1044 SER A CB  1 
ATOM   8433 O  OG  . SER A 1 1044 ? 74.175 45.979  -10.052 1.00 35.88 ? 1044 SER A OG  1 
HETATM 8434 C  C1  . NAG B 2 .    ? 57.883 44.388  13.416  1.00 35.99 ? 2001 NAG A C1  1 
HETATM 8435 C  C2  . NAG B 2 .    ? 59.207 44.131  14.180  1.00 41.69 ? 2001 NAG A C2  1 
HETATM 8436 C  C3  . NAG B 2 .    ? 59.855 42.871  13.628  1.00 43.59 ? 2001 NAG A C3  1 
HETATM 8437 C  C4  . NAG B 2 .    ? 58.729 41.898  13.340  1.00 47.87 ? 2001 NAG A C4  1 
HETATM 8438 C  C5  . NAG B 2 .    ? 58.014 42.406  12.069  1.00 48.58 ? 2001 NAG A C5  1 
HETATM 8439 C  C6  . NAG B 2 .    ? 56.602 41.891  11.895  1.00 50.04 ? 2001 NAG A C6  1 
HETATM 8440 C  C7  . NAG B 2 .    ? 61.208 45.311  13.372  1.00 47.97 ? 2001 NAG A C7  1 
HETATM 8441 C  C8  . NAG B 2 .    ? 62.522 45.121  14.115  1.00 50.68 ? 2001 NAG A C8  1 
HETATM 8442 N  N2  . NAG B 2 .    ? 60.097 45.286  14.110  1.00 44.21 ? 2001 NAG A N2  1 
HETATM 8443 O  O3  . NAG B 2 .    ? 60.746 42.332  14.580  1.00 47.79 ? 2001 NAG A O3  1 
HETATM 8444 O  O4  . NAG B 2 .    ? 59.252 40.594  13.159  1.00 50.79 ? 2001 NAG A O4  1 
HETATM 8445 O  O5  . NAG B 2 .    ? 57.933 43.869  12.085  1.00 45.04 ? 2001 NAG A O5  1 
HETATM 8446 O  O6  . NAG B 2 .    ? 55.896 42.695  10.955  1.00 55.38 ? 2001 NAG A O6  1 
HETATM 8447 O  O7  . NAG B 2 .    ? 61.217 45.508  12.147  1.00 49.84 ? 2001 NAG A O7  1 
HETATM 8448 ZN ZN  . ZN  C 3 .    ? 35.068 64.435  8.011   1.00 12.90 ? 2004 ZN  A ZN  1 
HETATM 8449 C  C5  A FMF D 4 .    ? 30.387 66.462  7.234   0.50 16.19 ? 2003 FMF A C5  1 
HETATM 8450 C  C5  B FMF D 4 .    ? 30.348 66.473  7.191   0.50 16.32 ? 2003 FMF A C5  1 
HETATM 8451 C  C2  A FMF D 4 .    ? 32.291 65.904  9.036   0.50 12.74 ? 2003 FMF A C2  1 
HETATM 8452 C  C2  B FMF D 4 .    ? 32.306 65.766  8.963   0.50 14.27 ? 2003 FMF A C2  1 
HETATM 8453 F  F2  A FMF D 4 .    ? 33.352 65.369  9.652   0.50 13.97 ? 2003 FMF A F2  1 
HETATM 8454 F  F2  B FMF D 4 .    ? 33.413 65.321  9.637   0.50 18.12 ? 2003 FMF A F2  1 
HETATM 8455 C  C3  A FMF D 4 .    ? 32.701 66.633  7.663   0.50 11.62 ? 2003 FMF A C3  1 
HETATM 8456 C  C3  B FMF D 4 .    ? 32.727 66.689  7.732   0.50 14.05 ? 2003 FMF A C3  1 
HETATM 8457 O  O3  A FMF D 4 .    ? 33.965 66.010  7.223   0.50 6.65  ? 2003 FMF A O3  1 
HETATM 8458 O  O3  B FMF D 4 .    ? 34.068 66.234  7.244   0.50 21.92 ? 2003 FMF A O3  1 
HETATM 8459 C  C4  A FMF D 4 .    ? 31.679 66.665  6.476   0.50 11.53 ? 2003 FMF A C4  1 
HETATM 8460 C  C4  B FMF D 4 .    ? 31.700 66.677  6.490   0.50 13.59 ? 2003 FMF A C4  1 
HETATM 8461 O  O4  A FMF D 4 .    ? 31.796 67.842  5.833   0.50 11.76 ? 2003 FMF A O4  1 
HETATM 8462 O  O4  B FMF D 4 .    ? 31.788 67.880  5.830   0.50 11.63 ? 2003 FMF A O4  1 
HETATM 8463 C  C6  A FMF D 4 .    ? 29.322 66.462  6.229   0.50 15.87 ? 2003 FMF A C6  1 
HETATM 8464 C  C6  B FMF D 4 .    ? 29.242 66.445  6.179   0.50 15.13 ? 2003 FMF A C6  1 
HETATM 8465 O  O6  A FMF D 4 .    ? 28.057 66.586  6.941   0.50 16.61 ? 2003 FMF A O6  1 
HETATM 8466 O  O6  B FMF D 4 .    ? 27.984 66.614  6.894   0.50 14.91 ? 2003 FMF A O6  1 
HETATM 8467 O  O   A FMF D 4 .    ? 30.367 65.195  7.850   0.50 13.04 ? 2003 FMF A O   1 
HETATM 8468 O  O   B FMF D 4 .    ? 30.306 65.208  7.877   0.50 17.09 ? 2003 FMF A O   1 
HETATM 8469 C  C1  A FMF D 4 .    ? 31.196 64.882  8.897   0.50 14.58 ? 2003 FMF A C1  1 
HETATM 8470 C  C1  B FMF D 4 .    ? 31.525 64.607  8.282   0.50 14.23 ? 2003 FMF A C1  1 
HETATM 8471 C  C1  . MPD E 5 .    ? 14.814 61.183  10.239  1.00 14.50 ? 2002 MPD A C1  1 
HETATM 8472 C  C2  . MPD E 5 .    ? 16.244 61.222  10.572  1.00 16.86 ? 2002 MPD A C2  1 
HETATM 8473 O  O2  . MPD E 5 .    ? 16.920 60.205  9.767   1.00 25.44 ? 2002 MPD A O2  1 
HETATM 8474 C  CM  . MPD E 5 .    ? 16.838 62.588  10.203  1.00 22.82 ? 2002 MPD A CM  1 
HETATM 8475 C  C3  . MPD E 5 .    ? 16.315 60.893  12.091  1.00 17.78 ? 2002 MPD A C3  1 
HETATM 8476 C  C4  . MPD E 5 .    ? 17.652 60.690  12.736  1.00 17.64 ? 2002 MPD A C4  1 
HETATM 8477 O  O4  . MPD E 5 .    ? 17.551 59.745  13.827  1.00 15.40 ? 2002 MPD A O4  1 
HETATM 8478 C  C5  . MPD E 5 .    ? 18.180 61.962  13.431  1.00 21.37 ? 2002 MPD A C5  1 
HETATM 8479 O  O   . HOH F 6 .    ? 42.173 63.584  -7.206  1.00 7.46  ? 2005 HOH A O   1 
HETATM 8480 O  O   . HOH F 6 .    ? 53.763 64.906  -19.934 1.00 9.42  ? 2006 HOH A O   1 
HETATM 8481 O  O   . HOH F 6 .    ? 39.369 62.970  -19.199 1.00 8.62  ? 2007 HOH A O   1 
HETATM 8482 O  O   . HOH F 6 .    ? 52.343 54.167  -4.872  1.00 8.71  ? 2008 HOH A O   1 
HETATM 8483 O  O   . HOH F 6 .    ? 56.303 53.474  -0.670  1.00 8.54  ? 2009 HOH A O   1 
HETATM 8484 O  O   . HOH F 6 .    ? 31.395 50.002  -24.091 1.00 11.28 ? 2010 HOH A O   1 
HETATM 8485 O  O   . HOH F 6 .    ? 49.998 48.517  1.366   1.00 9.68  ? 2011 HOH A O   1 
HETATM 8486 O  O   . HOH F 6 .    ? 36.864 57.760  13.456  1.00 10.40 ? 2012 HOH A O   1 
HETATM 8487 O  O   . HOH F 6 .    ? 26.916 69.030  -9.265  1.00 9.62  ? 2013 HOH A O   1 
HETATM 8488 O  O   . HOH F 6 .    ? 39.336 64.906  -14.792 1.00 11.61 ? 2014 HOH A O   1 
HETATM 8489 O  O   . HOH F 6 .    ? 34.371 58.677  -8.793  1.00 8.20  ? 2015 HOH A O   1 
HETATM 8490 O  O   . HOH F 6 .    ? 61.229 59.767  -8.291  1.00 8.76  ? 2016 HOH A O   1 
HETATM 8491 O  O   . HOH F 6 .    ? 36.708 72.726  0.250   1.00 9.51  ? 2017 HOH A O   1 
HETATM 8492 O  O   . HOH F 6 .    ? 31.845 47.114  -8.099  1.00 8.97  ? 2018 HOH A O   1 
HETATM 8493 O  O   . HOH F 6 .    ? 30.217 55.848  17.308  1.00 9.83  ? 2019 HOH A O   1 
HETATM 8494 O  O   . HOH F 6 .    ? 26.189 49.701  -13.713 1.00 9.22  ? 2020 HOH A O   1 
HETATM 8495 O  O   . HOH F 6 .    ? 37.719 52.213  -21.185 1.00 11.76 ? 2021 HOH A O   1 
HETATM 8496 O  O   . HOH F 6 .    ? 33.208 62.871  0.073   1.00 7.88  ? 2022 HOH A O   1 
HETATM 8497 O  O   . HOH F 6 .    ? 24.823 53.006  -11.755 1.00 9.73  ? 2023 HOH A O   1 
HETATM 8498 O  O   . HOH F 6 .    ? 63.311 61.406  -7.642  1.00 10.27 ? 2024 HOH A O   1 
HETATM 8499 O  O   . HOH F 6 .    ? 41.321 59.174  13.379  1.00 12.67 ? 2025 HOH A O   1 
HETATM 8500 O  O   . HOH F 6 .    ? 47.419 55.813  -15.450 1.00 16.20 ? 2026 HOH A O   1 
HETATM 8501 O  O   . HOH F 6 .    ? 56.525 55.814  -2.151  1.00 10.95 ? 2027 HOH A O   1 
HETATM 8502 O  O   . HOH F 6 .    ? 67.689 60.741  -5.733  1.00 13.19 ? 2028 HOH A O   1 
HETATM 8503 O  O   . HOH F 6 .    ? 26.371 48.989  -10.975 1.00 10.24 ? 2029 HOH A O   1 
HETATM 8504 O  O   . HOH F 6 .    ? 65.817 60.377  -7.773  1.00 10.99 ? 2030 HOH A O   1 
HETATM 8505 O  O   . HOH F 6 .    ? 32.694 60.203  -1.805  1.00 9.01  ? 2031 HOH A O   1 
HETATM 8506 O  O   . HOH F 6 .    ? 20.051 54.787  16.222  1.00 11.61 ? 2032 HOH A O   1 
HETATM 8507 O  O   . HOH F 6 .    ? 23.841 55.604  -23.445 1.00 10.27 ? 2033 HOH A O   1 
HETATM 8508 O  O   . HOH F 6 .    ? 39.390 57.490  14.843  1.00 9.89  ? 2034 HOH A O   1 
HETATM 8509 O  O   . HOH F 6 .    ? 20.401 58.863  -22.028 1.00 10.82 ? 2035 HOH A O   1 
HETATM 8510 O  O   . HOH F 6 .    ? 27.960 61.034  19.576  1.00 11.54 ? 2036 HOH A O   1 
HETATM 8511 O  O   . HOH F 6 .    ? 34.204 56.406  -26.378 1.00 10.77 ? 2037 HOH A O   1 
HETATM 8512 O  O   . HOH F 6 .    ? 26.344 40.153  7.949   1.00 11.82 ? 2038 HOH A O   1 
HETATM 8513 O  O   . HOH F 6 .    ? 63.962 50.189  -14.089 1.00 13.38 ? 2039 HOH A O   1 
HETATM 8514 O  O   . HOH F 6 .    ? 37.616 57.135  1.767   1.00 9.89  ? 2040 HOH A O   1 
HETATM 8515 O  O   . HOH F 6 .    ? 24.097 42.038  6.897   1.00 10.97 ? 2041 HOH A O   1 
HETATM 8516 O  O   . HOH F 6 .    ? 31.895 65.640  19.074  1.00 16.95 ? 2042 HOH A O   1 
HETATM 8517 O  O   . HOH F 6 .    ? 51.603 56.759  -5.636  1.00 9.80  ? 2043 HOH A O   1 
HETATM 8518 O  O   . HOH F 6 .    ? 20.111 56.086  7.133   1.00 13.30 ? 2044 HOH A O   1 
HETATM 8519 O  O   . HOH F 6 .    ? 28.326 43.951  13.224  1.00 10.91 ? 2045 HOH A O   1 
HETATM 8520 O  O   . HOH F 6 .    ? 30.299 58.559  -11.820 1.00 8.79  ? 2046 HOH A O   1 
HETATM 8521 O  O   . HOH F 6 .    ? 65.062 59.324  -3.661  1.00 14.54 ? 2047 HOH A O   1 
HETATM 8522 O  O   . HOH F 6 .    ? 46.584 67.752  -15.626 1.00 14.89 ? 2048 HOH A O   1 
HETATM 8523 O  O   . HOH F 6 .    ? 60.933 58.351  -2.886  1.00 11.81 ? 2049 HOH A O   1 
HETATM 8524 O  O   . HOH F 6 .    ? 60.693 62.290  -1.304  1.00 12.26 ? 2050 HOH A O   1 
HETATM 8525 O  O   . HOH F 6 .    ? 53.850 59.948  -9.454  1.00 12.50 ? 2051 HOH A O   1 
HETATM 8526 O  O   . HOH F 6 .    ? 18.699 51.138  -12.464 1.00 12.55 ? 2052 HOH A O   1 
HETATM 8527 O  O   . HOH F 6 .    ? 28.945 42.823  -11.940 1.00 10.83 ? 2053 HOH A O   1 
HETATM 8528 O  O   . HOH F 6 .    ? 34.656 79.253  -9.168  1.00 12.56 ? 2054 HOH A O   1 
HETATM 8529 O  O   . HOH F 6 .    ? 21.621 58.060  -7.821  1.00 10.36 ? 2055 HOH A O   1 
HETATM 8530 O  O   . HOH F 6 .    ? 37.180 71.994  -4.577  1.00 8.90  ? 2056 HOH A O   1 
HETATM 8531 O  O   . HOH F 6 .    ? 55.741 59.434  -11.523 1.00 9.19  ? 2057 HOH A O   1 
HETATM 8532 O  O   . HOH F 6 .    ? 36.828 45.050  -5.483  1.00 10.05 ? 2058 HOH A O   1 
HETATM 8533 O  O   . HOH F 6 .    ? 51.401 53.353  -24.010 1.00 12.39 ? 2059 HOH A O   1 
HETATM 8534 O  O   . HOH F 6 .    ? 35.251 50.659  -17.604 1.00 15.17 ? 2060 HOH A O   1 
HETATM 8535 O  O   . HOH F 6 .    ? 60.741 54.835  -0.418  1.00 13.73 ? 2061 HOH A O   1 
HETATM 8536 O  O   . HOH F 6 .    ? 43.104 56.882  6.126   1.00 11.20 ? 2062 HOH A O   1 
HETATM 8537 O  O   . HOH F 6 .    ? 47.969 59.356  -25.762 1.00 12.76 ? 2063 HOH A O   1 
HETATM 8538 O  O   . HOH F 6 .    ? 37.967 73.421  -2.242  1.00 11.25 ? 2064 HOH A O   1 
HETATM 8539 O  O   . HOH F 6 .    ? 19.368 55.323  11.569  1.00 12.73 ? 2065 HOH A O   1 
HETATM 8540 O  O   . HOH F 6 .    ? 25.933 39.813  5.248   1.00 10.77 ? 2066 HOH A O   1 
HETATM 8541 O  O   . HOH F 6 .    ? 23.423 54.071  -3.626  1.00 14.31 ? 2067 HOH A O   1 
HETATM 8542 O  O   . HOH F 6 .    ? 34.359 52.520  -0.955  1.00 9.18  ? 2068 HOH A O   1 
HETATM 8543 O  O   . HOH F 6 .    ? 51.166 44.326  -8.026  1.00 11.43 ? 2069 HOH A O   1 
HETATM 8544 O  O   . HOH F 6 .    ? 16.487 49.086  24.116  1.00 15.57 ? 2070 HOH A O   1 
HETATM 8545 O  O   . HOH F 6 .    ? 19.390 53.576  8.176   1.00 11.54 ? 2071 HOH A O   1 
HETATM 8546 O  O   . HOH F 6 .    ? 11.811 51.531  14.278  1.00 15.61 ? 2072 HOH A O   1 
HETATM 8547 O  O   . HOH F 6 .    ? 17.056 56.296  10.272  1.00 13.34 ? 2073 HOH A O   1 
HETATM 8548 O  O   . HOH F 6 .    ? 68.186 65.664  -3.488  1.00 15.22 ? 2074 HOH A O   1 
HETATM 8549 O  O   . HOH F 6 .    ? 22.921 53.134  -24.468 1.00 13.29 ? 2075 HOH A O   1 
HETATM 8550 O  O   . HOH F 6 .    ? 52.301 50.637  6.357   1.00 11.83 ? 2076 HOH A O   1 
HETATM 8551 O  O   . HOH F 6 .    ? 17.652 52.807  6.307   1.00 11.37 ? 2077 HOH A O   1 
HETATM 8552 O  O   . HOH F 6 .    ? 69.020 58.325  -5.135  1.00 14.03 ? 2078 HOH A O   1 
HETATM 8553 O  O   . HOH F 6 .    ? 33.599 48.223  -10.150 1.00 9.42  ? 2079 HOH A O   1 
HETATM 8554 O  O   . HOH F 6 .    ? 26.816 41.626  -13.224 1.00 13.33 ? 2080 HOH A O   1 
HETATM 8555 O  O   . HOH F 6 .    ? 26.862 60.992  -3.344  1.00 9.69  ? 2081 HOH A O   1 
HETATM 8556 O  O   . HOH F 6 .    ? 49.749 62.356  -8.696  1.00 11.11 ? 2082 HOH A O   1 
HETATM 8557 O  O   . HOH F 6 .    ? 41.195 52.432  -16.984 1.00 12.69 ? 2083 HOH A O   1 
HETATM 8558 O  O   . HOH F 6 .    ? 31.505 76.921  -6.374  1.00 11.77 ? 2084 HOH A O   1 
HETATM 8559 O  O   . HOH F 6 .    ? 43.511 68.351  -25.078 1.00 14.91 ? 2085 HOH A O   1 
HETATM 8560 O  O   . HOH F 6 .    ? 32.880 81.192  -11.746 1.00 11.10 ? 2086 HOH A O   1 
HETATM 8561 O  O   . HOH F 6 .    ? 20.628 66.272  -19.669 1.00 13.21 ? 2087 HOH A O   1 
HETATM 8562 O  O   . HOH F 6 .    ? 40.559 62.885  6.067   1.00 9.43  ? 2088 HOH A O   1 
HETATM 8563 O  O   . HOH F 6 .    ? 42.310 47.368  -24.608 1.00 13.85 ? 2089 HOH A O   1 
HETATM 8564 O  O   . HOH F 6 .    ? 44.642 41.911  -0.486  1.00 14.76 ? 2090 HOH A O   1 
HETATM 8565 O  O   . HOH F 6 .    ? 38.789 55.241  -31.805 1.00 16.24 ? 2091 HOH A O   1 
HETATM 8566 O  O   . HOH F 6 .    ? 22.397 54.465  -12.039 1.00 11.56 ? 2092 HOH A O   1 
HETATM 8567 O  O   . HOH F 6 .    ? 48.395 89.325  -30.824 1.00 16.04 ? 2093 HOH A O   1 
HETATM 8568 O  O   . HOH F 6 .    ? 36.804 51.788  3.810   1.00 12.11 ? 2094 HOH A O   1 
HETATM 8569 O  O   . HOH F 6 .    ? 38.990 62.286  8.285   1.00 11.58 ? 2095 HOH A O   1 
HETATM 8570 O  O   . HOH F 6 .    ? 47.615 46.036  3.680   1.00 10.52 ? 2096 HOH A O   1 
HETATM 8571 O  O   . HOH F 6 .    ? 33.651 57.124  -36.014 1.00 17.35 ? 2097 HOH A O   1 
HETATM 8572 O  O   . HOH F 6 .    ? 32.469 77.752  -29.724 1.00 13.89 ? 2098 HOH A O   1 
HETATM 8573 O  O   . HOH F 6 .    ? 39.327 39.014  17.362  1.00 17.18 ? 2099 HOH A O   1 
HETATM 8574 O  O   . HOH F 6 .    ? 36.060 53.216  1.343   1.00 11.90 ? 2100 HOH A O   1 
HETATM 8575 O  O   . HOH F 6 .    ? 14.466 60.134  5.188   1.00 13.72 ? 2101 HOH A O   1 
HETATM 8576 O  O   . HOH F 6 .    ? 21.719 57.214  5.013   1.00 12.26 ? 2102 HOH A O   1 
HETATM 8577 O  O   . HOH F 6 .    ? 43.161 48.136  11.233  1.00 14.30 ? 2103 HOH A O   1 
HETATM 8578 O  O   . HOH F 6 .    ? 26.193 72.813  5.606   1.00 13.22 ? 2104 HOH A O   1 
HETATM 8579 O  O   . HOH F 6 .    ? 27.590 48.548  -21.697 1.00 17.03 ? 2105 HOH A O   1 
HETATM 8580 O  O   . HOH F 6 .    ? 33.486 78.737  -5.161  1.00 12.33 ? 2106 HOH A O   1 
HETATM 8581 O  O   . HOH F 6 .    ? 50.163 59.592  -11.581 1.00 11.87 ? 2107 HOH A O   1 
HETATM 8582 O  O   . HOH F 6 .    ? 25.624 51.321  -9.524  1.00 12.69 ? 2108 HOH A O   1 
HETATM 8583 O  O   . HOH F 6 .    ? 40.270 56.358  5.793   1.00 12.42 ? 2109 HOH A O   1 
HETATM 8584 O  O   . HOH F 6 .    ? 14.150 59.815  -3.429  1.00 16.19 ? 2110 HOH A O   1 
HETATM 8585 O  O   . HOH F 6 .    ? 19.765 53.642  -11.802 1.00 11.56 ? 2111 HOH A O   1 
HETATM 8586 O  O   . HOH F 6 .    ? 26.352 63.774  17.138  1.00 21.00 ? 2112 HOH A O   1 
HETATM 8587 O  O   . HOH F 6 .    ? 19.914 57.490  -11.803 1.00 15.19 ? 2113 HOH A O   1 
HETATM 8588 O  O   . HOH F 6 .    ? 47.153 48.601  11.559  1.00 17.34 ? 2114 HOH A O   1 
HETATM 8589 O  O   . HOH F 6 .    ? 67.975 81.769  -25.784 1.00 14.03 ? 2115 HOH A O   1 
HETATM 8590 O  O   . HOH F 6 .    ? 23.083 51.867  -8.581  1.00 17.31 ? 2116 HOH A O   1 
HETATM 8591 O  O   . HOH F 6 .    ? 46.706 70.392  -36.825 1.00 16.54 ? 2117 HOH A O   1 
HETATM 8592 O  O   . HOH F 6 .    ? 20.687 57.501  -5.280  1.00 11.18 ? 2118 HOH A O   1 
HETATM 8593 O  O   . HOH F 6 .    ? 18.062 60.703  24.500  1.00 17.52 ? 2119 HOH A O   1 
HETATM 8594 O  O   . HOH F 6 .    ? 41.370 68.472  -32.648 1.00 15.13 ? 2120 HOH A O   1 
HETATM 8595 O  O   . HOH F 6 .    ? 38.419 40.147  1.732   1.00 12.87 ? 2121 HOH A O   1 
HETATM 8596 O  O   . HOH F 6 .    ? 23.899 58.233  6.317   1.00 12.57 ? 2122 HOH A O   1 
HETATM 8597 O  O   . HOH F 6 .    ? 18.243 59.859  -20.089 1.00 17.96 ? 2123 HOH A O   1 
HETATM 8598 O  O   . HOH F 6 .    ? 41.409 77.676  -14.163 1.00 13.30 ? 2124 HOH A O   1 
HETATM 8599 O  O   . HOH F 6 .    ? 52.945 58.994  -1.789  1.00 13.96 ? 2125 HOH A O   1 
HETATM 8600 O  O   . HOH F 6 .    ? 48.065 49.640  13.839  1.00 12.78 ? 2126 HOH A O   1 
HETATM 8601 O  O   . HOH F 6 .    ? 35.243 43.672  28.754  1.00 14.59 ? 2127 HOH A O   1 
HETATM 8602 O  O   . HOH F 6 .    ? 59.651 60.678  -6.273  1.00 13.58 ? 2128 HOH A O   1 
HETATM 8603 O  O   . HOH F 6 .    ? 53.787 72.723  -19.312 1.00 14.60 ? 2129 HOH A O   1 
HETATM 8604 O  O   . HOH F 6 .    ? 39.830 54.021  -20.845 1.00 15.37 ? 2130 HOH A O   1 
HETATM 8605 O  O   . HOH F 6 .    ? 33.369 36.741  -4.414  1.00 16.07 ? 2131 HOH A O   1 
HETATM 8606 O  O   . HOH F 6 .    ? 14.476 63.988  -16.388 1.00 16.82 ? 2132 HOH A O   1 
HETATM 8607 O  O   . HOH F 6 .    ? 47.572 43.081  -2.408  1.00 14.91 ? 2133 HOH A O   1 
HETATM 8608 O  O   . HOH F 6 .    ? 47.011 55.871  -25.557 1.00 14.23 ? 2134 HOH A O   1 
HETATM 8609 O  O   . HOH F 6 .    ? 32.190 58.691  -28.543 1.00 13.97 ? 2135 HOH A O   1 
HETATM 8610 O  O   . HOH F 6 .    ? 49.358 50.105  28.294  1.00 15.86 ? 2136 HOH A O   1 
HETATM 8611 O  O   . HOH F 6 .    ? 26.363 37.413  29.432  1.00 18.76 ? 2137 HOH A O   1 
HETATM 8612 O  O   . HOH F 6 .    ? 52.020 46.615  1.305   1.00 11.27 ? 2138 HOH A O   1 
HETATM 8613 O  O   . HOH F 6 .    ? 41.794 58.816  -16.066 1.00 15.21 ? 2139 HOH A O   1 
HETATM 8614 O  O   . HOH F 6 .    ? 13.868 54.214  4.373   1.00 15.76 ? 2140 HOH A O   1 
HETATM 8615 O  O   . HOH F 6 .    ? 67.954 79.004  -25.408 1.00 13.22 ? 2141 HOH A O   1 
HETATM 8616 O  O   . HOH F 6 .    ? 42.281 75.382  -16.035 1.00 13.56 ? 2142 HOH A O   1 
HETATM 8617 O  O   . HOH F 6 .    ? 23.076 56.098  30.923  1.00 16.50 ? 2143 HOH A O   1 
HETATM 8618 O  O   . HOH F 6 .    ? 57.135 61.121  1.552   1.00 15.83 ? 2144 HOH A O   1 
HETATM 8619 O  O   . HOH F 6 .    ? 20.160 74.447  -6.840  1.00 13.45 ? 2145 HOH A O   1 
HETATM 8620 O  O   . HOH F 6 .    ? 13.480 53.620  1.792   1.00 18.02 ? 2146 HOH A O   1 
HETATM 8621 O  O   . HOH F 6 .    ? 34.382 34.443  16.228  1.00 20.54 ? 2147 HOH A O   1 
HETATM 8622 O  O   . HOH F 6 .    ? 34.000 64.603  -32.368 1.00 13.98 ? 2148 HOH A O   1 
HETATM 8623 O  O   . HOH F 6 .    ? 13.983 49.115  15.363  1.00 16.16 ? 2149 HOH A O   1 
HETATM 8624 O  O   . HOH F 6 .    ? 30.404 35.228  -12.415 1.00 23.12 ? 2150 HOH A O   1 
HETATM 8625 O  O   . HOH F 6 .    ? 18.330 55.005  14.185  1.00 13.04 ? 2151 HOH A O   1 
HETATM 8626 O  O   . HOH F 6 .    ? 15.476 60.416  15.486  1.00 15.84 ? 2152 HOH A O   1 
HETATM 8627 O  O   . HOH F 6 .    ? 16.938 74.709  -3.014  1.00 14.57 ? 2153 HOH A O   1 
HETATM 8628 O  O   . HOH F 6 .    ? 56.681 46.253  -17.421 1.00 16.17 ? 2154 HOH A O   1 
HETATM 8629 O  O   . HOH F 6 .    ? 45.808 60.015  -18.305 1.00 13.41 ? 2155 HOH A O   1 
HETATM 8630 O  O   . HOH F 6 .    ? 28.108 84.680  -35.558 1.00 16.18 ? 2156 HOH A O   1 
HETATM 8631 O  O   . HOH F 6 .    ? 73.209 65.107  -7.870  1.00 22.40 ? 2157 HOH A O   1 
HETATM 8632 O  O   . HOH F 6 .    ? 74.083 65.991  -17.686 1.00 16.44 ? 2158 HOH A O   1 
HETATM 8633 O  O   . HOH F 6 .    ? 59.458 50.042  -0.687  1.00 15.44 ? 2159 HOH A O   1 
HETATM 8634 O  O   . HOH F 6 .    ? 23.260 78.494  -24.875 1.00 17.26 ? 2160 HOH A O   1 
HETATM 8635 O  O   . HOH F 6 .    ? 14.367 54.482  -16.172 1.00 18.61 ? 2161 HOH A O   1 
HETATM 8636 O  O   . HOH F 6 .    ? 43.696 73.247  5.800   1.00 12.12 ? 2162 HOH A O   1 
HETATM 8637 O  O   . HOH F 6 .    ? 11.835 55.117  -12.425 1.00 18.67 ? 2163 HOH A O   1 
HETATM 8638 O  O   . HOH F 6 .    ? 63.727 44.698  -6.839  1.00 16.31 ? 2164 HOH A O   1 
HETATM 8639 O  O   . HOH F 6 .    ? 24.790 51.162  -24.103 1.00 13.78 ? 2165 HOH A O   1 
HETATM 8640 O  O   . HOH F 6 .    ? 35.685 45.295  -27.476 1.00 16.71 ? 2166 HOH A O   1 
HETATM 8641 O  O   . HOH F 6 .    ? 28.740 49.786  -24.480 1.00 16.38 ? 2167 HOH A O   1 
HETATM 8642 O  O   . HOH F 6 .    ? 55.056 81.158  -23.692 1.00 14.50 ? 2168 HOH A O   1 
HETATM 8643 O  O   . HOH F 6 .    ? 24.211 63.559  7.509   1.00 12.10 ? 2169 HOH A O   1 
HETATM 8644 O  O   . HOH F 6 .    ? 49.925 57.711  -7.617  1.00 11.42 ? 2170 HOH A O   1 
HETATM 8645 O  O   . HOH F 6 .    ? 46.226 71.014  0.045   1.00 15.59 ? 2171 HOH A O   1 
HETATM 8646 O  O   . HOH F 6 .    ? 24.458 55.781  -1.743  1.00 12.55 ? 2172 HOH A O   1 
HETATM 8647 O  O   . HOH F 6 .    ? 28.675 41.351  -21.721 1.00 14.03 ? 2173 HOH A O   1 
HETATM 8648 O  O   . HOH F 6 .    ? 37.147 45.613  27.513  1.00 13.78 ? 2174 HOH A O   1 
HETATM 8649 O  O   . HOH F 6 .    ? 41.671 41.274  -17.631 1.00 18.46 ? 2175 HOH A O   1 
HETATM 8650 O  O   . HOH F 6 .    ? 40.357 62.574  -32.063 1.00 17.50 ? 2176 HOH A O   1 
HETATM 8651 O  O   . HOH F 6 .    ? 49.354 59.365  -28.771 1.00 18.47 ? 2177 HOH A O   1 
HETATM 8652 O  O   . HOH F 6 .    ? 64.502 39.391  -10.429 1.00 23.13 ? 2178 HOH A O   1 
HETATM 8653 O  O   . HOH F 6 .    ? 19.250 72.560  2.933   1.00 16.77 ? 2179 HOH A O   1 
HETATM 8654 O  O   . HOH F 6 .    ? 17.143 70.432  -16.363 1.00 13.29 ? 2180 HOH A O   1 
HETATM 8655 O  O   . HOH F 6 .    ? 9.390  52.497  16.849  1.00 19.88 ? 2181 HOH A O   1 
HETATM 8656 O  O   . HOH F 6 .    ? 54.039 71.369  -36.966 1.00 13.14 ? 2182 HOH A O   1 
HETATM 8657 O  O   . HOH F 6 .    ? 51.015 70.951  -23.641 1.00 17.13 ? 2183 HOH A O   1 
HETATM 8658 O  O   . HOH F 6 .    ? 49.523 44.240  4.437   1.00 14.21 ? 2184 HOH A O   1 
HETATM 8659 O  O   . HOH F 6 .    ? 59.521 68.315  2.468   1.00 25.12 ? 2185 HOH A O   1 
HETATM 8660 O  O   . HOH F 6 .    ? 25.529 53.875  11.050  1.00 15.59 ? 2186 HOH A O   1 
HETATM 8661 O  O   . HOH F 6 .    ? 69.339 61.475  -2.456  1.00 15.40 ? 2187 HOH A O   1 
HETATM 8662 O  O   . HOH F 6 .    ? 58.480 77.351  -38.608 1.00 13.99 ? 2188 HOH A O   1 
HETATM 8663 O  O   . HOH F 6 .    ? 44.544 46.119  10.038  1.00 15.74 ? 2189 HOH A O   1 
HETATM 8664 O  O   . HOH F 6 .    ? 46.700 57.408  -18.806 1.00 13.56 ? 2190 HOH A O   1 
HETATM 8665 O  O   . HOH F 6 .    ? 33.689 83.691  -10.453 1.00 15.12 ? 2191 HOH A O   1 
HETATM 8666 O  O   . HOH F 6 .    ? 47.246 68.615  -30.369 1.00 15.78 ? 2192 HOH A O   1 
HETATM 8667 O  O   . HOH F 6 .    ? 44.626 56.148  -15.407 1.00 16.39 ? 2193 HOH A O   1 
HETATM 8668 O  O   . HOH F 6 .    ? 13.207 66.924  -4.806  1.00 15.32 ? 2194 HOH A O   1 
HETATM 8669 O  O   . HOH F 6 .    ? 24.530 39.208  -11.554 1.00 22.02 ? 2195 HOH A O   1 
HETATM 8670 O  O   . HOH F 6 .    ? 41.716 61.302  -29.837 1.00 16.24 ? 2196 HOH A O   1 
HETATM 8671 O  O   . HOH F 6 .    ? 27.279 41.436  13.319  1.00 14.31 ? 2197 HOH A O   1 
HETATM 8672 O  O   . HOH F 6 .    ? 42.193 87.874  -41.013 1.00 16.79 ? 2198 HOH A O   1 
HETATM 8673 O  O   . HOH F 6 .    ? 70.190 69.982  -12.742 1.00 14.25 ? 2199 HOH A O   1 
HETATM 8674 O  O   . HOH F 6 .    ? 64.419 77.984  -35.421 1.00 14.54 ? 2200 HOH A O   1 
HETATM 8675 O  O   . HOH F 6 .    ? 20.834 65.480  7.789   1.00 15.98 ? 2201 HOH A O   1 
HETATM 8676 O  O   . HOH F 6 .    ? 11.446 61.414  -18.372 1.00 21.01 ? 2202 HOH A O   1 
HETATM 8677 O  O   . HOH F 6 .    ? 24.720 70.659  -8.758  1.00 12.83 ? 2203 HOH A O   1 
HETATM 8678 O  O   . HOH F 6 .    ? 25.032 40.028  14.230  1.00 15.97 ? 2204 HOH A O   1 
HETATM 8679 O  O   . HOH F 6 .    ? 22.655 63.403  -33.190 1.00 21.75 ? 2205 HOH A O   1 
HETATM 8680 O  O   . HOH F 6 .    ? 41.831 43.302  8.075   1.00 18.33 ? 2206 HOH A O   1 
HETATM 8681 O  O   . HOH F 6 .    ? 20.925 51.906  47.594  1.00 17.11 ? 2207 HOH A O   1 
HETATM 8682 O  O   . HOH F 6 .    ? 41.400 50.462  33.324  1.00 27.50 ? 2208 HOH A O   1 
HETATM 8683 O  O   . HOH F 6 .    ? 46.135 52.822  -19.188 1.00 19.07 ? 2209 HOH A O   1 
HETATM 8684 O  O   . HOH F 6 .    ? 51.568 76.434  -41.091 1.00 27.79 ? 2210 HOH A O   1 
HETATM 8685 O  O   . HOH F 6 .    ? 25.665 86.242  -31.985 1.00 18.24 ? 2211 HOH A O   1 
HETATM 8686 O  O   . HOH F 6 .    ? 12.521 56.361  5.349   1.00 16.31 ? 2212 HOH A O   1 
HETATM 8687 O  O   . HOH F 6 .    ? 22.524 56.862  -34.237 1.00 19.20 ? 2213 HOH A O   1 
HETATM 8688 O  O   . HOH F 6 .    ? 43.933 72.605  -42.009 1.00 21.35 ? 2214 HOH A O   1 
HETATM 8689 O  O   . HOH F 6 .    ? 44.654 58.811  -16.007 1.00 15.07 ? 2215 HOH A O   1 
HETATM 8690 O  O   . HOH F 6 .    ? 31.489 81.865  0.467   1.00 18.01 ? 2216 HOH A O   1 
HETATM 8691 O  O   . HOH F 6 .    ? 52.226 56.406  -30.424 1.00 21.23 ? 2217 HOH A O   1 
HETATM 8692 O  O   . HOH F 6 .    ? 17.370 70.242  -23.475 1.00 19.83 ? 2218 HOH A O   1 
HETATM 8693 O  O   . HOH F 6 .    ? 37.633 47.082  29.840  1.00 21.71 ? 2219 HOH A O   1 
HETATM 8694 O  O   . HOH F 6 .    ? 49.925 55.124  -29.142 1.00 16.36 ? 2220 HOH A O   1 
HETATM 8695 O  O   . HOH F 6 .    ? 36.430 79.331  -5.054  1.00 20.98 ? 2221 HOH A O   1 
HETATM 8696 O  O   . HOH F 6 .    ? 62.251 62.613  25.836  1.00 18.10 ? 2222 HOH A O   1 
HETATM 8697 O  O   . HOH F 6 .    ? 11.401 53.224  6.791   1.00 15.91 ? 2223 HOH A O   1 
HETATM 8698 O  O   . HOH F 6 .    ? 13.929 60.930  -22.505 1.00 16.37 ? 2224 HOH A O   1 
HETATM 8699 O  O   . HOH F 6 .    ? 50.763 62.008  26.452  1.00 19.73 ? 2225 HOH A O   1 
HETATM 8700 O  O   . HOH F 6 .    ? 68.756 78.944  -18.248 1.00 21.06 ? 2226 HOH A O   1 
