data_2F1A
# 
_entry.id   2F1A 
# 
_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   2F1A         
RCSB  RCSB035327   
WWPDB D_1000035327 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 1HTY . unspecified 
PDB 1HWW . unspecified 
PDB 1HXK . unspecified 
PDB 1PS2 . unspecified 
PDB 1QWN . unspecified 
PDB 1QX1 . unspecified 
PDB 1R33 . unspecified 
PDB 1R34 . unspecified 
PDB 1TQS . unspecified 
PDB 1TQT . unspecified 
PDB 1TQU . unspecified 
PDB 1TQW . unspecified 
PDB 2ALW . unspecified 
PDB 2F18 . unspecified 
PDB 2F1B . unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        2F1A 
_pdbx_database_status.recvd_initial_deposition_date   2005-11-14 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Kuntz, D.A.' 1 
'Rose, D.R.'  2 
# 
_citation.id                        primary 
_citation.title                     
'Evaluation of docking programs for predicting binding of Golgi alpha-mannosidase II inhibitors: a comparison with crystallography.' 
_citation.journal_abbrev            Proteins 
_citation.journal_volume            69 
_citation.page_first                160 
_citation.page_last                 176 
_citation.year                      2007 
_citation.journal_id_ASTM           PSFGEY 
_citation.country                   US 
_citation.journal_id_ISSN           0887-3585 
_citation.journal_id_CSD            0867 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   17557336 
_citation.pdbx_database_id_DOI      10.1002/prot.21479 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Englebienne, P.'    1 
primary 'Fiaux, H.'          2 
primary 'Kuntz, D.A.'        3 
primary 'Corbeil, C.R.'      4 
primary 'Gerber-Lemaire, S.' 5 
primary 'Rose, D.R.'         6 
primary 'Moitessier, N.'     7 
# 
_cell.entry_id           2F1A 
_cell.length_a           68.904 
_cell.length_b           109.360 
_cell.length_c           138.585 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         2F1A 
_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 
_symmetry.space_group_name_Hall            ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'alpha-mannosidase II'                                                           119701.617 1    3.2.1.114 ? 
'CATALYTIC DOMAIN' ? 
2 non-polymer man N-ACETYL-D-GLUCOSAMINE                                                           221.208    1    ?         ? ? ? 
3 non-polymer syn 'PHOSPHATE ION'                                                                  94.971     1    ?         ? ? ? 
4 non-polymer syn 'ZINC ION'                                                                       65.409     1    ?         ? ? ? 
5 non-polymer syn '(2R,3R,4S)-2-({[(1S)-2-HYDROXY-1-PHENYLETHYL]AMINO}METHYL)PYRROLIDINE-3,4-DIOL' 252.309    1    ?         ? ? ? 
6 non-polymer syn '(4S)-2-METHYL-2,4-PENTANEDIOL'                                                  118.174    1    ?         ? ? ? 
7 water       nat water                                                                            18.015     1099 ?         ? ? ? 
# 
_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
QWKKKAELYRTNVLLIPLGDDFRFKQNTEWDVQRVNYERLFEHINSQAHFNVQAQFGTLQEYFDAVHQAERAGQAEFPTL
SGDFFTYADRSDNYWSGYYTSRPYHKRMDRVLMHYVRAAEMLSAWHSWDGMARIEERLEQARRELSLFQHHDGITGTAKT
HVVVDYEQRMQEALKACQMVMQQSVYRLLTKPSIYSPDFSFSYFTLDDSRWPGSGVEDSRTTIILGEDILPSKHVVMHNT
LPHWREQLVDFYVSSPFVSVTDLANNPVEAQVSPVWSWHHDTLTKTIHPQGSTTKYRIIFKARVPPMGLATYVLTISDSK
PEHTSYASNLLLRKNPTSLPLGQYPEDVKFGDPREISLRVGNGPTLAFSEQGLLKSIQLTQDSPHVPVHFKFLKYGVRSH
GDRSGAYLFLPNGPASPVELGQPVVLVTKGKLESSVSVGLPSVVHQTIMRGGAPEIRNLVDIGSLDNTEIVMRLETHIDS
GDIFYTDLNGLQFIKRRRLDKLPLQANYYPIPSGMFIEDANTRLTLLTGQPLGGSSLASGELEIMQDRRLASDDERGLGQ
GVLDNKPVLHIYRLVLEKVNNCVRPSKLHPAGYLTSAAHKASQSLLDPLDKFIFAENEWIGAQGQFGGDHPSAREDLDVS
VMRRLTKSSAKTQRVGYVLHRTNLMQCGTPEEHTQKLDVCHLLPNVARCERTTLTFLQNLEHLDGMVAPEVCPMETAAYV
SSHSS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;RSSHHHHHHGEFDDPIRPPLKVARSPRPGQCQDVVQDVPNVDVQMLELYDRMSFKDIDGGVWKQGWNIKYDPLKYNAHHK
LKVFVVPHSHNDPGWIQTFEEYYQHDTKHILSNALRHLHDNPEMKFIWAEISYFARFYHDLGENKKLQMKSIVKNGQLEF
VTGGWVMPDEANSHWRNVLLQLTEGQTWLKQFMNVTPTASWAIDPFGHSPTMPYILQKSGFKNMLIQRTHYSVKKELAQQ
RQLEFLWRQIWDNKGDTALFTHMMPFYSYDIPHTCGPDPKVCCQFDFKRMGSFGLSCPWKVPPRTISDQNVAARSDLLVD
QWKKKAELYRTNVLLIPLGDDFRFKQNTEWDVQRVNYERLFEHINSQAHFNVQAQFGTLQEYFDAVHQAERAGQAEFPTL
SGDFFTYADRSDNYWSGYYTSRPYHKRMDRVLMHYVRAAEMLSAWHSWDGMARIEERLEQARRELSLFQHHDGITGTAKT
HVVVDYEQRMQEALKACQMVMQQSVYRLLTKPSIYSPDFSFSYFTLDDSRWPGSGVEDSRTTIILGEDILPSKHVVMHNT
LPHWREQLVDFYVSSPFVSVTDLANNPVEAQVSPVWSWHHDTLTKTIHPQGSTTKYRIIFKARVPPMGLATYVLTISDSK
PEHTSYASNLLLRKNPTSLPLGQYPEDVKFGDPREISLRVGNGPTLAFSEQGLLKSIQLTQDSPHVPVHFKFLKYGVRSH
GDRSGAYLFLPNGPASPVELGQPVVLVTKGKLESSVSVGLPSVVHQTIMRGGAPEIRNLVDIGSLDNTEIVMRLETHIDS
GDIFYTDLNGLQFIKRRRLDKLPLQANYYPIPSGMFIEDANTRLTLLTGQPLGGSSLASGELEIMQDRRLASDDERGLGQ
GVLDNKPVLHIYRLVLEKVNNCVRPSKLHPAGYLTSAAHKASQSLLDPLDKFIFAENEWIGAQGQFGGDHPSAREDLDVS
VMRRLTKSSAKTQRVGYVLHRTNLMQCGTPEEHTQKLDVCHLLPNVARCERTTLTFLQNLEHLDGMVAPEVCPMETAAYV
SSHSS
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1    ARG n 
1 2    SER n 
1 3    SER n 
1 4    HIS n 
1 5    HIS n 
1 6    HIS n 
1 7    HIS n 
1 8    HIS n 
1 9    HIS n 
1 10   GLY n 
1 11   GLU n 
1 12   PHE n 
1 13   ASP n 
1 14   ASP n 
1 15   PRO n 
1 16   ILE n 
1 17   ARG n 
1 18   PRO n 
1 19   PRO n 
1 20   LEU n 
1 21   LYS n 
1 22   VAL n 
1 23   ALA n 
1 24   ARG n 
1 25   SER n 
1 26   PRO n 
1 27   ARG n 
1 28   PRO n 
1 29   GLY n 
1 30   GLN n 
1 31   CYS n 
1 32   GLN n 
1 33   ASP n 
1 34   VAL n 
1 35   VAL n 
1 36   GLN n 
1 37   ASP n 
1 38   VAL n 
1 39   PRO n 
1 40   ASN n 
1 41   VAL n 
1 42   ASP n 
1 43   VAL n 
1 44   GLN n 
1 45   MET n 
1 46   LEU n 
1 47   GLU n 
1 48   LEU n 
1 49   TYR n 
1 50   ASP n 
1 51   ARG n 
1 52   MET n 
1 53   SER n 
1 54   PHE n 
1 55   LYS n 
1 56   ASP n 
1 57   ILE n 
1 58   ASP n 
1 59   GLY n 
1 60   GLY n 
1 61   VAL n 
1 62   TRP n 
1 63   LYS n 
1 64   GLN n 
1 65   GLY n 
1 66   TRP n 
1 67   ASN n 
1 68   ILE n 
1 69   LYS n 
1 70   TYR n 
1 71   ASP n 
1 72   PRO n 
1 73   LEU n 
1 74   LYS n 
1 75   TYR n 
1 76   ASN n 
1 77   ALA n 
1 78   HIS n 
1 79   HIS n 
1 80   LYS n 
1 81   LEU n 
1 82   LYS n 
1 83   VAL n 
1 84   PHE n 
1 85   VAL n 
1 86   VAL n 
1 87   PRO n 
1 88   HIS n 
1 89   SER n 
1 90   HIS n 
1 91   ASN n 
1 92   ASP n 
1 93   PRO n 
1 94   GLY n 
1 95   TRP n 
1 96   ILE n 
1 97   GLN n 
1 98   THR n 
1 99   PHE n 
1 100  GLU n 
1 101  GLU n 
1 102  TYR n 
1 103  TYR n 
1 104  GLN n 
1 105  HIS n 
1 106  ASP n 
1 107  THR n 
1 108  LYS n 
1 109  HIS n 
1 110  ILE n 
1 111  LEU n 
1 112  SER n 
1 113  ASN n 
1 114  ALA n 
1 115  LEU n 
1 116  ARG n 
1 117  HIS n 
1 118  LEU n 
1 119  HIS n 
1 120  ASP n 
1 121  ASN n 
1 122  PRO n 
1 123  GLU n 
1 124  MET n 
1 125  LYS n 
1 126  PHE n 
1 127  ILE n 
1 128  TRP n 
1 129  ALA n 
1 130  GLU n 
1 131  ILE n 
1 132  SER n 
1 133  TYR n 
1 134  PHE n 
1 135  ALA n 
1 136  ARG n 
1 137  PHE n 
1 138  TYR n 
1 139  HIS n 
1 140  ASP n 
1 141  LEU n 
1 142  GLY n 
1 143  GLU n 
1 144  ASN n 
1 145  LYS n 
1 146  LYS n 
1 147  LEU n 
1 148  GLN n 
1 149  MET n 
1 150  LYS n 
1 151  SER n 
1 152  ILE n 
1 153  VAL n 
1 154  LYS n 
1 155  ASN n 
1 156  GLY n 
1 157  GLN n 
1 158  LEU n 
1 159  GLU n 
1 160  PHE n 
1 161  VAL n 
1 162  THR n 
1 163  GLY n 
1 164  GLY n 
1 165  TRP n 
1 166  VAL n 
1 167  MET n 
1 168  PRO n 
1 169  ASP n 
1 170  GLU n 
1 171  ALA n 
1 172  ASN n 
1 173  SER n 
1 174  HIS n 
1 175  TRP n 
1 176  ARG n 
1 177  ASN n 
1 178  VAL n 
1 179  LEU n 
1 180  LEU n 
1 181  GLN n 
1 182  LEU n 
1 183  THR n 
1 184  GLU n 
1 185  GLY n 
1 186  GLN n 
1 187  THR n 
1 188  TRP n 
1 189  LEU n 
1 190  LYS n 
1 191  GLN n 
1 192  PHE n 
1 193  MET n 
1 194  ASN n 
1 195  VAL n 
1 196  THR n 
1 197  PRO n 
1 198  THR n 
1 199  ALA n 
1 200  SER n 
1 201  TRP n 
1 202  ALA n 
1 203  ILE n 
1 204  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  ASP n 
1 342  PHE n 
1 343  ARG n 
1 344  PHE n 
1 345  LYS n 
1 346  GLN n 
1 347  ASN n 
1 348  THR n 
1 349  GLU n 
1 350  TRP n 
1 351  ASP n 
1 352  VAL n 
1 353  GLN n 
1 354  ARG n 
1 355  VAL n 
1 356  ASN n 
1 357  TYR n 
1 358  GLU n 
1 359  ARG n 
1 360  LEU n 
1 361  PHE n 
1 362  GLU n 
1 363  HIS n 
1 364  ILE n 
1 365  ASN n 
1 366  SER n 
1 367  GLN n 
1 368  ALA n 
1 369  HIS n 
1 370  PHE n 
1 371  ASN n 
1 372  VAL n 
1 373  GLN n 
1 374  ALA n 
1 375  GLN n 
1 376  PHE n 
1 377  GLY n 
1 378  THR n 
1 379  LEU n 
1 380  GLN n 
1 381  GLU n 
1 382  TYR n 
1 383  PHE n 
1 384  ASP n 
1 385  ALA n 
1 386  VAL n 
1 387  HIS n 
1 388  GLN n 
1 389  ALA n 
1 390  GLU n 
1 391  ARG n 
1 392  ALA n 
1 393  GLY n 
1 394  GLN n 
1 395  ALA n 
1 396  GLU n 
1 397  PHE n 
1 398  PRO n 
1 399  THR n 
1 400  LEU n 
1 401  SER n 
1 402  GLY n 
1 403  ASP n 
1 404  PHE n 
1 405  PHE n 
1 406  THR n 
1 407  TYR n 
1 408  ALA n 
1 409  ASP n 
1 410  ARG n 
1 411  SER n 
1 412  ASP n 
1 413  ASN n 
1 414  TYR n 
1 415  TRP n 
1 416  SER n 
1 417  GLY n 
1 418  TYR n 
1 419  TYR n 
1 420  THR n 
1 421  SER n 
1 422  ARG n 
1 423  PRO n 
1 424  TYR n 
1 425  HIS n 
1 426  LYS n 
1 427  ARG n 
1 428  MET n 
1 429  ASP n 
1 430  ARG n 
1 431  VAL n 
1 432  LEU n 
1 433  MET n 
1 434  HIS n 
1 435  TYR n 
1 436  VAL n 
1 437  ARG n 
1 438  ALA n 
1 439  ALA n 
1 440  GLU n 
1 441  MET n 
1 442  LEU n 
1 443  SER n 
1 444  ALA n 
1 445  TRP n 
1 446  HIS n 
1 447  SER n 
1 448  TRP n 
1 449  ASP n 
1 450  GLY n 
1 451  MET n 
1 452  ALA n 
1 453  ARG n 
1 454  ILE n 
1 455  GLU n 
1 456  GLU n 
1 457  ARG n 
1 458  LEU n 
1 459  GLU n 
1 460  GLN n 
1 461  ALA n 
1 462  ARG n 
1 463  ARG n 
1 464  GLU n 
1 465  LEU n 
1 466  SER n 
1 467  LEU n 
1 468  PHE n 
1 469  GLN n 
1 470  HIS n 
1 471  HIS n 
1 472  ASP n 
1 473  GLY n 
1 474  ILE n 
1 475  THR n 
1 476  GLY n 
1 477  THR n 
1 478  ALA n 
1 479  LYS n 
1 480  THR n 
1 481  HIS n 
1 482  VAL n 
1 483  VAL n 
1 484  VAL n 
1 485  ASP n 
1 486  TYR n 
1 487  GLU n 
1 488  GLN n 
1 489  ARG n 
1 490  MET n 
1 491  GLN n 
1 492  GLU n 
1 493  ALA n 
1 494  LEU n 
1 495  LYS n 
1 496  ALA n 
1 497  CYS n 
1 498  GLN n 
1 499  MET n 
1 500  VAL n 
1 501  MET n 
1 502  GLN n 
1 503  GLN n 
1 504  SER n 
1 505  VAL n 
1 506  TYR n 
1 507  ARG n 
1 508  LEU n 
1 509  LEU n 
1 510  THR n 
1 511  LYS n 
1 512  PRO n 
1 513  SER n 
1 514  ILE n 
1 515  TYR n 
1 516  SER n 
1 517  PRO n 
1 518  ASP n 
1 519  PHE n 
1 520  SER n 
1 521  PHE n 
1 522  SER n 
1 523  TYR n 
1 524  PHE n 
1 525  THR n 
1 526  LEU n 
1 527  ASP n 
1 528  ASP n 
1 529  SER n 
1 530  ARG n 
1 531  TRP n 
1 532  PRO n 
1 533  GLY n 
1 534  SER n 
1 535  GLY n 
1 536  VAL n 
1 537  GLU n 
1 538  ASP n 
1 539  SER n 
1 540  ARG n 
1 541  THR n 
1 542  THR n 
1 543  ILE n 
1 544  ILE n 
1 545  LEU n 
1 546  GLY n 
1 547  GLU n 
1 548  ASP n 
1 549  ILE n 
1 550  LEU n 
1 551  PRO n 
1 552  SER n 
1 553  LYS n 
1 554  HIS n 
1 555  VAL n 
1 556  VAL n 
1 557  MET n 
1 558  HIS n 
1 559  ASN n 
1 560  THR n 
1 561  LEU n 
1 562  PRO n 
1 563  HIS n 
1 564  TRP n 
1 565  ARG n 
1 566  GLU n 
1 567  GLN n 
1 568  LEU n 
1 569  VAL n 
1 570  ASP n 
1 571  PHE n 
1 572  TYR n 
1 573  VAL n 
1 574  SER n 
1 575  SER n 
1 576  PRO n 
1 577  PHE n 
1 578  VAL n 
1 579  SER n 
1 580  VAL n 
1 581  THR n 
1 582  ASP n 
1 583  LEU n 
1 584  ALA n 
1 585  ASN n 
1 586  ASN n 
1 587  PRO n 
1 588  VAL n 
1 589  GLU n 
1 590  ALA n 
1 591  GLN n 
1 592  VAL n 
1 593  SER n 
1 594  PRO n 
1 595  VAL n 
1 596  TRP n 
1 597  SER n 
1 598  TRP n 
1 599  HIS n 
1 600  HIS n 
1 601  ASP n 
1 602  THR n 
1 603  LEU n 
1 604  THR n 
1 605  LYS n 
1 606  THR n 
1 607  ILE n 
1 608  HIS n 
1 609  PRO n 
1 610  GLN n 
1 611  GLY n 
1 612  SER n 
1 613  THR n 
1 614  THR n 
1 615  LYS n 
1 616  TYR n 
1 617  ARG n 
1 618  ILE n 
1 619  ILE n 
1 620  PHE n 
1 621  LYS n 
1 622  ALA n 
1 623  ARG n 
1 624  VAL n 
1 625  PRO n 
1 626  PRO n 
1 627  MET n 
1 628  GLY n 
1 629  LEU n 
1 630  ALA n 
1 631  THR n 
1 632  TYR n 
1 633  VAL n 
1 634  LEU n 
1 635  THR n 
1 636  ILE n 
1 637  SER n 
1 638  ASP n 
1 639  SER n 
1 640  LYS n 
1 641  PRO n 
1 642  GLU n 
1 643  HIS n 
1 644  THR n 
1 645  SER n 
1 646  TYR n 
1 647  ALA n 
1 648  SER n 
1 649  ASN n 
1 650  LEU n 
1 651  LEU n 
1 652  LEU n 
1 653  ARG n 
1 654  LYS n 
1 655  ASN n 
1 656  PRO n 
1 657  THR n 
1 658  SER n 
1 659  LEU n 
1 660  PRO n 
1 661  LEU n 
1 662  GLY n 
1 663  GLN n 
1 664  TYR n 
1 665  PRO n 
1 666  GLU n 
1 667  ASP n 
1 668  VAL n 
1 669  LYS n 
1 670  PHE n 
1 671  GLY n 
1 672  ASP n 
1 673  PRO n 
1 674  ARG n 
1 675  GLU n 
1 676  ILE n 
1 677  SER n 
1 678  LEU n 
1 679  ARG n 
1 680  VAL n 
1 681  GLY n 
1 682  ASN n 
1 683  GLY n 
1 684  PRO n 
1 685  THR n 
1 686  LEU n 
1 687  ALA n 
1 688  PHE n 
1 689  SER n 
1 690  GLU n 
1 691  GLN n 
1 692  GLY n 
1 693  LEU n 
1 694  LEU n 
1 695  LYS n 
1 696  SER n 
1 697  ILE n 
1 698  GLN n 
1 699  LEU n 
1 700  THR n 
1 701  GLN n 
1 702  ASP n 
1 703  SER n 
1 704  PRO n 
1 705  HIS n 
1 706  VAL n 
1 707  PRO n 
1 708  VAL n 
1 709  HIS n 
1 710  PHE n 
1 711  LYS n 
1 712  PHE n 
1 713  LEU n 
1 714  LYS n 
1 715  TYR n 
1 716  GLY n 
1 717  VAL n 
1 718  ARG n 
1 719  SER n 
1 720  HIS n 
1 721  GLY n 
1 722  ASP n 
1 723  ARG n 
1 724  SER n 
1 725  GLY n 
1 726  ALA n 
1 727  TYR n 
1 728  LEU n 
1 729  PHE n 
1 730  LEU n 
1 731  PRO n 
1 732  ASN n 
1 733  GLY n 
1 734  PRO n 
1 735  ALA n 
1 736  SER n 
1 737  PRO n 
1 738  VAL n 
1 739  GLU n 
1 740  LEU n 
1 741  GLY n 
1 742  GLN n 
1 743  PRO n 
1 744  VAL n 
1 745  VAL n 
1 746  LEU n 
1 747  VAL n 
1 748  THR n 
1 749  LYS n 
1 750  GLY n 
1 751  LYS n 
1 752  LEU n 
1 753  GLU n 
1 754  SER n 
1 755  SER n 
1 756  VAL n 
1 757  SER n 
1 758  VAL n 
1 759  GLY n 
1 760  LEU n 
1 761  PRO n 
1 762  SER n 
1 763  VAL n 
1 764  VAL n 
1 765  HIS n 
1 766  GLN n 
1 767  THR n 
1 768  ILE n 
1 769  MET n 
1 770  ARG n 
1 771  GLY n 
1 772  GLY n 
1 773  ALA n 
1 774  PRO n 
1 775  GLU n 
1 776  ILE n 
1 777  ARG n 
1 778  ASN n 
1 779  LEU n 
1 780  VAL n 
1 781  ASP n 
1 782  ILE n 
1 783  GLY n 
1 784  SER n 
1 785  LEU n 
1 786  ASP n 
1 787  ASN n 
1 788  THR n 
1 789  GLU n 
1 790  ILE n 
1 791  VAL n 
1 792  MET n 
1 793  ARG n 
1 794  LEU n 
1 795  GLU n 
1 796  THR n 
1 797  HIS n 
1 798  ILE n 
1 799  ASP n 
1 800  SER n 
1 801  GLY n 
1 802  ASP n 
1 803  ILE n 
1 804  PHE n 
1 805  TYR n 
1 806  THR n 
1 807  ASP n 
1 808  LEU n 
1 809  ASN n 
1 810  GLY n 
1 811  LEU n 
1 812  GLN n 
1 813  PHE n 
1 814  ILE n 
1 815  LYS n 
1 816  ARG n 
1 817  ARG n 
1 818  ARG n 
1 819  LEU n 
1 820  ASP n 
1 821  LYS n 
1 822  LEU n 
1 823  PRO n 
1 824  LEU n 
1 825  GLN n 
1 826  ALA n 
1 827  ASN n 
1 828  TYR n 
1 829  TYR n 
1 830  PRO n 
1 831  ILE n 
1 832  PRO n 
1 833  SER n 
1 834  GLY n 
1 835  MET n 
1 836  PHE n 
1 837  ILE n 
1 838  GLU n 
1 839  ASP n 
1 840  ALA n 
1 841  ASN n 
1 842  THR n 
1 843  ARG n 
1 844  LEU n 
1 845  THR n 
1 846  LEU n 
1 847  LEU n 
1 848  THR n 
1 849  GLY n 
1 850  GLN n 
1 851  PRO n 
1 852  LEU n 
1 853  GLY n 
1 854  GLY n 
1 855  SER n 
1 856  SER n 
1 857  LEU n 
1 858  ALA n 
1 859  SER n 
1 860  GLY n 
1 861  GLU n 
1 862  LEU n 
1 863  GLU n 
1 864  ILE n 
1 865  MET n 
1 866  GLN n 
1 867  ASP n 
1 868  ARG n 
1 869  ARG n 
1 870  LEU n 
1 871  ALA n 
1 872  SER n 
1 873  ASP n 
1 874  ASP n 
1 875  GLU n 
1 876  ARG n 
1 877  GLY n 
1 878  LEU n 
1 879  GLY n 
1 880  GLN n 
1 881  GLY n 
1 882  VAL n 
1 883  LEU n 
1 884  ASP n 
1 885  ASN n 
1 886  LYS n 
1 887  PRO n 
1 888  VAL n 
1 889  LEU n 
1 890  HIS n 
1 891  ILE n 
1 892  TYR n 
1 893  ARG n 
1 894  LEU n 
1 895  VAL n 
1 896  LEU n 
1 897  GLU n 
1 898  LYS n 
1 899  VAL n 
1 900  ASN n 
1 901  ASN n 
1 902  CYS n 
1 903  VAL n 
1 904  ARG n 
1 905  PRO n 
1 906  SER n 
1 907  LYS n 
1 908  LEU n 
1 909  HIS n 
1 910  PRO n 
1 911  ALA n 
1 912  GLY n 
1 913  TYR n 
1 914  LEU n 
1 915  THR n 
1 916  SER n 
1 917  ALA n 
1 918  ALA n 
1 919  HIS n 
1 920  LYS n 
1 921  ALA n 
1 922  SER n 
1 923  GLN n 
1 924  SER n 
1 925  LEU n 
1 926  LEU n 
1 927  ASP n 
1 928  PRO n 
1 929  LEU n 
1 930  ASP n 
1 931  LYS n 
1 932  PHE n 
1 933  ILE n 
1 934  PHE n 
1 935  ALA n 
1 936  GLU n 
1 937  ASN n 
1 938  GLU n 
1 939  TRP n 
1 940  ILE n 
1 941  GLY n 
1 942  ALA n 
1 943  GLN n 
1 944  GLY n 
1 945  GLN n 
1 946  PHE n 
1 947  GLY n 
1 948  GLY n 
1 949  ASP n 
1 950  HIS n 
1 951  PRO n 
1 952  SER n 
1 953  ALA n 
1 954  ARG n 
1 955  GLU n 
1 956  ASP n 
1 957  LEU n 
1 958  ASP n 
1 959  VAL n 
1 960  SER n 
1 961  VAL n 
1 962  MET n 
1 963  ARG n 
1 964  ARG n 
1 965  LEU n 
1 966  THR n 
1 967  LYS n 
1 968  SER n 
1 969  SER n 
1 970  ALA n 
1 971  LYS n 
1 972  THR n 
1 973  GLN n 
1 974  ARG n 
1 975  VAL n 
1 976  GLY n 
1 977  TYR n 
1 978  VAL n 
1 979  LEU n 
1 980  HIS n 
1 981  ARG n 
1 982  THR n 
1 983  ASN n 
1 984  LEU n 
1 985  MET n 
1 986  GLN n 
1 987  CYS n 
1 988  GLY n 
1 989  THR n 
1 990  PRO n 
1 991  GLU n 
1 992  GLU n 
1 993  HIS n 
1 994  THR n 
1 995  GLN n 
1 996  LYS n 
1 997  LEU n 
1 998  ASP n 
1 999  VAL n 
1 1000 CYS n 
1 1001 HIS n 
1 1002 LEU n 
1 1003 LEU n 
1 1004 PRO n 
1 1005 ASN n 
1 1006 VAL n 
1 1007 ALA n 
1 1008 ARG n 
1 1009 CYS n 
1 1010 GLU n 
1 1011 ARG n 
1 1012 THR n 
1 1013 THR n 
1 1014 LEU n 
1 1015 THR n 
1 1016 PHE n 
1 1017 LEU n 
1 1018 GLN n 
1 1019 ASN n 
1 1020 LEU n 
1 1021 GLU n 
1 1022 HIS n 
1 1023 LEU n 
1 1024 ASP n 
1 1025 GLY n 
1 1026 MET n 
1 1027 VAL n 
1 1028 ALA n 
1 1029 PRO n 
1 1030 GLU n 
1 1031 VAL n 
1 1032 CYS n 
1 1033 PRO n 
1 1034 MET n 
1 1035 GLU n 
1 1036 THR n 
1 1037 ALA n 
1 1038 ALA n 
1 1039 TYR n 
1 1040 VAL n 
1 1041 SER n 
1 1042 SER n 
1 1043 HIS n 
1 1044 SER n 
1 1045 SER n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               'fruit fly' 
_entity_src_gen.gene_src_genus                     Drosophila 
_entity_src_gen.pdbx_gene_src_gene                 'alpha-Man-II, GmII' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Drosophila melanogaster' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     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 cells' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          'Stable transfection plasmid' 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pMTBIP_NHIS 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    GB 
_struct_ref.db_code                    CAA54732 
_struct_ref.pdbx_db_accession          517481 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;DDPIRPPLKVARSPRPGQCQDVVQDVPNVDVQMLELYDRMSFKDIDGGVWKQGWNIKYDPLKYNAHHKLKVFVVPHSHND
PGWIQTFEEYYQHDTKHILSNALRHLHDNPEMKFIWAEISYFARFYHDLGENKKLQMKSIVKNGQLEFVTGGWVMPDEAN
SHWRNVLLQLTEGQTWLKQFMNVTPTASWAIDPFGHSPTMPYILQKSGFKNMLIQRTHYSVKKELAQQRQLEFLWRQIWD
NKGDTALFTHMMPFYSYDIPHTCGPDPKVCCQFDFKRMGSFGLSCPWKVPPRTISDQNVAARSDLLVDQWKKKAELYRTN
VLLIPLGDDFRFKQNTEWDVQRVNYERLFEHINSQAHFNVQAQFGTLQEYFDAVHQAERAGQAEFPTLSGDFFTYADRSD
NYWSGYYTSRPYHKRMDRVLMHYVRAAEMLSAWHSWDGMARIEERLEQARRELSLFQHHDGITGTAKTHVVVDYEQRMQE
ALKACQMVMQQSVYRLLTKPSIYSPDFSFSYFTLDDSRWPGSGVEDSRTTIILGEDILPSKHVVMHNTLPHWREQLVDFY
VSSPFVSVTDLANNPVEAQVSPVWSWHHDTLTKTIHPQGSTTKYRIIFKARVPPMGLATYVLTISDSKPEHTSYASNLLL
RKNPTSLPLGQYPEDVKFGDPREISLRVGNGPTLAFSEQGLLKSIQLTQDSPHVPVHFKFLKYGVRSHGDRSGAYLFLPN
GPASPVELGQPVVLVTKGKLESSVSVGLPSVVHQTIMRGGAPEIRNLVDIGSLDNTEIVMRLETHIDSGDIFYTDLNGLQ
FIKRRRLDKLPLQANYYPIPSGMFIEDANTRLTLLTGQPLGGSSLASGELEIMQDRRLASDDERGLGQGVLDNKPVLHIY
RLVLEKVNNCVRPSKLHPAGYLTSAAHKASQSLLDPLDKFIFAENEWIGAQGQFGGDHPSAREDLDVSVMRRLTKSSAKT
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              2F1A 
_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             517481 
_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 2F1A ARG A 1  ? GB 517481 ? ? 'EXPRESSION TAG' 1  1  
1 2F1A SER A 2  ? GB 517481 ? ? 'EXPRESSION TAG' 2  2  
1 2F1A SER A 3  ? GB 517481 ? ? 'EXPRESSION TAG' 3  3  
1 2F1A HIS A 4  ? GB 517481 ? ? 'EXPRESSION TAG' 4  4  
1 2F1A HIS A 5  ? GB 517481 ? ? 'EXPRESSION TAG' 5  5  
1 2F1A HIS A 6  ? GB 517481 ? ? 'EXPRESSION TAG' 6  6  
1 2F1A HIS A 7  ? GB 517481 ? ? 'EXPRESSION TAG' 7  7  
1 2F1A HIS A 8  ? GB 517481 ? ? 'EXPRESSION TAG' 8  8  
1 2F1A HIS A 9  ? GB 517481 ? ? 'EXPRESSION TAG' 9  9  
1 2F1A GLY A 10 ? GB 517481 ? ? 'EXPRESSION TAG' 10 10 
1 2F1A GLU A 11 ? GB 517481 ? ? 'EXPRESSION TAG' 11 11 
1 2F1A PHE A 12 ? GB 517481 ? ? 'EXPRESSION TAG' 12 12 
# 
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 
GB2 non-polymer         . '(2R,3R,4S)-2-({[(1S)-2-HYDROXY-1-PHENYLETHYL]AMINO}METHYL)PYRROLIDINE-3,4-DIOL' ? 'C13 H20 N2 O3'  
252.309 
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 
PO4 non-polymer         . 'PHOSPHATE ION'                                                                  ? 'O4 P -3'        
94.971  
PRO 'L-peptide linking' y PROLINE                                                                          ? 'C5 H9 N O2'     
115.130 
SER 'L-peptide linking' y SERINE                                                                           ? 'C3 H7 N O3'     
105.093 
THR 'L-peptide linking' y THREONINE                                                                        ? 'C4 H9 N O3'     
119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                       ? 'C11 H12 N2 O2'  
204.225 
TYR 'L-peptide linking' y TYROSINE                                                                         ? 'C9 H11 N O3'    
181.189 
VAL 'L-peptide linking' y VALINE                                                                           ? 'C5 H11 N O2'    
117.146 
ZN  non-polymer         . 'ZINC ION'                                                                       ? 'Zn 2'           
65.409  
# 
_exptl.entry_id          2F1A 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   2 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.18 
_exptl_crystal.density_percent_sol   43.57 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              7 
_exptl_crystal_grow.pdbx_details    'Tris, PEG 6K, MPD, NaCl, 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   2004-12-10 
_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                    ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9793376 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'APS BEAMLINE 19-ID' 
_diffrn_source.pdbx_synchrotron_site       APS 
_diffrn_source.pdbx_synchrotron_beamline   19-ID 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        0.9793376 
# 
_reflns.entry_id                     2F1A 
_reflns.observed_criterion_sigma_I   2 
_reflns.observed_criterion_sigma_F   2 
_reflns.d_resolution_low             30 
_reflns.d_resolution_high            1.45 
_reflns.number_obs                   180243 
_reflns.number_all                   187133 
_reflns.percent_possible_obs         96.3 
_reflns.pdbx_Rmerge_I_obs            0.06 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        18.5 
_reflns.B_iso_Wilson_estimate        18.4 
_reflns.pdbx_redundancy              12.5 
_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_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high             1.45 
_reflns_shell.d_res_low              1.50 
_reflns_shell.percent_possible_all   88 
_reflns_shell.Rmerge_I_obs           0.57 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    3.72 
_reflns_shell.pdbx_redundancy        10 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      17773 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.pdbx_diffrn_id         1 
# 
_refine.entry_id                                 2F1A 
_refine.ls_number_reflns_obs                     174398 
_refine.ls_number_reflns_all                     185304 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          2 
_refine.pdbx_data_cutoff_high_absF               96240.67 
_refine.pdbx_data_cutoff_low_absF                0.000000 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             29.78 
_refine.ls_d_res_high                            1.45 
_refine.ls_percent_reflns_obs                    93.9 
_refine.ls_R_factor_obs                          0.168 
_refine.ls_R_factor_all                          0.169 
_refine.ls_R_factor_R_work                       0.168 
_refine.ls_R_factor_R_free                       0.189 
_refine.ls_R_factor_R_free_error                 0.003 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 2.3 
_refine.ls_number_reflns_R_free                  3983 
_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                               21.5 
_refine.aniso_B[1][1]                            -1.42 
_refine.aniso_B[2][2]                            0.75 
_refine.aniso_B[3][3]                            0.67 
_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                 0.332052 
_refine.solvent_model_param_bsol                 43.9683 
_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                      'pdb entry 1HWW' 
_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.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_analyze.entry_id                        2F1A 
_refine_analyze.Luzzati_coordinate_error_obs    0.14 
_refine_analyze.Luzzati_sigma_a_obs             0.10 
_refine_analyze.Luzzati_d_res_low_obs           30.00 
_refine_analyze.Luzzati_coordinate_error_free   0.17 
_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        8188 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         46 
_refine_hist.number_atoms_solvent             1099 
_refine_hist.number_atoms_total               9333 
_refine_hist.d_res_high                       1.45 
_refine_hist.d_res_low                        29.78 
# 
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                0.015 ?    ? ? '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             1.7   ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg_na          ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg_prot        ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d      25.1  ?    ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d_na   ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d_prot ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d      1.18  ?    ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d_na   ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d_prot ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
c_mcbond_it             1.30  1.50 ? ? 'X-RAY DIFFRACTION' ? 
c_mcangle_it            2.05  2.00 ? ? 'X-RAY DIFFRACTION' ? 
c_scbond_it             2.46  2.00 ? ? 'X-RAY DIFFRACTION' ? 
c_scangle_it            3.73  2.50 ? ? 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_total_number_of_bins_used   6 
_refine_ls_shell.d_res_high                       1.45 
_refine_ls_shell.d_res_low                        1.54 
_refine_ls_shell.number_reflns_R_work             24945 
_refine_ls_shell.R_factor_R_work                  0.226 
_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            0.012 
_refine_ls_shell.percent_reflns_R_free            2.1 
_refine_ls_shell.number_reflns_R_free             524 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
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 GB2.par            ion.top          'X-RAY DIFFRACTION' 
6 ?                  po4.top          'X-RAY DIFFRACTION' 
7 ?                  GB2.top          'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  2F1A 
_struct.title                     
'GOLGI ALPHA-MANNOSIDASE II COMPLEX WITH (2R,3R,4S)-2-({[(1S)-2-hydroxy-1-phenylethyl]amino}methyl)pyrrolidine-3,4-diol' 
_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        2F1A 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            'GLYCOSYL HYDROLASE FAMILY 38, Hydrolase' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
G N N 7 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  1  MET A 45   ? MET A 52   ? MET A 45   MET A 52   1 ? 8  
HELX_P HELX_P2  2  ASP A 71   ? TYR A 75   ? ASP A 71   TYR A 75   5 ? 5  
HELX_P HELX_P3  3  THR A 98   ? ASP A 106  ? THR A 98   ASP A 106  1 ? 9  
HELX_P HELX_P4  4  ASP A 106  ? ASN A 121  ? ASP A 106  ASN A 121  1 ? 16 
HELX_P HELX_P5  5  GLU A 130  ? HIS A 139  ? GLU A 130  HIS A 139  1 ? 10 
HELX_P HELX_P6  6  GLY A 142  ? ASN A 155  ? GLY A 142  ASN A 155  1 ? 14 
HELX_P HELX_P7  7  HIS A 174  ? ASN A 194  ? HIS A 174  ASN A 194  1 ? 21 
HELX_P HELX_P8  8  PRO A 210  ? LYS A 218  ? PRO A 210  LYS A 218  1 ? 9  
HELX_P HELX_P9  9  HIS A 230  ? GLN A 240  ? HIS A 230  GLN A 240  1 ? 11 
HELX_P HELX_P10 10 ASP A 270  ? THR A 274  ? ASP A 270  THR A 274  5 ? 5  
HELX_P HELX_P11 11 ASP A 278  ? CYS A 283  ? ASP A 278  CYS A 283  1 ? 6  
HELX_P HELX_P12 12 GLN A 284  ? MET A 290  ? GLN A 284  MET A 290  5 ? 7  
HELX_P HELX_P13 13 ASN A 310  ? GLU A 327  ? ASN A 310  GLU A 327  1 ? 18 
HELX_P HELX_P14 14 GLN A 346  ? GLN A 367  ? GLN A 346  GLN A 367  1 ? 22 
HELX_P HELX_P15 15 ALA A 368  ? PHE A 370  ? ALA A 368  PHE A 370  5 ? 3  
HELX_P HELX_P16 16 THR A 378  ? ALA A 392  ? THR A 378  ALA A 392  1 ? 15 
HELX_P HELX_P17 17 SER A 416  ? THR A 420  ? SER A 416  THR A 420  5 ? 5  
HELX_P HELX_P18 18 ARG A 422  ? TRP A 445  ? ARG A 422  TRP A 445  1 ? 24 
HELX_P HELX_P19 19 ASP A 449  ? ALA A 452  ? ASP A 449  ALA A 452  5 ? 4  
HELX_P HELX_P20 20 ARG A 453  ? GLN A 469  ? ARG A 453  GLN A 469  1 ? 17 
HELX_P HELX_P21 21 LYS A 479  ? LEU A 509  ? LYS A 479  LEU A 509  1 ? 31 
HELX_P HELX_P22 22 PRO A 823  ? TYR A 828  ? PRO A 823  TYR A 828  5 ? 6  
HELX_P HELX_P23 23 THR A 915  ? ASP A 927  ? THR A 915  ASP A 927  1 ? 13 
HELX_P HELX_P24 24 ASP A 998  ? LEU A 1002 ? ASP A 998  LEU A 1002 5 ? 5  
HELX_P HELX_P25 25 ASP A 1024 ? VAL A 1027 ? ASP A 1024 VAL A 1027 5 ? 4  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1 disulf ? ? A CYS 31   SG  ? ? ? 1_555 A CYS 1032 SG ? ? A CYS 31   A CYS 1032 1_555 ? ? ? ? ? ? ? 2.048 ? 
disulf2 disulf ? ? A CYS 275  SG  ? ? ? 1_555 A CYS 282  SG ? ? A CYS 275  A CYS 282  1_555 ? ? ? ? ? ? ? 2.036 ? 
disulf3 disulf ? ? A CYS 283  SG  ? ? ? 1_555 A CYS 297  SG ? ? A CYS 283  A CYS 297  1_555 ? ? ? ? ? ? ? 2.088 ? 
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 ? ? ? ? ? ? ? 2.008 ? 
covale1 covale ? ? A ASN 194  ND2 ? ? ? 1_555 B NAG .    C1 ? ? A ASN 194  A NAG 1802 1_555 ? ? ? ? ? ? ? 1.446 ? 
metalc1 metalc ? ? A HIS 90   NE2 ? ? ? 1_555 D ZN  .    ZN ? ? A HIS 90   A ZN  1805 1_555 ? ? ? ? ? ? ? 2.107 ? 
metalc2 metalc ? ? A ASP 92   OD1 ? ? ? 1_555 D ZN  .    ZN ? ? A ASP 92   A ZN  1805 1_555 ? ? ? ? ? ? ? 2.156 ? 
metalc3 metalc ? ? A ASP 204  OD2 ? ? ? 1_555 D ZN  .    ZN ? ? A ASP 204  A ZN  1805 1_555 ? ? ? ? ? ? ? 2.079 ? 
metalc4 metalc ? ? A HIS 471  NE2 ? ? ? 1_555 D ZN  .    ZN ? ? A HIS 471  A ZN  1805 1_555 ? ? ? ? ? ? ? 2.091 ? 
metalc5 metalc ? ? D ZN  .    ZN  ? ? ? 1_555 E GB2 .    O3 ? ? A ZN  1805 A GB2 1804 1_555 ? ? ? ? ? ? ? 2.199 ? 
metalc6 metalc ? ? D ZN  .    ZN  ? ? ? 1_555 E GB2 .    O4 ? ? A ZN  1805 A GB2 1804 1_555 ? ? ? ? ? ? ? 2.349 ? 
# 
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 -1.27 
2 TRP 531 A . ? TRP 531 A PRO 532 A ? PRO 532 A 1 0.21  
# 
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  ? ASP A 341  ? VAL A 333  ASP A 341  
B 2  LEU A 81   ? HIS A 90   ? LEU A 81   HIS A 90   
B 3  VAL A 372  ? PHE A 376  ? VAL A 372  PHE A 376  
C 1  PHE A 126  ? TRP A 128  ? PHE A 126  TRP A 128  
C 2  LEU A 158  ? PHE A 160  ? LEU A 158  PHE A 160  
D 1  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  VAL A 706  ? TYR A 715  ? VAL A 706  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  VAL A 706  ? TYR A 715  ? VAL A 706  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 ASN A 223  ? O ASN A 223  N SER A 200  ? N SER A 200  
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 PHE A 571  ? N PHE A 571  O ILE A 618  ? O ILE A 618  
G 3  4  O ARG A 617  ? O ARG A 617  N SER A 593  ? N SER A 593  
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 MET A 865  ? O MET A 865  N GLY A 853  ? N GLY A 853  
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 LEU A 979  ? N LEU A 979  O ALA A 1037 ? O ALA A 1037 
K 3  4  O SER A 1042 ? O SER A 1042 N ALA A 1007 ? N ALA A 1007 
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 ? ? ? ? 1  'BINDING SITE FOR RESIDUE NAG A 1802' 
AC2 Software ? ? ? ? 9  'BINDING SITE FOR RESIDUE PO4 A 1803' 
AC3 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE ZN A 1805'  
AC4 Software ? ? ? ? 16 'BINDING SITE FOR RESIDUE GB2 A 1804' 
AC5 Software ? ? ? ? 8  'BINDING SITE FOR RESIDUE MPD A 1801' 
# 
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 1  ASN A 194 ? ASN A 194  . ? 1_555 ? 