HETATM 8701 O  O   . HOH F 6 .    ? 84.506 68.363  -17.347 1.00 18.12 ? 2227 HOH A O   1 
HETATM 8702 O  O   . HOH F 6 .    ? 22.072 40.336  -8.757  1.00 26.30 ? 2228 HOH A O   1 
HETATM 8703 O  O   . HOH F 6 .    ? 52.996 69.689  18.342  1.00 27.23 ? 2229 HOH A O   1 
HETATM 8704 O  O   . HOH F 6 .    ? 42.836 53.353  35.668  1.00 22.66 ? 2230 HOH A O   1 
HETATM 8705 O  O   . HOH F 6 .    ? 70.742 52.134  -12.731 1.00 20.70 ? 2231 HOH A O   1 
HETATM 8706 O  O   . HOH F 6 .    ? 34.634 71.384  13.335  1.00 21.92 ? 2232 HOH A O   1 
HETATM 8707 O  O   . HOH F 6 .    ? 27.280 46.435  13.699  1.00 13.59 ? 2233 HOH A O   1 
HETATM 8708 O  O   . HOH F 6 .    ? 14.231 49.836  19.801  1.00 18.21 ? 2234 HOH A O   1 
HETATM 8709 O  O   . HOH F 6 .    ? 49.942 73.509  -21.880 1.00 25.83 ? 2235 HOH A O   1 
HETATM 8710 O  O   . HOH F 6 .    ? 48.901 44.284  -6.172  1.00 17.88 ? 2236 HOH A O   1 
HETATM 8711 O  O   . HOH F 6 .    ? 61.519 76.789  -39.903 1.00 21.53 ? 2237 HOH A O   1 
HETATM 8712 O  O   . HOH F 6 .    ? 22.898 78.729  -30.427 1.00 22.21 ? 2238 HOH A O   1 
HETATM 8713 O  O   . HOH F 6 .    ? 43.674 88.520  -38.755 1.00 16.42 ? 2239 HOH A O   1 
HETATM 8714 O  O   . HOH F 6 .    ? 35.917 77.657  -7.360  1.00 13.84 ? 2240 HOH A O   1 
HETATM 8715 O  O   . HOH F 6 .    ? 24.768 68.449  21.989  1.00 20.45 ? 2241 HOH A O   1 
HETATM 8716 O  O   . HOH F 6 .    ? 68.302 49.394  -1.058  1.00 23.25 ? 2242 HOH A O   1 
HETATM 8717 O  O   . HOH F 6 .    ? 54.313 47.808  15.581  1.00 21.55 ? 2243 HOH A O   1 
HETATM 8718 O  O   . HOH F 6 .    ? 55.298 50.365  16.924  1.00 26.90 ? 2244 HOH A O   1 
HETATM 8719 O  O   . HOH F 6 .    ? 39.539 48.879  -33.007 1.00 24.63 ? 2245 HOH A O   1 
HETATM 8720 O  O   . HOH F 6 .    ? 22.651 45.403  -13.499 1.00 17.14 ? 2246 HOH A O   1 
HETATM 8721 O  O   . HOH F 6 .    ? 67.345 55.276  0.930   1.00 16.14 ? 2247 HOH A O   1 
HETATM 8722 O  O   . HOH F 6 .    ? 48.104 44.032  -8.675  1.00 19.72 ? 2248 HOH A O   1 
HETATM 8723 O  O   . HOH F 6 .    ? 26.966 87.838  -23.750 1.00 22.60 ? 2249 HOH A O   1 
HETATM 8724 O  O   . HOH F 6 .    ? 18.818 48.747  37.694  1.00 18.09 ? 2250 HOH A O   1 
HETATM 8725 O  O   . HOH F 6 .    ? 83.757 67.722  -22.829 1.00 26.68 ? 2251 HOH A O   1 
HETATM 8726 O  O   . HOH F 6 .    ? 43.074 59.569  -18.894 1.00 23.45 ? 2252 HOH A O   1 
HETATM 8727 O  O   . HOH F 6 .    ? 47.554 79.167  -40.533 1.00 18.76 ? 2253 HOH A O   1 
HETATM 8728 O  O   . HOH F 6 .    ? 8.661  57.761  -6.836  1.00 24.58 ? 2254 HOH A O   1 
HETATM 8729 O  O   . HOH F 6 .    ? 54.966 90.383  -23.605 1.00 27.94 ? 2255 HOH A O   1 
HETATM 8730 O  O   . HOH F 6 .    ? 27.744 36.515  -19.691 1.00 24.66 ? 2256 HOH A O   1 
HETATM 8731 O  O   . HOH F 6 .    ? 72.416 58.850  -11.287 1.00 22.34 ? 2257 HOH A O   1 
HETATM 8732 O  O   . HOH F 6 .    ? 11.844 59.534  -5.016  1.00 21.71 ? 2258 HOH A O   1 
HETATM 8733 O  O   . HOH F 6 .    ? 23.681 46.056  -15.900 1.00 20.35 ? 2259 HOH A O   1 
HETATM 8734 O  O   . HOH F 6 .    ? 50.179 70.881  -17.665 1.00 24.63 ? 2260 HOH A O   1 
HETATM 8735 O  O   . HOH F 6 .    ? 45.298 90.159  -25.586 1.00 19.85 ? 2261 HOH A O   1 
HETATM 8736 O  O   . HOH F 6 .    ? 16.121 72.193  -19.110 1.00 19.17 ? 2262 HOH A O   1 
HETATM 8737 O  O   . HOH F 6 .    ? 20.191 52.732  -24.328 1.00 18.00 ? 2263 HOH A O   1 
HETATM 8738 O  O   . HOH F 6 .    ? 59.664 76.618  -9.042  1.00 17.25 ? 2264 HOH A O   1 
HETATM 8739 O  O   . HOH F 6 .    ? 67.027 60.043  -27.208 1.00 21.28 ? 2265 HOH A O   1 
HETATM 8740 O  O   . HOH F 6 .    ? 38.607 51.382  -29.818 1.00 28.70 ? 2266 HOH A O   1 
HETATM 8741 O  O   . HOH F 6 .    ? 40.518 82.920  -10.719 1.00 16.30 ? 2267 HOH A O   1 
HETATM 8742 O  O   . HOH F 6 .    ? 42.197 48.901  31.303  1.00 19.83 ? 2268 HOH A O   1 
HETATM 8743 O  O   . HOH F 6 .    ? 24.269 53.287  -6.248  1.00 18.56 ? 2269 HOH A O   1 
HETATM 8744 O  O   . HOH F 6 .    ? 53.408 47.141  -25.112 1.00 17.47 ? 2270 HOH A O   1 
HETATM 8745 O  O   . HOH F 6 .    ? 32.589 89.261  -43.155 1.00 22.67 ? 2271 HOH A O   1 
HETATM 8746 O  O   . HOH F 6 .    ? 36.081 36.150  -4.588  1.00 20.16 ? 2272 HOH A O   1 
HETATM 8747 O  O   . HOH F 6 .    ? 70.181 83.085  -29.980 1.00 22.71 ? 2273 HOH A O   1 
HETATM 8748 O  O   . HOH F 6 .    ? 49.900 82.519  -43.992 1.00 20.44 ? 2274 HOH A O   1 
HETATM 8749 O  O   . HOH F 6 .    ? 68.536 79.734  -34.954 1.00 24.55 ? 2275 HOH A O   1 
HETATM 8750 O  O   . HOH F 6 .    ? 29.144 46.993  37.189  1.00 22.17 ? 2276 HOH A O   1 
HETATM 8751 O  O   . HOH F 6 .    ? 18.596 70.077  4.178   1.00 14.67 ? 2277 HOH A O   1 
HETATM 8752 O  O   . HOH F 6 .    ? 14.129 68.377  -7.874  1.00 19.61 ? 2278 HOH A O   1 
HETATM 8753 O  O   . HOH F 6 .    ? 50.556 72.494  9.194   1.00 26.29 ? 2279 HOH A O   1 
HETATM 8754 O  O   . HOH F 6 .    ? 39.686 75.681  -40.367 1.00 17.36 ? 2280 HOH A O   1 
HETATM 8755 O  O   . HOH F 6 .    ? 28.625 65.249  19.844  1.00 17.63 ? 2281 HOH A O   1 
HETATM 8756 O  O   . HOH F 6 .    ? 11.669 58.799  7.898   1.00 24.48 ? 2282 HOH A O   1 
HETATM 8757 O  O   . HOH F 6 .    ? 52.682 79.170  -17.594 1.00 24.37 ? 2283 HOH A O   1 
HETATM 8758 O  O   . HOH F 6 .    ? 18.484 65.123  -27.036 1.00 20.84 ? 2284 HOH A O   1 
HETATM 8759 O  O   . HOH F 6 .    ? 44.812 79.413  -33.347 1.00 21.04 ? 2285 HOH A O   1 
HETATM 8760 O  O   . HOH F 6 .    ? 36.254 81.227  6.372   1.00 19.45 ? 2286 HOH A O   1 
HETATM 8761 O  O   . HOH F 6 .    ? 16.724 60.726  -28.119 1.00 19.55 ? 2287 HOH A O   1 
HETATM 8762 O  O   . HOH F 6 .    ? 29.682 87.413  -17.867 1.00 28.45 ? 2288 HOH A O   1 
HETATM 8763 O  O   . HOH F 6 .    ? 8.781  55.123  -6.065  1.00 25.47 ? 2289 HOH A O   1 
HETATM 8764 O  O   . HOH F 6 .    ? 46.801 61.764  -26.021 1.00 19.18 ? 2290 HOH A O   1 
HETATM 8765 O  O   . HOH F 6 .    ? 43.212 82.381  -10.029 1.00 25.50 ? 2291 HOH A O   1 
HETATM 8766 O  O   . HOH F 6 .    ? 10.345 50.729  18.862  1.00 22.09 ? 2292 HOH A O   1 
HETATM 8767 O  O   . HOH F 6 .    ? 12.935 42.479  12.529  1.00 21.43 ? 2293 HOH A O   1 
HETATM 8768 O  O   . HOH F 6 .    ? 35.962 45.139  30.905  1.00 20.72 ? 2294 HOH A O   1 
HETATM 8769 O  O   . HOH F 6 .    ? 15.928 75.327  -11.735 1.00 20.79 ? 2295 HOH A O   1 
HETATM 8770 O  O   . HOH F 6 .    ? 25.231 47.041  -20.949 1.00 22.12 ? 2296 HOH A O   1 
HETATM 8771 O  O   . HOH F 6 .    ? 56.938 64.953  24.342  1.00 22.53 ? 2297 HOH A O   1 
HETATM 8772 O  O   . HOH F 6 .    ? 38.693 94.162  -42.249 1.00 23.88 ? 2298 HOH A O   1 
HETATM 8773 O  O   . HOH F 6 .    ? 34.836 59.553  -35.058 1.00 19.06 ? 2299 HOH A O   1 
HETATM 8774 O  O   . HOH F 6 .    ? 33.052 40.913  -18.195 1.00 24.34 ? 2300 HOH A O   1 
HETATM 8775 O  O   . HOH F 6 .    ? 20.797 42.768  -7.431  1.00 18.47 ? 2301 HOH A O   1 
HETATM 8776 O  O   . HOH F 6 .    ? 19.138 76.769  4.783   1.00 27.56 ? 2302 HOH A O   1 
HETATM 8777 O  O   . HOH F 6 .    ? 43.507 80.964  4.957   1.00 20.63 ? 2303 HOH A O   1 
HETATM 8778 O  O   . HOH F 6 .    ? 32.995 85.483  -5.558  1.00 19.67 ? 2304 HOH A O   1 
HETATM 8779 O  O   . HOH F 6 .    ? 31.318 33.677  2.811   1.00 24.46 ? 2305 HOH A O   1 
HETATM 8780 O  O   . HOH F 6 .    ? 21.454 78.634  -1.406  1.00 18.15 ? 2306 HOH A O   1 
HETATM 8781 O  O   . HOH F 6 .    ? 55.471 59.112  3.895   1.00 17.04 ? 2307 HOH A O   1 
HETATM 8782 O  O   . HOH F 6 .    ? 13.418 62.476  -20.067 1.00 19.92 ? 2308 HOH A O   1 
HETATM 8783 O  O   . HOH F 6 .    ? 17.065 50.858  -19.358 1.00 23.81 ? 2309 HOH A O   1 
HETATM 8784 O  O   . HOH F 6 .    ? 14.257 62.964  -12.132 1.00 20.80 ? 2310 HOH A O   1 
HETATM 8785 O  O   . HOH F 6 .    ? 53.318 86.728  -21.475 1.00 24.97 ? 2311 HOH A O   1 
HETATM 8786 O  O   . HOH F 6 .    ? 71.165 49.540  -0.119  1.00 22.69 ? 2312 HOH A O   1 
HETATM 8787 O  O   . HOH F 6 .    ? 58.162 42.428  1.548   1.00 22.84 ? 2313 HOH A O   1 
HETATM 8788 O  O   . HOH F 6 .    ? 74.947 76.650  -14.182 1.00 26.17 ? 2314 HOH A O   1 
HETATM 8789 O  O   . HOH F 6 .    ? 24.958 83.237  -16.921 1.00 22.57 ? 2315 HOH A O   1 
HETATM 8790 O  O   . HOH F 6 .    ? 56.994 67.747  -35.499 1.00 23.45 ? 2316 HOH A O   1 
HETATM 8791 O  O   . HOH F 6 .    ? 48.993 50.779  -29.632 1.00 22.85 ? 2317 HOH A O   1 
HETATM 8792 O  O   . HOH F 6 .    ? 66.805 71.619  -6.929  1.00 20.93 ? 2318 HOH A O   1 
HETATM 8793 O  O   . HOH F 6 .    ? 28.831 93.901  -38.586 1.00 22.80 ? 2319 HOH A O   1 
HETATM 8794 O  O   . HOH F 6 .    ? 32.658 64.891  -10.007 1.00 18.87 ? 2320 HOH A O   1 
HETATM 8795 O  O   . HOH F 6 .    ? 13.484 51.005  -1.651  1.00 24.20 ? 2321 HOH A O   1 
HETATM 8796 O  O   . HOH F 6 .    ? 39.412 49.292  30.136  1.00 28.31 ? 2322 HOH A O   1 
HETATM 8797 O  O   . HOH F 6 .    ? 68.064 58.778  -24.226 1.00 19.74 ? 2323 HOH A O   1 
HETATM 8798 O  O   . HOH F 6 .    ? 20.850 59.084  -34.575 1.00 18.49 ? 2324 HOH A O   1 
HETATM 8799 O  O   . HOH F 6 .    ? 37.656 75.725  -42.554 1.00 21.72 ? 2325 HOH A O   1 
HETATM 8800 O  O   . HOH F 6 .    ? 31.951 51.374  -35.447 1.00 24.05 ? 2326 HOH A O   1 
HETATM 8801 O  O   . HOH F 6 .    ? 12.741 71.197  -0.452  1.00 25.95 ? 2327 HOH A O   1 
HETATM 8802 O  O   . HOH F 6 .    ? 37.035 41.134  -24.754 1.00 26.86 ? 2328 HOH A O   1 
HETATM 8803 O  O   . HOH F 6 .    ? 19.258 42.772  -2.531  1.00 25.96 ? 2329 HOH A O   1 
HETATM 8804 O  O   . HOH F 6 .    ? 50.156 44.130  7.081   1.00 18.58 ? 2330 HOH A O   1 
HETATM 8805 O  O   . HOH F 6 .    ? 37.500 45.398  -25.498 1.00 21.66 ? 2331 HOH A O   1 
HETATM 8806 O  O   . HOH F 6 .    ? 75.506 74.215  -19.499 1.00 24.00 ? 2332 HOH A O   1 
HETATM 8807 O  O   . HOH F 6 .    ? 50.440 61.146  -31.237 1.00 18.97 ? 2333 HOH A O   1 
HETATM 8808 O  O   . HOH F 6 .    ? 42.963 56.810  -31.642 1.00 22.12 ? 2334 HOH A O   1 
HETATM 8809 O  O   . HOH F 6 .    ? 13.266 68.903  0.877   1.00 22.66 ? 2335 HOH A O   1 
HETATM 8810 O  O   . HOH F 6 .    ? 40.707 83.005  -31.441 1.00 26.47 ? 2336 HOH A O   1 
HETATM 8811 O  O   . HOH F 6 .    ? 27.016 51.697  22.647  1.00 21.89 ? 2337 HOH A O   1 
HETATM 8812 O  O   . HOH F 6 .    ? 12.739 66.444  -9.704  1.00 19.59 ? 2338 HOH A O   1 
HETATM 8813 O  O   . HOH F 6 .    ? 42.556 39.555  -15.830 1.00 20.76 ? 2339 HOH A O   1 
HETATM 8814 O  O   . HOH F 6 .    ? 48.169 48.477  16.446  1.00 16.86 ? 2340 HOH A O   1 
HETATM 8815 O  O   . HOH F 6 .    ? 11.491 46.931  17.829  1.00 24.07 ? 2341 HOH A O   1 
HETATM 8816 O  O   . HOH F 6 .    ? 16.519 67.968  -19.816 1.00 20.38 ? 2342 HOH A O   1 
HETATM 8817 O  O   . HOH F 6 .    ? 5.056  52.900  -5.948  1.00 30.91 ? 2343 HOH A O   1 
HETATM 8818 O  O   . HOH F 6 .    ? 56.518 91.113  -25.799 1.00 22.72 ? 2344 HOH A O   1 
HETATM 8819 O  O   . HOH F 6 .    ? 39.214 83.278  -27.427 1.00 21.90 ? 2345 HOH A O   1 
HETATM 8820 O  O   . HOH F 6 .    ? 60.942 56.803  15.962  1.00 29.00 ? 2346 HOH A O   1 
HETATM 8821 O  O   . HOH F 6 .    ? 13.408 51.502  21.720  1.00 19.43 ? 2347 HOH A O   1 
HETATM 8822 O  O   . HOH F 6 .    ? 43.501 93.969  -37.907 1.00 21.84 ? 2348 HOH A O   1 
HETATM 8823 O  O   . HOH F 6 .    ? 28.258 35.370  -6.774  1.00 21.42 ? 2349 HOH A O   1 
HETATM 8824 O  O   . HOH F 6 .    ? 80.602 64.224  -21.553 1.00 23.40 ? 2350 HOH A O   1 
HETATM 8825 O  O   . HOH F 6 .    ? 51.590 45.154  9.825   1.00 28.87 ? 2351 HOH A O   1 
HETATM 8826 O  O   . HOH F 6 .    ? 21.501 46.920  -17.541 1.00 27.58 ? 2352 HOH A O   1 
HETATM 8827 O  O   . HOH F 6 .    ? 47.561 71.952  -20.373 1.00 23.50 ? 2353 HOH A O   1 
HETATM 8828 O  O   . HOH F 6 .    ? 21.572 86.030  -30.857 1.00 33.05 ? 2354 HOH A O   1 
HETATM 8829 O  O   . HOH F 6 .    ? 33.141 67.061  21.414  1.00 20.58 ? 2355 HOH A O   1 
HETATM 8830 O  O   . HOH F 6 .    ? 14.661 62.048  -14.537 1.00 20.76 ? 2356 HOH A O   1 
HETATM 8831 O  O   . HOH F 6 .    ? 50.561 73.809  -25.400 1.00 23.00 ? 2357 HOH A O   1 
HETATM 8832 O  O   . HOH F 6 .    ? 42.062 79.466  -23.478 1.00 25.57 ? 2358 HOH A O   1 
HETATM 8833 O  O   . HOH F 6 .    ? 39.968 45.404  25.535  1.00 27.14 ? 2359 HOH A O   1 
HETATM 8834 O  O   . HOH F 6 .    ? 51.020 76.566  14.510  1.00 21.97 ? 2360 HOH A O   1 
HETATM 8835 O  O   . HOH F 6 .    ? 38.651 45.177  -33.788 1.00 22.92 ? 2361 HOH A O   1 
HETATM 8836 O  O   . HOH F 6 .    ? 61.444 54.391  -29.023 1.00 23.30 ? 2362 HOH A O   1 
HETATM 8837 O  O   . HOH F 6 .    ? 53.840 46.694  23.391  1.00 30.69 ? 2363 HOH A O   1 
HETATM 8838 O  O   . HOH F 6 .    ? 57.197 43.179  -20.012 1.00 23.29 ? 2364 HOH A O   1 
HETATM 8839 O  O   . HOH F 6 .    ? 67.842 54.863  -18.305 1.00 23.90 ? 2365 HOH A O   1 
HETATM 8840 O  O   . HOH F 6 .    ? 42.561 80.180  -31.779 1.00 30.45 ? 2366 HOH A O   1 
HETATM 8841 O  O   . HOH F 6 .    ? 29.190 62.338  -39.845 1.00 24.62 ? 2367 HOH A O   1 
HETATM 8842 O  O   . HOH F 6 .    ? 27.105 61.306  10.424  1.00 24.84 ? 2368 HOH A O   1 
HETATM 8843 O  O   . HOH F 6 .    ? 45.801 45.204  23.187  1.00 28.66 ? 2369 HOH A O   1 
HETATM 8844 O  O   . HOH F 6 .    ? 34.903 51.249  35.972  1.00 34.00 ? 2370 HOH A O   1 
HETATM 8845 O  O   . HOH F 6 .    ? 57.808 62.548  7.871   1.00 27.77 ? 2371 HOH A O   1 
HETATM 8846 O  O   . HOH F 6 .    ? 25.290 33.527  13.399  1.00 28.62 ? 2372 HOH A O   1 
HETATM 8847 O  O   . HOH F 6 .    ? 27.234 59.527  8.540   1.00 18.07 ? 2373 HOH A O   1 
HETATM 8848 O  O   . HOH F 6 .    ? 42.887 94.548  -30.436 1.00 44.39 ? 2374 HOH A O   1 
HETATM 8849 O  O   . HOH F 6 .    ? 14.058 58.011  -1.382  1.00 20.67 ? 2375 HOH A O   1 
HETATM 8850 O  O   . HOH F 6 .    ? 49.347 76.409  5.512   1.00 34.34 ? 2376 HOH A O   1 
HETATM 8851 O  O   . HOH F 6 .    ? 27.703 67.853  28.603  1.00 24.90 ? 2377 HOH A O   1 
HETATM 8852 O  O   . HOH F 6 .    ? 41.961 39.280  16.607  1.00 29.66 ? 2378 HOH A O   1 
HETATM 8853 O  O   . HOH F 6 .    ? 59.070 46.484  -1.418  1.00 21.64 ? 2379 HOH A O   1 
HETATM 8854 O  O   . HOH F 6 .    ? 73.438 76.956  -18.355 1.00 29.11 ? 2380 HOH A O   1 
HETATM 8855 O  O   . HOH F 6 .    ? 19.690 39.266  17.544  1.00 19.34 ? 2381 HOH A O   1 
HETATM 8856 O  O   . HOH F 6 .    ? 39.776 58.981  -18.087 1.00 21.50 ? 2382 HOH A O   1 
HETATM 8857 O  O   . HOH F 6 .    ? 28.182 47.150  -31.669 1.00 28.38 ? 2383 HOH A O   1 
HETATM 8858 O  O   . HOH F 6 .    ? 68.765 47.008  -16.756 1.00 30.08 ? 2384 HOH A O   1 
HETATM 8859 O  O   . HOH F 6 .    ? 66.670 62.598  -13.115 1.00 16.09 ? 2385 HOH A O   1 
HETATM 8860 O  O   . HOH F 6 .    ? 40.184 39.487  9.133   1.00 25.36 ? 2386 HOH A O   1 
HETATM 8861 O  O   . HOH F 6 .    ? 21.067 47.494  39.085  1.00 19.59 ? 2387 HOH A O   1 
HETATM 8862 O  O   . HOH F 6 .    ? 42.345 74.902  -41.557 1.00 25.66 ? 2388 HOH A O   1 
HETATM 8863 O  O   . HOH F 6 .    ? 14.558 55.235  27.225  1.00 33.32 ? 2389 HOH A O   1 
HETATM 8864 O  O   . HOH F 6 .    ? 28.706 59.859  -39.259 1.00 31.13 ? 2390 HOH A O   1 
HETATM 8865 O  O   . HOH F 6 .    ? 39.017 43.063  22.811  1.00 25.43 ? 2391 HOH A O   1 
HETATM 8866 O  O   . HOH F 6 .    ? 16.606 53.008  -22.544 1.00 28.80 ? 2392 HOH A O   1 
HETATM 8867 O  O   . HOH F 6 .    ? 27.215 35.035  29.524  1.00 25.28 ? 2393 HOH A O   1 
HETATM 8868 O  O   . HOH F 6 .    ? 17.358 80.827  -7.513  1.00 23.48 ? 2394 HOH A O   1 
HETATM 8869 O  O   . HOH F 6 .    ? 48.228 41.853  3.681   1.00 19.87 ? 2395 HOH A O   1 
HETATM 8870 O  O   . HOH F 6 .    ? 73.435 51.362  -11.436 1.00 34.35 ? 2396 HOH A O   1 
HETATM 8871 O  O   . HOH F 6 .    ? 58.899 53.799  -22.285 1.00 20.33 ? 2397 HOH A O   1 
HETATM 8872 O  O   . HOH F 6 .    ? 47.649 79.688  -18.474 1.00 24.30 ? 2398 HOH A O   1 
HETATM 8873 O  O   . HOH F 6 .    ? 40.854 96.645  -37.537 1.00 23.46 ? 2399 HOH A O   1 
HETATM 8874 O  O   . HOH F 6 .    ? 61.199 63.650  15.310  1.00 21.91 ? 2400 HOH A O   1 
HETATM 8875 O  O   . HOH F 6 .    ? 59.475 37.754  -15.327 1.00 24.88 ? 2401 HOH A O   1 
HETATM 8876 O  O   . HOH F 6 .    ? 21.068 30.235  17.823  1.00 33.96 ? 2402 HOH A O   1 
HETATM 8877 O  O   . HOH F 6 .    ? 46.173 97.057  -43.990 1.00 23.63 ? 2403 HOH A O   1 
HETATM 8878 O  O   . HOH F 6 .    ? 21.609 86.256  -19.259 1.00 27.38 ? 2404 HOH A O   1 
HETATM 8879 O  O   . HOH F 6 .    ? 20.525 68.455  22.370  1.00 24.39 ? 2405 HOH A O   1 
HETATM 8880 O  O   . HOH F 6 .    ? 45.293 69.343  -17.373 1.00 23.01 ? 2406 HOH A O   1 
HETATM 8881 O  O   . HOH F 6 .    ? 16.695 70.653  6.183   1.00 34.46 ? 2407 HOH A O   1 
HETATM 8882 O  O   . HOH F 6 .    ? 51.272 52.762  -28.747 1.00 19.80 ? 2408 HOH A O   1 
HETATM 8883 O  O   . HOH F 6 .    ? 19.172 83.484  -25.862 1.00 29.78 ? 2409 HOH A O   1 
HETATM 8884 O  O   . HOH F 6 .    ? 40.242 86.101  -22.008 1.00 27.20 ? 2410 HOH A O   1 
HETATM 8885 O  O   . HOH F 6 .    ? 22.525 66.361  29.215  1.00 32.79 ? 2411 HOH A O   1 
HETATM 8886 O  O   . HOH F 6 .    ? 25.016 59.468  -36.221 1.00 32.22 ? 2412 HOH A O   1 
HETATM 8887 O  O   . HOH F 6 .    ? 58.585 34.811  -5.657  1.00 33.44 ? 2413 HOH A O   1 
HETATM 8888 O  O   . HOH F 6 .    ? 50.749 79.190  -15.702 1.00 25.40 ? 2414 HOH A O   1 
HETATM 8889 O  O   . HOH F 6 .    ? 56.582 92.887  -29.585 1.00 27.13 ? 2415 HOH A O   1 
HETATM 8890 O  O   . HOH F 6 .    ? 52.738 73.134  4.104   1.00 37.77 ? 2416 HOH A O   1 
HETATM 8891 O  O   . HOH F 6 .    ? 22.064 36.875  0.192   1.00 23.46 ? 2417 HOH A O   1 
HETATM 8892 O  O   . HOH F 6 .    ? 10.703 77.299  -5.147  1.00 32.34 ? 2418 HOH A O   1 
HETATM 8893 O  O   . HOH F 6 .    ? 72.966 64.051  -21.028 1.00 24.81 ? 2419 HOH A O   1 
HETATM 8894 O  O   . HOH F 6 .    ? 79.972 74.026  -17.836 1.00 28.59 ? 2420 HOH A O   1 
HETATM 8895 O  O   . HOH F 6 .    ? 67.049 74.533  -4.410  1.00 28.43 ? 2421 HOH A O   1 
HETATM 8896 O  O   . HOH F 6 .    ? 48.256 64.474  -28.536 1.00 21.08 ? 2422 HOH A O   1 
HETATM 8897 O  O   . HOH F 6 .    ? 42.602 39.466  -1.516  1.00 27.15 ? 2423 HOH A O   1 
HETATM 8898 O  O   . HOH F 6 .    ? 63.363 67.842  -31.770 1.00 35.13 ? 2424 HOH A O   1 
HETATM 8899 O  O   . HOH F 6 .    ? 24.388 42.069  -14.654 1.00 23.79 ? 2425 HOH A O   1 
HETATM 8900 O  O   . HOH F 6 .    ? 27.618 50.993  13.355  1.00 16.54 ? 2426 HOH A O   1 
HETATM 8901 O  O   . HOH F 6 .    ? 38.812 83.715  -39.889 1.00 25.58 ? 2427 HOH A O   1 
HETATM 8902 O  O   . HOH F 6 .    ? 76.904 74.147  -26.797 1.00 29.70 ? 2428 HOH A O   1 
HETATM 8903 O  O   . HOH F 6 .    ? 28.857 72.519  22.519  1.00 26.21 ? 2429 HOH A O   1 
HETATM 8904 O  O   . HOH F 6 .    ? 20.921 55.182  -35.887 1.00 32.75 ? 2430 HOH A O   1 
HETATM 8905 O  O   . HOH F 6 .    ? 23.984 57.368  38.795  1.00 30.86 ? 2431 HOH A O   1 
HETATM 8906 O  O   . HOH F 6 .    ? 23.527 82.627  -40.816 1.00 21.87 ? 2432 HOH A O   1 
HETATM 8907 O  O   . HOH F 6 .    ? 17.197 67.248  -26.176 1.00 32.47 ? 2433 HOH A O   1 
HETATM 8908 O  O   . HOH F 6 .    ? 66.506 84.617  -22.407 1.00 34.38 ? 2434 HOH A O   1 
HETATM 8909 O  O   . HOH F 6 .    ? 20.716 68.106  8.444   1.00 19.45 ? 2435 HOH A O   1 
HETATM 8910 O  O   . HOH F 6 .    ? 61.894 63.947  -30.864 1.00 35.69 ? 2436 HOH A O   1 
HETATM 8911 O  O   . HOH F 6 .    ? 9.791  59.890  6.382   1.00 36.01 ? 2437 HOH A O   1 
HETATM 8912 O  O   . HOH F 6 .    ? 31.681 85.900  -19.954 1.00 22.78 ? 2438 HOH A O   1 
HETATM 8913 O  O   . HOH F 6 .    ? 28.224 88.073  -41.770 1.00 28.87 ? 2439 HOH A O   1 
HETATM 8914 O  O   . HOH F 6 .    ? 44.878 82.707  -30.581 1.00 21.73 ? 2440 HOH A O   1 
HETATM 8915 O  O   . HOH F 6 .    ? 59.657 67.072  -34.669 1.00 26.83 ? 2441 HOH A O   1 
HETATM 8916 O  O   . HOH F 6 .    ? 70.525 56.506  -12.501 1.00 32.88 ? 2442 HOH A O   1 
HETATM 8917 O  O   . HOH F 6 .    ? 46.267 46.278  16.267  1.00 31.97 ? 2443 HOH A O   1 
HETATM 8918 O  O   . HOH F 6 .    ? 45.986 82.806  -25.342 1.00 31.60 ? 2444 HOH A O   1 
HETATM 8919 O  O   . HOH F 6 .    ? 56.994 87.741  -20.079 1.00 28.24 ? 2445 HOH A O   1 
HETATM 8920 O  O   . HOH F 6 .    ? 73.832 74.245  -5.811  1.00 23.55 ? 2446 HOH A O   1 
HETATM 8921 O  O   . HOH F 6 .    ? 19.900 43.247  33.961  1.00 25.45 ? 2447 HOH A O   1 
HETATM 8922 O  O   . HOH F 6 .    ? 79.438 51.229  -0.645  1.00 22.68 ? 2448 HOH A O   1 
HETATM 8923 O  O   . HOH F 6 .    ? 66.444 45.453  -3.350  1.00 28.53 ? 2449 HOH A O   1 
HETATM 8924 O  O   . HOH F 6 .    ? 48.629 78.132  -9.758  1.00 26.10 ? 2450 HOH A O   1 
HETATM 8925 O  O   . HOH F 6 .    ? 30.079 34.159  -1.558  1.00 25.91 ? 2451 HOH A O   1 
HETATM 8926 O  O   . HOH F 6 .    ? 16.227 75.270  -24.136 1.00 36.03 ? 2452 HOH A O   1 
HETATM 8927 O  O   . HOH F 6 .    ? 22.407 31.196  29.459  1.00 30.84 ? 2453 HOH A O   1 
HETATM 8928 O  O   . HOH F 6 .    ? 33.463 84.487  -18.359 1.00 16.72 ? 2454 HOH A O   1 
HETATM 8929 O  O   . HOH F 6 .    ? 41.408 94.907  -39.620 1.00 25.92 ? 2455 HOH A O   1 
HETATM 8930 O  O   . HOH F 6 .    ? 44.478 83.852  -27.907 1.00 25.49 ? 2456 HOH A O   1 
HETATM 8931 O  O   . HOH F 6 .    ? 30.985 57.368  4.653   1.00 13.94 ? 2457 HOH A O   1 
HETATM 8932 O  O   . HOH F 6 .    ? 66.151 66.192  -0.546  1.00 23.47 ? 2458 HOH A O   1 
HETATM 8933 O  O   . HOH F 6 .    ? 46.420 68.783  26.468  1.00 31.51 ? 2459 HOH A O   1 
HETATM 8934 O  O   . HOH F 6 .    ? 70.376 61.856  -20.437 1.00 28.54 ? 2460 HOH A O   1 
HETATM 8935 O  O   . HOH F 6 .    ? 23.871 91.072  -26.175 1.00 34.82 ? 2461 HOH A O   1 
HETATM 8936 O  O   . HOH F 6 .    ? 25.202 71.299  22.663  1.00 35.27 ? 2462 HOH A O   1 
HETATM 8937 O  O   . HOH F 6 .    ? 14.064 69.449  26.907  1.00 22.72 ? 2463 HOH A O   1 
HETATM 8938 O  O   . HOH F 6 .    ? 62.400 80.798  -18.989 1.00 24.05 ? 2464 HOH A O   1 
HETATM 8939 O  O   . HOH F 6 .    ? 27.700 47.588  45.871  1.00 37.20 ? 2465 HOH A O   1 
HETATM 8940 O  O   . HOH F 6 .    ? 24.891 34.398  0.310   1.00 41.26 ? 2466 HOH A O   1 
HETATM 8941 O  O   . HOH F 6 .    ? 57.774 67.849  13.995  1.00 52.15 ? 2467 HOH A O   1 
HETATM 8942 O  O   . HOH F 6 .    ? 8.018  48.225  11.931  1.00 24.32 ? 2468 HOH A O   1 
HETATM 8943 O  O   . HOH F 6 .    ? 71.590 59.852  0.983   1.00 35.85 ? 2469 HOH A O   1 
HETATM 8944 O  O   . HOH F 6 .    ? 67.903 88.188  -23.569 1.00 25.43 ? 2470 HOH A O   1 
HETATM 8945 O  O   . HOH F 6 .    ? 12.419 75.129  -13.540 1.00 30.56 ? 2471 HOH A O   1 
HETATM 8946 O  O   . HOH F 6 .    ? 27.678 52.085  42.591  1.00 29.94 ? 2472 HOH A O   1 
HETATM 8947 O  O   . HOH F 6 .    ? 22.104 62.895  33.791  1.00 32.64 ? 2473 HOH A O   1 
HETATM 8948 O  O   . HOH F 6 .    ? 34.545 87.227  -10.612 1.00 32.54 ? 2474 HOH A O   1 
HETATM 8949 O  O   . HOH F 6 .    ? 30.194 36.570  29.109  1.00 26.06 ? 2475 HOH A O   1 
HETATM 8950 O  O   . HOH F 6 .    ? 8.486  49.782  5.728   1.00 42.76 ? 2476 HOH A O   1 
HETATM 8951 O  O   . HOH F 6 .    ? 42.054 67.460  29.351  1.00 27.40 ? 2477 HOH A O   1 
HETATM 8952 O  O   . HOH F 6 .    ? 72.666 75.917  -27.354 1.00 34.61 ? 2478 HOH A O   1 
HETATM 8953 O  O   . HOH F 6 .    ? 8.797  44.535  12.804  1.00 31.20 ? 2479 HOH A O   1 
HETATM 8954 O  O   . HOH F 6 .    ? 41.542 44.727  -24.434 1.00 22.44 ? 2480 HOH A O   1 
HETATM 8955 O  O   . HOH F 6 .    ? 39.822 67.003  31.390  1.00 25.00 ? 2481 HOH A O   1 
HETATM 8956 O  O   . HOH F 6 .    ? 53.494 52.656  26.296  1.00 21.15 ? 2482 HOH A O   1 
HETATM 8957 O  O   . HOH F 6 .    ? 26.358 44.404  -27.285 1.00 29.81 ? 2483 HOH A O   1 
HETATM 8958 O  O   . HOH F 6 .    ? 19.811 52.552  -27.180 1.00 27.64 ? 2484 HOH A O   1 
HETATM 8959 O  O   . HOH F 6 .    ? 70.627 95.475  -35.112 1.00 45.57 ? 2485 HOH A O   1 
HETATM 8960 O  O   . HOH F 6 .    ? 48.298 64.935  -25.860 1.00 23.41 ? 2486 HOH A O   1 
HETATM 8961 O  O   . HOH F 6 .    ? 44.499 64.432  -35.553 1.00 51.97 ? 2487 HOH A O   1 
HETATM 8962 O  O   . HOH F 6 .    ? 17.601 53.401  35.213  1.00 30.16 ? 2488 HOH A O   1 
HETATM 8963 O  O   . HOH F 6 .    ? 83.772 70.230  -20.245 1.00 26.30 ? 2489 HOH A O   1 
HETATM 8964 O  O   . HOH F 6 .    ? 44.034 79.918  -42.604 1.00 29.60 ? 2490 HOH A O   1 
HETATM 8965 O  O   . HOH F 6 .    ? 22.652 62.618  16.172  1.00 24.46 ? 2491 HOH A O   1 
HETATM 8966 O  O   . HOH F 6 .    ? 45.868 79.358  -7.914  1.00 23.82 ? 2492 HOH A O   1 
HETATM 8967 O  O   . HOH F 6 .    ? 38.777 42.296  -22.190 1.00 26.65 ? 2493 HOH A O   1 
HETATM 8968 O  O   . HOH F 6 .    ? 36.950 29.274  13.168  1.00 32.48 ? 2494 HOH A O   1 
HETATM 8969 O  O   . HOH F 6 .    ? 20.453 65.553  27.341  1.00 25.68 ? 2495 HOH A O   1 
HETATM 8970 O  O   . HOH F 6 .    ? 7.031  59.715  2.244   1.00 44.13 ? 2496 HOH A O   1 
HETATM 8971 O  O   . HOH F 6 .    ? 61.357 77.596  -13.059 1.00 21.38 ? 2497 HOH A O   1 
HETATM 8972 O  O   . HOH F 6 .    ? 28.148 49.376  38.523  1.00 27.12 ? 2498 HOH A O   1 
HETATM 8973 O  O   . HOH F 6 .    ? 19.543 67.411  -2.809  1.00 27.80 ? 2499 HOH A O   1 
HETATM 8974 O  O   . HOH F 6 .    ? 43.685 41.915  -7.575  1.00 24.22 ? 2500 HOH A O   1 
HETATM 8975 O  O   . HOH F 6 .    ? 48.707 54.994  -22.828 1.00 19.20 ? 2501 HOH A O   1 
HETATM 8976 O  O   . HOH F 6 .    ? 35.854 39.059  -16.220 1.00 27.46 ? 2502 HOH A O   1 
HETATM 8977 O  O   . HOH F 6 .    ? 58.682 51.200  22.368  1.00 19.12 ? 2503 HOH A O   1 
HETATM 8978 O  O   . HOH F 6 .    ? 46.667 80.363  -42.742 1.00 27.96 ? 2504 HOH A O   1 
HETATM 8979 O  O   . HOH F 6 .    ? 71.933 84.693  -20.180 1.00 27.92 ? 2505 HOH A O   1 
HETATM 8980 O  O   . HOH F 6 .    ? 61.426 67.809  -36.444 1.00 32.58 ? 2506 HOH A O   1 
HETATM 8981 O  O   . HOH F 6 .    ? 58.650 34.925  -12.440 1.00 38.16 ? 2507 HOH A O   1 
HETATM 8982 O  O   . HOH F 6 .    ? 21.172 79.580  -23.601 1.00 23.60 ? 2508 HOH A O   1 
HETATM 8983 O  O   . HOH F 6 .    ? 51.379 71.481  -20.231 1.00 19.79 ? 2509 HOH A O   1 
HETATM 8984 O  O   . HOH F 6 .    ? 32.218 85.337  -8.603  1.00 20.73 ? 2510 HOH A O   1 
HETATM 8985 O  O   . HOH F 6 .    ? 21.821 29.141  28.099  1.00 35.55 ? 2511 HOH A O   1 
HETATM 8986 O  O   . HOH F 6 .    ? 31.558 57.418  37.489  1.00 27.57 ? 2512 HOH A O   1 
HETATM 8987 O  O   . HOH F 6 .    ? 17.573 81.351  -17.185 1.00 48.09 ? 2513 HOH A O   1 
HETATM 8988 O  O   . HOH F 6 .    ? 22.121 80.320  -36.195 1.00 24.39 ? 2514 HOH A O   1 
HETATM 8989 O  O   . HOH F 6 .    ? 25.420 73.939  8.740   1.00 27.85 ? 2515 HOH A O   1 
HETATM 8990 O  O   . HOH F 6 .    ? 21.601 79.922  5.319   1.00 28.03 ? 2516 HOH A O   1 
HETATM 8991 O  O   . HOH F 6 .    ? 40.026 38.928  -3.479  1.00 21.73 ? 2517 HOH A O   1 
HETATM 8992 O  O   . HOH F 6 .    ? 36.817 35.239  -15.929 1.00 29.10 ? 2518 HOH A O   1 
HETATM 8993 O  O   . HOH F 6 .    ? 34.837 45.772  33.367  1.00 18.60 ? 2519 HOH A O   1 
HETATM 8994 O  O   . HOH F 6 .    ? 46.492 74.382  22.459  1.00 31.58 ? 2520 HOH A O   1 
HETATM 8995 O  O   . HOH F 6 .    ? 60.600 91.994  -28.645 1.00 28.98 ? 2521 HOH A O   1 
HETATM 8996 O  O   . HOH F 6 .    ? 37.745 62.323  35.589  1.00 35.37 ? 2522 HOH A O   1 
HETATM 8997 O  O   . HOH F 6 .    ? 63.110 42.816  -20.955 1.00 25.92 ? 2523 HOH A O   1 
HETATM 8998 O  O   . HOH F 6 .    ? 30.537 34.880  -9.621  1.00 34.56 ? 2524 HOH A O   1 
HETATM 8999 O  O   . HOH F 6 .    ? 29.555 31.397  21.994  1.00 36.90 ? 2525 HOH A O   1 
HETATM 9000 O  O   . HOH F 6 .    ? 78.922 68.924  -12.180 1.00 29.84 ? 2526 HOH A O   1 
HETATM 9001 O  O   . HOH F 6 .    ? 31.308 69.371  -45.574 1.00 39.24 ? 2527 HOH A O   1 
HETATM 9002 O  O   . HOH F 6 .    ? 73.605 82.320  -21.265 1.00 27.08 ? 2528 HOH A O   1 
HETATM 9003 O  O   . HOH F 6 .    ? 20.596 37.961  12.114  1.00 28.86 ? 2529 HOH A O   1 
HETATM 9004 O  O   . HOH F 6 .    ? 35.166 95.004  -32.353 1.00 29.89 ? 2530 HOH A O   1 
HETATM 9005 O  O   . HOH F 6 .    ? 17.458 41.748  9.280   1.00 26.78 ? 2531 HOH A O   1 
HETATM 9006 O  O   . HOH F 6 .    ? 20.613 80.348  -33.650 1.00 44.91 ? 2532 HOH A O   1 
HETATM 9007 O  O   . HOH F 6 .    ? 49.485 91.967  -24.618 1.00 33.54 ? 2533 HOH A O   1 
HETATM 9008 O  O   . HOH F 6 .    ? 43.917 45.017  19.312  1.00 35.90 ? 2534 HOH A O   1 
HETATM 9009 O  O   . HOH F 6 .    ? 21.214 35.726  -5.000  1.00 36.20 ? 2535 HOH A O   1 
HETATM 9010 O  O   . HOH F 6 .    ? 46.982 53.975  -21.522 1.00 27.07 ? 2536 HOH A O   1 
HETATM 9011 O  O   . HOH F 6 .    ? 71.562 63.108  -27.231 1.00 47.05 ? 2537 HOH A O   1 
HETATM 9012 O  O   . HOH F 6 .    ? 19.861 35.611  25.550  1.00 28.32 ? 2538 HOH A O   1 
HETATM 9013 O  O   . HOH F 6 .    ? 59.411 86.877  -45.961 1.00 40.80 ? 2539 HOH A O   1 
HETATM 9014 O  O   . HOH F 6 .    ? 28.865 69.848  -39.632 1.00 22.44 ? 2540 HOH A O   1 
HETATM 9015 O  O   . HOH F 6 .    ? 45.382 83.598  -43.190 1.00 36.53 ? 2541 HOH A O   1 
HETATM 9016 O  O   . HOH F 6 .    ? 29.667 81.445  -43.209 1.00 41.28 ? 2542 HOH A O   1 
HETATM 9017 O  O   . HOH F 6 .    ? 28.194 90.922  -42.744 1.00 28.83 ? 2543 HOH A O   1 
HETATM 9018 O  O   . HOH F 6 .    ? 21.045 41.775  35.280  1.00 28.74 ? 2544 HOH A O   1 
HETATM 9019 O  O   . HOH F 6 .    ? 62.469 85.559  -23.060 1.00 30.21 ? 2545 HOH A O   1 
HETATM 9020 O  O   . HOH F 6 .    ? 31.162 68.679  14.209  1.00 25.80 ? 2546 HOH A O   1 
HETATM 9021 O  O   . HOH F 6 .    ? 27.510 67.364  33.829  1.00 38.88 ? 2547 HOH A O   1 
HETATM 9022 O  O   . HOH F 6 .    ? 15.063 63.762  -25.829 1.00 23.34 ? 2548 HOH A O   1 
HETATM 9023 O  O   . HOH F 6 .    ? 29.590 72.270  12.362  1.00 31.21 ? 2549 HOH A O   1 
HETATM 9024 O  O   . HOH F 6 .    ? 60.782 93.112  -38.555 1.00 47.99 ? 2550 HOH A O   1 
HETATM 9025 O  O   . HOH F 6 .    ? 59.155 62.406  25.849  1.00 23.13 ? 2551 HOH A O   1 
HETATM 9026 O  O   . HOH F 6 .    ? 51.464 79.437  -1.785  1.00 24.61 ? 2552 HOH A O   1 
HETATM 9027 O  O   . HOH F 6 .    ? 59.739 91.259  -35.537 1.00 25.52 ? 2553 HOH A O   1 
HETATM 9028 O  O   . HOH F 6 .    ? 24.058 60.818  36.139  1.00 31.79 ? 2554 HOH A O   1 
HETATM 9029 O  O   . HOH F 6 .    ? 55.448 80.664  -19.425 1.00 24.37 ? 2555 HOH A O   1 
HETATM 9030 O  O   . HOH F 6 .    ? 16.796 74.471  -28.783 1.00 49.29 ? 2556 HOH A O   1 
HETATM 9031 O  O   . HOH F 6 .    ? 40.987 40.756  -21.603 1.00 24.59 ? 2557 HOH A O   1 
HETATM 9032 O  O   . HOH F 6 .    ? 40.080 35.483  11.340  1.00 24.13 ? 2558 HOH A O   1 
HETATM 9033 O  O   . HOH F 6 .    ? 18.998 80.760  -11.740 1.00 31.30 ? 2559 HOH A O   1 
HETATM 9034 O  O   . HOH F 6 .    ? 73.298 43.755  -12.329 1.00 46.39 ? 2560 HOH A O   1 
HETATM 9035 O  O   . HOH F 6 .    ? 12.883 74.426  -19.089 1.00 38.13 ? 2561 HOH A O   1 
HETATM 9036 O  O   . HOH F 6 .    ? 57.293 75.617  -3.016  1.00 25.60 ? 2562 HOH A O   1 
HETATM 9037 O  O   . HOH F 6 .    ? 50.951 77.161  2.137   1.00 38.38 ? 2563 HOH A O   1 
HETATM 9038 O  O   . HOH F 6 .    ? 23.224 36.972  13.383  1.00 28.08 ? 2564 HOH A O   1 
HETATM 9039 O  O   . HOH F 6 .    ? 29.632 88.851  -26.277 1.00 13.04 ? 2565 HOH A O   1 
HETATM 9040 O  O   . HOH F 6 .    ? 37.203 33.622  6.060   1.00 48.19 ? 2566 HOH A O   1 
HETATM 9041 O  O   . HOH F 6 .    ? 71.897 62.690  -18.078 1.00 32.18 ? 2567 HOH A O   1 
HETATM 9042 O  O   . HOH F 6 .    ? 34.142 70.340  -44.814 1.00 41.15 ? 2568 HOH A O   1 
HETATM 9043 O  O   . HOH F 6 .    ? 64.663 77.327  0.375   1.00 38.62 ? 2569 HOH A O   1 
HETATM 9044 O  O   . HOH F 6 .    ? 20.954 54.812  47.322  1.00 45.36 ? 2570 HOH A O   1 
HETATM 9045 O  O   . HOH F 6 .    ? 14.517 50.726  1.026   1.00 29.21 ? 2571 HOH A O   1 
HETATM 9046 O  O   . HOH F 6 .    ? 55.631 38.606  1.011   1.00 48.04 ? 2572 HOH A O   1 
HETATM 9047 O  O   . HOH F 6 .    ? 67.019 81.458  -11.338 1.00 30.92 ? 2573 HOH A O   1 
HETATM 9048 O  O   . HOH F 6 .    ? 43.680 56.706  33.823  1.00 24.92 ? 2574 HOH A O   1 
HETATM 9049 O  O   . HOH F 6 .    ? 56.459 50.028  -30.217 1.00 39.48 ? 2575 HOH A O   1 
HETATM 9050 O  O   . HOH F 6 .    ? 63.452 57.677  25.864  1.00 38.88 ? 2576 HOH A O   1 
HETATM 9051 O  O   . HOH F 6 .    ? 62.150 48.242  -21.095 1.00 36.66 ? 2577 HOH A O   1 
HETATM 9052 O  O   . HOH F 6 .    ? 26.788 91.845  -27.704 1.00 28.26 ? 2578 HOH A O   1 
HETATM 9053 O  O   . HOH F 6 .    ? 13.664 70.248  -9.669  1.00 28.28 ? 2579 HOH A O   1 
HETATM 9054 O  O   . HOH F 6 .    ? 60.867 79.004  -41.668 1.00 28.47 ? 2580 HOH A O   1 
HETATM 9055 O  O   . HOH F 6 .    ? 36.564 62.775  -38.348 1.00 31.18 ? 2581 HOH A O   1 
HETATM 9056 O  O   . HOH F 6 .    ? 37.799 80.584  -0.688  1.00 19.29 ? 2582 HOH A O   1 
HETATM 9057 O  O   . HOH F 6 .    ? 47.471 53.546  35.898  1.00 39.20 ? 2583 HOH A O   1 
HETATM 9058 O  O   . HOH F 6 .    ? 48.663 97.922  -33.925 1.00 34.06 ? 2584 HOH A O   1 
HETATM 9059 O  O   . HOH F 6 .    ? 63.169 74.681  -46.177 1.00 36.35 ? 2585 HOH A O   1 
HETATM 9060 O  O   . HOH F 6 .    ? 41.182 48.019  -29.144 1.00 40.87 ? 2586 HOH A O   1 
HETATM 9061 O  O   . HOH F 6 .    ? 63.656 52.004  -0.476  1.00 29.21 ? 2587 HOH A O   1 
HETATM 9062 O  O   . HOH F 6 .    ? 22.931 49.011  -36.362 1.00 40.34 ? 2588 HOH A O   1 
HETATM 9063 O  O   . HOH F 6 .    ? 18.639 71.058  -29.925 1.00 43.32 ? 2589 HOH A O   1 
HETATM 9064 O  O   . HOH F 6 .    ? 27.498 50.005  23.254  1.00 33.08 ? 2590 HOH A O   1 
HETATM 9065 O  O   . HOH F 6 .    ? 60.066 52.948  -30.621 1.00 30.14 ? 2591 HOH A O   1 
HETATM 9066 O  O   . HOH F 6 .    ? 34.302 47.978  36.295  1.00 35.03 ? 2592 HOH A O   1 
HETATM 9067 O  O   . HOH F 6 .    ? 27.534 82.469  3.220   1.00 33.04 ? 2593 HOH A O   1 
HETATM 9068 O  O   . HOH F 6 .    ? 53.445 70.949  -17.082 1.00 28.29 ? 2594 HOH A O   1 
HETATM 9069 O  O   . HOH F 6 .    ? 28.557 44.334  -29.678 1.00 33.12 ? 2595 HOH A O   1 
HETATM 9070 O  O   . HOH F 6 .    ? 49.543 49.155  -38.176 1.00 51.26 ? 2596 HOH A O   1 
HETATM 9071 O  O   . HOH F 6 .    ? 35.752 77.534  -43.160 1.00 32.63 ? 2597 HOH A O   1 
HETATM 9072 O  O   . HOH F 6 .    ? 65.516 78.826  -5.894  1.00 27.42 ? 2598 HOH A O   1 
HETATM 9073 O  O   . HOH F 6 .    ? 49.490 50.794  32.629  1.00 28.42 ? 2599 HOH A O   1 
HETATM 9074 O  O   . HOH F 6 .    ? 17.581 45.738  -14.074 1.00 30.44 ? 2600 HOH A O   1 
HETATM 9075 O  O   . HOH F 6 .    ? 28.458 55.455  40.059  1.00 28.04 ? 2601 HOH A O   1 
HETATM 9076 O  O   . HOH F 6 .    ? 51.021 59.978  -8.968  1.00 12.12 ? 2602 HOH A O   1 
HETATM 9077 O  O   . HOH F 6 .    ? 43.927 63.080  -28.716 1.00 10.73 ? 2603 HOH A O   1 
HETATM 9078 O  O   . HOH F 6 .    ? 38.246 81.862  -31.453 1.00 13.59 ? 2604 HOH A O   1 
HETATM 9079 O  O   . HOH F 6 .    ? 32.412 39.239  -4.932  1.00 11.65 ? 2605 HOH A O   1 
HETATM 9080 O  O   . HOH F 6 .    ? 60.589 61.018  -18.205 1.00 10.46 ? 2606 HOH A O   1 
HETATM 9081 O  O   . HOH F 6 .    ? 63.372 58.677  -1.459  1.00 16.20 ? 2607 HOH A O   1 
HETATM 9082 O  O   . HOH F 6 .    ? 60.868 60.922  -3.653  1.00 13.11 ? 2608 HOH A O   1 
HETATM 9083 O  O   . HOH F 6 .    ? 46.862 74.584  7.766   1.00 12.05 ? 2609 HOH A O   1 
HETATM 9084 O  O   . HOH F 6 .    ? 55.208 57.675  -0.497  1.00 16.53 ? 2610 HOH A O   1 
HETATM 9085 O  O   . HOH F 6 .    ? 30.377 75.047  -29.343 1.00 13.32 ? 2611 HOH A O   1 
HETATM 9086 O  O   . HOH F 6 .    ? 59.106 56.839  -1.464  1.00 12.42 ? 2612 HOH A O   1 
HETATM 9087 O  O   . HOH F 6 .    ? 58.934 52.707  -0.150  1.00 13.34 ? 2613 HOH A O   1 
HETATM 9088 O  O   . HOH F 6 .    ? 63.280 61.169  -4.917  1.00 14.52 ? 2614 HOH A O   1 
HETATM 9089 O  O   . HOH F 6 .    ? 27.974 48.687  12.126  1.00 14.28 ? 2615 HOH A O   1 
HETATM 9090 O  O   . HOH F 6 .    ? 66.768 56.280  -20.322 1.00 17.88 ? 2616 HOH A O   1 
HETATM 9091 O  O   . HOH F 6 .    ? 19.997 46.809  -14.377 1.00 19.24 ? 2617 HOH A O   1 
HETATM 9092 O  O   . HOH F 6 .    ? 38.783 69.300  -38.243 1.00 17.11 ? 2618 HOH A O   1 
HETATM 9093 O  O   . HOH F 6 .    ? 33.639 60.269  23.247  1.00 13.42 ? 2619 HOH A O   1 
HETATM 9094 O  O   . HOH F 6 .    ? 39.760 55.788  3.029   1.00 12.95 ? 2620 HOH A O   1 
HETATM 9095 O  O   . HOH F 6 .    ? 24.662 61.466  9.232   1.00 14.85 ? 2621 HOH A O   1 
HETATM 9096 O  O   . HOH F 6 .    ? 16.741 57.122  12.988  1.00 14.15 ? 2622 HOH A O   1 
HETATM 9097 O  O   . HOH F 6 .    ? 39.447 69.224  -35.500 1.00 15.96 ? 2623 HOH A O   1 
HETATM 9098 O  O   . HOH F 6 .    ? 50.040 67.592  4.238   1.00 17.19 ? 2624 HOH A O   1 
HETATM 9099 O  O   . HOH F 6 .    ? 27.734 53.359  20.188  1.00 15.80 ? 2625 HOH A O   1 
HETATM 9100 O  O   . HOH F 6 .    ? 29.960 83.164  2.492   1.00 20.65 ? 2626 HOH A O   1 
HETATM 9101 O  O   . HOH F 6 .    ? 28.149 91.008  -25.408 1.00 19.72 ? 2627 HOH A O   1 
HETATM 9102 O  O   . HOH F 6 .    ? 46.276 77.782  9.514   1.00 20.28 ? 2628 HOH A O   1 
HETATM 9103 O  O   . HOH F 6 .    ? 12.544 49.512  17.729  1.00 21.50 ? 2629 HOH A O   1 
HETATM 9104 O  O   . HOH F 6 .    ? 81.502 68.631  -11.528 1.00 24.98 ? 2630 HOH A O   1 
HETATM 9105 O  O   . HOH F 6 .    ? 41.586 44.860  -6.904  1.00 13.11 ? 2631 HOH A O   1 
HETATM 9106 O  O   . HOH F 6 .    ? 45.622 67.917  -27.798 1.00 21.53 ? 2632 HOH A O   1 
HETATM 9107 O  O   . HOH F 6 .    ? 14.083 50.493  24.216  1.00 21.10 ? 2633 HOH A O   1 
HETATM 9108 O  O   . HOH F 6 .    ? 67.736 46.625  -1.408  1.00 23.78 ? 2634 HOH A O   1 
HETATM 9109 O  O   . HOH F 6 .    ? 9.051  50.513  7.952   1.00 28.93 ? 2635 HOH A O   1 
HETATM 9110 O  O   . HOH F 6 .    ? 48.662 40.973  -1.034  1.00 23.85 ? 2636 HOH A O   1 
HETATM 9111 O  O   . HOH F 6 .    ? 17.896 74.617  3.862   1.00 23.17 ? 2637 HOH A O   1 
HETATM 9112 O  O   . HOH F 6 .    ? 45.062 55.105  -18.215 1.00 24.70 ? 2638 HOH A O   1 
HETATM 9113 O  O   . HOH F 6 .    ? 83.650 66.470  -15.466 1.00 22.00 ? 2639 HOH A O   1 
HETATM 9114 O  O   . HOH F 6 .    ? 49.132 69.165  -36.958 1.00 25.95 ? 2640 HOH A O   1 
HETATM 9115 O  O   . HOH F 6 .    ? 51.715 70.188  -38.106 1.00 23.08 ? 2641 HOH A O   1 
HETATM 9116 O  O   . HOH F 6 .    ? 29.694 72.380  34.459  1.00 25.92 ? 2642 HOH A O   1 
HETATM 9117 O  O   . HOH F 6 .    ? 37.706 61.503  -32.578 1.00 22.31 ? 2643 HOH A O   1 
HETATM 9118 O  O   . HOH F 6 .    ? 57.409 48.972  21.425  1.00 21.34 ? 2644 HOH A O   1 
HETATM 9119 O  O   . HOH F 6 .    ? 43.117 59.610  -31.533 1.00 21.00 ? 2645 HOH A O   1 
HETATM 9120 O  O   . HOH F 6 .    ? 32.130 34.465  -3.253  1.00 21.02 ? 2646 HOH A O   1 
HETATM 9121 O  O   . HOH F 6 .    ? 37.173 59.102  -33.653 1.00 24.28 ? 2647 HOH A O   1 
HETATM 9122 O  O   . HOH F 6 .    ? 61.736 59.032  14.976  1.00 25.33 ? 2648 HOH A O   1 
HETATM 9123 O  O   . HOH F 6 .    ? 40.411 56.317  -19.260 1.00 27.29 ? 2649 HOH A O   1 
HETATM 9124 O  O   . HOH F 6 .    ? 61.956 76.460  -10.657 1.00 18.38 ? 2650 HOH A O   1 
HETATM 9125 O  O   . HOH F 6 .    ? 79.662 50.950  -11.496 1.00 44.32 ? 2651 HOH A O   1 
HETATM 9126 O  O   . HOH F 6 .    ? 37.720 51.642  -18.573 1.00 17.81 ? 2652 HOH A O   1 
HETATM 9127 O  O   . HOH F 6 .    ? 25.584 52.323  13.001  1.00 18.74 ? 2653 HOH A O   1 
HETATM 9128 O  O   . HOH F 6 .    ? 69.758 63.939  -28.800 1.00 26.50 ? 2654 HOH A O   1 
HETATM 9129 O  O   . HOH F 6 .    ? 73.169 66.625  -10.120 1.00 22.21 ? 2655 HOH A O   1 
HETATM 9130 O  O   . HOH F 6 .    ? 42.904 56.550  2.758   1.00 18.12 ? 2656 HOH A O   1 
HETATM 9131 O  O   . HOH F 6 .    ? 56.286 65.132  -36.283 1.00 20.32 ? 2657 HOH A O   1 
HETATM 9132 O  O   . HOH F 6 .    ? 17.889 66.074  28.004  1.00 24.25 ? 2658 HOH A O   1 
HETATM 9133 O  O   . HOH F 6 .    ? 11.742 63.670  -16.917 1.00 22.23 ? 2659 HOH A O   1 
HETATM 9134 O  O   . HOH F 6 .    ? 35.564 86.326  -18.034 1.00 26.59 ? 2660 HOH A O   1 
HETATM 9135 O  O   . HOH F 6 .    ? 9.906  60.401  -20.414 1.00 26.88 ? 2661 HOH A O   1 
HETATM 9136 O  O   . HOH F 6 .    ? 11.605 48.713  -2.486  1.00 30.11 ? 2662 HOH A O   1 
HETATM 9137 O  O   . HOH F 6 .    ? 40.027 52.873  36.393  1.00 28.54 ? 2663 HOH A O   1 
HETATM 9138 O  O   . HOH F 6 .    ? 49.996 47.467  28.986  1.00 20.64 ? 2664 HOH A O   1 
HETATM 9139 O  O   . HOH F 6 .    ? 24.133 34.421  15.511  1.00 27.51 ? 2665 HOH A O   1 
HETATM 9140 O  O   . HOH F 6 .    ? 59.627 50.955  24.836  1.00 26.00 ? 2666 HOH A O   1 
HETATM 9141 O  O   . HOH F 6 .    ? 38.150 83.436  -1.198  1.00 26.61 ? 2667 HOH A O   1 
HETATM 9142 O  O   . HOH F 6 .    ? 12.928 51.712  -12.197 1.00 26.85 ? 2668 HOH A O   1 
HETATM 9143 O  O   . HOH F 6 .    ? 48.349 50.936  35.193  1.00 29.09 ? 2669 HOH A O   1 
HETATM 9144 O  O   . HOH F 6 .    ? 48.186 41.633  -5.403  1.00 26.32 ? 2670 HOH A O   1 
HETATM 9145 O  O   . HOH F 6 .    ? 22.285 40.821  -11.279 1.00 22.03 ? 2671 HOH A O   1 
HETATM 9146 O  O   . HOH F 6 .    ? 16.234 36.430  16.395  1.00 30.41 ? 2672 HOH A O   1 
HETATM 9147 O  O   . HOH F 6 .    ? 22.449 68.253  20.504  1.00 24.57 ? 2673 HOH A O   1 
HETATM 9148 O  O   . HOH F 6 .    ? 40.970 85.290  -12.216 1.00 26.63 ? 2674 HOH A O   1 
HETATM 9149 O  O   . HOH F 6 .    ? 56.953 46.772  15.889  1.00 27.36 ? 2675 HOH A O   1 
HETATM 9150 O  O   . HOH F 6 .    ? 51.835 64.040  24.620  1.00 23.22 ? 2676 HOH A O   1 
HETATM 9151 O  O   . HOH F 6 .    ? 56.764 58.642  1.309   1.00 28.44 ? 2677 HOH A O   1 
HETATM 9152 O  O   . HOH F 6 .    ? 57.687 58.563  5.519   1.00 25.93 ? 2678 HOH A O   1 
HETATM 9153 O  O   . HOH F 6 .    ? 75.340 64.209  -16.396 1.00 29.94 ? 2679 HOH A O   1 
HETATM 9154 O  O   . HOH F 6 .    ? 14.698 70.633  -23.076 1.00 27.87 ? 2680 HOH A O   1 
HETATM 9155 O  O   . HOH F 6 .    ? 13.260 52.237  -15.050 1.00 28.78 ? 2681 HOH A O   1 
HETATM 9156 O  O   . HOH F 6 .    ? 23.280 86.953  -32.691 1.00 34.49 ? 2682 HOH A O   1 
HETATM 9157 O  O   . HOH F 6 .    ? 66.486 81.848  -14.304 1.00 27.58 ? 2683 HOH A O   1 
HETATM 9158 O  O   . HOH F 6 .    ? 47.466 61.517  -28.887 1.00 26.21 ? 2684 HOH A O   1 
HETATM 9159 O  O   . HOH F 6 .    ? 52.201 70.653  6.026   1.00 34.74 ? 2685 HOH A O   1 
HETATM 9160 O  O   . HOH F 6 .    ? 41.040 56.032  -33.316 1.00 26.34 ? 2686 HOH A O   1 
HETATM 9161 O  O   . HOH F 6 .    ? 39.902 39.846  20.057  1.00 31.43 ? 2687 HOH A O   1 
HETATM 9162 O  O   . HOH F 6 .    ? 44.350 55.683  36.173  1.00 36.73 ? 2688 HOH A O   1 
HETATM 9163 O  O   . HOH F 6 .    ? 13.811 62.535  14.629  1.00 28.97 ? 2689 HOH A O   1 
HETATM 9164 O  O   . HOH F 6 .    ? 40.111 39.799  -0.354  1.00 22.69 ? 2690 HOH A O   1 
HETATM 9165 O  O   . HOH F 6 .    ? 27.076 41.707  -27.616 1.00 33.54 ? 2691 HOH A O   1 
HETATM 9166 O  O   . HOH F 6 .    ? 19.888 41.661  -4.987  1.00 27.16 ? 2692 HOH A O   1 
HETATM 9167 O  O   . HOH F 6 .    ? 13.717 60.800  7.705   1.00 26.28 ? 2693 HOH A O   1 
HETATM 9168 O  O   . HOH F 6 .    ? 47.110 46.059  11.429  1.00 33.54 ? 2694 HOH A O   1 
HETATM 9169 O  O   . HOH F 6 .    ? 43.088 68.593  -30.103 1.00 30.08 ? 2695 HOH A O   1 
HETATM 9170 O  O   . HOH F 6 .    ? 47.864 69.982  -16.733 1.00 31.92 ? 2696 HOH A O   1 
HETATM 9171 O  O   . HOH F 6 .    ? 58.932 93.492  -27.329 1.00 36.23 ? 2697 HOH A O   1 
HETATM 9172 O  O   . HOH F 6 .    ? 31.490 79.227  -43.027 1.00 28.04 ? 2698 HOH A O   1 
HETATM 9173 O  O   . HOH F 6 .    ? 22.252 42.830  -13.257 1.00 25.52 ? 2699 HOH A O   1 
HETATM 9174 O  O   . HOH F 6 .    ? 52.794 92.141  -23.498 1.00 30.99 ? 2700 HOH A O   1 
HETATM 9175 O  O   . HOH F 6 .    ? 60.507 50.955  20.360  1.00 29.96 ? 2701 HOH A O   1 
HETATM 9176 O  O   . HOH F 6 .    ? 19.642 58.674  -36.930 1.00 25.91 ? 2702 HOH A O   1 
HETATM 9177 O  O   . HOH F 6 .    ? 26.299 66.969  19.972  1.00 28.43 ? 2703 HOH A O   1 
HETATM 9178 O  O   . HOH F 6 .    ? 11.727 41.467  19.738  1.00 29.68 ? 2704 HOH A O   1 
HETATM 9179 O  O   . HOH F 6 .    ? 69.427 77.115  -34.242 1.00 30.14 ? 2705 HOH A O   1 
HETATM 9180 O  O   . HOH F 6 .    ? 16.625 42.915  -2.531  1.00 29.23 ? 2706 HOH A O   1 
HETATM 9181 O  O   . HOH F 6 .    ? 34.628 66.189  -42.649 1.00 34.48 ? 2707 HOH A O   1 
HETATM 9182 O  O   . HOH F 6 .    ? 57.343 35.995  -14.292 1.00 30.95 ? 2708 HOH A O   1 
HETATM 9183 O  O   . HOH F 6 .    ? 37.354 37.614  2.880   1.00 34.95 ? 2709 HOH A O   1 
HETATM 9184 O  O   . HOH F 6 .    ? 51.463 66.713  8.470   1.00 24.00 ? 2710 HOH A O   1 
HETATM 9185 O  O   . HOH F 6 .    ? 10.749 51.479  21.361  1.00 24.99 ? 2711 HOH A O   1 
HETATM 9186 O  O   . HOH F 6 .    ? 30.367 87.284  -15.077 1.00 26.05 ? 2712 HOH A O   1 
HETATM 9187 O  O   . HOH F 6 .    ? 41.883 54.899  -17.322 1.00 27.69 ? 2713 HOH A O   1 
HETATM 9188 O  O   . HOH F 6 .    ? 48.442 76.586  8.260   1.00 35.37 ? 2714 HOH A O   1 
HETATM 9189 O  O   . HOH F 6 .    ? 29.838 75.647  11.013  1.00 29.39 ? 2715 HOH A O   1 
HETATM 9190 O  O   . HOH F 6 .    ? 43.222 98.126  -37.334 1.00 31.39 ? 2716 HOH A O   1 
HETATM 9191 O  O   . HOH F 6 .    ? 64.760 78.732  -1.694  1.00 27.28 ? 2717 HOH A O   1 
HETATM 9192 O  O   . HOH F 6 .    ? 43.403 40.614  -23.039 1.00 29.47 ? 2718 HOH A O   1 
HETATM 9193 O  O   . HOH F 6 .    ? 59.655 49.071  2.226   1.00 32.77 ? 2719 HOH A O   1 
HETATM 9194 O  O   . HOH F 6 .    ? 69.041 41.692  -17.172 1.00 38.36 ? 2720 HOH A O   1 
HETATM 9195 O  O   . HOH F 6 .    ? 24.724 71.763  -39.909 1.00 25.01 ? 2721 HOH A O   1 
HETATM 9196 O  O   . HOH F 6 .    ? 24.030 48.492  -24.253 1.00 33.96 ? 2722 HOH A O   1 
HETATM 9197 O  O   . HOH F 6 .    ? 47.111 68.306  -24.613 1.00 22.72 ? 2723 HOH A O   1 
HETATM 9198 O  O   . HOH F 6 .    ? 53.530 53.463  -30.182 1.00 27.95 ? 2724 HOH A O   1 
HETATM 9199 O  O   . HOH F 6 .    ? 24.612 34.494  35.817  1.00 33.37 ? 2725 HOH A O   1 
HETATM 9200 O  O   . HOH F 6 .    ? 13.157 52.449  25.926  1.00 32.58 ? 2726 HOH A O   1 
HETATM 9201 O  O   . HOH F 6 .    ? 51.861 44.556  3.124   1.00 21.52 ? 2727 HOH A O   1 
HETATM 9202 O  O   . HOH F 6 .    ? 21.686 55.357  40.157  1.00 29.94 ? 2728 HOH A O   1 
HETATM 9203 O  O   . HOH F 6 .    ? 64.269 70.716  -5.328  1.00 17.97 ? 2729 HOH A O   1 
HETATM 9204 O  O   . HOH F 6 .    ? 47.126 89.642  -23.451 1.00 39.50 ? 2730 HOH A O   1 
HETATM 9205 O  O   . HOH F 6 .    ? 8.123  53.213  -7.723  1.00 32.34 ? 2731 HOH A O   1 
HETATM 9206 O  O   . HOH F 6 .    ? 22.262 80.938  -42.537 1.00 30.46 ? 2732 HOH A O   1 
HETATM 9207 O  O   . HOH F 6 .    ? 64.090 65.445  -30.287 1.00 31.27 ? 2733 HOH A O   1 
HETATM 9208 O  O   . HOH F 6 .    ? 18.461 48.666  -19.844 1.00 39.43 ? 2734 HOH A O   1 
HETATM 9209 O  O   . HOH F 6 .    ? 59.375 76.982  -4.214  1.00 35.03 ? 2735 HOH A O   1 
HETATM 9210 O  O   . HOH F 6 .    ? 21.075 84.066  -12.388 1.00 33.91 ? 2736 HOH A O   1 
HETATM 9211 O  O   . HOH F 6 .    ? 19.446 52.181  -31.364 1.00 36.66 ? 2737 HOH A O   1 
HETATM 9212 O  O   . HOH F 6 .    ? 67.402 85.542  -36.151 1.00 41.60 ? 2738 HOH A O   1 
HETATM 9213 O  O   . HOH F 6 .    ? 29.671 75.056  22.367  1.00 24.96 ? 2739 HOH A O   1 
HETATM 9214 O  O   . HOH F 6 .    ? 32.897 84.372  0.381   1.00 27.96 ? 2740 HOH A O   1 
HETATM 9215 O  O   . HOH F 6 .    ? 12.918 62.078  -2.359  1.00 26.02 ? 2741 HOH A O   1 
HETATM 9216 O  O   . HOH F 6 .    ? 25.794 63.153  13.602  1.00 33.22 ? 2742 HOH A O   1 
HETATM 9217 O  O   . HOH F 6 .    ? 28.249 34.879  32.302  1.00 33.78 ? 2743 HOH A O   1 
HETATM 9218 O  O   . HOH F 6 .    ? 35.946 68.551  23.923  1.00 32.66 ? 2744 HOH A O   1 
HETATM 9219 O  O   . HOH F 6 .    ? 32.014 33.730  17.150  1.00 30.70 ? 2745 HOH A O   1 
HETATM 9220 O  O   . HOH F 6 .    ? 41.563 84.437  -2.027  1.00 43.12 ? 2746 HOH A O   1 
HETATM 9221 O  O   . HOH F 6 .    ? 40.049 100.142 -31.941 1.00 39.02 ? 2747 HOH A O   1 
HETATM 9222 O  O   . HOH F 6 .    ? 54.075 82.756  -44.908 1.00 41.73 ? 2748 HOH A O   1 
HETATM 9223 O  O   . HOH F 6 .    ? 70.257 53.651  -10.190 1.00 29.58 ? 2749 HOH A O   1 
HETATM 9224 O  O   . HOH F 6 .    ? 12.405 64.627  -12.473 1.00 30.27 ? 2750 HOH A O   1 
HETATM 9225 O  O   . HOH F 6 .    ? 39.342 50.206  36.394  1.00 37.56 ? 2751 HOH A O   1 
HETATM 9226 O  O   . HOH F 6 .    ? 28.055 44.577  38.319  1.00 31.62 ? 2752 HOH A O   1 
HETATM 9227 O  O   . HOH F 6 .    ? 72.444 95.791  -31.498 1.00 31.52 ? 2753 HOH A O   1 
HETATM 9228 O  O   . HOH F 6 .    ? 21.682 48.919  -38.935 1.00 39.36 ? 2754 HOH A O   1 
HETATM 9229 O  O   . HOH F 6 .    ? 20.994 31.667  31.559  1.00 41.11 ? 2755 HOH A O   1 
HETATM 9230 O  O   . HOH F 6 .    ? 42.760 47.378  -27.371 1.00 35.37 ? 2756 HOH A O   1 
HETATM 9231 O  O   . HOH F 6 .    ? 55.948 52.080  27.496  1.00 24.95 ? 2757 HOH A O   1 
HETATM 9232 O  O   . HOH F 6 .    ? 31.104 58.278  -40.350 1.00 35.88 ? 2758 HOH A O   1 
HETATM 9233 O  O   . HOH F 6 .    ? 62.159 81.550  -44.466 1.00 35.28 ? 2759 HOH A O   1 
HETATM 9234 O  O   . HOH F 6 .    ? 7.543  54.573  17.338  1.00 35.17 ? 2760 HOH A O   1 
HETATM 9235 O  O   . HOH F 6 .    ? 17.998 41.755  25.361  1.00 34.70 ? 2761 HOH A O   1 
HETATM 9236 O  O   . HOH F 6 .    ? 39.087 53.164  2.231   1.00 36.07 ? 2762 HOH A O   1 
HETATM 9237 O  O   . HOH F 6 .    ? 4.275  56.541  -6.412  1.00 28.47 ? 2763 HOH A O   1 