2  AC2 9  ARG A 770 ? ARG A 770  . ? 1_555 ? 
3  AC2 9  ARG A 893 ? ARG A 893  . ? 1_555 ? 
4  AC2 9  SER A 924 ? SER A 924  . ? 1_555 ? 
5  AC2 9  HOH G .   ? HOH A 2619 . ? 1_555 ? 
6  AC2 9  HOH G .   ? HOH A 2620 . ? 1_555 ? 
7  AC2 9  HOH G .   ? HOH A 2694 . ? 1_555 ? 
8  AC2 9  HOH G .   ? HOH A 2696 . ? 1_555 ? 
9  AC2 9  HOH G .   ? HOH A 2697 . ? 1_555 ? 
10 AC2 9  HOH G .   ? HOH A 2699 . ? 1_555 ? 
11 AC3 5  HIS A 90  ? HIS A 90   . ? 1_555 ? 
12 AC3 5  ASP A 92  ? ASP A 92   . ? 1_555 ? 
13 AC3 5  ASP A 204 ? ASP A 204  . ? 1_555 ? 
14 AC3 5  HIS A 471 ? HIS A 471  . ? 1_555 ? 
15 AC3 5  GB2 E .   ? GB2 A 1804 . ? 1_555 ? 
16 AC4 16 HIS A 90  ? HIS A 90   . ? 1_555 ? 
17 AC4 16 ASP A 92  ? ASP A 92   . ? 1_555 ? 
18 AC4 16 TRP A 95  ? TRP A 95   . ? 1_555 ? 
19 AC4 16 ASP A 204 ? ASP A 204  . ? 1_555 ? 
20 AC4 16 TYR A 269 ? TYR A 269  . ? 1_555 ? 
21 AC4 16 ASP A 341 ? ASP A 341  . ? 1_555 ? 
22 AC4 16 HIS A 471 ? HIS A 471  . ? 1_555 ? 
23 AC4 16 ASP A 472 ? ASP A 472  . ? 1_555 ? 
24 AC4 16 TYR A 727 ? TYR A 727  . ? 1_555 ? 
25 AC4 16 GLY A 877 ? GLY A 877  . ? 1_555 ? 
26 AC4 16 ZN  D .   ? ZN  A 1805 . ? 1_555 ? 
27 AC4 16 HOH G .   ? HOH A 2309 . ? 1_555 ? 
28 AC4 16 HOH G .   ? HOH A 2329 . ? 1_555 ? 
29 AC4 16 HOH G .   ? HOH A 2333 . ? 1_555 ? 
30 AC4 16 HOH G .   ? HOH A 2460 . ? 1_555 ? 
31 AC4 16 HOH G .   ? HOH A 2904 . ? 1_555 ? 
32 AC5 8  LYS A 63  ? LYS A 63   . ? 1_555 ? 
33 AC5 8  GLN A 64  ? GLN A 64   . ? 1_555 ? 
34 AC5 8  TYR A 267 ? TYR A 267  . ? 1_555 ? 
35 AC5 8  HIS A 273 ? HIS A 273  . ? 1_555 ? 
36 AC5 8  HOH G .   ? HOH A 2470 . ? 1_555 ? 
37 AC5 8  HOH G .   ? HOH A 2525 . ? 1_555 ? 
38 AC5 8  HOH G .   ? HOH A 2534 . ? 1_555 ? 
39 AC5 8  HOH G .   ? HOH A 2827 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          2F1A 
_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                    2F1A 
_atom_sites.fract_transf_matrix[1][1]   0.014513 
_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]   0.009144 
_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]   0.007216 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
P  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . CYS A 1 31   ? 44.160 35.768  -18.733 1.00 30.26 ? 31   CYS A N   1 
ATOM   2    C  CA  . CYS A 1 31   ? 43.410 37.034  -18.442 1.00 28.48 ? 31   CYS A CA  1 
ATOM   3    C  C   . CYS A 1 31   ? 41.902 36.842  -18.533 1.00 26.70 ? 31   CYS A C   1 
ATOM   4    O  O   . CYS A 1 31   ? 41.409 36.282  -19.517 1.00 26.39 ? 31   CYS A O   1 
ATOM   5    C  CB  . CYS A 1 31   ? 43.776 38.151  -19.433 1.00 27.77 ? 31   CYS A CB  1 
ATOM   6    S  SG  . CYS A 1 31   ? 45.448 38.873  -19.368 1.00 29.75 ? 31   CYS A SG  1 
ATOM   7    N  N   . GLN A 1 32   ? 41.169 37.327  -17.532 1.00 25.13 ? 32   GLN A N   1 
ATOM   8    C  CA  . GLN A 1 32   ? 39.716 37.264  -17.536 1.00 25.50 ? 32   GLN A CA  1 
ATOM   9    C  C   . GLN A 1 32   ? 39.217 38.206  -18.643 1.00 22.48 ? 32   GLN A C   1 
ATOM   10   O  O   . GLN A 1 32   ? 39.825 39.256  -18.940 1.00 21.44 ? 32   GLN A O   1 
ATOM   11   C  CB  . GLN A 1 32   ? 39.105 37.800  -16.230 1.00 27.03 ? 32   GLN A CB  1 
ATOM   12   C  CG  . GLN A 1 32   ? 39.275 36.985  -14.972 1.00 30.20 ? 32   GLN A CG  1 
ATOM   13   C  CD  . GLN A 1 32   ? 38.180 37.333  -13.941 1.00 31.53 ? 32   GLN A CD  1 
ATOM   14   O  OE1 . GLN A 1 32   ? 37.058 36.819  -14.007 1.00 33.18 ? 32   GLN A OE1 1 
ATOM   15   N  NE2 . GLN A 1 32   ? 38.500 38.226  -13.005 1.00 30.40 ? 32   GLN A NE2 1 
ATOM   16   N  N   . ASP A 1 33   ? 38.103 37.833  -19.248 1.00 22.83 ? 33   ASP A N   1 
ATOM   17   C  CA  . ASP A 1 33   ? 37.484 38.651  -20.281 1.00 19.40 ? 33   ASP A CA  1 
ATOM   18   C  C   . ASP A 1 33   ? 36.544 39.621  -19.528 1.00 22.20 ? 33   ASP A C   1 
ATOM   19   O  O   . ASP A 1 33   ? 35.575 39.214  -18.870 1.00 24.50 ? 33   ASP A O   1 
ATOM   20   C  CB  . ASP A 1 33   ? 36.724 37.705  -21.233 1.00 21.71 ? 33   ASP A CB  1 
ATOM   21   C  CG  . ASP A 1 33   ? 36.007 38.427  -22.366 1.00 27.05 ? 33   ASP A CG  1 
ATOM   22   O  OD1 . ASP A 1 33   ? 35.548 39.577  -22.211 1.00 24.97 ? 33   ASP A OD1 1 
ATOM   23   O  OD2 . ASP A 1 33   ? 35.850 37.789  -23.431 1.00 27.92 ? 33   ASP A OD2 1 
ATOM   24   N  N   . VAL A 1 34   ? 36.821 40.914  -19.632 1.00 16.22 ? 34   VAL A N   1 
ATOM   25   C  CA  . VAL A 1 34   ? 36.030 41.878  -18.894 1.00 15.52 ? 34   VAL A CA  1 
ATOM   26   C  C   . VAL A 1 34   ? 34.848 42.444  -19.662 1.00 14.83 ? 34   VAL A C   1 
ATOM   27   O  O   . VAL A 1 34   ? 34.116 43.292  -19.175 1.00 16.35 ? 34   VAL A O   1 
ATOM   28   C  CB  . VAL A 1 34   ? 36.921 43.049  -18.409 1.00 15.29 ? 34   VAL A CB  1 
ATOM   29   C  CG1 . VAL A 1 34   ? 38.151 42.489  -17.671 1.00 17.50 ? 34   VAL A CG1 1 
ATOM   30   C  CG2 . VAL A 1 34   ? 37.432 43.901  -19.595 1.00 15.81 ? 34   VAL A CG2 1 
ATOM   31   N  N   . VAL A 1 35   ? 34.614 41.892  -20.849 1.00 15.65 ? 35   VAL A N   1 
ATOM   32   C  CA  . VAL A 1 35   ? 33.505 42.371  -21.675 1.00 15.70 ? 35   VAL A CA  1 
ATOM   33   C  C   . VAL A 1 35   ? 32.318 41.396  -21.902 1.00 15.48 ? 35   VAL A C   1 
ATOM   34   O  O   . VAL A 1 35   ? 31.153 41.769  -21.817 1.00 16.27 ? 35   VAL A O   1 
ATOM   35   C  CB  . VAL A 1 35   ? 34.023 42.723  -23.075 1.00 15.70 ? 35   VAL A CB  1 
ATOM   36   C  CG1 . VAL A 1 35   ? 32.840 43.104  -23.995 1.00 16.46 ? 35   VAL A CG1 1 
ATOM   37   C  CG2 . VAL A 1 35   ? 35.109 43.864  -22.993 1.00 15.87 ? 35   VAL A CG2 1 
ATOM   38   N  N   . GLN A 1 36   ? 32.652 40.143  -22.171 1.00 17.12 ? 36   GLN A N   1 
ATOM   39   C  CA  . GLN A 1 36   ? 31.687 39.131  -22.589 1.00 19.23 ? 36   GLN A CA  1 
ATOM   40   C  C   . GLN A 1 36   ? 31.073 38.217  -21.564 1.00 22.28 ? 36   GLN A C   1 
ATOM   41   O  O   . GLN A 1 36   ? 30.157 37.494  -21.889 1.00 27.10 ? 36   GLN A O   1 
ATOM   42   C  CB  . GLN A 1 36   ? 32.363 38.297  -23.679 1.00 18.78 ? 36   GLN A CB  1 
ATOM   43   C  CG  . GLN A 1 36   ? 32.991 39.160  -24.748 1.00 21.40 ? 36   GLN A CG  1 
ATOM   44   C  CD  . GLN A 1 36   ? 33.448 38.371  -25.933 1.00 23.82 ? 36   GLN A CD  1 
ATOM   45   O  OE1 . GLN A 1 36   ? 32.686 38.169  -26.866 1.00 25.10 ? 36   GLN A OE1 1 
ATOM   46   N  NE2 . GLN A 1 36   ? 34.685 37.906  -25.903 1.00 22.35 ? 36   GLN A NE2 1 
ATOM   47   N  N   . ASP A 1 37   ? 31.559 38.249  -20.334 1.00 23.06 ? 37   ASP A N   1 
ATOM   48   C  CA  . ASP A 1 37   ? 31.045 37.389  -19.287 1.00 24.80 ? 37   ASP A CA  1 
ATOM   49   C  C   . ASP A 1 37   ? 30.349 38.206  -18.177 1.00 22.28 ? 37   ASP A C   1 
ATOM   50   O  O   . ASP A 1 37   ? 31.026 38.809  -17.340 1.00 25.13 ? 37   ASP A O   1 
ATOM   51   C  CB  . ASP A 1 37   ? 32.215 36.584  -18.672 1.00 27.44 ? 37   ASP A CB  1 
ATOM   52   C  CG  . ASP A 1 37   ? 32.873 35.604  -19.667 1.00 30.15 ? 37   ASP A CG  1 
ATOM   53   O  OD1 . ASP A 1 37   ? 32.132 34.961  -20.427 1.00 32.56 ? 37   ASP A OD1 1 
ATOM   54   O  OD2 . ASP A 1 37   ? 34.122 35.472  -19.677 1.00 30.70 ? 37   ASP A OD2 1 
ATOM   55   N  N   . VAL A 1 38   ? 29.031 38.210  -18.151 1.00 21.22 ? 38   VAL A N   1 
ATOM   56   C  CA  . VAL A 1 38   ? 28.318 38.957  -17.104 1.00 19.55 ? 38   VAL A CA  1 
ATOM   57   C  C   . VAL A 1 38   ? 28.497 38.245  -15.760 1.00 21.11 ? 38   VAL A C   1 
ATOM   58   O  O   . VAL A 1 38   ? 28.071 37.102  -15.609 1.00 20.64 ? 38   VAL A O   1 
ATOM   59   C  CB  . VAL A 1 38   ? 26.818 39.055  -17.403 1.00 20.53 ? 38   VAL A CB  1 
ATOM   60   C  CG1 . VAL A 1 38   ? 26.085 39.802  -16.261 1.00 18.68 ? 38   VAL A CG1 1 
ATOM   61   C  CG2 . VAL A 1 38   ? 26.604 39.759  -18.781 1.00 20.20 ? 38   VAL A CG2 1 
ATOM   62   N  N   . PRO A 1 39   ? 29.109 38.905  -14.762 1.00 19.12 ? 39   PRO A N   1 
ATOM   63   C  CA  . PRO A 1 39   ? 29.282 38.213  -13.478 1.00 16.77 ? 39   PRO A CA  1 
ATOM   64   C  C   . PRO A 1 39   ? 27.981 37.863  -12.807 1.00 17.79 ? 39   PRO A C   1 
ATOM   65   O  O   . PRO A 1 39   ? 26.999 38.595  -12.867 1.00 17.37 ? 39   PRO A O   1 
ATOM   66   C  CB  . PRO A 1 39   ? 30.060 39.219  -12.630 1.00 18.15 ? 39   PRO A CB  1 
ATOM   67   C  CG  . PRO A 1 39   ? 30.883 40.011  -13.668 1.00 16.98 ? 39   PRO A CG  1 
ATOM   68   C  CD  . PRO A 1 39   ? 29.813 40.209  -14.771 1.00 17.90 ? 39   PRO A CD  1 
ATOM   69   N  N   . ASN A 1 40   ? 27.995 36.712  -12.131 1.00 18.15 ? 40   ASN A N   1 
ATOM   70   C  CA  . ASN A 1 40   ? 26.826 36.297  -11.398 1.00 19.87 ? 40   ASN A CA  1 
ATOM   71   C  C   . ASN A 1 40   ? 27.090 36.675  -9.936  1.00 17.61 ? 40   ASN A C   1 
ATOM   72   O  O   . ASN A 1 40   ? 27.990 36.120  -9.279  1.00 18.86 ? 40   ASN A O   1 
ATOM   73   C  CB  . ASN A 1 40   ? 26.629 34.789  -11.593 1.00 24.70 ? 40   ASN A CB  1 
ATOM   74   C  CG  . ASN A 1 40   ? 25.547 34.220  -10.719 1.00 28.58 ? 40   ASN A CG  1 
ATOM   75   O  OD1 . ASN A 1 40   ? 24.500 34.842  -10.486 1.00 33.86 ? 40   ASN A OD1 1 
ATOM   76   N  ND2 . ASN A 1 40   ? 25.786 33.009  -10.224 1.00 35.00 ? 40   ASN A ND2 1 
ATOM   77   N  N   . VAL A 1 41   ? 26.324 37.643  -9.448  1.00 16.61 ? 41   VAL A N   1 
ATOM   78   C  CA  . VAL A 1 41   ? 26.475 38.106  -8.060  1.00 15.10 ? 41   VAL A CA  1 
ATOM   79   C  C   . VAL A 1 41   ? 25.124 38.100  -7.386  1.00 16.58 ? 41   VAL A C   1 
ATOM   80   O  O   . VAL A 1 41   ? 24.069 38.211  -8.016  1.00 19.01 ? 41   VAL A O   1 
ATOM   81   C  CB  . VAL A 1 41   ? 27.093 39.565  -7.985  1.00 15.17 ? 41   VAL A CB  1 
ATOM   82   C  CG1 . VAL A 1 41   ? 28.543 39.555  -8.441  1.00 16.56 ? 41   VAL A CG1 1 
ATOM   83   C  CG2 . VAL A 1 41   ? 26.252 40.536  -8.826  1.00 15.77 ? 41   VAL A CG2 1 
ATOM   84   N  N   . ASP A 1 42   ? 25.135 38.014  -6.062  1.00 15.18 ? 42   ASP A N   1 
ATOM   85   C  CA  . ASP A 1 42   ? 23.880 38.029  -5.336  1.00 14.78 ? 42   ASP A CA  1 
ATOM   86   C  C   . ASP A 1 42   ? 23.174 39.389  -5.335  1.00 15.59 ? 42   ASP A C   1 
ATOM   87   O  O   . ASP A 1 42   ? 21.937 39.478  -5.345  1.00 17.55 ? 42   ASP A O   1 
ATOM   88   C  CB  . ASP A 1 42   ? 24.106 37.584  -3.877  1.00 17.23 ? 42   ASP A CB  1 
ATOM   89   C  CG  . ASP A 1 42   ? 24.651 36.177  -3.784  1.00 21.92 ? 42   ASP A CG  1 
ATOM   90   O  OD1 . ASP A 1 42   ? 24.046 35.264  -4.412  1.00 21.74 ? 42   ASP A OD1 1 
ATOM   91   O  OD2 . ASP A 1 42   ? 25.675 35.953  -3.108  1.00 17.93 ? 42   ASP A OD2 1 
ATOM   92   N  N   . VAL A 1 43   ? 23.963 40.463  -5.276  1.00 14.95 ? 43   VAL A N   1 
ATOM   93   C  CA  . VAL A 1 43   ? 23.435 41.819  -5.272  1.00 15.20 ? 43   VAL A CA  1 
ATOM   94   C  C   . VAL A 1 43   ? 24.206 42.591  -6.357  1.00 13.56 ? 43   VAL A C   1 
ATOM   95   O  O   . VAL A 1 43   ? 25.439 42.662  -6.309  1.00 15.12 ? 43   VAL A O   1 
ATOM   96   C  CB  . VAL A 1 43   ? 23.664 42.539  -3.923  1.00 15.27 ? 43   VAL A CB  1 
ATOM   97   C  CG1 . VAL A 1 43   ? 23.081 43.954  -3.992  1.00 15.22 ? 43   VAL A CG1 1 
ATOM   98   C  CG2 . VAL A 1 43   ? 22.967 41.754  -2.772  1.00 16.51 ? 43   VAL A CG2 1 
ATOM   99   N  N   . GLN A 1 44   ? 23.477 43.124  -7.342  1.00 13.69 ? 44   GLN A N   1 
ATOM   100  C  CA  . GLN A 1 44   ? 24.129 43.927  -8.383  1.00 14.52 ? 44   GLN A CA  1 
ATOM   101  C  C   . GLN A 1 44   ? 23.404 45.255  -8.223  1.00 14.47 ? 44   GLN A C   1 
ATOM   102  O  O   . GLN A 1 44   ? 22.207 45.344  -8.384  1.00 14.74 ? 44   GLN A O   1 
ATOM   103  C  CB  . GLN A 1 44   ? 23.925 43.282  -9.746  1.00 15.82 ? 44   GLN A CB  1 
ATOM   104  C  CG  . GLN A 1 44   ? 24.993 43.695  -10.749 1.00 13.87 ? 44   GLN A CG  1 
ATOM   105  C  CD  . GLN A 1 44   ? 25.057 45.216  -10.906 1.00 14.22 ? 44   GLN A CD  1 
ATOM   106  O  OE1 . GLN A 1 44   ? 24.061 45.846  -11.250 1.00 16.25 ? 44   GLN A OE1 1 
ATOM   107  N  NE2 . GLN A 1 44   ? 26.226 45.811  -10.617 1.00 13.07 ? 44   GLN A NE2 1 
ATOM   108  N  N   . MET A 1 45   ? 24.140 46.301  -7.840  1.00 13.03 ? 45   MET A N   1 
ATOM   109  C  CA  . MET A 1 45   ? 23.462 47.532  -7.492  1.00 12.91 ? 45   MET A CA  1 
ATOM   110  C  C   . MET A 1 45   ? 22.552 48.197  -8.532  1.00 12.91 ? 45   MET A C   1 
ATOM   111  O  O   . MET A 1 45   ? 21.550 48.818  -8.150  1.00 13.13 ? 45   MET A O   1 
ATOM   112  C  CB  . MET A 1 45   ? 24.464 48.519  -6.912  1.00 13.76 ? 45   MET A CB  1 
ATOM   113  C  CG  . MET A 1 45   ? 25.076 48.067  -5.577  1.00 12.66 ? 45   MET A CG  1 
ATOM   114  S  SD  . MET A 1 45   ? 23.863 47.785  -4.277  1.00 16.01 ? 45   MET A SD  1 
ATOM   115  C  CE  . MET A 1 45   ? 23.236 49.512  -4.104  1.00 17.27 ? 45   MET A CE  1 
ATOM   116  N  N   . LEU A 1 46   ? 22.910 48.076  -9.806  1.00 13.01 ? 46   LEU A N   1 
ATOM   117  C  CA  . LEU A 1 46   ? 22.043 48.674  -10.830 1.00 13.65 ? 46   LEU A CA  1 
ATOM   118  C  C   . LEU A 1 46   ? 20.707 47.885  -10.861 1.00 15.48 ? 46   LEU A C   1 
ATOM   119  O  O   . LEU A 1 46   ? 19.638 48.477  -10.968 1.00 14.22 ? 46   LEU A O   1 
ATOM   120  C  CB  . LEU A 1 46   ? 22.715 48.636  -12.179 1.00 15.06 ? 46   LEU A CB  1 
ATOM   121  C  CG  . LEU A 1 46   ? 21.886 49.369  -13.247 1.00 14.26 ? 46   LEU A CG  1 
ATOM   122  C  CD1 . LEU A 1 46   ? 21.905 50.885  -13.025 1.00 15.71 ? 46   LEU A CD1 1 
ATOM   123  C  CD2 . LEU A 1 46   ? 22.469 49.003  -14.566 1.00 16.24 ? 46   LEU A CD2 1 
ATOM   124  N  N   . GLU A 1 47   ? 20.799 46.565  -10.729 1.00 15.63 ? 47   GLU A N   1 
ATOM   125  C  CA  . GLU A 1 47   ? 19.594 45.732  -10.720 1.00 16.30 ? 47   GLU A CA  1 
ATOM   126  C  C   . GLU A 1 47   ? 18.774 46.038  -9.477  1.00 17.75 ? 47   GLU A C   1 
ATOM   127  O  O   . GLU A 1 47   ? 17.555 46.203  -9.532  1.00 18.11 ? 47   GLU A O   1 
ATOM   128  C  CB  . GLU A 1 47   ? 19.998 44.250  -10.770 1.00 17.06 ? 47   GLU A CB  1 
ATOM   129  C  CG  . GLU A 1 47   ? 18.822 43.284  -11.006 1.00 20.56 ? 47   GLU A CG  1 
ATOM   130  C  CD  . GLU A 1 47   ? 18.032 42.961  -9.775  1.00 24.27 ? 47   GLU A CD  1 
ATOM   131  O  OE1 . GLU A 1 47   ? 18.539 43.099  -8.638  1.00 24.47 ? 47   GLU A OE1 1 
ATOM   132  O  OE2 . GLU A 1 47   ? 16.868 42.530  -9.930  1.00 29.40 ? 47   GLU A OE2 1 
ATOM   133  N  N   . LEU A 1 48   ? 19.448 46.184  -8.337  1.00 14.23 ? 48   LEU A N   1 
ATOM   134  C  CA  . LEU A 1 48   ? 18.757 46.491  -7.106  1.00 16.38 ? 48   LEU A CA  1 
ATOM   135  C  C   . LEU A 1 48   ? 18.024 47.807  -7.256  1.00 16.28 ? 48   LEU A C   1 
ATOM   136  O  O   . LEU A 1 48   ? 16.869 47.956  -6.880  1.00 18.38 ? 48   LEU A O   1 
ATOM   137  C  CB  . LEU A 1 48   ? 19.749 46.556  -5.929  1.00 17.62 ? 48   LEU A CB  1 
ATOM   138  C  CG  . LEU A 1 48   ? 19.054 46.690  -4.587  1.00 17.71 ? 48   LEU A CG  1 
ATOM   139  C  CD1 . LEU A 1 48   ? 18.127 45.495  -4.372  1.00 26.27 ? 48   LEU A CD1 1 
ATOM   140  C  CD2 . LEU A 1 48   ? 20.090 46.714  -3.439  1.00 21.67 ? 48   LEU A CD2 1 
ATOM   141  N  N   . TYR A 1 49   ? 18.702 48.813  -7.792  1.00 15.44 ? 49   TYR A N   1 
ATOM   142  C  CA  . TYR A 1 49   ? 18.036 50.080  -7.999  1.00 16.24 ? 49   TYR A CA  1 
ATOM   143  C  C   . TYR A 1 49   ? 16.801 50.007  -8.919  1.00 15.91 ? 49   TYR A C   1 
ATOM   144  O  O   . TYR A 1 49   ? 15.834 50.729  -8.712  1.00 17.04 ? 49   TYR A O   1 
ATOM   145  C  CB  . TYR A 1 49   ? 19.059 51.071  -8.590  1.00 14.73 ? 49   TYR A CB  1 
ATOM   146  C  CG  . TYR A 1 49   ? 19.633 52.012  -7.561  1.00 14.31 ? 49   TYR A CG  1 
ATOM   147  C  CD1 . TYR A 1 49   ? 20.109 51.532  -6.346  1.00 14.76 ? 49   TYR A CD1 1 
ATOM   148  C  CD2 . TYR A 1 49   ? 19.640 53.385  -7.779  1.00 13.75 ? 49   TYR A CD2 1 
ATOM   149  C  CE1 . TYR A 1 49   ? 20.559 52.382  -5.383  1.00 14.14 ? 49   TYR A CE1 1 
ATOM   150  C  CE2 . TYR A 1 49   ? 20.082 54.269  -6.808  1.00 14.71 ? 49   TYR A CE2 1 
ATOM   151  C  CZ  . TYR A 1 49   ? 20.532 53.752  -5.601  1.00 14.24 ? 49   TYR A CZ  1 
ATOM   152  O  OH  . TYR A 1 49   ? 20.887 54.593  -4.591  1.00 15.50 ? 49   TYR A OH  1 
ATOM   153  N  N   . ASP A 1 50   ? 16.848 49.151  -9.927  1.00 16.11 ? 50   ASP A N   1 
ATOM   154  C  CA  . ASP A 1 50   ? 15.718 49.087  -10.837 1.00 18.61 ? 50   ASP A CA  1 
ATOM   155  C  C   . ASP A 1 50   ? 14.471 48.533  -10.130 1.00 19.45 ? 50   ASP A C   1 
ATOM   156  O  O   . ASP A 1 50   ? 13.339 48.942  -10.486 1.00 20.23 ? 50   ASP A O   1 
ATOM   157  C  CB  . ASP A 1 50   ? 16.116 48.219  -12.007 1.00 18.65 ? 50   ASP A CB  1 
ATOM   158  C  CG  . ASP A 1 50   ? 15.262 48.419  -13.217 1.00 24.33 ? 50   ASP A CG  1 
ATOM   159  O  OD1 . ASP A 1 50   ? 14.557 49.436  -13.313 1.00 27.84 ? 50   ASP A OD1 1 
ATOM   160  O  OD2 . ASP A 1 50   ? 15.361 47.538  -14.101 1.00 30.03 ? 50   ASP A OD2 1 
ATOM   161  N  N   . ARG A 1 51   ? 14.692 47.630  -9.173  1.00 19.50 ? 51   ARG A N   1 
ATOM   162  C  CA  . ARG A 1 51   ? 13.622 46.952  -8.401  1.00 21.23 ? 51   ARG A CA  1 
ATOM   163  C  C   . ARG A 1 51   ? 13.105 47.691  -7.183  1.00 21.46 ? 51   ARG A C   1 
ATOM   164  O  O   . ARG A 1 51   ? 11.928 47.587  -6.856  1.00 24.23 ? 51   ARG A O   1 
ATOM   165  C  CB  . ARG A 1 51   ? 14.106 45.586  -7.866  1.00 24.83 ? 51   ARG A CB  1 
ATOM   166  C  CG  . ARG A 1 51   ? 14.377 44.508  -8.857  1.00 32.74 ? 51   ARG A CG  1 
ATOM   167  C  CD  . ARG A 1 51   ? 15.323 43.447  -8.230  1.00 37.40 ? 51   ARG A CD  1 
ATOM   168  N  NE  . ARG A 1 51   ? 15.105 43.264  -6.805  1.00 39.10 ? 51   ARG A NE  1 
ATOM   169  C  CZ  . ARG A 1 51   ? 16.057 42.958  -5.927  1.00 40.27 ? 51   ARG A CZ  1 
ATOM   170  N  NH1 . ARG A 1 51   ? 17.318 42.781  -6.317  1.00 39.57 ? 51   ARG A NH1 1 
ATOM   171  N  NH2 . ARG A 1 51   ? 15.743 42.875  -4.640  1.00 41.19 ? 51   ARG A NH2 1 
ATOM   172  N  N   . MET A 1 52   ? 13.989 48.418  -6.500  1.00 20.56 ? 52   MET A N   1 
ATOM   173  C  CA  . MET A 1 52   ? 13.628 49.149  -5.287  1.00 21.25 ? 52   MET A CA  1 
ATOM   174  C  C   . MET A 1 52   ? 12.590 50.230  -5.463  1.00 20.53 ? 52   MET A C   1 
ATOM   175  O  O   . MET A 1 52   ? 12.570 50.919  -6.473  1.00 20.57 ? 52   MET A O   1 
ATOM   176  C  CB  . MET A 1 52   ? 14.871 49.806  -4.683  1.00 20.78 ? 52   MET A CB  1 
ATOM   177  C  CG  A MET A 1 52   ? 15.878 48.842  -4.127  0.50 21.39 ? 52   MET A CG  1 
ATOM   178  C  CG  B MET A 1 52   ? 15.613 48.726  -3.748  0.50 22.42 ? 52   MET A CG  1 
ATOM   179  S  SD  A MET A 1 52   ? 17.457 49.713  -3.698  0.50 21.09 ? 52   MET A SD  1 
ATOM   180  S  SD  B MET A 1 52   ? 17.208 49.465  -3.231  0.50 24.89 ? 52   MET A SD  1 
ATOM   181  C  CE  A MET A 1 52   ? 16.921 51.009  -2.537  0.50 18.64 ? 52   MET A CE  1 
ATOM   182  C  CE  B MET A 1 52   ? 16.708 50.960  -2.407  0.50 24.05 ? 52   MET A CE  1 
ATOM   183  N  N   . SER A 1 53   ? 11.746 50.402  -4.446  1.00 19.88 ? 53   SER A N   1 
ATOM   184  C  CA  . SER A 1 53   ? 10.698 51.425  -4.472  1.00 21.65 ? 53   SER A CA  1 
ATOM   185  C  C   . SER A 1 53   ? 11.138 52.773  -3.891  1.00 20.10 ? 53   SER A C   1 
ATOM   186  O  O   . SER A 1 53   ? 10.530 53.809  -4.160  1.00 21.28 ? 53   SER A O   1 
ATOM   187  C  CB  A SER A 1 53   ? 9.470  50.924  -3.696  0.50 21.98 ? 53   SER A CB  1 
ATOM   188  C  CB  B SER A 1 53   ? 9.343  51.059  -3.964  0.50 21.56 ? 53   SER A CB  1 
ATOM   189  O  OG  A SER A 1 53   ? 8.929  49.793  -4.345  0.50 26.32 ? 53   SER A OG  1 
ATOM   190  O  OG  B SER A 1 53   ? 9.443  50.803  -2.578  0.50 22.79 ? 53   SER A OG  1 
ATOM   191  N  N   . PHE A 1 54   ? 12.171 52.752  -3.064  1.00 19.40 ? 54   PHE A N   1 
ATOM   192  C  CA  . PHE A 1 54   ? 12.684 53.964  -2.436  1.00 17.54 ? 54   PHE A CA  1 
ATOM   193  C  C   . PHE A 1 54   ? 11.653 54.773  -1.626  1.00 19.25 ? 54   PHE A C   1 
ATOM   194  O  O   . PHE A 1 54   ? 11.752 56.010  -1.484  1.00 19.76 ? 54   PHE A O   1 
ATOM   195  C  CB  . PHE A 1 54   ? 13.343 54.891  -3.480  1.00 18.96 ? 54   PHE A CB  1 
ATOM   196  C  CG  . PHE A 1 54   ? 14.615 54.340  -4.084  1.00 15.71 ? 54   PHE A CG  1 
ATOM   197  C  CD1 . PHE A 1 54   ? 14.561 53.509  -5.182  1.00 17.99 ? 54   PHE A CD1 1 
ATOM   198  C  CD2 . PHE A 1 54   ? 15.860 54.695  -3.567  1.00 17.52 ? 54   PHE A CD2 1 
ATOM   199  C  CE1 . PHE A 1 54   ? 15.734 53.020  -5.781  1.00 16.87 ? 54   PHE A CE1 1 
ATOM   200  C  CE2 . PHE A 1 54   ? 17.032 54.235  -4.146  1.00 17.81 ? 54   PHE A CE2 1 
ATOM   201  C  CZ  . PHE A 1 54   ? 16.988 53.390  -5.257  1.00 18.01 ? 54   PHE A CZ  1 
ATOM   202  N  N   . LYS A 1 55   ? 10.665 54.081  -1.053  1.00 20.47 ? 55   LYS A N   1 
ATOM   203  C  CA  . LYS A 1 55   ? 9.681  54.817  -0.247  1.00 21.47 ? 55   LYS A CA  1 
ATOM   204  C  C   . LYS A 1 55   ? 10.287 55.263  1.047   1.00 21.81 ? 55   LYS A C   1 
ATOM   205  O  O   . LYS A 1 55   ? 10.999 54.515  1.694   1.00 22.44 ? 55   LYS A O   1 
ATOM   206  C  CB  . LYS A 1 55   ? 8.448  53.957  0.084   1.00 21.61 ? 55   LYS A CB  1 
ATOM   207  C  CG  . LYS A 1 55   ? 7.692  53.492  -1.131  1.00 22.92 ? 55   LYS A CG  1 
ATOM   208  C  CD  . LYS A 1 55   ? 7.454  54.621  -2.142  1.00 23.36 ? 55   LYS A CD  1 
ATOM   209  C  CE  . LYS A 1 55   ? 6.683  54.100  -3.362  1.00 25.88 ? 55   LYS A CE  1 
ATOM   210  N  NZ  . LYS A 1 55   ? 6.270  55.230  -4.285  1.00 27.87 ? 55   LYS A NZ  1 
ATOM   211  N  N   . ASP A 1 56   ? 9.993  56.489  1.436   1.00 21.22 ? 56   ASP A N   1 
ATOM   212  C  CA  . ASP A 1 56   ? 10.527 57.052  2.647   1.00 21.42 ? 56   ASP A CA  1 
ATOM   213  C  C   . ASP A 1 56   ? 9.475  57.069  3.760   1.00 23.00 ? 56   ASP A C   1 
ATOM   214  O  O   . ASP A 1 56   ? 8.889  58.104  4.089   1.00 25.98 ? 56   ASP A O   1 
ATOM   215  C  CB  . ASP A 1 56   ? 11.042 58.459  2.305   1.00 20.21 ? 56   ASP A CB  1 
ATOM   216  C  CG  . ASP A 1 56   ? 11.669 59.170  3.486   1.00 20.28 ? 56   ASP A CG  1 
ATOM   217  O  OD1 . ASP A 1 56   ? 12.211 58.525  4.404   1.00 20.89 ? 56   ASP A OD1 1 
ATOM   218  O  OD2 . ASP A 1 56   ? 11.626 60.418  3.464   1.00 24.19 ? 56   ASP A OD2 1 
ATOM   219  N  N   . ILE A 1 57   ? 9.272  55.915  4.368   1.00 22.60 ? 57   ILE A N   1 
ATOM   220  C  CA  . ILE A 1 57   ? 8.267  55.852  5.402   1.00 24.17 ? 57   ILE A CA  1 
ATOM   221  C  C   . ILE A 1 57   ? 8.862  55.850  6.779   1.00 23.57 ? 57   ILE A C   1 
ATOM   222  O  O   . ILE A 1 57   ? 9.999  55.431  6.996   1.00 23.69 ? 57   ILE A O   1 
ATOM   223  C  CB  . ILE A 1 57   ? 7.345  54.617  5.226   1.00 26.87 ? 57   ILE A CB  1 
ATOM   224  C  CG1 . ILE A 1 57   ? 8.132  53.342  5.415   1.00 28.37 ? 57   ILE A CG1 1 
ATOM   225  C  CG2 . ILE A 1 57   ? 6.704  54.593  3.803   1.00 26.53 ? 57   ILE A CG2 1 
ATOM   226  C  CD1 . ILE A 1 57   ? 7.240  52.185  5.803   1.00 30.30 ? 57   ILE A CD1 1 
ATOM   227  N  N   . ASP A 1 58   ? 8.064  56.315  7.732   1.00 23.14 ? 58   ASP A N   1 
ATOM   228  C  CA  . ASP A 1 58   ? 8.477  56.386  9.122   1.00 24.81 ? 58   ASP A CA  1 
ATOM   229  C  C   . ASP A 1 58   ? 8.526  54.971  9.683   1.00 24.46 ? 58   ASP A C   1 
ATOM   230  O  O   . ASP A 1 58   ? 7.490  54.341  9.861   1.00 25.20 ? 58   ASP A O   1 
ATOM   231  C  CB  . ASP A 1 58   ? 7.462  57.229  9.876   1.00 26.83 ? 58   ASP A CB  1 
ATOM   232  C  CG  . ASP A 1 58   ? 7.864  57.493  11.310  1.00 29.00 ? 58   ASP A CG  1 
ATOM   233  O  OD1 . ASP A 1 58   ? 8.719  56.772  11.850  1.00 26.46 ? 58   ASP A OD1 1 
ATOM   234  O  OD2 . ASP A 1 58   ? 7.312  58.445  11.917  1.00 34.45 ? 58   ASP A OD2 1 
ATOM   235  N  N   . GLY A 1 59   ? 9.721  54.450  9.937   1.00 22.01 ? 59   GLY A N   1 
ATOM   236  C  CA  . GLY A 1 59   ? 9.832  53.096  10.451  1.00 22.10 ? 59   GLY A CA  1 
ATOM   237  C  C   . GLY A 1 59   ? 9.763  52.985  11.967  1.00 20.49 ? 59   GLY A C   1 
ATOM   238  O  O   . GLY A 1 59   ? 9.961  51.903  12.484  1.00 22.25 ? 59   GLY A O   1 
ATOM   239  N  N   . GLY A 1 60   ? 9.522  54.098  12.664  1.00 21.87 ? 60   GLY A N   1 
ATOM   240  C  CA  . GLY A 1 60   ? 9.478  54.068  14.117  1.00 22.11 ? 60   GLY A CA  1 
ATOM   241  C  C   . GLY A 1 60   ? 10.735 54.677  14.726  1.00 20.66 ? 60   GLY A C   1 
ATOM   242  O  O   . GLY A 1 60   ? 11.287 55.644  14.183  1.00 21.03 ? 60   GLY A O   1 
ATOM   243  N  N   . VAL A 1 61   ? 11.214 54.139  15.852  1.00 20.06 ? 61   VAL A N   1 
ATOM   244  C  CA  . VAL A 1 61   ? 12.395 54.737  16.465  1.00 18.45 ? 61   VAL A CA  1 
ATOM   245  C  C   . VAL A 1 61   ? 13.575 54.651  15.445  1.00 17.48 ? 61   VAL A C   1 
ATOM   246  O  O   . VAL A 1 61   ? 14.440 55.542  15.434  1.00 17.83 ? 61   VAL A O   1 
ATOM   247  C  CB  . VAL A 1 61   ? 12.774 54.099  17.834  1.00 18.51 ? 61   VAL A CB  1 
ATOM   248  C  CG1 . VAL A 1 61   ? 11.690 54.432  18.895  1.00 20.55 ? 61   VAL A CG1 1 
ATOM   249  C  CG2 . VAL A 1 61   ? 12.949 52.589  17.699  1.00 20.18 ? 61   VAL A CG2 1 
ATOM   250  N  N   . TRP A 1 62   ? 13.626 53.587  14.654  1.00 18.71 ? 62   TRP A N   1 
ATOM   251  C  CA  . TRP A 1 62   ? 14.640 53.486  13.589  1.00 16.04 ? 62   TRP A CA  1 
ATOM   252  C  C   . TRP A 1 62   ? 13.841 54.121  12.473  1.00 16.86 ? 62   TRP A C   1 
ATOM   253  O  O   . TRP A 1 62   ? 13.086 53.444  11.762  1.00 17.78 ? 62   TRP A O   1 
ATOM   254  C  CB  . TRP A 1 62   ? 14.963 52.042  13.244  1.00 15.53 ? 62   TRP A CB  1 
ATOM   255  C  CG  . TRP A 1 62   ? 15.953 51.930  12.119  1.00 14.56 ? 62   TRP A CG  1 
ATOM   256  C  CD1 . TRP A 1 62   ? 16.644 52.969  11.511  1.00 16.17 ? 62   TRP A CD1 1 
ATOM   257  C  CD2 . TRP A 1 62   ? 16.307 50.749  11.440  1.00 15.76 ? 62   TRP A CD2 1 
ATOM   258  N  NE1 . TRP A 1 62   ? 17.389 52.469  10.484  1.00 15.73 ? 62   TRP A NE1 1 
ATOM   259  C  CE2 . TRP A 1 62   ? 17.214 51.108  10.413  1.00 15.95 ? 62   TRP A CE2 1 
ATOM   260  C  CE3 . TRP A 1 62   ? 15.945 49.399  11.587  1.00 14.32 ? 62   TRP A CE3 1 
ATOM   261  C  CZ2 . TRP A 1 62   ? 17.771 50.159  9.523   1.00 16.42 ? 62   TRP A CZ2 1 
ATOM   262  C  CZ3 . TRP A 1 62   ? 16.490 48.461  10.721  1.00 15.01 ? 62   TRP A CZ3 1 
ATOM   263  C  CH2 . TRP A 1 62   ? 17.406 48.844  9.686   1.00 15.71 ? 62   TRP A CH2 1 
ATOM   264  N  N   . LYS A 1 63   ? 14.031 55.433  12.286  1.00 16.61 ? 63   LYS A N   1 
ATOM   265  C  CA  . LYS A 1 63   ? 13.185 56.158  11.332  1.00 17.03 ? 63   LYS A CA  1 
ATOM   266  C  C   . LYS A 1 63   ? 13.151 55.665  9.909   1.00 18.76 ? 63   LYS A C   1 
ATOM   267  O  O   . LYS A 1 63   ? 12.111 55.760  9.233   1.00 21.34 ? 63   LYS A O   1 
ATOM   268  C  CB  . LYS A 1 63   ? 13.564 57.643  11.354  1.00 17.54 ? 63   LYS A CB  1 
ATOM   269  C  CG  . LYS A 1 63   ? 13.154 58.375  12.652  1.00 24.79 ? 63   LYS A CG  1 
ATOM   270  C  CD  . LYS A 1 63   ? 11.639 58.713  12.651  1.00 28.59 ? 63   LYS A CD  1 
ATOM   271  C  CE  . LYS A 1 63   ? 11.195 59.528  13.863  1.00 32.96 ? 63   LYS A CE  1 
ATOM   272  N  NZ  . LYS A 1 63   ? 11.227 58.797  15.192  1.00 36.65 ? 63   LYS A NZ  1 
ATOM   273  N  N   . GLN A 1 64   ? 14.269 55.132  9.437   1.00 17.24 ? 64   GLN A N   1 
ATOM   274  C  CA  . GLN A 1 64   ? 14.355 54.669  8.064   1.00 17.33 ? 64   GLN A CA  1 
ATOM   275  C  C   . GLN A 1 64   ? 14.421 53.173  7.916   1.00 15.96 ? 64   GLN A C   1 
ATOM   276  O  O   . GLN A 1 64   ? 14.723 52.642  6.844   1.00 16.66 ? 64   GLN A O   1 
ATOM   277  C  CB  . GLN A 1 64   ? 15.567 55.344  7.371   1.00 16.07 ? 64   GLN A CB  1 
ATOM   278  C  CG  . GLN A 1 64   ? 15.442 56.861  7.396   1.00 17.72 ? 64   GLN A CG  1 
ATOM   279  C  CD  . GLN A 1 64   ? 16.810 57.548  7.270   1.00 15.93 ? 64   GLN A CD  1 
ATOM   280  O  OE1 . GLN A 1 64   ? 17.741 57.233  8.007   1.00 17.44 ? 64   GLN A OE1 1 
ATOM   281  N  NE2 . GLN A 1 64   ? 16.903 58.510  6.358   1.00 15.17 ? 64   GLN A NE2 1 
ATOM   282  N  N   . GLY A 1 65   ? 14.055 52.493  9.010   1.00 16.23 ? 65   GLY A N   1 
ATOM   283  C  CA  . GLY A 1 65   ? 14.014 51.029  9.002   1.00 16.70 ? 65   GLY A CA  1 
ATOM   284  C  C   . GLY A 1 65   ? 12.656 50.467  9.421   1.00 18.52 ? 65   GLY A C   1 
ATOM   285  O  O   . GLY A 1 65   ? 11.615 50.823  8.841   1.00 19.17 ? 65   GLY A O   1 
ATOM   286  N  N   . TRP A 1 66   ? 12.683 49.604  10.424  1.00 18.12 ? 66   TRP A N   1 
ATOM   287  C  CA  . TRP A 1 66   ? 11.431 48.996  10.943  1.00 18.32 ? 66   TRP A CA  1 
ATOM   288  C  C   . TRP A 1 66   ? 11.696 48.608  12.371  1.00 20.07 ? 66   TRP A C   1 
ATOM   289  O  O   . TRP A 1 66   ? 12.823 48.720  12.851  1.00 19.21 ? 66   TRP A O   1 
ATOM   290  C  CB  . TRP A 1 66   ? 11.041 47.773  10.089  1.00 19.19 ? 66   TRP A CB  1 
ATOM   291  C  CG  . TRP A 1 66   ? 12.001 46.612  10.260  1.00 18.33 ? 66   TRP A CG  1 
ATOM   292  C  CD1 . TRP A 1 66   ? 11.912 45.587  11.177  1.00 18.52 ? 66   TRP A CD1 1 
ATOM   293  C  CD2 . TRP A 1 66   ? 13.210 46.371  9.525   1.00 17.50 ? 66   TRP A CD2 1 
ATOM   294  N  NE1 . TRP A 1 66   ? 12.974 44.730  11.061  1.00 19.43 ? 66   TRP A NE1 1 
ATOM   295  C  CE2 . TRP A 1 66   ? 13.795 45.178  10.054  1.00 17.46 ? 66   TRP A CE2 1 
ATOM   296  C  CE3 . TRP A 1 66   ? 13.862 47.040  8.471   1.00 17.86 ? 66   TRP A CE3 1 
ATOM   297  C  CZ2 . TRP A 1 66   ? 14.989 44.644  9.574   1.00 20.42 ? 66   TRP A CZ2 1 
ATOM   298  C  CZ3 . TRP A 1 66   ? 15.046 46.504  7.997   1.00 19.29 ? 66   TRP A CZ3 1 
ATOM   299  C  CH2 . TRP A 1 66   ? 15.605 45.320  8.547   1.00 17.23 ? 66   TRP A CH2 1 
ATOM   300  N  N   . ASN A 1 67   ? 10.657 48.184  13.105  1.00 20.11 ? 67   ASN A N   1 
ATOM   301  C  CA  . ASN A 1 67   ? 10.883 47.765  14.497  1.00 20.43 ? 67   ASN A CA  1 
ATOM   302  C  C   . ASN A 1 67   ? 11.481 46.361  14.514  1.00 20.09 ? 67   ASN A C   1 
ATOM   303  O  O   . ASN A 1 67   ? 10.789 45.352  14.235  1.00 19.04 ? 67   ASN A O   1 
ATOM   304  C  CB  . ASN A 1 67   ? 9.576  47.728  15.297  1.00 22.53 ? 67   ASN A CB  1 
ATOM   305  C  CG  . ASN A 1 67   ? 8.958  49.071  15.472  1.00 24.79 ? 67   ASN A CG  1 
ATOM   306  O  OD1 . ASN A 1 67   ? 9.647  50.090  15.605  1.00 26.71 ? 67   ASN A OD1 1 
ATOM   307  N  ND2 . ASN A 1 67   ? 7.628  49.094  15.520  1.00 29.89 ? 67   ASN A ND2 1 
ATOM   308  N  N   . ILE A 1 68   ? 12.759 46.289  14.845  1.00 18.88 ? 68   ILE A N   1 
ATOM   309  C  CA  . ILE A 1 68   ? 13.459 45.031  14.841  1.00 19.89 ? 68   ILE A CA  1 
ATOM   310  C  C   . ILE A 1 68   ? 13.016 44.126  15.987  1.00 21.36 ? 68   ILE A C   1 
ATOM   311  O  O   . ILE A 1 68   ? 12.924 44.563  17.127  1.00 22.37 ? 68   ILE A O   1 
ATOM   312  C  CB  . ILE A 1 68   ? 15.011 45.237  14.931  1.00 20.54 ? 68   ILE A CB  1 
ATOM   313  C  CG1 . ILE A 1 68   ? 15.539 46.037  13.721  1.00 21.02 ? 68   ILE A CG1 1 
ATOM   314  C  CG2 . ILE A 1 68   ? 15.700 43.877  14.985  1.00 21.28 ? 68   ILE A CG2 1 
ATOM   315  C  CD1 . ILE A 1 68   ? 17.006 46.530  13.935  1.00 19.62 ? 68   ILE A CD1 1 
ATOM   316  N  N   . LYS A 1 69   ? 12.768 42.865  15.665  1.00 23.90 ? 69   LYS A N   1 
ATOM   317  C  CA  . LYS A 1 69   ? 12.383 41.892  16.686  1.00 24.59 ? 69   LYS A CA  1 
ATOM   318  C  C   . LYS A 1 69   ? 13.414 40.764  16.641  1.00 23.92 ? 69   LYS A C   1 
ATOM   319  O  O   . LYS A 1 69   ? 13.972 40.454  15.589  1.00 23.62 ? 69   LYS A O   1 
ATOM   320  C  CB  . LYS A 1 69   ? 10.977 41.336  16.401  1.00 29.34 ? 69   LYS A CB  1 
ATOM   321  C  CG  . LYS A 1 69   ? 9.842  42.318  16.707  1.00 33.66 ? 69   LYS A CG  1 
ATOM   322  C  CD  . LYS A 1 69   ? 8.524  41.895  16.038  1.00 41.21 ? 69   LYS A CD  1 
ATOM   323  C  CE  . LYS A 1 69   ? 8.132  40.433  16.372  1.00 45.30 ? 69   LYS A CE  1 
ATOM   324  N  NZ  . LYS A 1 69   ? 6.898  39.971  15.628  1.00 45.81 ? 69   LYS A NZ  1 
ATOM   325  N  N   . TYR A 1 70   ? 13.708 40.180  17.793  1.00 23.74 ? 70   TYR A N   1 
ATOM   326  C  CA  . TYR A 1 70   ? 14.651 39.058  17.830  1.00 22.31 ? 70   TYR A CA  1 
ATOM   327  C  C   . TYR A 1 70   ? 14.100 37.998  18.798  1.00 25.22 ? 70   TYR A C   1 
ATOM   328  O  O   . TYR A 1 70   ? 13.269 38.308  19.656  1.00 25.43 ? 70   TYR A O   1 
ATOM   329  C  CB  . TYR A 1 70   ? 16.050 39.508  18.302  1.00 22.43 ? 70   TYR A CB  1 
ATOM   330  C  CG  . TYR A 1 70   ? 16.100 40.129  19.670  1.00 20.69 ? 70   TYR A CG  1 
ATOM   331  C  CD1 . TYR A 1 70   ? 15.851 41.472  19.843  1.00 22.02 ? 70   TYR A CD1 1 
ATOM   332  C  CD2 . TYR A 1 70   ? 16.427 39.367  20.801  1.00 22.30 ? 70   TYR A CD2 1 
ATOM   333  C  CE1 . TYR A 1 70   ? 15.922 42.067  21.079  1.00 24.21 ? 70   TYR A CE1 1 
ATOM   334  C  CE2 . TYR A 1 70   ? 16.504 39.968  22.067  1.00 24.09 ? 70   TYR A CE2 1 
ATOM   335  C  CZ  . TYR A 1 70   ? 16.242 41.318  22.188  1.00 22.55 ? 70   TYR A CZ  1 
ATOM   336  O  OH  . TYR A 1 70   ? 16.251 41.927  23.426  1.00 26.03 ? 70   TYR A OH  1 
ATOM   337  N  N   . ASP A 1 71   ? 14.558 36.765  18.610  1.00 26.48 ? 71   ASP A N   1 
ATOM   338  C  CA  . ASP A 1 71   ? 14.181 35.631  19.444  1.00 28.14 ? 71   ASP A CA  1 
ATOM   339  C  C   . ASP A 1 71   ? 15.168 35.568  20.596  1.00 27.84 ? 71   ASP A C   1 
ATOM   340  O  O   . ASP A 1 71   ? 16.329 35.221  20.413  1.00 28.49 ? 71   ASP A O   1 
ATOM   341  C  CB  . ASP A 1 71   ? 14.251 34.347  18.632  1.00 30.16 ? 71   ASP A CB  1 