HETATM 9238 O  O   . HOH F 6 .    ? 22.147 76.819  8.815   1.00 29.93 ? 2764 HOH A O   1 
HETATM 9239 O  O   . HOH F 6 .    ? 25.875 87.979  -42.861 1.00 35.45 ? 2765 HOH A O   1 
HETATM 9240 O  O   . HOH F 6 .    ? 10.817 62.583  -12.144 1.00 31.71 ? 2766 HOH A O   1 
HETATM 9241 O  O   . HOH F 6 .    ? 44.571 71.997  -44.792 1.00 41.86 ? 2767 HOH A O   1 
HETATM 9242 O  O   . HOH F 6 .    ? 37.261 40.062  26.370  1.00 37.04 ? 2768 HOH A O   1 
HETATM 9243 O  O   . HOH F 6 .    ? 23.305 88.909  -37.872 1.00 32.92 ? 2769 HOH A O   1 
HETATM 9244 O  O   . HOH F 6 .    ? 70.134 62.867  -24.024 1.00 33.67 ? 2770 HOH A O   1 
HETATM 9245 O  O   . HOH F 6 .    ? 22.821 64.389  18.369  1.00 30.51 ? 2771 HOH A O   1 
HETATM 9246 O  O   . HOH F 6 .    ? 67.139 38.370  -9.800  1.00 31.63 ? 2772 HOH A O   1 
HETATM 9247 O  O   . HOH F 6 .    ? 65.707 88.171  -41.100 1.00 44.85 ? 2773 HOH A O   1 
HETATM 9248 O  O   . HOH F 6 .    ? 13.328 45.030  29.497  1.00 47.44 ? 2774 HOH A O   1 
HETATM 9249 O  O   . HOH F 6 .    ? 13.410 48.434  1.619   1.00 31.48 ? 2775 HOH A O   1 
HETATM 9250 O  O   . HOH F 6 .    ? 55.510 69.136  -37.839 1.00 28.64 ? 2776 HOH A O   1 
HETATM 9251 O  O   . HOH F 6 .    ? 27.004 47.653  -23.859 1.00 30.39 ? 2777 HOH A O   1 
HETATM 9252 O  O   . HOH F 6 .    ? 69.986 82.063  -34.131 1.00 38.71 ? 2778 HOH A O   1 
HETATM 9253 O  O   . HOH F 6 .    ? 11.935 62.152  23.023  1.00 37.56 ? 2779 HOH A O   1 
HETATM 9254 O  O   . HOH F 6 .    ? 31.135 29.795  5.577   1.00 42.21 ? 2780 HOH A O   1 
HETATM 9255 O  O   . HOH F 6 .    ? 19.187 36.514  22.577  1.00 36.89 ? 2781 HOH A O   1 
HETATM 9256 O  O   . HOH F 6 .    ? 27.834 86.429  -14.735 1.00 30.63 ? 2782 HOH A O   1 
HETATM 9257 O  O   . HOH F 6 .    ? 66.068 50.498  0.269   1.00 32.66 ? 2783 HOH A O   1 
HETATM 9258 O  O   . HOH F 6 .    ? 28.302 63.867  14.007  1.00 29.50 ? 2784 HOH A O   1 
HETATM 9259 O  O   . HOH F 6 .    ? 52.560 72.616  18.401  1.00 26.14 ? 2785 HOH A O   1 
HETATM 9260 O  O   . HOH F 6 .    ? 47.156 75.081  -26.357 1.00 34.14 ? 2786 HOH A O   1 
HETATM 9261 O  O   . HOH F 6 .    ? 48.764 72.384  -26.287 1.00 27.45 ? 2787 HOH A O   1 
HETATM 9262 O  O   . HOH F 6 .    ? 60.150 68.758  -38.912 1.00 29.70 ? 2788 HOH A O   1 
HETATM 9263 O  O   . HOH F 6 .    ? 59.214 55.395  27.094  1.00 23.66 ? 2789 HOH A O   1 
HETATM 9264 O  O   . HOH F 6 .    ? 43.908 87.774  -16.065 1.00 45.79 ? 2790 HOH A O   1 
HETATM 9265 O  O   . HOH F 6 .    ? 13.963 58.296  16.304  1.00 15.95 ? 2791 HOH A O   1 
HETATM 9266 O  O   . HOH F 6 .    ? 13.969 57.695  19.061  1.00 19.95 ? 2792 HOH A O   1 
HETATM 9267 O  O   . HOH F 6 .    ? 28.167 39.676  11.289  1.00 13.20 ? 2793 HOH A O   1 
HETATM 9268 O  O   . HOH F 6 .    ? 28.956 81.954  -35.751 1.00 18.41 ? 2794 HOH A O   1 
HETATM 9269 O  O   . HOH F 6 .    ? 12.410 55.876  -15.173 1.00 20.70 ? 2795 HOH A O   1 
HETATM 9270 O  O   . HOH F 6 .    ? 81.806 67.157  -13.671 1.00 22.51 ? 2796 HOH A O   1 
HETATM 9271 O  O   . HOH F 6 .    ? 59.134 58.245  0.987   1.00 23.52 ? 2797 HOH A O   1 
HETATM 9272 O  O   . HOH F 6 .    ? 49.510 68.368  6.681   1.00 22.39 ? 2798 HOH A O   1 
HETATM 9273 O  O   . HOH F 6 .    ? 68.587 79.435  -28.695 1.00 20.37 ? 2799 HOH A O   1 
HETATM 9274 O  O   . HOH F 6 .    ? 26.052 32.811  28.686  1.00 27.04 ? 2800 HOH A O   1 
HETATM 9275 O  O   . HOH F 6 .    ? 32.735 69.320  24.750  1.00 24.31 ? 2801 HOH A O   1 
HETATM 9276 O  O   . HOH F 6 .    ? 28.054 102.488 -19.334 1.00 22.92 ? 2802 HOH A O   1 
HETATM 9277 O  O   . HOH F 6 .    ? 71.869 73.918  -29.360 1.00 25.64 ? 2803 HOH A O   1 
HETATM 9278 O  O   . HOH F 6 .    ? 79.503 50.728  -9.035  1.00 29.00 ? 2804 HOH A O   1 
HETATM 9279 O  O   . HOH F 6 .    ? 37.437 83.524  -4.035  1.00 28.09 ? 2805 HOH A O   1 
HETATM 9280 O  O   . HOH F 6 .    ? 59.563 52.106  2.512   1.00 24.80 ? 2806 HOH A O   1 
HETATM 9281 O  O   . HOH F 6 .    ? 19.829 84.446  -18.370 1.00 30.06 ? 2807 HOH A O   1 
HETATM 9282 O  O   . HOH F 6 .    ? 44.206 79.279  -21.538 1.00 30.45 ? 2808 HOH A O   1 
HETATM 9283 O  O   . HOH F 6 .    ? 58.086 52.876  26.233  1.00 26.59 ? 2809 HOH A O   1 
HETATM 9284 O  O   . HOH F 6 .    ? 17.094 57.424  -36.491 1.00 30.96 ? 2810 HOH A O   1 
HETATM 9285 O  O   . HOH F 6 .    ? 46.828 42.978  9.643   1.00 34.07 ? 2811 HOH A O   1 
HETATM 9286 O  O   . HOH F 6 .    ? 27.178 72.219  34.069  1.00 33.90 ? 2812 HOH A O   1 
HETATM 9287 O  O   . HOH F 6 .    ? 7.549  54.182  -10.270 1.00 27.09 ? 2813 HOH A O   1 
HETATM 9288 O  O   . HOH F 6 .    ? 50.057 46.849  -30.681 1.00 32.71 ? 2814 HOH A O   1 
HETATM 9289 O  O   . HOH F 6 .    ? 42.772 78.561  -29.811 1.00 33.08 ? 2815 HOH A O   1 
HETATM 9290 O  O   . HOH F 6 .    ? 27.735 88.999  -12.160 1.00 33.84 ? 2816 HOH A O   1 
HETATM 9291 O  O   . HOH F 6 .    ? 56.768 89.973  -43.828 1.00 34.66 ? 2817 HOH A O   1 
HETATM 9292 O  O   . HOH F 6 .    ? 13.962 44.705  26.965  1.00 32.91 ? 2818 HOH A O   1 
HETATM 9293 O  O   . HOH F 6 .    ? 69.509 83.887  -36.192 1.00 28.92 ? 2819 HOH A O   1 
HETATM 9294 O  O   . HOH F 6 .    ? 58.201 93.304  -25.011 1.00 27.14 ? 2820 HOH A O   1 
HETATM 9295 O  O   . HOH F 6 .    ? 46.191 39.893  -0.062  1.00 27.20 ? 2821 HOH A O   1 
HETATM 9296 O  O   . HOH F 6 .    ? 37.186 37.502  25.052  1.00 36.14 ? 2822 HOH A O   1 
HETATM 9297 O  O   . HOH F 6 .    ? 52.737 68.331  4.681   1.00 29.61 ? 2823 HOH A O   1 
HETATM 9298 O  O   . HOH F 6 .    ? 17.835 50.899  38.098  1.00 45.71 ? 2824 HOH A O   1 
HETATM 9299 O  O   . HOH F 6 .    ? 15.365 77.106  -13.642 1.00 33.99 ? 2825 HOH A O   1 
HETATM 9300 O  O   . HOH F 6 .    ? 20.103 39.763  -12.634 1.00 42.77 ? 2826 HOH A O   1 
HETATM 9301 O  O   . HOH F 6 .    ? 49.546 45.653  31.068  1.00 23.68 ? 2827 HOH A O   1 
HETATM 9302 O  O   . HOH F 6 .    ? 70.748 78.049  -26.330 1.00 24.48 ? 2828 HOH A O   1 
HETATM 9303 O  O   . HOH F 6 .    ? 58.587 52.852  4.773   1.00 23.81 ? 2829 HOH A O   1 
HETATM 9304 O  O   . HOH F 6 .    ? 35.171 55.333  -34.654 1.00 40.30 ? 2830 HOH A O   1 
HETATM 9305 O  O   . HOH F 6 .    ? 41.439 82.933  -28.993 1.00 27.16 ? 2831 HOH A O   1 
HETATM 9306 O  O   . HOH F 6 .    ? 47.741 66.192  26.914  1.00 29.38 ? 2832 HOH A O   1 
HETATM 9307 O  O   . HOH F 6 .    ? 39.881 81.856  -22.151 1.00 31.85 ? 2833 HOH A O   1 
HETATM 9308 O  O   . HOH F 6 .    ? 22.152 65.665  32.304  1.00 30.23 ? 2834 HOH A O   1 
HETATM 9309 O  O   . HOH F 6 .    ? 58.939 48.811  19.120  1.00 28.91 ? 2835 HOH A O   1 
HETATM 9310 O  O   . HOH F 6 .    ? 32.003 80.403  7.190   1.00 41.92 ? 2836 HOH A O   1 
HETATM 9311 O  O   . HOH F 6 .    ? 50.589 44.984  -24.853 1.00 24.30 ? 2837 HOH A O   1 
HETATM 9312 O  O   . HOH F 6 .    ? 62.519 60.834  0.434   1.00 29.64 ? 2838 HOH A O   1 
HETATM 9313 O  O   . HOH F 6 .    ? 68.127 75.211  -35.201 1.00 28.63 ? 2839 HOH A O   1 
HETATM 9314 O  O   . HOH F 6 .    ? 22.989 39.311  -15.338 1.00 36.94 ? 2840 HOH A O   1 
HETATM 9315 O  O   . HOH F 6 .    ? 36.441 93.979  -29.726 1.00 37.64 ? 2841 HOH A O   1 
HETATM 9316 O  O   . HOH F 6 .    ? 74.182 79.998  -11.027 1.00 41.74 ? 2842 HOH A O   1 
HETATM 9317 O  O   . HOH F 6 .    ? 41.278 81.839  -3.740  1.00 36.78 ? 2843 HOH A O   1 
HETATM 9318 O  O   . HOH F 6 .    ? 13.237 63.002  11.895  1.00 29.31 ? 2844 HOH A O   1 
HETATM 9319 O  O   . HOH F 6 .    ? 56.945 76.085  0.077   1.00 38.07 ? 2845 HOH A O   1 
HETATM 9320 O  O   . HOH F 6 .    ? 74.511 52.176  1.409   1.00 30.58 ? 2846 HOH A O   1 
HETATM 9321 O  O   . HOH F 6 .    ? 21.560 61.500  -34.734 1.00 27.43 ? 2847 HOH A O   1 
HETATM 9322 O  O   . HOH F 6 .    ? 17.109 41.871  32.173  1.00 33.64 ? 2848 HOH A O   1 
HETATM 9323 O  O   . HOH F 6 .    ? 10.201 62.930  -14.849 1.00 36.89 ? 2849 HOH A O   1 
HETATM 9324 O  O   . HOH F 6 .    ? 46.143 79.849  4.763   1.00 28.45 ? 2850 HOH A O   1 
HETATM 9325 O  O   . HOH F 6 .    ? 14.526 46.959  32.442  1.00 28.33 ? 2851 HOH A O   1 
HETATM 9326 O  O   . HOH F 6 .    ? 47.514 40.257  5.984   1.00 40.34 ? 2852 HOH A O   1 
HETATM 9327 O  O   . HOH F 6 .    ? 19.981 39.303  -3.745  1.00 37.06 ? 2853 HOH A O   1 
HETATM 9328 O  O   . HOH F 6 .    ? 25.906 58.982  -39.104 1.00 34.40 ? 2854 HOH A O   1 
HETATM 9329 O  O   . HOH F 6 .    ? 10.497 58.075  -20.856 1.00 33.22 ? 2855 HOH A O   1 
HETATM 9330 O  O   . HOH F 6 .    ? 8.694  56.693  16.286  1.00 37.17 ? 2856 HOH A O   1 
HETATM 9331 O  O   . HOH F 6 .    ? 78.217 72.364  -10.277 1.00 29.23 ? 2857 HOH A O   1 
HETATM 9332 O  O   . HOH F 6 .    ? 24.176 83.188  -4.033  1.00 40.30 ? 2858 HOH A O   1 
HETATM 9333 O  O   . HOH F 6 .    ? 35.331 62.352  34.123  1.00 29.92 ? 2859 HOH A O   1 
HETATM 9334 O  O   . HOH F 6 .    ? 27.005 90.294  -31.562 1.00 39.06 ? 2860 HOH A O   1 
HETATM 9335 O  O   . HOH F 6 .    ? 74.867 77.267  -20.573 1.00 34.32 ? 2861 HOH A O   1 
HETATM 9336 O  O   . HOH F 6 .    ? 49.124 41.835  8.240   1.00 31.52 ? 2862 HOH A O   1 
HETATM 9337 O  O   . HOH F 6 .    ? 44.999 92.694  -25.475 1.00 34.59 ? 2863 HOH A O   1 
HETATM 9338 O  O   . HOH F 6 .    ? 52.422 48.957  25.725  1.00 29.67 ? 2864 HOH A O   1 
HETATM 9339 O  O   . HOH F 6 .    ? 58.912 51.030  14.934  1.00 32.92 ? 2865 HOH A O   1 
HETATM 9340 O  O   . HOH F 6 .    ? 52.023 50.472  27.475  1.00 25.40 ? 2866 HOH A O   1 
HETATM 9341 O  O   . HOH F 6 .    ? 11.530 58.413  20.044  1.00 34.14 ? 2867 HOH A O   1 
HETATM 9342 O  O   . HOH F 6 .    ? 18.884 60.706  -38.038 1.00 24.45 ? 2868 HOH A O   1 
HETATM 9343 O  O   . HOH F 6 .    ? 45.684 60.137  -31.738 1.00 41.98 ? 2869 HOH A O   1 
HETATM 9344 O  O   . HOH F 6 .    ? 5.375  57.737  6.959   1.00 33.65 ? 2870 HOH A O   1 
HETATM 9345 O  O   . HOH F 6 .    ? 47.427 81.476  -17.125 1.00 24.15 ? 2871 HOH A O   1 
HETATM 9346 O  O   . HOH F 6 .    ? 28.896 69.628  12.567  1.00 37.87 ? 2872 HOH A O   1 
HETATM 9347 O  O   . HOH F 6 .    ? 31.778 72.172  13.605  1.00 34.98 ? 2873 HOH A O   1 
HETATM 9348 O  O   . HOH F 6 .    ? 25.664 66.125  17.259  1.00 35.33 ? 2874 HOH A O   1 
HETATM 9349 O  O   . HOH F 6 .    ? 78.913 62.575  -23.064 1.00 38.05 ? 2875 HOH A O   1 
HETATM 9350 O  O   . HOH F 6 .    ? 29.724 66.204  10.792  1.00 25.98 ? 2876 HOH A O   1 
HETATM 9351 O  O   . HOH F 6 .    ? 28.683 63.592  10.971  1.00 26.76 ? 2877 HOH A O   1 
HETATM 9352 O  O   . HOH F 6 .    ? 33.819 68.708  13.644  1.00 21.68 ? 2878 HOH A O   1 
HETATM 9353 O  O   . HOH F 6 .    ? 24.317 63.448  11.653  1.00 32.62 ? 2879 HOH A O   1 
HETATM 9354 O  O   . HOH F 6 .    ? 33.480 68.792  17.492  1.00 38.34 ? 2880 HOH A O   1 
HETATM 9355 O  O   . HOH F 6 .    ? 37.540 59.040  11.097  1.00 15.17 ? 2881 HOH A O   1 
HETATM 9356 O  O   . HOH F 6 .    ? 26.666 75.005  2.197   1.00 20.92 ? 2882 HOH A O   1 
HETATM 9357 O  O   . HOH F 6 .    ? 24.806 33.089  6.523   1.00 25.27 ? 2883 HOH A O   1 
HETATM 9358 O  O   . HOH F 6 .    ? 53.674 66.538  6.953   1.00 28.68 ? 2884 HOH A O   1 
HETATM 9359 O  O   . HOH F 6 .    ? 39.009 86.662  -41.619 1.00 27.46 ? 2885 HOH A O   1 
HETATM 9360 O  O   . HOH F 6 .    ? 52.596 45.543  -27.366 1.00 33.03 ? 2886 HOH A O   1 
HETATM 9361 O  O   . HOH F 6 .    ? 52.053 69.291  9.512   1.00 30.96 ? 2887 HOH A O   1 
HETATM 9362 O  O   . HOH F 6 .    ? 56.537 66.924  5.350   1.00 33.77 ? 2888 HOH A O   1 
HETATM 9363 O  O   . HOH F 6 .    ? 74.043 54.098  -13.901 1.00 40.32 ? 2889 HOH A O   1 
HETATM 9364 O  O   . HOH F 6 .    ? 47.415 41.394  -14.883 1.00 24.85 ? 2890 HOH A O   1 
HETATM 9365 O  O   . HOH F 6 .    ? 39.089 60.486  11.794  1.00 25.44 ? 2891 HOH A O   1 
HETATM 9366 O  O   . HOH F 6 .    ? 38.823 80.418  -3.347  1.00 26.04 ? 2892 HOH A O   1 
HETATM 9367 O  O   . HOH F 6 .    ? 47.561 78.433  11.524  1.00 30.09 ? 2893 HOH A O   1 
HETATM 9368 O  O   . HOH F 6 .    ? 34.897 66.317  12.449  1.00 22.93 ? 2894 HOH A O   1 
HETATM 9369 O  O   . HOH F 6 .    ? 27.214 65.346  9.198   1.00 27.13 ? 2895 HOH A O   1 
HETATM 9370 O  O   . HOH F 6 .    ? 75.598 73.842  -16.298 1.00 33.50 ? 2896 HOH A O   1 
HETATM 9371 O  O   . HOH F 6 .    ? 30.160 59.207  35.312  1.00 29.59 ? 2897 HOH A O   1 
HETATM 9372 O  O   . HOH F 6 .    ? 43.472 64.536  -31.451 1.00 28.04 ? 2898 HOH A O   1 
HETATM 9373 O  O   . HOH F 6 .    ? 14.717 55.064  -26.397 1.00 32.71 ? 2899 HOH A O   1 
HETATM 9374 O  O   . HOH F 6 .    ? 70.334 60.453  -23.330 1.00 33.40 ? 2900 HOH A O   1 
HETATM 9375 O  O   . HOH F 6 .    ? 63.563 59.689  17.038  1.00 29.62 ? 2901 HOH A O   1 
HETATM 9376 O  O   . HOH F 6 .    ? 28.905 64.516  30.233  1.00 25.09 ? 2902 HOH A O   1 
HETATM 9377 O  O   . HOH F 6 .    ? 7.920  81.178  -4.292  1.00 31.00 ? 2903 HOH A O   1 
HETATM 9378 O  O   . HOH F 6 .    ? 56.160 53.500  29.837  1.00 34.93 ? 2904 HOH A O   1 
HETATM 9379 O  O   . HOH F 6 .    ? 49.823 41.011  1.304   1.00 31.17 ? 2905 HOH A O   1 
HETATM 9380 O  O   . HOH F 6 .    ? 15.512 73.742  5.380   1.00 31.66 ? 2906 HOH A O   1 
HETATM 9381 O  O   . HOH F 6 .    ? 38.366 73.838  18.211  1.00 28.02 ? 2907 HOH A O   1 
HETATM 9382 O  O   . HOH F 6 .    ? 49.476 46.029  26.618  1.00 34.09 ? 2908 HOH A O   1 
HETATM 9383 O  O   . HOH F 6 .    ? 50.171 58.456  -31.147 1.00 32.36 ? 2909 HOH A O   1 
HETATM 9384 O  O   . HOH F 6 .    ? 17.824 66.596  30.737  1.00 33.28 ? 2910 HOH A O   1 
HETATM 9385 O  O   . HOH F 6 .    ? 60.512 91.189  -31.408 1.00 30.73 ? 2911 HOH A O   1 
HETATM 9386 O  O   . HOH F 6 .    ? 18.296 36.782  5.881   1.00 32.74 ? 2912 HOH A O   1 
HETATM 9387 O  O   . HOH F 6 .    ? 36.068 63.572  -34.005 1.00 32.90 ? 2913 HOH A O   1 
HETATM 9388 O  O   . HOH F 6 .    ? 59.941 45.458  16.370  1.00 40.74 ? 2914 HOH A O   1 
HETATM 9389 O  O   . HOH F 6 .    ? 35.529 85.138  -0.937  1.00 35.28 ? 2915 HOH A O   1 
HETATM 9390 O  O   . HOH F 6 .    ? 46.383 70.511  -39.858 1.00 31.17 ? 2916 HOH A O   1 
HETATM 9391 O  O   . HOH F 6 .    ? 42.403 68.990  26.280  1.00 35.34 ? 2917 HOH A O   1 
HETATM 9392 O  O   . HOH F 6 .    ? 57.682 49.327  16.594  1.00 28.55 ? 2918 HOH A O   1 
HETATM 9393 O  O   . HOH F 6 .    ? 45.489 71.897  -25.972 1.00 28.07 ? 2919 HOH A O   1 
HETATM 9394 O  O   . HOH F 6 .    ? 5.324  81.191  -3.335  1.00 35.73 ? 2920 HOH A O   1 
HETATM 9395 O  O   . HOH F 6 .    ? 53.990 40.764  -20.635 1.00 35.36 ? 2921 HOH A O   1 
HETATM 9396 O  O   . HOH F 6 .    ? 31.952 96.832  -27.393 1.00 32.12 ? 2922 HOH A O   1 
HETATM 9397 O  O   . HOH F 6 .    ? 21.876 47.112  -34.474 1.00 39.11 ? 2923 HOH A O   1 
HETATM 9398 O  O   . HOH F 6 .    ? 61.547 68.870  -41.559 1.00 37.94 ? 2924 HOH A O   1 
HETATM 9399 O  O   . HOH F 6 .    ? 29.569 102.300 -16.665 1.00 33.49 ? 2925 HOH A O   1 
HETATM 9400 O  O   . HOH F 6 .    ? 26.260 57.603  40.498  1.00 39.31 ? 2926 HOH A O   1 
HETATM 9401 O  O   . HOH F 6 .    ? 65.406 41.458  -20.938 1.00 34.25 ? 2927 HOH A O   1 
HETATM 9402 O  O   . HOH F 6 .    ? 44.388 40.886  7.809   1.00 36.96 ? 2928 HOH A O   1 
HETATM 9403 O  O   . HOH F 6 .    ? 56.790 69.988  -39.703 1.00 34.55 ? 2929 HOH A O   1 
HETATM 9404 O  O   . HOH F 6 .    ? 36.163 70.349  19.258  1.00 32.10 ? 2930 HOH A O   1 
HETATM 9405 O  O   . HOH F 6 .    ? 55.361 68.561  3.449   1.00 38.95 ? 2931 HOH A O   1 
HETATM 9406 O  O   . HOH F 6 .    ? 65.746 77.522  2.889   1.00 36.96 ? 2932 HOH A O   1 
HETATM 9407 O  O   . HOH F 6 .    ? 57.004 39.057  -19.461 1.00 29.86 ? 2933 HOH A O   1 
HETATM 9408 O  O   . HOH F 6 .    ? 24.619 33.071  9.548   1.00 31.15 ? 2934 HOH A O   1 
HETATM 9409 O  O   . HOH F 6 .    ? 50.089 79.975  -11.194 1.00 38.33 ? 2935 HOH A O   1 
HETATM 9410 O  O   . HOH F 6 .    ? 7.206  51.512  9.321   1.00 39.30 ? 2936 HOH A O   1 
HETATM 9411 O  O   . HOH F 6 .    ? 36.303 78.740  11.618  1.00 33.66 ? 2937 HOH A O   1 
HETATM 9412 O  O   . HOH F 6 .    ? 51.837 41.101  -13.148 1.00 32.29 ? 2938 HOH A O   1 
HETATM 9413 O  O   . HOH F 6 .    ? 34.214 86.799  -43.811 1.00 35.69 ? 2939 HOH A O   1 
HETATM 9414 O  O   . HOH F 6 .    ? 67.865 77.315  -38.769 1.00 39.48 ? 2940 HOH A O   1 
HETATM 9415 O  O   . HOH F 6 .    ? 25.788 36.335  -15.435 1.00 30.29 ? 2941 HOH A O   1 
HETATM 9416 O  O   . HOH F 6 .    ? 36.734 70.958  16.696  1.00 35.84 ? 2942 HOH A O   1 
HETATM 9417 O  O   . HOH F 6 .    ? 68.815 57.253  -21.945 1.00 31.23 ? 2943 HOH A O   1 
HETATM 9418 O  O   . HOH F 6 .    ? 47.609 100.022 -33.100 1.00 36.10 ? 2944 HOH A O   1 
HETATM 9419 O  O   . HOH F 6 .    ? 60.391 51.439  6.231   1.00 31.36 ? 2945 HOH A O   1 
HETATM 9420 O  O   . HOH F 6 .    ? 50.034 50.129  36.929  1.00 34.09 ? 2946 HOH A O   1 
HETATM 9421 O  O   . HOH F 6 .    ? 29.582 35.077  -16.428 1.00 32.06 ? 2947 HOH A O   1 
HETATM 9422 O  O   . HOH F 6 .    ? 19.128 81.488  -27.393 1.00 44.32 ? 2948 HOH A O   1 
HETATM 9423 O  O   . HOH F 6 .    ? 44.844 80.665  12.626  1.00 37.48 ? 2949 HOH A O   1 
HETATM 9424 O  O   . HOH F 6 .    ? 59.731 68.674  16.454  1.00 32.60 ? 2950 HOH A O   1 
HETATM 9425 O  O   . HOH F 6 .    ? 20.460 50.901  -37.936 1.00 35.62 ? 2951 HOH A O   1 
HETATM 9426 O  O   . HOH F 6 .    ? 43.838 42.911  -24.763 1.00 34.09 ? 2952 HOH A O   1 
HETATM 9427 O  O   . HOH F 6 .    ? 49.708 62.058  -33.921 1.00 31.00 ? 2953 HOH A O   1 
HETATM 9428 O  O   . HOH F 6 .    ? 47.746 43.804  30.411  1.00 35.89 ? 2954 HOH A O   1 
HETATM 9429 O  O   . HOH F 6 .    ? 23.863 65.491  -43.783 1.00 40.64 ? 2955 HOH A O   1 
HETATM 9430 O  O   . HOH F 6 .    ? 35.497 73.698  15.123  1.00 35.23 ? 2956 HOH A O   1 
HETATM 9431 O  O   . HOH F 6 .    ? 22.119 34.667  12.587  1.00 39.44 ? 2957 HOH A O   1 
HETATM 9432 O  O   . HOH F 6 .    ? 68.242 88.189  -35.363 1.00 34.15 ? 2958 HOH A O   1 
HETATM 9433 O  O   . HOH F 6 .    ? 49.702 84.148  -19.116 1.00 33.22 ? 2959 HOH A O   1 
HETATM 9434 O  O   . HOH F 6 .    ? 60.870 46.828  -22.453 1.00 35.64 ? 2960 HOH A O   1 
HETATM 9435 O  O   . HOH F 6 .    ? 14.381 47.264  26.969  1.00 42.74 ? 2961 HOH A O   1 
HETATM 9436 O  O   . HOH F 6 .    ? 23.467 87.287  -16.506 1.00 39.43 ? 2962 HOH A O   1 
HETATM 9437 O  O   . HOH F 6 .    ? 34.961 36.652  3.404   1.00 33.75 ? 2963 HOH A O   1 
HETATM 9438 O  O   . HOH F 6 .    ? 11.404 62.251  5.266   1.00 42.79 ? 2964 HOH A O   1 
HETATM 9439 O  O   . HOH F 6 .    ? 58.768 43.997  -28.135 1.00 31.96 ? 2965 HOH A O   1 
HETATM 9440 O  O   . HOH F 6 .    ? 63.937 57.132  0.928   1.00 32.70 ? 2966 HOH A O   1 
HETATM 9441 O  O   . HOH F 6 .    ? 75.630 75.951  -5.990  1.00 41.49 ? 2967 HOH A O   1 
HETATM 9442 O  O   . HOH F 6 .    ? 12.163 47.372  31.355  1.00 36.21 ? 2968 HOH A O   1 
HETATM 9443 O  O   . HOH F 6 .    ? 45.770 56.542  -32.759 1.00 34.77 ? 2969 HOH A O   1 
HETATM 9444 O  O   . HOH F 6 .    ? 74.676 60.169  -9.674  1.00 34.26 ? 2970 HOH A O   1 
HETATM 9445 O  O   . HOH F 6 .    ? 60.845 80.116  -12.161 1.00 31.81 ? 2971 HOH A O   1 
HETATM 9446 O  O   . HOH F 6 .    ? 22.571 59.752  38.353  1.00 44.01 ? 2972 HOH A O   1 
HETATM 9447 O  O   . HOH F 6 .    ? 64.305 49.566  -21.859 1.00 42.05 ? 2973 HOH A O   1 
HETATM 9448 O  O   . HOH F 6 .    ? 38.283 87.030  -16.960 1.00 37.23 ? 2974 HOH A O   1 
HETATM 9449 O  O   . HOH F 6 .    ? 58.353 64.756  26.709  1.00 35.31 ? 2975 HOH A O   1 
HETATM 9450 O  O   . HOH F 6 .    ? 36.505 65.905  22.309  1.00 33.61 ? 2976 HOH A O   1 
HETATM 9451 O  O   . HOH F 6 .    ? 43.616 81.114  -25.380 1.00 39.65 ? 2977 HOH A O   1 
HETATM 9452 O  O   . HOH F 6 .    ? 52.032 71.558  22.131  1.00 33.73 ? 2978 HOH A O   1 
HETATM 9453 O  O   . HOH F 6 .    ? 22.210 35.155  35.051  1.00 39.20 ? 2979 HOH A O   1 
HETATM 9454 O  O   . HOH F 6 .    ? 61.044 61.464  13.657  1.00 34.19 ? 2980 HOH A O   1 
HETATM 9455 O  O   . HOH F 6 .    ? 16.132 30.998  18.139  1.00 42.47 ? 2981 HOH A O   1 
HETATM 9456 O  O   . HOH F 6 .    ? 62.894 82.809  -17.401 1.00 35.68 ? 2982 HOH A O   1 
HETATM 9457 O  O   . HOH F 6 .    ? 40.790 36.448  8.709   1.00 34.51 ? 2983 HOH A O   1 
HETATM 9458 O  O   . HOH F 6 .    ? 26.302 75.095  10.877  1.00 39.23 ? 2984 HOH A O   1 
HETATM 9459 O  O   . HOH F 6 .    ? 25.300 34.582  -7.029  1.00 41.50 ? 2985 HOH A O   1 
HETATM 9460 O  O   . HOH F 6 .    ? 29.806 66.902  16.214  1.00 47.51 ? 2986 HOH A O   1 
HETATM 9461 O  O   . HOH F 6 .    ? 69.488 63.845  2.037   1.00 41.51 ? 2987 HOH A O   1 
HETATM 9462 O  O   . HOH F 6 .    ? 18.972 39.661  26.387  1.00 34.36 ? 2988 HOH A O   1 
HETATM 9463 O  O   . HOH F 6 .    ? 24.665 87.320  -1.007  1.00 40.38 ? 2989 HOH A O   1 
HETATM 9464 O  O   . HOH F 6 .    ? 43.995 55.115  -26.876 1.00 30.63 ? 2990 HOH A O   1 
HETATM 9465 O  O   . HOH F 6 .    ? 15.153 69.909  24.297  1.00 37.07 ? 2991 HOH A O   1 
HETATM 9466 O  O   . HOH F 6 .    ? 18.687 37.617  19.691  1.00 33.23 ? 2992 HOH A O   1 
HETATM 9467 O  O   . HOH F 6 .    ? 50.953 90.903  -21.719 1.00 36.60 ? 2993 HOH A O   1 
HETATM 9468 O  O   . HOH F 6 .    ? 36.974 35.913  -18.633 1.00 41.17 ? 2994 HOH A O   1 
HETATM 9469 O  O   . HOH F 6 .    ? 45.237 58.143  32.357  1.00 40.35 ? 2995 HOH A O   1 
HETATM 9470 O  O   . HOH F 6 .    ? 62.919 44.707  -0.555  1.00 33.95 ? 2996 HOH A O   1 
HETATM 9471 O  O   . HOH F 6 .    ? 17.888 35.221  13.263  1.00 40.72 ? 2997 HOH A O   1 
HETATM 9472 O  O   . HOH F 6 .    ? 26.781 99.057  -26.516 1.00 36.37 ? 2998 HOH A O   1 
HETATM 9473 O  O   . HOH F 6 .    ? 27.324 30.885  30.574  1.00 41.71 ? 2999 HOH A O   1 
HETATM 9474 O  O   . HOH F 6 .    ? 56.140 49.294  27.242  1.00 36.73 ? 3000 HOH A O   1 
HETATM 9475 O  O   . HOH F 6 .    ? 38.627 54.335  -17.591 1.00 34.75 ? 3001 HOH A O   1 
HETATM 9476 O  O   . HOH F 6 .    ? 75.338 52.547  -15.873 1.00 36.46 ? 3002 HOH A O   1 
HETATM 9477 O  O   . HOH F 6 .    ? 13.989 88.294  -20.142 1.00 34.32 ? 3003 HOH A O   1 
HETATM 9478 O  O   . HOH F 6 .    ? 25.698 88.026  -15.946 1.00 38.75 ? 3004 HOH A O   1 
HETATM 9479 O  O   . HOH F 6 .    ? 63.951 45.636  -3.064  1.00 38.78 ? 3005 HOH A O   1 
HETATM 9480 O  O   . HOH F 6 .    ? 44.698 76.233  -28.476 1.00 39.79 ? 3006 HOH A O   1 
HETATM 9481 O  O   . HOH F 6 .    ? 73.741 63.138  -0.760  1.00 37.81 ? 3007 HOH A O   1 
HETATM 9482 O  O   . HOH F 6 .    ? 19.430 50.425  -23.654 1.00 37.08 ? 3008 HOH A O   1 
HETATM 9483 O  O   . HOH F 6 .    ? 58.459 37.353  -17.931 1.00 39.94 ? 3009 HOH A O   1 
HETATM 9484 O  O   . HOH F 6 .    ? 16.137 53.241  -25.741 1.00 47.38 ? 3010 HOH A O   1 
HETATM 9485 O  O   . HOH F 6 .    ? 46.143 94.994  -37.779 1.00 38.67 ? 3011 HOH A O   1 
HETATM 9486 O  O   . HOH F 6 .    ? 22.315 68.120  -40.183 1.00 33.90 ? 3012 HOH A O   1 
HETATM 9487 O  O   . HOH F 6 .    ? 41.981 58.443  34.644  1.00 38.65 ? 3013 HOH A O   1 
HETATM 9488 O  O   . HOH F 6 .    ? 63.875 82.665  -14.647 1.00 33.69 ? 3014 HOH A O   1 
HETATM 9489 O  O   . HOH F 6 .    ? 27.716 39.699  -24.784 1.00 46.79 ? 3015 HOH A O   1 
HETATM 9490 O  O   . HOH F 6 .    ? 58.113 48.468  25.584  1.00 44.48 ? 3016 HOH A O   1 
HETATM 9491 O  O   . HOH F 6 .    ? 19.585 81.732  -42.485 1.00 39.07 ? 3017 HOH A O   1 
HETATM 9492 O  O   . HOH F 6 .    ? 36.182 42.260  -26.732 1.00 43.68 ? 3018 HOH A O   1 
HETATM 9493 O  O   . HOH F 6 .    ? 60.521 54.397  14.909  1.00 28.49 ? 3019 HOH A O   1 
HETATM 9494 O  O   . HOH F 6 .    ? 29.483 41.176  -25.686 1.00 25.27 ? 3020 HOH A O   1 
HETATM 9495 O  O   . HOH F 6 .    ? 10.158 58.118  -3.251  1.00 30.26 ? 3021 HOH A O   1 
HETATM 9496 O  O   . HOH F 6 .    ? 55.267 93.694  -31.647 1.00 32.62 ? 3022 HOH A O   1 
HETATM 9497 O  O   . HOH F 6 .    ? 39.433 38.311  -10.786 1.00 33.56 ? 3023 HOH A O   1 
HETATM 9498 O  O   . HOH F 6 .    ? 35.646 67.975  20.598  1.00 33.14 ? 3024 HOH A O   1 
HETATM 9499 O  O   . HOH F 6 .    ? 32.632 69.621  22.264  1.00 30.25 ? 3025 HOH A O   1 
HETATM 9500 O  O   . HOH F 6 .    ? 10.829 53.706  4.070   1.00 28.58 ? 3026 HOH A O   1 
HETATM 9501 O  O   . HOH F 6 .    ? 61.001 56.181  2.033   1.00 35.82 ? 3027 HOH A O   1 
HETATM 9502 O  O   . HOH F 6 .    ? 56.851 47.063  23.230  1.00 35.29 ? 3028 HOH A O   1 
HETATM 9503 O  O   . HOH F 6 .    ? 22.906 77.397  -27.416 1.00 33.76 ? 3029 HOH A O   1 
HETATM 9504 O  O   . HOH F 6 .    ? 42.196 40.641  -9.885  1.00 33.53 ? 3030 HOH A O   1 
HETATM 9505 O  O   . HOH F 6 .    ? 29.793 29.888  24.298  1.00 39.98 ? 3031 HOH A O   1 
HETATM 9506 O  O   . HOH F 6 .    ? 52.033 60.454  28.200  1.00 31.35 ? 3032 HOH A O   1 
HETATM 9507 O  O   . HOH F 6 .    ? 22.837 88.529  -18.746 1.00 40.87 ? 3033 HOH A O   1 
HETATM 9508 O  O   . HOH F 6 .    ? 70.484 62.018  -0.058  1.00 34.07 ? 3034 HOH A O   1 
HETATM 9509 O  O   . HOH F 6 .    ? 39.950 45.306  -26.561 1.00 39.15 ? 3035 HOH A O   1 
HETATM 9510 O  O   . HOH F 6 .    ? 14.264 68.665  5.261   1.00 38.16 ? 3036 HOH A O   1 
HETATM 9511 O  O   . HOH F 6 .    ? 46.274 43.739  28.239  1.00 41.94 ? 3037 HOH A O   1 
HETATM 9512 O  O   . HOH F 6 .    ? 10.353 62.288  1.940   1.00 37.90 ? 3038 HOH A O   1 
HETATM 9513 O  O   . HOH F 6 .    ? 12.697 55.173  25.270  1.00 39.31 ? 3039 HOH A O   1 
HETATM 9514 O  O   . HOH F 6 .    ? 31.802 92.699  -36.749 1.00 27.29 ? 3040 HOH A O   1 
HETATM 9515 O  O   . HOH F 6 .    ? 47.074 72.636  -17.636 1.00 27.14 ? 3041 HOH A O   1 
HETATM 9516 O  O   . HOH F 6 .    ? 21.785 37.980  15.610  1.00 33.11 ? 3042 HOH A O   1 
HETATM 9517 O  O   . HOH F 6 .    ? 38.307 87.210  -19.975 1.00 38.85 ? 3043 HOH A O   1 
HETATM 9518 O  O   . HOH F 6 .    ? 46.858 45.642  26.321  1.00 34.80 ? 3044 HOH A O   1 
HETATM 9519 O  O   . HOH F 6 .    ? 21.025 68.862  -31.601 1.00 30.98 ? 3045 HOH A O   1 
HETATM 9520 O  O   . HOH F 6 .    ? 26.016 65.341  8.194   1.00 31.71 ? 3046 HOH A O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1    ARG 1    1    ?    ?   ?   A . n 
A 1 2    SER 2    2    ?    ?   ?   A . n 
A 1 3    SER 3    3    ?    ?   ?   A . n 
A 1 4    HIS 4    4    ?    ?   ?   A . n 
A 1 5    HIS 5    5    ?    ?   ?   A . n 
A 1 6    HIS 6    6    ?    ?   ?   A . n 
A 1 7    HIS 7    7    ?    ?   ?   A . n 
A 1 8    HIS 8    8    ?    ?   ?   A . n 
A 1 9    HIS 9    9    ?    ?   ?   A . n 
A 1 10   GLY 10   10   ?    ?   ?   A . n 
A 1 11   GLU 11   11   ?    ?   ?   A . n 
A 1 12   PHE 12   12   ?    ?   ?   A . n 
A 1 13   ASP 13   13   ?    ?   ?   A . n 
A 1 14   ASP 14   14   ?    ?   ?   A . n 
A 1 15   PRO 15   15   ?    ?   ?   A . n 
A 1 16   ILE 16   16   ?    ?   ?   A . n 
A 1 17   ARG 17   17   ?    ?   ?   A . n 
A 1 18   PRO 18   18   ?    ?   ?   A . n 
A 1 19   PRO 19   19   ?    ?   ?   A . n 
A 1 20   LEU 20   20   ?    ?   ?   A . n 
A 1 21   LYS 21   21   ?    ?   ?   A . n 
A 1 22   VAL 22   22   ?    ?   ?   A . n 
A 1 23   ALA 23   23   ?    ?   ?   A . n 
A 1 24   ARG 24   24   ?    ?   ?   A . n 
A 1 25   SER 25   25   ?    ?   ?   A . n 
A 1 26   PRO 26   26   ?    ?   ?   A . n 
A 1 27   ARG 27   27   ?    ?   ?   A . n 
A 1 28   PRO 28   28   ?    ?   ?   A . n 
A 1 29   GLY 29   29   ?    ?   ?   A . n 
A 1 30   GLN 30   30   ?    ?   ?   A . n 
A 1 31   CYS 31   31   31   CYS CYS A . n 
A 1 32   GLN 32   32   32   GLN GLN A . n 
A 1 33   ASP 33   33   33   ASP ASP A . n 
A 1 34   VAL 34   34   34   VAL VAL A . n 
A 1 35   VAL 35   35   35   VAL VAL A . n 
A 1 36   GLN 36   36   36   GLN GLN A . n 
A 1 37   ASP 37   37   37   ASP ASP A . n 
A 1 38   VAL 38   38   38   VAL VAL A . n 
A 1 39   PRO 39   39   39   PRO PRO A . n 
A 1 40   ASN 40   40   40   ASN ASN A . n 
A 1 41   VAL 41   41   41   VAL VAL A . n 
A 1 42   ASP 42   42   42   ASP ASP A . n 
A 1 43   VAL 43   43   43   VAL VAL A . n 
A 1 44   GLN 44   44   44   GLN GLN A . n 
A 1 45   MET 45   45   45   MET MET A . n 
A 1 46   LEU 46   46   46   LEU LEU A . n 
A 1 47   GLU 47   47   47   GLU GLU A . n 
A 1 48   LEU 48   48   48   LEU LEU A . n 
A 1 49   TYR 49   49   49   TYR TYR A . n 
A 1 50   ASP 50   50   50   ASP ASP A . n 
A 1 51   ARG 51   51   51   ARG ARG A . n 
A 1 52   MET 52   52   52   MET MET A . n 
A 1 53   SER 53   53   53   SER SER A . n 
A 1 54   PHE 54   54   54   PHE PHE A . n 
A 1 55   LYS 55   55   55   LYS LYS A . n 
A 1 56   ASP 56   56   56   ASP ASP A . n 
A 1 57   ILE 57   57   57   ILE ILE A . n 
A 1 58   ASP 58   58   58   ASP ASP A . n 
A 1 59   GLY 59   59   59   GLY GLY A . n 
A 1 60   GLY 60   60   60   GLY GLY A . n 
A 1 61   VAL 61   61   61   VAL VAL A . n 
A 1 62   TRP 62   62   62   TRP TRP A . n 
A 1 63   LYS 63   63   63   LYS LYS A . n 
A 1 64   GLN 64   64   64   GLN GLN A . n 
A 1 65   GLY 65   65   65   GLY GLY A . n 
A 1 66   TRP 66   66   66   TRP TRP A . n 
A 1 67   ASN 67   67   67   ASN ASN A . n 
A 1 68   ILE 68   68   68   ILE ILE A . n 
A 1 69   LYS 69   69   69   LYS LYS A . n 
A 1 70   TYR 70   70   70   TYR TYR A . n 
A 1 71   ASP 71   71   71   ASP ASP A . n 
A 1 72   PRO 72   72   72   PRO PRO A . n 
A 1 73   LEU 73   73   73   LEU LEU A . n 
A 1 74   LYS 74   74   74   LYS LYS A . n 
A 1 75   TYR 75   75   75   TYR TYR A . n 
A 1 76   ASN 76   76   76   ASN ASN A . n 
A 1 77   ALA 77   77   77   ALA ALA A . n 
A 1 78   HIS 78   78   78   HIS HIS A . n 
A 1 79   HIS 79   79   79   HIS HIS A . n 
A 1 80   LYS 80   80   80   LYS LYS A . n 
A 1 81   LEU 81   81   81   LEU LEU A . n 
A 1 82   LYS 82   82   82   LYS LYS A . n 
A 1 83   VAL 83   83   83   VAL VAL A . n 
A 1 84   PHE 84   84   84   PHE PHE A . n 
A 1 85   VAL 85   85   85   VAL VAL A . n 
A 1 86   VAL 86   86   86   VAL VAL A . n 
A 1 87   PRO 87   87   87   PRO PRO A . n 
A 1 88   HIS 88   88   88   HIS HIS A . n 
A 1 89   SER 89   89   89   SER SER A . n 
A 1 90   HIS 90   90   90   HIS HIS A . n 
A 1 91   ASN 91   91   91   ASN ASN A . n 
A 1 92   ASP 92   92   92   ASP ASP A . n 
A 1 93   PRO 93   93   93   PRO PRO A . n 
A 1 94   GLY 94   94   94   GLY GLY A . n 
A 1 95   TRP 95   95   95   TRP TRP A . n 
A 1 96   ILE 96   96   96   ILE ILE A . n 
A 1 97   GLN 97   97   97   GLN GLN A . n 
A 1 98   THR 98   98   98   THR THR A . n 
A 1 99   PHE 99   99   99   PHE PHE A . n 
A 1 100  GLU 100  100  100  GLU GLU A . n 
A 1 101  GLU 101  101  101  GLU GLU A . n 
A 1 102  TYR 102  102  102  TYR TYR A . n 
A 1 103  TYR 103  103  103  TYR TYR A . n 
A 1 104  GLN 104  104  104  GLN GLN A . n 
A 1 105  HIS 105  105  105  HIS HIS A . n 
A 1 106  ASP 106  106  106  ASP ASP A . n 
A 1 107  THR 107  107  107  THR THR A . n 
A 1 108  LYS 108  108  108  LYS LYS A . n 
A 1 109  HIS 109  109  109  HIS HIS A . n 
A 1 110  ILE 110  110  110  ILE ILE A . n 
A 1 111  LEU 111  111  111  LEU LEU A . n 
A 1 112  SER 112  112  112  SER SER A . n 
A 1 113  ASN 113  113  113  ASN ASN A . n 
A 1 114  ALA 114  114  114  ALA ALA A . n 
A 1 115  LEU 115  115  115  LEU LEU A . n 
A 1 116  ARG 116  116  116  ARG ARG A . n 
A 1 117  HIS 117  117  117  HIS HIS A . n 
A 1 118  LEU 118  118  118  LEU LEU A . n 
A 1 119  HIS 119  119  119  HIS HIS A . n 
A 1 120  ASP 120  120  120  ASP ASP A . n 
A 1 121  ASN 121  121  121  ASN ASN A . n 
A 1 122  PRO 122  122  122  PRO PRO A . n 
A 1 123  GLU 123  123  123  GLU GLU A . n 
A 1 124  MET 124  124  124  MET MET A . n 
A 1 125  LYS 125  125  125  LYS LYS A . n 
A 1 126  PHE 126  126  126  PHE PHE A . n 
A 1 127  ILE 127  127  127  ILE ILE A . n 
A 1 128  TRP 128  128  128  TRP TRP A . n 
A 1 129  ALA 129  129  129  ALA ALA A . n 
A 1 130  GLU 130  130  130  GLU GLU A . n 
A 1 131  ILE 131  131  131  ILE ILE A . n 
A 1 132  SER 132  132  132  SER SER A . n 
A 1 133  TYR 133  133  133  TYR TYR A . n 
A 1 134  PHE 134  134  134  PHE PHE A . n 
A 1 135  ALA 135  135  135  ALA ALA A . n 
A 1 136  ARG 136  136  136  ARG ARG A . n 
A 1 137  PHE 137  137  137  PHE PHE A . n 
A 1 138  TYR 138  138  138  TYR TYR A . n 
A 1 139  HIS 139  139  139  HIS HIS A . n 
A 1 140  ASP 140  140  140  ASP ASP A . n 
A 1 141  LEU 141  141  141  LEU LEU A . n 
A 1 142  GLY 142  142  142  GLY GLY A . n 
A 1 143  GLU 143  143  143  GLU GLU A . n 
A 1 144  ASN 144  144  144  ASN ASN A . n 
A 1 145  LYS 145  145  145  LYS LYS A . n 
A 1 146  LYS 146  146  146  LYS LYS A . n 
A 1 147  LEU 147  147  147  LEU LEU A . n 
A 1 148  GLN 148  148  148  GLN GLN A . n 
A 1 149  MET 149  149  149  MET MET A . n 
A 1 150  LYS 150  150  150  LYS LYS A . n 
A 1 151  SER 151  151  151  SER SER A . n 
A 1 152  ILE 152  152  152  ILE ILE A . n 
A 1 153  VAL 153  153  153  VAL VAL A . n 
A 1 154  LYS 154  154  154  LYS LYS A . n 
A 1 155  ASN 155  155  155  ASN ASN A . n 
A 1 156  GLY 156  156  156  GLY GLY A . n 
A 1 157  GLN 157  157  157  GLN GLN A . n 
A 1 158  LEU 158  158  158  LEU LEU A . n 
A 1 159  GLU 159  159  159  GLU GLU A . n 
A 1 160  PHE 160  160  160  PHE PHE A . n 
A 1 161  VAL 161  161  161  VAL VAL A . n 
A 1 162  THR 162  162  162  THR THR A . n 
A 1 163  GLY 163  163  163  GLY GLY A . n 
A 1 164  GLY 164  164  164  GLY GLY A . n 
A 1 165  TRP 165  165  165  TRP TRP A . n 
A 1 166  VAL 166  166  166  VAL VAL A . n 
A 1 167  MET 167  167  167  MET MET A . n 
A 1 168  PRO 168  168  168  PRO PRO A . n 
A 1 169  ASP 169  169  169  ASP ASP A . n 
A 1 170  GLU 170  170  170  GLU GLU A . n 
A 1 171  ALA 171  171  171  ALA ALA A . n 
A 1 172  ASN 172  172  172  ASN ASN A . n 
A 1 173  SER 173  173  173  SER SER A . n 
A 1 174  HIS 174  174  174  HIS HIS A . n 
A 1 175  TRP 175  175  175  TRP TRP A . n 
A 1 176  ARG 176  176  176  ARG ARG A . n 
A 1 177  ASN 177  177  177  ASN ASN A . n 
A 1 178  VAL 178  178  178  VAL VAL A . n 
A 1 179  LEU 179  179  179  LEU LEU A . n 
A 1 180  LEU 180  180  180  LEU LEU A . n 
A 1 181  GLN 181  181  181  GLN GLN A . n 
A 1 182  LEU 182  182  182  LEU LEU A . n 
A 1 183  THR 183  183  183  THR THR A . n 
A 1 184  GLU 184  184  184  GLU GLU A . n 
A 1 185  GLY 185  185  185  GLY GLY A . n 
A 1 186  GLN 186  186  186  GLN GLN A . n 
A 1 187  THR 187  187  187  THR THR A . n 
A 1 188  TRP 188  188  188  TRP TRP A . n 
A 1 189  LEU 189  189  189  LEU LEU A . n 
A 1 190  LYS 190  190  190  LYS LYS A . n 
A 1 191  GLN 191  191  191  GLN GLN A . n 
A 1 192  PHE 192  192  192  PHE PHE A . n 
A 1 193  MET 193  193  193  MET MET A . n 
A 1 194  ASN 194  194  194  ASN ASN A . n 
A 1 195  VAL 195  195  195  VAL VAL A . n 
A 1 196  THR 196  196  196  THR THR A . n 
A 1 197  PRO 197  197  197  PRO PRO A . n 
A 1 198  THR 198  198  198  THR THR A . n 
A 1 199  ALA 199  199  199  ALA ALA A . n 
A 1 200  SER 200  200  200  SER SER A . n 
A 1 201  TRP 201  201  201  TRP TRP A . n 
A 1 202  ALA 202  202  202  ALA ALA A . n 
A 1 203  ILE 203  203  203  ILE ILE A . n 
A 1 204  ASP 204  204  204  ASP ASP A . n 
A 1 205  PRO 205  205  205  PRO PRO A . n 
A 1 206  PHE 206  206  206  PHE PHE A . n 
A 1 207  GLY 207  207  207  GLY GLY A . n 
A 1 208  HIS 208  208  208  HIS HIS A . n 
A 1 209  SER 209  209  209  SER SER A . n 
A 1 210  PRO 210  210  210  PRO PRO A . n 
A 1 211  THR 211  211  211  THR THR A . n 
A 1 212  MET 212  212  212  MET MET A . n 
A 1 213  PRO 213  213  213  PRO PRO A . n 
A 1 214  TYR 214  214  214  TYR TYR A . n 
A 1 215  ILE 215  215  215  ILE ILE A . n 
A 1 216  LEU 216  216  216  LEU LEU A . n 
A 1 217  GLN 217  217  217  GLN GLN A . n 
A 1 218  LYS 218  218  218  LYS LYS A . n 
A 1 219  SER 219  219  219  SER SER A . n 
A 1 220  GLY 220  220  220  GLY GLY A . n 
A 1 221  PHE 221  221  221  PHE PHE A . n 
A 1 222  LYS 222  222  222  LYS LYS A . n 
A 1 223  ASN 223  223  223  ASN ASN A . n 
A 1 224  MET 224  224  224  MET MET A . n 
A 1 225  LEU 225  225  225  LEU LEU A . n 
A 1 226  ILE 226  226  226  ILE ILE A . n 
A 1 227  GLN 227  227  227  GLN GLN A . n 
A 1 228  ARG 228  228  228  ARG ARG A . n 
A 1 229  THR 229  229  229  THR THR A . n 
A 1 230  HIS 230  230  230  HIS HIS A . n 
A 1 231  TYR 231  231  231  TYR TYR A . n 
A 1 232  SER 232  232  232  SER SER A . n 
A 1 233  VAL 233  233  233  VAL VAL A . n 
A 1 234  LYS 234  234  234  LYS LYS A . n 
A 1 235  LYS 235  235  235  LYS LYS A . n 
A 1 236  GLU 236  236  236  GLU GLU A . n 
A 1 237  LEU 237  237  237  LEU LEU A . n 
A 1 238  ALA 238  238  238  ALA ALA A . n 
A 1 239  GLN 239  239  239  GLN GLN A . n 
A 1 240  GLN 240  240  240  GLN GLN A . n 
A 1 241  ARG 241  241  241  ARG ARG A . n 
A 1 242  GLN 242  242  242  GLN GLN A . n 
A 1 243  LEU 243  243  243  LEU LEU A . n 
A 1 244  GLU 244  244  244  GLU GLU A . n 
A 1 245  PHE 245  245  245  PHE PHE A . n 
A 1 246  LEU 246  246  246  LEU LEU A . n 
A 1 247  TRP 247  247  247  TRP TRP A . n 
A 1 248  ARG 248  248  248  ARG ARG A . n 
A 1 249  GLN 249  249  249  GLN GLN A . n 
A 1 250  ILE 250  250  250  ILE ILE A . n 
A 1 251  TRP 251  251  251  TRP TRP A . n 
A 1 252  ASP 252  252  252  ASP ASP A . n 
A 1 253  ASN 253  253  253  ASN ASN A . n 
A 1 254  LYS 254  254  254  LYS LYS A . n 
A 1 255  GLY 255  255  255  GLY GLY A . n 
A 1 256  ASP 256  256  256  ASP ASP A . n 
A 1 257  THR 257  257  257  THR THR A . n 
A 1 258  ALA 258  258  258  ALA ALA A . n 
A 1 259  LEU 259  259  259  LEU LEU A . n 
A 1 260  PHE 260  260  260  PHE PHE A . n 
A 1 261  THR 261  261  261  THR THR A . n 
A 1 262  HIS 262  262  262  HIS HIS A . n 
A 1 263  MET 263  263  263  MET MET A . n 
A 1 264  MET 264  264  264  MET MET A . n 
A 1 265  PRO 265  265  265  PRO PRO A . n 
A 1 266  PHE 266  266  266  PHE PHE A . n 
A 1 267  TYR 267  267  267  TYR TYR A . n 
A 1 268  SER 268  268  268  SER SER A . n 
A 1 269  TYR 269  269  269  TYR TYR A . n 
A 1 270  ASP 270  270  270  ASP ASP A . n 
A 1 271  ILE 271  271  271  ILE ILE A . n 
A 1 272  PRO 272  272  272  PRO PRO A . n 
A 1 273  HIS 273  273  273  HIS HIS A . n 
A 1 274  THR 274  274  274  THR THR A . n 
A 1 275  CYS 275  275  275  CYS CYS A . n 
A 1 276  GLY 276  276  276  GLY GLY A . n 
A 1 277  PRO 277  277  277  PRO PRO A . n 
A 1 278  ASP 278  278  278  ASP ASP A . n 
A 1 279  PRO 279  279  279  PRO PRO A . n 
A 1 280  LYS 280  280  280  LYS LYS A . n 
A 1 281  VAL 281  281  281  VAL VAL A . n 
A 1 282  CYS 282  282  282  CYS CYS A . n 
A 1 283  CYS 283  283  283  CYS CYS A . n 
A 1 284  GLN 284  284  284  GLN GLN A . n 
A 1 285  PHE 285  285  285  PHE PHE A . n 
A 1 286  ASP 286  286  286  ASP ASP A . n 
A 1 287  PHE 287  287  287  PHE PHE A . n 
A 1 288  LYS 288  288  288  LYS LYS A . n 
A 1 289  ARG 289  289  289  ARG ARG A . n 
A 1 290  MET 290  290  290  MET MET A . n 
A 1 291  GLY 291  291  291  GLY GLY A . n 
A 1 292  SER 292  292  292  SER SER A . n 
A 1 293  PHE 293  293  293  PHE PHE A . n 
A 1 294  GLY 294  294  294  GLY GLY A . n 
A 1 295  LEU 295  295  295  LEU LEU A . n 
A 1 296  SER 296  296  296  SER SER A . n 
A 1 297  CYS 297  297  297  CYS CYS A . n 
A 1 298  PRO 298  298  298  PRO PRO A . n 
A 1 299  TRP 299  299  299  TRP TRP A . n 
A 1 300  LYS 300  300  300  LYS LYS A . n 
A 1 301  VAL 301  301  301  VAL VAL A . n 
A 1 302  PRO 302  302  302  PRO PRO A . n 
A 1 303  PRO 303  303  303  PRO PRO A . n 
A 1 304  ARG 304  304  304  ARG ARG A . n 
A 1 305  THR 305  305  305  THR THR A . n 
A 1 306  ILE 306  306  306  ILE ILE A . n 
A 1 307  SER 307  307  307  SER SER A . n 
A 1 308  ASP 308  308  308  ASP ASP A . n 
A 1 309  GLN 309  309  309  GLN GLN A . n 
A 1 310  ASN 310  310  310  ASN ASN A . n 
A 1 311  VAL 311  311  311  VAL VAL A . n 
A 1 312  ALA 312  312  312  ALA ALA A . n 
A 1 313  ALA 313  313  313  ALA ALA A . n 
A 1 314  ARG 314  314  314  ARG ARG A . n 
A 1 315  SER 315  315  315  SER SER A . n 
A 1 316  ASP 316  316  316  ASP ASP A . n 
A 1 317  LEU 317  317  317  LEU LEU A . n 
A 1 318  LEU 318  318  318  LEU LEU A . n 
A 1 319  VAL 319  319  319  VAL VAL A . n 
A 1 320  ASP 320  320  320  ASP ASP A . n 
A 1 321  GLN 321  321  321  GLN GLN A . n 
A 1 322  TRP 322  322  322  TRP TRP A . n 
A 1 323  LYS 323  323  323  LYS LYS A . n 
A 1 324  LYS 324  324  324  LYS LYS A . n 
A 1 325  LYS 325  325  325  LYS LYS A . n 
A 1 326  ALA 326  326  326  ALA ALA A . n 
A 1 327  GLU 327  327  327  GLU GLU A . n 
A 1 328  LEU 328  328  328  LEU LEU A . n 
A 1 329  TYR 329  329  329  TYR TYR A . n 
A 1 330  ARG 330  330  330  ARG ARG A . n 
A 1 331  THR 331  331  331  THR THR A . n 
A 1 332  ASN 332  332  332  ASN ASN A . n 
A 1 333  VAL 333  333  333  VAL VAL A . n 
A 1 334  LEU 334  334  334  LEU LEU A . n 
A 1 335  LEU 335  335  335  LEU LEU A . n 
A 1 336  ILE 336  336  336  ILE ILE A . n 
A 1 337  PRO 337  337  337  PRO PRO A . n 
A 1 338  LEU 338  338  338  LEU LEU A . n 
A 1 339  GLY 339  339  339  GLY GLY A . n 
A 1 340  ASP 340  340  340  ASP ASP A . n 
A 1 341  ASN 341  341  341  ASN ASN A . n 
A 1 342  PHE 342  342  342  PHE PHE A . n 
A 1 343  ARG 343  343  343  ARG ARG A . n 
A 1 344  PHE 344  344  344  PHE PHE A . n 
A 1 345  LYS 345  345  345  LYS LYS A . n 
A 1 346  GLN 346  346  346  GLN GLN A . n 
A 1 347  ASN 347  347  347  ASN ASN A . n 
A 1 348  THR 348  348  348  THR THR A . n 
A 1 349  GLU 349  349  349  GLU GLU A . n 
A 1 350  TRP 350  350  350  TRP TRP A . n 
A 1 351  ASP 351  351  351  ASP ASP A . n 
A 1 352  VAL 352  352  352  VAL VAL A . n 
A 1 353  GLN 353  353  353  GLN GLN A . n 
A 1 354  ARG 354  354  354  ARG ARG A . n 
A 1 355  VAL 355  355  355  VAL VAL A . n 
A 1 356  ASN 356  356  356  ASN ASN A . n 
A 1 357  TYR 357  357  357  TYR TYR A . n 
A 1 358  GLU 358  358  358  GLU GLU A . n 
A 1 359  ARG 359  359  359  ARG ARG A . n 
A 1 360  LEU 360  360  360  LEU LEU A . n 
A 1 361  PHE 361  361  361  PHE PHE A . n 
A 1 362  GLU 362  362  362  GLU GLU A . n 
A 1 363  HIS 363  363  363  HIS HIS A . n 
A 1 364  ILE 364  364  364  ILE ILE A . n 
A 1 365  ASN 365  365  365  ASN ASN A . n 
A 1 366  SER 366  366  366  SER SER A . n 
A 1 367  GLN 367  367  367  GLN GLN A . n 
A 1 368  ALA 368  368  368  ALA ALA A . n 
A 1 369  HIS 369  369  369  HIS HIS A . n 
A 1 370  PHE 370  370  370  PHE PHE A . n 
A 1 371  ASN 371  371  371  ASN ASN A . n 
A 1 372  VAL 372  372  372  VAL VAL A . n 
A 1 373  GLN 373  373  373  GLN GLN A . n 
A 1 374  ALA 374  374  374  ALA ALA A . n 
A 1 375  GLN 375  375  375  GLN GLN A . n 
A 1 376  PHE 376  376  376  PHE PHE A . n 
A 1 377  GLY 377  377  377  GLY GLY A . n 
A 1 378  THR 378  378  378  THR THR A . n 
A 1 379  LEU 379  379  379  LEU LEU A . n 
A 1 380  GLN 380  380  380  GLN GLN A . n 
A 1 381  GLU 381  381  381  GLU GLU A . n 
A 1 382  TYR 382  382  382  TYR TYR A . n 
A 1 383  PHE 383  383  383  PHE PHE A . n 
A 1 384  ASP 384  384  384  ASP ASP A . n 
A 1 385  ALA 385  385  385  ALA ALA A . n 
A 1 386  VAL 386  386  386  VAL VAL A . n 
A 1 387  HIS 387  387  387  HIS HIS A . n 
A 1 388  GLN 388  388  388  GLN GLN A . n 
A 1 389  ALA 389  389  389  ALA ALA A . n 
A 1 390  GLU 390  390  390  GLU GLU A . n 
A 1 391  ARG 391  391  391  ARG ARG A . n 
A 1 392  ALA 392  392  392  ALA ALA A . n 
A 1 393  GLY 393  393  393  GLY GLY A . n 
A 1 394  GLN 394  394  394  GLN GLN A . n 
A 1 395  ALA 395  395  395  ALA ALA A . n 
A 1 396  GLU 396  396  396  GLU GLU A . n 
A 1 397  PHE 397  397  397  PHE PHE A . n 
A 1 398  PRO 398  398  398  PRO PRO A . n 
A 1 399  THR 399  399  399  THR THR A . n 
A 1 400  LEU 400  400  400  LEU LEU A . n 
A 1 401  SER 401  401  401  SER SER A . n 
A 1 402  GLY 402  402  402  GLY GLY A . n 
A 1 403  ASP 403  403  403  ASP ASP A . n 
A 1 404  PHE 404  404  404  PHE PHE A . n 
A 1 405  PHE 405  405  405  PHE PHE A . n 
A 1 406  THR 406  406  406  THR THR A . n 
A 1 407  TYR 407  407  407  TYR TYR A . n 
A 1 408  ALA 408  408  408  ALA ALA A . n 
A 1 409  ASP 409  409  409  ASP ASP A . n 
A 1 410  ARG 410  410  410  ARG ARG A . n 
A 1 411  SER 411  411  411  SER SER A . n 
A 1 412  ASP 412  412  412  ASP ASP A . n 
A 1 413  ASN 413  413  413  ASN ASN A . n 
A 1 414  TYR 414  414  414  TYR TYR A . n 
A 1 415  TRP 415  415  415  TRP TRP A . n 
A 1 416  SER 416  416  416  SER SER A . n 
A 1 417  GLY 417  417  417  GLY GLY A . n 
A 1 418  TYR 418  418  418  TYR TYR A . n 
A 1 419  TYR 419  419  419  TYR TYR A . n 
A 1 420  THR 420  420  420  THR THR A . n 
A 1 421  SER 421  421  421  SER SER A . n 
A 1 422  ARG 422  422  422  ARG ARG A . n 
A 1 423  PRO 423  423  423  PRO PRO A . n 
A 1 424  TYR 424  424  424  TYR TYR A . n 
A 1 425  HIS 425  425  425  HIS HIS A . n 
A 1 426  LYS 426  426  426  LYS LYS A . n 
A 1 427  ARG 427  427  427  ARG ARG A . n 
A 1 428  MET 428  428  428  MET MET A . n 
A 1 429  ASP 429  429  429  ASP ASP A . n 
A 1 430  ARG 430  430  430  ARG ARG A . n 
A 1 431  VAL 431  431  431  VAL VAL A . n 
A 1 432  LEU 432  432  432  LEU LEU A . n 
A 1 433  MET 433  433  433  MET MET A . n 
A 1 434  HIS 434  434  434  HIS HIS A . n 
A 1 435  TYR 435  435  435  TYR TYR A . n 
A 1 436  VAL 436  436  436  VAL VAL A . n 
A 1 437  ARG 437  437  437  ARG ARG A . n 
A 1 438  ALA 438  438  438  ALA ALA A . n 
A 1 439  ALA 439  439  439  ALA ALA A . n 
A 1 440  GLU 440  440  440  GLU GLU A . n 
A 1 441  MET 441  441  441  MET MET A . n 
A 1 442  LEU 442  442  442  LEU LEU A . n 
A 1 443  SER 443  443  443  SER SER A . n 
A 1 444  ALA 444  444  444  ALA ALA A . n 
A 1 445  TRP 445  445  445  TRP TRP A . n 
A 1 446  HIS 446  446  446  HIS HIS A . n 
A 1 447  SER 447  447  447  SER SER A . n 
A 1 448  TRP 448  448  448  TRP TRP A . n 
A 1 449  ASP 449  449  449  ASP ASP A . n 
A 1 450  GLY 450  450  450  GLY GLY A . n 
A 1 451  MET 451  451  451  MET MET A . n 
A 1 452  ALA 452  452  452  ALA ALA A . n 
A 1 453  ARG 453  453  453  ARG ARG A . n 
A 1 454  ILE 454  454  454  ILE ILE A . n 
A 1 455  GLU 455  455  455  GLU GLU A . n 
A 1 456  GLU 456  456  456  GLU GLU A . n 
A 1 457  ARG 457  457  457  ARG ARG A . n 
A 1 458  LEU 458  458  458  LEU LEU A . n 
A 1 459  GLU 459  459  459  GLU GLU A . n 
A 1 460  GLN 460  460  460  GLN GLN A . n 
A 1 461  ALA 461  461  461  ALA ALA A . n 
A 1 462  ARG 462  462  462  ARG ARG A . n 
A 1 463  ARG 463  463  463  ARG ARG A . n 
A 1 464  GLU 464  464  464  GLU GLU A . n 
A 1 465  LEU 465  465  465  LEU LEU A . n 
A 1 466  SER 466  466  466  SER SER A . n 
A 1 467  LEU 467  467  467  LEU LEU A . n 
A 1 468  PHE 468  468  468  PHE PHE A . n 
A 1 469  GLN 469  469  469  GLN GLN A . n 
A 1 470  HIS 470  470  470  HIS HIS A . n 
A 1 471  HIS 471  471  471  HIS HIS A . n 
A 1 472  ASP 472  472  472  ASP ASP A . n 
A 1 473  GLY 473  473  473  GLY GLY A . n 
A 1 474  ILE 474  474  474  ILE ILE A . n 
A 1 475  THR 475  475  475  THR THR A . n 
A 1 476  GLY 476  476  476  GLY GLY A . n 
A 1 477  THR 477  477  477  THR THR A . n 
A 1 478  ALA 478  478  478  ALA ALA A . n 
A 1 479  LYS 479  479  479  LYS LYS A . n 
A 1 480  THR 480  480  480  THR THR A . n 
A 1 481  HIS 481  481  481  HIS HIS A . n 
A 1 482  VAL 482  482  482  VAL VAL A . n 
A 1 483  VAL 483  483  483  VAL VAL A . n 
A 1 484  VAL 484  484  484  VAL VAL A . n 
A 1 485  ASP 485  485  485  ASP ASP A . n 
A 1 486  TYR 486  486  486  TYR TYR A . n 
A 1 487  GLU 487  487  487  GLU GLU A . n 
A 1 488  GLN 488  488  488  GLN GLN A . n 
A 1 489  ARG 489  489  489  ARG ARG A . n 
A 1 490  MET 490  490  490  MET MET A . n 
A 1 491  GLN 491  491  491  GLN GLN A . n 
A 1 492  GLU 492  492  492  GLU GLU A . n 
A 1 493  ALA 493  493  493  ALA ALA A . n 
A 1 494  LEU 494  494  494  LEU LEU A . n 
A 1 495  LYS 495  495  495  LYS LYS A . n 
A 1 496  ALA 496  496  496  ALA ALA A . n 
A 1 497  CYS 497  497  497  CYS CYS A . n 
A 1 498  GLN 498  498  498  GLN GLN A . n 
A 1 499  MET 499  499  499  MET MET A . n 
A 1 500  VAL 500  500  500  VAL VAL A . n 
A 1 501  MET 501  501  501  MET MET A . n 
A 1 502  GLN 502  502  502  GLN GLN A . n 
A 1 503  GLN 503  503  503  GLN GLN A . n 
A 1 504  SER 504  504  504  SER SER A . n 
A 1 505  VAL 505  505  505  VAL VAL A . n 
A 1 506  TYR 506  506  506  TYR TYR A . n 
A 1 507  ARG 507  507  507  ARG ARG A . n 
A 1 508  LEU 508  508  508  LEU LEU A . n 
A 1 509  LEU 509  509  509  LEU LEU A . n 
A 1 510  THR 510  510  510  THR THR A . n 
A 1 511  LYS 511  511  511  LYS LYS A . n 
A 1 512  PRO 512  512  512  PRO PRO A . n 
A 1 513  SER 513  513  513  SER SER A . n 
A 1 514  ILE 514  514  514  ILE ILE A . n 
A 1 515  TYR 515  515  515  TYR TYR A . n 
A 1 516  SER 516  516  516  SER SER A . n 
A 1 517  PRO 517  517  517  PRO PRO A . n 
A 1 518  ASP 518  518  518  ASP ASP A . n 
A 1 519  PHE 519  519  519  PHE PHE A . n 
A 1 520  SER 520  520  520  SER SER A . n 
A 1 521  PHE 521  521  521  PHE PHE A . n 
A 1 522  SER 522  522  522  SER SER A . n 
A 1 523  TYR 523  523  523  TYR TYR A . n 
A 1 524  PHE 524  524  524  PHE PHE A . n 
A 1 525  THR 525  525  525  THR THR A . n 
A 1 526  LEU 526  526  526  LEU LEU A . n 
A 1 527  ASP 527  527  527  ASP ASP A . n 
A 1 528  ASP 528  528  528  ASP ASP A . n 
A 1 529  SER 529  529  529  SER SER A . n 
A 1 530  ARG 530  530  530  ARG ARG A . n 
A 1 531  TRP 531  531  531  TRP TRP A . n 
A 1 532  PRO 532  532  532  PRO PRO A . n 