ATOM   342  C  CG  . ASP A 1 71   ? 13.837 33.115  19.455  1.00 32.90 ? 71   ASP A CG  1 
ATOM   343  O  OD1 . ASP A 1 71   ? 13.675 33.233  20.690  1.00 33.51 ? 71   ASP A OD1 1 
ATOM   344  O  OD2 . ASP A 1 71   ? 13.680 32.040  18.852  1.00 36.53 ? 71   ASP A OD2 1 
ATOM   345  N  N   . PRO A 1 72   ? 14.715 35.916  21.807  1.00 30.02 ? 72   PRO A N   1 
ATOM   346  C  CA  . PRO A 1 72   ? 15.604 35.889  22.966  1.00 30.93 ? 72   PRO A CA  1 
ATOM   347  C  C   . PRO A 1 72   ? 16.369 34.573  23.137  1.00 29.58 ? 72   PRO A C   1 
ATOM   348  O  O   . PRO A 1 72   ? 17.464 34.560  23.682  1.00 31.56 ? 72   PRO A O   1 
ATOM   349  C  CB  . PRO A 1 72   ? 14.660 36.210  24.130  1.00 30.34 ? 72   PRO A CB  1 
ATOM   350  C  CG  . PRO A 1 72   ? 13.315 35.694  23.634  1.00 33.40 ? 72   PRO A CG  1 
ATOM   351  C  CD  . PRO A 1 72   ? 13.318 36.159  22.204  1.00 29.88 ? 72   PRO A CD  1 
ATOM   352  N  N   . LEU A 1 73   ? 15.812 33.476  22.639  1.00 30.28 ? 73   LEU A N   1 
ATOM   353  C  CA  . LEU A 1 73   ? 16.458 32.168  22.748  1.00 30.73 ? 73   LEU A CA  1 
ATOM   354  C  C   . LEU A 1 73   ? 17.534 31.917  21.694  1.00 29.03 ? 73   LEU A C   1 
ATOM   355  O  O   . LEU A 1 73   ? 18.150 30.856  21.671  1.00 29.81 ? 73   LEU A O   1 
ATOM   356  C  CB  . LEU A 1 73   ? 15.402 31.061  22.650  1.00 31.40 ? 73   LEU A CB  1 
ATOM   357  C  CG  . LEU A 1 73   ? 14.291 31.179  23.690  1.00 33.86 ? 73   LEU A CG  1 
ATOM   358  C  CD1 . LEU A 1 73   ? 13.214 30.094  23.468  1.00 35.37 ? 73   LEU A CD1 1 
ATOM   359  C  CD2 . LEU A 1 73   ? 14.928 31.076  25.066  1.00 32.73 ? 73   LEU A CD2 1 
ATOM   360  N  N   . LYS A 1 74   ? 17.753 32.881  20.799  1.00 28.38 ? 74   LYS A N   1 
ATOM   361  C  CA  . LYS A 1 74   ? 18.777 32.733  19.776  1.00 27.82 ? 74   LYS A CA  1 
ATOM   362  C  C   . LYS A 1 74   ? 20.162 32.574  20.409  1.00 27.53 ? 74   LYS A C   1 
ATOM   363  O  O   . LYS A 1 74   ? 21.028 31.839  19.912  1.00 28.09 ? 74   LYS A O   1 
ATOM   364  C  CB  . LYS A 1 74   ? 18.771 33.976  18.886  1.00 28.79 ? 74   LYS A CB  1 
ATOM   365  C  CG  . LYS A 1 74   ? 19.754 33.924  17.732  1.00 31.74 ? 74   LYS A CG  1 
ATOM   366  C  CD  . LYS A 1 74   ? 19.536 35.148  16.856  1.00 32.93 ? 74   LYS A CD  1 
ATOM   367  C  CE  . LYS A 1 74   ? 20.343 35.087  15.575  1.00 35.04 ? 74   LYS A CE  1 
ATOM   368  N  NZ  . LYS A 1 74   ? 19.836 36.150  14.657  1.00 38.04 ? 74   LYS A NZ  1 
ATOM   369  N  N   . TYR A 1 75   ? 20.406 33.313  21.485  1.00 28.91 ? 75   TYR A N   1 
ATOM   370  C  CA  . TYR A 1 75   ? 21.695 33.234  22.155  1.00 28.48 ? 75   TYR A CA  1 
ATOM   371  C  C   . TYR A 1 75   ? 21.492 32.504  23.483  1.00 28.69 ? 75   TYR A C   1 
ATOM   372  O  O   A TYR A 1 75   ? 20.461 32.678  24.132  0.50 30.37 ? 75   TYR A O   1 
ATOM   373  O  O   B TYR A 1 75   ? 20.304 32.292  23.984  0.50 29.74 ? 75   TYR A O   1 
ATOM   374  C  CB  A TYR A 1 75   ? 22.290 34.644  22.339  0.50 29.19 ? 75   TYR A CB  1 
ATOM   375  C  CB  B TYR A 1 75   ? 22.102 34.570  22.630  0.50 27.89 ? 75   TYR A CB  1 
ATOM   376  C  CG  A TYR A 1 75   ? 22.655 35.297  21.012  0.50 27.30 ? 75   TYR A CG  1 
ATOM   377  C  CG  B TYR A 1 75   ? 22.084 35.526  21.486  0.50 25.52 ? 75   TYR A CG  1 
ATOM   378  C  CD1 A TYR A 1 75   ? 21.838 36.275  20.434  0.50 29.18 ? 75   TYR A CD1 1 
ATOM   379  C  CD1 B TYR A 1 75   ? 21.031 36.416  21.324  0.50 26.30 ? 75   TYR A CD1 1 
ATOM   380  C  CD2 A TYR A 1 75   ? 23.767 34.864  20.289  0.50 27.91 ? 75   TYR A CD2 1 
ATOM   381  C  CD2 B TYR A 1 75   ? 23.081 35.495  20.521  0.50 24.99 ? 75   TYR A CD2 1 
ATOM   382  C  CE1 A TYR A 1 75   ? 22.119 36.799  19.162  0.50 28.32 ? 75   TYR A CE1 1 
ATOM   383  C  CE1 B TYR A 1 75   ? 20.967 37.255  20.225  0.50 24.42 ? 75   TYR A CE1 1 
ATOM   384  C  CE2 A TYR A 1 75   ? 24.054 35.371  19.017  0.50 28.43 ? 75   TYR A CE2 1 
ATOM   385  C  CE2 B TYR A 1 75   ? 23.028 36.330  19.413  0.50 25.53 ? 75   TYR A CE2 1 
ATOM   386  C  CZ  A TYR A 1 75   ? 23.230 36.332  18.456  0.50 27.58 ? 75   TYR A CZ  1 
ATOM   387  C  CZ  B TYR A 1 75   ? 21.967 37.204  19.277  0.50 24.16 ? 75   TYR A CZ  1 
ATOM   388  O  OH  A TYR A 1 75   ? 23.508 36.781  17.171  0.50 28.24 ? 75   TYR A OH  1 
ATOM   389  O  OH  B TYR A 1 75   ? 21.908 38.022  18.189  0.50 23.28 ? 75   TYR A OH  1 
ATOM   390  N  N   . ASN A 1 76   ? 22.476 31.685  23.852  1.00 27.67 ? 76   ASN A N   1 
ATOM   391  C  CA  . ASN A 1 76   ? 22.440 30.860  25.052  1.00 28.96 ? 76   ASN A CA  1 
ATOM   392  C  C   . ASN A 1 76   ? 23.867 30.557  25.515  1.00 29.17 ? 76   ASN A C   1 
ATOM   393  O  O   . ASN A 1 76   ? 24.834 31.097  24.980  1.00 28.18 ? 76   ASN A O   1 
ATOM   394  C  CB  . ASN A 1 76   ? 21.674 29.556  24.769  1.00 30.43 ? 76   ASN A CB  1 
ATOM   395  C  CG  . ASN A 1 76   ? 22.211 28.810  23.572  1.00 29.61 ? 76   ASN A CG  1 
ATOM   396  O  OD1 . ASN A 1 76   ? 23.377 28.446  23.534  1.00 31.29 ? 76   ASN A OD1 1 
ATOM   397  N  ND2 . ASN A 1 76   ? 21.343 28.568  22.577  1.00 35.66 ? 76   ASN A ND2 1 
ATOM   398  N  N   . ALA A 1 77   ? 24.019 29.675  26.497  1.00 28.89 ? 77   ALA A N   1 
ATOM   399  C  CA  . ALA A 1 77   ? 25.354 29.387  27.007  1.00 32.34 ? 77   ALA A CA  1 
ATOM   400  C  C   . ALA A 1 77   ? 26.347 28.902  25.951  1.00 33.22 ? 77   ALA A C   1 
ATOM   401  O  O   . ALA A 1 77   ? 27.539 29.169  26.053  1.00 33.14 ? 77   ALA A O   1 
ATOM   402  C  CB  . ALA A 1 77   ? 25.264 28.366  28.142  1.00 34.56 ? 77   ALA A CB  1 
ATOM   403  N  N   . HIS A 1 78   ? 25.844 28.220  24.925  1.00 35.25 ? 78   HIS A N   1 
ATOM   404  C  CA  . HIS A 1 78   ? 26.704 27.675  23.877  1.00 37.57 ? 78   HIS A CA  1 
ATOM   405  C  C   . HIS A 1 78   ? 26.789 28.544  22.640  1.00 36.78 ? 78   HIS A C   1 
ATOM   406  O  O   . HIS A 1 78   ? 27.502 28.216  21.679  1.00 38.16 ? 78   HIS A O   1 
ATOM   407  C  CB  . HIS A 1 78   ? 26.206 26.279  23.484  1.00 40.74 ? 78   HIS A CB  1 
ATOM   408  C  CG  . HIS A 1 78   ? 26.087 25.345  24.647  1.00 45.11 ? 78   HIS A CG  1 
ATOM   409  N  ND1 . HIS A 1 78   ? 27.187 24.864  25.330  1.00 47.54 ? 78   HIS A ND1 1 
ATOM   410  C  CD2 . HIS A 1 78   ? 24.999 24.849  25.285  1.00 45.85 ? 78   HIS A CD2 1 
ATOM   411  C  CE1 . HIS A 1 78   ? 26.781 24.111  26.339  1.00 47.63 ? 78   HIS A CE1 1 
ATOM   412  N  NE2 . HIS A 1 78   ? 25.459 24.087  26.335  1.00 48.95 ? 78   HIS A NE2 1 
ATOM   413  N  N   . HIS A 1 79   ? 26.046 29.640  22.655  1.00 32.96 ? 79   HIS A N   1 
ATOM   414  C  CA  . HIS A 1 79   ? 26.048 30.537  21.514  1.00 30.04 ? 79   HIS A CA  1 
ATOM   415  C  C   . HIS A 1 79   ? 25.813 31.939  22.032  1.00 24.05 ? 79   HIS A C   1 
ATOM   416  O  O   . HIS A 1 79   ? 24.686 32.397  22.085  1.00 24.09 ? 79   HIS A O   1 
ATOM   417  C  CB  . HIS A 1 79   ? 24.935 30.157  20.548  1.00 31.89 ? 79   HIS A CB  1 
ATOM   418  C  CG  . HIS A 1 79   ? 25.067 30.814  19.208  1.00 34.86 ? 79   HIS A CG  1 
ATOM   419  N  ND1 . HIS A 1 79   ? 24.247 31.844  18.796  1.00 35.95 ? 79   HIS A ND1 1 
ATOM   420  C  CD2 . HIS A 1 79   ? 25.959 30.615  18.206  1.00 33.47 ? 79   HIS A CD2 1 
ATOM   421  C  CE1 . HIS A 1 79   ? 24.630 32.252  17.598  1.00 35.42 ? 79   HIS A CE1 1 
ATOM   422  N  NE2 . HIS A 1 79   ? 25.666 31.524  17.219  1.00 33.89 ? 79   HIS A NE2 1 
ATOM   423  N  N   . LYS A 1 80   ? 26.901 32.589  22.419  1.00 23.08 ? 80   LYS A N   1 
ATOM   424  C  CA  . LYS A 1 80   ? 26.812 33.923  22.965  1.00 20.91 ? 80   LYS A CA  1 
ATOM   425  C  C   . LYS A 1 80   ? 27.047 34.965  21.885  1.00 20.64 ? 80   LYS A C   1 
ATOM   426  O  O   . LYS A 1 80   ? 27.663 34.675  20.844  1.00 21.96 ? 80   LYS A O   1 
ATOM   427  C  CB  . LYS A 1 80   ? 27.870 34.098  24.027  1.00 22.33 ? 80   LYS A CB  1 
ATOM   428  C  CG  . LYS A 1 80   ? 27.743 33.040  25.106  1.00 23.44 ? 80   LYS A CG  1 
ATOM   429  C  CD  . LYS A 1 80   ? 28.886 33.090  26.101  1.00 29.06 ? 80   LYS A CD  1 
ATOM   430  C  CE  . LYS A 1 80   ? 29.016 34.403  26.842  1.00 29.60 ? 80   LYS A CE  1 
ATOM   431  N  NZ  . LYS A 1 80   ? 29.891 34.203  28.078  1.00 33.06 ? 80   LYS A NZ  1 
ATOM   432  N  N   . LEU A 1 81   ? 26.557 36.165  22.151  1.00 17.85 ? 81   LEU A N   1 
ATOM   433  C  CA  . LEU A 1 81   ? 26.749 37.292  21.242  1.00 16.75 ? 81   LEU A CA  1 
ATOM   434  C  C   . LEU A 1 81   ? 28.039 37.952  21.712  1.00 18.07 ? 81   LEU A C   1 
ATOM   435  O  O   . LEU A 1 81   ? 28.146 38.355  22.889  1.00 17.34 ? 81   LEU A O   1 
ATOM   436  C  CB  . LEU A 1 81   ? 25.570 38.258  21.363  1.00 18.23 ? 81   LEU A CB  1 
ATOM   437  C  CG  . LEU A 1 81   ? 25.669 39.544  20.494  1.00 17.18 ? 81   LEU A CG  1 
ATOM   438  C  CD1 . LEU A 1 81   ? 25.643 39.188  19.002  1.00 17.74 ? 81   LEU A CD1 1 
ATOM   439  C  CD2 . LEU A 1 81   ? 24.499 40.466  20.832  1.00 20.08 ? 81   LEU A CD2 1 
ATOM   440  N  N   . LYS A 1 82   ? 29.029 38.064  20.813  1.00 15.71 ? 82   LYS A N   1 
ATOM   441  C  CA  . LYS A 1 82   ? 30.305 38.666  21.160  1.00 14.63 ? 82   LYS A CA  1 
ATOM   442  C  C   . LYS A 1 82   ? 30.247 40.081  20.637  1.00 15.85 ? 82   LYS A C   1 
ATOM   443  O  O   . LYS A 1 82   ? 30.039 40.284  19.434  1.00 18.29 ? 82   LYS A O   1 
ATOM   444  C  CB  . LYS A 1 82   ? 31.471 37.900  20.514  1.00 18.82 ? 82   LYS A CB  1 
ATOM   445  C  CG  . LYS A 1 82   ? 31.692 36.524  21.137  1.00 29.02 ? 82   LYS A CG  1 
ATOM   446  C  CD  . LYS A 1 82   ? 32.287 36.716  22.571  1.00 38.21 ? 82   LYS A CD  1 
ATOM   447  C  CE  . LYS A 1 82   ? 33.042 35.466  23.156  1.00 41.58 ? 82   LYS A CE  1 
ATOM   448  N  NZ  . LYS A 1 82   ? 32.168 34.410  23.766  1.00 43.04 ? 82   LYS A NZ  1 
ATOM   449  N  N   . VAL A 1 83   ? 30.389 41.047  21.530  1.00 13.74 ? 83   VAL A N   1 
ATOM   450  C  CA  . VAL A 1 83   ? 30.267 42.439  21.150  1.00 14.03 ? 83   VAL A CA  1 
ATOM   451  C  C   . VAL A 1 83   ? 31.604 43.171  21.302  1.00 14.57 ? 83   VAL A C   1 
ATOM   452  O  O   . VAL A 1 83   ? 32.229 43.153  22.369  1.00 15.89 ? 83   VAL A O   1 
ATOM   453  C  CB  . VAL A 1 83   ? 29.196 43.106  22.078  1.00 13.78 ? 83   VAL A CB  1 
ATOM   454  C  CG1 . VAL A 1 83   ? 28.995 44.607  21.754  1.00 14.65 ? 83   VAL A CG1 1 
ATOM   455  C  CG2 . VAL A 1 83   ? 27.823 42.381  21.939  1.00 15.68 ? 83   VAL A CG2 1 
ATOM   456  N  N   . PHE A 1 84   ? 32.035 43.859  20.247  1.00 14.71 ? 84   PHE A N   1 
ATOM   457  C  CA  . PHE A 1 84   ? 33.246 44.646  20.272  1.00 15.36 ? 84   PHE A CA  1 
ATOM   458  C  C   . PHE A 1 84   ? 32.862 46.110  20.203  1.00 14.51 ? 84   PHE A C   1 
ATOM   459  O  O   . PHE A 1 84   ? 32.313 46.572  19.191  1.00 14.83 ? 84   PHE A O   1 
ATOM   460  C  CB  . PHE A 1 84   ? 34.099 44.293  19.048  1.00 15.28 ? 84   PHE A CB  1 
ATOM   461  C  CG  . PHE A 1 84   ? 34.733 42.969  19.169  1.00 15.35 ? 84   PHE A CG  1 
ATOM   462  C  CD1 . PHE A 1 84   ? 35.796 42.776  20.048  1.00 19.99 ? 84   PHE A CD1 1 
ATOM   463  C  CD2 . PHE A 1 84   ? 34.239 41.880  18.472  1.00 18.75 ? 84   PHE A CD2 1 
ATOM   464  C  CE1 . PHE A 1 84   ? 36.381 41.515  20.242  1.00 20.30 ? 84   PHE A CE1 1 
ATOM   465  C  CE2 . PHE A 1 84   ? 34.799 40.599  18.652  1.00 20.29 ? 84   PHE A CE2 1 
ATOM   466  C  CZ  . PHE A 1 84   ? 35.883 40.418  19.542  1.00 21.01 ? 84   PHE A CZ  1 
ATOM   467  N  N   . VAL A 1 85   ? 33.153 46.842  21.265  1.00 12.44 ? 85   VAL A N   1 
ATOM   468  C  CA  . VAL A 1 85   ? 32.893 48.281  21.307  1.00 13.61 ? 85   VAL A CA  1 
ATOM   469  C  C   . VAL A 1 85   ? 34.217 48.916  20.908  1.00 12.00 ? 85   VAL A C   1 
ATOM   470  O  O   . VAL A 1 85   ? 35.268 48.739  21.571  1.00 13.08 ? 85   VAL A O   1 
ATOM   471  C  CB  . VAL A 1 85   ? 32.451 48.738  22.709  1.00 12.68 ? 85   VAL A CB  1 
ATOM   472  C  CG1 . VAL A 1 85   ? 32.283 50.273  22.760  1.00 15.85 ? 85   VAL A CG1 1 
ATOM   473  C  CG2 . VAL A 1 85   ? 31.167 47.988  23.080  1.00 16.40 ? 85   VAL A CG2 1 
ATOM   474  N  N   . VAL A 1 86   ? 34.177 49.644  19.784  1.00 12.34 ? 86   VAL A N   1 
ATOM   475  C  CA  . VAL A 1 86   ? 35.398 50.191  19.190  1.00 12.62 ? 86   VAL A CA  1 
ATOM   476  C  C   . VAL A 1 86   ? 35.461 51.720  19.280  1.00 11.44 ? 86   VAL A C   1 
ATOM   477  O  O   . VAL A 1 86   ? 34.827 52.421  18.501  1.00 12.43 ? 86   VAL A O   1 
ATOM   478  C  CB  . VAL A 1 86   ? 35.466 49.741  17.707  1.00 11.95 ? 86   VAL A CB  1 
ATOM   479  C  CG1 . VAL A 1 86   ? 36.771 50.308  17.072  1.00 13.96 ? 86   VAL A CG1 1 
ATOM   480  C  CG2 . VAL A 1 86   ? 35.398 48.175  17.593  1.00 13.73 ? 86   VAL A CG2 1 
ATOM   481  N  N   . PRO A 1 87   ? 36.224 52.256  20.248  1.00 13.24 ? 87   PRO A N   1 
ATOM   482  C  CA  . PRO A 1 87   ? 36.353 53.721  20.426  1.00 12.03 ? 87   PRO A CA  1 
ATOM   483  C  C   . PRO A 1 87   ? 37.092 54.321  19.226  1.00 11.39 ? 87   PRO A C   1 
ATOM   484  O  O   . PRO A 1 87   ? 38.102 53.740  18.725  1.00 12.03 ? 87   PRO A O   1 
ATOM   485  C  CB  . PRO A 1 87   ? 37.181 53.865  21.721  1.00 12.94 ? 87   PRO A CB  1 
ATOM   486  C  CG  . PRO A 1 87   ? 36.948 52.518  22.417  1.00 14.32 ? 87   PRO A CG  1 
ATOM   487  C  CD  . PRO A 1 87   ? 36.945 51.518  21.291  1.00 12.92 ? 87   PRO A CD  1 
ATOM   488  N  N   . HIS A 1 88   ? 36.572 55.451  18.777  1.00 11.33 ? 88   HIS A N   1 
ATOM   489  C  CA  . HIS A 1 88   ? 37.167 56.134  17.601  1.00 12.47 ? 88   HIS A CA  1 
ATOM   490  C  C   . HIS A 1 88   ? 36.914 57.609  17.680  1.00 13.80 ? 88   HIS A C   1 
ATOM   491  O  O   . HIS A 1 88   ? 36.083 58.075  18.471  1.00 12.26 ? 88   HIS A O   1 
ATOM   492  C  CB  . HIS A 1 88   ? 36.573 55.550  16.287  1.00 12.52 ? 88   HIS A CB  1 
ATOM   493  C  CG  . HIS A 1 88   ? 35.135 55.876  16.045  1.00 13.11 ? 88   HIS A CG  1 
ATOM   494  N  ND1 . HIS A 1 88   ? 34.709 56.948  15.273  1.00 13.57 ? 88   HIS A ND1 1 
ATOM   495  C  CD2 . HIS A 1 88   ? 34.010 55.266  16.498  1.00 11.96 ? 88   HIS A CD2 1 
ATOM   496  C  CE1 . HIS A 1 88   ? 33.390 56.969  15.256  1.00 14.97 ? 88   HIS A CE1 1 
ATOM   497  N  NE2 . HIS A 1 88   ? 32.939 55.960  16.001  1.00 13.87 ? 88   HIS A NE2 1 
ATOM   498  N  N   . SER A 1 89   ? 37.615 58.374  16.857  1.00 11.59 ? 89   SER A N   1 
ATOM   499  C  CA  . SER A 1 89   ? 37.510 59.826  16.840  1.00 12.91 ? 89   SER A CA  1 
ATOM   500  C  C   . SER A 1 89   ? 37.665 60.279  15.380  1.00 12.16 ? 89   SER A C   1 
ATOM   501  O  O   . SER A 1 89   ? 38.748 60.063  14.812  1.00 12.83 ? 89   SER A O   1 
ATOM   502  C  CB  . SER A 1 89   ? 38.645 60.377  17.697  1.00 13.76 ? 89   SER A CB  1 
ATOM   503  O  OG  . SER A 1 89   ? 38.645 61.786  17.714  1.00 13.56 ? 89   SER A OG  1 
ATOM   504  N  N   . HIS A 1 90   ? 36.609 60.841  14.801  1.00 11.77 ? 90   HIS A N   1 
ATOM   505  C  CA  . HIS A 1 90   ? 36.660 61.288  13.404  1.00 12.48 ? 90   HIS A CA  1 
ATOM   506  C  C   . HIS A 1 90   ? 37.355 62.645  13.340  1.00 11.85 ? 90   HIS A C   1 
ATOM   507  O  O   . HIS A 1 90   ? 36.834 63.648  13.828  1.00 12.94 ? 90   HIS A O   1 
ATOM   508  C  CB  . HIS A 1 90   ? 35.243 61.326  12.826  1.00 12.84 ? 90   HIS A CB  1 
ATOM   509  C  CG  . HIS A 1 90   ? 35.207 61.622  11.360  1.00 11.93 ? 90   HIS A CG  1 
ATOM   510  N  ND1 . HIS A 1 90   ? 35.829 60.832  10.412  1.00 12.86 ? 90   HIS A ND1 1 
ATOM   511  C  CD2 . HIS A 1 90   ? 34.639 62.640  10.700  1.00 12.25 ? 90   HIS A CD2 1 
ATOM   512  C  CE1 . HIS A 1 90   ? 35.650 61.379  9.217   1.00 12.11 ? 90   HIS A CE1 1 
ATOM   513  N  NE2 . HIS A 1 90   ? 34.937 62.480  9.361   1.00 12.87 ? 90   HIS A NE2 1 
ATOM   514  N  N   . ASN A 1 91   ? 38.538 62.669  12.732  1.00 12.54 ? 91   ASN A N   1 
ATOM   515  C  CA  . ASN A 1 91   ? 39.318 63.902  12.672  1.00 12.94 ? 91   ASN A CA  1 
ATOM   516  C  C   . ASN A 1 91   ? 39.485 64.379  11.240  1.00 14.94 ? 91   ASN A C   1 
ATOM   517  O  O   . ASN A 1 91   ? 40.362 63.875  10.486  1.00 16.62 ? 91   ASN A O   1 
ATOM   518  C  CB  . ASN A 1 91   ? 40.710 63.676  13.274  1.00 13.13 ? 91   ASN A CB  1 
ATOM   519  C  CG  . ASN A 1 91   ? 40.686 63.554  14.766  1.00 14.30 ? 91   ASN A CG  1 
ATOM   520  O  OD1 . ASN A 1 91   ? 40.085 62.615  15.314  1.00 15.90 ? 91   ASN A OD1 1 
ATOM   521  N  ND2 . ASN A 1 91   ? 41.340 64.450  15.435  1.00 11.33 ? 91   ASN A ND2 1 
ATOM   522  N  N   . ASP A 1 92   ? 38.713 65.371  10.869  1.00 11.33 ? 92   ASP A N   1 
ATOM   523  C  CA  . ASP A 1 92   ? 38.810 65.885  9.504   1.00 12.92 ? 92   ASP A CA  1 
ATOM   524  C  C   . ASP A 1 92   ? 40.056 66.715  9.292   1.00 12.86 ? 92   ASP A C   1 
ATOM   525  O  O   . ASP A 1 92   ? 40.286 67.654  10.051  1.00 13.67 ? 92   ASP A O   1 
ATOM   526  C  CB  . ASP A 1 92   ? 37.635 66.806  9.249   1.00 11.83 ? 92   ASP A CB  1 
ATOM   527  C  CG  . ASP A 1 92   ? 36.318 66.079  9.248   1.00 12.31 ? 92   ASP A CG  1 
ATOM   528  O  OD1 . ASP A 1 92   ? 36.201 65.154  8.444   1.00 12.74 ? 92   ASP A OD1 1 
ATOM   529  O  OD2 . ASP A 1 92   ? 35.394 66.453  10.041  1.00 14.82 ? 92   ASP A OD2 1 
ATOM   530  N  N   . PRO A 1 93   ? 40.899 66.403  8.289   1.00 12.37 ? 93   PRO A N   1 
ATOM   531  C  CA  . PRO A 1 93   ? 42.129 67.174  7.983   1.00 12.09 ? 93   PRO A CA  1 
ATOM   532  C  C   . PRO A 1 93   ? 41.721 68.453  7.221   1.00 13.27 ? 93   PRO A C   1 
ATOM   533  O  O   . PRO A 1 93   ? 42.071 68.657  6.033   1.00 14.90 ? 93   PRO A O   1 
ATOM   534  C  CB  . PRO A 1 93   ? 42.958 66.211  7.113   1.00 13.27 ? 93   PRO A CB  1 
ATOM   535  C  CG  . PRO A 1 93   ? 42.426 64.830  7.455   1.00 15.40 ? 93   PRO A CG  1 
ATOM   536  C  CD  . PRO A 1 93   ? 40.901 65.116  7.569   1.00 12.50 ? 93   PRO A CD  1 
ATOM   537  N  N   . GLY A 1 94   ? 40.980 69.302  7.933   1.00 12.62 ? 94   GLY A N   1 
ATOM   538  C  CA  . GLY A 1 94   ? 40.427 70.539  7.396   1.00 12.79 ? 94   GLY A CA  1 
ATOM   539  C  C   . GLY A 1 94   ? 38.932 70.363  7.134   1.00 13.67 ? 94   GLY A C   1 
ATOM   540  O  O   . GLY A 1 94   ? 38.489 69.312  6.621   1.00 14.96 ? 94   GLY A O   1 
ATOM   541  N  N   . TRP A 1 95   ? 38.138 71.348  7.536   1.00 14.59 ? 95   TRP A N   1 
ATOM   542  C  CA  . TRP A 1 95   ? 36.707 71.352  7.254   1.00 13.38 ? 95   TRP A CA  1 
ATOM   543  C  C   . TRP A 1 95   ? 36.206 72.736  7.700   1.00 14.51 ? 95   TRP A C   1 
ATOM   544  O  O   . TRP A 1 95   ? 36.161 73.653  6.885   1.00 14.18 ? 95   TRP A O   1 
ATOM   545  C  CB  . TRP A 1 95   ? 35.957 70.206  7.965   1.00 13.01 ? 95   TRP A CB  1 
ATOM   546  C  CG  . TRP A 1 95   ? 34.459 70.313  7.654   1.00 14.56 ? 95   TRP A CG  1 
ATOM   547  C  CD1 . TRP A 1 95   ? 33.871 70.700  6.460   1.00 12.85 ? 95   TRP A CD1 1 
ATOM   548  C  CD2 . TRP A 1 95   ? 33.381 70.003  8.533   1.00 14.61 ? 95   TRP A CD2 1 
ATOM   549  N  NE1 . TRP A 1 95   ? 32.492 70.646  6.564   1.00 14.17 ? 95   TRP A NE1 1 
ATOM   550  C  CE2 . TRP A 1 95   ? 32.173 70.212  7.828   1.00 13.72 ? 95   TRP A CE2 1 
ATOM   551  C  CE3 . TRP A 1 95   ? 33.323 69.550  9.858   1.00 14.56 ? 95   TRP A CE3 1 
ATOM   552  C  CZ2 . TRP A 1 95   ? 30.908 69.975  8.404   1.00 14.55 ? 95   TRP A CZ2 1 
ATOM   553  C  CZ3 . TRP A 1 95   ? 32.062 69.313  10.431  1.00 18.10 ? 95   TRP A CZ3 1 
ATOM   554  C  CH2 . TRP A 1 95   ? 30.874 69.529  9.690   1.00 17.28 ? 95   TRP A CH2 1 
ATOM   555  N  N   . ILE A 1 96   ? 35.865 72.879  8.988   1.00 14.97 ? 96   ILE A N   1 
ATOM   556  C  CA  . ILE A 1 96   ? 35.421 74.147  9.614   1.00 16.49 ? 96   ILE A CA  1 
ATOM   557  C  C   . ILE A 1 96   ? 36.646 74.955  10.053  1.00 14.55 ? 96   ILE A C   1 
ATOM   558  O  O   . ILE A 1 96   ? 36.566 76.177  10.220  1.00 18.75 ? 96   ILE A O   1 
ATOM   559  C  CB  . ILE A 1 96   ? 34.573 73.885  10.908  1.00 20.04 ? 96   ILE A CB  1 
ATOM   560  C  CG1 . ILE A 1 96   ? 33.351 73.089  10.569  1.00 24.63 ? 96   ILE A CG1 1 
ATOM   561  C  CG2 . ILE A 1 96   ? 34.149 75.191  11.559  1.00 22.95 ? 96   ILE A CG2 1 
ATOM   562  C  CD1 . ILE A 1 96   ? 32.782 73.552  9.265   1.00 20.52 ? 96   ILE A CD1 1 
ATOM   563  N  N   . GLN A 1 97   ? 37.764 74.270  10.260  1.00 13.33 ? 97   GLN A N   1 
ATOM   564  C  CA  . GLN A 1 97   ? 39.035 74.903  10.609  1.00 13.05 ? 97   GLN A CA  1 
ATOM   565  C  C   . GLN A 1 97   ? 40.063 74.279  9.660   1.00 12.60 ? 97   GLN A C   1 
ATOM   566  O  O   . GLN A 1 97   ? 39.769 73.287  8.989   1.00 13.02 ? 97   GLN A O   1 
ATOM   567  C  CB  . GLN A 1 97   ? 39.455 74.601  12.057  1.00 15.59 ? 97   GLN A CB  1 
ATOM   568  C  CG  . GLN A 1 97   ? 38.424 74.980  13.143  1.00 16.08 ? 97   GLN A CG  1 
ATOM   569  C  CD  A GLN A 1 97   ? 38.991 74.843  14.551  0.50 17.87 ? 97   GLN A CD  1 
ATOM   570  C  CD  B GLN A 1 97   ? 38.783 76.617  13.202  0.50 20.00 ? 97   GLN A CD  1 
ATOM   571  O  OE1 A GLN A 1 97   ? 40.053 75.377  14.860  0.50 21.66 ? 97   GLN A OE1 1 
ATOM   572  O  OE1 B GLN A 1 97   ? 38.172 77.398  12.486  0.50 23.33 ? 97   GLN A OE1 1 
ATOM   573  N  NE2 A GLN A 1 97   ? 38.279 74.133  15.408  0.50 21.86 ? 97   GLN A NE2 1 
ATOM   574  N  NE2 B GLN A 1 97   ? 39.704 77.017  14.065  0.50 20.10 ? 97   GLN A NE2 1 
ATOM   575  N  N   . THR A 1 98   ? 41.246 74.865  9.551   1.00 12.12 ? 98   THR A N   1 
ATOM   576  C  CA  . THR A 1 98   ? 42.285 74.301  8.690   1.00 12.37 ? 98   THR A CA  1 
ATOM   577  C  C   . THR A 1 98   ? 42.901 73.112  9.409   1.00 13.24 ? 98   THR A C   1 
ATOM   578  O  O   . THR A 1 98   ? 42.667 72.872  10.611  1.00 13.40 ? 98   THR A O   1 
ATOM   579  C  CB  . THR A 1 98   ? 43.413 75.285  8.446   1.00 12.33 ? 98   THR A CB  1 
ATOM   580  O  OG1 . THR A 1 98   ? 44.036 75.584  9.712   1.00 13.44 ? 98   THR A OG1 1 
ATOM   581  C  CG2 . THR A 1 98   ? 42.902 76.582  7.783   1.00 12.83 ? 98   THR A CG2 1 
ATOM   582  N  N   . PHE A 1 99   ? 43.676 72.326  8.681   1.00 12.82 ? 99   PHE A N   1 
ATOM   583  C  CA  . PHE A 1 99   ? 44.396 71.211  9.261   1.00 11.84 ? 99   PHE A CA  1 
ATOM   584  C  C   . PHE A 1 99   ? 45.194 71.670  10.474  1.00 12.11 ? 99   PHE A C   1 
ATOM   585  O  O   . PHE A 1 99   ? 45.137 71.047  11.538  1.00 12.92 ? 99   PHE A O   1 
ATOM   586  C  CB  . PHE A 1 99   ? 45.385 70.670  8.220   1.00 12.38 ? 99   PHE A CB  1 
ATOM   587  C  CG  . PHE A 1 99   ? 46.241 69.553  8.721   1.00 12.68 ? 99   PHE A CG  1 
ATOM   588  C  CD1 . PHE A 1 99   ? 45.832 68.210  8.618   1.00 12.57 ? 99   PHE A CD1 1 
ATOM   589  C  CD2 . PHE A 1 99   ? 47.452 69.832  9.332   1.00 13.13 ? 99   PHE A CD2 1 
ATOM   590  C  CE1 . PHE A 1 99   ? 46.620 67.188  9.113   1.00 12.90 ? 99   PHE A CE1 1 
ATOM   591  C  CE2 . PHE A 1 99   ? 48.257 68.810  9.835   1.00 15.10 ? 99   PHE A CE2 1 
ATOM   592  C  CZ  . PHE A 1 99   ? 47.837 67.480  9.724   1.00 13.67 ? 99   PHE A CZ  1 
ATOM   593  N  N   . GLU A 1 100  ? 45.957 72.750  10.330  1.00 13.10 ? 100  GLU A N   1 
ATOM   594  C  CA  . GLU A 1 100  ? 46.799 73.154  11.441  1.00 13.49 ? 100  GLU A CA  1 
ATOM   595  C  C   . GLU A 1 100  ? 45.991 73.682  12.617  1.00 13.06 ? 100  GLU A C   1 
ATOM   596  O  O   . GLU A 1 100  ? 46.372 73.414  13.764  1.00 14.11 ? 100  GLU A O   1 
ATOM   597  C  CB  . GLU A 1 100  ? 47.834 74.188  10.959  1.00 13.78 ? 100  GLU A CB  1 
ATOM   598  C  CG  . GLU A 1 100  ? 48.868 74.569  12.042  1.00 16.75 ? 100  GLU A CG  1 
ATOM   599  C  CD  . GLU A 1 100  ? 49.710 73.416  12.547  1.00 17.84 ? 100  GLU A CD  1 
ATOM   600  O  OE1 . GLU A 1 100  ? 49.870 72.386  11.866  1.00 17.31 ? 100  GLU A OE1 1 
ATOM   601  O  OE2 . GLU A 1 100  ? 50.325 73.574  13.645  1.00 20.11 ? 100  GLU A OE2 1 
ATOM   602  N  N   . GLU A 1 101  ? 44.894 74.386  12.356  1.00 13.35 ? 101  GLU A N   1 
ATOM   603  C  CA  . GLU A 1 101  ? 44.031 74.890  13.426  1.00 14.10 ? 101  GLU A CA  1 
ATOM   604  C  C   . GLU A 1 101  ? 43.424 73.727  14.187  1.00 14.41 ? 101  GLU A C   1 
ATOM   605  O  O   . GLU A 1 101  ? 43.442 73.729  15.435  1.00 14.65 ? 101  GLU A O   1 
ATOM   606  C  CB  . GLU A 1 101  ? 42.895 75.742  12.865  1.00 15.46 ? 101  GLU A CB  1 
ATOM   607  C  CG  . GLU A 1 101  ? 43.318 77.146  12.413  1.00 20.11 ? 101  GLU A CG  1 
ATOM   608  C  CD  . GLU A 1 101  ? 42.234 77.904  11.601  1.00 23.98 ? 101  GLU A CD  1 
ATOM   609  O  OE1 . GLU A 1 101  ? 41.289 77.318  11.011  1.00 18.97 ? 101  GLU A OE1 1 
ATOM   610  O  OE2 . GLU A 1 101  ? 42.353 79.148  11.525  1.00 28.40 ? 101  GLU A OE2 1 
ATOM   611  N  N   . TYR A 1 102  ? 42.856 72.748  13.502  1.00 13.10 ? 102  TYR A N   1 
ATOM   612  C  CA  . TYR A 1 102  ? 42.328 71.580  14.224  1.00 13.53 ? 102  TYR A CA  1 
ATOM   613  C  C   . TYR A 1 102  ? 43.437 70.860  14.982  1.00 14.96 ? 102  TYR A C   1 
ATOM   614  O  O   . TYR A 1 102  ? 43.205 70.341  16.097  1.00 14.29 ? 102  TYR A O   1 
ATOM   615  C  CB  . TYR A 1 102  ? 41.729 70.536  13.279  1.00 14.64 ? 102  TYR A CB  1 
ATOM   616  C  CG  . TYR A 1 102  ? 40.340 70.824  12.787  1.00 14.31 ? 102  TYR A CG  1 
ATOM   617  C  CD1 . TYR A 1 102  ? 39.276 71.061  13.675  1.00 14.80 ? 102  TYR A CD1 1 
ATOM   618  C  CD2 . TYR A 1 102  ? 40.049 70.685  11.429  1.00 15.20 ? 102  TYR A CD2 1 
ATOM   619  C  CE1 . TYR A 1 102  ? 37.938 71.146  13.189  1.00 14.60 ? 102  TYR A CE1 1 
ATOM   620  C  CE2 . TYR A 1 102  ? 38.761 70.744  10.950  1.00 14.17 ? 102  TYR A CE2 1 
ATOM   621  C  CZ  . TYR A 1 102  ? 37.703 70.974  11.831  1.00 13.86 ? 102  TYR A CZ  1 
ATOM   622  O  OH  . TYR A 1 102  ? 36.414 70.988  11.361  1.00 15.31 ? 102  TYR A OH  1 
ATOM   623  N  N   . TYR A 1 103  ? 44.618 70.726  14.390  1.00 13.17 ? 103  TYR A N   1 
ATOM   624  C  CA  . TYR A 1 103  ? 45.688 70.040  15.092  1.00 14.67 ? 103  TYR A CA  1 
ATOM   625  C  C   . TYR A 1 103  ? 46.003 70.722  16.407  1.00 14.69 ? 103  TYR A C   1 
ATOM   626  O  O   . TYR A 1 103  ? 46.139 70.068  17.413  1.00 15.15 ? 103  TYR A O   1 
ATOM   627  C  CB  . TYR A 1 103  ? 46.961 69.993  14.260  1.00 13.54 ? 103  TYR A CB  1 
ATOM   628  C  CG  . TYR A 1 103  ? 48.102 69.369  15.001  1.00 15.16 ? 103  TYR A CG  1 
ATOM   629  C  CD1 . TYR A 1 103  ? 48.141 67.988  15.269  1.00 14.94 ? 103  TYR A CD1 1 
ATOM   630  C  CD2 . TYR A 1 103  ? 49.151 70.178  15.476  1.00 14.98 ? 103  TYR A CD2 1 
ATOM   631  C  CE1 . TYR A 1 103  ? 49.194 67.430  15.988  1.00 15.09 ? 103  TYR A CE1 1 
ATOM   632  C  CE2 . TYR A 1 103  ? 50.199 69.624  16.199  1.00 15.65 ? 103  TYR A CE2 1 
ATOM   633  C  CZ  . TYR A 1 103  ? 50.218 68.266  16.462  1.00 15.29 ? 103  TYR A CZ  1 
ATOM   634  O  OH  . TYR A 1 103  ? 51.211 67.709  17.290  1.00 18.56 ? 103  TYR A OH  1 
ATOM   635  N  N   . GLN A 1 104  ? 46.123 72.040  16.376  1.00 14.27 ? 104  GLN A N   1 
ATOM   636  C  CA  . GLN A 1 104  ? 46.474 72.781  17.603  1.00 15.46 ? 104  GLN A CA  1 
ATOM   637  C  C   . GLN A 1 104  ? 45.383 72.800  18.635  1.00 17.85 ? 104  GLN A C   1 
ATOM   638  O  O   . GLN A 1 104  ? 45.654 72.683  19.830  1.00 18.04 ? 104  GLN A O   1 
ATOM   639  C  CB  . GLN A 1 104  ? 46.822 74.239  17.251  1.00 15.15 ? 104  GLN A CB  1 
ATOM   640  C  CG  . GLN A 1 104  ? 48.153 74.357  16.511  1.00 16.26 ? 104  GLN A CG  1 
ATOM   641  C  CD  . GLN A 1 104  ? 49.343 73.844  17.310  1.00 16.96 ? 104  GLN A CD  1 
ATOM   642  O  OE1 . GLN A 1 104  ? 49.374 73.955  18.542  1.00 19.10 ? 104  GLN A OE1 1 
ATOM   643  N  NE2 . GLN A 1 104  ? 50.329 73.306  16.622  1.00 18.53 ? 104  GLN A NE2 1 
ATOM   644  N  N   . HIS A 1 105  ? 44.144 72.949  18.183  1.00 15.87 ? 105  HIS A N   1 
ATOM   645  C  CA  . HIS A 1 105  ? 42.980 73.074  19.070  1.00 16.88 ? 105  HIS A CA  1 
ATOM   646  C  C   . HIS A 1 105  ? 42.386 71.771  19.553  1.00 18.01 ? 105  HIS A C   1 
ATOM   647  O  O   A HIS A 1 105  ? 41.817 71.713  20.639  0.50 19.10 ? 105  HIS A O   1 
ATOM   648  O  O   B HIS A 1 105  ? 42.120 71.588  20.781  0.50 19.11 ? 105  HIS A O   1 
ATOM   649  C  CB  . HIS A 1 105  ? 41.856 73.843  18.362  1.00 18.36 ? 105  HIS A CB  1 
ATOM   650  C  CG  A HIS A 1 105  ? 42.252 75.205  17.878  0.50 20.06 ? 105  HIS A CG  1 
ATOM   651  C  CG  B HIS A 1 105  ? 40.884 74.309  19.537  0.50 22.48 ? 105  HIS A CG  1 
ATOM   652  N  ND1 A HIS A 1 105  ? 41.583 75.851  16.862  0.50 24.52 ? 105  HIS A ND1 1 
ATOM   653  N  ND1 B HIS A 1 105  ? 39.820 73.520  19.913  0.50 25.64 ? 105  HIS A ND1 1 
ATOM   654  C  CD2 A HIS A 1 105  ? 43.241 76.042  18.270  0.50 23.22 ? 105  HIS A CD2 1 
ATOM   655  C  CD2 B HIS A 1 105  ? 40.761 75.463  20.236  0.50 27.02 ? 105  HIS A CD2 1 
ATOM   656  C  CE1 A HIS A 1 105  ? 42.147 77.026  16.646  0.50 23.95 ? 105  HIS A CE1 1 
ATOM   657  C  CE1 B HIS A 1 105  ? 39.082 74.167  20.800  0.50 26.92 ? 105  HIS A CE1 1 
ATOM   658  N  NE2 A HIS A 1 105  ? 43.155 77.166  17.487  0.50 23.30 ? 105  HIS A NE2 1 
ATOM   659  N  NE2 B HIS A 1 105  ? 39.633 75.350  21.013  0.50 27.38 ? 105  HIS A NE2 1 
ATOM   660  N  N   . ASP A 1 106  ? 42.492 70.724  18.733  1.00 16.57 ? 106  ASP A N   1 
ATOM   661  C  CA  . ASP A 1 106  ? 41.900 69.444  19.071  1.00 16.73 ? 106  ASP A CA  1 
ATOM   662  C  C   . ASP A 1 106  ? 42.712 68.205  18.945  1.00 14.96 ? 106  ASP A C   1 
ATOM   663  O  O   . ASP A 1 106  ? 42.908 67.503  19.936  1.00 16.09 ? 106  ASP A O   1 
ATOM   664  C  CB  . ASP A 1 106  ? 40.623 69.256  18.225  1.00 20.00 ? 106  ASP A CB  1 
ATOM   665  C  CG  . ASP A 1 106  ? 39.594 70.316  18.519  1.00 23.89 ? 106  ASP A CG  1 
ATOM   666  O  OD1 . ASP A 1 106  ? 38.866 70.144  19.509  1.00 23.07 ? 106  ASP A OD1 1 
ATOM   667  O  OD2 . ASP A 1 106  ? 39.544 71.315  17.767  1.00 26.55 ? 106  ASP A OD2 1 
ATOM   668  N  N   . THR A 1 107  ? 43.223 67.926  17.746  1.00 14.77 ? 107  THR A N   1 
ATOM   669  C  CA  . THR A 1 107  ? 43.872 66.646  17.505  1.00 13.64 ? 107  THR A CA  1 
ATOM   670  C  C   . THR A 1 107  ? 45.120 66.375  18.314  1.00 13.79 ? 107  THR A C   1 
ATOM   671  O  O   . THR A 1 107  ? 45.345 65.242  18.731  1.00 13.65 ? 107  THR A O   1 
ATOM   672  C  CB  . THR A 1 107  ? 44.124 66.484  15.981  1.00 13.79 ? 107  THR A CB  1 
ATOM   673  O  OG1 . THR A 1 107  ? 42.894 66.705  15.299  1.00 14.55 ? 107  THR A OG1 1 
ATOM   674  C  CG2 . THR A 1 107  ? 44.678 65.078  15.677  1.00 14.49 ? 107  THR A CG2 1 
ATOM   675  N  N   . LYS A 1 108  ? 45.926 67.403  18.578  1.00 13.38 ? 108  LYS A N   1 
ATOM   676  C  CA  . LYS A 1 108  ? 47.121 67.081  19.347  1.00 13.07 ? 108  LYS A CA  1 
ATOM   677  C  C   . LYS A 1 108  ? 46.768 66.639  20.757  1.00 13.36 ? 108  LYS A C   1 
ATOM   678  O  O   . LYS A 1 108  ? 47.472 65.829  21.321  1.00 15.18 ? 108  LYS A O   1 
ATOM   679  C  CB  . LYS A 1 108  ? 48.108 68.277  19.335  1.00 16.36 ? 108  LYS A CB  1 
ATOM   680  C  CG  . LYS A 1 108  ? 47.826 69.432  20.252  1.00 18.44 ? 108  LYS A CG  1 
ATOM   681  C  CD  . LYS A 1 108  ? 48.928 70.462  20.074  1.00 20.96 ? 108  LYS A CD  1 
ATOM   682  C  CE  . LYS A 1 108  ? 48.728 71.618  21.012  1.00 22.07 ? 108  LYS A CE  1 
ATOM   683  N  NZ  . LYS A 1 108  ? 49.886 72.572  20.939  1.00 25.03 ? 108  LYS A NZ  1 
ATOM   684  N  N   . HIS A 1 109  ? 45.672 67.171  21.273  1.00 13.92 ? 109  HIS A N   1 
ATOM   685  C  CA  . HIS A 1 109  ? 45.209 66.794  22.624  1.00 14.24 ? 109  HIS A CA  1 
ATOM   686  C  C   . HIS A 1 109  ? 44.571 65.424  22.599  1.00 15.36 ? 109  HIS A C   1 
ATOM   687  O  O   . HIS A 1 109  ? 44.795 64.626  23.509  1.00 14.91 ? 109  HIS A O   1 
ATOM   688  C  CB  . HIS A 1 109  ? 44.222 67.810  23.126  1.00 14.32 ? 109  HIS A CB  1 
ATOM   689  C  CG  . HIS A 1 109  ? 44.778 69.184  23.180  1.00 18.21 ? 109  HIS A CG  1 
ATOM   690  N  ND1 . HIS A 1 109  ? 45.810 69.523  24.033  1.00 23.03 ? 109  HIS A ND1 1 
ATOM   691  C  CD2 . HIS A 1 109  ? 44.484 70.289  22.460  1.00 22.08 ? 109  HIS A CD2 1 
ATOM   692  C  CE1 . HIS A 1 109  ? 46.126 70.790  23.833  1.00 21.56 ? 109  HIS A CE1 1 
ATOM   693  N  NE2 . HIS A 1 109  ? 45.337 71.277  22.885  1.00 22.92 ? 109  HIS A NE2 1 
ATOM   694  N  N   . ILE A 1 110  ? 43.784 65.120  21.562  1.00 14.11 ? 110  ILE A N   1 
ATOM   695  C  CA  . ILE A 1 110  ? 43.203 63.783  21.448  1.00 13.75 ? 110  ILE A CA  1 
ATOM   696  C  C   . ILE A 1 110  ? 44.314 62.729  21.441  1.00 14.27 ? 110  ILE A C   1 
ATOM   697  O  O   . ILE A 1 110  ? 44.237 61.716  22.141  1.00 14.87 ? 110  ILE A O   1 
ATOM   698  C  CB  . ILE A 1 110  ? 42.379 63.686  20.118  1.00 12.08 ? 110  ILE A CB  1 
ATOM   699  C  CG1 . ILE A 1 110  ? 41.156 64.586  20.208  1.00 13.06 ? 110  ILE A CG1 1 
ATOM   700  C  CG2 . ILE A 1 110  ? 42.033 62.217  19.806  1.00 14.28 ? 110  ILE A CG2 1 
ATOM   701  C  CD1 . ILE A 1 110  ? 40.416 64.841  18.835  1.00 14.06 ? 110  ILE A CD1 1 
ATOM   702  N  N   . LEU A 1 111  ? 45.333 62.933  20.624  1.00 13.14 ? 111  LEU A N   1 
ATOM   703  C  CA  . LEU A 1 111  ? 46.390 61.959  20.548  1.00 12.43 ? 111  LEU A CA  1 
ATOM   704  C  C   . LEU A 1 111  ? 47.252 61.873  21.795  1.00 13.22 ? 111  LEU A C   1 
ATOM   705  O  O   . LEU A 1 111  ? 47.667 60.787  22.181  1.00 14.52 ? 111  LEU A O   1 
ATOM   706  C  CB  . LEU A 1 111  ? 47.265 62.221  19.293  1.00 13.77 ? 111  LEU A CB  1 