A 1 533  GLY 533  533  533  GLY GLY A . n 
A 1 534  SER 534  534  534  SER SER A . n 
A 1 535  GLY 535  535  535  GLY GLY A . n 
A 1 536  VAL 536  536  536  VAL VAL A . n 
A 1 537  GLU 537  537  537  GLU GLU A . n 
A 1 538  ASP 538  538  538  ASP ASP A . n 
A 1 539  SER 539  539  539  SER SER A . n 
A 1 540  ARG 540  540  540  ARG ARG A . n 
A 1 541  THR 541  541  541  THR THR A . n 
A 1 542  THR 542  542  542  THR THR A . n 
A 1 543  ILE 543  543  543  ILE ILE A . n 
A 1 544  ILE 544  544  544  ILE ILE A . n 
A 1 545  LEU 545  545  545  LEU LEU A . n 
A 1 546  GLY 546  546  546  GLY GLY A . n 
A 1 547  GLU 547  547  547  GLU GLU A . n 
A 1 548  ASP 548  548  548  ASP ASP A . n 
A 1 549  ILE 549  549  549  ILE ILE A . n 
A 1 550  LEU 550  550  550  LEU LEU A . n 
A 1 551  PRO 551  551  551  PRO PRO A . n 
A 1 552  SER 552  552  552  SER SER A . n 
A 1 553  LYS 553  553  553  LYS LYS A . n 
A 1 554  HIS 554  554  554  HIS HIS A . n 
A 1 555  VAL 555  555  555  VAL VAL A . n 
A 1 556  VAL 556  556  556  VAL VAL A . n 
A 1 557  MET 557  557  557  MET MET A . n 
A 1 558  HIS 558  558  558  HIS HIS A . n 
A 1 559  ASN 559  559  559  ASN ASN A . n 
A 1 560  THR 560  560  560  THR THR A . n 
A 1 561  LEU 561  561  561  LEU LEU A . n 
A 1 562  PRO 562  562  562  PRO PRO A . n 
A 1 563  HIS 563  563  563  HIS HIS A . n 
A 1 564  TRP 564  564  564  TRP TRP A . n 
A 1 565  ARG 565  565  565  ARG ARG A . n 
A 1 566  GLU 566  566  566  GLU GLU A . n 
A 1 567  GLN 567  567  567  GLN GLN A . n 
A 1 568  LEU 568  568  568  LEU LEU A . n 
A 1 569  VAL 569  569  569  VAL VAL A . n 
A 1 570  ASP 570  570  570  ASP ASP A . n 
A 1 571  PHE 571  571  571  PHE PHE A . n 
A 1 572  TYR 572  572  572  TYR TYR A . n 
A 1 573  VAL 573  573  573  VAL VAL A . n 
A 1 574  SER 574  574  574  SER SER A . n 
A 1 575  SER 575  575  575  SER SER A . n 
A 1 576  PRO 576  576  576  PRO PRO A . n 
A 1 577  PHE 577  577  577  PHE PHE A . n 
A 1 578  VAL 578  578  578  VAL VAL A . n 
A 1 579  SER 579  579  579  SER SER A . n 
A 1 580  VAL 580  580  580  VAL VAL A . n 
A 1 581  THR 581  581  581  THR THR A . n 
A 1 582  ASP 582  582  582  ASP ASP A . n 
A 1 583  LEU 583  583  583  LEU LEU A . n 
A 1 584  ALA 584  584  584  ALA ALA A . n 
A 1 585  ASN 585  585  585  ASN ASN A . n 
A 1 586  ASN 586  586  586  ASN ASN A . n 
A 1 587  PRO 587  587  587  PRO PRO A . n 
A 1 588  VAL 588  588  588  VAL VAL A . n 
A 1 589  GLU 589  589  589  GLU GLU A . n 
A 1 590  ALA 590  590  590  ALA ALA A . n 
A 1 591  GLN 591  591  591  GLN GLN A . n 
A 1 592  VAL 592  592  592  VAL VAL A . n 
A 1 593  SER 593  593  593  SER SER A . n 
A 1 594  PRO 594  594  594  PRO PRO A . n 
A 1 595  VAL 595  595  595  VAL VAL A . n 
A 1 596  TRP 596  596  596  TRP TRP A . n 
A 1 597  SER 597  597  597  SER SER A . n 
A 1 598  TRP 598  598  598  TRP TRP A . n 
A 1 599  HIS 599  599  599  HIS HIS A . n 
A 1 600  HIS 600  600  600  HIS HIS A . n 
A 1 601  ASP 601  601  601  ASP ASP A . n 
A 1 602  THR 602  602  602  THR THR A . n 
A 1 603  LEU 603  603  603  LEU LEU A . n 
A 1 604  THR 604  604  604  THR THR A . n 
A 1 605  LYS 605  605  605  LYS LYS A . n 
A 1 606  THR 606  606  606  THR THR A . n 
A 1 607  ILE 607  607  607  ILE ILE A . n 
A 1 608  HIS 608  608  608  HIS HIS A . n 
A 1 609  PRO 609  609  609  PRO PRO A . n 
A 1 610  GLN 610  610  610  GLN GLN A . n 
A 1 611  GLY 611  611  611  GLY GLY A . n 
A 1 612  SER 612  612  612  SER SER A . n 
A 1 613  THR 613  613  613  THR THR A . n 
A 1 614  THR 614  614  614  THR THR A . n 
A 1 615  LYS 615  615  615  LYS LYS A . n 
A 1 616  TYR 616  616  616  TYR TYR A . n 
A 1 617  ARG 617  617  617  ARG ARG A . n 
A 1 618  ILE 618  618  618  ILE ILE A . n 
A 1 619  ILE 619  619  619  ILE ILE A . n 
A 1 620  PHE 620  620  620  PHE PHE A . n 
A 1 621  LYS 621  621  621  LYS LYS A . n 
A 1 622  ALA 622  622  622  ALA ALA A . n 
A 1 623  ARG 623  623  623  ARG ARG A . n 
A 1 624  VAL 624  624  624  VAL VAL A . n 
A 1 625  PRO 625  625  625  PRO PRO A . n 
A 1 626  PRO 626  626  626  PRO PRO A . n 
A 1 627  MET 627  627  627  MET MET A . n 
A 1 628  GLY 628  628  628  GLY GLY A . n 
A 1 629  LEU 629  629  629  LEU LEU A . n 
A 1 630  ALA 630  630  630  ALA ALA A . n 
A 1 631  THR 631  631  631  THR THR A . n 
A 1 632  TYR 632  632  632  TYR TYR A . n 
A 1 633  VAL 633  633  633  VAL VAL A . n 
A 1 634  LEU 634  634  634  LEU LEU A . n 
A 1 635  THR 635  635  635  THR THR A . n 
A 1 636  ILE 636  636  636  ILE ILE A . n 
A 1 637  SER 637  637  637  SER SER A . n 
A 1 638  ASP 638  638  638  ASP ASP A . n 
A 1 639  SER 639  639  639  SER SER A . n 
A 1 640  LYS 640  640  640  LYS LYS A . n 
A 1 641  PRO 641  641  641  PRO PRO A . n 
A 1 642  GLU 642  642  642  GLU GLU A . n 
A 1 643  HIS 643  643  643  HIS HIS A . n 
A 1 644  THR 644  644  644  THR THR A . n 
A 1 645  SER 645  645  645  SER SER A . n 
A 1 646  TYR 646  646  646  TYR TYR A . n 
A 1 647  ALA 647  647  647  ALA ALA A . n 
A 1 648  SER 648  648  648  SER SER A . n 
A 1 649  ASN 649  649  649  ASN ASN A . n 
A 1 650  LEU 650  650  650  LEU LEU A . n 
A 1 651  LEU 651  651  651  LEU LEU A . n 
A 1 652  LEU 652  652  652  LEU LEU A . n 
A 1 653  ARG 653  653  653  ARG ARG A . n 
A 1 654  LYS 654  654  654  LYS LYS A . n 
A 1 655  ASN 655  655  655  ASN ASN A . n 
A 1 656  PRO 656  656  656  PRO PRO A . n 
A 1 657  THR 657  657  657  THR THR A . n 
A 1 658  SER 658  658  658  SER SER A . n 
A 1 659  LEU 659  659  659  LEU LEU A . n 
A 1 660  PRO 660  660  660  PRO PRO A . n 
A 1 661  LEU 661  661  661  LEU LEU A . n 
A 1 662  GLY 662  662  662  GLY GLY A . n 
A 1 663  GLN 663  663  663  GLN GLN A . n 
A 1 664  TYR 664  664  664  TYR TYR A . n 
A 1 665  PRO 665  665  665  PRO PRO A . n 
A 1 666  GLU 666  666  666  GLU GLU A . n 
A 1 667  ASP 667  667  667  ASP ASP A . n 
A 1 668  VAL 668  668  668  VAL VAL A . n 
A 1 669  LYS 669  669  669  LYS LYS A . n 
A 1 670  PHE 670  670  670  PHE PHE A . n 
A 1 671  GLY 671  671  671  GLY GLY A . n 
A 1 672  ASP 672  672  672  ASP ASP A . n 
A 1 673  PRO 673  673  673  PRO PRO A . n 
A 1 674  ARG 674  674  674  ARG ARG A . n 
A 1 675  GLU 675  675  675  GLU GLU A . n 
A 1 676  ILE 676  676  676  ILE ILE A . n 
A 1 677  SER 677  677  677  SER SER A . n 
A 1 678  LEU 678  678  678  LEU LEU A . n 
A 1 679  ARG 679  679  679  ARG ARG A . n 
A 1 680  VAL 680  680  680  VAL VAL A . n 
A 1 681  GLY 681  681  681  GLY GLY A . n 
A 1 682  ASN 682  682  682  ASN ASN A . n 
A 1 683  GLY 683  683  683  GLY GLY A . n 
A 1 684  PRO 684  684  684  PRO PRO A . n 
A 1 685  THR 685  685  685  THR THR A . n 
A 1 686  LEU 686  686  686  LEU LEU A . n 
A 1 687  ALA 687  687  687  ALA ALA A . n 
A 1 688  PHE 688  688  688  PHE PHE A . n 
A 1 689  SER 689  689  689  SER SER A . n 
A 1 690  GLU 690  690  690  GLU GLU A . n 
A 1 691  GLN 691  691  691  GLN GLN A . n 
A 1 692  GLY 692  692  692  GLY GLY A . n 
A 1 693  LEU 693  693  693  LEU LEU A . n 
A 1 694  LEU 694  694  694  LEU LEU A . n 
A 1 695  LYS 695  695  695  LYS LYS A . n 
A 1 696  SER 696  696  696  SER SER A . n 
A 1 697  ILE 697  697  697  ILE ILE A . n 
A 1 698  GLN 698  698  698  GLN GLN A . n 
A 1 699  LEU 699  699  699  LEU LEU A . n 
A 1 700  THR 700  700  700  THR THR A . n 
A 1 701  GLN 701  701  701  GLN GLN A . n 
A 1 702  ASP 702  702  702  ASP ASP A . n 
A 1 703  SER 703  703  703  SER SER A . n 
A 1 704  PRO 704  704  704  PRO PRO A . n 
A 1 705  HIS 705  705  705  HIS HIS A . n 
A 1 706  VAL 706  706  706  VAL VAL A . n 
A 1 707  PRO 707  707  707  PRO PRO A . n 
A 1 708  VAL 708  708  708  VAL VAL A . n 
A 1 709  HIS 709  709  709  HIS HIS A . n 
A 1 710  PHE 710  710  710  PHE PHE A . n 
A 1 711  LYS 711  711  711  LYS LYS A . n 
A 1 712  PHE 712  712  712  PHE PHE A . n 
A 1 713  LEU 713  713  713  LEU LEU A . n 
A 1 714  LYS 714  714  714  LYS LYS A . n 
A 1 715  TYR 715  715  715  TYR TYR A . n 
A 1 716  GLY 716  716  716  GLY GLY A . n 
A 1 717  VAL 717  717  717  VAL VAL A . n 
A 1 718  ARG 718  718  718  ARG ARG A . n 
A 1 719  SER 719  719  719  SER SER A . n 
A 1 720  HIS 720  720  720  HIS HIS A . n 
A 1 721  GLY 721  721  721  GLY GLY A . n 
A 1 722  ASP 722  722  722  ASP ASP A . n 
A 1 723  ARG 723  723  723  ARG ARG A . n 
A 1 724  SER 724  724  724  SER SER A . n 
A 1 725  GLY 725  725  725  GLY GLY A . n 
A 1 726  ALA 726  726  726  ALA ALA A . n 
A 1 727  TYR 727  727  727  TYR TYR A . n 
A 1 728  LEU 728  728  728  LEU LEU A . n 
A 1 729  PHE 729  729  729  PHE PHE A . n 
A 1 730  LEU 730  730  730  LEU LEU A . n 
A 1 731  PRO 731  731  731  PRO PRO A . n 
A 1 732  ASN 732  732  732  ASN ASN A . n 
A 1 733  GLY 733  733  733  GLY GLY A . n 
A 1 734  PRO 734  734  734  PRO PRO A . n 
A 1 735  ALA 735  735  735  ALA ALA A . n 
A 1 736  SER 736  736  736  SER SER A . n 
A 1 737  PRO 737  737  737  PRO PRO A . n 
A 1 738  VAL 738  738  738  VAL VAL A . n 
A 1 739  GLU 739  739  739  GLU GLU A . n 
A 1 740  LEU 740  740  740  LEU LEU A . n 
A 1 741  GLY 741  741  741  GLY GLY A . n 
A 1 742  GLN 742  742  742  GLN GLN A . n 
A 1 743  PRO 743  743  743  PRO PRO A . n 
A 1 744  VAL 744  744  744  VAL VAL A . n 
A 1 745  VAL 745  745  745  VAL VAL A . n 
A 1 746  LEU 746  746  746  LEU LEU A . n 
A 1 747  VAL 747  747  747  VAL VAL A . n 
A 1 748  THR 748  748  748  THR THR A . n 
A 1 749  LYS 749  749  749  LYS LYS A . n 
A 1 750  GLY 750  750  750  GLY GLY A . n 
A 1 751  LYS 751  751  751  LYS LYS A . n 
A 1 752  LEU 752  752  752  LEU LEU A . n 
A 1 753  GLU 753  753  753  GLU GLU A . n 
A 1 754  SER 754  754  754  SER SER A . n 
A 1 755  SER 755  755  755  SER SER A . n 
A 1 756  VAL 756  756  756  VAL VAL A . n 
A 1 757  SER 757  757  757  SER SER A . n 
A 1 758  VAL 758  758  758  VAL VAL A . n 
A 1 759  GLY 759  759  759  GLY GLY A . n 
A 1 760  LEU 760  760  760  LEU LEU A . n 
A 1 761  PRO 761  761  761  PRO PRO A . n 
A 1 762  SER 762  762  762  SER SER A . n 
A 1 763  VAL 763  763  763  VAL VAL A . n 
A 1 764  VAL 764  764  764  VAL VAL A . n 
A 1 765  HIS 765  765  765  HIS HIS A . n 
A 1 766  GLN 766  766  766  GLN GLN A . n 
A 1 767  THR 767  767  767  THR THR A . n 
A 1 768  ILE 768  768  768  ILE ILE A . n 
A 1 769  MET 769  769  769  MET MET A . n 
A 1 770  ARG 770  770  770  ARG ARG A . n 
A 1 771  GLY 771  771  771  GLY GLY A . n 
A 1 772  GLY 772  772  772  GLY GLY A . n 
A 1 773  ALA 773  773  773  ALA ALA A . n 
A 1 774  PRO 774  774  774  PRO PRO A . n 
A 1 775  GLU 775  775  775  GLU GLU A . n 
A 1 776  ILE 776  776  776  ILE ILE A . n 
A 1 777  ARG 777  777  777  ARG ARG A . n 
A 1 778  ASN 778  778  778  ASN ASN A . n 
A 1 779  LEU 779  779  779  LEU LEU A . n 
A 1 780  VAL 780  780  780  VAL VAL A . n 
A 1 781  ASP 781  781  781  ASP ASP A . n 
A 1 782  ILE 782  782  782  ILE ILE A . n 
A 1 783  GLY 783  783  783  GLY GLY A . n 
A 1 784  SER 784  784  784  SER SER A . n 
A 1 785  LEU 785  785  785  LEU LEU A . n 
A 1 786  ASP 786  786  786  ASP ASP A . n 
A 1 787  ASN 787  787  787  ASN ASN A . n 
A 1 788  THR 788  788  788  THR THR A . n 
A 1 789  GLU 789  789  789  GLU GLU A . n 
A 1 790  ILE 790  790  790  ILE ILE A . n 
A 1 791  VAL 791  791  791  VAL VAL A . n 
A 1 792  MET 792  792  792  MET MET A . n 
A 1 793  ARG 793  793  793  ARG ARG A . n 
A 1 794  LEU 794  794  794  LEU LEU A . n 
A 1 795  GLU 795  795  795  GLU GLU A . n 
A 1 796  THR 796  796  796  THR THR A . n 
A 1 797  HIS 797  797  797  HIS HIS A . n 
A 1 798  ILE 798  798  798  ILE ILE A . n 
A 1 799  ASP 799  799  799  ASP ASP A . n 
A 1 800  SER 800  800  800  SER SER A . n 
A 1 801  GLY 801  801  801  GLY GLY A . n 
A 1 802  ASP 802  802  802  ASP ASP A . n 
A 1 803  ILE 803  803  803  ILE ILE A . n 
A 1 804  PHE 804  804  804  PHE PHE A . n 
A 1 805  TYR 805  805  805  TYR TYR A . n 
A 1 806  THR 806  806  806  THR THR A . n 
A 1 807  ASP 807  807  807  ASP ASP A . n 
A 1 808  LEU 808  808  808  LEU LEU A . n 
A 1 809  ASN 809  809  809  ASN ASN A . n 
A 1 810  GLY 810  810  810  GLY GLY A . n 
A 1 811  LEU 811  811  811  LEU LEU A . n 
A 1 812  GLN 812  812  812  GLN GLN A . n 
A 1 813  PHE 813  813  813  PHE PHE A . n 
A 1 814  ILE 814  814  814  ILE ILE A . n 
A 1 815  LYS 815  815  815  LYS LYS A . n 
A 1 816  ARG 816  816  816  ARG ARG A . n 
A 1 817  ARG 817  817  817  ARG ARG A . n 
A 1 818  ARG 818  818  818  ARG ARG A . n 
A 1 819  LEU 819  819  819  LEU LEU A . n 
A 1 820  ASP 820  820  820  ASP ASP A . n 
A 1 821  LYS 821  821  821  LYS LYS A . n 
A 1 822  LEU 822  822  822  LEU LEU A . n 
A 1 823  PRO 823  823  823  PRO PRO A . n 
A 1 824  LEU 824  824  824  LEU LEU A . n 
A 1 825  GLN 825  825  825  GLN GLN A . n 
A 1 826  ALA 826  826  826  ALA ALA A . n 
A 1 827  ASN 827  827  827  ASN ASN A . n 
A 1 828  TYR 828  828  828  TYR TYR A . n 
A 1 829  TYR 829  829  829  TYR TYR A . n 
A 1 830  PRO 830  830  830  PRO PRO A . n 
A 1 831  ILE 831  831  831  ILE ILE A . n 
A 1 832  PRO 832  832  832  PRO PRO A . n 
A 1 833  SER 833  833  833  SER SER A . n 
A 1 834  GLY 834  834  834  GLY GLY A . n 
A 1 835  MET 835  835  835  MET MET A . n 
A 1 836  PHE 836  836  836  PHE PHE A . n 
A 1 837  ILE 837  837  837  ILE ILE A . n 
A 1 838  GLU 838  838  838  GLU GLU A . n 
A 1 839  ASP 839  839  839  ASP ASP A . n 
A 1 840  ALA 840  840  840  ALA ALA A . n 
A 1 841  ASN 841  841  841  ASN ASN A . n 
A 1 842  THR 842  842  842  THR THR A . n 
A 1 843  ARG 843  843  843  ARG ARG A . n 
A 1 844  LEU 844  844  844  LEU LEU A . n 
A 1 845  THR 845  845  845  THR THR A . n 
A 1 846  LEU 846  846  846  LEU LEU A . n 
A 1 847  LEU 847  847  847  LEU LEU A . n 
A 1 848  THR 848  848  848  THR THR A . n 
A 1 849  GLY 849  849  849  GLY GLY A . n 
A 1 850  GLN 850  850  850  GLN GLN A . n 
A 1 851  PRO 851  851  851  PRO PRO A . n 
A 1 852  LEU 852  852  852  LEU LEU A . n 
A 1 853  GLY 853  853  853  GLY GLY A . n 
A 1 854  GLY 854  854  854  GLY GLY A . n 
A 1 855  SER 855  855  855  SER SER A . n 
A 1 856  SER 856  856  856  SER SER A . n 
A 1 857  LEU 857  857  857  LEU LEU A . n 
A 1 858  ALA 858  858  858  ALA ALA A . n 
A 1 859  SER 859  859  859  SER SER A . n 
A 1 860  GLY 860  860  860  GLY GLY A . n 
A 1 861  GLU 861  861  861  GLU GLU A . n 
A 1 862  LEU 862  862  862  LEU LEU A . n 
A 1 863  GLU 863  863  863  GLU GLU A . n 
A 1 864  ILE 864  864  864  ILE ILE A . n 
A 1 865  MET 865  865  865  MET MET A . n 
A 1 866  GLN 866  866  866  GLN GLN A . n 
A 1 867  ASP 867  867  867  ASP ASP A . n 
A 1 868  ARG 868  868  868  ARG ARG A . n 
A 1 869  ARG 869  869  869  ARG ARG A . n 
A 1 870  LEU 870  870  870  LEU LEU A . n 
A 1 871  ALA 871  871  871  ALA ALA A . n 
A 1 872  SER 872  872  872  SER SER A . n 
A 1 873  ASP 873  873  873  ASP ASP A . n 
A 1 874  ASP 874  874  874  ASP ASP A . n 
A 1 875  GLU 875  875  875  GLU GLU A . n 
A 1 876  ARG 876  876  876  ARG ARG A . n 
A 1 877  GLY 877  877  877  GLY GLY A . n 
A 1 878  LEU 878  878  878  LEU LEU A . n 
A 1 879  GLY 879  879  879  GLY GLY A . n 
A 1 880  GLN 880  880  880  GLN GLN A . n 
A 1 881  GLY 881  881  881  GLY GLY A . n 
A 1 882  VAL 882  882  882  VAL VAL A . n 
A 1 883  LEU 883  883  883  LEU LEU A . n 
A 1 884  ASP 884  884  884  ASP ASP A . n 
A 1 885  ASN 885  885  885  ASN ASN A . n 
A 1 886  LYS 886  886  886  LYS LYS A . n 
A 1 887  PRO 887  887  887  PRO PRO A . n 
A 1 888  VAL 888  888  888  VAL VAL A . n 
A 1 889  LEU 889  889  889  LEU LEU A . n 
A 1 890  HIS 890  890  890  HIS HIS A . n 
A 1 891  ILE 891  891  891  ILE ILE A . n 
A 1 892  TYR 892  892  892  TYR TYR A . n 
A 1 893  ARG 893  893  893  ARG ARG A . n 
A 1 894  LEU 894  894  894  LEU LEU A . n 
A 1 895  VAL 895  895  895  VAL VAL A . n 
A 1 896  LEU 896  896  896  LEU LEU A . n 
A 1 897  GLU 897  897  897  GLU GLU A . n 
A 1 898  LYS 898  898  898  LYS LYS A . n 
A 1 899  VAL 899  899  899  VAL VAL A . n 
A 1 900  ASN 900  900  900  ASN ASN A . n 
A 1 901  ASN 901  901  901  ASN ASN A . n 
A 1 902  CYS 902  902  902  CYS CYS A . n 
A 1 903  VAL 903  903  903  VAL VAL A . n 
A 1 904  ARG 904  904  904  ARG ARG A . n 
A 1 905  PRO 905  905  905  PRO PRO A . n 
A 1 906  SER 906  906  906  SER SER A . n 
A 1 907  LYS 907  907  907  LYS LYS A . n 
A 1 908  LEU 908  908  908  LEU LEU A . n 
A 1 909  HIS 909  909  909  HIS HIS A . n 
A 1 910  PRO 910  910  910  PRO PRO A . n 
A 1 911  ALA 911  911  911  ALA ALA A . n 
A 1 912  GLY 912  912  912  GLY GLY A . n 
A 1 913  TYR 913  913  913  TYR TYR A . n 
A 1 914  LEU 914  914  914  LEU LEU A . n 
A 1 915  THR 915  915  915  THR THR A . n 
A 1 916  SER 916  916  916  SER SER A . n 
A 1 917  ALA 917  917  917  ALA ALA A . n 
A 1 918  ALA 918  918  918  ALA ALA A . n 
A 1 919  HIS 919  919  919  HIS HIS A . n 
A 1 920  LYS 920  920  920  LYS LYS A . n 
A 1 921  ALA 921  921  921  ALA ALA A . n 
A 1 922  SER 922  922  922  SER SER A . n 
A 1 923  GLN 923  923  923  GLN GLN A . n 
A 1 924  SER 924  924  924  SER SER A . n 
A 1 925  LEU 925  925  925  LEU LEU A . n 
A 1 926  LEU 926  926  926  LEU LEU A . n 
A 1 927  ASP 927  927  927  ASP ASP A . n 
A 1 928  PRO 928  928  928  PRO PRO A . n 
A 1 929  LEU 929  929  929  LEU LEU A . n 
A 1 930  ASP 930  930  930  ASP ASP A . n 
A 1 931  LYS 931  931  931  LYS LYS A . n 
A 1 932  PHE 932  932  932  PHE PHE A . n 
A 1 933  ILE 933  933  933  ILE ILE A . n 
A 1 934  PHE 934  934  934  PHE PHE A . n 
A 1 935  ALA 935  935  935  ALA ALA A . n 
A 1 936  GLU 936  936  936  GLU GLU A . n 
A 1 937  ASN 937  937  937  ASN ASN A . n 
A 1 938  GLU 938  938  938  GLU GLU A . n 
A 1 939  TRP 939  939  939  TRP TRP A . n 
A 1 940  ILE 940  940  940  ILE ILE A . n 
A 1 941  GLY 941  941  941  GLY GLY A . n 
A 1 942  ALA 942  942  942  ALA ALA A . n 
A 1 943  GLN 943  943  943  GLN GLN A . n 
A 1 944  GLY 944  944  944  GLY GLY A . n 
A 1 945  GLN 945  945  945  GLN GLN A . n 
A 1 946  PHE 946  946  946  PHE PHE A . n 
A 1 947  GLY 947  947  947  GLY GLY A . n 
A 1 948  GLY 948  948  948  GLY GLY A . n 
A 1 949  ASP 949  949  949  ASP ASP A . n 
A 1 950  HIS 950  950  950  HIS HIS A . n 
A 1 951  PRO 951  951  951  PRO PRO A . n 
A 1 952  SER 952  952  952  SER SER A . n 
A 1 953  ALA 953  953  953  ALA ALA A . n 
A 1 954  ARG 954  954  954  ARG ARG A . n 
A 1 955  GLU 955  955  955  GLU GLU A . n 
A 1 956  ASP 956  956  956  ASP ASP A . n 
A 1 957  LEU 957  957  957  LEU LEU A . n 
A 1 958  ASP 958  958  958  ASP ASP A . n 
A 1 959  VAL 959  959  959  VAL VAL A . n 
A 1 960  SER 960  960  960  SER SER A . n 
A 1 961  VAL 961  961  961  VAL VAL A . n 
A 1 962  MET 962  962  962  MET MET A . n 
A 1 963  ARG 963  963  963  ARG ARG A . n 
A 1 964  ARG 964  964  964  ARG ARG A . n 
A 1 965  LEU 965  965  965  LEU LEU A . n 
A 1 966  THR 966  966  966  THR THR A . n 
A 1 967  LYS 967  967  967  LYS LYS A . n 
A 1 968  SER 968  968  968  SER SER A . n 
A 1 969  SER 969  969  969  SER SER A . n 
A 1 970  ALA 970  970  970  ALA ALA A . n 
A 1 971  LYS 971  971  971  LYS LYS A . n 
A 1 972  THR 972  972  972  THR THR A . n 
A 1 973  GLN 973  973  973  GLN GLN A . n 
A 1 974  ARG 974  974  974  ARG ARG A . n 
A 1 975  VAL 975  975  975  VAL VAL A . n 
A 1 976  GLY 976  976  976  GLY GLY A . n 
A 1 977  TYR 977  977  977  TYR TYR A . n 
A 1 978  VAL 978  978  978  VAL VAL A . n 
A 1 979  LEU 979  979  979  LEU LEU A . n 
A 1 980  HIS 980  980  980  HIS HIS A . n 
A 1 981  ARG 981  981  981  ARG ARG A . n 
A 1 982  THR 982  982  982  THR THR A . n 
A 1 983  ASN 983  983  983  ASN ASN A . n 
A 1 984  LEU 984  984  984  LEU LEU A . n 
A 1 985  MET 985  985  985  MET MET A . n 
A 1 986  GLN 986  986  986  GLN GLN A . n 
A 1 987  CYS 987  987  987  CYS CYS A . n 
A 1 988  GLY 988  988  988  GLY GLY A . n 
A 1 989  THR 989  989  989  THR THR A . n 
A 1 990  PRO 990  990  990  PRO PRO A . n 
A 1 991  GLU 991  991  991  GLU GLU A . n 
A 1 992  GLU 992  992  992  GLU GLU A . n 
A 1 993  HIS 993  993  993  HIS HIS A . n 
A 1 994  THR 994  994  994  THR THR A . n 
A 1 995  GLN 995  995  995  GLN GLN A . n 
A 1 996  LYS 996  996  996  LYS LYS A . n 
A 1 997  LEU 997  997  997  LEU LEU A . n 
A 1 998  ASP 998  998  998  ASP ASP A . n 
A 1 999  VAL 999  999  999  VAL VAL A . n 
A 1 1000 CYS 1000 1000 1000 CYS CYS A . n 
A 1 1001 HIS 1001 1001 1001 HIS HIS A . n 
A 1 1002 LEU 1002 1002 1002 LEU LEU A . n 
A 1 1003 LEU 1003 1003 1003 LEU LEU A . n 
A 1 1004 PRO 1004 1004 1004 PRO PRO A . n 
A 1 1005 ASN 1005 1005 1005 ASN ASN A . n 
A 1 1006 VAL 1006 1006 1006 VAL VAL A . n 
A 1 1007 ALA 1007 1007 1007 ALA ALA A . n 
A 1 1008 ARG 1008 1008 1008 ARG ARG A . n 
A 1 1009 CYS 1009 1009 1009 CYS CYS A . n 
A 1 1010 GLU 1010 1010 1010 GLU GLU A . n 
A 1 1011 ARG 1011 1011 1011 ARG ARG A . n 
A 1 1012 THR 1012 1012 1012 THR THR A . n 
A 1 1013 THR 1013 1013 1013 THR THR A . n 
A 1 1014 LEU 1014 1014 1014 LEU LEU A . n 
A 1 1015 THR 1015 1015 1015 THR THR A . n 
A 1 1016 PHE 1016 1016 1016 PHE PHE A . n 
A 1 1017 LEU 1017 1017 1017 LEU LEU A . n 
A 1 1018 GLN 1018 1018 1018 GLN GLN A . n 
A 1 1019 ASN 1019 1019 1019 ASN ASN A . n 
A 1 1020 LEU 1020 1020 1020 LEU LEU A . n 
A 1 1021 GLU 1021 1021 1021 GLU GLU A . n 
A 1 1022 HIS 1022 1022 1022 HIS HIS A . n 
A 1 1023 LEU 1023 1023 1023 LEU LEU A . n 
A 1 1024 ASP 1024 1024 1024 ASP ASP A . n 
A 1 1025 GLY 1025 1025 1025 GLY GLY A . n 
A 1 1026 MET 1026 1026 1026 MET MET A . n 
A 1 1027 VAL 1027 1027 1027 VAL VAL A . n 
A 1 1028 ALA 1028 1028 1028 ALA ALA A . n 
A 1 1029 PRO 1029 1029 1029 PRO PRO A . n 
A 1 1030 GLU 1030 1030 1030 GLU GLU A . n 
A 1 1031 VAL 1031 1031 1031 VAL VAL A . n 
A 1 1032 CYS 1032 1032 1032 CYS CYS A . n 
A 1 1033 PRO 1033 1033 1033 PRO PRO A . n 
A 1 1034 MET 1034 1034 1034 MET MET A . n 
A 1 1035 GLU 1035 1035 1035 GLU GLU A . n 
A 1 1036 THR 1036 1036 1036 THR THR A . n 
A 1 1037 ALA 1037 1037 1037 ALA ALA A . n 
A 1 1038 ALA 1038 1038 1038 ALA ALA A . n 
A 1 1039 TYR 1039 1039 1039 TYR TYR A . n 
A 1 1040 VAL 1040 1040 1040 VAL VAL A . n 
A 1 1041 SER 1041 1041 1041 SER SER A . n 
A 1 1042 SER 1042 1042 1042 SER SER A . n 
A 1 1043 HIS 1043 1043 1043 HIS HIS A . n 
A 1 1044 SER 1044 1044 1044 SER SER A . n 
A 1 1045 SER 1045 1045 ?    ?   ?   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    2001 2001 NAG NAG A . 
C 3 ZN  1    2004 2004 ZN  ZN  A . 
D 4 FMF 1    2003 2003 FMF FMF A . 
E 5 MPD 1    2002 2002 MPD MPD A . 
F 6 HOH 1    2005 1    HOH HOH A . 
F 6 HOH 2    2006 2    HOH HOH A . 
F 6 HOH 3    2007 3    HOH HOH A . 
F 6 HOH 4    2008 4    HOH HOH A . 
F 6 HOH 5    2009 5    HOH HOH A . 
F 6 HOH 6    2010 6    HOH HOH A . 
F 6 HOH 7    2011 7    HOH HOH A . 
F 6 HOH 8    2012 8    HOH HOH A . 
F 6 HOH 9    2013 9    HOH HOH A . 
F 6 HOH 10   2014 10   HOH HOH A . 
F 6 HOH 11   2015 11   HOH HOH A . 
F 6 HOH 12   2016 12   HOH HOH A . 
F 6 HOH 13   2017 13   HOH HOH A . 
F 6 HOH 14   2018 14   HOH HOH A . 
F 6 HOH 15   2019 15   HOH HOH A . 
F 6 HOH 16   2020 16   HOH HOH A . 
F 6 HOH 17   2021 17   HOH HOH A . 
F 6 HOH 18   2022 18   HOH HOH A . 
F 6 HOH 19   2023 19   HOH HOH A . 
F 6 HOH 20   2024 20   HOH HOH A . 
F 6 HOH 21   2025 21   HOH HOH A . 
F 6 HOH 22   2026 22   HOH HOH A . 
F 6 HOH 23   2027 23   HOH HOH A . 
F 6 HOH 24   2028 24   HOH HOH A . 
F 6 HOH 25   2029 25   HOH HOH A . 
F 6 HOH 26   2030 26   HOH HOH A . 
F 6 HOH 27   2031 27   HOH HOH A . 
F 6 HOH 28   2032 28   HOH HOH A . 
F 6 HOH 29   2033 29   HOH HOH A . 
F 6 HOH 30   2034 30   HOH HOH A . 
F 6 HOH 31   2035 31   HOH HOH A . 
F 6 HOH 32   2036 32   HOH HOH A . 
F 6 HOH 33   2037 33   HOH HOH A . 
F 6 HOH 34   2038 34   HOH HOH A . 
F 6 HOH 35   2039 35   HOH HOH A . 
F 6 HOH 36   2040 36   HOH HOH A . 
F 6 HOH 37   2041 37   HOH HOH A . 
F 6 HOH 38   2042 38   HOH HOH A . 
F 6 HOH 39   2043 39   HOH HOH A . 
F 6 HOH 40   2044 40   HOH HOH A . 
F 6 HOH 41   2045 41   HOH HOH A . 
F 6 HOH 42   2046 42   HOH HOH A . 
F 6 HOH 43   2047 43   HOH HOH A . 
F 6 HOH 44   2048 44   HOH HOH A . 
F 6 HOH 45   2049 45   HOH HOH A . 
F 6 HOH 46   2050 46   HOH HOH A . 
F 6 HOH 47   2051 47   HOH HOH A . 
F 6 HOH 48   2052 48   HOH HOH A . 
F 6 HOH 49   2053 49   HOH HOH A . 
F 6 HOH 50   2054 50   HOH HOH A . 
F 6 HOH 51   2055 51   HOH HOH A . 
F 6 HOH 52   2056 52   HOH HOH A . 
F 6 HOH 53   2057 53   HOH HOH A . 