ATOM   707  C  CG  . LEU A 1 111  ? 46.498 61.871  18.003  1.00 13.14 ? 111  LEU A CG  1 
ATOM   708  C  CD1 . LEU A 1 111  ? 47.361 62.356  16.825  1.00 13.22 ? 111  LEU A CD1 1 
ATOM   709  C  CD2 . LEU A 1 111  ? 46.215 60.380  17.919  1.00 16.59 ? 111  LEU A CD2 1 
ATOM   710  N  N   . SER A 1 112  ? 47.545 63.017  22.388  1.00 13.97 ? 112  SER A N   1 
ATOM   711  C  CA  . SER A 1 112  ? 48.366 63.012  23.598  1.00 14.76 ? 112  SER A CA  1 
ATOM   712  C  C   . SER A 1 112  ? 47.581 62.323  24.726  1.00 16.50 ? 112  SER A C   1 
ATOM   713  O  O   . SER A 1 112  ? 48.144 61.506  25.480  1.00 16.75 ? 112  SER A O   1 
ATOM   714  C  CB  A SER A 1 112  ? 48.730 64.444  23.966  0.50 15.88 ? 112  SER A CB  1 
ATOM   715  C  CB  B SER A 1 112  ? 48.547 64.500  24.050  0.50 19.58 ? 112  SER A CB  1 
ATOM   716  O  OG  A SER A 1 112  ? 49.434 64.479  25.191  0.50 16.05 ? 112  SER A OG  1 
ATOM   717  O  OG  B SER A 1 112  ? 49.300 65.183  23.087  0.50 22.53 ? 112  SER A OG  1 
ATOM   718  N  N   . ASN A 1 113  ? 46.288 62.614  24.828  1.00 15.98 ? 113  ASN A N   1 
ATOM   719  C  CA  . ASN A 1 113  ? 45.508 61.949  25.867  1.00 15.16 ? 113  ASN A CA  1 
ATOM   720  C  C   . ASN A 1 113  ? 45.248 60.494  25.520  1.00 16.94 ? 113  ASN A C   1 
ATOM   721  O  O   . ASN A 1 113  ? 45.161 59.663  26.432  1.00 16.04 ? 113  ASN A O   1 
ATOM   722  C  CB  . ASN A 1 113  ? 44.254 62.740  26.205  1.00 16.38 ? 113  ASN A CB  1 
ATOM   723  C  CG  . ASN A 1 113  ? 44.634 64.080  26.835  1.00 18.72 ? 113  ASN A CG  1 
ATOM   724  O  OD1 . ASN A 1 113  ? 45.727 64.194  27.443  1.00 23.44 ? 113  ASN A OD1 1 
ATOM   725  N  ND2 . ASN A 1 113  ? 43.799 65.084  26.677  1.00 20.70 ? 113  ASN A ND2 1 
ATOM   726  N  N   . ALA A 1 114  ? 45.152 60.134  24.230  1.00 15.61 ? 114  ALA A N   1 
ATOM   727  C  CA  . ALA A 1 114  ? 44.988 58.718  23.891  1.00 16.71 ? 114  ALA A CA  1 
ATOM   728  C  C   . ALA A 1 114  ? 46.240 57.968  24.366  1.00 15.59 ? 114  ALA A C   1 
ATOM   729  O  O   . ALA A 1 114  ? 46.167 56.839  24.901  1.00 17.07 ? 114  ALA A O   1 
ATOM   730  C  CB  . ALA A 1 114  ? 44.860 58.543  22.372  1.00 14.58 ? 114  ALA A CB  1 
ATOM   731  N  N   . LEU A 1 115  ? 47.425 58.557  24.150  1.00 15.87 ? 115  LEU A N   1 
ATOM   732  C  CA  . LEU A 1 115  ? 48.644 57.892  24.558  1.00 16.88 ? 115  LEU A CA  1 
ATOM   733  C  C   . LEU A 1 115  ? 48.650 57.647  26.063  1.00 18.66 ? 115  LEU A C   1 
ATOM   734  O  O   . LEU A 1 115  ? 48.933 56.543  26.524  1.00 18.97 ? 115  LEU A O   1 
ATOM   735  C  CB  . LEU A 1 115  ? 49.879 58.715  24.168  1.00 17.95 ? 115  LEU A CB  1 
ATOM   736  C  CG  . LEU A 1 115  ? 51.246 58.158  24.610  1.00 19.16 ? 115  LEU A CG  1 
ATOM   737  C  CD1 . LEU A 1 115  ? 51.472 56.746  24.145  1.00 22.58 ? 115  LEU A CD1 1 
ATOM   738  C  CD2 . LEU A 1 115  ? 52.310 59.059  24.029  1.00 19.69 ? 115  LEU A CD2 1 
ATOM   739  N  N   . ARG A 1 116  ? 48.289 58.674  26.802  1.00 17.98 ? 116  ARG A N   1 
ATOM   740  C  CA  . ARG A 1 116  ? 48.279 58.529  28.253  1.00 18.61 ? 116  ARG A CA  1 
ATOM   741  C  C   . ARG A 1 116  ? 47.214 57.528  28.731  1.00 18.14 ? 116  ARG A C   1 
ATOM   742  O  O   . ARG A 1 116  ? 47.528 56.594  29.491  1.00 18.02 ? 116  ARG A O   1 
ATOM   743  C  CB  . ARG A 1 116  ? 48.041 59.886  28.887  1.00 21.32 ? 116  ARG A CB  1 
ATOM   744  C  CG  . ARG A 1 116  ? 47.577 59.812  30.367  1.00 25.87 ? 116  ARG A CG  1 
ATOM   745  C  CD  . ARG A 1 116  ? 47.027 61.167  30.827  1.00 33.29 ? 116  ARG A CD  1 
ATOM   746  N  NE  . ARG A 1 116  ? 46.500 61.146  32.194  1.00 36.08 ? 116  ARG A NE  1 
ATOM   747  C  CZ  . ARG A 1 116  ? 46.062 62.233  32.828  1.00 38.62 ? 116  ARG A CZ  1 
ATOM   748  N  NH1 . ARG A 1 116  ? 46.091 63.412  32.211  1.00 38.49 ? 116  ARG A NH1 1 
ATOM   749  N  NH2 . ARG A 1 116  ? 45.611 62.148  34.079  1.00 40.42 ? 116  ARG A NH2 1 
ATOM   750  N  N   . HIS A 1 117  ? 45.984 57.679  28.252  1.00 16.35 ? 117  HIS A N   1 
ATOM   751  C  CA  . HIS A 1 117  ? 44.928 56.790  28.713  1.00 17.23 ? 117  HIS A CA  1 
ATOM   752  C  C   . HIS A 1 117  ? 45.072 55.370  28.284  1.00 17.85 ? 117  HIS A C   1 
ATOM   753  O  O   . HIS A 1 117  ? 44.760 54.487  29.058  1.00 18.05 ? 117  HIS A O   1 
ATOM   754  C  CB  . HIS A 1 117  ? 43.568 57.337  28.355  1.00 19.35 ? 117  HIS A CB  1 
ATOM   755  C  CG  . HIS A 1 117  ? 43.184 58.498  29.207  1.00 23.76 ? 117  HIS A CG  1 
ATOM   756  N  ND1 . HIS A 1 117  ? 42.609 58.345  30.458  1.00 21.54 ? 117  HIS A ND1 1 
ATOM   757  C  CD2 . HIS A 1 117  ? 43.404 59.823  29.045  1.00 25.32 ? 117  HIS A CD2 1 
ATOM   758  C  CE1 . HIS A 1 117  ? 42.503 59.538  31.030  1.00 24.32 ? 117  HIS A CE1 1 
ATOM   759  N  NE2 . HIS A 1 117  ? 42.979 60.450  30.198  1.00 26.63 ? 117  HIS A NE2 1 
ATOM   760  N  N   . LEU A 1 118  ? 45.538 55.099  27.068  1.00 16.38 ? 118  LEU A N   1 
ATOM   761  C  CA  . LEU A 1 118  ? 45.745 53.732  26.670  1.00 16.18 ? 118  LEU A CA  1 
ATOM   762  C  C   . LEU A 1 118  ? 46.916 53.136  27.437  1.00 16.36 ? 118  LEU A C   1 
ATOM   763  O  O   . LEU A 1 118  ? 46.858 51.983  27.901  1.00 18.08 ? 118  LEU A O   1 
ATOM   764  C  CB  . LEU A 1 118  ? 45.956 53.657  25.135  1.00 15.69 ? 118  LEU A CB  1 
ATOM   765  C  CG  . LEU A 1 118  ? 44.717 54.085  24.314  1.00 18.91 ? 118  LEU A CG  1 
ATOM   766  C  CD1 . LEU A 1 118  ? 45.134 54.242  22.818  1.00 18.04 ? 118  LEU A CD1 1 
ATOM   767  C  CD2 . LEU A 1 118  ? 43.611 53.083  24.484  1.00 17.26 ? 118  LEU A CD2 1 
ATOM   768  N  N   . HIS A 1 119  ? 47.979 53.898  27.606  1.00 17.05 ? 119  HIS A N   1 
ATOM   769  C  CA  . HIS A 1 119  ? 49.091 53.350  28.376  1.00 16.70 ? 119  HIS A CA  1 
ATOM   770  C  C   . HIS A 1 119  ? 48.609 52.923  29.773  1.00 19.38 ? 119  HIS A C   1 
ATOM   771  O  O   . HIS A 1 119  ? 48.910 51.817  30.227  1.00 20.40 ? 119  HIS A O   1 
ATOM   772  C  CB  . HIS A 1 119  ? 50.186 54.410  28.525  1.00 20.64 ? 119  HIS A CB  1 
ATOM   773  C  CG  . HIS A 1 119  ? 51.332 53.977  29.376  1.00 24.71 ? 119  HIS A CG  1 
ATOM   774  N  ND1 . HIS A 1 119  ? 51.475 54.376  30.690  1.00 30.76 ? 119  HIS A ND1 1 
ATOM   775  C  CD2 . HIS A 1 119  ? 52.374 53.156  29.114  1.00 28.95 ? 119  HIS A CD2 1 
ATOM   776  C  CE1 . HIS A 1 119  ? 52.559 53.817  31.200  1.00 30.03 ? 119  HIS A CE1 1 
ATOM   777  N  NE2 . HIS A 1 119  ? 53.124 53.073  30.265  1.00 30.25 ? 119  HIS A NE2 1 
ATOM   778  N  N   . ASP A 1 120  ? 47.851 53.786  30.427  1.00 19.43 ? 120  ASP A N   1 
ATOM   779  C  CA  . ASP A 1 120  ? 47.395 53.488  31.798  1.00 19.09 ? 120  ASP A CA  1 
ATOM   780  C  C   . ASP A 1 120  ? 46.226 52.516  31.969  1.00 22.33 ? 120  ASP A C   1 
ATOM   781  O  O   . ASP A 1 120  ? 45.952 52.102  33.097  1.00 21.28 ? 120  ASP A O   1 
ATOM   782  C  CB  . ASP A 1 120  ? 47.008 54.787  32.501  1.00 20.36 ? 120  ASP A CB  1 
ATOM   783  C  CG  . ASP A 1 120  ? 48.199 55.711  32.755  1.00 21.44 ? 120  ASP A CG  1 
ATOM   784  O  OD1 . ASP A 1 120  ? 49.363 55.279  32.634  1.00 24.18 ? 120  ASP A OD1 1 
ATOM   785  O  OD2 . ASP A 1 120  ? 47.962 56.879  33.091  1.00 25.46 ? 120  ASP A OD2 1 
ATOM   786  N  N   . ASN A 1 121  ? 45.528 52.148  30.896  1.00 18.82 ? 121  ASN A N   1 
ATOM   787  C  CA  . ASN A 1 121  ? 44.345 51.273  30.983  1.00 18.97 ? 121  ASN A CA  1 
ATOM   788  C  C   . ASN A 1 121  ? 44.509 50.230  29.904  1.00 19.19 ? 121  ASN A C   1 
ATOM   789  O  O   . ASN A 1 121  ? 43.961 50.354  28.811  1.00 19.02 ? 121  ASN A O   1 
ATOM   790  C  CB  . ASN A 1 121  ? 43.095 52.104  30.755  1.00 18.24 ? 121  ASN A CB  1 
ATOM   791  C  CG  . ASN A 1 121  ? 42.931 53.170  31.809  1.00 19.55 ? 121  ASN A CG  1 
ATOM   792  O  OD1 . ASN A 1 121  ? 43.320 54.347  31.615  1.00 21.68 ? 121  ASN A OD1 1 
ATOM   793  N  ND2 . ASN A 1 121  ? 42.361 52.775  32.953  1.00 19.91 ? 121  ASN A ND2 1 
ATOM   794  N  N   . PRO A 1 122  ? 45.236 49.167  30.201  1.00 17.29 ? 122  PRO A N   1 
ATOM   795  C  CA  . PRO A 1 122  ? 45.540 48.087  29.265  1.00 17.24 ? 122  PRO A CA  1 
ATOM   796  C  C   . PRO A 1 122  ? 44.435 47.449  28.460  1.00 17.82 ? 122  PRO A C   1 
ATOM   797  O  O   . PRO A 1 122  ? 44.739 46.925  27.352  1.00 20.21 ? 122  PRO A O   1 
ATOM   798  C  CB  . PRO A 1 122  ? 46.301 47.073  30.121  1.00 19.51 ? 122  PRO A CB  1 
ATOM   799  C  CG  . PRO A 1 122  ? 46.856 47.920  31.249  1.00 21.07 ? 122  PRO A CG  1 
ATOM   800  C  CD  . PRO A 1 122  ? 45.723 48.826  31.561  1.00 19.08 ? 122  PRO A CD  1 
ATOM   801  N  N   . GLU A 1 123  ? 43.189 47.457  28.954  1.00 16.41 ? 123  GLU A N   1 
ATOM   802  C  CA  . GLU A 1 123  ? 42.095 46.857  28.180  1.00 17.71 ? 123  GLU A CA  1 
ATOM   803  C  C   . GLU A 1 123  ? 41.382 47.855  27.271  1.00 17.18 ? 123  GLU A C   1 
ATOM   804  O  O   . GLU A 1 123  ? 40.553 47.457  26.458  1.00 19.02 ? 123  GLU A O   1 
ATOM   805  C  CB  . GLU A 1 123  ? 41.033 46.197  29.088  1.00 20.66 ? 123  GLU A CB  1 
ATOM   806  C  CG  . GLU A 1 123  ? 41.535 45.089  30.027  1.00 28.34 ? 123  GLU A CG  1 
ATOM   807  C  CD  . GLU A 1 123  ? 42.251 43.986  29.306  1.00 32.51 ? 123  GLU A CD  1 
ATOM   808  O  OE1 . GLU A 1 123  ? 41.685 43.445  28.326  1.00 35.99 ? 123  GLU A OE1 1 
ATOM   809  O  OE2 . GLU A 1 123  ? 43.388 43.651  29.722  1.00 39.12 ? 123  GLU A OE2 1 
ATOM   810  N  N   . MET A 1 124  ? 41.655 49.151  27.428  1.00 15.64 ? 124  MET A N   1 
ATOM   811  C  CA  . MET A 1 124  ? 41.035 50.175  26.588  1.00 16.28 ? 124  MET A CA  1 
ATOM   812  C  C   . MET A 1 124  ? 41.676 50.075  25.189  1.00 17.73 ? 124  MET A C   1 
ATOM   813  O  O   . MET A 1 124  ? 42.824 49.742  25.065  1.00 16.95 ? 124  MET A O   1 
ATOM   814  C  CB  . MET A 1 124  ? 41.295 51.564  27.181  1.00 17.48 ? 124  MET A CB  1 
ATOM   815  C  CG  . MET A 1 124  ? 40.565 52.711  26.476  1.00 18.29 ? 124  MET A CG  1 
ATOM   816  S  SD  . MET A 1 124  ? 38.792 52.427  26.348  1.00 19.08 ? 124  MET A SD  1 
ATOM   817  C  CE  . MET A 1 124  ? 38.317 53.969  25.521  1.00 19.71 ? 124  MET A CE  1 
ATOM   818  N  N   . LYS A 1 125  ? 40.890 50.385  24.152  1.00 15.64 ? 125  LYS A N   1 
ATOM   819  C  CA  . LYS A 1 125  ? 41.341 50.321  22.751  1.00 15.49 ? 125  LYS A CA  1 
ATOM   820  C  C   . LYS A 1 125  ? 40.930 51.601  22.038  1.00 14.93 ? 125  LYS A C   1 
ATOM   821  O  O   . LYS A 1 125  ? 40.065 52.368  22.520  1.00 14.74 ? 125  LYS A O   1 
ATOM   822  C  CB  . LYS A 1 125  ? 40.629 49.163  22.063  1.00 15.98 ? 125  LYS A CB  1 
ATOM   823  C  CG  . LYS A 1 125  ? 40.772 47.820  22.748  1.00 21.16 ? 125  LYS A CG  1 
ATOM   824  C  CD  . LYS A 1 125  ? 42.174 47.333  22.579  1.00 23.38 ? 125  LYS A CD  1 
ATOM   825  C  CE  . LYS A 1 125  ? 42.470 46.029  23.326  1.00 29.29 ? 125  LYS A CE  1 
ATOM   826  N  NZ  . LYS A 1 125  ? 41.536 44.956  22.998  1.00 29.27 ? 125  LYS A NZ  1 
ATOM   827  N  N   . PHE A 1 126  ? 41.560 51.850  20.874  1.00 13.02 ? 126  PHE A N   1 
ATOM   828  C  CA  . PHE A 1 126  ? 41.250 53.069  20.115  1.00 12.24 ? 126  PHE A CA  1 
ATOM   829  C  C   . PHE A 1 126  ? 41.727 52.814  18.664  1.00 12.27 ? 126  PHE A C   1 
ATOM   830  O  O   . PHE A 1 126  ? 42.768 52.214  18.455  1.00 13.61 ? 126  PHE A O   1 
ATOM   831  C  CB  . PHE A 1 126  ? 42.013 54.262  20.753  1.00 13.59 ? 126  PHE A CB  1 
ATOM   832  C  CG  . PHE A 1 126  ? 41.624 55.625  20.237  1.00 12.20 ? 126  PHE A CG  1 
ATOM   833  C  CD1 . PHE A 1 126  ? 40.305 56.061  20.249  1.00 13.91 ? 126  PHE A CD1 1 
ATOM   834  C  CD2 . PHE A 1 126  ? 42.649 56.541  19.875  1.00 12.29 ? 126  PHE A CD2 1 
ATOM   835  C  CE1 . PHE A 1 126  ? 39.979 57.403  19.910  1.00 12.91 ? 126  PHE A CE1 1 
ATOM   836  C  CE2 . PHE A 1 126  ? 42.350 57.862  19.534  1.00 13.14 ? 126  PHE A CE2 1 
ATOM   837  C  CZ  . PHE A 1 126  ? 41.032 58.306  19.542  1.00 12.64 ? 126  PHE A CZ  1 
ATOM   838  N  N   . ILE A 1 127  ? 40.941 53.276  17.698  1.00 11.69 ? 127  ILE A N   1 
ATOM   839  C  CA  . ILE A 1 127  ? 41.382 53.139  16.300  1.00 11.20 ? 127  ILE A CA  1 
ATOM   840  C  C   . ILE A 1 127  ? 41.637 54.523  15.740  1.00 12.51 ? 127  ILE A C   1 
ATOM   841  O  O   . ILE A 1 127  ? 41.013 55.504  16.170  1.00 13.27 ? 127  ILE A O   1 
ATOM   842  C  CB  . ILE A 1 127  ? 40.358 52.392  15.396  1.00 12.74 ? 127  ILE A CB  1 
ATOM   843  C  CG1 . ILE A 1 127  ? 38.945 53.007  15.442  1.00 11.93 ? 127  ILE A CG1 1 
ATOM   844  C  CG2 . ILE A 1 127  ? 40.350 50.908  15.813  1.00 13.72 ? 127  ILE A CG2 1 
ATOM   845  C  CD1 . ILE A 1 127  ? 37.983 52.411  14.331  1.00 14.26 ? 127  ILE A CD1 1 
ATOM   846  N  N   . TRP A 1 128  ? 42.578 54.601  14.804  1.00 12.40 ? 128  TRP A N   1 
ATOM   847  C  CA  . TRP A 1 128  ? 42.964 55.871  14.202  1.00 12.80 ? 128  TRP A CA  1 
ATOM   848  C  C   . TRP A 1 128  ? 43.087 55.743  12.689  1.00 12.31 ? 128  TRP A C   1 
ATOM   849  O  O   . TRP A 1 128  ? 43.777 54.836  12.215  1.00 12.41 ? 128  TRP A O   1 
ATOM   850  C  CB  . TRP A 1 128  ? 44.295 56.356  14.774  1.00 12.33 ? 128  TRP A CB  1 
ATOM   851  C  CG  . TRP A 1 128  ? 44.595 57.775  14.430  1.00 12.81 ? 128  TRP A CG  1 
ATOM   852  C  CD1 . TRP A 1 128  ? 45.316 58.268  13.349  1.00 13.06 ? 128  TRP A CD1 1 
ATOM   853  C  CD2 . TRP A 1 128  ? 44.022 58.903  15.072  1.00 11.15 ? 128  TRP A CD2 1 
ATOM   854  N  NE1 . TRP A 1 128  ? 45.204 59.638  13.309  1.00 11.81 ? 128  TRP A NE1 1 
ATOM   855  C  CE2 . TRP A 1 128  ? 44.412 60.050  14.356  1.00 12.04 ? 128  TRP A CE2 1 
ATOM   856  C  CE3 . TRP A 1 128  ? 43.186 59.054  16.214  1.00 11.26 ? 128  TRP A CE3 1 
ATOM   857  C  CZ2 . TRP A 1 128  ? 44.014 61.327  14.729  1.00 13.00 ? 128  TRP A CZ2 1 
ATOM   858  C  CZ3 . TRP A 1 128  ? 42.791 60.305  16.575  1.00 12.54 ? 128  TRP A CZ3 1 
ATOM   859  C  CH2 . TRP A 1 128  ? 43.206 61.444  15.829  1.00 14.08 ? 128  TRP A CH2 1 
ATOM   860  N  N   . ALA A 1 129  ? 42.474 56.694  11.977  1.00 13.16 ? 129  ALA A N   1 
ATOM   861  C  CA  . ALA A 1 129  ? 42.471 56.649  10.514  1.00 13.37 ? 129  ALA A CA  1 
ATOM   862  C  C   . ALA A 1 129  ? 43.377 57.613  9.771   1.00 12.42 ? 129  ALA A C   1 
ATOM   863  O  O   . ALA A 1 129  ? 43.966 57.217  8.774   1.00 14.25 ? 129  ALA A O   1 
ATOM   864  C  CB  . ALA A 1 129  ? 41.032 56.900  10.003  1.00 14.33 ? 129  ALA A CB  1 
ATOM   865  N  N   . GLU A 1 130  ? 43.447 58.862  10.204  1.00 12.60 ? 130  GLU A N   1 
ATOM   866  C  CA  . GLU A 1 130  ? 44.113 59.926  9.416   1.00 12.88 ? 130  GLU A CA  1 
ATOM   867  C  C   . GLU A 1 130  ? 45.579 60.052  9.745   1.00 13.35 ? 130  GLU A C   1 
ATOM   868  O  O   . GLU A 1 130  ? 45.972 60.681  10.739  1.00 12.50 ? 130  GLU A O   1 
ATOM   869  C  CB  . GLU A 1 130  ? 43.358 61.243  9.657   1.00 15.08 ? 130  GLU A CB  1 
ATOM   870  C  CG  . GLU A 1 130  ? 41.844 61.163  9.353   1.00 13.53 ? 130  GLU A CG  1 
ATOM   871  C  CD  . GLU A 1 130  ? 40.990 60.719  10.551  1.00 17.98 ? 130  GLU A CD  1 
ATOM   872  O  OE1 . GLU A 1 130  ? 41.541 60.453  11.641  1.00 16.77 ? 130  GLU A OE1 1 
ATOM   873  O  OE2 . GLU A 1 130  ? 39.763 60.641  10.382  1.00 18.29 ? 130  GLU A OE2 1 
ATOM   874  N  N   . ILE A 1 131  ? 46.428 59.511  8.874   1.00 11.91 ? 131  ILE A N   1 
ATOM   875  C  CA  . ILE A 1 131  ? 47.855 59.539  9.165   1.00 12.53 ? 131  ILE A CA  1 
ATOM   876  C  C   . ILE A 1 131  ? 48.480 60.922  9.011   1.00 13.56 ? 131  ILE A C   1 
ATOM   877  O  O   . ILE A 1 131  ? 49.496 61.196  9.672   1.00 15.09 ? 131  ILE A O   1 
ATOM   878  C  CB  . ILE A 1 131  ? 48.590 58.458  8.323   1.00 13.09 ? 131  ILE A CB  1 
ATOM   879  C  CG1 . ILE A 1 131  ? 47.936 57.097  8.606   1.00 12.01 ? 131  ILE A CG1 1 
ATOM   880  C  CG2 . ILE A 1 131  ? 50.072 58.401  8.680   1.00 14.38 ? 131  ILE A CG2 1 
ATOM   881  C  CD1 . ILE A 1 131  ? 47.738 56.720  10.121  1.00 15.25 ? 131  ILE A CD1 1 
ATOM   882  N  N   . SER A 1 132  ? 47.898 61.814  8.223   1.00 11.03 ? 132  SER A N   1 
ATOM   883  C  CA  . SER A 1 132  ? 48.440 63.173  8.140   1.00 10.90 ? 132  SER A CA  1 
ATOM   884  C  C   . SER A 1 132  ? 48.530 63.773  9.559   1.00 13.43 ? 132  SER A C   1 
ATOM   885  O  O   . SER A 1 132  ? 49.579 64.353  9.928   1.00 13.85 ? 132  SER A O   1 
ATOM   886  C  CB  . SER A 1 132  ? 47.524 64.050  7.275   1.00 11.54 ? 132  SER A CB  1 
ATOM   887  O  OG  . SER A 1 132  ? 46.163 64.005  7.722   1.00 12.82 ? 132  SER A OG  1 
ATOM   888  N  N   . TYR A 1 133  ? 47.464 63.600  10.365  1.00 11.70 ? 133  TYR A N   1 
ATOM   889  C  CA  . TYR A 1 133  ? 47.455 64.120  11.728  1.00 13.32 ? 133  TYR A CA  1 
ATOM   890  C  C   . TYR A 1 133  ? 48.390 63.308  12.597  1.00 12.46 ? 133  TYR A C   1 
ATOM   891  O  O   . TYR A 1 133  ? 49.073 63.909  13.448  1.00 13.45 ? 133  TYR A O   1 
ATOM   892  C  CB  . TYR A 1 133  ? 46.076 64.023  12.375  1.00 13.13 ? 133  TYR A CB  1 
ATOM   893  C  CG  . TYR A 1 133  ? 45.167 65.179  12.053  1.00 11.41 ? 133  TYR A CG  1 
ATOM   894  C  CD1 . TYR A 1 133  ? 45.548 66.495  12.312  1.00 12.70 ? 133  TYR A CD1 1 
ATOM   895  C  CD2 . TYR A 1 133  ? 43.911 64.952  11.478  1.00 11.29 ? 133  TYR A CD2 1 
ATOM   896  C  CE1 . TYR A 1 133  ? 44.695 67.547  12.023  1.00 12.80 ? 133  TYR A CE1 1 
ATOM   897  C  CE2 . TYR A 1 133  ? 43.031 65.990  11.178  1.00 11.22 ? 133  TYR A CE2 1 
ATOM   898  C  CZ  . TYR A 1 133  ? 43.441 67.294  11.458  1.00 12.49 ? 133  TYR A CZ  1 
ATOM   899  O  OH  . TYR A 1 133  ? 42.621 68.345  11.176  1.00 14.29 ? 133  TYR A OH  1 
ATOM   900  N  N   . PHE A 1 134  ? 48.434 61.988  12.431  1.00 11.40 ? 134  PHE A N   1 
ATOM   901  C  CA  . PHE A 1 134  ? 49.280 61.192  13.306  1.00 12.89 ? 134  PHE A CA  1 
ATOM   902  C  C   . PHE A 1 134  ? 50.760 61.508  13.090  1.00 13.58 ? 134  PHE A C   1 
ATOM   903  O  O   . PHE A 1 134  ? 51.535 61.641  14.071  1.00 15.28 ? 134  PHE A O   1 
ATOM   904  C  CB  . PHE A 1 134  ? 49.014 59.689  13.119  1.00 12.41 ? 134  PHE A CB  1 
ATOM   905  C  CG  . PHE A 1 134  ? 49.566 58.866  14.252  1.00 13.61 ? 134  PHE A CG  1 
ATOM   906  C  CD1 . PHE A 1 134  ? 48.838 58.666  15.446  1.00 13.59 ? 134  PHE A CD1 1 
ATOM   907  C  CD2 . PHE A 1 134  ? 50.841 58.367  14.154  1.00 15.33 ? 134  PHE A CD2 1 
ATOM   908  C  CE1 . PHE A 1 134  ? 49.440 57.946  16.522  1.00 13.18 ? 134  PHE A CE1 1 
ATOM   909  C  CE2 . PHE A 1 134  ? 51.435 57.656  15.198  1.00 16.26 ? 134  PHE A CE2 1 
ATOM   910  C  CZ  . PHE A 1 134  ? 50.714 57.449  16.387  1.00 14.39 ? 134  PHE A CZ  1 
ATOM   911  N  N   . ALA A 1 135  ? 51.154 61.707  11.820  1.00 14.33 ? 135  ALA A N   1 
ATOM   912  C  CA  . ALA A 1 135  ? 52.545 62.005  11.517  1.00 14.90 ? 135  ALA A CA  1 
ATOM   913  C  C   . ALA A 1 135  ? 52.867 63.419  12.059  1.00 15.22 ? 135  ALA A C   1 
ATOM   914  O  O   . ALA A 1 135  ? 53.978 63.626  12.597  1.00 18.97 ? 135  ALA A O   1 
ATOM   915  C  CB  . ALA A 1 135  ? 52.781 61.917  10.018  1.00 16.08 ? 135  ALA A CB  1 
ATOM   916  N  N   . ARG A 1 136  ? 51.936 64.358  11.952  1.00 14.90 ? 136  ARG A N   1 
ATOM   917  C  CA  . ARG A 1 136  ? 52.154 65.726  12.457  1.00 15.88 ? 136  ARG A CA  1 
ATOM   918  C  C   . ARG A 1 136  ? 52.411 65.689  13.979  1.00 18.46 ? 136  ARG A C   1 
ATOM   919  O  O   . ARG A 1 136  ? 53.237 66.442  14.508  1.00 20.79 ? 136  ARG A O   1 
ATOM   920  C  CB  . ARG A 1 136  ? 50.926 66.599  12.138  1.00 16.66 ? 136  ARG A CB  1 
ATOM   921  C  CG  . ARG A 1 136  ? 50.915 67.981  12.819  1.00 16.97 ? 136  ARG A CG  1 
ATOM   922  C  CD  . ARG A 1 136  ? 51.809 68.980  12.090  1.00 19.41 ? 136  ARG A CD  1 
ATOM   923  N  NE  . ARG A 1 136  ? 51.753 70.293  12.756  1.00 19.00 ? 136  ARG A NE  1 
ATOM   924  C  CZ  . ARG A 1 136  ? 52.508 70.588  13.809  1.00 19.45 ? 136  ARG A CZ  1 
ATOM   925  N  NH1 . ARG A 1 136  ? 53.358 69.669  14.272  1.00 20.42 ? 136  ARG A NH1 1 
ATOM   926  N  NH2 . ARG A 1 136  ? 52.390 71.783  14.396  1.00 19.04 ? 136  ARG A NH2 1 
ATOM   927  N  N   . PHE A 1 137  ? 51.702 64.800  14.672  1.00 16.74 ? 137  PHE A N   1 
ATOM   928  C  CA  . PHE A 1 137  ? 51.810 64.635  16.111  1.00 15.60 ? 137  PHE A CA  1 
ATOM   929  C  C   . PHE A 1 137  ? 53.088 63.914  16.516  1.00 17.02 ? 137  PHE A C   1 
ATOM   930  O  O   . PHE A 1 137  ? 53.865 64.403  17.374  1.00 17.20 ? 137  PHE A O   1 
ATOM   931  C  CB  . PHE A 1 137  ? 50.627 63.807  16.590  1.00 15.97 ? 137  PHE A CB  1 
ATOM   932  C  CG  . PHE A 1 137  ? 50.623 63.550  18.074  1.00 16.91 ? 137  PHE A CG  1 
ATOM   933  C  CD1 . PHE A 1 137  ? 50.322 64.585  18.949  1.00 18.81 ? 137  PHE A CD1 1 
ATOM   934  C  CD2 . PHE A 1 137  ? 50.956 62.291  18.565  1.00 19.32 ? 137  PHE A CD2 1 
ATOM   935  C  CE1 . PHE A 1 137  ? 50.346 64.387  20.325  1.00 18.76 ? 137  PHE A CE1 1 
ATOM   936  C  CE2 . PHE A 1 137  ? 51.004 62.074  19.983  1.00 19.26 ? 137  PHE A CE2 1 
ATOM   937  C  CZ  . PHE A 1 137  ? 50.690 63.137  20.836  1.00 17.33 ? 137  PHE A CZ  1 
ATOM   938  N  N   . TYR A 1 138  ? 53.332 62.769  15.888  1.00 17.68 ? 138  TYR A N   1 
ATOM   939  C  CA  . TYR A 1 138  ? 54.473 61.924  16.213  1.00 19.99 ? 138  TYR A CA  1 
ATOM   940  C  C   . TYR A 1 138  ? 55.837 62.596  16.074  1.00 21.46 ? 138  TYR A C   1 
ATOM   941  O  O   . TYR A 1 138  ? 56.741 62.366  16.902  1.00 21.70 ? 138  TYR A O   1 
ATOM   942  C  CB  A TYR A 1 138  ? 54.424 60.644  15.369  0.50 20.27 ? 138  TYR A CB  1 
ATOM   943  C  CB  B TYR A 1 138  ? 54.563 60.766  15.173  0.50 20.46 ? 138  TYR A CB  1 
ATOM   944  C  CG  A TYR A 1 138  ? 55.402 59.578  15.813  0.50 17.95 ? 138  TYR A CG  1 
ATOM   945  C  CG  B TYR A 1 138  ? 55.736 59.830  15.423  0.50 18.88 ? 138  TYR A CG  1 
ATOM   946  C  CD1 A TYR A 1 138  ? 55.094 58.710  16.862  0.50 17.63 ? 138  TYR A CD1 1 
ATOM   947  C  CD1 B TYR A 1 138  ? 55.619 58.768  16.313  0.50 18.82 ? 138  TYR A CD1 1 
ATOM   948  C  CD2 A TYR A 1 138  ? 56.620 59.428  15.166  0.50 17.18 ? 138  TYR A CD2 1 
ATOM   949  C  CD2 B TYR A 1 138  ? 56.947 59.995  14.746  0.50 18.15 ? 138  TYR A CD2 1 
ATOM   950  C  CE1 A TYR A 1 138  ? 55.989 57.708  17.252  0.50 16.72 ? 138  TYR A CE1 1 
ATOM   951  C  CE1 B TYR A 1 138  ? 56.688 57.884  16.527  0.50 19.69 ? 138  TYR A CE1 1 
ATOM   952  C  CE2 A TYR A 1 138  ? 57.524 58.432  15.540  0.50 16.13 ? 138  TYR A CE2 1 
ATOM   953  C  CE2 B TYR A 1 138  ? 58.017 59.105  14.953  0.50 17.47 ? 138  TYR A CE2 1 
ATOM   954  C  CZ  A TYR A 1 138  ? 57.197 57.576  16.581  0.50 16.27 ? 138  TYR A CZ  1 
ATOM   955  C  CZ  B TYR A 1 138  ? 57.871 58.069  15.839  0.50 19.91 ? 138  TYR A CZ  1 
ATOM   956  O  OH  A TYR A 1 138  ? 58.074 56.571  16.924  0.50 18.02 ? 138  TYR A OH  1 
ATOM   957  O  OH  B TYR A 1 138  ? 58.917 57.206  16.048  0.50 21.67 ? 138  TYR A OH  1 
ATOM   958  N  N   . HIS A 1 139  ? 56.010 63.419  15.052  1.00 22.57 ? 139  HIS A N   1 
ATOM   959  C  CA  . HIS A 1 139  ? 57.268 64.088  14.858  1.00 25.51 ? 139  HIS A CA  1 
ATOM   960  C  C   . HIS A 1 139  ? 57.543 65.180  15.863  1.00 26.88 ? 139  HIS A C   1 
ATOM   961  O  O   . HIS A 1 139  ? 58.690 65.637  15.982  1.00 29.74 ? 139  HIS A O   1 
ATOM   962  C  CB  . HIS A 1 139  ? 57.374 64.545  13.408  1.00 26.22 ? 139  HIS A CB  1 
ATOM   963  C  CG  . HIS A 1 139  ? 57.579 63.403  12.455  1.00 28.13 ? 139  HIS A CG  1 
ATOM   964  N  ND1 . HIS A 1 139  ? 58.677 62.569  12.526  1.00 30.20 ? 139  HIS A ND1 1 
ATOM   965  C  CD2 . HIS A 1 139  ? 56.806 62.930  11.444  1.00 25.15 ? 139  HIS A CD2 1 
ATOM   966  C  CE1 . HIS A 1 139  ? 58.575 61.632  11.598  1.00 30.27 ? 139  HIS A CE1 1 
ATOM   967  N  NE2 . HIS A 1 139  ? 57.452 61.829  10.924  1.00 28.39 ? 139  HIS A NE2 1 
ATOM   968  N  N   . ASP A 1 140  ? 56.510 65.576  16.614  1.00 24.11 ? 140  ASP A N   1 
ATOM   969  C  CA  . ASP A 1 140  ? 56.669 66.568  17.678  1.00 25.50 ? 140  ASP A CA  1 
ATOM   970  C  C   . ASP A 1 140  ? 56.857 65.935  19.065  1.00 22.86 ? 140  ASP A C   1 
ATOM   971  O  O   . ASP A 1 140  ? 57.064 66.637  20.061  1.00 25.71 ? 140  ASP A O   1 
ATOM   972  C  CB  . ASP A 1 140  ? 55.480 67.488  17.713  1.00 25.39 ? 140  ASP A CB  1 
ATOM   973  C  CG  . ASP A 1 140  ? 55.651 68.660  16.758  1.00 29.33 ? 140  ASP A CG  1 
ATOM   974  O  OD1 . ASP A 1 140  ? 56.532 68.570  15.867  1.00 33.44 ? 140  ASP A OD1 1 
ATOM   975  O  OD2 . ASP A 1 140  ? 54.923 69.648  16.900  1.00 30.28 ? 140  ASP A OD2 1 
ATOM   976  N  N   . LEU A 1 141  ? 56.780 64.617  19.132  1.00 23.16 ? 141  LEU A N   1 
ATOM   977  C  CA  . LEU A 1 141  ? 56.969 63.906  20.393  1.00 22.13 ? 141  LEU A CA  1 
ATOM   978  C  C   . LEU A 1 141  ? 58.422 63.683  20.749  1.00 23.94 ? 141  LEU A C   1 
ATOM   979  O  O   . LEU A 1 141  ? 59.263 63.502  19.884  1.00 24.27 ? 141  LEU A O   1 
ATOM   980  C  CB  . LEU A 1 141  ? 56.358 62.503  20.340  1.00 23.46 ? 141  LEU A CB  1 
ATOM   981  C  CG  . LEU A 1 141  ? 54.848 62.309  20.324  1.00 25.91 ? 141  LEU A CG  1 
ATOM   982  C  CD1 . LEU A 1 141  ? 54.546 60.791  20.331  1.00 22.77 ? 141  LEU A CD1 1 
ATOM   983  C  CD2 . LEU A 1 141  ? 54.215 62.998  21.545  1.00 25.28 ? 141  LEU A CD2 1 
ATOM   984  N  N   . GLY A 1 142  ? 58.700 63.654  22.049  1.00 23.88 ? 142  GLY A N   1 
ATOM   985  C  CA  . GLY A 1 142  ? 60.053 63.354  22.487  1.00 26.78 ? 142  GLY A CA  1 
ATOM   986  C  C   . GLY A 1 142  ? 60.224 61.843  22.373  1.00 26.02 ? 142  GLY A C   1 
ATOM   987  O  O   . GLY A 1 142  ? 59.219 61.107  22.285  1.00 27.02 ? 142  GLY A O   1 
ATOM   988  N  N   . GLU A 1 143  ? 61.462 61.371  22.399  1.00 27.14 ? 143  GLU A N   1 
ATOM   989  C  CA  . GLU A 1 143  ? 61.762 59.954  22.259  1.00 27.55 ? 143  GLU A CA  1 
ATOM   990  C  C   . GLU A 1 143  ? 61.053 59.080  23.285  1.00 26.94 ? 143  GLU A C   1 
ATOM   991  O  O   . GLU A 1 143  ? 60.582 57.989  22.976  1.00 26.18 ? 143  GLU A O   1 
ATOM   992  C  CB  . GLU A 1 143  ? 63.275 59.742  22.338  1.00 30.83 ? 143  GLU A CB  1 
ATOM   993  C  CG  . GLU A 1 143  ? 63.765 58.352  21.920  1.00 34.95 ? 143  GLU A CG  1 
ATOM   994  C  CD  . GLU A 1 143  ? 63.372 57.978  20.489  1.00 39.95 ? 143  GLU A CD  1 
ATOM   995  O  OE1 . GLU A 1 143  ? 63.464 58.849  19.581  1.00 43.18 ? 143  GLU A OE1 1 
ATOM   996  O  OE2 . GLU A 1 143  ? 62.975 56.806  20.278  1.00 43.67 ? 143  GLU A OE2 1 
ATOM   997  N  N   . ASN A 1 144  ? 60.959 59.548  24.510  1.00 26.64 ? 144  ASN A N   1 
ATOM   998  C  CA  . ASN A 1 144  ? 60.304 58.750  25.533  1.00 29.63 ? 144  ASN A CA  1 
ATOM   999  C  C   . ASN A 1 144  ? 58.847 58.424  25.100  1.00 26.47 ? 144  ASN A C   1 
ATOM   1000 O  O   . ASN A 1 144  ? 58.408 57.269  25.152  1.00 26.11 ? 144  ASN A O   1 
ATOM   1001 C  CB  . ASN A 1 144  ? 60.410 59.536  26.855  1.00 32.80 ? 144  ASN A CB  1 
ATOM   1002 C  CG  . ASN A 1 144  ? 59.546 58.982  27.962  1.00 41.59 ? 144  ASN A CG  1 
ATOM   1003 O  OD1 . ASN A 1 144  ? 58.383 59.396  28.133  1.00 46.11 ? 144  ASN A OD1 1 
ATOM   1004 N  ND2 . ASN A 1 144  ? 60.102 58.040  28.740  1.00 44.60 ? 144  ASN A ND2 1 
ATOM   1005 N  N   . LYS A 1 145  ? 58.127 59.435  24.634  1.00 25.70 ? 145  LYS A N   1 
ATOM   1006 C  CA  . LYS A 1 145  ? 56.745 59.243  24.220  1.00 24.22 ? 145  LYS A CA  1 
ATOM   1007 C  C   . LYS A 1 145  ? 56.646 58.470  22.909  1.00 23.09 ? 145  LYS A C   1 
ATOM   1008 O  O   . LYS A 1 145  ? 55.688 57.717  22.732  1.00 21.55 ? 145  LYS A O   1 
ATOM   1009 C  CB  . LYS A 1 145  ? 56.025 60.585  24.094  1.00 24.80 ? 145  LYS A CB  1 
ATOM   1010 C  CG  . LYS A 1 145  ? 55.819 61.300  25.425  1.00 27.98 ? 145  LYS A CG  1 
ATOM   1011 C  CD  . LYS A 1 145  ? 54.682 60.675  26.194  1.00 33.09 ? 145  LYS A CD  1 
ATOM   1012 C  CE  . LYS A 1 145  ? 54.370 61.440  27.477  1.00 37.96 ? 145  LYS A CE  1 
ATOM   1013 N  NZ  . LYS A 1 145  ? 55.343 61.118  28.553  1.00 40.78 ? 145  LYS A NZ  1 
ATOM   1014 N  N   . LYS A 1 146  ? 57.603 58.661  21.996  1.00 24.09 ? 146  LYS A N   1 
ATOM   1015 C  CA  . LYS A 1 146  ? 57.574 57.909  20.734  1.00 23.67 ? 146  LYS A CA  1 
ATOM   1016 C  C   . LYS A 1 146  ? 57.628 56.435  21.087  1.00 23.18 ? 146  LYS A C   1 
ATOM   1017 O  O   . LYS A 1 146  ? 56.913 55.612  20.516  1.00 21.31 ? 146  LYS A O   1 
ATOM   1018 C  CB  . LYS A 1 146  ? 58.750 58.255  19.810  1.00 21.62 ? 146  LYS A CB  1 
ATOM   1019 C  CG  . LYS A 1 146  ? 58.657 59.595  19.125  1.00 20.91 ? 146  LYS A CG  1 
ATOM   1020 C  CD  . LYS A 1 146  ? 59.861 59.846  18.209  1.00 21.83 ? 146  LYS A CD  1 
ATOM   1021 C  CE  . LYS A 1 146  ? 59.657 61.110  17.377  1.00 24.73 ? 146  LYS A CE  1 
ATOM   1022 N  NZ  . LYS A 1 146  ? 60.898 61.495  16.725  1.00 30.16 ? 146  LYS A NZ  1 
ATOM   1023 N  N   . LEU A 1 147  ? 58.462 56.090  22.058  1.00 23.94 ? 147  LEU A N   1 
ATOM   1024 C  CA  . LEU A 1 147  ? 58.590 54.699  22.479  1.00 23.41 ? 147  LEU A CA  1 
ATOM   1025 C  C   . LEU A 1 147  ? 57.297 54.179  23.134  1.00 21.86 ? 147  LEU A C   1 
ATOM   1026 O  O   . LEU A 1 147  ? 56.879 53.040  22.867  1.00 21.83 ? 147  LEU A O   1 
ATOM   1027 C  CB  . LEU A 1 147  ? 59.783 54.560  23.442  1.00 24.54 ? 147  LEU A CB  1 
ATOM   1028 C  CG  . LEU A 1 147  ? 61.154 54.674  22.771  1.00 26.97 ? 147  LEU A CG  1 
ATOM   1029 C  CD1 . LEU A 1 147  ? 62.177 54.609  23.906  1.00 28.81 ? 147  LEU A CD1 1 
ATOM   1030 C  CD2 . LEU A 1 147  ? 61.410 53.552  21.763  1.00 28.13 ? 147  LEU A CD2 1 
ATOM   1031 N  N   . GLN A 1 148  ? 56.673 54.997  23.981  1.00 20.55 ? 148  GLN A N   1 
ATOM   1032 C  CA  . GLN A 1 148  ? 55.415 54.589  24.604  1.00 21.52 ? 148  GLN A CA  1 
ATOM   1033 C  C   . GLN A 1 148  ? 54.369 54.399  23.494  1.00 20.17 ? 148  GLN A C   1 
ATOM   1034 O  O   . GLN A 1 148  ? 53.578 53.470  23.551  1.00 21.82 ? 148  GLN A O   1 
ATOM   1035 C  CB  . GLN A 1 148  ? 54.906 55.655  25.557  1.00 25.47 ? 148  GLN A CB  1 
ATOM   1036 C  CG  . GLN A 1 148  ? 55.646 55.730  26.847  1.00 32.49 ? 148  GLN A CG  1 
ATOM   1037 C  CD  . GLN A 1 148  ? 54.946 56.651  27.826  1.00 35.97 ? 148  GLN A CD  1 
ATOM   1038 O  OE1 . GLN A 1 148  ? 55.247 56.636  29.035  1.00 40.36 ? 148  GLN A OE1 1 
ATOM   1039 N  NE2 . GLN A 1 148  ? 54.014 57.470  27.320  1.00 36.65 ? 148  GLN A NE2 1 
ATOM   1040 N  N   . MET A 1 149  ? 54.386 55.288  22.509  1.00 20.21 ? 149  MET A N   1 
ATOM   1041 C  CA  . MET A 1 149  ? 53.406 55.175  21.420  1.00 20.39 ? 149  MET A CA  1 
ATOM   1042 C  C   . MET A 1 149  ? 53.618 53.890  20.644  1.00 20.22 ? 149  MET A C   1 
ATOM   1043 O  O   . MET A 1 149  ? 52.657 53.153  20.368  1.00 19.12 ? 149  MET A O   1 
ATOM   1044 C  CB  . MET A 1 149  ? 53.526 56.366  20.479  1.00 18.69 ? 149  MET A CB  1 
ATOM   1045 C  CG  . MET A 1 149  ? 52.481 56.371  19.348  1.00 19.31 ? 149  MET A CG  1 
ATOM   1046 S  SD  . MET A 1 149  ? 50.797 56.627  19.956  1.00 21.11 ? 149  MET A SD  1 
ATOM   1047 C  CE  . MET A 1 149  ? 50.682 58.398  20.004  1.00 25.01 ? 149  MET A CE  1 
ATOM   1048 N  N   . LYS A 1 150  ? 54.871 53.608  20.291  1.00 19.47 ? 150  LYS A N   1 
ATOM   1049 C  CA  . LYS A 1 150  ? 55.134 52.396  19.543  1.00 20.34 ? 150  LYS A CA  1 
ATOM   1050 C  C   . LYS A 1 150  ? 54.681 51.178  20.323  1.00 18.96 ? 150  LYS A C   1 
ATOM   1051 O  O   . LYS A 1 150  ? 54.223 50.203  19.739  1.00 21.21 ? 150  LYS A O   1 
ATOM   1052 C  CB  . LYS A 1 150  ? 56.620 52.268  19.183  1.00 20.40 ? 150  LYS A CB  1 
ATOM   1053 C  CG  . LYS A 1 150  ? 57.031 53.258  18.101  1.00 24.76 ? 150  LYS A CG  1 
ATOM   1054 C  CD  . LYS A 1 150  ? 58.421 53.000  17.598  1.00 31.12 ? 150  LYS A CD  1 
ATOM   1055 C  CE  . LYS A 1 150  ? 59.445 53.655  18.473  1.00 36.21 ? 150  LYS A CE  1 
ATOM   1056 N  NZ  . LYS A 1 150  ? 60.769 53.690  17.766  1.00 38.00 ? 150  LYS A NZ  1 
ATOM   1057 N  N   . SER A 1 151  ? 54.784 51.240  21.648  1.00 21.39 ? 151  SER A N   1 
ATOM   1058 C  CA  . SER A 1 151  ? 54.386 50.122  22.491  1.00 22.09 ? 151  SER A CA  1 
ATOM   1059 C  C   . SER A 1 151  ? 52.871 49.858  22.495  1.00 20.36 ? 151  SER A C   1 
ATOM   1060 O  O   . SER A 1 151  ? 52.464 48.707  22.421  1.00 20.72 ? 151  SER A O   1 
ATOM   1061 C  CB  . SER A 1 151  ? 54.898 50.323  23.931  1.00 23.18 ? 151  SER A CB  1 
ATOM   1062 O  OG  A SER A 1 151  ? 54.113 51.266  24.633  0.50 24.49 ? 151  SER A OG  1 
ATOM   1063 O  OG  B SER A 1 151  ? 54.746 49.088  24.625  0.50 23.02 ? 151  SER A OG  1 
ATOM   1064 N  N   . ILE A 1 152  ? 52.041 50.904  22.567  1.00 19.25 ? 152  ILE A N   1 
ATOM   1065 C  CA  . ILE A 1 152  ? 50.599 50.674  22.566  1.00 18.16 ? 152  ILE A CA  1 
ATOM   1066 C  C   . ILE A 1 152  ? 50.124 50.262  21.164  1.00 17.87 ? 152  ILE A C   1 
ATOM   1067 O  O   . ILE A 1 152  ? 49.059 49.687  21.028  1.00 19.77 ? 152  ILE A O   1 
ATOM   1068 C  CB  . ILE A 1 152  ? 49.755 51.847  23.147  1.00 18.15 ? 152  ILE A CB  1 
ATOM   1069 C  CG1 . ILE A 1 152  ? 50.039 53.167  22.451  1.00 18.46 ? 152  ILE A CG1 1 
ATOM   1070 C  CG2 . ILE A 1 152  ? 50.069 51.983  24.659  1.00 20.50 ? 152  ILE A CG2 1 
ATOM   1071 C  CD1 . ILE A 1 152  ? 48.974 54.245  22.739  1.00 18.53 ? 152  ILE A CD1 1 
ATOM   1072 N  N   . VAL A 1 153  ? 50.928 50.542  20.138  1.00 17.55 ? 153  VAL A N   1 