F 6 HOH 54   2058 54   HOH HOH A . 
F 6 HOH 55   2059 55   HOH HOH A . 
F 6 HOH 56   2060 56   HOH HOH A . 
F 6 HOH 57   2061 57   HOH HOH A . 
F 6 HOH 58   2062 58   HOH HOH A . 
F 6 HOH 59   2063 59   HOH HOH A . 
F 6 HOH 60   2064 60   HOH HOH A . 
F 6 HOH 61   2065 61   HOH HOH A . 
F 6 HOH 62   2066 62   HOH HOH A . 
F 6 HOH 63   2067 63   HOH HOH A . 
F 6 HOH 64   2068 64   HOH HOH A . 
F 6 HOH 65   2069 65   HOH HOH A . 
F 6 HOH 66   2070 66   HOH HOH A . 
F 6 HOH 67   2071 67   HOH HOH A . 
F 6 HOH 68   2072 68   HOH HOH A . 
F 6 HOH 69   2073 69   HOH HOH A . 
F 6 HOH 70   2074 70   HOH HOH A . 
F 6 HOH 71   2075 71   HOH HOH A . 
F 6 HOH 72   2076 72   HOH HOH A . 
F 6 HOH 73   2077 73   HOH HOH A . 
F 6 HOH 74   2078 74   HOH HOH A . 
F 6 HOH 75   2079 75   HOH HOH A . 
F 6 HOH 76   2080 76   HOH HOH A . 
F 6 HOH 77   2081 77   HOH HOH A . 
F 6 HOH 78   2082 78   HOH HOH A . 
F 6 HOH 79   2083 79   HOH HOH A . 
F 6 HOH 80   2084 80   HOH HOH A . 
F 6 HOH 81   2085 81   HOH HOH A . 
F 6 HOH 82   2086 82   HOH HOH A . 
F 6 HOH 83   2087 83   HOH HOH A . 
F 6 HOH 84   2088 84   HOH HOH A . 
F 6 HOH 85   2089 85   HOH HOH A . 
F 6 HOH 86   2090 86   HOH HOH A . 
F 6 HOH 87   2091 87   HOH HOH A . 
F 6 HOH 88   2092 88   HOH HOH A . 
F 6 HOH 89   2093 89   HOH HOH A . 
F 6 HOH 90   2094 90   HOH HOH A . 
F 6 HOH 91   2095 91   HOH HOH A . 
F 6 HOH 92   2096 92   HOH HOH A . 
F 6 HOH 93   2097 93   HOH HOH A . 
F 6 HOH 94   2098 94   HOH HOH A . 
F 6 HOH 95   2099 95   HOH HOH A . 
F 6 HOH 96   2100 96   HOH HOH A . 
F 6 HOH 97   2101 97   HOH HOH A . 
F 6 HOH 98   2102 98   HOH HOH A . 
F 6 HOH 99   2103 99   HOH HOH A . 
F 6 HOH 100  2104 100  HOH HOH A . 
F 6 HOH 101  2105 101  HOH HOH A . 
F 6 HOH 102  2106 102  HOH HOH A . 
F 6 HOH 103  2107 103  HOH HOH A . 
F 6 HOH 104  2108 104  HOH HOH A . 
F 6 HOH 105  2109 105  HOH HOH A . 
F 6 HOH 106  2110 106  HOH HOH A . 
F 6 HOH 107  2111 107  HOH HOH A . 
F 6 HOH 108  2112 108  HOH HOH A . 
F 6 HOH 109  2113 109  HOH HOH A . 
F 6 HOH 110  2114 110  HOH HOH A . 
F 6 HOH 111  2115 111  HOH HOH A . 
F 6 HOH 112  2116 112  HOH HOH A . 
F 6 HOH 113  2117 113  HOH HOH A . 
F 6 HOH 114  2118 114  HOH HOH A . 
F 6 HOH 115  2119 115  HOH HOH A . 
F 6 HOH 116  2120 116  HOH HOH A . 
F 6 HOH 117  2121 117  HOH HOH A . 
F 6 HOH 118  2122 118  HOH HOH A . 
F 6 HOH 119  2123 119  HOH HOH A . 
F 6 HOH 120  2124 120  HOH HOH A . 
F 6 HOH 121  2125 121  HOH HOH A . 
F 6 HOH 122  2126 122  HOH HOH A . 
F 6 HOH 123  2127 123  HOH HOH A . 
F 6 HOH 124  2128 124  HOH HOH A . 
F 6 HOH 125  2129 125  HOH HOH A . 
F 6 HOH 126  2130 126  HOH HOH A . 
F 6 HOH 127  2131 127  HOH HOH A . 
F 6 HOH 128  2132 128  HOH HOH A . 
F 6 HOH 129  2133 129  HOH HOH A . 
F 6 HOH 130  2134 130  HOH HOH A . 
F 6 HOH 131  2135 131  HOH HOH A . 
F 6 HOH 132  2136 132  HOH HOH A . 
F 6 HOH 133  2137 133  HOH HOH A . 
F 6 HOH 134  2138 134  HOH HOH A . 
F 6 HOH 135  2139 135  HOH HOH A . 
F 6 HOH 136  2140 136  HOH HOH A . 
F 6 HOH 137  2141 137  HOH HOH A . 
F 6 HOH 138  2142 138  HOH HOH A . 
F 6 HOH 139  2143 139  HOH HOH A . 
F 6 HOH 140  2144 140  HOH HOH A . 
F 6 HOH 141  2145 141  HOH HOH A . 
F 6 HOH 142  2146 142  HOH HOH A . 
F 6 HOH 143  2147 143  HOH HOH A . 
F 6 HOH 144  2148 144  HOH HOH A . 
F 6 HOH 145  2149 145  HOH HOH A . 
F 6 HOH 146  2150 146  HOH HOH A . 
F 6 HOH 147  2151 147  HOH HOH A . 
F 6 HOH 148  2152 148  HOH HOH A . 
F 6 HOH 149  2153 149  HOH HOH A . 
F 6 HOH 150  2154 150  HOH HOH A . 
F 6 HOH 151  2155 151  HOH HOH A . 
F 6 HOH 152  2156 152  HOH HOH A . 
F 6 HOH 153  2157 153  HOH HOH A . 
F 6 HOH 154  2158 154  HOH HOH A . 
F 6 HOH 155  2159 155  HOH HOH A . 
F 6 HOH 156  2160 156  HOH HOH A . 
F 6 HOH 157  2161 157  HOH HOH A . 
F 6 HOH 158  2162 158  HOH HOH A . 
F 6 HOH 159  2163 159  HOH HOH A . 
F 6 HOH 160  2164 160  HOH HOH A . 
F 6 HOH 161  2165 161  HOH HOH A . 
F 6 HOH 162  2166 162  HOH HOH A . 
F 6 HOH 163  2167 163  HOH HOH A . 
F 6 HOH 164  2168 164  HOH HOH A . 
F 6 HOH 165  2169 165  HOH HOH A . 
F 6 HOH 166  2170 166  HOH HOH A . 
F 6 HOH 167  2171 167  HOH HOH A . 
F 6 HOH 168  2172 168  HOH HOH A . 
F 6 HOH 169  2173 169  HOH HOH A . 
F 6 HOH 170  2174 170  HOH HOH A . 
F 6 HOH 171  2175 171  HOH HOH A . 
F 6 HOH 172  2176 172  HOH HOH A . 
F 6 HOH 173  2177 173  HOH HOH A . 
F 6 HOH 174  2178 174  HOH HOH A . 
F 6 HOH 175  2179 175  HOH HOH A . 
F 6 HOH 176  2180 176  HOH HOH A . 
F 6 HOH 177  2181 177  HOH HOH A . 
F 6 HOH 178  2182 178  HOH HOH A . 
F 6 HOH 179  2183 179  HOH HOH A . 
F 6 HOH 180  2184 180  HOH HOH A . 
F 6 HOH 181  2185 181  HOH HOH A . 
F 6 HOH 182  2186 182  HOH HOH A . 
F 6 HOH 183  2187 183  HOH HOH A . 
F 6 HOH 184  2188 184  HOH HOH A . 
F 6 HOH 185  2189 185  HOH HOH A . 
F 6 HOH 186  2190 186  HOH HOH A . 
F 6 HOH 187  2191 187  HOH HOH A . 
F 6 HOH 188  2192 188  HOH HOH A . 
F 6 HOH 189  2193 189  HOH HOH A . 
F 6 HOH 190  2194 190  HOH HOH A . 
F 6 HOH 191  2195 191  HOH HOH A . 
F 6 HOH 192  2196 192  HOH HOH A . 
F 6 HOH 193  2197 193  HOH HOH A . 
F 6 HOH 194  2198 194  HOH HOH A . 
F 6 HOH 195  2199 195  HOH HOH A . 
F 6 HOH 196  2200 196  HOH HOH A . 
F 6 HOH 197  2201 197  HOH HOH A . 
F 6 HOH 198  2202 198  HOH HOH A . 
F 6 HOH 199  2203 199  HOH HOH A . 
F 6 HOH 200  2204 200  HOH HOH A . 
F 6 HOH 201  2205 201  HOH HOH A . 
F 6 HOH 202  2206 202  HOH HOH A . 
F 6 HOH 203  2207 203  HOH HOH A . 
F 6 HOH 204  2208 204  HOH HOH A . 
F 6 HOH 205  2209 205  HOH HOH A . 
F 6 HOH 206  2210 206  HOH HOH A . 
F 6 HOH 207  2211 207  HOH HOH A . 
F 6 HOH 208  2212 208  HOH HOH A . 
F 6 HOH 209  2213 209  HOH HOH A . 
F 6 HOH 210  2214 210  HOH HOH A . 
F 6 HOH 211  2215 211  HOH HOH A . 
F 6 HOH 212  2216 212  HOH HOH A . 
F 6 HOH 213  2217 213  HOH HOH A . 
F 6 HOH 214  2218 214  HOH HOH A . 
F 6 HOH 215  2219 215  HOH HOH A . 
F 6 HOH 216  2220 216  HOH HOH A . 
F 6 HOH 217  2221 217  HOH HOH A . 
F 6 HOH 218  2222 218  HOH HOH A . 
F 6 HOH 219  2223 219  HOH HOH A . 
F 6 HOH 220  2224 220  HOH HOH A . 
F 6 HOH 221  2225 221  HOH HOH A . 
F 6 HOH 222  2226 222  HOH HOH A . 
F 6 HOH 223  2227 223  HOH HOH A . 
F 6 HOH 224  2228 224  HOH HOH A . 
F 6 HOH 225  2229 225  HOH HOH A . 
F 6 HOH 226  2230 226  HOH HOH A . 
F 6 HOH 227  2231 227  HOH HOH A . 
F 6 HOH 228  2232 228  HOH HOH A . 
F 6 HOH 229  2233 229  HOH HOH A . 
F 6 HOH 230  2234 230  HOH HOH A . 
F 6 HOH 231  2235 231  HOH HOH A . 
F 6 HOH 232  2236 232  HOH HOH A . 
F 6 HOH 233  2237 233  HOH HOH A . 
F 6 HOH 234  2238 234  HOH HOH A . 
F 6 HOH 235  2239 235  HOH HOH A . 
F 6 HOH 236  2240 236  HOH HOH A . 
F 6 HOH 237  2241 237  HOH HOH A . 
F 6 HOH 238  2242 238  HOH HOH A . 
F 6 HOH 239  2243 239  HOH HOH A . 
F 6 HOH 240  2244 240  HOH HOH A . 
F 6 HOH 241  2245 241  HOH HOH A . 
F 6 HOH 242  2246 242  HOH HOH A . 
F 6 HOH 243  2247 243  HOH HOH A . 
F 6 HOH 244  2248 244  HOH HOH A . 
F 6 HOH 245  2249 245  HOH HOH A . 
F 6 HOH 246  2250 246  HOH HOH A . 
F 6 HOH 247  2251 247  HOH HOH A . 
F 6 HOH 248  2252 248  HOH HOH A . 
F 6 HOH 249  2253 249  HOH HOH A . 
F 6 HOH 250  2254 250  HOH HOH A . 
F 6 HOH 251  2255 251  HOH HOH A . 
F 6 HOH 252  2256 252  HOH HOH A . 
F 6 HOH 253  2257 253  HOH HOH A . 
F 6 HOH 254  2258 254  HOH HOH A . 
F 6 HOH 255  2259 255  HOH HOH A . 
F 6 HOH 256  2260 256  HOH HOH A . 
F 6 HOH 257  2261 257  HOH HOH A . 
F 6 HOH 258  2262 258  HOH HOH A . 
F 6 HOH 259  2263 259  HOH HOH A . 
F 6 HOH 260  2264 260  HOH HOH A . 
F 6 HOH 261  2265 261  HOH HOH A . 
F 6 HOH 262  2266 262  HOH HOH A . 
F 6 HOH 263  2267 263  HOH HOH A . 
F 6 HOH 264  2268 264  HOH HOH A . 
F 6 HOH 265  2269 265  HOH HOH A . 
F 6 HOH 266  2270 266  HOH HOH A . 
F 6 HOH 267  2271 267  HOH HOH A . 
F 6 HOH 268  2272 268  HOH HOH A . 
F 6 HOH 269  2273 269  HOH HOH A . 
F 6 HOH 270  2274 270  HOH HOH A . 
F 6 HOH 271  2275 271  HOH HOH A . 
F 6 HOH 272  2276 272  HOH HOH A . 
F 6 HOH 273  2277 273  HOH HOH A . 
F 6 HOH 274  2278 274  HOH HOH A . 
F 6 HOH 275  2279 275  HOH HOH A . 
F 6 HOH 276  2280 276  HOH HOH A . 
F 6 HOH 277  2281 277  HOH HOH A . 
F 6 HOH 278  2282 278  HOH HOH A . 
F 6 HOH 279  2283 279  HOH HOH A . 
F 6 HOH 280  2284 280  HOH HOH A . 
F 6 HOH 281  2285 281  HOH HOH A . 
F 6 HOH 282  2286 282  HOH HOH A . 
F 6 HOH 283  2287 283  HOH HOH A . 
F 6 HOH 284  2288 284  HOH HOH A . 
F 6 HOH 285  2289 285  HOH HOH A . 
F 6 HOH 286  2290 286  HOH HOH A . 
F 6 HOH 287  2291 287  HOH HOH A . 
F 6 HOH 288  2292 288  HOH HOH A . 
F 6 HOH 289  2293 289  HOH HOH A . 
F 6 HOH 290  2294 290  HOH HOH A . 
F 6 HOH 291  2295 291  HOH HOH A . 
F 6 HOH 292  2296 292  HOH HOH A . 
F 6 HOH 293  2297 293  HOH HOH A . 
F 6 HOH 294  2298 294  HOH HOH A . 
F 6 HOH 295  2299 295  HOH HOH A . 
F 6 HOH 296  2300 296  HOH HOH A . 
F 6 HOH 297  2301 297  HOH HOH A . 
F 6 HOH 298  2302 298  HOH HOH A . 
F 6 HOH 299  2303 299  HOH HOH A . 
F 6 HOH 300  2304 300  HOH HOH A . 
F 6 HOH 301  2305 301  HOH HOH A . 
F 6 HOH 302  2306 302  HOH HOH A . 
F 6 HOH 303  2307 303  HOH HOH A . 
F 6 HOH 304  2308 304  HOH HOH A . 
F 6 HOH 305  2309 305  HOH HOH A . 
F 6 HOH 306  2310 306  HOH HOH A . 
F 6 HOH 307  2311 307  HOH HOH A . 
F 6 HOH 308  2312 308  HOH HOH A . 
F 6 HOH 309  2313 309  HOH HOH A . 
F 6 HOH 310  2314 310  HOH HOH A . 
F 6 HOH 311  2315 311  HOH HOH A . 
F 6 HOH 312  2316 312  HOH HOH A . 
F 6 HOH 313  2317 313  HOH HOH A . 
F 6 HOH 314  2318 314  HOH HOH A . 
F 6 HOH 315  2319 315  HOH HOH A . 
F 6 HOH 316  2320 316  HOH HOH A . 
F 6 HOH 317  2321 317  HOH HOH A . 
F 6 HOH 318  2322 318  HOH HOH A . 
F 6 HOH 319  2323 319  HOH HOH A . 
F 6 HOH 320  2324 320  HOH HOH A . 
F 6 HOH 321  2325 321  HOH HOH A . 
F 6 HOH 322  2326 322  HOH HOH A . 
F 6 HOH 323  2327 323  HOH HOH A . 
F 6 HOH 324  2328 324  HOH HOH A . 
F 6 HOH 325  2329 325  HOH HOH A . 
F 6 HOH 326  2330 326  HOH HOH A . 
F 6 HOH 327  2331 327  HOH HOH A . 
F 6 HOH 328  2332 328  HOH HOH A . 
F 6 HOH 329  2333 329  HOH HOH A . 
F 6 HOH 330  2334 330  HOH HOH A . 
F 6 HOH 331  2335 331  HOH HOH A . 
F 6 HOH 332  2336 332  HOH HOH A . 
F 6 HOH 333  2337 333  HOH HOH A . 
F 6 HOH 334  2338 334  HOH HOH A . 
F 6 HOH 335  2339 335  HOH HOH A . 
F 6 HOH 336  2340 336  HOH HOH A . 
F 6 HOH 337  2341 337  HOH HOH A . 
F 6 HOH 338  2342 338  HOH HOH A . 
F 6 HOH 339  2343 339  HOH HOH A . 
F 6 HOH 340  2344 340  HOH HOH A . 
F 6 HOH 341  2345 341  HOH HOH A . 
F 6 HOH 342  2346 342  HOH HOH A . 
F 6 HOH 343  2347 343  HOH HOH A . 
F 6 HOH 344  2348 344  HOH HOH A . 
F 6 HOH 345  2349 345  HOH HOH A . 
F 6 HOH 346  2350 346  HOH HOH A . 
F 6 HOH 347  2351 347  HOH HOH A . 
F 6 HOH 348  2352 348  HOH HOH A . 
F 6 HOH 349  2353 349  HOH HOH A . 
F 6 HOH 350  2354 350  HOH HOH A . 
F 6 HOH 351  2355 351  HOH HOH A . 
F 6 HOH 352  2356 352  HOH HOH A . 
F 6 HOH 353  2357 353  HOH HOH A . 
F 6 HOH 354  2358 354  HOH HOH A . 
F 6 HOH 355  2359 355  HOH HOH A . 
F 6 HOH 356  2360 356  HOH HOH A . 
F 6 HOH 357  2361 357  HOH HOH A . 
F 6 HOH 358  2362 358  HOH HOH A . 
F 6 HOH 359  2363 359  HOH HOH A . 
F 6 HOH 360  2364 360  HOH HOH A . 
F 6 HOH 361  2365 361  HOH HOH A . 
F 6 HOH 362  2366 362  HOH HOH A . 
F 6 HOH 363  2367 363  HOH HOH A . 
F 6 HOH 364  2368 364  HOH HOH A . 
F 6 HOH 365  2369 365  HOH HOH A . 
F 6 HOH 366  2370 366  HOH HOH A . 
F 6 HOH 367  2371 367  HOH HOH A . 
F 6 HOH 368  2372 368  HOH HOH A . 
F 6 HOH 369  2373 369  HOH HOH A . 
F 6 HOH 370  2374 370  HOH HOH A . 
F 6 HOH 371  2375 371  HOH HOH A . 
F 6 HOH 372  2376 372  HOH HOH A . 
F 6 HOH 373  2377 373  HOH HOH A . 
F 6 HOH 374  2378 374  HOH HOH A . 
F 6 HOH 375  2379 375  HOH HOH A . 
F 6 HOH 376  2380 376  HOH HOH A . 
F 6 HOH 377  2381 377  HOH HOH A . 
F 6 HOH 378  2382 378  HOH HOH A . 
F 6 HOH 379  2383 379  HOH HOH A . 
F 6 HOH 380  2384 380  HOH HOH A . 
F 6 HOH 381  2385 381  HOH HOH A . 
F 6 HOH 382  2386 382  HOH HOH A . 
F 6 HOH 383  2387 383  HOH HOH A . 
F 6 HOH 384  2388 384  HOH HOH A . 
F 6 HOH 385  2389 385  HOH HOH A . 
F 6 HOH 386  2390 386  HOH HOH A . 
F 6 HOH 387  2391 387  HOH HOH A . 
F 6 HOH 388  2392 388  HOH HOH A . 
F 6 HOH 389  2393 389  HOH HOH A . 
F 6 HOH 390  2394 390  HOH HOH A . 
F 6 HOH 391  2395 391  HOH HOH A . 
F 6 HOH 392  2396 392  HOH HOH A . 
F 6 HOH 393  2397 393  HOH HOH A . 
F 6 HOH 394  2398 394  HOH HOH A . 
F 6 HOH 395  2399 395  HOH HOH A . 
F 6 HOH 396  2400 396  HOH HOH A . 
F 6 HOH 397  2401 397  HOH HOH A . 
F 6 HOH 398  2402 398  HOH HOH A . 
F 6 HOH 399  2403 399  HOH HOH A . 
F 6 HOH 400  2404 400  HOH HOH A . 
F 6 HOH 401  2405 401  HOH HOH A . 
F 6 HOH 402  2406 402  HOH HOH A . 
F 6 HOH 403  2407 403  HOH HOH A . 
F 6 HOH 404  2408 404  HOH HOH A . 
F 6 HOH 405  2409 405  HOH HOH A . 
F 6 HOH 406  2410 406  HOH HOH A . 
F 6 HOH 407  2411 407  HOH HOH A . 
F 6 HOH 408  2412 408  HOH HOH A . 
F 6 HOH 409  2413 409  HOH HOH A . 
F 6 HOH 410  2414 410  HOH HOH A . 
F 6 HOH 411  2415 411  HOH HOH A . 
F 6 HOH 412  2416 412  HOH HOH A . 
F 6 HOH 413  2417 413  HOH HOH A . 
F 6 HOH 414  2418 414  HOH HOH A . 
F 6 HOH 415  2419 415  HOH HOH A . 
F 6 HOH 416  2420 416  HOH HOH A . 
F 6 HOH 417  2421 417  HOH HOH A . 
F 6 HOH 418  2422 418  HOH HOH A . 
F 6 HOH 419  2423 419  HOH HOH A . 
F 6 HOH 420  2424 420  HOH HOH A . 
F 6 HOH 421  2425 421  HOH HOH A . 
F 6 HOH 422  2426 422  HOH HOH A . 
F 6 HOH 423  2427 423  HOH HOH A . 
F 6 HOH 424  2428 424  HOH HOH A . 
F 6 HOH 425  2429 425  HOH HOH A . 
F 6 HOH 426  2430 426  HOH HOH A . 
F 6 HOH 427  2431 427  HOH HOH A . 
F 6 HOH 428  2432 428  HOH HOH A . 
F 6 HOH 429  2433 429  HOH HOH A . 
F 6 HOH 430  2434 430  HOH HOH A . 
F 6 HOH 431  2435 431  HOH HOH A . 
F 6 HOH 432  2436 432  HOH HOH A . 
F 6 HOH 433  2437 433  HOH HOH A . 
F 6 HOH 434  2438 434  HOH HOH A . 
F 6 HOH 435  2439 435  HOH HOH A . 
F 6 HOH 436  2440 436  HOH HOH A . 
F 6 HOH 437  2441 437  HOH HOH A . 
F 6 HOH 438  2442 438  HOH HOH A . 
F 6 HOH 439  2443 439  HOH HOH A . 
F 6 HOH 440  2444 440  HOH HOH A . 
F 6 HOH 441  2445 441  HOH HOH A . 
F 6 HOH 442  2446 442  HOH HOH A . 
F 6 HOH 443  2447 443  HOH HOH A . 
F 6 HOH 444  2448 444  HOH HOH A . 
F 6 HOH 445  2449 445  HOH HOH A . 
F 6 HOH 446  2450 446  HOH HOH A . 
F 6 HOH 447  2451 447  HOH HOH A . 
F 6 HOH 448  2452 448  HOH HOH A . 
F 6 HOH 449  2453 449  HOH HOH A . 
F 6 HOH 450  2454 450  HOH HOH A . 
F 6 HOH 451  2455 451  HOH HOH A . 
F 6 HOH 452  2456 452  HOH HOH A . 
F 6 HOH 453  2457 453  HOH HOH A . 
F 6 HOH 454  2458 454  HOH HOH A . 
F 6 HOH 455  2459 455  HOH HOH A . 
F 6 HOH 456  2460 456  HOH HOH A . 
F 6 HOH 457  2461 457  HOH HOH A . 
F 6 HOH 458  2462 458  HOH HOH A . 
F 6 HOH 459  2463 459  HOH HOH A . 
F 6 HOH 460  2464 460  HOH HOH A . 
F 6 HOH 461  2465 461  HOH HOH A . 
F 6 HOH 462  2466 462  HOH HOH A . 
F 6 HOH 463  2467 463  HOH HOH A . 
F 6 HOH 464  2468 464  HOH HOH A . 
F 6 HOH 465  2469 465  HOH HOH A . 
F 6 HOH 466  2470 466  HOH HOH A . 
F 6 HOH 467  2471 467  HOH HOH A . 
F 6 HOH 468  2472 468  HOH HOH A . 
F 6 HOH 469  2473 469  HOH HOH A . 
F 6 HOH 470  2474 470  HOH HOH A . 
F 6 HOH 471  2475 471  HOH HOH A . 
F 6 HOH 472  2476 472  HOH HOH A . 
F 6 HOH 473  2477 473  HOH HOH A . 
F 6 HOH 474  2478 474  HOH HOH A . 
F 6 HOH 475  2479 475  HOH HOH A . 
F 6 HOH 476  2480 476  HOH HOH A . 
F 6 HOH 477  2481 477  HOH HOH A . 
F 6 HOH 478  2482 478  HOH HOH A . 
F 6 HOH 479  2483 479  HOH HOH A . 
F 6 HOH 480  2484 480  HOH HOH A . 
F 6 HOH 481  2485 481  HOH HOH A . 
F 6 HOH 482  2486 482  HOH HOH A . 
F 6 HOH 483  2487 483  HOH HOH A . 
F 6 HOH 484  2488 484  HOH HOH A . 
F 6 HOH 485  2489 485  HOH HOH A . 
F 6 HOH 486  2490 486  HOH HOH A . 
F 6 HOH 487  2491 487  HOH HOH A . 
F 6 HOH 488  2492 488  HOH HOH A . 
F 6 HOH 489  2493 489  HOH HOH A . 
F 6 HOH 490  2494 490  HOH HOH A . 
F 6 HOH 491  2495 491  HOH HOH A . 
F 6 HOH 492  2496 492  HOH HOH A . 
F 6 HOH 493  2497 493  HOH HOH A . 
F 6 HOH 494  2498 494  HOH HOH A . 
F 6 HOH 495  2499 495  HOH HOH A . 
F 6 HOH 496  2500 496  HOH HOH A . 
F 6 HOH 497  2501 497  HOH HOH A . 
F 6 HOH 498  2502 498  HOH HOH A . 
F 6 HOH 499  2503 499  HOH HOH A . 
F 6 HOH 500  2504 500  HOH HOH A . 
F 6 HOH 501  2505 501  HOH HOH A . 
F 6 HOH 502  2506 502  HOH HOH A . 
F 6 HOH 503  2507 503  HOH HOH A . 
F 6 HOH 504  2508 504  HOH HOH A . 
F 6 HOH 505  2509 505  HOH HOH A . 
F 6 HOH 506  2510 506  HOH HOH A . 
F 6 HOH 507  2511 507  HOH HOH A . 
F 6 HOH 508  2512 508  HOH HOH A . 
F 6 HOH 509  2513 509  HOH HOH A . 
F 6 HOH 510  2514 510  HOH HOH A . 
F 6 HOH 511  2515 511  HOH HOH A . 
F 6 HOH 512  2516 512  HOH HOH A . 
F 6 HOH 513  2517 513  HOH HOH A . 
F 6 HOH 514  2518 514  HOH HOH A . 
F 6 HOH 515  2519 515  HOH HOH A . 
F 6 HOH 516  2520 516  HOH HOH A . 
F 6 HOH 517  2521 517  HOH HOH A . 
F 6 HOH 518  2522 518  HOH HOH A . 
F 6 HOH 519  2523 519  HOH HOH A . 
F 6 HOH 520  2524 520  HOH HOH A . 
F 6 HOH 521  2525 521  HOH HOH A . 
F 6 HOH 522  2526 522  HOH HOH A . 
F 6 HOH 523  2527 523  HOH HOH A . 
F 6 HOH 524  2528 524  HOH HOH A . 
F 6 HOH 525  2529 525  HOH HOH A . 
F 6 HOH 526  2530 526  HOH HOH A . 
F 6 HOH 527  2531 527  HOH HOH A . 
F 6 HOH 528  2532 528  HOH HOH A . 
F 6 HOH 529  2533 529  HOH HOH A . 
F 6 HOH 530  2534 530  HOH HOH A . 
F 6 HOH 531  2535 531  HOH HOH A . 
F 6 HOH 532  2536 532  HOH HOH A . 
F 6 HOH 533  2537 533  HOH HOH A . 
F 6 HOH 534  2538 534  HOH HOH A . 
F 6 HOH 535  2539 535  HOH HOH A . 
F 6 HOH 536  2540 536  HOH HOH A . 
F 6 HOH 537  2541 537  HOH HOH A . 
F 6 HOH 538  2542 538  HOH HOH A . 
F 6 HOH 539  2543 539  HOH HOH A . 
F 6 HOH 540  2544 540  HOH HOH A . 
F 6 HOH 541  2545 541  HOH HOH A . 
F 6 HOH 542  2546 542  HOH HOH A . 
F 6 HOH 543  2547 543  HOH HOH A . 
F 6 HOH 544  2548 544  HOH HOH A . 
F 6 HOH 545  2549 545  HOH HOH A . 
F 6 HOH 546  2550 546  HOH HOH A . 
F 6 HOH 547  2551 547  HOH HOH A . 
F 6 HOH 548  2552 548  HOH HOH A . 
F 6 HOH 549  2553 549  HOH HOH A . 
F 6 HOH 550  2554 550  HOH HOH A . 
F 6 HOH 551  2555 551  HOH HOH A . 
F 6 HOH 552  2556 552  HOH HOH A . 
F 6 HOH 553  2557 553  HOH HOH A . 
F 6 HOH 554  2558 554  HOH HOH A . 
F 6 HOH 555  2559 555  HOH HOH A . 
F 6 HOH 556  2560 556  HOH HOH A . 
F 6 HOH 557  2561 557  HOH HOH A . 
F 6 HOH 558  2562 558  HOH HOH A . 
F 6 HOH 559  2563 559  HOH HOH A . 
F 6 HOH 560  2564 560  HOH HOH A . 
F 6 HOH 561  2565 561  HOH HOH A . 
F 6 HOH 562  2566 562  HOH HOH A . 
F 6 HOH 563  2567 563  HOH HOH A . 
F 6 HOH 564  2568 564  HOH HOH A . 
F 6 HOH 565  2569 565  HOH HOH A . 
F 6 HOH 566  2570 566  HOH HOH A . 
F 6 HOH 567  2571 567  HOH HOH A . 
F 6 HOH 568  2572 568  HOH HOH A . 
F 6 HOH 569  2573 569  HOH HOH A . 
F 6 HOH 570  2574 570  HOH HOH A . 
F 6 HOH 571  2575 571  HOH HOH A . 
F 6 HOH 572  2576 572  HOH HOH A . 
F 6 HOH 573  2577 573  HOH HOH A . 
F 6 HOH 574  2578 574  HOH HOH A . 
F 6 HOH 575  2579 575  HOH HOH A . 
F 6 HOH 576  2580 576  HOH HOH A . 
F 6 HOH 577  2581 577  HOH HOH A . 
F 6 HOH 578  2582 578  HOH HOH A . 
F 6 HOH 579  2583 579  HOH HOH A . 
F 6 HOH 580  2584 580  HOH HOH A . 
F 6 HOH 581  2585 581  HOH HOH A . 
F 6 HOH 582  2586 582  HOH HOH A . 
F 6 HOH 583  2587 583  HOH HOH A . 
F 6 HOH 584  2588 584  HOH HOH A . 
F 6 HOH 585  2589 585  HOH HOH A . 
F 6 HOH 586  2590 586  HOH HOH A . 
F 6 HOH 587  2591 587  HOH HOH A . 
F 6 HOH 588  2592 588  HOH HOH A . 
F 6 HOH 589  2593 589  HOH HOH A . 
F 6 HOH 590  2594 590  HOH HOH A . 
F 6 HOH 591  2595 591  HOH HOH A . 
F 6 HOH 592  2596 592  HOH HOH A . 
F 6 HOH 593  2597 593  HOH HOH A . 
F 6 HOH 594  2598 594  HOH HOH A . 
F 6 HOH 595  2599 595  HOH HOH A . 
F 6 HOH 596  2600 596  HOH HOH A . 
F 6 HOH 597  2601 597  HOH HOH A . 
F 6 HOH 598  2602 598  HOH HOH A . 
F 6 HOH 599  2603 599  HOH HOH A . 
F 6 HOH 600  2604 600  HOH HOH A . 
F 6 HOH 601  2605 601  HOH HOH A . 
F 6 HOH 602  2606 602  HOH HOH A . 
F 6 HOH 603  2607 603  HOH HOH A . 
F 6 HOH 604  2608 604  HOH HOH A . 
F 6 HOH 605  2609 605  HOH HOH A . 
F 6 HOH 606  2610 606  HOH HOH A . 
F 6 HOH 607  2611 607  HOH HOH A . 
F 6 HOH 608  2612 608  HOH HOH A . 
F 6 HOH 609  2613 609  HOH HOH A . 
F 6 HOH 610  2614 610  HOH HOH A . 
F 6 HOH 611  2615 611  HOH HOH A . 
F 6 HOH 612  2616 612  HOH HOH A . 
F 6 HOH 613  2617 613  HOH HOH A . 
F 6 HOH 614  2618 614  HOH HOH A . 
F 6 HOH 615  2619 615  HOH HOH A . 
F 6 HOH 616  2620 616  HOH HOH A . 
F 6 HOH 617  2621 617  HOH HOH A . 
F 6 HOH 618  2622 618  HOH HOH A . 
F 6 HOH 619  2623 619  HOH HOH A . 
F 6 HOH 620  2624 620  HOH HOH A . 
F 6 HOH 621  2625 621  HOH HOH A . 
F 6 HOH 622  2626 622  HOH HOH A . 
F 6 HOH 623  2627 623  HOH HOH A . 
F 6 HOH 624  2628 624  HOH HOH A . 
F 6 HOH 625  2629 625  HOH HOH A . 
F 6 HOH 626  2630 626  HOH HOH A . 
F 6 HOH 627  2631 627  HOH HOH A . 
F 6 HOH 628  2632 628  HOH HOH A . 
F 6 HOH 629  2633 629  HOH HOH A . 
F 6 HOH 630  2634 630  HOH HOH A . 
F 6 HOH 631  2635 631  HOH HOH A . 
F 6 HOH 632  2636 632  HOH HOH A . 
F 6 HOH 633  2637 633  HOH HOH A . 
F 6 HOH 634  2638 634  HOH HOH A . 
F 6 HOH 635  2639 635  HOH HOH A . 
F 6 HOH 636  2640 636  HOH HOH A . 
F 6 HOH 637  2641 637  HOH HOH A . 
F 6 HOH 638  2642 638  HOH HOH A . 
F 6 HOH 639  2643 639  HOH HOH A . 
F 6 HOH 640  2644 640  HOH HOH A . 
F 6 HOH 641  2645 641  HOH HOH A . 
F 6 HOH 642  2646 642  HOH HOH A . 
F 6 HOH 643  2647 643  HOH HOH A . 
F 6 HOH 644  2648 644  HOH HOH A . 
F 6 HOH 645  2649 645  HOH HOH A . 
F 6 HOH 646  2650 646  HOH HOH A . 
F 6 HOH 647  2651 647  HOH HOH A . 
F 6 HOH 648  2652 648  HOH HOH A . 
F 6 HOH 649  2653 649  HOH HOH A . 
F 6 HOH 650  2654 650  HOH HOH A . 
F 6 HOH 651  2655 651  HOH HOH A . 
F 6 HOH 652  2656 652  HOH HOH A . 
F 6 HOH 653  2657 653  HOH HOH A . 
F 6 HOH 654  2658 654  HOH HOH A . 
F 6 HOH 655  2659 655  HOH HOH A . 
F 6 HOH 656  2660 656  HOH HOH A . 
F 6 HOH 657  2661 657  HOH HOH A . 
F 6 HOH 658  2662 658  HOH HOH A . 
F 6 HOH 659  2663 659  HOH HOH A . 
F 6 HOH 660  2664 660  HOH HOH A . 
F 6 HOH 661  2665 661  HOH HOH A . 
F 6 HOH 662  2666 662  HOH HOH A . 
F 6 HOH 663  2667 663  HOH HOH A . 
F 6 HOH 664  2668 664  HOH HOH A . 
F 6 HOH 665  2669 665  HOH HOH A . 
F 6 HOH 666  2670 666  HOH HOH A . 
F 6 HOH 667  2671 667  HOH HOH A . 
F 6 HOH 668  2672 668  HOH HOH A . 
F 6 HOH 669  2673 669  HOH HOH A . 
F 6 HOH 670  2674 670  HOH HOH A . 
F 6 HOH 671  2675 671  HOH HOH A . 
F 6 HOH 672  2676 672  HOH HOH A . 
F 6 HOH 673  2677 673  HOH HOH A . 
F 6 HOH 674  2678 674  HOH HOH A . 
F 6 HOH 675  2679 675  HOH HOH A . 
F 6 HOH 676  2680 676  HOH HOH A . 
F 6 HOH 677  2681 677  HOH HOH A . 
F 6 HOH 678  2682 678  HOH HOH A . 
F 6 HOH 679  2683 679  HOH HOH A . 
F 6 HOH 680  2684 680  HOH HOH A . 
F 6 HOH 681  2685 681  HOH HOH A . 
F 6 HOH 682  2686 682  HOH HOH A . 
F 6 HOH 683  2687 683  HOH HOH A . 
F 6 HOH 684  2688 684  HOH HOH A . 
F 6 HOH 685  2689 685  HOH HOH A . 
F 6 HOH 686  2690 686  HOH HOH A . 
F 6 HOH 687  2691 687  HOH HOH A . 
F 6 HOH 688  2692 688  HOH HOH A . 
F 6 HOH 689  2693 689  HOH HOH A . 