ATOM   1073 C  CA  . VAL A 1 153  ? 50.569 50.078  18.794  1.00 18.16 ? 153  VAL A CA  1 
ATOM   1074 C  C   . VAL A 1 153  ? 50.991 48.613  18.663  1.00 20.02 ? 153  VAL A C   1 
ATOM   1075 O  O   . VAL A 1 153  ? 50.208 47.763  18.230  1.00 19.48 ? 153  VAL A O   1 
ATOM   1076 C  CB  . VAL A 1 153  ? 51.237 50.953  17.726  1.00 17.68 ? 153  VAL A CB  1 
ATOM   1077 C  CG1 . VAL A 1 153  ? 51.062 50.329  16.319  1.00 18.90 ? 153  VAL A CG1 1 
ATOM   1078 C  CG2 . VAL A 1 153  ? 50.658 52.349  17.811  1.00 16.52 ? 153  VAL A CG2 1 
ATOM   1079 N  N   . LYS A 1 154  ? 52.215 48.305  19.097  1.00 20.14 ? 154  LYS A N   1 
ATOM   1080 C  CA  . LYS A 1 154  ? 52.681 46.929  19.027  1.00 20.49 ? 154  LYS A CA  1 
ATOM   1081 C  C   . LYS A 1 154  ? 51.799 45.972  19.846  1.00 20.35 ? 154  LYS A C   1 
ATOM   1082 O  O   . LYS A 1 154  ? 51.545 44.845  19.401  1.00 23.36 ? 154  LYS A O   1 
ATOM   1083 C  CB  . LYS A 1 154  ? 54.133 46.862  19.501  1.00 23.05 ? 154  LYS A CB  1 
ATOM   1084 C  CG  . LYS A 1 154  ? 54.800 45.530  19.183  1.00 28.78 ? 154  LYS A CG  1 
ATOM   1085 C  CD  . LYS A 1 154  ? 56.253 45.563  19.624  1.00 34.71 ? 154  LYS A CD  1 
ATOM   1086 C  CE  . LYS A 1 154  ? 56.368 45.903  21.116  1.00 40.15 ? 154  LYS A CE  1 
ATOM   1087 N  NZ  . LYS A 1 154  ? 55.648 44.905  21.993  1.00 44.43 ? 154  LYS A NZ  1 
ATOM   1088 N  N   . ASN A 1 155  ? 51.324 46.407  21.017  1.00 21.50 ? 155  ASN A N   1 
ATOM   1089 C  CA  . ASN A 1 155  ? 50.461 45.551  21.858  1.00 21.26 ? 155  ASN A CA  1 
ATOM   1090 C  C   . ASN A 1 155  ? 48.975 45.514  21.436  1.00 22.30 ? 155  ASN A C   1 
ATOM   1091 O  O   . ASN A 1 155  ? 48.153 44.863  22.067  1.00 24.49 ? 155  ASN A O   1 
ATOM   1092 C  CB  . ASN A 1 155  ? 50.577 45.904  23.367  1.00 25.48 ? 155  ASN A CB  1 
ATOM   1093 C  CG  . ASN A 1 155  ? 49.743 47.138  23.789  1.00 25.82 ? 155  ASN A CG  1 
ATOM   1094 O  OD1 . ASN A 1 155  ? 49.017 47.708  22.989  1.00 27.55 ? 155  ASN A OD1 1 
ATOM   1095 N  ND2 . ASN A 1 155  ? 49.858 47.550  25.060  1.00 25.48 ? 155  ASN A ND2 1 
ATOM   1096 N  N   . GLY A 1 156  ? 48.648 46.246  20.378  1.00 19.13 ? 156  GLY A N   1 
ATOM   1097 C  CA  . GLY A 1 156  ? 47.289 46.216  19.858  1.00 19.77 ? 156  GLY A CA  1 
ATOM   1098 C  C   . GLY A 1 156  ? 46.247 47.133  20.459  1.00 19.59 ? 156  GLY A C   1 
ATOM   1099 O  O   . GLY A 1 156  ? 45.090 47.051  20.072  1.00 19.78 ? 156  GLY A O   1 
ATOM   1100 N  N   . GLN A 1 157  ? 46.626 48.032  21.363  1.00 14.51 ? 157  GLN A N   1 
ATOM   1101 C  CA  . GLN A 1 157  ? 45.619 48.888  21.955  1.00 15.42 ? 157  GLN A CA  1 
ATOM   1102 C  C   . GLN A 1 157  ? 45.222 50.017  20.999  1.00 14.21 ? 157  GLN A C   1 
ATOM   1103 O  O   . GLN A 1 157  ? 44.054 50.361  20.912  1.00 14.72 ? 157  GLN A O   1 
ATOM   1104 C  CB  . GLN A 1 157  ? 46.135 49.496  23.241  1.00 15.78 ? 157  GLN A CB  1 
ATOM   1105 C  CG  . GLN A 1 157  ? 46.035 48.579  24.442  1.00 16.41 ? 157  GLN A CG  1 
ATOM   1106 C  CD  . GLN A 1 157  ? 46.385 49.353  25.705  1.00 16.35 ? 157  GLN A CD  1 
ATOM   1107 O  OE1 . GLN A 1 157  ? 45.561 50.068  26.287  1.00 19.53 ? 157  GLN A OE1 1 
ATOM   1108 N  NE2 . GLN A 1 157  ? 47.627 49.276  26.070  1.00 14.68 ? 157  GLN A NE2 1 
ATOM   1109 N  N   . LEU A 1 158  ? 46.214 50.610  20.335  1.00 15.70 ? 158  LEU A N   1 
ATOM   1110 C  CA  . LEU A 1 158  ? 45.944 51.660  19.357  1.00 14.89 ? 158  LEU A CA  1 
ATOM   1111 C  C   . LEU A 1 158  ? 46.165 50.959  18.019  1.00 15.47 ? 158  LEU A C   1 
ATOM   1112 O  O   A LEU A 1 158  ? 47.206 50.354  17.768  0.50 15.43 ? 158  LEU A O   1 
ATOM   1113 O  O   B LEU A 1 158  ? 47.293 50.583  17.668  0.50 15.12 ? 158  LEU A O   1 
ATOM   1114 C  CB  . LEU A 1 158  ? 46.905 52.839  19.555  1.00 17.21 ? 158  LEU A CB  1 
ATOM   1115 C  CG  A LEU A 1 158  ? 46.695 54.091  18.696  0.50 20.37 ? 158  LEU A CG  1 
ATOM   1116 C  CG  B LEU A 1 158  ? 46.990 53.819  18.421  0.50 15.31 ? 158  LEU A CG  1 
ATOM   1117 C  CD1 A LEU A 1 158  ? 47.852 55.064  18.986  0.50 22.26 ? 158  LEU A CD1 1 
ATOM   1118 C  CD1 B LEU A 1 158  ? 45.671 54.557  18.487  0.50 13.84 ? 158  LEU A CD1 1 
ATOM   1119 C  CD2 A LEU A 1 158  ? 46.689 53.746  17.222  0.50 22.84 ? 158  LEU A CD2 1 
ATOM   1120 C  CD2 B LEU A 1 158  ? 48.192 54.779  18.541  0.50 16.41 ? 158  LEU A CD2 1 
ATOM   1121 N  N   . GLU A 1 159  ? 45.124 50.989  17.198  1.00 13.78 ? 159  GLU A N   1 
ATOM   1122 C  CA  . GLU A 1 159  ? 45.198 50.342  15.888  1.00 14.43 ? 159  GLU A CA  1 
ATOM   1123 C  C   . GLU A 1 159  ? 44.855 51.283  14.765  1.00 12.85 ? 159  GLU A C   1 
ATOM   1124 O  O   . GLU A 1 159  ? 43.835 51.965  14.782  1.00 12.97 ? 159  GLU A O   1 
ATOM   1125 C  CB  . GLU A 1 159  ? 44.230 49.156  15.877  1.00 14.31 ? 159  GLU A CB  1 
ATOM   1126 C  CG  . GLU A 1 159  ? 44.140 48.448  14.547  1.00 15.80 ? 159  GLU A CG  1 
ATOM   1127 C  CD  . GLU A 1 159  ? 43.166 47.293  14.604  1.00 17.16 ? 159  GLU A CD  1 
ATOM   1128 O  OE1 . GLU A 1 159  ? 43.477 46.285  15.315  1.00 16.93 ? 159  GLU A OE1 1 
ATOM   1129 O  OE2 . GLU A 1 159  ? 42.099 47.397  13.958  1.00 14.97 ? 159  GLU A OE2 1 
ATOM   1130 N  N   . PHE A 1 160  ? 45.719 51.281  13.762  1.00 12.92 ? 160  PHE A N   1 
ATOM   1131 C  CA  . PHE A 1 160  ? 45.460 52.110  12.603  1.00 12.04 ? 160  PHE A CA  1 
ATOM   1132 C  C   . PHE A 1 160  ? 44.524 51.387  11.649  1.00 12.98 ? 160  PHE A C   1 
ATOM   1133 O  O   . PHE A 1 160  ? 44.680 50.190  11.354  1.00 13.78 ? 160  PHE A O   1 
ATOM   1134 C  CB  . PHE A 1 160  ? 46.803 52.426  11.933  1.00 13.01 ? 160  PHE A CB  1 
ATOM   1135 C  CG  . PHE A 1 160  ? 47.693 53.260  12.800  1.00 11.49 ? 160  PHE A CG  1 
ATOM   1136 C  CD1 . PHE A 1 160  ? 47.400 54.608  12.994  1.00 13.38 ? 160  PHE A CD1 1 
ATOM   1137 C  CD2 . PHE A 1 160  ? 48.770 52.681  13.484  1.00 14.08 ? 160  PHE A CD2 1 
ATOM   1138 C  CE1 . PHE A 1 160  ? 48.176 55.400  13.872  1.00 13.72 ? 160  PHE A CE1 1 
ATOM   1139 C  CE2 . PHE A 1 160  ? 49.538 53.467  14.346  1.00 14.26 ? 160  PHE A CE2 1 
ATOM   1140 C  CZ  . PHE A 1 160  ? 49.238 54.804  14.534  1.00 14.62 ? 160  PHE A CZ  1 
ATOM   1141 N  N   . VAL A 1 161  ? 43.552 52.146  11.176  1.00 10.80 ? 161  VAL A N   1 
ATOM   1142 C  CA  . VAL A 1 161  ? 42.564 51.651  10.210  1.00 12.27 ? 161  VAL A CA  1 
ATOM   1143 C  C   . VAL A 1 161  ? 42.765 52.445  8.928   1.00 11.49 ? 161  VAL A C   1 
ATOM   1144 O  O   . VAL A 1 161  ? 42.894 53.684  8.944   1.00 13.16 ? 161  VAL A O   1 
ATOM   1145 C  CB  . VAL A 1 161  ? 41.124 51.741  10.775  1.00 11.63 ? 161  VAL A CB  1 
ATOM   1146 C  CG1 . VAL A 1 161  ? 41.026 50.726  11.951  1.00 13.52 ? 161  VAL A CG1 1 
ATOM   1147 C  CG2 . VAL A 1 161  ? 40.802 53.123  11.279  1.00 13.46 ? 161  VAL A CG2 1 
ATOM   1148 N  N   . THR A 1 162  ? 42.830 51.674  7.828   1.00 11.44 ? 162  THR A N   1 
ATOM   1149 C  CA  . THR A 1 162  ? 43.136 52.151  6.447   1.00 12.16 ? 162  THR A CA  1 
ATOM   1150 C  C   . THR A 1 162  ? 44.601 52.602  6.390   1.00 13.00 ? 162  THR A C   1 
ATOM   1151 O  O   . THR A 1 162  ? 45.437 52.020  5.695   1.00 14.16 ? 162  THR A O   1 
ATOM   1152 C  CB  . THR A 1 162  ? 42.267 53.295  5.977   1.00 11.90 ? 162  THR A CB  1 
ATOM   1153 O  OG1 . THR A 1 162  ? 40.900 52.905  6.037   1.00 14.34 ? 162  THR A OG1 1 
ATOM   1154 C  CG2 . THR A 1 162  ? 42.603 53.556  4.475   1.00 13.90 ? 162  THR A CG2 1 
ATOM   1155 N  N   . GLY A 1 163  ? 44.929 53.640  7.145   1.00 12.05 ? 163  GLY A N   1 
ATOM   1156 C  CA  . GLY A 1 163  ? 46.303 54.130  7.164   1.00 12.71 ? 163  GLY A CA  1 
ATOM   1157 C  C   . GLY A 1 163  ? 46.670 55.071  6.049   1.00 12.37 ? 163  GLY A C   1 
ATOM   1158 O  O   . GLY A 1 163  ? 47.838 55.251  5.727   1.00 12.68 ? 163  GLY A O   1 
ATOM   1159 N  N   . GLY A 1 164  ? 45.650 55.648  5.410   1.00 11.44 ? 164  GLY A N   1 
ATOM   1160 C  CA  . GLY A 1 164  ? 45.957 56.636  4.382   1.00 12.38 ? 164  GLY A CA  1 
ATOM   1161 C  C   . GLY A 1 164  ? 46.248 57.976  5.026   1.00 12.18 ? 164  GLY A C   1 
ATOM   1162 O  O   . GLY A 1 164  ? 45.954 58.228  6.203   1.00 11.72 ? 164  GLY A O   1 
ATOM   1163 N  N   . TRP A 1 165  ? 46.854 58.870  4.263   1.00 10.10 ? 165  TRP A N   1 
ATOM   1164 C  CA  . TRP A 1 165  ? 47.112 60.223  4.732   1.00 9.68  ? 165  TRP A CA  1 
ATOM   1165 C  C   . TRP A 1 165  ? 45.790 60.845  5.209   1.00 11.46 ? 165  TRP A C   1 
ATOM   1166 O  O   . TRP A 1 165  ? 45.772 61.584  6.186   1.00 11.30 ? 165  TRP A O   1 
ATOM   1167 C  CB  . TRP A 1 165  ? 47.710 61.042  3.570   1.00 11.42 ? 165  TRP A CB  1 
ATOM   1168 C  CG  . TRP A 1 165  ? 48.552 62.188  4.048   1.00 11.69 ? 165  TRP A CG  1 
ATOM   1169 C  CD1 . TRP A 1 165  ? 48.382 63.515  3.737   1.00 13.39 ? 165  TRP A CD1 1 
ATOM   1170 C  CD2 . TRP A 1 165  ? 49.733 62.113  4.852   1.00 12.92 ? 165  TRP A CD2 1 
ATOM   1171 N  NE1 . TRP A 1 165  ? 49.403 64.271  4.288   1.00 14.27 ? 165  TRP A NE1 1 
ATOM   1172 C  CE2 . TRP A 1 165  ? 50.235 63.433  4.982   1.00 12.50 ? 165  TRP A CE2 1 
ATOM   1173 C  CE3 . TRP A 1 165  ? 50.416 61.057  5.461   1.00 14.17 ? 165  TRP A CE3 1 
ATOM   1174 C  CZ2 . TRP A 1 165  ? 51.421 63.724  5.737   1.00 16.24 ? 165  TRP A CZ2 1 
ATOM   1175 C  CZ3 . TRP A 1 165  ? 51.594 61.344  6.204   1.00 17.43 ? 165  TRP A CZ3 1 
ATOM   1176 C  CH2 . TRP A 1 165  ? 52.067 62.659  6.324   1.00 17.44 ? 165  TRP A CH2 1 
ATOM   1177 N  N   . VAL A 1 166  ? 44.702 60.571  4.484   1.00 9.90  ? 166  VAL A N   1 
ATOM   1178 C  CA  . VAL A 1 166  ? 43.360 61.063  4.815   1.00 11.35 ? 166  VAL A CA  1 
ATOM   1179 C  C   . VAL A 1 166  ? 42.347 59.907  4.625   1.00 11.16 ? 166  VAL A C   1 
ATOM   1180 O  O   . VAL A 1 166  ? 42.738 58.758  4.351   1.00 12.02 ? 166  VAL A O   1 
ATOM   1181 C  CB  . VAL A 1 166  ? 42.926 62.230  3.870   1.00 11.00 ? 166  VAL A CB  1 
ATOM   1182 C  CG1 . VAL A 1 166  ? 43.946 63.344  3.960   1.00 12.52 ? 166  VAL A CG1 1 
ATOM   1183 C  CG2 . VAL A 1 166  ? 42.806 61.731  2.409   1.00 13.46 ? 166  VAL A CG2 1 
ATOM   1184 N  N   . MET A 1 167  ? 41.067 60.222  4.863   1.00 11.19 ? 167  MET A N   1 
ATOM   1185 C  CA  . MET A 1 167  ? 39.943 59.289  4.531   1.00 11.16 ? 167  MET A CA  1 
ATOM   1186 C  C   . MET A 1 167  ? 39.393 60.031  3.293   1.00 11.22 ? 167  MET A C   1 
ATOM   1187 O  O   . MET A 1 167  ? 38.616 60.967  3.387   1.00 12.65 ? 167  MET A O   1 
ATOM   1188 C  CB  . MET A 1 167  ? 38.954 59.290  5.696   1.00 12.71 ? 167  MET A CB  1 
ATOM   1189 C  CG  . MET A 1 167  ? 37.673 58.530  5.371   1.00 11.77 ? 167  MET A CG  1 
ATOM   1190 S  SD  . MET A 1 167  ? 36.506 58.593  6.767   1.00 13.19 ? 167  MET A SD  1 
ATOM   1191 C  CE  . MET A 1 167  ? 37.517 57.864  8.081   1.00 12.75 ? 167  MET A CE  1 
ATOM   1192 N  N   . PRO A 1 168  ? 39.783 59.580  2.109   1.00 10.74 ? 168  PRO A N   1 
ATOM   1193 C  CA  . PRO A 1 168  ? 39.370 60.318  0.929   1.00 10.72 ? 168  PRO A CA  1 
ATOM   1194 C  C   . PRO A 1 168  ? 37.980 60.329  0.460   1.00 9.94  ? 168  PRO A C   1 
ATOM   1195 O  O   . PRO A 1 168  ? 37.222 59.406  0.711   1.00 11.39 ? 168  PRO A O   1 
ATOM   1196 C  CB  . PRO A 1 168  ? 40.303 59.735  -0.164  1.00 11.31 ? 168  PRO A CB  1 
ATOM   1197 C  CG  . PRO A 1 168  ? 40.384 58.312  0.192   1.00 11.87 ? 168  PRO A CG  1 
ATOM   1198 C  CD  . PRO A 1 168  ? 40.615 58.413  1.746   1.00 11.11 ? 168  PRO A CD  1 
ATOM   1199 N  N   . ASP A 1 169  ? 37.655 61.424  -0.231  1.00 10.59 ? 169  ASP A N   1 
ATOM   1200 C  CA  . ASP A 1 169  ? 36.421 61.444  -0.987  1.00 10.59 ? 169  ASP A CA  1 
ATOM   1201 C  C   . ASP A 1 169  ? 36.544 60.272  -1.974  1.00 11.27 ? 169  ASP A C   1 
ATOM   1202 O  O   . ASP A 1 169  ? 37.644 59.939  -2.442  1.00 10.36 ? 169  ASP A O   1 
ATOM   1203 C  CB  . ASP A 1 169  ? 36.379 62.755  -1.771  1.00 9.86  ? 169  ASP A CB  1 
ATOM   1204 C  CG  . ASP A 1 169  ? 35.219 62.797  -2.764  1.00 10.86 ? 169  ASP A CG  1 
ATOM   1205 O  OD1 . ASP A 1 169  ? 34.132 62.277  -2.453  1.00 12.52 ? 169  ASP A OD1 1 
ATOM   1206 O  OD2 . ASP A 1 169  ? 35.389 63.385  -3.844  1.00 13.32 ? 169  ASP A OD2 1 
ATOM   1207 N  N   . GLU A 1 170  ? 35.414 59.651  -2.302  1.00 9.90  ? 170  GLU A N   1 
ATOM   1208 C  CA  . GLU A 1 170  ? 35.371 58.527  -3.258  1.00 10.61 ? 170  GLU A CA  1 
ATOM   1209 C  C   . GLU A 1 170  ? 34.660 58.922  -4.546  1.00 10.03 ? 170  GLU A C   1 
ATOM   1210 O  O   . GLU A 1 170  ? 34.680 58.134  -5.489  1.00 11.96 ? 170  GLU A O   1 
ATOM   1211 C  CB  . GLU A 1 170  ? 34.703 57.321  -2.564  1.00 11.31 ? 170  GLU A CB  1 
ATOM   1212 C  CG  . GLU A 1 170  ? 35.528 56.903  -1.319  1.00 11.44 ? 170  GLU A CG  1 
ATOM   1213 C  CD  . GLU A 1 170  ? 34.959 55.666  -0.616  1.00 12.88 ? 170  GLU A CD  1 
ATOM   1214 O  OE1 . GLU A 1 170  ? 34.189 54.911  -1.264  1.00 12.22 ? 170  GLU A OE1 1 
ATOM   1215 O  OE2 . GLU A 1 170  ? 35.346 55.454  0.562   1.00 14.60 ? 170  GLU A OE2 1 
ATOM   1216 N  N   . ALA A 1 171  ? 34.072 60.108  -4.628  1.00 10.14 ? 171  ALA A N   1 
ATOM   1217 C  CA  . ALA A 1 171  ? 33.346 60.529  -5.855  1.00 9.25  ? 171  ALA A CA  1 
ATOM   1218 C  C   . ALA A 1 171  ? 34.197 61.258  -6.864  1.00 10.17 ? 171  ALA A C   1 
ATOM   1219 O  O   . ALA A 1 171  ? 34.182 60.916  -8.026  1.00 11.29 ? 171  ALA A O   1 
ATOM   1220 C  CB  . ALA A 1 171  ? 32.170 61.415  -5.478  1.00 11.01 ? 171  ALA A CB  1 
ATOM   1221 N  N   . ASN A 1 172  ? 34.914 62.279  -6.391  1.00 10.41 ? 172  ASN A N   1 
ATOM   1222 C  CA  . ASN A 1 172  ? 35.673 63.159  -7.293  1.00 10.04 ? 172  ASN A CA  1 
ATOM   1223 C  C   . ASN A 1 172  ? 37.124 62.786  -7.432  1.00 11.15 ? 172  ASN A C   1 
ATOM   1224 O  O   . ASN A 1 172  ? 37.797 63.205  -8.372  1.00 12.28 ? 172  ASN A O   1 
ATOM   1225 C  CB  . ASN A 1 172  ? 35.630 64.579  -6.719  1.00 10.17 ? 172  ASN A CB  1 
ATOM   1226 C  CG  . ASN A 1 172  ? 34.234 65.145  -6.598  1.00 13.72 ? 172  ASN A CG  1 
ATOM   1227 O  OD1 . ASN A 1 172  ? 33.569 65.358  -7.587  1.00 15.18 ? 172  ASN A OD1 1 
ATOM   1228 N  ND2 . ASN A 1 172  ? 33.800 65.421  -5.373  1.00 13.10 ? 172  ASN A ND2 1 
ATOM   1229 N  N   . SER A 1 173  ? 37.622 62.008  -6.492  1.00 9.47  ? 173  SER A N   1 
ATOM   1230 C  CA  . SER A 1 173  ? 39.032 61.647  -6.499  1.00 8.49  ? 173  SER A CA  1 
ATOM   1231 C  C   . SER A 1 173  ? 39.411 60.759  -7.653  1.00 9.14  ? 173  SER A C   1 
ATOM   1232 O  O   A SER A 1 173  ? 38.628 59.941  -8.123  0.50 10.51 ? 173  SER A O   1 
ATOM   1233 O  O   B SER A 1 173  ? 38.782 59.717  -7.929  0.50 12.50 ? 173  SER A O   1 
ATOM   1234 C  CB  . SER A 1 173  ? 39.391 60.970  -5.182  1.00 6.97  ? 173  SER A CB  1 
ATOM   1235 O  OG  A SER A 1 173  ? 38.520 59.867  -4.957  0.50 5.29  ? 173  SER A OG  1 
ATOM   1236 O  OG  B SER A 1 173  ? 40.712 60.585  -5.068  0.50 26.25 ? 173  SER A OG  1 
ATOM   1237 N  N   . HIS A 1 174  ? 40.617 60.971  -8.158  1.00 9.57  ? 174  HIS A N   1 
ATOM   1238 C  CA  . HIS A 1 174  ? 41.131 60.105  -9.216  1.00 8.52  ? 174  HIS A CA  1 
ATOM   1239 C  C   . HIS A 1 174  ? 41.770 58.922  -8.517  1.00 8.87  ? 174  HIS A C   1 
ATOM   1240 O  O   . HIS A 1 174  ? 42.453 59.101  -7.486  1.00 9.22  ? 174  HIS A O   1 
ATOM   1241 C  CB  . HIS A 1 174  ? 42.162 60.827  -10.044 1.00 10.26 ? 174  HIS A CB  1 
ATOM   1242 C  CG  . HIS A 1 174  ? 42.422 60.158  -11.346 1.00 11.17 ? 174  HIS A CG  1 
ATOM   1243 N  ND1 . HIS A 1 174  ? 43.147 58.989  -11.444 1.00 11.47 ? 174  HIS A ND1 1 
ATOM   1244 C  CD2 . HIS A 1 174  ? 41.975 60.454  -12.589 1.00 11.51 ? 174  HIS A CD2 1 
ATOM   1245 C  CE1 . HIS A 1 174  ? 43.127 58.587  -12.705 1.00 12.30 ? 174  HIS A CE1 1 
ATOM   1246 N  NE2 . HIS A 1 174  ? 42.423 59.459  -13.407 1.00 12.17 ? 174  HIS A NE2 1 
ATOM   1247 N  N   . TRP A 1 175  ? 41.611 57.726  -9.077  1.00 8.91  ? 175  TRP A N   1 
ATOM   1248 C  CA  . TRP A 1 175  ? 42.224 56.559  -8.428  1.00 9.41  ? 175  TRP A CA  1 
ATOM   1249 C  C   . TRP A 1 175  ? 43.719 56.718  -8.191  1.00 10.89 ? 175  TRP A C   1 
ATOM   1250 O  O   . TRP A 1 175  ? 44.247 56.201  -7.210  1.00 10.58 ? 175  TRP A O   1 
ATOM   1251 C  CB  . TRP A 1 175  ? 41.940 55.287  -9.223  1.00 9.67  ? 175  TRP A CB  1 
ATOM   1252 C  CG  . TRP A 1 175  ? 42.780 55.093  -10.475 1.00 9.38  ? 175  TRP A CG  1 
ATOM   1253 C  CD1 . TRP A 1 175  ? 42.423 55.453  -11.769 1.00 11.12 ? 175  TRP A CD1 1 
ATOM   1254 C  CD2 . TRP A 1 175  ? 44.065 54.469  -10.561 1.00 10.47 ? 175  TRP A CD2 1 
ATOM   1255 N  NE1 . TRP A 1 175  ? 43.459 55.068  -12.623 1.00 11.03 ? 175  TRP A NE1 1 
ATOM   1256 C  CE2 . TRP A 1 175  ? 44.460 54.466  -11.903 1.00 11.50 ? 175  TRP A CE2 1 
ATOM   1257 C  CE3 . TRP A 1 175  ? 44.924 53.894  -9.611  1.00 11.46 ? 175  TRP A CE3 1 
ATOM   1258 C  CZ2 . TRP A 1 175  ? 45.678 53.917  -12.327 1.00 11.51 ? 175  TRP A CZ2 1 
ATOM   1259 C  CZ3 . TRP A 1 175  ? 46.123 53.338  -10.039 1.00 12.92 ? 175  TRP A CZ3 1 
ATOM   1260 C  CH2 . TRP A 1 175  ? 46.495 53.356  -11.387 1.00 12.89 ? 175  TRP A CH2 1 
ATOM   1261 N  N   . ARG A 1 176  ? 44.429 57.406  -9.098  1.00 10.78 ? 176  ARG A N   1 
ATOM   1262 C  CA  . ARG A 1 176  ? 45.860 57.594  -8.901  1.00 10.81 ? 176  ARG A CA  1 
ATOM   1263 C  C   . ARG A 1 176  ? 46.130 58.350  -7.625  1.00 10.15 ? 176  ARG A C   1 
ATOM   1264 O  O   . ARG A 1 176  ? 47.122 58.052  -6.946  1.00 10.56 ? 176  ARG A O   1 
ATOM   1265 C  CB  . ARG A 1 176  ? 46.464 58.354  -10.127 1.00 12.53 ? 176  ARG A CB  1 
ATOM   1266 C  CG  . ARG A 1 176  ? 46.413 57.469  -11.379 1.00 12.47 ? 176  ARG A CG  1 
ATOM   1267 C  CD  . ARG A 1 176  ? 46.372 58.307  -12.670 1.00 15.25 ? 176  ARG A CD  1 
ATOM   1268 N  NE  . ARG A 1 176  ? 47.491 59.209  -12.751 1.00 15.00 ? 176  ARG A NE  1 
ATOM   1269 C  CZ  . ARG A 1 176  ? 47.637 60.044  -13.773 1.00 15.41 ? 176  ARG A CZ  1 
ATOM   1270 N  NH1 . ARG A 1 176  ? 46.729 60.036  -14.758 1.00 14.78 ? 176  ARG A NH1 1 
ATOM   1271 N  NH2 . ARG A 1 176  ? 48.613 60.934  -13.752 1.00 16.50 ? 176  ARG A NH2 1 
ATOM   1272 N  N   . ASN A 1 177  ? 45.290 59.327  -7.277  1.00 9.77  ? 177  ASN A N   1 
ATOM   1273 C  CA  . ASN A 1 177  ? 45.519 60.100  -6.045  1.00 9.58  ? 177  ASN A CA  1 
ATOM   1274 C  C   . ASN A 1 177  ? 44.980 59.362  -4.829  1.00 9.87  ? 177  ASN A C   1 
ATOM   1275 O  O   . ASN A 1 177  ? 45.511 59.576  -3.721  1.00 10.78 ? 177  ASN A O   1 
ATOM   1276 C  CB  . ASN A 1 177  ? 44.885 61.488  -6.136  1.00 10.34 ? 177  ASN A CB  1 
ATOM   1277 C  CG  . ASN A 1 177  ? 45.571 62.350  -7.163  1.00 12.38 ? 177  ASN A CG  1 
ATOM   1278 O  OD1 . ASN A 1 177  ? 46.724 62.134  -7.491  1.00 11.47 ? 177  ASN A OD1 1 
ATOM   1279 N  ND2 . ASN A 1 177  ? 44.838 63.335  -7.702  1.00 13.93 ? 177  ASN A ND2 1 
ATOM   1280 N  N   . VAL A 1 178  ? 44.000 58.496  -5.003  1.00 10.29 ? 178  VAL A N   1 
ATOM   1281 C  CA  . VAL A 1 178  ? 43.564 57.680  -3.877  1.00 9.57  ? 178  VAL A CA  1 
ATOM   1282 C  C   . VAL A 1 178  ? 44.767 56.791  -3.530  1.00 10.50 ? 178  VAL A C   1 
ATOM   1283 O  O   . VAL A 1 178  ? 45.113 56.623  -2.357  1.00 11.03 ? 178  VAL A O   1 
ATOM   1284 C  CB  . VAL A 1 178  ? 42.362 56.793  -4.255  1.00 9.57  ? 178  VAL A CB  1 
ATOM   1285 C  CG1 . VAL A 1 178  ? 42.056 55.808  -3.137  1.00 12.16 ? 178  VAL A CG1 1 
ATOM   1286 C  CG2 . VAL A 1 178  ? 41.115 57.673  -4.481  1.00 13.14 ? 178  VAL A CG2 1 
ATOM   1287 N  N   . LEU A 1 179  ? 45.444 56.213  -4.537  1.00 10.79 ? 179  LEU A N   1 
ATOM   1288 C  CA  . LEU A 1 179  ? 46.603 55.377  -4.257  1.00 10.26 ? 179  LEU A CA  1 
ATOM   1289 C  C   . LEU A 1 179  ? 47.742 56.207  -3.684  1.00 10.90 ? 179  LEU A C   1 
ATOM   1290 O  O   . LEU A 1 179  ? 48.421 55.748  -2.747  1.00 10.85 ? 179  LEU A O   1 
ATOM   1291 C  CB  . LEU A 1 179  ? 47.097 54.689  -5.560  1.00 11.33 ? 179  LEU A CB  1 
ATOM   1292 C  CG  . LEU A 1 179  ? 48.408 53.855  -5.399  1.00 11.40 ? 179  LEU A CG  1 
ATOM   1293 C  CD1 . LEU A 1 179  ? 48.235 52.714  -4.383  1.00 12.68 ? 179  LEU A CD1 1 
ATOM   1294 C  CD2 . LEU A 1 179  ? 48.785 53.234  -6.763  1.00 12.96 ? 179  LEU A CD2 1 
ATOM   1295 N  N   . LEU A 1 180  ? 47.941 57.428  -4.173  1.00 10.28 ? 180  LEU A N   1 
ATOM   1296 C  CA  . LEU A 1 180  ? 49.042 58.268  -3.708  1.00 9.90  ? 180  LEU A CA  1 
ATOM   1297 C  C   . LEU A 1 180  ? 48.861 58.502  -2.208  1.00 9.90  ? 180  LEU A C   1 
ATOM   1298 O  O   . LEU A 1 180  ? 49.851 58.318  -1.434  1.00 10.44 ? 180  LEU A O   1 
ATOM   1299 C  CB  . LEU A 1 180  ? 48.994 59.620  -4.456  1.00 11.24 ? 180  LEU A CB  1 
ATOM   1300 C  CG  . LEU A 1 180  ? 50.121 60.588  -4.093  1.00 12.41 ? 180  LEU A CG  1 
ATOM   1301 C  CD1 . LEU A 1 180  ? 51.415 60.038  -4.685  1.00 14.22 ? 180  LEU A CD1 1 
ATOM   1302 C  CD2 . LEU A 1 180  ? 49.844 61.967  -4.644  1.00 13.27 ? 180  LEU A CD2 1 
ATOM   1303 N  N   . GLN A 1 181  ? 47.660 58.908  -1.781  1.00 10.20 ? 181  GLN A N   1 
ATOM   1304 C  CA  . GLN A 1 181  ? 47.480 59.221  -0.348  1.00 9.71  ? 181  GLN A CA  1 
ATOM   1305 C  C   . GLN A 1 181  ? 47.525 57.980  0.529   1.00 11.26 ? 181  GLN A C   1 
ATOM   1306 O  O   . GLN A 1 181  ? 48.078 58.042  1.628   1.00 10.70 ? 181  GLN A O   1 
ATOM   1307 C  CB  . GLN A 1 181  ? 46.204 60.051  -0.143  1.00 9.83  ? 181  GLN A CB  1 
ATOM   1308 C  CG  . GLN A 1 181  ? 44.894 59.340  -0.368  1.00 10.67 ? 181  GLN A CG  1 
ATOM   1309 C  CD  . GLN A 1 181  ? 44.520 58.388  0.759   1.00 13.59 ? 181  GLN A CD  1 
ATOM   1310 O  OE1 . GLN A 1 181  ? 44.748 58.693  1.930   1.00 13.21 ? 181  GLN A OE1 1 
ATOM   1311 N  NE2 . GLN A 1 181  ? 43.903 57.255  0.406   1.00 12.29 ? 181  GLN A NE2 1 
ATOM   1312 N  N   . LEU A 1 182  ? 47.042 56.850  0.025   1.00 10.12 ? 182  LEU A N   1 
ATOM   1313 C  CA  . LEU A 1 182  ? 47.128 55.598  0.774   1.00 9.43  ? 182  LEU A CA  1 
ATOM   1314 C  C   . LEU A 1 182  ? 48.595 55.245  0.948   1.00 11.52 ? 182  LEU A C   1 
ATOM   1315 O  O   . LEU A 1 182  ? 49.028 54.848  2.029   1.00 11.53 ? 182  LEU A O   1 
ATOM   1316 C  CB  . LEU A 1 182  ? 46.389 54.469  0.025   1.00 9.82  ? 182  LEU A CB  1 
ATOM   1317 C  CG  . LEU A 1 182  ? 46.492 53.081  0.660   1.00 9.23  ? 182  LEU A CG  1 
ATOM   1318 C  CD1 . LEU A 1 182  ? 45.762 53.083  2.049   1.00 13.04 ? 182  LEU A CD1 1 
ATOM   1319 C  CD2 . LEU A 1 182  ? 45.832 52.040  -0.275  1.00 11.64 ? 182  LEU A CD2 1 
ATOM   1320 N  N   . THR A 1 183  ? 49.391 55.363  -0.101  1.00 10.82 ? 183  THR A N   1 
ATOM   1321 C  CA  . THR A 1 183  ? 50.797 55.025  -0.041  1.00 11.74 ? 183  THR A CA  1 
ATOM   1322 C  C   . THR A 1 183  ? 51.528 55.994  0.889   1.00 11.31 ? 183  THR A C   1 
ATOM   1323 O  O   . THR A 1 183  ? 52.428 55.567  1.645   1.00 11.57 ? 183  THR A O   1 
ATOM   1324 C  CB  . THR A 1 183  ? 51.419 55.096  -1.466  1.00 11.98 ? 183  THR A CB  1 
ATOM   1325 O  OG1 . THR A 1 183  ? 50.727 54.207  -2.331  1.00 11.51 ? 183  THR A OG1 1 
ATOM   1326 C  CG2 . THR A 1 183  ? 52.869 54.703  -1.403  1.00 13.44 ? 183  THR A CG2 1 
ATOM   1327 N  N   . GLU A 1 184  ? 51.164 57.271  0.890   1.00 10.40 ? 184  GLU A N   1 
ATOM   1328 C  CA  . GLU A 1 184  ? 51.868 58.224  1.745   1.00 10.57 ? 184  GLU A CA  1 
ATOM   1329 C  C   . GLU A 1 184  ? 51.652 57.858  3.209   1.00 10.31 ? 184  GLU A C   1 
ATOM   1330 O  O   . GLU A 1 184  ? 52.621 57.849  3.989   1.00 13.40 ? 184  GLU A O   1 
ATOM   1331 C  CB  . GLU A 1 184  ? 51.313 59.630  1.472   1.00 12.86 ? 184  GLU A CB  1 
ATOM   1332 C  CG  . GLU A 1 184  ? 52.162 60.793  1.977   1.00 15.36 ? 184  GLU A CG  1 
ATOM   1333 C  CD  . GLU A 1 184  ? 53.571 60.844  1.335   1.00 14.53 ? 184  GLU A CD  1 
ATOM   1334 O  OE1 . GLU A 1 184  ? 53.761 60.442  0.177   1.00 15.87 ? 184  GLU A OE1 1 
ATOM   1335 O  OE2 . GLU A 1 184  ? 54.485 61.303  2.011   1.00 17.33 ? 184  GLU A OE2 1 
ATOM   1336 N  N   . GLY A 1 185  ? 50.415 57.542  3.562   1.00 11.44 ? 185  GLY A N   1 
ATOM   1337 C  CA  . GLY A 1 185  ? 50.141 57.186  4.951   1.00 11.51 ? 185  GLY A CA  1 
ATOM   1338 C  C   . GLY A 1 185  ? 50.733 55.844  5.322   1.00 12.50 ? 185  GLY A C   1 
ATOM   1339 O  O   . GLY A 1 185  ? 51.363 55.716  6.407   1.00 12.29 ? 185  GLY A O   1 
ATOM   1340 N  N   . GLN A 1 186  ? 50.604 54.846  4.466   1.00 10.70 ? 186  GLN A N   1 
ATOM   1341 C  CA  . GLN A 1 186  ? 51.125 53.525  4.838   1.00 11.19 ? 186  GLN A CA  1 
ATOM   1342 C  C   . GLN A 1 186  ? 52.647 53.475  4.819   1.00 12.50 ? 186  GLN A C   1 
ATOM   1343 O  O   . GLN A 1 186  ? 53.254 52.703  5.601   1.00 11.39 ? 186  GLN A O   1 
ATOM   1344 C  CB  . GLN A 1 186  ? 50.518 52.427  3.942   1.00 10.86 ? 186  GLN A CB  1 
ATOM   1345 C  CG  . GLN A 1 186  ? 49.002 52.268  4.154   1.00 13.34 ? 186  GLN A CG  1 
ATOM   1346 C  CD  . GLN A 1 186  ? 48.578 50.879  3.944   1.00 13.29 ? 186  GLN A CD  1 
ATOM   1347 O  OE1 . GLN A 1 186  ? 49.190 50.170  3.158   1.00 17.44 ? 186  GLN A OE1 1 
ATOM   1348 N  NE2 . GLN A 1 186  ? 47.542 50.444  4.636   1.00 14.52 ? 186  GLN A NE2 1 
ATOM   1349 N  N   . THR A 1 187  ? 53.321 54.260  3.981   1.00 12.86 ? 187  THR A N   1 
ATOM   1350 C  CA  . THR A 1 187  ? 54.771 54.215  3.965   1.00 12.32 ? 187  THR A CA  1 
ATOM   1351 C  C   . THR A 1 187  ? 55.249 54.815  5.272   1.00 13.60 ? 187  THR A C   1 
ATOM   1352 O  O   . THR A 1 187  ? 56.198 54.297  5.885   1.00 13.27 ? 187  THR A O   1 
ATOM   1353 C  CB  . THR A 1 187  ? 55.282 54.981  2.740   1.00 11.91 ? 187  THR A CB  1 
ATOM   1354 O  OG1 . THR A 1 187  ? 54.756 54.323  1.562   1.00 12.92 ? 187  THR A OG1 1 
ATOM   1355 C  CG2 . THR A 1 187  ? 56.845 54.977  2.692   1.00 13.35 ? 187  THR A CG2 1 
ATOM   1356 N  N   . TRP A 1 188  ? 54.579 55.868  5.724   1.00 12.94 ? 188  TRP A N   1 
ATOM   1357 C  CA  . TRP A 1 188  ? 54.935 56.502  7.003   1.00 12.83 ? 188  TRP A CA  1 
ATOM   1358 C  C   . TRP A 1 188  ? 54.707 55.477  8.129   1.00 13.44 ? 188  TRP A C   1 
ATOM   1359 O  O   . TRP A 1 188  ? 55.600 55.250  8.987   1.00 13.26 ? 188  TRP A O   1 
ATOM   1360 C  CB  . TRP A 1 188  ? 54.042 57.720  7.239   1.00 14.24 ? 188  TRP A CB  1 
ATOM   1361 C  CG  . TRP A 1 188  ? 54.498 58.518  8.447   1.00 14.97 ? 188  TRP A CG  1 
ATOM   1362 C  CD1 . TRP A 1 188  ? 55.381 59.536  8.437   1.00 15.43 ? 188  TRP A CD1 1 
ATOM   1363 C  CD2 . TRP A 1 188  ? 54.170 58.256  9.826   1.00 13.94 ? 188  TRP A CD2 1 
ATOM   1364 N  NE1 . TRP A 1 188  ? 55.672 59.936  9.739   1.00 15.13 ? 188  TRP A NE1 1 
ATOM   1365 C  CE2 . TRP A 1 188  ? 54.931 59.162  10.604  1.00 14.16 ? 188  TRP A CE2 1 
ATOM   1366 C  CE3 . TRP A 1 188  ? 53.330 57.342  10.462  1.00 14.24 ? 188  TRP A CE3 1 
ATOM   1367 C  CZ2 . TRP A 1 188  ? 54.876 59.170  12.010  1.00 15.11 ? 188  TRP A CZ2 1 
ATOM   1368 C  CZ3 . TRP A 1 188  ? 53.277 57.340  11.883  1.00 15.57 ? 188  TRP A CZ3 1 
ATOM   1369 C  CH2 . TRP A 1 188  ? 54.047 58.253  12.620  1.00 15.05 ? 188  TRP A CH2 1 
ATOM   1370 N  N   . LEU A 1 189  ? 53.574 54.792  8.104   1.00 12.19 ? 189  LEU A N   1 
ATOM   1371 C  CA  . LEU A 1 189  ? 53.285 53.805  9.170   1.00 13.11 ? 189  LEU A CA  1 
ATOM   1372 C  C   . LEU A 1 189  ? 54.283 52.661  9.174   1.00 15.50 ? 189  LEU A C   1 
ATOM   1373 O  O   . LEU A 1 189  ? 54.676 52.176  10.252  1.00 15.68 ? 189  LEU A O   1 
ATOM   1374 C  CB  . LEU A 1 189  ? 51.870 53.212  9.034   1.00 12.49 ? 189  LEU A CB  1 
ATOM   1375 C  CG  . LEU A 1 189  ? 50.710 54.079  9.464   1.00 11.14 ? 189  LEU A CG  1 
ATOM   1376 C  CD1 . LEU A 1 189  ? 49.390 53.391  9.122   1.00 12.92 ? 189  LEU A CD1 1 
ATOM   1377 C  CD2 . LEU A 1 189  ? 50.766 54.292  11.013  1.00 12.94 ? 189  LEU A CD2 1 
ATOM   1378 N  N   . LYS A 1 190  ? 54.718 52.180  8.019   1.00 12.65 ? 190  LYS A N   1 
ATOM   1379 C  CA  . LYS A 1 190  ? 55.662 51.077  8.036   1.00 14.52 ? 190  LYS A CA  1 
ATOM   1380 C  C   . LYS A 1 190  ? 56.999 51.545  8.621   1.00 14.40 ? 190  LYS A C   1 
ATOM   1381 O  O   . LYS A 1 190  ? 57.611 50.822  9.427   1.00 15.66 ? 190  LYS A O   1 
ATOM   1382 C  CB  . LYS A 1 190  ? 55.894 50.495  6.626   1.00 16.28 ? 190  LYS A CB  1 
ATOM   1383 C  CG  . LYS A 1 190  ? 56.796 49.259  6.641   1.00 19.42 ? 190  LYS A CG  1 
ATOM   1384 C  CD  . LYS A 1 190  ? 57.069 48.754  5.265   1.00 26.47 ? 190  LYS A CD  1 
ATOM   1385 C  CE  . LYS A 1 190  ? 57.778 47.412  5.310   1.00 30.27 ? 190  LYS A CE  1 
ATOM   1386 N  NZ  . LYS A 1 190  ? 58.050 46.964  3.899   1.00 31.52 ? 190  LYS A NZ  1 
ATOM   1387 N  N   . GLN A 1 191  ? 57.443 52.720  8.208   1.00 14.80 ? 191  GLN A N   1 
ATOM   1388 C  CA  . GLN A 1 191  ? 58.714 53.256  8.658   1.00 19.13 ? 191  GLN A CA  1 
ATOM   1389 C  C   . GLN A 1 191  ? 58.735 53.543  10.142  1.00 18.34 ? 191  GLN A C   1 
ATOM   1390 O  O   . GLN A 1 191  ? 59.684 53.142  10.850  1.00 21.90 ? 191  GLN A O   1 
ATOM   1391 C  CB  . GLN A 1 191  ? 59.054 54.546  7.903   1.00 19.90 ? 191  GLN A CB  1 
ATOM   1392 C  CG  . GLN A 1 191  ? 60.429 55.098  8.341   1.00 26.81 ? 191  GLN A CG  1 
ATOM   1393 C  CD  . GLN A 1 191  ? 60.938 56.260  7.482   1.00 31.17 ? 191  GLN A CD  1 
ATOM   1394 O  OE1 . GLN A 1 191  ? 62.017 56.797  7.755   1.00 36.06 ? 191  GLN A OE1 1 
ATOM   1395 N  NE2 . GLN A 1 191  ? 60.174 56.652  6.461   1.00 32.88 ? 191  GLN A NE2 1 
ATOM   1396 N  N   . PHE A 1 192  ? 57.712 54.208  10.645  1.00 16.56 ? 192  PHE A N   1 
ATOM   1397 C  CA  . PHE A 1 192  ? 57.727 54.600  12.037  1.00 17.00 ? 192  PHE A CA  1 
ATOM   1398 C  C   . PHE A 1 192  ? 56.979 53.783  13.072  1.00 18.23 ? 192  PHE A C   1 
ATOM   1399 O  O   . PHE A 1 192  ? 57.359 53.802  14.248  1.00 21.84 ? 192  PHE A O   1 
ATOM   1400 C  CB  . PHE A 1 192  ? 57.296 56.054  12.148  1.00 16.25 ? 192  PHE A CB  1 
ATOM   1401 C  CG  . PHE A 1 192  ? 58.200 56.995  11.401  1.00 16.45 ? 192  PHE A CG  1 
ATOM   1402 C  CD1 . PHE A 1 192  ? 59.436 57.378  11.957  1.00 19.48 ? 192  PHE A CD1 1 
ATOM   1403 C  CD2 . PHE A 1 192  ? 57.852 57.456  10.127  1.00 16.74 ? 192  PHE A CD2 1 
ATOM   1404 C  CE1 . PHE A 1 192  ? 60.318 58.217  11.247  1.00 19.91 ? 192  PHE A CE1 1 
ATOM   1405 C  CE2 . PHE A 1 192  ? 58.711 58.288  9.406   1.00 16.84 ? 192  PHE A CE2 1 
ATOM   1406 C  CZ  . PHE A 1 192  ? 59.967 58.681  9.971   1.00 18.39 ? 192  PHE A CZ  1 
ATOM   1407 N  N   . MET A 1 193  ? 55.937 53.068  12.666  1.00 16.46 ? 193  MET A N   1 
ATOM   1408 C  CA  . MET A 1 193  ? 55.143 52.250  13.599  1.00 16.11 ? 193  MET A CA  1 
ATOM   1409 C  C   . MET A 1 193  ? 55.295 50.766  13.304  1.00 16.36 ? 193  MET A C   1 
ATOM   1410 O  O   . MET A 1 193  ? 54.761 49.919  14.040  1.00 17.41 ? 193  MET A O   1 
ATOM   1411 C  CB  . MET A 1 193  ? 53.644 52.611  13.504  1.00 15.74 ? 193  MET A CB  1 
ATOM   1412 C  CG  A MET A 1 193  ? 53.259 53.974  14.094  0.50 14.17 ? 193  MET A CG  1 
ATOM   1413 C  CG  B MET A 1 193  ? 53.519 54.237  13.691  0.50 18.64 ? 193  MET A CG  1 
ATOM   1414 S  SD  A MET A 1 193  ? 53.459 53.990  15.924  0.50 16.53 ? 193  MET A SD  1 
ATOM   1415 S  SD  B MET A 1 193  ? 54.453 55.045  14.984  0.50 24.32 ? 193  MET A SD  1 
ATOM   1416 C  CE  A MET A 1 193  ? 54.854 55.098  16.120  0.50 20.25 ? 193  MET A CE  1 
ATOM   1417 C  CE  B MET A 1 193  ? 53.650 54.176  16.288  0.50 23.07 ? 193  MET A CE  1 
ATOM   1418 N  N   . ASN A 1 194  ? 55.982 50.436  12.212  1.00 16.01 ? 194  ASN A N   1 
ATOM   1419 C  CA  . ASN A 1 194  ? 56.151 49.046  11.807  1.00 17.70 ? 194  ASN A CA  1 
ATOM   1420 C  C   . ASN A 1 194  ? 54.846 48.256  11.692  1.00 16.90 ? 194  ASN A C   1 
ATOM   1421 O  O   . ASN A 1 194  ? 54.737 47.106  12.152  1.00 18.40 ? 194  ASN A O   1 
ATOM   1422 C  CB  . ASN A 1 194  ? 57.078 48.338  12.807  1.00 19.96 ? 194  ASN A CB  1 
ATOM   1423 C  CG  . ASN A 1 194  ? 57.585 47.021  12.286  1.00 26.62 ? 194  ASN A CG  1 
ATOM   1424 O  OD1 . ASN A 1 194  ? 57.737 46.839  11.085  1.00 25.51 ? 194  ASN A OD1 1 
ATOM   1425 N  ND2 . ASN A 1 194  ? 57.868 46.108  13.205  1.00 31.70 ? 194  ASN A ND2 1 
ATOM   1426 N  N   . VAL A 1 195  ? 53.828 48.883  11.091  1.00 15.84 ? 195  VAL A N   1 
ATOM   1427 C  CA  . VAL A 1 195  ? 52.565 48.210  10.883  1.00 16.11 ? 195  VAL A CA  1 
ATOM   1428 C  C   . VAL A 1 195  ? 51.983 48.669  9.555   1.00 14.86 ? 195  VAL A C   1 
ATOM   1429 O  O   . VAL A 1 195  ? 52.250 49.786  9.120   1.00 15.26 ? 195  VAL A O   1 
ATOM   1430 C  CB  . VAL A 1 195  ? 51.475 48.534  11.990  1.00 16.04 ? 195  VAL A CB  1 
ATOM   1431 C  CG1 . VAL A 1 195  ? 51.911 48.066  13.365  1.00 22.72 ? 195  VAL A CG1 1 
ATOM   1432 C  CG2 . VAL A 1 195  ? 51.152 49.999  12.027  1.00 16.63 ? 195  VAL A CG2 1 
ATOM   1433 N  N   . THR A 1 196  ? 51.246 47.751  8.938   1.00 14.05 ? 196  THR A N   1 
ATOM   1434 C  CA  . THR A 1 196  ? 50.496 47.998  7.690   1.00 14.44 ? 196  THR A CA  1 
ATOM   1435 C  C   . THR A 1 196  ? 49.053 47.501  7.875   1.00 14.63 ? 196  THR A C   1 
ATOM   1436 O  O   . THR A 1 196  ? 48.791 46.300  7.924   1.00 15.13 ? 196  THR A O   1 
ATOM   1437 C  CB  . THR A 1 196  ? 51.131 47.256  6.498   1.00 15.71 ? 196  THR A CB  1 
ATOM   1438 O  OG1 . THR A 1 196  ? 52.498 47.686  6.353   1.00 17.18 ? 196  THR A OG1 1 
ATOM   1439 C  CG2 . THR A 1 196  ? 50.349 47.589  5.208   1.00 18.28 ? 196  THR A CG2 1 
ATOM   1440 N  N   . PRO A 1 197  ? 48.086 48.423  7.995   1.00 14.09 ? 197  PRO A N   1 
ATOM   1441 C  CA  . PRO A 1 197  ? 46.687 48.048  8.182   1.00 12.87 ? 197  PRO A CA  1 
ATOM   1442 C  C   . PRO A 1 197  ? 46.177 47.171  7.062   1.00 12.66 ? 197  PRO A C   1 
ATOM   1443 O  O   . PRO A 1 197  ? 46.530 47.416  5.874   1.00 13.81 ? 197  PRO A O   1 
ATOM   1444 C  CB  . PRO A 1 197  ? 45.950 49.406  8.163   1.00 12.76 ? 197  PRO A CB  1 
ATOM   1445 C  CG  . PRO A 1 197  ? 46.973 50.345  8.696   1.00 13.49 ? 197  PRO A CG  1 
ATOM   1446 C  CD  . PRO A 1 197  ? 48.261 49.877  8.104   1.00 13.53 ? 197  PRO A CD  1 
ATOM   1447 N  N   . THR A 1 198  ? 45.344 46.199  7.408   1.00 12.43 ? 198  THR A N   1 
ATOM   1448 C  CA  . THR A 1 198  ? 44.708 45.357  6.396   1.00 13.98 ? 198  THR A CA  1 
ATOM   1449 C  C   . THR A 1 198  ? 43.188 45.516  6.474   1.00 13.16 ? 198  THR A C   1 
ATOM   1450 O  O   . THR A 1 198  ? 42.449 44.832  5.760   1.00 13.21 ? 198  THR A O   1 
ATOM   1451 C  CB  . THR A 1 198  ? 45.037 43.876  6.554   1.00 15.46 ? 198  THR A CB  1 
ATOM   1452 O  OG1 . THR A 1 198  ? 44.588 43.449  7.839   1.00 16.23 ? 198  THR A OG1 1 
ATOM   1453 C  CG2 . THR A 1 198  ? 46.524 43.615  6.400   1.00 16.66 ? 198  THR A CG2 1 
ATOM   1454 N  N   . ALA A 1 199  ? 42.704 46.402  7.349   1.00 12.60 ? 199  ALA A N   1 
ATOM   1455 C  CA  . ALA A 1 199  ? 41.277 46.715  7.459   1.00 12.81 ? 199  ALA A CA  1 
ATOM   1456 C  C   . ALA A 1 199  ? 41.086 48.211  7.225   1.00 12.66 ? 199  ALA A C   1 
ATOM   1457 O  O   . ALA A 1 199  ? 41.826 49.012  7.776   1.00 11.70 ? 199  ALA A O   1 
ATOM   1458 C  CB  . ALA A 1 199  ? 40.737 46.337  8.862   1.00 13.82 ? 199  ALA A CB  1 
ATOM   1459 N  N   . SER A 1 200  ? 40.128 48.575  6.383   1.00 11.87 ? 200  SER A N   1 
ATOM   1460 C  CA  . SER A 1 200  ? 39.846 49.963  6.066   1.00 12.58 ? 200  SER A CA  1 
ATOM   1461 C  C   . SER A 1 200  ? 38.570 50.451  6.775   1.00 12.58 ? 200  SER A C   1 
ATOM   1462 O  O   . SER A 1 200  ? 37.616 49.679  6.959   1.00 12.49 ? 200  SER A O   1 
ATOM   1463 C  CB  . SER A 1 200  ? 39.710 50.097  4.548   1.00 11.84 ? 200  SER A CB  1 
ATOM   1464 O  OG  . SER A 1 200  ? 39.463 51.446  4.190   1.00 15.36 ? 200  SER A OG  1 
ATOM   1465 N  N   . TRP A 1 201  ? 38.576 51.731  7.146   1.00 12.25 ? 201  TRP A N   1 
ATOM   1466 C  CA  . TRP A 1 201  ? 37.486 52.390  7.861   1.00 11.20 ? 201  TRP A CA  1 
ATOM   1467 C  C   . TRP A 1 201  ? 37.141 53.686  7.120   1.00 12.83 ? 201  TRP A C   1 
ATOM   1468 O  O   . TRP A 1 201  ? 37.955 54.606  7.085   1.00 12.74 ? 201  TRP A O   1 
ATOM   1469 C  CB  . TRP A 1 201  ? 38.035 52.680  9.265   1.00 12.23 ? 201  TRP A CB  1 
ATOM   1470 C  CG  . TRP A 1 201  ? 37.179 53.521  10.214  1.00 12.31 ? 201  TRP A CG  1 
ATOM   1471 C  CD1 . TRP A 1 201  ? 37.330 54.858  10.509  1.00 14.18 ? 201  TRP A CD1 1 
ATOM   1472 C  CD2 . TRP A 1 201  ? 36.207 53.029  11.134  1.00 12.68 ? 201  TRP A CD2 1 
ATOM   1473 N  NE1 . TRP A 1 201  ? 36.524 55.209  11.549  1.00 13.10 ? 201  TRP A NE1 1 
ATOM   1474 C  CE2 . TRP A 1 201  ? 35.829 54.109  11.963  1.00 11.23 ? 201  TRP A CE2 1 
ATOM   1475 C  CE3 . TRP A 1 201  ? 35.635 51.775  11.353  1.00 13.09 ? 201  TRP A CE3 1 
ATOM   1476 C  CZ2 . TRP A 1 201  ? 34.887 53.971  13.010  1.00 12.41 ? 201  TRP A CZ2 1 
ATOM   1477 C  CZ3 . TRP A 1 201  ? 34.696 51.620  12.400  1.00 13.60 ? 201  TRP A CZ3 1 
ATOM   1478 C  CH2 . TRP A 1 201  ? 34.340 52.723  13.210  1.00 14.30 ? 201  TRP A CH2 1 
ATOM   1479 N  N   . ALA A 1 202  ? 35.970 53.726  6.501   1.00 11.24 ? 202  ALA A N   1 
ATOM   1480 C  CA  . ALA A 1 202  ? 35.523 54.914  5.745   1.00 11.25 ? 202  ALA A CA  1 
ATOM   1481 C  C   . ALA A 1 202  ? 34.096 55.272  6.167   1.00 11.67 ? 202  ALA A C   1 
ATOM   1482 O  O   . ALA A 1 202  ? 33.080 54.872  5.572   1.00 12.26 ? 202  ALA A O   1 
ATOM   1483 C  CB  . ALA A 1 202  ? 35.606 54.645  4.246   1.00 12.52 ? 202  ALA A CB  1 
ATOM   1484 N  N   . ILE A 1 203  ? 34.046 55.978  7.276   1.00 11.51 ? 203  ILE A N   1 
ATOM   1485 C  CA  . ILE A 1 203  ? 32.760 56.332  7.877   1.00 11.70 ? 203  ILE A CA  1 
ATOM   1486 C  C   . ILE A 1 203  ? 32.093 57.609  7.402   1.00 12.50 ? 203  ILE A C   1 
ATOM   1487 O  O   . ILE A 1 203  ? 30.914 57.816  7.638   1.00 13.52 ? 203  ILE A O   1 
ATOM   1488 C  CB  . ILE A 1 203  ? 32.855 56.409  9.435   1.00 11.32 ? 203  ILE A CB  1 
ATOM   1489 C  CG1 . ILE A 1 203  ? 34.000 57.324  9.897   1.00 12.51 ? 203  ILE A CG1 1 
ATOM   1490 C  CG2 . ILE A 1 203  ? 33.106 54.934  9.975   1.00 13.53 ? 203  ILE A CG2 1 
ATOM   1491 C  CD1 . ILE A 1 203  ? 33.897 57.692  11.408  1.00 11.61 ? 203  ILE A CD1 1 
ATOM   1492 N  N   . ASP A 1 204  ? 32.850 58.451  6.688   1.00 11.21 ? 204  ASP A N   1 
ATOM   1493 C  CA  . ASP A 1 204  ? 32.277 59.729  6.282   1.00 11.98 ? 204  ASP A CA  1 
ATOM   1494 C  C   . ASP A 1 204  ? 32.224 60.136  4.794   1.00 10.86 ? 204  ASP A C   1 
ATOM   1495 O  O   . ASP A 1 204  ? 31.530 61.090  4.520   1.00 14.20 ? 204  ASP A O   1 
ATOM   1496 C  CB  . ASP A 1 204  ? 32.967 60.850  7.086   1.00 12.03 ? 204  ASP A CB  1 
ATOM   1497 C  CG  . ASP A 1 204  ? 32.062 62.073  7.297   1.00 12.98 ? 204  ASP A CG  1 
ATOM   1498 O  OD1 . ASP A 1 204  ? 30.811 62.005  7.418   1.00 13.50 ? 204  ASP A OD1 1 
ATOM   1499 O  OD2 . ASP A 1 204  ? 32.635 63.189  7.363   1.00 13.54 ? 204  ASP A OD2 1 
ATOM   1500 N  N   . PRO A 1 205  ? 32.972 59.471  3.866   1.00 11.46 ? 205  PRO A N   1 
ATOM   1501 C  CA  . PRO A 1 205  ? 32.819 59.943  2.462   1.00 12.50 ? 205  PRO A CA  1 
ATOM   1502 C  C   . PRO A 1 205  ? 31.343 59.886  2.051   1.00 12.99 ? 205  PRO A C   1 
ATOM   1503 O  O   . PRO A 1 205  ? 30.588 58.996  2.496   1.00 13.78 ? 205  PRO A O   1 
ATOM   1504 C  CB  . PRO A 1 205  ? 33.687 58.994  1.673   1.00 12.84 ? 205  PRO A CB  1 
ATOM   1505 C  CG  . PRO A 1 205  ? 34.786 58.567  2.686   1.00 15.85 ? 205  PRO A CG  1 
ATOM   1506 C  CD  . PRO A 1 205  ? 33.974 58.395  3.970   1.00 14.74 ? 205  PRO A CD  1 
ATOM   1507 N  N   . PHE A 1 206  ? 30.916 60.804  1.185   1.00 13.35 ? 206  PHE A N   1 
ATOM   1508 C  CA  . PHE A 1 206  ? 29.459 60.943  0.909   1.00 12.59 ? 206  PHE A CA  1 
ATOM   1509 C  C   . PHE A 1 206  ? 29.064 60.050  -0.258  1.00 12.70 ? 206  PHE A C   1 
ATOM   1510 O  O   . PHE A 1 206  ? 28.836 60.494  -1.401  1.00 13.28 ? 206  PHE A O   1 
ATOM   1511 C  CB  . PHE A 1 206  ? 29.140 62.444  0.644   1.00 12.15 ? 206  PHE A CB  1 
ATOM   1512 C  CG  . PHE A 1 206  ? 29.995 63.404  1.462   1.00 11.61 ? 206  PHE A CG  1 
ATOM   1513 C  CD1 . PHE A 1 206  ? 30.211 63.180  2.825   1.00 12.29 ? 206  PHE A CD1 1 
ATOM   1514 C  CD2 . PHE A 1 206  ? 30.608 64.510  0.847   1.00 12.57 ? 206  PHE A CD2 1 
ATOM   1515 C  CE1 . PHE A 1 206  ? 31.023 64.038  3.571   1.00 15.72 ? 206  PHE A CE1 1 
ATOM   1516 C  CE2 . PHE A 1 206  ? 31.417 65.382  1.581   1.00 12.59 ? 206  PHE A CE2 1 
ATOM   1517 C  CZ  . PHE A 1 206  ? 31.634 65.149  2.959   1.00 13.38 ? 206  PHE A CZ  1 
ATOM   1518 N  N   . GLY A 1 207  ? 28.923 58.766  0.071   1.00 12.12 ? 207  GLY A N   1 
ATOM   1519 C  CA  . GLY A 1 207  ? 28.720 57.756  -0.946  1.00 12.54 ? 207  GLY A CA  1 
ATOM   1520 C  C   . GLY A 1 207  ? 30.040 57.017  -1.119  1.00 11.07 ? 207  GLY A C   1 
ATOM   1521 O  O   . GLY A 1 207  ? 31.124 57.549  -0.815  1.00 11.58 ? 207  GLY A O   1 
ATOM   1522 N  N   . HIS A 1 208  ? 29.972 55.819  -1.686  1.00 12.03 ? 208  HIS A N   1 
ATOM   1523 C  CA  . HIS A 1 208  ? 31.173 54.950  -1.787  1.00 10.66 ? 208  HIS A CA  1 
ATOM   1524 C  C   . HIS A 1 208  ? 31.352 54.343  -3.150  1.00 10.21 ? 208  HIS A C   1 
ATOM   1525 O  O   . HIS A 1 208  ? 30.359 53.969  -3.847  1.00 11.25 ? 208  HIS A O   1 
ATOM   1526 C  CB  . HIS A 1 208  ? 31.023 53.837  -0.734  1.00 10.54 ? 208  HIS A CB  1 
ATOM   1527 C  CG  . HIS A 1 208  ? 31.109 54.345  0.687   1.00 10.17 ? 208  HIS A CG  1 
ATOM   1528 N  ND1 . HIS A 1 208  ? 32.318 54.644  1.292   1.00 13.90 ? 208  HIS A ND1 1 
ATOM   1529 C  CD2 . HIS A 1 208  ? 30.134 54.641  1.588   1.00 13.47 ? 208  HIS A CD2 1 
ATOM   1530 C  CE1 . HIS A 1 208  ? 32.070 55.071  2.524   1.00 13.93 ? 208  HIS A CE1 1 
ATOM   1531 N  NE2 . HIS A 1 208  ? 30.768 55.076  2.730   1.00 14.54 ? 208  HIS A NE2 1 
ATOM   1532 N  N   . SER A 1 209  ? 32.621 54.184  -3.508  1.00 9.98  ? 209  SER A N   1 
ATOM   1533 C  CA  . SER A 1 209  ? 33.036 53.691  -4.806  1.00 10.07 ? 209  SER A CA  1 
ATOM   1534 C  C   . SER A 1 209  ? 33.760 52.383  -4.760  1.00 10.96 ? 209  SER A C   1 
ATOM   1535 O  O   . SER A 1 209  ? 34.565 52.145  -3.857  1.00 10.70 ? 209  SER A O   1 
ATOM   1536 C  CB  . SER A 1 209  ? 33.963 54.731  -5.400  1.00 11.63 ? 209  SER A CB  1 
ATOM   1537 O  OG  . SER A 1 209  ? 34.499 54.241  -6.639  1.00 12.76 ? 209  SER A OG  1 
ATOM   1538 N  N   . PRO A 1 210  ? 33.478 51.487  -5.741  1.00 10.81 ? 210  PRO A N   1 
ATOM   1539 C  CA  . PRO A 1 210  ? 34.181 50.192  -5.787  1.00 11.46 ? 210  PRO A CA  1 
ATOM   1540 C  C   . PRO A 1 210  ? 35.670 50.372  -6.136  1.00 10.86 ? 210  PRO A C   1 
ATOM   1541 O  O   . PRO A 1 210  ? 36.438 49.421  -6.067  1.00 11.21 ? 210  PRO A O   1 
ATOM   1542 C  CB  . PRO A 1 210  ? 33.437 49.417  -6.883  1.00 11.12 ? 210  PRO A CB  1 
ATOM   1543 C  CG  . PRO A 1 210  ? 32.911 50.513  -7.767  1.00 11.98 ? 210  PRO A CG  1 
ATOM   1544 C  CD  . PRO A 1 210  ? 32.478 51.594  -6.814  1.00 10.78 ? 210  PRO A CD  1 
ATOM   1545 N  N   . THR A 1 211  ? 36.099 51.600  -6.494  1.00 11.49 ? 211  THR A N   1 
ATOM   1546 C  CA  . THR A 1 211  ? 37.509 51.823  -6.716  1.00 11.82 ? 211  THR A CA  1 
ATOM   1547 C  C   . THR A 1 211  ? 38.279 51.566  -5.415  1.00 11.67 ? 211  THR A C   1 
ATOM   1548 O  O   . THR A 1 211  ? 39.455 51.183  -5.458  1.00 12.23 ? 211  THR A O   1 
ATOM   1549 C  CB  . THR A 1 211  ? 37.740 53.256  -7.197  1.00 11.83 ? 211  THR A CB  1 
ATOM   1550 O  OG1 . THR A 1 211  ? 37.161 53.315  -8.525  1.00 12.99 ? 211  THR A OG1 1 
ATOM   1551 C  CG2 . THR A 1 211  ? 39.210 53.641  -7.191  1.00 13.79 ? 211  THR A CG2 1 
ATOM   1552 N  N   . MET A 1 212  ? 37.617 51.828  -4.271  1.00 10.92 ? 212  MET A N   1 
ATOM   1553 C  CA  . MET A 1 212  ? 38.279 51.555  -2.992  1.00 12.01 ? 212  MET A CA  1 
ATOM   1554 C  C   . MET A 1 212  ? 38.654 50.080  -2.776  1.00 11.46 ? 212  MET A C   1 
ATOM   1555 O  O   . MET A 1 212  ? 39.833 49.754  -2.579  1.00 11.92 ? 212  MET A O   1 
ATOM   1556 C  CB  . MET A 1 212  ? 37.422 52.097  -1.852  1.00 11.43 ? 212  MET A CB  1 
ATOM   1557 C  CG  . MET A 1 212  ? 37.224 53.602  -1.917  1.00 14.84 ? 212  MET A CG  1 
ATOM   1558 S  SD  . MET A 1 212  ? 38.667 54.613  -2.249  1.00 17.54 ? 212  MET A SD  1 
ATOM   1559 C  CE  . MET A 1 212  ? 39.487 54.527  -0.668  1.00 19.29 ? 212  MET A CE  1 
ATOM   1560 N  N   . PRO A 1 213  ? 37.670 49.158  -2.814  1.00 11.46 ? 213  PRO A N   1 
ATOM   1561 C  CA  . PRO A 1 213  ? 38.103 47.766  -2.639  1.00 11.26 ? 213  PRO A CA  1 
ATOM   1562 C  C   . PRO A 1 213  ? 39.078 47.366  -3.755  1.00 12.16 ? 213  PRO A C   1 
ATOM   1563 O  O   . PRO A 1 213  ? 39.953 46.533  -3.536  1.00 13.64 ? 213  PRO A O   1 
ATOM   1564 C  CB  . PRO A 1 213  ? 36.798 46.943  -2.702  1.00 11.47 ? 213  PRO A CB  1 
ATOM   1565 C  CG  . PRO A 1 213  ? 35.796 47.906  -3.379  1.00 10.64 ? 213  PRO A CG  1 
ATOM   1566 C  CD  . PRO A 1 213  ? 36.201 49.270  -2.834  1.00 11.12 ? 213  PRO A CD  1 
ATOM   1567 N  N   . TYR A 1 214  ? 38.934 47.934  -4.966  1.00 12.53 ? 214  TYR A N   1 
ATOM   1568 C  CA  . TYR A 1 214  ? 39.895 47.560  -6.035  1.00 11.85 ? 214  TYR A CA  1 
ATOM   1569 C  C   . TYR A 1 214  ? 41.345 47.834  -5.581  1.00 12.22 ? 214  TYR A C   1 
ATOM   1570 O  O   . TYR A 1 214  ? 42.243 46.962  -5.687  1.00 13.16 ? 214  TYR A O   1 
ATOM   1571 C  CB  . TYR A 1 214  ? 39.609 48.368  -7.297  1.00 11.54 ? 214  TYR A CB  1 
ATOM   1572 C  CG  . TYR A 1 214  ? 40.566 48.120  -8.469  1.00 12.26 ? 214  TYR A CG  1 
ATOM   1573 C  CD1 . TYR A 1 214  ? 40.341 47.047  -9.340  1.00 17.81 ? 214  TYR A CD1 1 
ATOM   1574 C  CD2 . TYR A 1 214  ? 41.626 48.980  -8.708  1.00 11.90 ? 214  TYR A CD2 1 
ATOM   1575 C  CE1 . TYR A 1 214  ? 41.160 46.866  -10.448 1.00 19.28 ? 214  TYR A CE1 1 
ATOM   1576 C  CE2 . TYR A 1 214  ? 42.451 48.801  -9.797  1.00 13.63 ? 214  TYR A CE2 1 
ATOM   1577 C  CZ  . TYR A 1 214  ? 42.192 47.752  -10.661 1.00 17.12 ? 214  TYR A CZ  1 
ATOM   1578 O  OH  . TYR A 1 214  ? 42.927 47.634  -11.832 1.00 19.23 ? 214  TYR A OH  1 
ATOM   1579 N  N   . ILE A 1 215  ? 41.595 49.079  -5.161  1.00 10.68 ? 215  ILE A N   1 
ATOM   1580 C  CA  . ILE A 1 215  ? 42.921 49.478  -4.731  1.00 11.30 ? 215  ILE A CA  1 
ATOM   1581 C  C   . ILE A 1 215  ? 43.335 48.771  -3.439  1.00 10.68 ? 215  ILE A C   1 
ATOM   1582 O  O   . ILE A 1 215  ? 44.452 48.263  -3.331  1.00 12.40 ? 215  ILE A O   1 
ATOM   1583 C  CB  . ILE A 1 215  ? 42.987 51.012  -4.512  1.00 11.63 ? 215  ILE A CB  1 
ATOM   1584 C  CG1 . ILE A 1 215  ? 42.814 51.730  -5.829  1.00 12.98 ? 215  ILE A CG1 1 
ATOM   1585 C  CG2 . ILE A 1 215  ? 44.323 51.407  -3.804  1.00 13.72 ? 215  ILE A CG2 1 
ATOM   1586 C  CD1 . ILE A 1 215  ? 42.728 53.224  -5.691  1.00 15.79 ? 215  ILE A CD1 1 
ATOM   1587 N  N   . LEU A 1 216  ? 42.414 48.722  -2.473  1.00 11.41 ? 216  LEU A N   1 
ATOM   1588 C  CA  . LEU A 1 216  ? 42.743 48.097  -1.169  1.00 11.35 ? 216  LEU A CA  1 
ATOM   1589 C  C   . LEU A 1 216  ? 43.094 46.610  -1.312  1.00 11.26 ? 216  LEU A C   1 
ATOM   1590 O  O   . LEU A 1 216  ? 44.108 46.159  -0.766  1.00 12.03 ? 216  LEU A O   1 
ATOM   1591 C  CB  . LEU A 1 216  ? 41.566 48.256  -0.201  1.00 11.21 ? 216  LEU A CB  1 
ATOM   1592 C  CG  . LEU A 1 216  ? 41.162 49.689  0.161   1.00 10.98 ? 216  LEU A CG  1 
ATOM   1593 C  CD1 . LEU A 1 216  ? 39.913 49.675  0.948   1.00 13.09 ? 216  LEU A CD1 1 
ATOM   1594 C  CD2 . LEU A 1 216  ? 42.303 50.344  0.974   1.00 13.60 ? 216  LEU A CD2 1 
ATOM   1595 N  N   . GLN A 1 217  ? 42.318 45.881  -2.129  1.00 12.01 ? 217  GLN A N   1 
ATOM   1596 C  CA  . GLN A 1 217  ? 42.580 44.455  -2.289  1.00 11.94 ? 217  GLN A CA  1 
ATOM   1597 C  C   . GLN A 1 217  ? 43.939 44.209  -2.967  1.00 12.84 ? 217  GLN A C   1 
ATOM   1598 O  O   . GLN A 1 217  ? 44.598 43.186  -2.710  1.00 16.27 ? 217  GLN A O   1 
ATOM   1599 C  CB  . GLN A 1 217  ? 41.415 43.808  -3.049  1.00 15.63 ? 217  GLN A CB  1 
ATOM   1600 C  CG  . GLN A 1 217  ? 41.402 42.263  -3.101  1.00 15.58 ? 217  GLN A CG  1 
ATOM   1601 C  CD  . GLN A 1 217  ? 42.317 41.723  -4.157  1.00 19.57 ? 217  GLN A CD  1 
ATOM   1602 O  OE1 . GLN A 1 217  ? 42.476 42.341  -5.202  1.00 21.13 ? 217  GLN A OE1 1 
ATOM   1603 N  NE2 . GLN A 1 217  ? 42.912 40.551  -3.911  1.00 21.64 ? 217  GLN A NE2 1 
ATOM   1604 N  N   . LYS A 1 218  ? 44.411 45.163  -3.777  1.00 12.69 ? 218  LYS A N   1 
ATOM   1605 C  CA  . LYS A 1 218  ? 45.715 45.040  -4.434  1.00 11.65 ? 218  LYS A CA  1 
ATOM   1606 C  C   . LYS A 1 218  ? 46.846 45.651  -3.569  1.00 12.76 ? 218  LYS A C   1 
ATOM   1607 O  O   . LYS A 1 218  ? 47.992 45.749  -4.015  1.00 13.14 ? 218  LYS A O   1 
ATOM   1608 C  CB  . LYS A 1 218  ? 45.650 45.751  -5.806  1.00 12.54 ? 218  LYS A CB  1 
ATOM   1609 C  CG  . LYS A 1 218  ? 44.819 44.946  -6.805  1.00 13.81 ? 218  LYS A CG  1 
ATOM   1610 C  CD  . LYS A 1 218  ? 44.519 45.804  -8.056  1.00 13.76 ? 218  LYS A CD  1 
ATOM   1611 C  CE  . LYS A 1 218  ? 44.173 44.961  -9.242  1.00 16.91 ? 218  LYS A CE  1 
ATOM   1612 N  NZ  . LYS A 1 218  ? 43.079 43.980  -9.082  1.00 17.58 ? 218  LYS A NZ  1 
ATOM   1613 N  N   . SER A 1 219  ? 46.475 46.077  -2.363  1.00 12.09 ? 219  SER A N   1 
ATOM   1614 C  CA  . SER A 1 219  ? 47.376 46.669  -1.396  1.00 12.09 ? 219  SER A CA  1 
ATOM   1615 C  C   . SER A 1 219  ? 47.380 45.895  -0.090  1.00 12.27 ? 219  SER A C   1 
ATOM   1616 O  O   . SER A 1 219  ? 47.714 46.462  0.948   1.00 12.96 ? 219  SER A O   1 
ATOM   1617 C  CB  . SER A 1 219  ? 47.029 48.142  -1.145  1.00 11.76 ? 219  SER A CB  1 
ATOM   1618 O  OG  . SER A 1 219  ? 47.066 48.871  -2.389  1.00 12.98 ? 219  SER A OG  1 
ATOM   1619 N  N   . GLY A 1 220  ? 47.057 44.606  -0.163  1.00 13.39 ? 220  GLY A N   1 
ATOM   1620 C  CA  . GLY A 1 220  ? 47.132 43.752  1.014   1.00 12.80 ? 220  GLY A CA  1 
ATOM   1621 C  C   . GLY A 1 220  ? 45.929 43.709  1.944   1.00 12.84 ? 220  GLY A C   1 
ATOM   1622 O  O   . GLY A 1 220  ? 45.952 42.956  2.911   1.00 14.50 ? 220  GLY A O   1 
ATOM   1623 N  N   . PHE A 1 221  ? 44.888 44.493  1.676   1.00 13.17 ? 221  PHE A N   1 
ATOM   1624 C  CA  . PHE A 1 221  ? 43.735 44.513  2.585   1.00 10.62 ? 221  PHE A CA  1 
ATOM   1625 C  C   . PHE A 1 221  ? 42.916 43.254  2.512   1.00 11.70 ? 221  PHE A C   1 
ATOM   1626 O  O   . PHE A 1 221  ? 42.846 42.603  1.474   1.00 13.77 ? 221  PHE A O   1 
ATOM   1627 C  CB  . PHE A 1 221  ? 42.831 45.718  2.313   1.00 11.89 ? 221  PHE A CB  1 
ATOM   1628 C  CG  . PHE A 1 221  ? 43.398 46.994  2.830   1.00 10.34 ? 221  PHE A CG  1 
ATOM   1629 C  CD1 . PHE A 1 221  ? 44.529 47.601  2.222   1.00 10.68 ? 221  PHE A CD1 1 
ATOM   1630 C  CD2 . PHE A 1 221  ? 42.833 47.620  3.952   1.00 11.18 ? 221  PHE A CD2 1 
ATOM   1631 C  CE1 . PHE A 1 221  ? 45.053 48.786  2.745   1.00 11.21 ? 221  PHE A CE1 1 
ATOM   1632 C  CE2 . PHE A 1 221  ? 43.344 48.786  4.457   1.00 11.48 ? 221  PHE A CE2 1 
ATOM   1633 C  CZ  . PHE A 1 221  ? 44.474 49.408  3.862   1.00 11.43 ? 221  PHE A CZ  1 
ATOM   1634 N  N   . LYS A 1 222  ? 42.241 42.986  3.622   1.00 12.87 ? 222  LYS A N   1 
ATOM   1635 C  CA  . LYS A 1 222  ? 41.362 41.851  3.710   1.00 12.96 ? 222  LYS A CA  1 
ATOM   1636 C  C   . LYS A 1 222  ? 39.946 42.240  4.098   1.00 13.25 ? 222  LYS A C   1 
ATOM   1637 O  O   . LYS A 1 222  ? 39.020 41.446  3.891   1.00 13.88 ? 222  LYS A O   1 
ATOM   1638 C  CB  . LYS A 1 222  ? 41.885 40.865  4.747   1.00 16.33 ? 222  LYS A CB  1 
ATOM   1639 C  CG  . LYS A 1 222  ? 43.302 40.374  4.521   1.00 19.74 ? 222  LYS A CG  1 
ATOM   1640 C  CD  . LYS A 1 222  ? 43.552 39.613  3.249   1.00 26.60 ? 222  LYS A CD  1 
ATOM   1641 C  CE  . LYS A 1 222  ? 45.014 39.122  3.281   1.00 33.05 ? 222  LYS A CE  1 
ATOM   1642 N  NZ  . LYS A 1 222  ? 45.350 38.228  2.146   1.00 37.84 ? 222  LYS A NZ  1 
ATOM   1643 N  N   . ASN A 1 223  ? 39.760 43.455  4.594   1.00 11.74 ? 223  ASN A N   1 
ATOM   1644 C  CA  . ASN A 1 223  ? 38.440 43.877  5.032   1.00 12.09 ? 223  ASN A CA  1 
ATOM   1645 C  C   . ASN A 1 223  ? 38.274 45.373  4.913   1.00 11.93 ? 223  ASN A C   1 
ATOM   1646 O  O   . ASN A 1 223  ? 39.252 46.104  4.991   1.00 12.02 ? 223  ASN A O   1 
ATOM   1647 C  CB  . ASN A 1 223  ? 38.207 43.531  6.541   1.00 12.34 ? 223  ASN A CB  1 
ATOM   1648 C  CG  . ASN A 1 223  ? 38.278 42.044  6.821   1.00 13.98 ? 223  ASN A CG  1 
ATOM   1649 O  OD1 . ASN A 1 223  ? 39.335 41.534  7.291   1.00 17.56 ? 223  ASN A OD1 1 
ATOM   1650 N  ND2 . ASN A 1 223  ? 37.213 41.334  6.503   1.00 11.41 ? 223  ASN A ND2 1 
ATOM   1651 N  N   . MET A 1 224  ? 37.039 45.814  4.754   1.00 11.50 ? 224  MET A N   1 
ATOM   1652 C  CA  . MET A 1 224  ? 36.764 47.254  4.719   1.00 11.20 ? 224  MET A CA  1 
ATOM   1653 C  C   . MET A 1 224  ? 35.349 47.548  5.281   1.00 12.40 ? 224  MET A C   1 
ATOM   1654 O  O   . MET A 1 224  ? 34.451 46.666  5.280   1.00 12.56 ? 224  MET A O   1 
ATOM   1655 C  CB  . MET A 1 224  ? 36.897 47.841  3.288   1.00 14.47 ? 224  MET A CB  1 
ATOM   1656 C  CG  . MET A 1 224  ? 35.826 47.328  2.317   1.00 14.12 ? 224  MET A CG  1 
ATOM   1657 S  SD  . MET A 1 224  ? 36.029 48.095  0.676   1.00 13.96 ? 224  MET A SD  1 
ATOM   1658 C  CE  . MET A 1 224  ? 35.573 49.710  1.046   1.00 17.13 ? 224  MET A CE  1 
ATOM   1659 N  N   . LEU A 1 225  ? 35.165 48.778  5.740   1.00 12.47 ? 225  LEU A N   1 
ATOM   1660 C  CA  . LEU A 1 225  ? 33.923 49.201  6.316   1.00 11.50 ? 225  LEU A CA  1 
ATOM   1661 C  C   . LEU A 1 225  ? 33.501 50.513  5.677   1.00 13.29 ? 225  LEU A C   1 
ATOM   1662 O  O   . LEU A 1 225  ? 34.336 51.405  5.487   1.00 11.62 ? 225  LEU A O   1 
ATOM   1663 C  CB  . LEU A 1 225  ? 34.117 49.370  7.846   1.00 11.85 ? 225  LEU A CB  1 
ATOM   1664 C  CG  . LEU A 1 225  ? 32.909 49.963  8.588   1.00 12.01 ? 225  LEU A CG  1 
ATOM   1665 C  CD1 . LEU A 1 225  ? 32.814 49.356  10.002  1.00 13.60 ? 225  LEU A CD1 1 
ATOM   1666 C  CD2 . LEU A 1 225  ? 32.975 51.492  8.650   1.00 12.91 ? 225  LEU A CD2 1 
ATOM   1667 N  N   . ILE A 1 226  ? 32.214 50.625  5.403   1.00 11.92 ? 226  ILE A N   1 
ATOM   1668 C  CA  . ILE A 1 226  ? 31.622 51.834  4.840   1.00 11.09 ? 226  ILE A CA  1 
ATOM   1669 C  C   . ILE A 1 226  ? 30.382 52.228  5.610   1.00 11.80 ? 226  ILE A C   1 
ATOM   1670 O  O   . ILE A 1 226  ? 29.807 51.391  6.341   1.00 12.73 ? 226  ILE A O   1 
ATOM   1671 C  CB  . ILE A 1 226  ? 31.328 51.668  3.317   1.00 12.48 ? 226  ILE A CB  1 
ATOM   1672 C  CG1 . ILE A 1 226  ? 30.250 50.607  3.106   1.00 12.15 ? 226  ILE A CG1 1 
ATOM   1673 C  CG2 . ILE A 1 226  ? 32.596 51.295  2.580   1.00 13.53 ? 226  ILE A CG2 1 
ATOM   1674 C  CD1 . ILE A 1 226  ? 29.883 50.400  1.577   1.00 12.83 ? 226  ILE A CD1 1 
ATOM   1675 N  N   . GLN A 1 227  ? 29.933 53.469  5.447   1.00 12.65 ? 227  GLN A N   1 
ATOM   1676 C  CA  . GLN A 1 227  ? 28.791 53.970  6.197   1.00 11.56 ? 227  GLN A CA  1 
ATOM   1677 C  C   . GLN A 1 227  ? 27.788 54.800  5.405   1.00 13.92 ? 227  GLN A C   1 
ATOM   1678 O  O   . GLN A 1 227  ? 26.591 54.570  5.532   1.00 13.87 ? 227  GLN A O   1 
ATOM   1679 C  CB  . GLN A 1 227  ? 29.322 54.804  7.390   1.00 13.43 ? 227  GLN A CB  1 
ATOM   1680 C  CG  . GLN A 1 227  ? 28.341 55.867  7.980   1.00 14.53 ? 227  GLN A CG  1 
ATOM   1681 C  CD  . GLN A 1 227  ? 27.010 55.337  8.494   1.00 14.71 ? 227  GLN A CD  1 
ATOM   1682 O  OE1 . GLN A 1 227  ? 26.870 54.168  8.844   1.00 16.87 ? 227  GLN A OE1 1 
ATOM   1683 N  NE2 . GLN A 1 227  ? 26.032 56.229  8.553   1.00 14.47 ? 227  GLN A NE2 1 
ATOM   1684 N  N   . ARG A 1 228  ? 28.249 55.744  4.596   1.00 13.47 ? 228  ARG A N   1 
ATOM   1685 C  CA  . ARG A 1 228  ? 27.266 56.608  3.958   1.00 11.93 ? 228  ARG A CA  1 
ATOM   1686 C  C   . ARG A 1 228  ? 26.715 56.097  2.680   1.00 13.29 ? 228  ARG A C   1 
ATOM   1687 O  O   . ARG A 1 228  ? 27.279 56.339  1.611   1.00 13.78 ? 228  ARG A O   1 
ATOM   1688 C  CB  . ARG A 1 228  ? 27.833 58.031  3.748   1.00 12.17 ? 228  ARG A CB  1 
ATOM   1689 C  CG  . ARG A 1 228  ? 28.072 58.800  5.042   1.00 11.90 ? 228  ARG A CG  1 
ATOM   1690 C  CD  . ARG A 1 228  ? 28.336 60.289  4.688   1.00 12.49 ? 228  ARG A CD  1 
ATOM   1691 N  NE  . ARG A 1 228  ? 28.633 61.156  5.853   1.00 12.43 ? 228  ARG A NE  1 
ATOM   1692 C  CZ  . ARG A 1 228  ? 27.726 61.845  6.540   1.00 14.71 ? 228  ARG A CZ  1 
ATOM   1693 N  NH1 . ARG A 1 228  ? 26.446 61.745  6.222   1.00 15.03 ? 228  ARG A NH1 1 
ATOM   1694 N  NH2 . ARG A 1 228  ? 28.123 62.725  7.464   1.00 17.03 ? 228  ARG A NH2 1 
ATOM   1695 N  N   . THR A 1 229  ? 25.669 55.289  2.819   1.00 11.78 ? 229  THR A N   1 
ATOM   1696 C  CA  . THR A 1 229  ? 24.952 54.762  1.677   1.00 12.58 ? 229  THR A CA  1 
ATOM   1697 C  C   . THR A 1 229  ? 23.490 55.174  1.868   1.00 12.66 ? 229  THR A C   1 
ATOM   1698 O  O   . THR A 1 229  ? 22.998 55.430  2.983   1.00 14.00 ? 229  THR A O   1 
ATOM   1699 C  CB  . THR A 1 229  ? 25.073 53.213  1.547   1.00 13.68 ? 229  THR A CB  1 
ATOM   1700 O  OG1 . THR A 1 229  ? 24.443 52.616  2.690   1.00 14.00 ? 229  THR A OG1 1 
ATOM   1701 C  CG2 . THR A 1 229  ? 26.538 52.782  1.461   1.00 14.56 ? 229  THR A CG2 1 
ATOM   1702 N  N   . HIS A 1 230  ? 22.789 55.242  0.730   1.00 12.59 ? 230  HIS A N   1 
ATOM   1703 C  CA  . HIS A 1 230  ? 21.377 55.692  0.733   1.00 13.39 ? 230  HIS A CA  1 
ATOM   1704 C  C   . HIS A 1 230  ? 20.558 54.938  1.802   1.00 12.31 ? 230  HIS A C   1 
ATOM   1705 O  O   . HIS A 1 230  ? 20.660 53.730  1.923   1.00 13.27 ? 230  HIS A O   1 
ATOM   1706 C  CB  . HIS A 1 230  ? 20.829 55.447  -0.671  1.00 12.86 ? 230  HIS A CB  1 
ATOM   1707 C  CG  . HIS A 1 230  ? 19.544 56.146  -0.982  1.00 14.32 ? 230  HIS A CG  1 
ATOM   1708 N  ND1 . HIS A 1 230  ? 18.380 55.917  -0.285  1.00 13.75 ? 230  HIS A ND1 1 
ATOM   1709 C  CD2 . HIS A 1 230  ? 19.230 57.022  -1.966  1.00 14.50 ? 230  HIS A CD2 1 
ATOM   1710 C  CE1 . HIS A 1 230  ? 17.404 56.636  -0.809  1.00 14.99 ? 230  HIS A CE1 1 
ATOM   1711 N  NE2 . HIS A 1 230  ? 17.893 57.310  -1.839  1.00 14.53 ? 230  HIS A NE2 1 
ATOM   1712 N  N   . TYR A 1 231  ? 19.748 55.693  2.551   1.00 13.75 ? 231  TYR A N   1 
ATOM   1713 C  CA  . TYR A 1 231  ? 18.949 55.077  3.595   1.00 13.48 ? 231  TYR A CA  1 
ATOM   1714 C  C   . TYR A 1 231  ? 18.075 53.953  3.038   1.00 15.07 ? 231  TYR A C   1 
ATOM   1715 O  O   . TYR A 1 231  ? 17.810 52.977  3.756   1.00 15.73 ? 231  TYR A O   1 
ATOM   1716 C  CB  . TYR A 1 231  ? 18.124 56.130  4.330   1.00 15.01 ? 231  TYR A CB  1 
ATOM   1717 C  CG  . TYR A 1 231  ? 17.117 56.894  3.460   1.00 14.53 ? 231  TYR A CG  1 
ATOM   1718 C  CD1 . TYR A 1 231  ? 15.825 56.400  3.248   1.00 15.75 ? 231  TYR A CD1 1 
ATOM   1719 C  CD2 . TYR A 1 231  ? 17.479 58.110  2.853   1.00 14.43 ? 231  TYR A CD2 1 
ATOM   1720 C  CE1 . TYR A 1 231  ? 14.909 57.085  2.461   1.00 16.51 ? 231  TYR A CE1 1 
ATOM   1721 C  CE2 . TYR A 1 231  ? 16.587 58.807  2.057   1.00 15.85 ? 231  TYR A CE2 1 
ATOM   1722 C  CZ  . TYR A 1 231  ? 15.291 58.292  1.866   1.00 15.34 ? 231  TYR A CZ  1 
ATOM   1723 O  OH  . TYR A 1 231  ? 14.366 59.005  1.103   1.00 17.15 ? 231  TYR A OH  1 
ATOM   1724 N  N   . SER A 1 232  ? 17.657 54.032  1.775   1.00 14.42 ? 232  SER A N   1 
ATOM   1725 C  CA  . SER A 1 232  ? 16.824 52.949  1.233   1.00 15.30 ? 232  SER A CA  1 
ATOM   1726 C  C   . SER A 1 232  ? 17.639 51.697  0.978   1.00 15.17 ? 232  SER A C   1 
ATOM   1727 O  O   . SER A 1 232  ? 17.139 50.573  1.090   1.00 15.04 ? 232  SER A O   1 
ATOM   1728 C  CB  . SER A 1 232  ? 16.157 53.366  -0.067  1.00 16.03 ? 232  SER A CB  1 
ATOM   1729 O  OG  . SER A 1 232  ? 15.224 54.380  0.172   1.00 18.79 ? 232  SER A OG  1 
ATOM   1730 N  N   . VAL A 1 233  ? 18.901 51.886  0.608   1.00 15.32 ? 233  VAL A N   1 
ATOM   1731 C  CA  . VAL A 1 233  ? 19.795 50.757  0.410   1.00 15.03 ? 233  VAL A CA  1 
ATOM   1732 C  C   . VAL A 1 233  ? 20.077 50.075  1.750   1.00 15.14 ? 233  VAL A C   1 
ATOM   1733 O  O   . VAL A 1 233  ? 20.094 48.837  1.829   1.00 15.32 ? 233  VAL A O   1 
ATOM   1734 C  CB  . VAL A 1 233  ? 21.122 51.236  -0.283  1.00 13.97 ? 233  VAL A CB  1 
ATOM   1735 C  CG1 . VAL A 1 233  ? 22.168 50.150  -0.254  1.00 13.97 ? 233  VAL A CG1 1 
ATOM   1736 C  CG2 . VAL A 1 233  ? 20.815 51.584  -1.743  1.00 15.39 ? 233  VAL A CG2 1 
ATOM   1737 N  N   . LYS A 1 234  ? 20.373 50.862  2.784   1.00 14.05 ? 234  LYS A N   1 
ATOM   1738 C  CA  . LYS A 1 234  ? 20.588 50.256  4.100   1.00 15.27 ? 234  LYS A CA  1 
ATOM   1739 C  C   . LYS A 1 234  ? 19.361 49.418  4.495   1.00 15.11 ? 234  LYS A C   1 
ATOM   1740 O  O   . LYS A 1 234  ? 19.536 48.300  4.988   1.00 14.85 ? 234  LYS A O   1 
ATOM   1741 C  CB  . LYS A 1 234  ? 20.788 51.328  5.164   1.00 14.74 ? 234  LYS A CB  1 
ATOM   1742 C  CG  . LYS A 1 234  ? 22.187 51.975  5.120   1.00 16.19 ? 234  LYS A CG  1 
ATOM   1743 C  CD  . LYS A 1 234  ? 22.191 53.293  5.868   1.00 15.90 ? 234  LYS A CD  1 
ATOM   1744 C  CE  . LYS A 1 234  ? 23.614 53.940  5.802   1.00 13.86 ? 234  LYS A CE  1 
ATOM   1745 N  NZ  . LYS A 1 234  ? 24.497 53.377  6.895   1.00 12.79 ? 234  LYS A NZ  1 
ATOM   1746 N  N   . LYS A 1 235  ? 18.144 49.950  4.305   1.00 14.70 ? 235  LYS A N   1 
ATOM   1747 C  CA  . LYS A 1 235  ? 16.938 49.155  4.671   1.00 14.29 ? 235  LYS A CA  1 
ATOM   1748 C  C   . LYS A 1 235  ? 16.826 47.874  3.871   1.00 15.35 ? 235  LYS A C   1 
ATOM   1749 O  O   . LYS A 1 235  ? 16.591 46.785  4.429   1.00 16.38 ? 235  LYS A O   1 
ATOM   1750 C  CB  . LYS A 1 235  ? 15.690 50.009  4.472   1.00 16.22 ? 235  LYS A CB  1 
ATOM   1751 C  CG  . LYS A 1 235  ? 14.383 49.316  4.925   1.00 17.38 ? 235  LYS A CG  1 
ATOM   1752 C  CD  . LYS A 1 235  ? 13.219 50.296  4.820   1.00 16.63 ? 235  LYS A CD  1 
ATOM   1753 C  CE  . LYS A 1 235  ? 11.930 49.601  5.293   1.00 20.35 ? 235  LYS A CE  1 
ATOM   1754 N  NZ  . LYS A 1 235  ? 10.749 50.525  5.253   1.00 30.18 ? 235  LYS A NZ  1 
ATOM   1755 N  N   . GLU A 1 236  ? 17.009 47.960  2.568   1.00 15.27 ? 236  GLU A N   1 
ATOM   1756 C  CA  . GLU A 1 236  ? 16.897 46.799  1.710   1.00 16.13 ? 236  GLU A CA  1 
ATOM   1757 C  C   . GLU A 1 236  ? 17.921 45.720  2.041   1.00 17.67 ? 236  GLU A C   1 
ATOM   1758 O  O   . GLU A 1 236  ? 17.613 44.526  2.133   1.00 17.69 ? 236  GLU A O   1 
ATOM   1759 C  CB  . GLU A 1 236  ? 17.086 47.256  0.268   1.00 19.60 ? 236  GLU A CB  1 
ATOM   1760 C  CG  . GLU A 1 236  ? 16.809 46.190  -0.782  1.00 25.65 ? 236  GLU A CG  1 
ATOM   1761 C  CD  . GLU A 1 236  ? 15.311 45.875  -0.926  1.00 31.10 ? 236  GLU A CD  1 
ATOM   1762 O  OE1 . GLU A 1 236  ? 14.449 46.655  -0.443  1.00 33.61 ? 236  GLU A OE1 1 
ATOM   1763 O  OE2 . GLU A 1 236  ? 15.009 44.837  -1.535  1.00 34.42 ? 236  GLU A OE2 1 
ATOM   1764 N  N   . LEU A 1 237  ? 19.171 46.129  2.203   1.00 15.02 ? 237  LEU A N   1 
ATOM   1765 C  CA  . LEU A 1 237  ? 20.200 45.141  2.509   1.00 16.48 ? 237  LEU A CA  1 
ATOM   1766 C  C   . LEU A 1 237  ? 20.039 44.604  3.928   1.00 15.62 ? 237  LEU A C   1 
ATOM   1767 O  O   . LEU A 1 237  ? 20.272 43.399  4.156   1.00 18.13 ? 237  LEU A O   1 
ATOM   1768 C  CB  . LEU A 1 237  ? 21.609 45.712  2.300   1.00 15.15 ? 237  LEU A CB  1 
ATOM   1769 C  CG  . LEU A 1 237  ? 21.948 46.130  0.862   1.00 14.70 ? 237  LEU A CG  1 
ATOM   1770 C  CD1 . LEU A 1 237  ? 23.365 46.758  0.908   1.00 16.42 ? 237  LEU A CD1 1 
ATOM   1771 C  CD2 . LEU A 1 237  ? 21.850 44.971  -0.134  1.00 16.66 ? 237  LEU A CD2 1 
ATOM   1772 N  N   . ALA A 1 238  ? 19.612 45.445  4.864   1.00 16.00 ? 238  ALA A N   1 
ATOM   1773 C  CA  . ALA A 1 238  ? 19.395 44.970  6.226   1.00 15.48 ? 238  ALA A CA  1 
ATOM   1774 C  C   . ALA A 1 238  ? 18.315 43.891  6.240   1.00 18.42 ? 238  ALA A C   1 
ATOM   1775 O  O   . ALA A 1 238  ? 18.474 42.882  6.946   1.00 17.58 ? 238  ALA A O   1 
ATOM   1776 C  CB  . ALA A 1 238  ? 18.989 46.119  7.132   1.00 16.02 ? 238  ALA A CB  1 
ATOM   1777 N  N   . GLN A 1 239  ? 17.246 44.096  5.467   1.00 16.52 ? 239  GLN A N   1 
ATOM   1778 C  CA  . GLN A 1 239  ? 16.159 43.110  5.466   1.00 18.69 ? 239  GLN A CA  1 
ATOM   1779 C  C   . GLN A 1 239  ? 16.624 41.737  5.013   1.00 20.83 ? 239  GLN A C   1 
ATOM   1780 O  O   . GLN A 1 239  ? 16.087 40.725  5.455   1.00 21.51 ? 239  GLN A O   1 
ATOM   1781 C  CB  . GLN A 1 239  ? 15.027 43.600  4.593   1.00 17.57 ? 239  GLN A CB  1 
ATOM   1782 C  CG  . GLN A 1 239  ? 14.283 44.752  5.257   1.00 22.65 ? 239  GLN A CG  1 
ATOM   1783 C  CD  . GLN A 1 239  ? 13.160 45.344  4.411   1.00 26.98 ? 239  GLN A CD  1 
ATOM   1784 O  OE1 . GLN A 1 239  ? 13.250 45.444  3.175   1.00 31.47 ? 239  GLN A OE1 1 
ATOM   1785 N  NE2 . GLN A 1 239  ? 12.101 45.774  5.086   1.00 32.33 ? 239  GLN A NE2 1 
ATOM   1786 N  N   . GLN A 1 240  ? 17.612 41.684  4.125   1.00 18.38 ? 240  GLN A N   1 
ATOM   1787 C  CA  . GLN A 1 240  ? 18.140 40.421  3.621   1.00 19.23 ? 240  GLN A CA  1 
ATOM   1788 C  C   . GLN A 1 240  ? 19.446 40.001  4.288   1.00 16.71 ? 240  GLN A C   1 
ATOM   1789 O  O   . GLN A 1 240  ? 20.058 39.035  3.862   1.00 16.57 ? 240  GLN A O   1 
ATOM   1790 C  CB  . GLN A 1 240  ? 18.413 40.521  2.118   1.00 20.23 ? 240  GLN A CB  1 
ATOM   1791 C  CG  . GLN A 1 240  ? 17.253 41.091  1.309   1.00 23.99 ? 240  GLN A CG  1 
ATOM   1792 C  CD  . GLN A 1 240  ? 16.013 40.242  1.458   1.00 25.67 ? 240  GLN A CD  1 
ATOM   1793 O  OE1 . GLN A 1 240  ? 14.881 40.760  1.540   1.00 32.75 ? 240  GLN A OE1 1 
ATOM   1794 N  NE2 . GLN A 1 240  ? 16.207 38.938  1.504   1.00 26.56 ? 240  GLN A NE2 1 
ATOM   1795 N  N   . ARG A 1 241  ? 19.853 40.721  5.334   1.00 16.77 ? 241  ARG A N   1 
ATOM   1796 C  CA  . ARG A 1 241  ? 21.132 40.476  5.995   1.00 15.12 ? 241  ARG A CA  1 
ATOM   1797 C  C   . ARG A 1 241  ? 22.247 40.430  4.959   1.00 14.89 ? 241  ARG A C   1 
ATOM   1798 O  O   . ARG A 1 241  ? 23.075 39.525  4.920   1.00 13.97 ? 241  ARG A O   1 
ATOM   1799 C  CB  . ARG A 1 241  ? 21.123 39.189  6.834   1.00 15.58 ? 241  ARG A CB  1 
ATOM   1800 C  CG  . ARG A 1 241  ? 20.109 39.288  7.974   1.00 17.07 ? 241  ARG A CG  1 
ATOM   1801 C  CD  . ARG A 1 241  ? 20.194 38.142  8.966   1.00 19.50 ? 241  ARG A CD  1 
ATOM   1802 N  NE  . ARG A 1 241  ? 20.185 36.841  8.337   1.00 27.50 ? 241  ARG A NE  1 