F 6 HOH 690  2694 690  HOH HOH A . 
F 6 HOH 691  2695 691  HOH HOH A . 
F 6 HOH 692  2696 692  HOH HOH A . 
F 6 HOH 693  2697 693  HOH HOH A . 
F 6 HOH 694  2698 694  HOH HOH A . 
F 6 HOH 695  2699 695  HOH HOH A . 
F 6 HOH 696  2700 696  HOH HOH A . 
F 6 HOH 697  2701 697  HOH HOH A . 
F 6 HOH 698  2702 698  HOH HOH A . 
F 6 HOH 699  2703 699  HOH HOH A . 
F 6 HOH 700  2704 700  HOH HOH A . 
F 6 HOH 701  2705 701  HOH HOH A . 
F 6 HOH 702  2706 702  HOH HOH A . 
F 6 HOH 703  2707 703  HOH HOH A . 
F 6 HOH 704  2708 704  HOH HOH A . 
F 6 HOH 705  2709 705  HOH HOH A . 
F 6 HOH 706  2710 706  HOH HOH A . 
F 6 HOH 707  2711 707  HOH HOH A . 
F 6 HOH 708  2712 708  HOH HOH A . 
F 6 HOH 709  2713 709  HOH HOH A . 
F 6 HOH 710  2714 710  HOH HOH A . 
F 6 HOH 711  2715 711  HOH HOH A . 
F 6 HOH 712  2716 712  HOH HOH A . 
F 6 HOH 713  2717 713  HOH HOH A . 
F 6 HOH 714  2718 714  HOH HOH A . 
F 6 HOH 715  2719 715  HOH HOH A . 
F 6 HOH 716  2720 716  HOH HOH A . 
F 6 HOH 717  2721 717  HOH HOH A . 
F 6 HOH 718  2722 718  HOH HOH A . 
F 6 HOH 719  2723 719  HOH HOH A . 
F 6 HOH 720  2724 720  HOH HOH A . 
F 6 HOH 721  2725 721  HOH HOH A . 
F 6 HOH 722  2726 722  HOH HOH A . 
F 6 HOH 723  2727 723  HOH HOH A . 
F 6 HOH 724  2728 724  HOH HOH A . 
F 6 HOH 725  2729 725  HOH HOH A . 
F 6 HOH 726  2730 726  HOH HOH A . 
F 6 HOH 727  2731 727  HOH HOH A . 
F 6 HOH 728  2732 728  HOH HOH A . 
F 6 HOH 729  2733 729  HOH HOH A . 
F 6 HOH 730  2734 730  HOH HOH A . 
F 6 HOH 731  2735 731  HOH HOH A . 
F 6 HOH 732  2736 732  HOH HOH A . 
F 6 HOH 733  2737 733  HOH HOH A . 
F 6 HOH 734  2738 734  HOH HOH A . 
F 6 HOH 735  2739 735  HOH HOH A . 
F 6 HOH 736  2740 736  HOH HOH A . 
F 6 HOH 737  2741 737  HOH HOH A . 
F 6 HOH 738  2742 738  HOH HOH A . 
F 6 HOH 739  2743 739  HOH HOH A . 
F 6 HOH 740  2744 740  HOH HOH A . 
F 6 HOH 741  2745 741  HOH HOH A . 
F 6 HOH 742  2746 742  HOH HOH A . 
F 6 HOH 743  2747 743  HOH HOH A . 
F 6 HOH 744  2748 744  HOH HOH A . 
F 6 HOH 745  2749 745  HOH HOH A . 
F 6 HOH 746  2750 746  HOH HOH A . 
F 6 HOH 747  2751 747  HOH HOH A . 
F 6 HOH 748  2752 748  HOH HOH A . 
F 6 HOH 749  2753 749  HOH HOH A . 
F 6 HOH 750  2754 750  HOH HOH A . 
F 6 HOH 751  2755 751  HOH HOH A . 
F 6 HOH 752  2756 752  HOH HOH A . 
F 6 HOH 753  2757 753  HOH HOH A . 
F 6 HOH 754  2758 754  HOH HOH A . 
F 6 HOH 755  2759 755  HOH HOH A . 
F 6 HOH 756  2760 756  HOH HOH A . 
F 6 HOH 757  2761 757  HOH HOH A . 
F 6 HOH 758  2762 758  HOH HOH A . 
F 6 HOH 759  2763 759  HOH HOH A . 
F 6 HOH 760  2764 760  HOH HOH A . 
F 6 HOH 761  2765 761  HOH HOH A . 
F 6 HOH 762  2766 762  HOH HOH A . 
F 6 HOH 763  2767 763  HOH HOH A . 
F 6 HOH 764  2768 764  HOH HOH A . 
F 6 HOH 765  2769 765  HOH HOH A . 
F 6 HOH 766  2770 766  HOH HOH A . 
F 6 HOH 767  2771 767  HOH HOH A . 
F 6 HOH 768  2772 768  HOH HOH A . 
F 6 HOH 769  2773 769  HOH HOH A . 
F 6 HOH 770  2774 770  HOH HOH A . 
F 6 HOH 771  2775 771  HOH HOH A . 
F 6 HOH 772  2776 772  HOH HOH A . 
F 6 HOH 773  2777 773  HOH HOH A . 
F 6 HOH 774  2778 774  HOH HOH A . 
F 6 HOH 775  2779 775  HOH HOH A . 
F 6 HOH 776  2780 776  HOH HOH A . 
F 6 HOH 777  2781 777  HOH HOH A . 
F 6 HOH 778  2782 778  HOH HOH A . 
F 6 HOH 779  2783 779  HOH HOH A . 
F 6 HOH 780  2784 780  HOH HOH A . 
F 6 HOH 781  2785 781  HOH HOH A . 
F 6 HOH 782  2786 782  HOH HOH A . 
F 6 HOH 783  2787 783  HOH HOH A . 
F 6 HOH 784  2788 784  HOH HOH A . 
F 6 HOH 785  2789 785  HOH HOH A . 
F 6 HOH 786  2790 786  HOH HOH A . 
F 6 HOH 787  2791 787  HOH HOH A . 
F 6 HOH 788  2792 788  HOH HOH A . 
F 6 HOH 789  2793 789  HOH HOH A . 
F 6 HOH 790  2794 790  HOH HOH A . 
F 6 HOH 791  2795 791  HOH HOH A . 
F 6 HOH 792  2796 792  HOH HOH A . 
F 6 HOH 793  2797 793  HOH HOH A . 
F 6 HOH 794  2798 794  HOH HOH A . 
F 6 HOH 795  2799 795  HOH HOH A . 
F 6 HOH 796  2800 796  HOH HOH A . 
F 6 HOH 797  2801 797  HOH HOH A . 
F 6 HOH 798  2802 798  HOH HOH A . 
F 6 HOH 799  2803 799  HOH HOH A . 
F 6 HOH 800  2804 800  HOH HOH A . 
F 6 HOH 801  2805 801  HOH HOH A . 
F 6 HOH 802  2806 802  HOH HOH A . 
F 6 HOH 803  2807 803  HOH HOH A . 
F 6 HOH 804  2808 804  HOH HOH A . 
F 6 HOH 805  2809 805  HOH HOH A . 
F 6 HOH 806  2810 806  HOH HOH A . 
F 6 HOH 807  2811 807  HOH HOH A . 
F 6 HOH 808  2812 808  HOH HOH A . 
F 6 HOH 809  2813 809  HOH HOH A . 
F 6 HOH 810  2814 810  HOH HOH A . 
F 6 HOH 811  2815 811  HOH HOH A . 
F 6 HOH 812  2816 812  HOH HOH A . 
F 6 HOH 813  2817 813  HOH HOH A . 
F 6 HOH 814  2818 814  HOH HOH A . 
F 6 HOH 815  2819 815  HOH HOH A . 
F 6 HOH 816  2820 816  HOH HOH A . 
F 6 HOH 817  2821 817  HOH HOH A . 
F 6 HOH 818  2822 818  HOH HOH A . 
F 6 HOH 819  2823 819  HOH HOH A . 
F 6 HOH 820  2824 820  HOH HOH A . 
F 6 HOH 821  2825 821  HOH HOH A . 
F 6 HOH 822  2826 822  HOH HOH A . 
F 6 HOH 823  2827 823  HOH HOH A . 
F 6 HOH 824  2828 824  HOH HOH A . 
F 6 HOH 825  2829 825  HOH HOH A . 
F 6 HOH 826  2830 826  HOH HOH A . 
F 6 HOH 827  2831 827  HOH HOH A . 
F 6 HOH 828  2832 828  HOH HOH A . 
F 6 HOH 829  2833 829  HOH HOH A . 
F 6 HOH 830  2834 830  HOH HOH A . 
F 6 HOH 831  2835 831  HOH HOH A . 
F 6 HOH 832  2836 832  HOH HOH A . 
F 6 HOH 833  2837 833  HOH HOH A . 
F 6 HOH 834  2838 834  HOH HOH A . 
F 6 HOH 835  2839 835  HOH HOH A . 
F 6 HOH 836  2840 836  HOH HOH A . 
F 6 HOH 837  2841 837  HOH HOH A . 
F 6 HOH 838  2842 838  HOH HOH A . 
F 6 HOH 839  2843 839  HOH HOH A . 
F 6 HOH 840  2844 840  HOH HOH A . 
F 6 HOH 841  2845 841  HOH HOH A . 
F 6 HOH 842  2846 842  HOH HOH A . 
F 6 HOH 843  2847 843  HOH HOH A . 
F 6 HOH 844  2848 844  HOH HOH A . 
F 6 HOH 845  2849 845  HOH HOH A . 
F 6 HOH 846  2850 846  HOH HOH A . 
F 6 HOH 847  2851 847  HOH HOH A . 
F 6 HOH 848  2852 848  HOH HOH A . 
F 6 HOH 849  2853 849  HOH HOH A . 
F 6 HOH 850  2854 850  HOH HOH A . 
F 6 HOH 851  2855 851  HOH HOH A . 
F 6 HOH 852  2856 852  HOH HOH A . 
F 6 HOH 853  2857 853  HOH HOH A . 
F 6 HOH 854  2858 854  HOH HOH A . 
F 6 HOH 855  2859 855  HOH HOH A . 
F 6 HOH 856  2860 856  HOH HOH A . 
F 6 HOH 857  2861 857  HOH HOH A . 
F 6 HOH 858  2862 858  HOH HOH A . 
F 6 HOH 859  2863 859  HOH HOH A . 
F 6 HOH 860  2864 860  HOH HOH A . 
F 6 HOH 861  2865 861  HOH HOH A . 
F 6 HOH 862  2866 862  HOH HOH A . 
F 6 HOH 863  2867 863  HOH HOH A . 
F 6 HOH 864  2868 864  HOH HOH A . 
F 6 HOH 865  2869 865  HOH HOH A . 
F 6 HOH 866  2870 866  HOH HOH A . 
F 6 HOH 867  2871 867  HOH HOH A . 
F 6 HOH 868  2872 868  HOH HOH A . 
F 6 HOH 869  2873 869  HOH HOH A . 
F 6 HOH 870  2874 870  HOH HOH A . 
F 6 HOH 871  2875 871  HOH HOH A . 
F 6 HOH 872  2876 872  HOH HOH A . 
F 6 HOH 873  2877 873  HOH HOH A . 
F 6 HOH 874  2878 874  HOH HOH A . 
F 6 HOH 875  2879 875  HOH HOH A . 
F 6 HOH 876  2880 876  HOH HOH A . 
F 6 HOH 877  2881 877  HOH HOH A . 
F 6 HOH 878  2882 878  HOH HOH A . 
F 6 HOH 879  2883 879  HOH HOH A . 
F 6 HOH 880  2884 880  HOH HOH A . 
F 6 HOH 881  2885 881  HOH HOH A . 
F 6 HOH 882  2886 882  HOH HOH A . 
F 6 HOH 883  2887 883  HOH HOH A . 
F 6 HOH 884  2888 884  HOH HOH A . 
F 6 HOH 885  2889 885  HOH HOH A . 
F 6 HOH 886  2890 886  HOH HOH A . 
F 6 HOH 887  2891 887  HOH HOH A . 
F 6 HOH 888  2892 888  HOH HOH A . 
F 6 HOH 889  2893 889  HOH HOH A . 
F 6 HOH 890  2894 890  HOH HOH A . 
F 6 HOH 891  2895 891  HOH HOH A . 
F 6 HOH 892  2896 892  HOH HOH A . 
F 6 HOH 893  2897 893  HOH HOH A . 
F 6 HOH 894  2898 894  HOH HOH A . 
F 6 HOH 895  2899 895  HOH HOH A . 
F 6 HOH 896  2900 896  HOH HOH A . 
F 6 HOH 897  2901 897  HOH HOH A . 
F 6 HOH 898  2902 898  HOH HOH A . 
F 6 HOH 899  2903 899  HOH HOH A . 
F 6 HOH 900  2904 900  HOH HOH A . 
F 6 HOH 901  2905 901  HOH HOH A . 
F 6 HOH 902  2906 902  HOH HOH A . 
F 6 HOH 903  2907 903  HOH HOH A . 
F 6 HOH 904  2908 904  HOH HOH A . 
F 6 HOH 905  2909 905  HOH HOH A . 
F 6 HOH 906  2910 906  HOH HOH A . 
F 6 HOH 907  2911 907  HOH HOH A . 
F 6 HOH 908  2912 908  HOH HOH A . 
F 6 HOH 909  2913 909  HOH HOH A . 
F 6 HOH 910  2914 910  HOH HOH A . 
F 6 HOH 911  2915 911  HOH HOH A . 
F 6 HOH 912  2916 912  HOH HOH A . 
F 6 HOH 913  2917 913  HOH HOH A . 
F 6 HOH 914  2918 914  HOH HOH A . 
F 6 HOH 915  2919 915  HOH HOH A . 
F 6 HOH 916  2920 916  HOH HOH A . 
F 6 HOH 917  2921 917  HOH HOH A . 
F 6 HOH 918  2922 918  HOH HOH A . 
F 6 HOH 919  2923 919  HOH HOH A . 
F 6 HOH 920  2924 920  HOH HOH A . 
F 6 HOH 921  2925 921  HOH HOH A . 
F 6 HOH 922  2926 922  HOH HOH A . 
F 6 HOH 923  2927 923  HOH HOH A . 
F 6 HOH 924  2928 924  HOH HOH A . 
F 6 HOH 925  2929 925  HOH HOH A . 
F 6 HOH 926  2930 926  HOH HOH A . 
F 6 HOH 927  2931 927  HOH HOH A . 
F 6 HOH 928  2932 928  HOH HOH A . 
F 6 HOH 929  2933 929  HOH HOH A . 
F 6 HOH 930  2934 930  HOH HOH A . 
F 6 HOH 931  2935 931  HOH HOH A . 
F 6 HOH 932  2936 932  HOH HOH A . 
F 6 HOH 933  2937 933  HOH HOH A . 
F 6 HOH 934  2938 934  HOH HOH A . 
F 6 HOH 935  2939 935  HOH HOH A . 
F 6 HOH 936  2940 936  HOH HOH A . 
F 6 HOH 937  2941 937  HOH HOH A . 
F 6 HOH 938  2942 938  HOH HOH A . 
F 6 HOH 939  2943 939  HOH HOH A . 
F 6 HOH 940  2944 940  HOH HOH A . 
F 6 HOH 941  2945 941  HOH HOH A . 
F 6 HOH 942  2946 942  HOH HOH A . 
F 6 HOH 943  2947 943  HOH HOH A . 
F 6 HOH 944  2948 944  HOH HOH A . 
F 6 HOH 945  2949 945  HOH HOH A . 
F 6 HOH 946  2950 946  HOH HOH A . 
F 6 HOH 947  2951 947  HOH HOH A . 
F 6 HOH 948  2952 948  HOH HOH A . 
F 6 HOH 949  2953 949  HOH HOH A . 
F 6 HOH 950  2954 950  HOH HOH A . 
F 6 HOH 951  2955 951  HOH HOH A . 
F 6 HOH 952  2956 952  HOH HOH A . 
F 6 HOH 953  2957 953  HOH HOH A . 
F 6 HOH 954  2958 954  HOH HOH A . 
F 6 HOH 955  2959 955  HOH HOH A . 
F 6 HOH 956  2960 956  HOH HOH A . 
F 6 HOH 957  2961 957  HOH HOH A . 
F 6 HOH 958  2962 958  HOH HOH A . 
F 6 HOH 959  2963 959  HOH HOH A . 
F 6 HOH 960  2964 960  HOH HOH A . 
F 6 HOH 961  2965 961  HOH HOH A . 
F 6 HOH 962  2966 962  HOH HOH A . 
F 6 HOH 963  2967 963  HOH HOH A . 
F 6 HOH 964  2968 964  HOH HOH A . 
F 6 HOH 965  2969 965  HOH HOH A . 
F 6 HOH 966  2970 966  HOH HOH A . 
F 6 HOH 967  2971 967  HOH HOH A . 
F 6 HOH 968  2972 968  HOH HOH A . 
F 6 HOH 969  2973 969  HOH HOH A . 
F 6 HOH 970  2974 970  HOH HOH A . 
F 6 HOH 971  2975 971  HOH HOH A . 
F 6 HOH 972  2976 972  HOH HOH A . 
F 6 HOH 973  2977 973  HOH HOH A . 
F 6 HOH 974  2978 974  HOH HOH A . 
F 6 HOH 975  2979 975  HOH HOH A . 
F 6 HOH 976  2980 976  HOH HOH A . 
F 6 HOH 977  2981 977  HOH HOH A . 
F 6 HOH 978  2982 978  HOH HOH A . 
F 6 HOH 979  2983 979  HOH HOH A . 
F 6 HOH 980  2984 980  HOH HOH A . 
F 6 HOH 981  2985 981  HOH HOH A . 
F 6 HOH 982  2986 982  HOH HOH A . 
F 6 HOH 983  2987 983  HOH HOH A . 
F 6 HOH 984  2988 984  HOH HOH A . 
F 6 HOH 985  2989 985  HOH HOH A . 
F 6 HOH 986  2990 986  HOH HOH A . 
F 6 HOH 987  2991 987  HOH HOH A . 
F 6 HOH 988  2992 988  HOH HOH A . 
F 6 HOH 989  2993 989  HOH HOH A . 
F 6 HOH 990  2994 990  HOH HOH A . 
F 6 HOH 991  2995 991  HOH HOH A . 
F 6 HOH 992  2996 992  HOH HOH A . 
F 6 HOH 993  2997 993  HOH HOH A . 
F 6 HOH 994  2998 994  HOH HOH A . 
F 6 HOH 995  2999 995  HOH HOH A . 
F 6 HOH 996  3000 996  HOH HOH A . 
F 6 HOH 997  3001 997  HOH HOH A . 
F 6 HOH 998  3002 998  HOH HOH A . 
F 6 HOH 999  3003 999  HOH HOH A . 
F 6 HOH 1000 3004 1000 HOH HOH A . 
F 6 HOH 1001 3005 1001 HOH HOH A . 
F 6 HOH 1002 3006 1002 HOH HOH A . 
F 6 HOH 1003 3007 1003 HOH HOH A . 
F 6 HOH 1004 3008 1004 HOH HOH A . 
F 6 HOH 1005 3009 1005 HOH HOH A . 
F 6 HOH 1006 3010 1006 HOH HOH A . 
F 6 HOH 1007 3011 1007 HOH HOH A . 
F 6 HOH 1008 3012 1008 HOH HOH A . 
F 6 HOH 1009 3013 1009 HOH HOH A . 
F 6 HOH 1010 3014 1010 HOH HOH A . 
F 6 HOH 1011 3015 1011 HOH HOH A . 
F 6 HOH 1012 3016 1012 HOH HOH A . 
F 6 HOH 1013 3017 1013 HOH HOH A . 
F 6 HOH 1014 3018 1014 HOH HOH A . 
F 6 HOH 1015 3019 1015 HOH HOH A . 
F 6 HOH 1016 3020 1016 HOH HOH A . 
F 6 HOH 1017 3021 1017 HOH HOH A . 
F 6 HOH 1018 3022 1018 HOH HOH A . 
F 6 HOH 1019 3023 1019 HOH HOH A . 
F 6 HOH 1020 3024 1020 HOH HOH A . 
F 6 HOH 1021 3025 1021 HOH HOH A . 
F 6 HOH 1022 3026 1022 HOH HOH A . 
F 6 HOH 1023 3027 1023 HOH HOH A . 
F 6 HOH 1024 3028 1024 HOH HOH A . 
F 6 HOH 1025 3029 1025 HOH HOH A . 
F 6 HOH 1026 3030 1026 HOH HOH A . 
F 6 HOH 1027 3031 1027 HOH HOH A . 
F 6 HOH 1028 3032 1028 HOH HOH A . 
F 6 HOH 1029 3033 1029 HOH HOH A . 
F 6 HOH 1030 3034 1030 HOH HOH A . 
F 6 HOH 1031 3035 1031 HOH HOH A . 
F 6 HOH 1032 3036 1032 HOH HOH A . 
F 6 HOH 1033 3037 1033 HOH HOH A . 
F 6 HOH 1034 3038 1034 HOH HOH A . 
F 6 HOH 1035 3039 1035 HOH HOH A . 
F 6 HOH 1036 3040 1036 HOH HOH A . 
F 6 HOH 1037 3041 1037 HOH HOH A . 
F 6 HOH 1038 3042 1038 HOH HOH A . 
F 6 HOH 1039 3043 1039 HOH HOH A . 
F 6 HOH 1040 3044 1040 HOH HOH A . 
F 6 HOH 1041 3045 1041 HOH HOH A . 
F 6 HOH 1042 3046 1042 HOH HOH A . 
# 
_pdbx_struct_mod_residue.id               1 
_pdbx_struct_mod_residue.label_asym_id    A 
_pdbx_struct_mod_residue.label_comp_id    ASN 
_pdbx_struct_mod_residue.label_seq_id     194 
_pdbx_struct_mod_residue.auth_asym_id     A 
_pdbx_struct_mod_residue.auth_comp_id     ASN 
_pdbx_struct_mod_residue.auth_seq_id      194 
_pdbx_struct_mod_residue.PDB_ins_code     ? 
_pdbx_struct_mod_residue.parent_comp_id   ASN 
_pdbx_struct_mod_residue.details          'GLYCOSYLATION SITE' 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_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 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OD1 ? A ASP 92  ? A ASP 92   ? 1_555 ZN ? C ZN . ? A ZN 2004 ? 1_555 F2  B D FMF .   ? A FMF 2003 ? 1_555 101.0 ? 
2  OD1 ? A ASP 92  ? A ASP 92   ? 1_555 ZN ? C ZN . ? A ZN 2004 ? 1_555 O3  A D FMF .   ? A FMF 2003 ? 1_555 93.8  ? 
3  F2  B D FMF .   ? A FMF 2003 ? 1_555 ZN ? C ZN . ? A ZN 2004 ? 1_555 O3  A D FMF .   ? A FMF 2003 ? 1_555 67.9  ? 
4  OD1 ? A ASP 92  ? A ASP 92   ? 1_555 ZN ? C ZN . ? A ZN 2004 ? 1_555 O3  B D FMF .   ? A FMF 2003 ? 1_555 88.0  ? 
5  F2  B D FMF .   ? A FMF 2003 ? 1_555 ZN ? C ZN . ? A ZN 2004 ? 1_555 O3  B D FMF .   ? A FMF 2003 ? 1_555 68.5  ? 
6  O3  A D FMF .   ? A FMF 2003 ? 1_555 ZN ? C ZN . ? A ZN 2004 ? 1_555 O3  B D FMF .   ? A FMF 2003 ? 1_555 5.8   ? 
7  OD1 ? A ASP 92  ? A ASP 92   ? 1_555 ZN ? C ZN . ? A ZN 2004 ? 1_555 NE2 ? A HIS 471 ? A HIS 471  ? 1_555 101.3 ? 
8  F2  B D FMF .   ? A FMF 2003 ? 1_555 ZN ? C ZN . ? A ZN 2004 ? 1_555 NE2 ? A HIS 471 ? A HIS 471  ? 1_555 153.3 ? 
9  O3  A D FMF .   ? A FMF 2003 ? 1_555 ZN ? C ZN . ? A ZN 2004 ? 1_555 NE2 ? A HIS 471 ? A HIS 471  ? 1_555 96.2  ? 
10 O3  B D FMF .   ? A FMF 2003 ? 1_555 ZN ? C ZN . ? A ZN 2004 ? 1_555 NE2 ? A HIS 471 ? A HIS 471  ? 1_555 98.0  ? 
11 OD1 ? A ASP 92  ? A ASP 92   ? 1_555 ZN ? C ZN . ? A ZN 2004 ? 1_555 NE2 ? A HIS 90  ? A HIS 90   ? 1_555 102.3 ? 
12 F2  B D FMF .   ? A FMF 2003 ? 1_555 ZN ? C ZN . ? A ZN 2004 ? 1_555 NE2 ? A HIS 90  ? A HIS 90   ? 1_555 81.4  ? 
13 O3  A D FMF .   ? A FMF 2003 ? 1_555 ZN ? C ZN . ? A ZN 2004 ? 1_555 NE2 ? A HIS 90  ? A HIS 90   ? 1_555 147.6 ? 
14 O3  B D FMF .   ? A FMF 2003 ? 1_555 ZN ? C ZN . ? A ZN 2004 ? 1_555 NE2 ? A HIS 90  ? A HIS 90   ? 1_555 149.6 ? 
15 NE2 ? A HIS 471 ? A HIS 471  ? 1_555 ZN ? C ZN . ? A ZN 2004 ? 1_555 NE2 ? A HIS 90  ? A HIS 90   ? 1_555 107.7 ? 
16 OD1 ? A ASP 92  ? A ASP 92   ? 1_555 ZN ? C ZN . ? A ZN 2004 ? 1_555 F2  A D FMF .   ? A FMF 2003 ? 1_555 101.1 ? 
17 F2  B D FMF .   ? A FMF 2003 ? 1_555 ZN ? C ZN . ? A ZN 2004 ? 1_555 F2  A D FMF .   ? A FMF 2003 ? 1_555 0.9   ? 
18 O3  A D FMF .   ? A FMF 2003 ? 1_555 ZN ? C ZN . ? A ZN 2004 ? 1_555 F2  A D FMF .   ? A FMF 2003 ? 1_555 67.0  ? 
19 O3  B D FMF .   ? A FMF 2003 ? 1_555 ZN ? C ZN . ? A ZN 2004 ? 1_555 F2  A D FMF .   ? A FMF 2003 ? 1_555 67.6  ? 
20 NE2 ? A HIS 471 ? A HIS 471  ? 1_555 ZN ? C ZN . ? A ZN 2004 ? 1_555 F2  A D FMF .   ? A FMF 2003 ? 1_555 152.7 ? 
21 NE2 ? A HIS 90  ? A HIS 90   ? 1_555 ZN ? C ZN . ? A ZN 2004 ? 1_555 F2  A D FMF .   ? A FMF 2003 ? 1_555 82.3  ? 
22 OD1 ? A ASP 92  ? A ASP 92   ? 1_555 ZN ? C ZN . ? A ZN 2004 ? 1_555 OD1 ? A ASP 204 ? A ASP 204  ? 1_555 161.2 ? 
23 F2  B D FMF .   ? A FMF 2003 ? 1_555 ZN ? C ZN . ? A ZN 2004 ? 1_555 OD1 ? A ASP 204 ? A ASP 204  ? 1_555 63.3  ? 
24 O3  A D FMF .   ? A FMF 2003 ? 1_555 ZN ? C ZN . ? A ZN 2004 ? 1_555 OD1 ? A ASP 204 ? A ASP 204  ? 1_555 71.2  ? 
25 O3  B D FMF .   ? A FMF 2003 ? 1_555 ZN ? C ZN . ? A ZN 2004 ? 1_555 OD1 ? A ASP 204 ? A ASP 204  ? 1_555 76.7  ? 
26 NE2 ? A HIS 471 ? A HIS 471  ? 1_555 ZN ? C ZN . ? A ZN 2004 ? 1_555 OD1 ? A ASP 204 ? A ASP 204  ? 1_555 91.8  ? 
27 NE2 ? A HIS 90  ? A HIS 90   ? 1_555 ZN ? C ZN . ? A ZN 2004 ? 1_555 OD1 ? A ASP 204 ? A ASP 204  ? 1_555 86.2  ? 
28 F2  A D FMF .   ? A FMF 2003 ? 1_555 ZN ? C ZN . ? A ZN 2004 ? 1_555 OD1 ? A ASP 204 ? A ASP 204  ? 1_555 63.0  ? 
# 
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 2003-10-07 
2 'Structure model' 1 1 2008-04-29 
3 'Structure model' 1 2 2011-07-13 
# 
_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' 'Non-polymer description'   
3 3 'Structure model' 'Version format compliance' 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
CNS       refinement       1.0 ? 1 
DENZO     'data reduction' .   ? 2 
SCALEPACK 'data scaling'   .   ? 3 
CNS       phasing          .   ? 4 
# 
_pdbx_database_remark.id     999 
_pdbx_database_remark.text   
;SEQUENCE
The E -> K conflict for residue 970
is noted in Swiss-Prot entry Q24451.
;
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 OH  A TYR 506  ? B O   A HOH 2896 ? ? 1.55 
2  1 O   A HOH 2895 ? ? O   A HOH 3046 ? ? 1.56 
3  1 CE1 A TYR 435  ? B O   A HOH 2594 ? ? 1.80 
4  1 O   A HOH 2337 ? ? O   A HOH 2590 ? ? 1.86 
5  1 OH  A TYR 75   ? B O   A HOH 2381 ? ? 1.87 
6  1 CE1 A TYR 75   ? B O   A HOH 2992 ? ? 2.02 
7  1 OE1 A GLU 47   ? ? NH1 A ARG 51   ? ? 2.03 
8  1 OE2 A GLU 130  ? ? O   A HOH 2891 ? ? 2.10 
9  1 OH  A TYR 75   ? B O   A HOH 3042 ? ? 2.14 
10 1 CD2 A HIS 709  ? A O   A HOH 3045 ? ? 2.16 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    OG 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    SER 
_pdbx_validate_symm_contact.auth_seq_id_1     53 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    B 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     2448 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   1_455 
_pdbx_validate_symm_contact.dist              2.19 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 C   A ASP 316 ? B N   A LEU 317 ? ? 1.646 1.336 0.310  0.023 Y 
2 1 SD  A MET 501 ? ? CE  A MET 501 ? ? 1.394 1.774 -0.380 0.056 N 
3 1 CE2 A TYR 506 ? B CD2 A TYR 506 ? B 1.479 1.389 0.090  0.015 N 
4 1 C   A HIS 599 ? B N   A HIS 600 ? ? 1.554 1.336 0.218  0.023 Y 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1  1 CA A ASP 316 ? B C  A ASP 316 ? B N   A LEU 317 ? ? 100.99 117.20 -16.21 2.20 Y 
2  1 O  A ASP 316 ? B C  A ASP 316 ? B N   A LEU 317 ? ? 134.32 122.70 11.62  1.60 Y 
3  1 NE A ARG 343 ? ? CZ A ARG 343 ? ? NH2 A ARG 343 ? ? 117.30 120.30 -3.00  0.50 N 
4  1 NE A ARG 427 ? ? CZ A ARG 427 ? ? NH1 A ARG 427 ? ? 124.13 120.30 3.83   0.50 N 
5  1 NE A ARG 427 ? ? CZ A ARG 427 ? ? NH2 A ARG 427 ? ? 117.15 120.30 -3.15  0.50 N 
6  1 O  A TYR 435 ? B C  A TYR 435 ? B N   A VAL 436 ? ? 112.75 122.70 -9.95  1.60 Y 
7  1 NE A ARG 457 ? ? CZ A ARG 457 ? ? NH2 A ARG 457 ? ? 117.18 120.30 -3.12  0.50 N 
8  1 CG A MET 501 ? ? SD A MET 501 ? ? CE  A MET 501 ? ? 89.12  100.20 -11.08 1.60 N 
9  1 NE A ARG 565 ? ? CZ A ARG 565 ? ? NH2 A ARG 565 ? ? 117.17 120.30 -3.13  0.50 N 
10 1 CA A HIS 599 ? B C  A HIS 599 ? B N   A HIS 600 ? ? 102.24 117.20 -14.96 2.20 Y 
11 1 NE A ARG 963 ? ? CZ A ARG 963 ? ? NH2 A ARG 963 ? ? 117.03 120.30 -3.27  0.50 N 
12 1 CA A LEU 979 ? A CB A LEU 979 ? A CG  A LEU 979 ? A 131.25 115.30 15.95  2.30 N 
13 1 CA A LEU 979 ? B CB A LEU 979 ? B CG  A LEU 979 ? B 131.24 115.30 15.94  2.30 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 HIS A 79  ? ? -155.10 83.56   
2  1 TRP A 95  ? ? -168.71 -84.36  
3  1 ASP A 106 ? ? -133.89 -59.59  
4  1 THR A 162 ? ? 68.34   -65.65  
5  1 GLN A 227 ? ? -134.40 -49.77  
6  1 ARG A 289 ? ? -97.73  34.79   
7  1 ASP A 340 ? ? -170.10 -168.67 
8  1 SER A 411 ? A 41.30   -125.23 
9  1 SER A 411 ? B 46.56   -122.91 
10 1 ILE A 549 ? ? -144.11 -46.47  
11 1 LEU A 550 ? ? -168.44 116.49  
12 1 PRO A 562 ? ? -82.15  39.81   
13 1 ASN A 732 ? ? -93.04  59.53   
14 1 SER A 762 ? ? 71.76   -4.56   
15 1 ILE A 831 ? ? -118.80 78.15   
16 1 SER A 833 ? ? -150.19 -14.74  
17 1 ASP A 839 ? ? -126.57 -161.22 
18 1 GLU A 991 ? ? 13.54   109.47  
19 1 GLU A 992 ? ? -121.33 -122.45 
20 1 HIS A 993 ? ? -18.85  99.89   
# 
loop_
_pdbx_validate_main_chain_plane.id 
_pdbx_validate_main_chain_plane.PDB_model_num 
_pdbx_validate_main_chain_plane.auth_comp_id 
_pdbx_validate_main_chain_plane.auth_asym_id 
_pdbx_validate_main_chain_plane.auth_seq_id 
_pdbx_validate_main_chain_plane.PDB_ins_code 
_pdbx_validate_main_chain_plane.label_alt_id 
_pdbx_validate_main_chain_plane.improper_torsion_angle 
1 1 TYR A 435 ? B -10.58 
2 1 HIS A 599 ? B 11.50  
# 
_pdbx_validate_chiral.id              1 
_pdbx_validate_chiral.PDB_model_num   1 
_pdbx_validate_chiral.auth_atom_id    C4 
_pdbx_validate_chiral.label_alt_id    ? 
_pdbx_validate_chiral.auth_asym_id    A 
_pdbx_validate_chiral.auth_comp_id    MPD 
_pdbx_validate_chiral.auth_seq_id     2002 
_pdbx_validate_chiral.PDB_ins_code    ? 
_pdbx_validate_chiral.details         'WRONG HAND' 
_pdbx_validate_chiral.omega           . 
# 
_pdbx_validate_polymer_linkage.id               1 
_pdbx_validate_polymer_linkage.PDB_model_num    1 
_pdbx_validate_polymer_linkage.auth_atom_id_1   C 
_pdbx_validate_polymer_linkage.auth_asym_id_1   A 
_pdbx_validate_polymer_linkage.auth_comp_id_1   ASP 
_pdbx_validate_polymer_linkage.auth_seq_id_1    316 
_pdbx_validate_polymer_linkage.PDB_ins_code_1   ? 
_pdbx_validate_polymer_linkage.label_alt_id_1   B 
_pdbx_validate_polymer_linkage.auth_atom_id_2   N 
_pdbx_validate_polymer_linkage.auth_asym_id_2   A 
_pdbx_validate_polymer_linkage.auth_comp_id_2   LEU 
_pdbx_validate_polymer_linkage.auth_seq_id_2    317 
_pdbx_validate_polymer_linkage.PDB_ins_code_2   ? 
_pdbx_validate_polymer_linkage.label_alt_id_2   ? 
_pdbx_validate_polymer_linkage.dist             1.65 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A ARG 1    ? A ARG 1    
2  1 Y 1 A SER 2    ? A SER 2    
3  1 Y 1 A SER 3    ? A SER 3    
4  1 Y 1 A HIS 4    ? A HIS 4    
5  1 Y 1 A HIS 5    ? A HIS 5    
6  1 Y 1 A HIS 6    ? A HIS 6    
7  1 Y 1 A HIS 7    ? A HIS 7    
8  1 Y 1 A HIS 8    ? A HIS 8    
9  1 Y 1 A HIS 9    ? A HIS 9    
10 1 Y 1 A GLY 10   ? A GLY 10   
11 1 Y 1 A GLU 11   ? A GLU 11   
12 1 Y 1 A PHE 12   ? A PHE 12   
13 1 Y 1 A ASP 13   ? A ASP 13   
14 1 Y 1 A ASP 14   ? A ASP 14   
15 1 Y 1 A PRO 15   ? A PRO 15   
16 1 Y 1 A ILE 16   ? A ILE 16   
17 1 Y 1 A ARG 17   ? A ARG 17   
18 1 Y 1 A PRO 18   ? A PRO 18   
19 1 Y 1 A PRO 19   ? A PRO 19   
20 1 Y 1 A LEU 20   ? A LEU 20   
21 1 Y 1 A LYS 21   ? A LYS 21   
22 1 Y 1 A VAL 22   ? A VAL 22   
23 1 Y 1 A ALA 23   ? A ALA 23   
24 1 Y 1 A ARG 24   ? A ARG 24   
25 1 Y 1 A SER 25   ? A SER 25   
26 1 Y 1 A PRO 26   ? A PRO 26   
27 1 Y 1 A ARG 27   ? A ARG 27   
28 1 Y 1 A PRO 28   ? A PRO 28   
29 1 Y 1 A GLY 29   ? A GLY 29   
30 1 Y 1 A GLN 30   ? A GLN 30   
31 1 Y 1 A SER 1045 ? A SER 1045 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 N-ACETYL-D-GLUCOSAMINE                   NAG 
3 'ZINC ION'                               ZN  
4 '2-DEOXY-2-FLUOROHEXOPYRANOSYL FLUORIDE' FMF 
5 '(4S)-2-METHYL-2,4-PENTANEDIOL'          MPD 
6 water                                    HOH 
# 