ATOM   1803 C  CZ  . ARG A 1 241  ? 20.627 35.734  8.935   1.00 30.65 ? 241  ARG A CZ  1 
ATOM   1804 N  NH1 . ARG A 1 241  ? 21.102 35.796  10.180  1.00 31.70 ? 241  ARG A NH1 1 
ATOM   1805 N  NH2 . ARG A 1 241  ? 20.639 34.582  8.271   1.00 31.33 ? 241  ARG A NH2 1 
ATOM   1806 N  N   . GLN A 1 242  ? 22.247 41.466  4.110   1.00 14.56 ? 242  GLN A N   1 
ATOM   1807 C  CA  . GLN A 1 242  ? 23.274 41.594  3.061   1.00 13.75 ? 242  GLN A CA  1 
ATOM   1808 C  C   . GLN A 1 242  ? 24.129 42.840  3.307   1.00 14.02 ? 242  GLN A C   1 
ATOM   1809 O  O   . GLN A 1 242  ? 24.704 43.416  2.361   1.00 15.56 ? 242  GLN A O   1 
ATOM   1810 C  CB  . GLN A 1 242  ? 22.601 41.648  1.679   1.00 14.91 ? 242  GLN A CB  1 
ATOM   1811 C  CG  . GLN A 1 242  ? 21.974 40.305  1.280   1.00 15.51 ? 242  GLN A CG  1 
ATOM   1812 C  CD  . GLN A 1 242  ? 21.151 40.425  0.024   1.00 15.74 ? 242  GLN A CD  1 
ATOM   1813 O  OE1 . GLN A 1 242  ? 20.606 41.486  -0.269  1.00 16.89 ? 242  GLN A OE1 1 
ATOM   1814 N  NE2 . GLN A 1 242  ? 21.080 39.337  -0.727  1.00 17.80 ? 242  GLN A NE2 1 
ATOM   1815 N  N   . LEU A 1 243  ? 24.234 43.229  4.585   1.00 14.83 ? 243  LEU A N   1 
ATOM   1816 C  CA  . LEU A 1 243  ? 25.060 44.385  4.942   1.00 13.46 ? 243  LEU A CA  1 
ATOM   1817 C  C   . LEU A 1 243  ? 26.547 44.041  4.974   1.00 14.02 ? 243  LEU A C   1 
ATOM   1818 O  O   . LEU A 1 243  ? 27.373 44.959  4.982   1.00 13.97 ? 243  LEU A O   1 
ATOM   1819 C  CB  . LEU A 1 243  ? 24.614 44.962  6.283   1.00 12.22 ? 243  LEU A CB  1 
ATOM   1820 C  CG  . LEU A 1 243  ? 23.250 45.673  6.267   1.00 15.00 ? 243  LEU A CG  1 
ATOM   1821 C  CD1 . LEU A 1 243  ? 22.813 45.849  7.723   1.00 18.18 ? 243  LEU A CD1 1 
ATOM   1822 C  CD2 . LEU A 1 243  ? 23.303 47.055  5.542   1.00 15.74 ? 243  LEU A CD2 1 
ATOM   1823 N  N   . GLU A 1 244  ? 26.908 42.757  5.043   1.00 12.35 ? 244  GLU A N   1 
ATOM   1824 C  CA  . GLU A 1 244  ? 28.281 42.322  4.929   1.00 12.89 ? 244  GLU A CA  1 
ATOM   1825 C  C   . GLU A 1 244  ? 28.297 41.526  3.642   1.00 12.45 ? 244  GLU A C   1 
ATOM   1826 O  O   . GLU A 1 244  ? 27.466 40.610  3.450   1.00 14.45 ? 244  GLU A O   1 
ATOM   1827 C  CB  . GLU A 1 244  ? 28.717 41.480  6.132   1.00 12.60 ? 244  GLU A CB  1 
ATOM   1828 C  CG  . GLU A 1 244  ? 29.001 42.406  7.320   1.00 13.03 ? 244  GLU A CG  1 
ATOM   1829 C  CD  . GLU A 1 244  ? 29.342 41.705  8.607   1.00 13.37 ? 244  GLU A CD  1 
ATOM   1830 O  OE1 . GLU A 1 244  ? 28.766 40.645  8.898   1.00 15.72 ? 244  GLU A OE1 1 
ATOM   1831 O  OE2 . GLU A 1 244  ? 30.180 42.269  9.340   1.00 13.22 ? 244  GLU A OE2 1 
ATOM   1832 N  N   . PHE A 1 245  ? 29.247 41.835  2.764   1.00 12.22 ? 245  PHE A N   1 
ATOM   1833 C  CA  . PHE A 1 245  ? 29.297 41.188  1.467   1.00 12.62 ? 245  PHE A CA  1 
ATOM   1834 C  C   . PHE A 1 245  ? 30.703 41.164  0.905   1.00 12.20 ? 245  PHE A C   1 
ATOM   1835 O  O   . PHE A 1 245  ? 31.593 41.922  1.355   1.00 12.96 ? 245  PHE A O   1 
ATOM   1836 C  CB  . PHE A 1 245  ? 28.346 41.936  0.487   1.00 12.90 ? 245  PHE A CB  1 
ATOM   1837 C  CG  . PHE A 1 245  ? 28.490 43.423  0.528   1.00 12.71 ? 245  PHE A CG  1 
ATOM   1838 C  CD1 . PHE A 1 245  ? 29.431 44.063  -0.279  1.00 12.11 ? 245  PHE A CD1 1 
ATOM   1839 C  CD2 . PHE A 1 245  ? 27.687 44.199  1.383   1.00 13.18 ? 245  PHE A CD2 1 
ATOM   1840 C  CE1 . PHE A 1 245  ? 29.579 45.503  -0.255  1.00 13.49 ? 245  PHE A CE1 1 
ATOM   1841 C  CE2 . PHE A 1 245  ? 27.836 45.618  1.416   1.00 12.73 ? 245  PHE A CE2 1 
ATOM   1842 C  CZ  . PHE A 1 245  ? 28.791 46.253  0.578   1.00 12.22 ? 245  PHE A CZ  1 
ATOM   1843 N  N   . LEU A 1 246  ? 30.915 40.321  -0.098  1.00 13.06 ? 246  LEU A N   1 
ATOM   1844 C  CA  . LEU A 1 246  ? 32.188 40.225  -0.813  1.00 11.83 ? 246  LEU A CA  1 
ATOM   1845 C  C   . LEU A 1 246  ? 32.029 41.155  -1.998  1.00 12.43 ? 246  LEU A C   1 
ATOM   1846 O  O   . LEU A 1 246  ? 31.364 40.836  -2.995  1.00 12.55 ? 246  LEU A O   1 
ATOM   1847 C  CB  . LEU A 1 246  ? 32.432 38.761  -1.229  1.00 13.12 ? 246  LEU A CB  1 
ATOM   1848 C  CG  . LEU A 1 246  ? 32.764 37.876  -0.004  1.00 16.63 ? 246  LEU A CG  1 
ATOM   1849 C  CD1 . LEU A 1 246  ? 32.733 36.387  -0.427  1.00 20.39 ? 246  LEU A CD1 1 
ATOM   1850 C  CD2 . LEU A 1 246  ? 34.155 38.213  0.481   1.00 21.34 ? 246  LEU A CD2 1 
ATOM   1851 N  N   . TRP A 1 247  ? 32.649 42.315  -1.909  1.00 12.13 ? 247  TRP A N   1 
ATOM   1852 C  CA  . TRP A 1 247  ? 32.480 43.347  -2.929  1.00 11.22 ? 247  TRP A CA  1 
ATOM   1853 C  C   . TRP A 1 247  ? 33.509 43.153  -4.041  1.00 12.29 ? 247  TRP A C   1 
ATOM   1854 O  O   . TRP A 1 247  ? 34.714 43.344  -3.831  1.00 12.19 ? 247  TRP A O   1 
ATOM   1855 C  CB  . TRP A 1 247  ? 32.694 44.715  -2.272  1.00 11.75 ? 247  TRP A CB  1 
ATOM   1856 C  CG  . TRP A 1 247  ? 32.209 45.902  -3.101  1.00 11.79 ? 247  TRP A CG  1 
ATOM   1857 C  CD1 . TRP A 1 247  ? 31.652 45.880  -4.352  1.00 10.90 ? 247  TRP A CD1 1 
ATOM   1858 C  CD2 . TRP A 1 247  ? 32.226 47.256  -2.690  1.00 11.33 ? 247  TRP A CD2 1 
ATOM   1859 N  NE1 . TRP A 1 247  ? 31.300 47.177  -4.732  1.00 11.30 ? 247  TRP A NE1 1 
ATOM   1860 C  CE2 . TRP A 1 247  ? 31.639 48.035  -3.721  1.00 10.66 ? 247  TRP A CE2 1 
ATOM   1861 C  CE3 . TRP A 1 247  ? 32.664 47.899  -1.536  1.00 12.18 ? 247  TRP A CE3 1 
ATOM   1862 C  CZ2 . TRP A 1 247  ? 31.489 49.424  -3.628  1.00 13.32 ? 247  TRP A CZ2 1 
ATOM   1863 C  CZ3 . TRP A 1 247  ? 32.515 49.284  -1.440  1.00 10.51 ? 247  TRP A CZ3 1 
ATOM   1864 C  CH2 . TRP A 1 247  ? 31.938 50.039  -2.470  1.00 11.43 ? 247  TRP A CH2 1 
ATOM   1865 N  N   . ARG A 1 248  ? 33.017 42.744  -5.216  1.00 11.44 ? 248  ARG A N   1 
ATOM   1866 C  CA  . ARG A 1 248  ? 33.909 42.576  -6.357  1.00 12.39 ? 248  ARG A CA  1 
ATOM   1867 C  C   . ARG A 1 248  ? 33.613 43.628  -7.399  1.00 11.89 ? 248  ARG A C   1 
ATOM   1868 O  O   . ARG A 1 248  ? 32.561 44.262  -7.355  1.00 11.67 ? 248  ARG A O   1 
ATOM   1869 C  CB  . ARG A 1 248  ? 33.704 41.204  -7.037  1.00 13.53 ? 248  ARG A CB  1 
ATOM   1870 C  CG  . ARG A 1 248  ? 32.299 41.039  -7.654  1.00 11.92 ? 248  ARG A CG  1 
ATOM   1871 C  CD  . ARG A 1 248  ? 32.227 39.730  -8.487  1.00 15.35 ? 248  ARG A CD  1 
ATOM   1872 N  NE  . ARG A 1 248  ? 32.273 38.568  -7.617  1.00 15.51 ? 248  ARG A NE  1 
ATOM   1873 C  CZ  . ARG A 1 248  ? 32.220 37.311  -8.055  1.00 19.03 ? 248  ARG A CZ  1 
ATOM   1874 N  NH1 . ARG A 1 248  ? 32.142 37.071  -9.360  1.00 18.38 ? 248  ARG A NH1 1 
ATOM   1875 N  NH2 . ARG A 1 248  ? 32.213 36.302  -7.186  1.00 19.91 ? 248  ARG A NH2 1 
ATOM   1876 N  N   . GLN A 1 249  ? 34.542 43.766  -8.353  1.00 12.01 ? 249  GLN A N   1 
ATOM   1877 C  CA  . GLN A 1 249  ? 34.340 44.739  -9.432  1.00 12.03 ? 249  GLN A CA  1 
ATOM   1878 C  C   . GLN A 1 249  ? 33.233 44.288  -10.378 1.00 13.36 ? 249  GLN A C   1 
ATOM   1879 O  O   . GLN A 1 249  ? 32.933 43.107  -10.519 1.00 13.90 ? 249  GLN A O   1 
ATOM   1880 C  CB  . GLN A 1 249  ? 35.671 44.931  -10.193 1.00 12.37 ? 249  GLN A CB  1 
ATOM   1881 C  CG  . GLN A 1 249  ? 36.787 45.426  -9.250  1.00 13.00 ? 249  GLN A CG  1 
ATOM   1882 C  CD  . GLN A 1 249  ? 36.385 46.719  -8.522  1.00 14.96 ? 249  GLN A CD  1 
ATOM   1883 O  OE1 . GLN A 1 249  ? 36.367 46.788  -7.235  1.00 15.57 ? 249  GLN A OE1 1 
ATOM   1884 N  NE2 . GLN A 1 249  ? 36.063 47.743  -9.282  1.00 10.80 ? 249  GLN A NE2 1 
ATOM   1885 N  N   . ILE A 1 250  ? 32.602 45.266  -11.010 1.00 12.37 ? 250  ILE A N   1 
ATOM   1886 C  CA  . ILE A 1 250  ? 31.468 44.954  -11.886 1.00 13.78 ? 250  ILE A CA  1 
ATOM   1887 C  C   . ILE A 1 250  ? 31.746 44.032  -13.056 1.00 14.17 ? 250  ILE A C   1 
ATOM   1888 O  O   . ILE A 1 250  ? 30.814 43.377  -13.530 1.00 15.45 ? 250  ILE A O   1 
ATOM   1889 C  CB  . ILE A 1 250  ? 30.764 46.248  -12.403 1.00 14.40 ? 250  ILE A CB  1 
ATOM   1890 C  CG1 . ILE A 1 250  ? 31.748 47.151  -13.155 1.00 15.56 ? 250  ILE A CG1 1 
ATOM   1891 C  CG2 . ILE A 1 250  ? 30.091 46.977  -11.238 1.00 14.87 ? 250  ILE A CG2 1 
ATOM   1892 C  CD1 . ILE A 1 250  ? 31.114 48.495  -13.645 1.00 17.23 ? 250  ILE A CD1 1 
ATOM   1893 N  N   . TRP A 1 251  ? 32.998 43.994  -13.511 1.00 14.94 ? 251  TRP A N   1 
ATOM   1894 C  CA  . TRP A 1 251  ? 33.361 43.131  -14.628 1.00 15.86 ? 251  TRP A CA  1 
ATOM   1895 C  C   . TRP A 1 251  ? 33.995 41.826  -14.204 1.00 20.78 ? 251  TRP A C   1 
ATOM   1896 O  O   . TRP A 1 251  ? 34.340 41.021  -15.061 1.00 19.34 ? 251  TRP A O   1 
ATOM   1897 C  CB  . TRP A 1 251  ? 34.360 43.854  -15.528 1.00 16.53 ? 251  TRP A CB  1 
ATOM   1898 C  CG  . TRP A 1 251  ? 35.620 44.022  -14.831 1.00 20.81 ? 251  TRP A CG  1 
ATOM   1899 C  CD1 . TRP A 1 251  ? 36.593 43.055  -14.638 1.00 20.77 ? 251  TRP A CD1 1 
ATOM   1900 C  CD2 . TRP A 1 251  ? 36.050 45.164  -14.123 1.00 19.67 ? 251  TRP A CD2 1 
ATOM   1901 N  NE1 . TRP A 1 251  ? 37.577 43.539  -13.863 1.00 20.25 ? 251  TRP A NE1 1 
ATOM   1902 C  CE2 . TRP A 1 251  ? 37.283 44.832  -13.522 1.00 18.15 ? 251  TRP A CE2 1 
ATOM   1903 C  CE3 . TRP A 1 251  ? 35.515 46.431  -13.920 1.00 19.19 ? 251  TRP A CE3 1 
ATOM   1904 C  CZ2 . TRP A 1 251  ? 37.996 45.717  -12.728 1.00 17.31 ? 251  TRP A CZ2 1 
ATOM   1905 C  CZ3 . TRP A 1 251  ? 36.224 47.325  -13.120 1.00 19.76 ? 251  TRP A CZ3 1 
ATOM   1906 C  CH2 . TRP A 1 251  ? 37.456 46.957  -12.536 1.00 21.33 ? 251  TRP A CH2 1 
ATOM   1907 N  N   . ASP A 1 252  ? 34.148 41.607  -12.901 1.00 16.87 ? 252  ASP A N   1 
ATOM   1908 C  CA  . ASP A 1 252  ? 34.866 40.440  -12.393 1.00 18.82 ? 252  ASP A CA  1 
ATOM   1909 C  C   . ASP A 1 252  ? 34.045 39.182  -12.291 1.00 18.80 ? 252  ASP A C   1 
ATOM   1910 O  O   . ASP A 1 252  ? 33.278 38.965  -11.378 1.00 17.72 ? 252  ASP A O   1 
ATOM   1911 C  CB  . ASP A 1 252  ? 35.486 40.839  -11.044 1.00 16.27 ? 252  ASP A CB  1 
ATOM   1912 C  CG  . ASP A 1 252  ? 36.257 39.703  -10.398 1.00 20.27 ? 252  ASP A CG  1 
ATOM   1913 O  OD1 . ASP A 1 252  ? 36.525 38.708  -11.097 1.00 23.93 ? 252  ASP A OD1 1 
ATOM   1914 O  OD2 . ASP A 1 252  ? 36.587 39.818  -9.201  1.00 18.74 ? 252  ASP A OD2 1 
ATOM   1915 N  N   . ASN A 1 253  ? 34.205 38.331  -13.293 1.00 21.03 ? 253  ASN A N   1 
ATOM   1916 C  CA  . ASN A 1 253  ? 33.444 37.108  -13.369 1.00 21.53 ? 253  ASN A CA  1 
ATOM   1917 C  C   . ASN A 1 253  ? 33.874 36.066  -12.334 1.00 19.23 ? 253  ASN A C   1 
ATOM   1918 O  O   . ASN A 1 253  ? 33.030 35.393  -11.755 1.00 23.80 ? 253  ASN A O   1 
ATOM   1919 C  CB  . ASN A 1 253  ? 33.618 36.548  -14.781 1.00 23.22 ? 253  ASN A CB  1 
ATOM   1920 C  CG  . ASN A 1 253  ? 32.822 35.305  -15.011 1.00 30.08 ? 253  ASN A CG  1 
ATOM   1921 O  OD1 . ASN A 1 253  ? 33.347 34.322  -15.553 1.00 34.64 ? 253  ASN A OD1 1 
ATOM   1922 N  ND2 . ASN A 1 253  ? 31.550 35.324  -14.625 1.00 28.48 ? 253  ASN A ND2 1 
ATOM   1923 N  N   . LYS A 1 254  ? 35.175 35.981  -12.113 1.00 22.72 ? 254  LYS A N   1 
ATOM   1924 C  CA  . LYS A 1 254  ? 35.747 34.993  -11.192 1.00 24.70 ? 254  LYS A CA  1 
ATOM   1925 C  C   . LYS A 1 254  ? 35.645 35.349  -9.725  1.00 24.43 ? 254  LYS A C   1 
ATOM   1926 O  O   . LYS A 1 254  ? 35.463 34.471  -8.873  1.00 25.70 ? 254  LYS A O   1 
ATOM   1927 C  CB  . LYS A 1 254  ? 37.219 34.772  -11.547 1.00 29.80 ? 254  LYS A CB  1 
ATOM   1928 C  CG  . LYS A 1 254  ? 37.828 33.484  -11.002 1.00 35.70 ? 254  LYS A CG  1 
ATOM   1929 C  CD  . LYS A 1 254  ? 39.225 33.246  -11.601 1.00 38.40 ? 254  LYS A CD  1 
ATOM   1930 C  CE  . LYS A 1 254  ? 39.948 32.100  -10.864 1.00 39.49 ? 254  LYS A CE  1 
ATOM   1931 N  NZ  . LYS A 1 254  ? 39.940 32.262  -9.372  1.00 40.20 ? 254  LYS A NZ  1 
ATOM   1932 N  N   . GLY A 1 255  ? 35.765 36.639  -9.434  1.00 23.46 ? 255  GLY A N   1 
ATOM   1933 C  CA  . GLY A 1 255  ? 35.705 37.101  -8.059  1.00 20.78 ? 255  GLY A CA  1 
ATOM   1934 C  C   . GLY A 1 255  ? 37.069 37.361  -7.425  1.00 20.43 ? 255  GLY A C   1 
ATOM   1935 O  O   . GLY A 1 255  ? 37.096 37.626  -6.227  1.00 20.04 ? 255  GLY A O   1 
ATOM   1936 N  N   . ASP A 1 256  ? 38.180 37.340  -8.160  1.00 19.77 ? 256  ASP A N   1 
ATOM   1937 C  CA  . ASP A 1 256  ? 39.467 37.561  -7.510  1.00 22.33 ? 256  ASP A CA  1 
ATOM   1938 C  C   . ASP A 1 256  ? 39.676 38.961  -6.993  1.00 19.77 ? 256  ASP A C   1 
ATOM   1939 O  O   . ASP A 1 256  ? 40.622 39.195  -6.239  1.00 20.71 ? 256  ASP A O   1 
ATOM   1940 C  CB  . ASP A 1 256  ? 40.656 37.235  -8.427  1.00 27.25 ? 256  ASP A CB  1 
ATOM   1941 C  CG  . ASP A 1 256  ? 40.608 35.830  -8.977  1.00 34.79 ? 256  ASP A CG  1 
ATOM   1942 O  OD1 . ASP A 1 256  ? 40.094 34.921  -8.273  1.00 37.58 ? 256  ASP A OD1 1 
ATOM   1943 O  OD2 . ASP A 1 256  ? 41.108 35.655  -10.117 1.00 37.71 ? 256  ASP A OD2 1 
ATOM   1944 N  N   . THR A 1 257  ? 38.827 39.909  -7.397  1.00 15.63 ? 257  THR A N   1 
ATOM   1945 C  CA  . THR A 1 257  ? 38.954 41.271  -6.867  1.00 16.09 ? 257  THR A CA  1 
ATOM   1946 C  C   . THR A 1 257  ? 38.159 41.453  -5.564  1.00 16.49 ? 257  THR A C   1 
ATOM   1947 O  O   . THR A 1 257  ? 38.276 42.524  -4.945  1.00 16.17 ? 257  THR A O   1 
ATOM   1948 C  CB  . THR A 1 257  ? 38.422 42.347  -7.861  1.00 15.71 ? 257  THR A CB  1 
ATOM   1949 O  OG1 . THR A 1 257  ? 37.011 42.150  -8.062  1.00 15.06 ? 257  THR A OG1 1 
ATOM   1950 C  CG2 . THR A 1 257  ? 39.226 42.243  -9.218  1.00 17.09 ? 257  THR A CG2 1 
ATOM   1951 N  N   . ALA A 1 258  ? 37.393 40.432  -5.152  1.00 15.80 ? 258  ALA A N   1 
ATOM   1952 C  CA  . ALA A 1 258  ? 36.519 40.570  -3.979  1.00 14.06 ? 258  ALA A CA  1 
ATOM   1953 C  C   . ALA A 1 258  ? 37.208 40.961  -2.696  1.00 13.80 ? 258  ALA A C   1 
ATOM   1954 O  O   . ALA A 1 258  ? 38.309 40.469  -2.375  1.00 15.88 ? 258  ALA A O   1 
ATOM   1955 C  CB  . ALA A 1 258  ? 35.764 39.316  -3.715  1.00 16.76 ? 258  ALA A CB  1 
ATOM   1956 N  N   . LEU A 1 259  ? 36.542 41.855  -1.971  1.00 11.21 ? 259  LEU A N   1 
ATOM   1957 C  CA  . LEU A 1 259  ? 37.043 42.302  -0.655  1.00 12.41 ? 259  LEU A CA  1 
ATOM   1958 C  C   . LEU A 1 259  ? 35.863 42.289  0.265   1.00 12.49 ? 259  LEU A C   1 
ATOM   1959 O  O   . LEU A 1 259  ? 34.803 42.877  -0.019  1.00 12.48 ? 259  LEU A O   1 
ATOM   1960 C  CB  . LEU A 1 259  ? 37.614 43.723  -0.714  1.00 12.48 ? 259  LEU A CB  1 
ATOM   1961 C  CG  . LEU A 1 259  ? 38.406 44.128  0.556   1.00 11.83 ? 259  LEU A CG  1 
ATOM   1962 C  CD1 . LEU A 1 259  ? 39.645 43.196  0.787   1.00 12.96 ? 259  LEU A CD1 1 
ATOM   1963 C  CD2 . LEU A 1 259  ? 38.858 45.623  0.414   1.00 14.79 ? 259  LEU A CD2 1 
ATOM   1964 N  N   . PHE A 1 260  ? 36.036 41.648  1.424   1.00 12.66 ? 260  PHE A N   1 
ATOM   1965 C  CA  . PHE A 1 260  ? 34.953 41.589  2.406   1.00 12.77 ? 260  PHE A CA  1 
ATOM   1966 C  C   . PHE A 1 260  ? 34.630 42.990  2.895   1.00 11.82 ? 260  PHE A C   1 
ATOM   1967 O  O   . PHE A 1 260  ? 35.542 43.732  3.322   1.00 12.12 ? 260  PHE A O   1 
ATOM   1968 C  CB  . PHE A 1 260  ? 35.364 40.712  3.592   1.00 12.82 ? 260  PHE A CB  1 
ATOM   1969 C  CG  . PHE A 1 260  ? 34.255 40.527  4.591   1.00 12.53 ? 260  PHE A CG  1 
ATOM   1970 C  CD1 . PHE A 1 260  ? 33.276 39.541  4.383   1.00 14.52 ? 260  PHE A CD1 1 
ATOM   1971 C  CD2 . PHE A 1 260  ? 34.167 41.323  5.715   1.00 13.00 ? 260  PHE A CD2 1 
ATOM   1972 C  CE1 . PHE A 1 260  ? 32.232 39.379  5.320   1.00 16.56 ? 260  PHE A CE1 1 
ATOM   1973 C  CE2 . PHE A 1 260  ? 33.133 41.178  6.634   1.00 15.34 ? 260  PHE A CE2 1 
ATOM   1974 C  CZ  . PHE A 1 260  ? 32.174 40.210  6.437   1.00 14.36 ? 260  PHE A CZ  1 
ATOM   1975 N  N   . THR A 1 261  ? 33.347 43.368  2.862   1.00 11.88 ? 261  THR A N   1 
ATOM   1976 C  CA  . THR A 1 261  ? 32.924 44.716  3.211   1.00 11.40 ? 261  THR A CA  1 
ATOM   1977 C  C   . THR A 1 261  ? 31.811 44.673  4.218   1.00 10.04 ? 261  THR A C   1 
ATOM   1978 O  O   . THR A 1 261  ? 30.882 43.899  4.099   1.00 12.24 ? 261  THR A O   1 
ATOM   1979 C  CB  . THR A 1 261  ? 32.412 45.427  1.937   1.00 12.53 ? 261  THR A CB  1 
ATOM   1980 O  OG1 . THR A 1 261  ? 33.475 45.467  0.978   1.00 12.08 ? 261  THR A OG1 1 
ATOM   1981 C  CG2 . THR A 1 261  ? 31.958 46.833  2.240   1.00 11.57 ? 261  THR A CG2 1 
ATOM   1982 N  N   . HIS A 1 262  ? 31.911 45.543  5.215   1.00 11.52 ? 262  HIS A N   1 
ATOM   1983 C  CA  . HIS A 1 262  ? 30.854 45.714  6.223   1.00 11.51 ? 262  HIS A CA  1 
ATOM   1984 C  C   . HIS A 1 262  ? 30.204 47.084  6.029   1.00 12.12 ? 262  HIS A C   1 
ATOM   1985 O  O   . HIS A 1 262  ? 30.917 48.113  6.098   1.00 11.86 ? 262  HIS A O   1 
ATOM   1986 C  CB  . HIS A 1 262  ? 31.481 45.659  7.633   1.00 12.34 ? 262  HIS A CB  1 
ATOM   1987 C  CG  . HIS A 1 262  ? 30.527 46.034  8.730   1.00 10.52 ? 262  HIS A CG  1 
ATOM   1988 N  ND1 . HIS A 1 262  ? 29.911 45.079  9.519   1.00 11.85 ? 262  HIS A ND1 1 
ATOM   1989 C  CD2 . HIS A 1 262  ? 30.084 47.243  9.176   1.00 11.34 ? 262  HIS A CD2 1 
ATOM   1990 C  CE1 . HIS A 1 262  ? 29.140 45.694  10.417  1.00 13.03 ? 262  HIS A CE1 1 
ATOM   1991 N  NE2 . HIS A 1 262  ? 29.219 46.999  10.233  1.00 13.29 ? 262  HIS A NE2 1 
ATOM   1992 N  N   . MET A 1 263  ? 28.910 47.127  5.740   1.00 11.59 ? 263  MET A N   1 
ATOM   1993 C  CA  . MET A 1 263  ? 28.217 48.395  5.674   1.00 11.39 ? 263  MET A CA  1 
ATOM   1994 C  C   . MET A 1 263  ? 27.466 48.606  7.003   1.00 13.26 ? 263  MET A C   1 
ATOM   1995 O  O   . MET A 1 263  ? 26.692 47.717  7.438   1.00 13.64 ? 263  MET A O   1 
ATOM   1996 C  CB  . MET A 1 263  ? 27.187 48.384  4.526   1.00 13.36 ? 263  MET A CB  1 
ATOM   1997 C  CG  . MET A 1 263  ? 26.369 49.684  4.422   1.00 12.43 ? 263  MET A CG  1 
ATOM   1998 S  SD  . MET A 1 263  ? 25.025 49.508  3.176   1.00 13.39 ? 263  MET A SD  1 
ATOM   1999 C  CE  . MET A 1 263  ? 25.907 49.084  1.679   1.00 14.29 ? 263  MET A CE  1 
ATOM   2000 N  N   . MET A 1 264  ? 27.694 49.748  7.646   1.00 12.26 ? 264  MET A N   1 
ATOM   2001 C  CA  . MET A 1 264  ? 26.986 50.069  8.890   1.00 13.02 ? 264  MET A CA  1 
ATOM   2002 C  C   . MET A 1 264  ? 25.518 50.286  8.483   1.00 12.67 ? 264  MET A C   1 
ATOM   2003 O  O   . MET A 1 264  ? 25.221 50.753  7.376   1.00 11.98 ? 264  MET A O   1 
ATOM   2004 C  CB  A MET A 1 264  ? 27.595 51.305  9.528   0.50 11.76 ? 264  MET A CB  1 
ATOM   2005 C  CB  B MET A 1 264  ? 27.647 51.145  9.652   0.50 12.74 ? 264  MET A CB  1 
ATOM   2006 C  CG  A MET A 1 264  ? 29.016 51.052  9.953   0.50 10.91 ? 264  MET A CG  1 
ATOM   2007 C  CG  B MET A 1 264  ? 29.024 50.672  10.079  0.50 16.52 ? 264  MET A CG  1 
ATOM   2008 S  SD  A MET A 1 264  ? 30.022 52.524  10.435  0.50 15.66 ? 264  MET A SD  1 
ATOM   2009 S  SD  B MET A 1 264  ? 29.688 51.501  11.537  0.50 17.60 ? 264  MET A SD  1 
ATOM   2010 C  CE  A MET A 1 264  ? 28.960 53.414  11.493  0.50 13.65 ? 264  MET A CE  1 
ATOM   2011 C  CE  B MET A 1 264  ? 30.165 52.910  10.593  0.50 20.08 ? 264  MET A CE  1 
ATOM   2012 N  N   . PRO A 1 265  ? 24.570 49.949  9.375   1.00 14.51 ? 265  PRO A N   1 
ATOM   2013 C  CA  . PRO A 1 265  ? 23.154 50.075  9.084   1.00 14.42 ? 265  PRO A CA  1 
ATOM   2014 C  C   . PRO A 1 265  ? 22.342 51.291  9.288   1.00 14.33 ? 265  PRO A C   1 
ATOM   2015 O  O   . PRO A 1 265  ? 21.265 51.407  8.708   1.00 14.83 ? 265  PRO A O   1 
ATOM   2016 C  CB  . PRO A 1 265  ? 22.562 48.927  9.922   1.00 14.93 ? 265  PRO A CB  1 
ATOM   2017 C  CG  . PRO A 1 265  ? 23.383 49.005  11.167  1.00 14.79 ? 265  PRO A CG  1 
ATOM   2018 C  CD  . PRO A 1 265  ? 24.787 49.485  10.763  1.00 13.17 ? 265  PRO A CD  1 
ATOM   2019 N  N   . PHE A 1 266  ? 22.885 52.205  10.068  1.00 14.30 ? 266  PHE A N   1 
ATOM   2020 C  CA  . PHE A 1 266  ? 22.128 53.350  10.498  1.00 14.38 ? 266  PHE A CA  1 
ATOM   2021 C  C   . PHE A 1 266  ? 22.480 54.682  9.908   1.00 14.14 ? 266  PHE A C   1 
ATOM   2022 O  O   . PHE A 1 266  ? 23.355 54.780  9.080   1.00 14.69 ? 266  PHE A O   1 
ATOM   2023 C  CB  . PHE A 1 266  ? 22.103 53.349  12.044  1.00 14.54 ? 266  PHE A CB  1 
ATOM   2024 C  CG  . PHE A 1 266  ? 21.543 52.040  12.643  1.00 15.34 ? 266  PHE A CG  1 
ATOM   2025 C  CD1 . PHE A 1 266  ? 20.408 51.432  12.121  1.00 15.36 ? 266  PHE A CD1 1 
ATOM   2026 C  CD2 . PHE A 1 266  ? 22.173 51.446  13.722  1.00 14.12 ? 266  PHE A CD2 1 
ATOM   2027 C  CE1 . PHE A 1 266  ? 19.912 50.230  12.680  1.00 15.33 ? 266  PHE A CE1 1 
ATOM   2028 C  CE2 . PHE A 1 266  ? 21.691 50.252  14.295  1.00 15.24 ? 266  PHE A CE2 1 
ATOM   2029 C  CZ  . PHE A 1 266  ? 20.548 49.651  13.748  1.00 14.55 ? 266  PHE A CZ  1 
ATOM   2030 N  N   . TYR A 1 267  ? 21.802 55.706  10.345  1.00 14.64 ? 267  TYR A N   1 
ATOM   2031 C  CA  . TYR A 1 267  ? 21.917 57.023  9.744   1.00 13.98 ? 267  TYR A CA  1 
ATOM   2032 C  C   . TYR A 1 267  ? 23.247 57.754  9.935   1.00 13.28 ? 267  TYR A C   1 
ATOM   2033 O  O   . TYR A 1 267  ? 23.626 58.576  9.095   1.00 14.41 ? 267  TYR A O   1 
ATOM   2034 C  CB  . TYR A 1 267  ? 20.722 57.839  10.280  1.00 15.86 ? 267  TYR A CB  1 
ATOM   2035 C  CG  . TYR A 1 267  ? 20.812 59.327  10.137  1.00 16.03 ? 267  TYR A CG  1 
ATOM   2036 C  CD1 . TYR A 1 267  ? 20.438 59.962  8.959   1.00 16.63 ? 267  TYR A CD1 1 
ATOM   2037 C  CD2 . TYR A 1 267  ? 21.231 60.110  11.216  1.00 18.63 ? 267  TYR A CD2 1 
ATOM   2038 C  CE1 . TYR A 1 267  ? 20.471 61.361  8.857   1.00 18.22 ? 267  TYR A CE1 1 
ATOM   2039 C  CE2 . TYR A 1 267  ? 21.267 61.505  11.120  1.00 19.34 ? 267  TYR A CE2 1 
ATOM   2040 C  CZ  . TYR A 1 267  ? 20.881 62.109  9.950   1.00 19.08 ? 267  TYR A CZ  1 
ATOM   2041 O  OH  . TYR A 1 267  ? 20.864 63.495  9.878   1.00 25.04 ? 267  TYR A OH  1 
ATOM   2042 N  N   . SER A 1 268  ? 23.943 57.482  11.020  1.00 14.45 ? 268  SER A N   1 
ATOM   2043 C  CA  . SER A 1 268  ? 25.193 58.164  11.319  1.00 13.15 ? 268  SER A CA  1 
ATOM   2044 C  C   . SER A 1 268  ? 26.187 57.237  11.989  1.00 14.90 ? 268  SER A C   1 
ATOM   2045 O  O   . SER A 1 268  ? 25.828 56.136  12.406  1.00 13.77 ? 268  SER A O   1 
ATOM   2046 C  CB  . SER A 1 268  ? 24.876 59.358  12.233  1.00 16.46 ? 268  SER A CB  1 
ATOM   2047 O  OG  . SER A 1 268  ? 26.042 60.028  12.659  1.00 16.94 ? 268  SER A OG  1 
ATOM   2048 N  N   . TYR A 1 269  ? 27.458 57.650  12.034  1.00 14.22 ? 269  TYR A N   1 
ATOM   2049 C  CA  . TYR A 1 269  ? 28.467 56.900  12.779  1.00 13.11 ? 269  TYR A CA  1 
ATOM   2050 C  C   . TYR A 1 269  ? 28.572 57.397  14.253  1.00 13.26 ? 269  TYR A C   1 
ATOM   2051 O  O   . TYR A 1 269  ? 29.428 56.907  14.998  1.00 13.57 ? 269  TYR A O   1 
ATOM   2052 C  CB  . TYR A 1 269  ? 29.846 57.078  12.083  1.00 12.88 ? 269  TYR A CB  1 
ATOM   2053 C  CG  . TYR A 1 269  ? 30.253 58.518  11.841  1.00 12.84 ? 269  TYR A CG  1 
ATOM   2054 C  CD1 . TYR A 1 269  ? 30.681 59.336  12.913  1.00 14.18 ? 269  TYR A CD1 1 
ATOM   2055 C  CD2 . TYR A 1 269  ? 30.181 59.073  10.554  1.00 14.34 ? 269  TYR A CD2 1 
ATOM   2056 C  CE1 . TYR A 1 269  ? 31.027 60.705  12.696  1.00 16.21 ? 269  TYR A CE1 1 
ATOM   2057 C  CE2 . TYR A 1 269  ? 30.528 60.414  10.339  1.00 13.50 ? 269  TYR A CE2 1 
ATOM   2058 C  CZ  . TYR A 1 269  ? 30.937 61.204  11.410  1.00 16.37 ? 269  TYR A CZ  1 
ATOM   2059 O  OH  . TYR A 1 269  ? 31.228 62.517  11.169  1.00 16.45 ? 269  TYR A OH  1 
ATOM   2060 N  N   . ASP A 1 270  ? 27.730 58.354  14.653  1.00 13.50 ? 270  ASP A N   1 
ATOM   2061 C  CA  . ASP A 1 270  ? 27.778 58.875  16.024  1.00 12.84 ? 270  ASP A CA  1 
ATOM   2062 C  C   . ASP A 1 270  ? 27.206 57.848  16.992  1.00 14.80 ? 270  ASP A C   1 
ATOM   2063 O  O   . ASP A 1 270  ? 26.636 56.823  16.584  1.00 14.82 ? 270  ASP A O   1 
ATOM   2064 C  CB  . ASP A 1 270  ? 27.100 60.254  16.126  1.00 15.24 ? 270  ASP A CB  1 
ATOM   2065 C  CG  . ASP A 1 270  ? 25.601 60.241  15.909  1.00 17.63 ? 270  ASP A CG  1 
ATOM   2066 O  OD1 . ASP A 1 270  ? 24.977 59.162  15.823  1.00 16.26 ? 270  ASP A OD1 1 
ATOM   2067 O  OD2 . ASP A 1 270  ? 25.034 61.367  15.854  1.00 20.12 ? 270  ASP A OD2 1 
ATOM   2068 N  N   . ILE A 1 271  ? 27.427 58.085  18.281  1.00 14.33 ? 271  ILE A N   1 
ATOM   2069 C  CA  . ILE A 1 271  ? 26.985 57.084  19.267  1.00 14.28 ? 271  ILE A CA  1 
ATOM   2070 C  C   . ILE A 1 271  ? 25.485 56.812  19.229  1.00 14.22 ? 271  ILE A C   1 
ATOM   2071 O  O   . ILE A 1 271  ? 25.095 55.655  19.229  1.00 14.44 ? 271  ILE A O   1 
ATOM   2072 C  CB  . ILE A 1 271  ? 27.516 57.444  20.664  1.00 16.48 ? 271  ILE A CB  1 
ATOM   2073 C  CG1 . ILE A 1 271  ? 29.029 57.291  20.613  1.00 14.66 ? 271  ILE A CG1 1 
ATOM   2074 C  CG2 . ILE A 1 271  ? 26.987 56.443  21.728  1.00 13.57 ? 271  ILE A CG2 1 
ATOM   2075 C  CD1 . ILE A 1 271  ? 29.810 57.979  21.755  1.00 15.41 ? 271  ILE A CD1 1 
ATOM   2076 N  N   . PRO A 1 272  ? 24.633 57.846  19.099  1.00 13.85 ? 272  PRO A N   1 
ATOM   2077 C  CA  . PRO A 1 272  ? 23.182 57.562  19.045  1.00 15.66 ? 272  PRO A CA  1 
ATOM   2078 C  C   . PRO A 1 272  ? 22.791 56.629  17.898  1.00 15.85 ? 272  PRO A C   1 
ATOM   2079 O  O   . PRO A 1 272  ? 21.760 55.933  17.982  1.00 16.57 ? 272  PRO A O   1 
ATOM   2080 C  CB  . PRO A 1 272  ? 22.530 58.936  18.852  1.00 14.76 ? 272  PRO A CB  1 
ATOM   2081 C  CG  . PRO A 1 272  ? 23.529 59.909  19.498  1.00 16.54 ? 272  PRO A CG  1 
ATOM   2082 C  CD  . PRO A 1 272  ? 24.914 59.298  19.204  1.00 15.00 ? 272  PRO A CD  1 
ATOM   2083 N  N   . HIS A 1 273  ? 23.610 56.577  16.823  1.00 13.69 ? 273  HIS A N   1 
ATOM   2084 C  CA  . HIS A 1 273  ? 23.242 55.714  15.679  1.00 13.55 ? 273  HIS A CA  1 
ATOM   2085 C  C   . HIS A 1 273  ? 24.178 54.538  15.491  1.00 15.17 ? 273  HIS A C   1 
ATOM   2086 O  O   . HIS A 1 273  ? 24.244 53.944  14.406  1.00 15.84 ? 273  HIS A O   1 
ATOM   2087 C  CB  . HIS A 1 273  ? 23.115 56.565  14.385  1.00 12.88 ? 273  HIS A CB  1 
ATOM   2088 C  CG  . HIS A 1 273  ? 22.115 57.681  14.518  1.00 14.77 ? 273  HIS A CG  1 
ATOM   2089 N  ND1 . HIS A 1 273  ? 20.780 57.585  14.176  1.00 18.45 ? 273  HIS A ND1 1 
ATOM   2090 C  CD2 . HIS A 1 273  ? 22.281 58.922  15.026  1.00 12.38 ? 273  HIS A CD2 1 
ATOM   2091 C  CE1 . HIS A 1 273  ? 20.171 58.720  14.475  1.00 12.65 ? 273  HIS A CE1 1 
ATOM   2092 N  NE2 . HIS A 1 273  ? 21.057 59.548  14.997  1.00 17.57 ? 273  HIS A NE2 1 
ATOM   2093 N  N   . THR A 1 274  ? 24.866 54.135  16.555  1.00 13.83 ? 274  THR A N   1 
ATOM   2094 C  CA  . THR A 1 274  ? 25.746 52.987  16.416  1.00 12.84 ? 274  THR A CA  1 
ATOM   2095 C  C   . THR A 1 274  ? 25.526 51.912  17.476  1.00 14.21 ? 274  THR A C   1 
ATOM   2096 O  O   . THR A 1 274  ? 26.041 50.822  17.346  1.00 15.97 ? 274  THR A O   1 
ATOM   2097 C  CB  . THR A 1 274  ? 27.238 53.392  16.401  1.00 15.09 ? 274  THR A CB  1 
ATOM   2098 O  OG1 . THR A 1 274  ? 27.494 54.317  17.464  1.00 15.23 ? 274  THR A OG1 1 
ATOM   2099 C  CG2 . THR A 1 274  ? 27.602 54.031  15.084  1.00 14.68 ? 274  THR A CG2 1 
ATOM   2100 N  N   . CYS A 1 275  ? 24.746 52.184  18.530  1.00 14.65 ? 275  CYS A N   1 
ATOM   2101 C  CA  . CYS A 1 275  ? 24.562 51.097  19.496  1.00 16.52 ? 275  CYS A CA  1 
ATOM   2102 C  C   . CYS A 1 275  ? 23.407 50.155  19.136  1.00 16.66 ? 275  CYS A C   1 
ATOM   2103 O  O   . CYS A 1 275  ? 23.355 49.005  19.590  1.00 16.79 ? 275  CYS A O   1 
ATOM   2104 C  CB  . CYS A 1 275  ? 24.289 51.682  20.894  1.00 17.59 ? 275  CYS A CB  1 
ATOM   2105 S  SG  . CYS A 1 275  ? 22.561 51.780  21.507  1.00 18.94 ? 275  CYS A SG  1 
ATOM   2106 N  N   . GLY A 1 276  ? 22.498 50.636  18.309  1.00 16.18 ? 276  GLY A N   1 
ATOM   2107 C  CA  . GLY A 1 276  ? 21.295 49.879  17.997  1.00 16.24 ? 276  GLY A CA  1 
ATOM   2108 C  C   . GLY A 1 276  ? 20.357 50.776  17.232  1.00 15.86 ? 276  GLY A C   1 
ATOM   2109 O  O   . GLY A 1 276  ? 20.701 51.932  16.972  1.00 15.99 ? 276  GLY A O   1 
ATOM   2110 N  N   . PRO A 1 277  ? 19.136 50.323  16.912  1.00 16.09 ? 277  PRO A N   1 
ATOM   2111 C  CA  . PRO A 1 277  ? 18.172 51.096  16.140  1.00 16.44 ? 277  PRO A CA  1 
ATOM   2112 C  C   . PRO A 1 277  ? 17.477 52.303  16.736  1.00 15.39 ? 277  PRO A C   1 
ATOM   2113 O  O   . PRO A 1 277  ? 16.883 53.091  15.998  1.00 17.01 ? 277  PRO A O   1 
ATOM   2114 C  CB  . PRO A 1 277  ? 17.138 50.047  15.723  1.00 17.38 ? 277  PRO A CB  1 
ATOM   2115 C  CG  . PRO A 1 277  ? 17.129 49.113  16.940  1.00 15.22 ? 277  PRO A CG  1 
ATOM   2116 C  CD  . PRO A 1 277  ? 18.598 48.983  17.262  1.00 17.37 ? 277  PRO A CD  1 
ATOM   2117 N  N   . ASP A 1 278  ? 17.553 52.445  18.053  1.00 17.27 ? 278  ASP A N   1 
ATOM   2118 C  CA  . ASP A 1 278  ? 16.820 53.550  18.701  1.00 17.29 ? 278  ASP A CA  1 
ATOM   2119 C  C   . ASP A 1 278  ? 17.754 54.583  19.253  1.00 16.12 ? 278  ASP A C   1 
ATOM   2120 O  O   . ASP A 1 278  ? 18.325 54.406  20.314  1.00 18.06 ? 278  ASP A O   1 
ATOM   2121 C  CB  . ASP A 1 278  ? 15.932 52.993  19.833  1.00 17.95 ? 278  ASP A CB  1 
ATOM   2122 C  CG  . ASP A 1 278  ? 15.043 54.060  20.438  1.00 20.99 ? 278  ASP A CG  1 
ATOM   2123 O  OD1 . ASP A 1 278  ? 15.168 55.250  20.092  1.00 21.34 ? 278  ASP A OD1 1 
ATOM   2124 O  OD2 . ASP A 1 278  ? 14.193 53.707  21.275  1.00 21.87 ? 278  ASP A OD2 1 
ATOM   2125 N  N   . PRO A 1 279  ? 17.893 55.701  18.535  1.00 17.93 ? 279  PRO A N   1 
ATOM   2126 C  CA  . PRO A 1 279  ? 18.805 56.757  19.000  1.00 17.93 ? 279  PRO A CA  1 
ATOM   2127 C  C   . PRO A 1 279  ? 18.475 57.369  20.334  1.00 16.50 ? 279  PRO A C   1 
ATOM   2128 O  O   . PRO A 1 279  ? 19.385 57.803  21.035  1.00 18.35 ? 279  PRO A O   1 
ATOM   2129 C  CB  . PRO A 1 279  ? 18.795 57.778  17.859  1.00 19.31 ? 279  PRO A CB  1 
ATOM   2130 C  CG  . PRO A 1 279  ? 17.426 57.640  17.290  1.00 18.71 ? 279  PRO A CG  1 
ATOM   2131 C  CD  . PRO A 1 279  ? 17.086 56.134  17.380  1.00 16.90 ? 279  PRO A CD  1 
ATOM   2132 N  N   . LYS A 1 280  ? 17.191 57.351  20.721  1.00 17.86 ? 280  LYS A N   1 
ATOM   2133 C  CA  . LYS A 1 280  ? 16.818 57.917  22.021  1.00 19.32 ? 280  LYS A CA  1 
ATOM   2134 C  C   . LYS A 1 280  ? 17.427 57.081  23.134  1.00 18.30 ? 280  LYS A C   1 
ATOM   2135 O  O   . LYS A 1 280  ? 17.825 57.604  24.183  1.00 20.61 ? 280  LYS A O   1 
ATOM   2136 C  CB  . LYS A 1 280  ? 15.306 57.978  22.135  1.00 21.53 ? 280  LYS A CB  1 
ATOM   2137 C  CG  . LYS A 1 280  ? 14.795 58.271  23.539  1.00 24.10 ? 280  LYS A CG  1 
ATOM   2138 C  CD  . LYS A 1 280  ? 13.345 58.754  23.413  1.00 29.82 ? 280  LYS A CD  1 
ATOM   2139 C  CE  . LYS A 1 280  ? 12.465 58.243  24.523  1.00 36.34 ? 280  LYS A CE  1 
ATOM   2140 N  NZ  . LYS A 1 280  ? 13.292 57.755  25.664  1.00 40.36 ? 280  LYS A NZ  1 
ATOM   2141 N  N   . VAL A 1 281  ? 17.569 55.774  22.902  1.00 17.97 ? 281  VAL A N   1 
ATOM   2142 C  CA  . VAL A 1 281  ? 18.212 54.909  23.880  1.00 17.02 ? 281  VAL A CA  1 
ATOM   2143 C  C   . VAL A 1 281  ? 19.745 54.971  23.765  1.00 17.36 ? 281  VAL A C   1 
ATOM   2144 O  O   . VAL A 1 281  ? 20.477 55.124  24.756  1.00 17.72 ? 281  VAL A O   1 
ATOM   2145 C  CB  . VAL A 1 281  ? 17.772 53.434  23.708  1.00 17.95 ? 281  VAL A CB  1 
ATOM   2146 C  CG1 . VAL A 1 281  ? 18.605 52.512  24.652  1.00 17.32 ? 281  VAL A CG1 1 
ATOM   2147 C  CG2 . VAL A 1 281  ? 16.246 53.338  23.959  1.00 18.19 ? 281  VAL A CG2 1 
ATOM   2148 N  N   . CYS A 1 282  ? 20.249 54.887  22.529  1.00 17.77 ? 282  CYS A N   1 
ATOM   2149 C  CA  . CYS A 1 282  ? 21.697 54.882  22.373  1.00 17.52 ? 282  CYS A CA  1 
ATOM   2150 C  C   . CYS A 1 282  ? 22.388 56.165  22.859  1.00 15.26 ? 282  CYS A C   1 
ATOM   2151 O  O   . CYS A 1 282  ? 23.524 56.112  23.363  1.00 16.78 ? 282  CYS A O   1 
ATOM   2152 C  CB  . CYS A 1 282  ? 22.088 54.683  20.897  1.00 16.62 ? 282  CYS A CB  1 
ATOM   2153 S  SG  . CYS A 1 282  ? 21.659 53.068  20.214  1.00 18.37 ? 282  CYS A SG  1 
ATOM   2154 N  N   . CYS A 1 283  ? 21.684 57.285  22.700  1.00 17.41 ? 283  CYS A N   1 
ATOM   2155 C  CA  . CYS A 1 283  ? 22.239 58.549  23.114  1.00 16.49 ? 283  CYS A CA  1 
ATOM   2156 C  C   . CYS A 1 283  ? 22.541 58.516  24.604  1.00 15.81 ? 283  CYS A C   1 
ATOM   2157 O  O   . CYS A 1 283  ? 23.437 59.189  25.061  1.00 15.43 ? 283  CYS A O   1 
ATOM   2158 C  CB  . CYS A 1 283  ? 21.261 59.666  22.770  1.00 17.04 ? 283  CYS A CB  1 
ATOM   2159 S  SG  . CYS A 1 283  ? 22.087 61.297  22.880  1.00 20.34 ? 283  CYS A SG  1 
ATOM   2160 N  N   . GLN A 1 284  ? 21.782 57.702  25.366  1.00 16.55 ? 284  GLN A N   1 
ATOM   2161 C  CA  . GLN A 1 284  ? 22.027 57.602  26.803  1.00 17.07 ? 284  GLN A CA  1 
ATOM   2162 C  C   . GLN A 1 284  ? 23.298 56.843  27.177  1.00 15.39 ? 284  GLN A C   1 
ATOM   2163 O  O   . GLN A 1 284  ? 23.653 56.735  28.337  1.00 18.32 ? 284  GLN A O   1 
ATOM   2164 C  CB  . GLN A 1 284  ? 20.823 56.930  27.497  1.00 18.26 ? 284  GLN A CB  1 
ATOM   2165 C  CG  . GLN A 1 284  ? 19.519 57.648  27.285  1.00 18.34 ? 284  GLN A CG  1 
ATOM   2166 C  CD  . GLN A 1 284  ? 18.360 56.860  27.842  1.00 20.11 ? 284  GLN A CD  1 
ATOM   2167 O  OE1 . GLN A 1 284  ? 18.391 56.465  29.006  1.00 22.19 ? 284  GLN A OE1 1 
ATOM   2168 N  NE2 . GLN A 1 284  ? 17.344 56.630  27.028  1.00 20.51 ? 284  GLN A NE2 1 
ATOM   2169 N  N   . PHE A 1 285  ? 24.007 56.336  26.154  1.00 15.89 ? 285  PHE A N   1 
ATOM   2170 C  CA  . PHE A 1 285  ? 25.237 55.616  26.348  1.00 15.17 ? 285  PHE A CA  1 
ATOM   2171 C  C   . PHE A 1 285  ? 26.413 56.366  25.719  1.00 14.47 ? 285  PHE A C   1 
ATOM   2172 O  O   . PHE A 1 285  ? 27.481 55.798  25.467  1.00 16.53 ? 285  PHE A O   1 
ATOM   2173 C  CB  . PHE A 1 285  ? 25.096 54.155  25.893  1.00 16.67 ? 285  PHE A CB  1 
ATOM   2174 C  CG  . PHE A 1 285  ? 24.096 53.391  26.746  1.00 16.67 ? 285  PHE A CG  1 
ATOM   2175 C  CD1 . PHE A 1 285  ? 24.478 52.785  27.943  1.00 18.54 ? 285  PHE A CD1 1 
ATOM   2176 C  CD2 . PHE A 1 285  ? 22.760 53.397  26.386  1.00 16.49 ? 285  PHE A CD2 1 
ATOM   2177 C  CE1 . PHE A 1 285  ? 23.508 52.195  28.786  1.00 19.27 ? 285  PHE A CE1 1 
ATOM   2178 C  CE2 . PHE A 1 285  ? 21.773 52.804  27.238  1.00 20.36 ? 285  PHE A CE2 1 
ATOM   2179 C  CZ  . PHE A 1 285  ? 22.164 52.217  28.423  1.00 19.00 ? 285  PHE A CZ  1 
ATOM   2180 N  N   . ASP A 1 286  ? 26.162 57.637  25.448  1.00 14.82 ? 286  ASP A N   1 
ATOM   2181 C  CA  . ASP A 1 286  ? 27.234 58.548  25.021  1.00 15.73 ? 286  ASP A CA  1 
ATOM   2182 C  C   . ASP A 1 286  ? 27.477 59.377  26.308  1.00 14.79 ? 286  ASP A C   1 
ATOM   2183 O  O   . ASP A 1 286  ? 26.800 60.390  26.541  1.00 15.79 ? 286  ASP A O   1 
ATOM   2184 C  CB  . ASP A 1 286  ? 26.797 59.438  23.880  1.00 15.61 ? 286  ASP A CB  1 
ATOM   2185 C  CG  . ASP A 1 286  ? 27.941 60.337  23.382  1.00 14.15 ? 286  ASP A CG  1 
ATOM   2186 O  OD1 . ASP A 1 286  ? 28.978 60.402  24.090  1.00 14.54 ? 286  ASP A OD1 1 
ATOM   2187 O  OD2 . ASP A 1 286  ? 27.749 60.977  22.329  1.00 15.33 ? 286  ASP A OD2 1 
ATOM   2188 N  N   . PHE A 1 287  ? 28.453 58.967  27.104  1.00 14.14 ? 287  PHE A N   1 
ATOM   2189 C  CA  . PHE A 1 287  ? 28.614 59.616  28.396  1.00 15.16 ? 287  PHE A CA  1 
ATOM   2190 C  C   . PHE A 1 287  ? 29.183 61.008  28.365  1.00 17.37 ? 287  PHE A C   1 
ATOM   2191 O  O   . PHE A 1 287  ? 29.315 61.653  29.411  1.00 18.35 ? 287  PHE A O   1 
ATOM   2192 C  CB  . PHE A 1 287  ? 29.342 58.673  29.362  1.00 16.47 ? 287  PHE A CB  1 
ATOM   2193 C  CG  . PHE A 1 287  ? 28.551 57.384  29.625  1.00 15.94 ? 287  PHE A CG  1 
ATOM   2194 C  CD1 . PHE A 1 287  ? 27.548 57.362  30.614  1.00 17.13 ? 287  PHE A CD1 1 
ATOM   2195 C  CD2 . PHE A 1 287  ? 28.770 56.223  28.894  1.00 16.67 ? 287  PHE A CD2 1 
ATOM   2196 C  CE1 . PHE A 1 287  ? 26.793 56.211  30.854  1.00 17.98 ? 287  PHE A CE1 1 
ATOM   2197 C  CE2 . PHE A 1 287  ? 28.014 55.060  29.134  1.00 19.32 ? 287  PHE A CE2 1 
ATOM   2198 C  CZ  . PHE A 1 287  ? 27.014 55.059  30.129  1.00 16.93 ? 287  PHE A CZ  1 
ATOM   2199 N  N   . LYS A 1 288  ? 29.502 61.513  27.171  1.00 16.86 ? 288  LYS A N   1 
ATOM   2200 C  CA  . LYS A 1 288  ? 29.958 62.898  27.096  1.00 17.39 ? 288  LYS A CA  1 
ATOM   2201 C  C   . LYS A 1 288  ? 28.740 63.835  27.018  1.00 18.43 ? 288  LYS A C   1 
ATOM   2202 O  O   . LYS A 1 288  ? 28.904 65.050  26.937  1.00 19.39 ? 288  LYS A O   1 
ATOM   2203 C  CB  . LYS A 1 288  ? 30.822 63.102  25.819  1.00 17.62 ? 288  LYS A CB  1 
ATOM   2204 C  CG  . LYS A 1 288  ? 31.709 64.379  25.850  1.00 14.27 ? 288  LYS A CG  1 
ATOM   2205 C  CD  . LYS A 1 288  ? 32.523 64.527  24.544  1.00 14.05 ? 288  LYS A CD  1 
ATOM   2206 C  CE  . LYS A 1 288  ? 33.366 65.765  24.731  1.00 15.62 ? 288  LYS A CE  1 
ATOM   2207 N  NZ  . LYS A 1 288  ? 34.279 65.958  23.497  1.00 19.06 ? 288  LYS A NZ  1 
ATOM   2208 N  N   . ARG A 1 289  ? 27.511 63.301  27.018  1.00 17.79 ? 289  ARG A N   1 
ATOM   2209 C  CA  . ARG A 1 289  ? 26.324 64.142  26.885  1.00 20.59 ? 289  ARG A CA  1 
ATOM   2210 C  C   . ARG A 1 289  ? 25.514 64.444  28.172  1.00 21.09 ? 289  ARG A C   1 
ATOM   2211 O  O   . ARG A 1 289  ? 24.319 64.699  28.075  1.00 22.32 ? 289  ARG A O   1 
ATOM   2212 C  CB  . ARG A 1 289  ? 25.370 63.522  25.848  1.00 18.62 ? 289  ARG A CB  1 
ATOM   2213 C  CG  . ARG A 1 289  ? 26.005 63.356  24.471  1.00 16.77 ? 289  ARG A CG  1 
ATOM   2214 C  CD  . ARG A 1 289  ? 24.996 62.908  23.494  1.00 16.20 ? 289  ARG A CD  1 
ATOM   2215 N  NE  . ARG A 1 289  ? 25.558 62.601  22.167  1.00 16.51 ? 289  ARG A NE  1 
ATOM   2216 C  CZ  . ARG A 1 289  ? 25.111 63.131  21.041  1.00 17.77 ? 289  ARG A CZ  1 
ATOM   2217 N  NH1 . ARG A 1 289  ? 24.118 64.018  21.005  1.00 19.18 ? 289  ARG A NH1 1 
ATOM   2218 N  NH2 . ARG A 1 289  ? 25.660 62.727  19.893  1.00 16.64 ? 289  ARG A NH2 1 
ATOM   2219 N  N   . MET A 1 290  ? 26.147 64.452  29.343  1.00 25.55 ? 290  MET A N   1 
ATOM   2220 C  CA  . MET A 1 290  ? 25.375 64.717  30.560  1.00 27.57 ? 290  MET A CA  1 
ATOM   2221 C  C   . MET A 1 290  ? 25.339 66.212  30.968  1.00 30.34 ? 290  MET A C   1 
ATOM   2222 O  O   . MET A 1 290  ? 24.592 66.594  31.917  1.00 32.00 ? 290  MET A O   1 
ATOM   2223 C  CB  . MET A 1 290  ? 25.863 63.809  31.718  1.00 25.50 ? 290  MET A CB  1 
ATOM   2224 C  CG  . MET A 1 290  ? 25.875 62.330  31.364  1.00 25.89 ? 290  MET A CG  1 
ATOM   2225 S  SD  . MET A 1 290  ? 26.258 61.209  32.772  1.00 27.84 ? 290  MET A SD  1 
ATOM   2226 C  CE  . MET A 1 290  ? 28.040 61.070  32.683  1.00 29.89 ? 290  MET A CE  1 
ATOM   2227 N  N   . GLY A 1 291  ? 26.108 67.059  30.265  1.00 29.02 ? 291  GLY A N   1 
ATOM   2228 C  CA  . GLY A 1 291  ? 26.077 68.488  30.556  1.00 28.10 ? 291  GLY A CA  1 
ATOM   2229 C  C   . GLY A 1 291  ? 27.348 69.339  30.645  1.00 28.01 ? 291  GLY A C   1 
ATOM   2230 O  O   . GLY A 1 291  ? 27.438 70.414  30.021  1.00 26.93 ? 291  GLY A O   1 
ATOM   2231 N  N   . SER A 1 292  ? 28.331 68.871  31.414  1.00 25.86 ? 292  SER A N   1 
ATOM   2232 C  CA  . SER A 1 292  ? 29.559 69.626  31.622  1.00 22.10 ? 292  SER A CA  1 
ATOM   2233 C  C   . SER A 1 292  ? 30.416 69.818  30.358  1.00 21.09 ? 292  SER A C   1 
ATOM   2234 O  O   . SER A 1 292  ? 31.315 70.675  30.328  1.00 19.77 ? 292  SER A O   1 
ATOM   2235 C  CB  . SER A 1 292  ? 30.382 68.942  32.703  1.00 23.29 ? 292  SER A CB  1 
ATOM   2236 O  OG  . SER A 1 292  ? 30.815 67.671  32.236  1.00 24.32 ? 292  SER A OG  1 
ATOM   2237 N  N   . PHE A 1 293  ? 30.132 69.024  29.325  1.00 19.17 ? 293  PHE A N   1 
ATOM   2238 C  CA  . PHE A 1 293  ? 30.871 69.122  28.058  1.00 16.97 ? 293  PHE A CA  1 
ATOM   2239 C  C   . PHE A 1 293  ? 30.099 69.938  27.043  1.00 18.20 ? 293  PHE A C   1 
ATOM   2240 O  O   . PHE A 1 293  ? 30.536 70.036  25.896  1.00 19.25 ? 293  PHE A O   1 
ATOM   2241 C  CB  . PHE A 1 293  ? 31.125 67.710  27.456  1.00 17.49 ? 293  PHE A CB  1 
ATOM   2242 C  CG  . PHE A 1 293  ? 32.050 66.867  28.262  1.00 16.77 ? 293  PHE A CG  1 
ATOM   2243 C  CD1 . PHE A 1 293  ? 33.405 67.012  28.137  1.00 17.97 ? 293  PHE A CD1 1 
ATOM   2244 C  CD2 . PHE A 1 293  ? 31.537 65.943  29.151  1.00 18.09 ? 293  PHE A CD2 1 
ATOM   2245 C  CE1 . PHE A 1 293  ? 34.289 66.224  28.894  1.00 19.75 ? 293  PHE A CE1 1 
ATOM   2246 C  CE2 . PHE A 1 293  ? 32.416 65.136  29.929  1.00 18.94 ? 293  PHE A CE2 1 
ATOM   2247 C  CZ  . PHE A 1 293  ? 33.778 65.292  29.781  1.00 19.54 ? 293  PHE A CZ  1 
ATOM   2248 N  N   . GLY A 1 294  ? 28.959 70.493  27.469  1.00 18.33 ? 294  GLY A N   1 
ATOM   2249 C  CA  . GLY A 1 294  ? 28.156 71.288  26.565  1.00 19.81 ? 294  GLY A CA  1 
ATOM   2250 C  C   . GLY A 1 294  ? 27.451 70.487  25.490  1.00 19.22 ? 294  GLY A C   1 
ATOM   2251 O  O   . GLY A 1 294  ? 27.120 71.019  24.424  1.00 22.16 ? 294  GLY A O   1 
ATOM   2252 N  N   . LEU A 1 295  ? 27.244 69.202  25.756  1.00 19.34 ? 295  LEU A N   1 
ATOM   2253 C  CA  . LEU A 1 295  ? 26.524 68.356  24.827  1.00 18.01 ? 295  LEU A CA  1 
ATOM   2254 C  C   . LEU A 1 295  ? 25.299 67.835  25.548  1.00 19.10 ? 295  LEU A C   1 
ATOM   2255 O  O   . LEU A 1 295  ? 25.283 67.756  26.762  1.00 20.00 ? 295  LEU A O   1 
ATOM   2256 C  CB  . LEU A 1 295  ? 27.391 67.179  24.361  1.00 19.74 ? 295  LEU A CB  1 
ATOM   2257 C  CG  . LEU A 1 295  ? 28.670 67.597  23.590  1.00 21.23 ? 295  LEU A CG  1 
ATOM   2258 C  CD1 . LEU A 1 295  ? 29.525 66.374  23.289  1.00 22.94 ? 295  LEU A CD1 1 
ATOM   2259 C  CD2 . LEU A 1 295  ? 28.305 68.327  22.275  1.00 22.98 ? 295  LEU A CD2 1 
ATOM   2260 N  N   . SER A 1 296  ? 24.294 67.474  24.765  1.00 19.76 ? 296  SER A N   1 
ATOM   2261 C  CA  . SER A 1 296  ? 23.042 66.916  25.310  1.00 21.94 ? 296  SER A CA  1 
ATOM   2262 C  C   . SER A 1 296  ? 22.442 65.954  24.303  1.00 22.53 ? 296  SER A C   1 
ATOM   2263 O  O   . SER A 1 296  ? 22.969 65.806  23.196  1.00 21.12 ? 296  SER A O   1 
ATOM   2264 C  CB  . SER A 1 296  ? 22.061 68.070  25.624  1.00 20.40 ? 296  SER A CB  1 
ATOM   2265 O  OG  . SER A 1 296  ? 21.752 68.835  24.477  1.00 24.61 ? 296  SER A OG  1 
ATOM   2266 N  N   . CYS A 1 297  ? 21.355 65.275  24.681  1.00 22.42 ? 297  CYS A N   1 
ATOM   2267 C  CA  . CYS A 1 297  ? 20.666 64.329  23.795  1.00 21.81 ? 297  CYS A CA  1 
ATOM   2268 C  C   . CYS A 1 297  ? 19.432 64.972  23.210  1.00 21.82 ? 297  CYS A C   1 
ATOM   2269 O  O   . CYS A 1 297  ? 18.530 65.340  23.967  1.00 23.94 ? 297  CYS A O   1 
ATOM   2270 C  CB  . CYS A 1 297  ? 20.263 63.068  24.583  1.00 23.65 ? 297  CYS A CB  1 
ATOM   2271 S  SG  . CYS A 1 297  ? 21.674 61.927  24.827  1.00 25.35 ? 297  CYS A SG  1 
ATOM   2272 N  N   . PRO A 1 298  ? 19.341 65.088  21.876  1.00 22.04 ? 298  PRO A N   1 
ATOM   2273 C  CA  . PRO A 1 298  ? 18.150 65.723  21.302  1.00 23.25 ? 298  PRO A CA  1 
ATOM   2274 C  C   . PRO A 1 298  ? 16.854 64.980  21.545  1.00 22.38 ? 298  PRO A C   1 
ATOM   2275 O  O   . PRO A 1 298  ? 15.775 65.590  21.475  1.00 23.48 ? 298  PRO A O   1 
ATOM   2276 C  CB  . PRO A 1 298  ? 18.488 65.883  19.811  1.00 26.66 ? 298  PRO A CB  1 
ATOM   2277 C  CG  . PRO A 1 298  ? 19.604 64.937  19.570  1.00 24.92 ? 298  PRO A CG  1 
ATOM   2278 C  CD  . PRO A 1 298  ? 20.390 64.890  20.846  1.00 21.40 ? 298  PRO A CD  1 
ATOM   2279 N  N   . TRP A 1 299  ? 16.972 63.699  21.890  1.00 20.80 ? 299  TRP A N   1 
ATOM   2280 C  CA  . TRP A 1 299  ? 15.776 62.874  22.148  1.00 21.79 ? 299  TRP A CA  1 
ATOM   2281 C  C   . TRP A 1 299  ? 15.273 63.099  23.565  1.00 24.39 ? 299  TRP A C   1 
ATOM   2282 O  O   . TRP A 1 299  ? 14.339 62.433  24.028  1.00 23.93 ? 299  TRP A O   1 
ATOM   2283 C  CB  . TRP A 1 299  ? 16.074 61.390  21.876  1.00 20.18 ? 299  TRP A CB  1 
ATOM   2284 C  CG  . TRP A 1 299  ? 16.412 61.169  20.428  1.00 19.69 ? 299  TRP A CG  1 
ATOM   2285 C  CD1 . TRP A 1 299  ? 15.548 60.980  19.396  1.00 19.87 ? 299  TRP A CD1 1 
ATOM   2286 C  CD2 . TRP A 1 299  ? 17.726 61.258  19.847  1.00 17.64 ? 299  TRP A CD2 1 
ATOM   2287 N  NE1 . TRP A 1 299  ? 16.242 60.950  18.201  1.00 21.28 ? 299  TRP A NE1 1 
ATOM   2288 C  CE2 . TRP A 1 299  ? 17.576 61.122  18.462  1.00 20.23 ? 299  TRP A CE2 1 
ATOM   2289 C  CE3 . TRP A 1 299  ? 19.004 61.442  20.381  1.00 20.48 ? 299  TRP A CE3 1 
ATOM   2290 C  CZ2 . TRP A 1 299  ? 18.668 61.167  17.583  1.00 19.06 ? 299  TRP A CZ2 1 
ATOM   2291 C  CZ3 . TRP A 1 299  ? 20.087 61.479  19.510  1.00 18.71 ? 299  TRP A CZ3 1 
ATOM   2292 C  CH2 . TRP A 1 299  ? 19.897 61.344  18.125  1.00 19.56 ? 299  TRP A CH2 1 
ATOM   2293 N  N   . LYS A 1 300  ? 15.949 64.005  24.265  1.00 24.27 ? 300  LYS A N   1 
ATOM   2294 C  CA  . LYS A 1 300  ? 15.519 64.449  25.593  1.00 26.58 ? 300  LYS A CA  1 
ATOM   2295 C  C   . LYS A 1 300  ? 15.705 63.567  26.817  1.00 26.81 ? 300  LYS A C   1 
ATOM   2296 O  O   . LYS A 1 300  ? 15.188 63.882  27.893  1.00 28.29 ? 300  LYS A O   1 
ATOM   2297 C  CB  . LYS A 1 300  ? 14.056 64.895  25.505  1.00 27.93 ? 300  LYS A CB  1 
ATOM   2298 C  CG  . LYS A 1 300  ? 13.809 66.067  24.595  1.00 30.93 ? 300  LYS A CG  1 
ATOM   2299 C  CD  . LYS A 1 300  ? 12.313 66.347  24.449  1.00 34.44 ? 300  LYS A CD  1 
ATOM   2300 C  CE  . LYS A 1 300  ? 12.040 67.716  23.833  1.00 37.67 ? 300  LYS A CE  1 
ATOM   2301 N  NZ  . LYS A 1 300  ? 12.768 67.911  22.537  1.00 39.12 ? 300  LYS A NZ  1 
ATOM   2302 N  N   . VAL A 1 301  ? 16.399 62.451  26.677  1.00 24.91 ? 301  VAL A N   1 
ATOM   2303 C  CA  . VAL A 1 301  ? 16.666 61.605  27.817  1.00 23.74 ? 301  VAL A CA  1 
ATOM   2304 C  C   . VAL A 1 301  ? 18.176 61.606  27.891  1.00 23.91 ? 301  VAL A C   1 
ATOM   2305 O  O   . VAL A 1 301  ? 18.848 61.122  26.979  1.00 24.80 ? 301  VAL A O   1 
ATOM   2306 C  CB  . VAL A 1 301  ? 16.158 60.157  27.643  1.00 25.58 ? 301  VAL A CB  1 
ATOM   2307 C  CG1 . VAL A 1 301  ? 16.449 59.377  28.918  1.00 25.03 ? 301  VAL A CG1 1 
ATOM   2308 C  CG2 . VAL A 1 301  ? 14.658 60.142  27.341  1.00 26.91 ? 301  VAL A CG2 1 
ATOM   2309 N  N   . PRO A 1 302  ? 18.744 62.118  28.978  1.00 22.43 ? 302  PRO A N   1 
ATOM   2310 C  CA  . PRO A 1 302  ? 20.188 62.165  29.092  1.00 22.72 ? 302  PRO A CA  1 
ATOM   2311 C  C   . PRO A 1 302  ? 20.849 60.895  29.555  1.00 22.07 ? 302  PRO A C   1 
ATOM   2312 O  O   . PRO A 1 302  ? 20.212 59.970  30.069  1.00 22.97 ? 302  PRO A O   1 
ATOM   2313 C  CB  . PRO A 1 302  ? 20.398 63.300  30.082  1.00 25.48 ? 302  PRO A CB  1 
ATOM   2314 C  CG  . PRO A 1 302  ? 19.256 63.065  31.071  1.00 25.10 ? 302  PRO A CG  1 
ATOM   2315 C  CD  . PRO A 1 302  ? 18.098 62.763  30.147  1.00 21.46 ? 302  PRO A CD  1 
ATOM   2316 N  N   . PRO A 1 303  ? 22.166 60.801  29.340  1.00 20.35 ? 303  PRO A N   1 
ATOM   2317 C  CA  . PRO A 1 303  ? 22.854 59.602  29.802  1.00 20.06 ? 303  PRO A CA  1 
ATOM   2318 C  C   . PRO A 1 303  ? 22.852 59.726  31.325  1.00 22.08 ? 303  PRO A C   1 
ATOM   2319 O  O   . PRO A 1 303  ? 22.746 60.830  31.867  1.00 21.29 ? 303  PRO A O   1 
ATOM   2320 C  CB  . PRO A 1 303  ? 24.299 59.771  29.298  1.00 19.93 ? 303  PRO A CB  1 
ATOM   2321 C  CG  . PRO A 1 303  ? 24.243 60.937  28.326  1.00 22.59 ? 303  PRO A CG  1 
ATOM   2322 C  CD  . PRO A 1 303  ? 23.087 61.782  28.736  1.00 21.67 ? 303  PRO A CD  1 
ATOM   2323 N  N   . ARG A 1 304  ? 23.008 58.599  32.006  1.00 24.08 ? 304  ARG A N   1 
ATOM   2324 C  CA  . ARG A 1 304  ? 23.109 58.605  33.446  1.00 24.66 ? 304  ARG A CA  1 
ATOM   2325 C  C   . ARG A 1 304  ? 24.312 57.779  33.849  1.00 22.61 ? 304  ARG A C   1 
ATOM   2326 O  O   . ARG A 1 304  ? 24.545 56.701  33.280  1.00 21.99 ? 304  ARG A O   1 
ATOM   2327 C  CB  . ARG A 1 304  ? 21.852 57.997  34.087  1.00 29.30 ? 304  ARG A CB  1 
ATOM   2328 C  CG  . ARG A 1 304  ? 20.704 58.978  34.245  1.00 36.85 ? 304  ARG A CG  1 
ATOM   2329 C  CD  . ARG A 1 304  ? 19.576 58.303  35.000  1.00 42.20 ? 304  ARG A CD  1 
ATOM   2330 N  NE  . ARG A 1 304  ? 19.213 57.049  34.342  1.00 49.07 ? 304  ARG A NE  1 
ATOM   2331 C  CZ  . ARG A 1 304  ? 18.354 56.156  34.822  1.00 51.75 ? 304  ARG A CZ  1 
ATOM   2332 N  NH1 . ARG A 1 304  ? 17.737 56.349  35.987  1.00 53.58 ? 304  ARG A NH1 1 
ATOM   2333 N  NH2 . ARG A 1 304  ? 18.112 55.057  34.125  1.00 54.58 ? 304  ARG A NH2 1 
ATOM   2334 N  N   . THR A 1 305  ? 25.070 58.268  34.821  1.00 22.19 ? 305  THR A N   1 
ATOM   2335 C  CA  . THR A 1 305  ? 26.233 57.569  35.313  1.00 22.87 ? 305  THR A CA  1 
ATOM   2336 C  C   . THR A 1 305  ? 25.859 56.166  35.786  1.00 22.41 ? 305  THR A C   1 
ATOM   2337 O  O   . THR A 1 305  ? 24.901 55.987  36.542  1.00 23.97 ? 305  THR A O   1 
ATOM   2338 C  CB  . THR A 1 305  ? 26.875 58.390  36.461  1.00 23.36 ? 305  THR A CB  1 
ATOM   2339 O  OG1 . THR A 1 305  ? 27.367 59.611  35.890  1.00 26.92 ? 305  THR A OG1 1 
ATOM   2340 C  CG2 . THR A 1 305  ? 27.994 57.653  37.145  1.00 22.55 ? 305  THR A CG2 1 
ATOM   2341 N  N   . ILE A 1 306  ? 26.590 55.165  35.331  1.00 19.45 ? 306  ILE A N   1 
ATOM   2342 C  CA  . ILE A 1 306  ? 26.292 53.782  35.702  1.00 20.14 ? 306  ILE A CA  1 
ATOM   2343 C  C   . ILE A 1 306  ? 26.738 53.558  37.146  1.00 20.24 ? 306  ILE A C   1 
ATOM   2344 O  O   . ILE A 1 306  ? 27.851 53.920  37.560  1.00 21.50 ? 306  ILE A O   1 
ATOM   2345 C  CB  . ILE A 1 306  ? 27.031 52.788  34.756  1.00 20.61 ? 306  ILE A CB  1 
ATOM   2346 C  CG1 . ILE A 1 306  ? 26.679 53.081  33.289  1.00 18.68 ? 306  ILE A CG1 1 
ATOM   2347 C  CG2 . ILE A 1 306  ? 26.698 51.308  35.144  1.00 19.50 ? 306  ILE A CG2 1 
ATOM   2348 C  CD1 . ILE A 1 306  ? 25.226 53.067  32.954  1.00 19.46 ? 306  ILE A CD1 1 
ATOM   2349 N  N   . SER A 1 307  ? 25.834 52.946  37.918  1.00 22.06 ? 307  SER A N   1 
ATOM   2350 C  CA  . SER A 1 307  ? 26.077 52.632  39.326  1.00 23.33 ? 307  SER A CA  1 
ATOM   2351 C  C   . SER A 1 307  ? 25.573 51.231  39.608  1.00 23.85 ? 307  SER A C   1 
ATOM   2352 O  O   . SER A 1 307  ? 24.903 50.622  38.784  1.00 22.34 ? 307  SER A O   1 
ATOM   2353 C  CB  . SER A 1 307  ? 25.260 53.570  40.214  1.00 22.99 ? 307  SER A CB  1 
ATOM   2354 O  OG  . SER A 1 307  ? 23.869 53.363  40.018  1.00 21.91 ? 307  SER A OG  1 
ATOM   2355 N  N   . ASP A 1 308  ? 25.847 50.737  40.800  1.00 25.36 ? 308  ASP A N   1 
ATOM   2356 C  CA  . ASP A 1 308  ? 25.335 49.416  41.140  1.00 27.53 ? 308  ASP A CA  1 
ATOM   2357 C  C   . ASP A 1 308  ? 23.801 49.359  41.190  1.00 26.78 ? 308  ASP A C   1 
ATOM   2358 O  O   . ASP A 1 308  ? 23.240 48.300  40.920  1.00 25.03 ? 308  ASP A O   1 
ATOM   2359 C  CB  . ASP A 1 308  ? 25.931 48.929  42.461  1.00 31.64 ? 308  ASP A CB  1 
ATOM   2360 C  CG  . ASP A 1 308  ? 27.424 48.672  42.363  1.00 35.50 ? 308  ASP A CG  1 
ATOM   2361 O  OD1 . ASP A 1 308  ? 27.953 48.568  41.233  1.00 39.50 ? 308  ASP A OD1 1 
ATOM   2362 O  OD2 . ASP A 1 308  ? 28.089 48.551  43.409  1.00 38.87 ? 308  ASP A OD2 1 
ATOM   2363 N  N   . GLN A 1 309  ? 23.126 50.468  41.480  1.00 25.45 ? 309  GLN A N   1 
ATOM   2364 C  CA  . GLN A 1 309  ? 21.652 50.507  41.543  1.00 26.85 ? 309  GLN A CA  1 
ATOM   2365 C  C   . GLN A 1 309  ? 20.961 50.645  40.200  1.00 27.42 ? 309  GLN A C   1 
ATOM   2366 O  O   . GLN A 1 309  ? 19.732 50.465  40.088  1.00 25.33 ? 309  GLN A O   1 
ATOM   2367 C  CB  . GLN A 1 309  ? 21.133 51.658  42.435  1.00 25.21 ? 309  GLN A CB  1 
ATOM   2368 C  CG  . GLN A 1 309  ? 21.582 51.584  43.888  1.00 29.97 ? 309  GLN A CG  1 
ATOM   2369 C  CD  . GLN A 1 309  ? 23.084 51.747  44.022  1.00 31.11 ? 309  GLN A CD  1 
ATOM   2370 O  OE1 . GLN A 1 309  ? 23.662 52.702  43.476  1.00 32.93 ? 309  GLN A OE1 1 
ATOM   2371 N  NE2 . GLN A 1 309  ? 23.732 50.823  44.746  1.00 31.56 ? 309  GLN A NE2 1 
ATOM   2372 N  N   . ASN A 1 310  ? 21.703 51.013  39.159  1.00 23.77 ? 310  ASN A N   1 
ATOM   2373 C  CA  . ASN A 1 310  ? 21.007 51.130  37.895  1.00 22.17 ? 310  ASN A CA  1 
ATOM   2374 C  C   . ASN A 1 310  ? 21.685 50.279  36.830  1.00 20.88 ? 310  ASN A C   1 
ATOM   2375 O  O   . ASN A 1 310  ? 21.143 50.189  35.754  1.00 20.29 ? 310  ASN A O   1 
ATOM   2376 C  CB  . ASN A 1 310  ? 20.933 52.596  37.414  1.00 23.19 ? 310  ASN A CB  1 
ATOM   2377 C  CG  . ASN A 1 310  ? 22.307 53.190  37.052  1.00 22.24 ? 310  ASN A CG  1 
ATOM   2378 O  OD1 . ASN A 1 310  ? 23.280 52.469  36.800  1.00 22.35 ? 310  ASN A OD1 1 
ATOM   2379 N  ND2 . ASN A 1 310  ? 22.364 54.513  37.000  1.00 24.16 ? 310  ASN A ND2 1 
ATOM   2380 N  N   . VAL A 1 311  ? 22.797 49.630  37.155  1.00 19.67 ? 311  VAL A N   1 
ATOM   2381 C  CA  . VAL A 1 311  ? 23.529 48.889  36.074  1.00 18.92 ? 311  VAL A CA  1 
ATOM   2382 C  C   . VAL A 1 311  ? 22.687 47.766  35.479  1.00 21.85 ? 311  VAL A C   1 
ATOM   2383 O  O   . VAL A 1 311  ? 22.774 47.492  34.272  1.00 21.12 ? 311  VAL A O   1 
ATOM   2384 C  CB  . VAL A 1 311  ? 24.901 48.345  36.548  1.00 20.00 ? 311  VAL A CB  1 
ATOM   2385 C  CG1 . VAL A 1 311  ? 24.737 47.252  37.569  1.00 20.40 ? 311  VAL A CG1 1 
ATOM   2386 C  CG2 . VAL A 1 311  ? 25.733 47.825  35.311  1.00 19.40 ? 311  VAL A CG2 1 
ATOM   2387 N  N   . ALA A 1 312  ? 21.829 47.129  36.270  1.00 19.55 ? 312  ALA A N   1 
ATOM   2388 C  CA  . ALA A 1 312  ? 21.038 46.058  35.679  1.00 20.78 ? 312  ALA A CA  1 
ATOM   2389 C  C   . ALA A 1 312  ? 20.028 46.615  34.698  1.00 23.26 ? 312  ALA A C   1 
ATOM   2390 O  O   . ALA A 1 312  ? 19.864 46.053  33.611  1.00 22.41 ? 312  ALA A O   1 
ATOM   2391 C  CB  . ALA A 1 312  ? 20.323 45.209  36.797  1.00 21.71 ? 312  ALA A CB  1 
ATOM   2392 N  N   . ALA A 1 313  ? 19.355 47.712  35.026  1.00 19.83 ? 313  ALA A N   1 
ATOM   2393 C  CA  . ALA A 1 313  ? 18.371 48.292  34.127  1.00 21.34 ? 313  ALA A CA  1 
ATOM   2394 C  C   . ALA A 1 313  ? 19.041 48.900  32.898  1.00 22.01 ? 313  ALA A C   1 
ATOM   2395 O  O   . ALA A 1 313  ? 18.524 48.779  31.793  1.00 21.85 ? 313  ALA A O   1 
ATOM   2396 C  CB  . ALA A 1 313  ? 17.517 49.365  34.865  1.00 22.64 ? 313  ALA A CB  1 
ATOM   2397 N  N   . ARG A 1 314  ? 20.149 49.590  33.106  1.00 22.34 ? 314  ARG A N   1 
ATOM   2398 C  CA  . ARG A 1 314  ? 20.877 50.195  31.976  1.00 22.11 ? 314  ARG A CA  1 
ATOM   2399 C  C   . ARG A 1 314  ? 21.384 49.089  31.050  1.00 21.36 ? 314  ARG A C   1 
ATOM   2400 O  O   . ARG A 1 314  ? 21.302 49.245  29.815  1.00 20.26 ? 314  ARG A O   1 
ATOM   2401 C  CB  . ARG A 1 314  ? 22.060 51.017  32.487  1.00 19.98 ? 314  ARG A CB  1 
ATOM   2402 C  CG  . ARG A 1 314  ? 21.669 52.178  33.376  1.00 22.79 ? 314  ARG A CG  1 
ATOM   2403 C  CD  . ARG A 1 314  ? 21.394 53.411  32.589  1.00 25.58 ? 314  ARG A CD  1 
ATOM   2404 N  NE  . ARG A 1 314  ? 20.035 53.436  32.102  1.00 27.75 ? 314  ARG A NE  1 
ATOM   2405 C  CZ  . ARG A 1 314  ? 19.552 54.322  31.245  1.00 28.07 ? 314  ARG A CZ  1 
ATOM   2406 N  NH1 . ARG A 1 314  ? 20.336 55.279  30.737  1.00 29.80 ? 314  ARG A NH1 1 
ATOM   2407 N  NH2 . ARG A 1 314  ? 18.256 54.309  30.945  1.00 28.79 ? 314  ARG A NH2 1 
ATOM   2408 N  N   . SER A 1 315  ? 21.888 48.000  31.626  1.00 20.87 ? 315  SER A N   1 
ATOM   2409 C  CA  . SER A 1 315  ? 22.378 46.856  30.810  1.00 20.81 ? 315  SER A CA  1 
ATOM   2410 C  C   . SER A 1 315  ? 21.244 46.226  30.053  1.00 23.32 ? 315  SER A C   1 
ATOM   2411 O  O   . SER A 1 315  ? 21.398 45.806  28.896  1.00 22.64 ? 315  SER A O   1 
ATOM   2412 C  CB  . SER A 1 315  ? 23.018 45.795  31.678  1.00 19.34 ? 315  SER A CB  1 
ATOM   2413 O  OG  . SER A 1 315  ? 24.211 46.280  32.236  1.00 21.08 ? 315  SER A OG  1 
ATOM   2414 N  N   . ASP A 1 316  ? 20.083 46.112  30.684  1.00 22.55 ? 316  ASP A N   1 
ATOM   2415 C  CA  . ASP A 1 316  ? 18.952 45.533  29.981  1.00 25.29 ? 316  ASP A CA  1 
ATOM   2416 C  C   . ASP A 1 316  ? 18.589 46.382  28.743  1.00 24.00 ? 316  ASP A C   1 
ATOM   2417 O  O   . ASP A 1 316  ? 18.281 45.837  27.659  1.00 22.34 ? 316  ASP A O   1 
ATOM   2418 C  CB  . ASP A 1 316  ? 17.742 45.434  30.920  1.00 27.61 ? 316  ASP A CB  1 
ATOM   2419 C  CG  . ASP A 1 316  ? 16.785 44.360  30.482  1.00 33.97 ? 316  ASP A CG  1 
ATOM   2420 O  OD1 . ASP A 1 316  ? 17.294 43.258  30.134  1.00 34.29 ? 316  ASP A OD1 1 
ATOM   2421 O  OD2 . ASP A 1 316  ? 15.556 44.617  30.469  1.00 36.15 ? 316  ASP A OD2 1 
ATOM   2422 N  N   . LEU A 1 317  ? 18.629 47.707  28.872  1.00 21.77 ? 317  LEU A N   1 
ATOM   2423 C  CA  . LEU A 1 317  ? 18.295 48.572  27.738  1.00 22.09 ? 317  LEU A CA  1 
ATOM   2424 C  C   . LEU A 1 317  ? 19.346 48.458  26.641  1.00 18.87 ? 317  LEU A C   1 
ATOM   2425 O  O   . LEU A 1 317  ? 19.001 48.347  25.465  1.00 18.53 ? 317  LEU A O   1 
ATOM   2426 C  CB  . LEU A 1 317  ? 18.209 50.051  28.155  1.00 24.53 ? 317  LEU A CB  1 
ATOM   2427 C  CG  . LEU A 1 317  ? 16.848 50.597  28.573  1.00 28.63 ? 317  LEU A CG  1 
ATOM   2428 C  CD1 . LEU A 1 317  ? 17.093 51.910  29.326  1.00 29.59 ? 317  LEU A CD1 1 
ATOM   2429 C  CD2 . LEU A 1 317  ? 15.933 50.810  27.360  1.00 27.94 ? 317  LEU A CD2 1 
ATOM   2430 N  N   . LEU A 1 318  ? 20.602 48.461  27.051  1.00 17.95 ? 318  LEU A N   1 
ATOM   2431 C  CA  . LEU A 1 318  ? 21.717 48.432  26.071  1.00 17.35 ? 318  LEU A CA  1 
ATOM   2432 C  C   . LEU A 1 318  ? 21.818 47.109  25.367  1.00 17.95 ? 318  LEU A C   1 
ATOM   2433 O  O   . LEU A 1 318  ? 21.971 47.058  24.124  1.00 17.79 ? 318  LEU A O   1 
ATOM   2434 C  CB  . LEU A 1 318  ? 23.032 48.761  26.764  1.00 16.56 ? 318  LEU A CB  1 
ATOM   2435 C  CG  . LEU A 1 318  ? 24.281 48.845  25.846  1.00 17.59 ? 318  LEU A CG  1 
ATOM   2436 C  CD1 . LEU A 1 318  ? 24.050 49.944  24.789  1.00 18.99 ? 318  LEU A CD1 1 
ATOM   2437 C  CD2 . LEU A 1 318  ? 25.537 49.126  26.684  1.00 18.03 ? 318  LEU A CD2 1 
ATOM   2438 N  N   . VAL A 1 319  ? 21.747 46.017  26.108  1.00 17.08 ? 319  VAL A N   1 
ATOM   2439 C  CA  . VAL A 1 319  ? 21.862 44.694  25.479  1.00 16.78 ? 319  VAL A CA  1 
ATOM   2440 C  C   . VAL A 1 319  ? 20.694 44.485  24.503  1.00 17.66 ? 319  VAL A C   1 
ATOM   2441 O  O   . VAL A 1 319  ? 20.852 43.841  23.462  1.00 17.29 ? 319  VAL A O   1 
ATOM   2442 C  CB  . VAL A 1 319  ? 21.889 43.543  26.525  1.00 17.06 ? 319  VAL A CB  1 
ATOM   2443 C  CG1 . VAL A 1 319  ? 21.737 42.193  25.795  1.00 19.57 ? 319  VAL A CG1 1 
ATOM   2444 C  CG2 . VAL A 1 319  ? 23.182 43.541  27.304  1.00 18.79 ? 319  VAL A CG2 1 
ATOM   2445 N  N   . ASP A 1 320  ? 19.523 45.019  24.823  1.00 18.36 ? 320  ASP A N   1 
ATOM   2446 C  CA  . ASP A 1 320  ? 18.380 44.906  23.912  1.00 17.90 ? 320  ASP A CA  1 
ATOM   2447 C  C   . ASP A 1 320  ? 18.710 45.633  22.584  1.00 17.70 ? 320  ASP A C   1 
ATOM   2448 O  O   . ASP A 1 320  ? 18.378 45.108  21.504  1.00 18.23 ? 320  ASP A O   1 
ATOM   2449 C  CB  . ASP A 1 320  ? 17.111 45.473  24.593  1.00 21.55 ? 320  ASP A CB  1 
ATOM   2450 C  CG  . ASP A 1 320  ? 15.924 45.531  23.672  1.00 19.12 ? 320  ASP A CG  1 
ATOM   2451 O  OD1 . ASP A 1 320  ? 15.421 44.446  23.291  1.00 23.33 ? 320  ASP A OD1 1 
ATOM   2452 O  OD2 . ASP A 1 320  ? 15.448 46.623  23.315  1.00 21.51 ? 320  ASP A OD2 1 
ATOM   2453 N  N   . GLN A 1 321  ? 19.329 46.820  22.658  1.00 16.47 ? 321  GLN A N   1 
ATOM   2454 C  CA  . GLN A 1 321  ? 19.713 47.525  21.422  1.00 15.61 ? 321  GLN A CA  1 
ATOM   2455 C  C   . GLN A 1 321  ? 20.726 46.661  20.640  1.00 14.57 ? 321  GLN A C   1 
ATOM   2456 O  O   . GLN A 1 321  ? 20.591 46.539  19.429  1.00 16.11 ? 321  GLN A O   1 
ATOM   2457 C  CB  . GLN A 1 321  ? 20.364 48.873  21.771  1.00 14.40 ? 321  GLN A CB  1 
ATOM   2458 C  CG  . GLN A 1 321  ? 19.365 49.934  22.209  1.00 17.11 ? 321  GLN A CG  1 
ATOM   2459 C  CD  . GLN A 1 321  ? 18.281 50.123  21.144  1.00 19.00 ? 321  GLN A CD  1 
ATOM   2460 O  OE1 . GLN A 1 321  ? 18.571 50.528  20.033  1.00 18.92 ? 321  GLN A OE1 1 
ATOM   2461 N  NE2 . GLN A 1 321  ? 17.014 49.831  21.491  1.00 19.48 ? 321  GLN A NE2 1 
ATOM   2462 N  N   . TRP A 1 322  ? 21.748 46.138  21.315  1.00 15.01 ? 322  TRP A N   1 
ATOM   2463 C  CA  . TRP A 1 322  ? 22.746 45.287  20.657  1.00 14.60 ? 322  TRP A CA  1 
ATOM   2464 C  C   . TRP A 1 322  ? 22.113 44.081  19.970  1.00 15.97 ? 322  TRP A C   1 
ATOM   2465 O  O   . TRP A 1 322  ? 22.462 43.744  18.822  1.00 16.51 ? 322  TRP A O   1 
ATOM   2466 C  CB  . TRP A 1 322  ? 23.770 44.794  21.667  1.00 14.59 ? 322  TRP A CB  1 
ATOM   2467 C  CG  . TRP A 1 322  ? 24.690 45.862  22.216  1.00 16.22 ? 322  TRP A CG  1 
ATOM   2468 C  CD1 . TRP A 1 322  ? 24.879 47.157  21.754  1.00 15.61 ? 322  TRP A CD1 1 
ATOM   2469 C  CD2 . TRP A 1 322  ? 25.574 45.702  23.311  1.00 15.30 ? 322  TRP A CD2 1 
ATOM   2470 N  NE1 . TRP A 1 322  ? 25.844 47.796  22.520  1.00 16.90 ? 322  TRP A NE1 1 
ATOM   2471 C  CE2 . TRP A 1 322  ? 26.282 46.926  23.477  1.00 15.00 ? 322  TRP A CE2 1 
ATOM   2472 C  CE3 . TRP A 1 322  ? 25.850 44.638  24.180  1.00 17.33 ? 322  TRP A CE3 1 
ATOM   2473 C  CZ2 . TRP A 1 322  ? 27.245 47.112  24.489  1.00 16.94 ? 322  TRP A CZ2 1 
ATOM   2474 C  CZ3 . TRP A 1 322  ? 26.812 44.813  25.182  1.00 15.04 ? 322  TRP A CZ3 1 
ATOM   2475 C  CH2 . TRP A 1 322  ? 27.495 46.037  25.331  1.00 17.77 ? 322  TRP A CH2 1 
ATOM   2476 N  N   . LYS A 1 323  ? 21.193 43.418  20.664  1.00 16.01 ? 323  LYS A N   1 
ATOM   2477 C  CA  . LYS A 1 323  ? 20.581 42.221  20.056  1.00 17.28 ? 323  LYS A CA  1 
ATOM   2478 C  C   . LYS A 1 323  ? 19.734 42.559  18.856  1.00 16.87 ? 323  LYS A C   1 
ATOM   2479 O  O   . LYS A 1 323  ? 19.639 41.788  17.908  1.00 16.77 ? 323  LYS A O   1 
ATOM   2480 C  CB  . LYS A 1 323  ? 19.794 41.401  21.116  1.00 18.69 ? 323  LYS A CB  1 
ATOM   2481 C  CG  . LYS A 1 323  ? 20.778 40.606  21.997  1.00 17.62 ? 323  LYS A CG  1 
ATOM   2482 C  CD  . LYS A 1 323  ? 20.096 39.784  23.085  1.00 18.49 ? 323  LYS A CD  1 
ATOM   2483 C  CE  . LYS A 1 323  ? 21.107 38.880  23.733  1.00 20.92 ? 323  LYS A CE  1 
ATOM   2484 N  NZ  . LYS A 1 323  ? 20.429 38.109  24.798  1.00 26.42 ? 323  LYS A NZ  1 
ATOM   2485 N  N   . LYS A 1 324  ? 19.122 43.716  18.858  1.00 15.89 ? 324  LYS A N   1 
ATOM   2486 C  CA  . LYS A 1 324  ? 18.358 44.179  17.693  1.00 16.82 ? 324  LYS A CA  1 
ATOM   2487 C  C   . LYS A 1 324  ? 19.344 44.466  16.543  1.00 15.60 ? 324  LYS A C   1 
ATOM   2488 O  O   . LYS A 1 324  ? 19.103 44.079  15.413  1.00 16.36 ? 324  LYS A O   1 
ATOM   2489 C  CB  . LYS A 1 324  ? 17.566 45.449  18.037  1.00 16.10 ? 324  LYS A CB  1 
ATOM   2490 C  CG  . LYS A 1 324  ? 16.324 45.093  18.838  1.00 16.72 ? 324  LYS A CG  1 
ATOM   2491 C  CD  . LYS A 1 324  ? 15.696 46.323  19.449  1.00 19.13 ? 324  LYS A CD  1 
ATOM   2492 C  CE  . LYS A 1 324  ? 14.395 45.885  20.175  1.00 21.53 ? 324  LYS A CE  1 
ATOM   2493 N  NZ  . LYS A 1 324  ? 13.795 47.009  20.940  1.00 22.54 ? 324  LYS A NZ  1 
ATOM   2494 N  N   . LYS A 1 325  ? 20.454 45.156  16.818  1.00 15.10 ? 325  LYS A N   1 
ATOM   2495 C  CA  . LYS A 1 325  ? 21.413 45.430  15.737  1.00 13.30 ? 325  LYS A CA  1 
ATOM   2496 C  C   . LYS A 1 325  ? 21.959 44.116  15.202  1.00 13.86 ? 325  LYS A C   1 
ATOM   2497 O  O   . LYS A 1 325  ? 22.169 43.962  13.981  1.00 13.83 ? 325  LYS A O   1 
ATOM   2498 C  CB  . LYS A 1 325  ? 22.557 46.302  16.270  1.00 12.51 ? 325  LYS A CB  1 
ATOM   2499 C  CG  . LYS A 1 325  ? 23.443 46.902  15.144  1.00 14.09 ? 325  LYS A CG  1 
ATOM   2500 C  CD  . LYS A 1 325  ? 24.561 47.779  15.730  1.00 14.28 ? 325  LYS A CD  1 
ATOM   2501 C  CE  . LYS A 1 325  ? 25.349 48.482  14.581  1.00 13.64 ? 325  LYS A CE  1 
ATOM   2502 N  NZ  . LYS A 1 325  ? 26.541 49.148  15.192  1.00 16.17 ? 325  LYS A NZ  1 
ATOM   2503 N  N   . ALA A 1 326  ? 22.214 43.157  16.085  1.00 15.08 ? 326  ALA A N   1 
ATOM   2504 C  CA  . ALA A 1 326  ? 22.753 41.857  15.666  1.00 16.07 ? 326  ALA A CA  1 
ATOM   2505 C  C   . ALA A 1 326  ? 21.814 41.103  14.725  1.00 16.10 ? 326  ALA A C   1 
ATOM   2506 O  O   . ALA A 1 326  ? 22.278 40.250  13.955  1.00 15.58 ? 326  ALA A O   1 
ATOM   2507 C  CB  . ALA A 1 326  ? 23.084 41.002  16.888  1.00 15.89 ? 326  ALA A CB  1 
ATOM   2508 N  N   . GLU A 1 327  ? 20.520 41.403  14.783  1.00 16.90 ? 327  GLU A N   1 
ATOM   2509 C  CA  . GLU A 1 327  ? 19.569 40.759  13.876  1.00 17.72 ? 327  GLU A CA  1 
ATOM   2510 C  C   . GLU A 1 327  ? 19.818 41.102  12.419  1.00 19.56 ? 327  GLU A C   1 
ATOM   2511 O  O   . GLU A 1 327  ? 19.368 40.384  11.530  1.00 19.67 ? 327  GLU A O   1 
ATOM   2512 C  CB  . GLU A 1 327  ? 18.129 41.172  14.195  1.00 20.92 ? 327  GLU A CB  1 
ATOM   2513 C  CG  . GLU A 1 327  ? 17.508 40.395  15.289  1.00 25.04 ? 327  GLU A CG  1 
ATOM   2514 C  CD  . GLU A 1 327  ? 17.540 38.885  15.033  1.00 21.21 ? 327  GLU A CD  1 
ATOM   2515 O  OE1 . GLU A 1 327  ? 16.889 38.365  14.083  1.00 26.56 ? 327  GLU A OE1 1 
ATOM   2516 O  OE2 . GLU A 1 327  ? 18.236 38.217  15.803  1.00 23.82 ? 327  GLU A OE2 1 
ATOM   2517 N  N   . LEU A 1 328  ? 20.521 42.209  12.169  1.00 15.89 ? 328  LEU A N   1 
ATOM   2518 C  CA  . LEU A 1 328  ? 20.759 42.654  10.791  1.00 14.03 ? 328  LEU A CA  1 
ATOM   2519 C  C   . LEU A 1 328  ? 21.965 42.003  10.146  1.00 15.87 ? 328  LEU A C   1 
ATOM   2520 O  O   . LEU A 1 328  ? 22.234 42.264  8.976   1.00 16.50 ? 328  LEU A O   1 
ATOM   2521 C  CB  . LEU A 1 328  ? 20.962 44.174  10.793  1.00 14.18 ? 328  LEU A CB  1 
ATOM   2522 C  CG  . LEU A 1 328  ? 19.855 44.965  11.509  1.00 14.73 ? 328  LEU A CG  1 
ATOM   2523 C  CD1 . LEU A 1 328  ? 20.082 46.483  11.289  1.00 16.19 ? 328  LEU A CD1 1 
ATOM   2524 C  CD2 . LEU A 1 328  ? 18.446 44.590  10.975  1.00 16.99 ? 328  LEU A CD2 1 
ATOM   2525 N  N   . TYR A 1 329  ? 22.701 41.193  10.902  1.00 14.95 ? 329  TYR A N   1 
ATOM   2526 C  CA  . TYR A 1 329  ? 23.918 40.564  10.435  1.00 13.91 ? 329  TYR A CA  1 
ATOM   2527 C  C   . TYR A 1 329  ? 23.888 39.067  10.628  1.00 16.05 ? 329  TYR A C   1 
ATOM   2528 O  O   . TYR A 1 329  ? 23.061 38.541  11.384  1.00 18.57 ? 329  TYR A O   1 
ATOM   2529 C  CB  . TYR A 1 329  ? 25.160 41.164  11.136  1.00 15.88 ? 329  TYR A CB  1 
ATOM   2530 C  CG  . TYR A 1 329  ? 25.374 42.638  10.807  1.00 14.39 ? 329  TYR A CG  1 
ATOM   2531 C  CD1 . TYR A 1 329  ? 26.093 42.999  9.698   1.00 15.23 ? 329  TYR A CD1 1 
ATOM   2532 C  CD2 . TYR A 1 329  ? 24.789 43.647  11.588  1.00 14.03 ? 329  TYR A CD2 1 
ATOM   2533 C  CE1 . TYR A 1 329  ? 26.223 44.350  9.342   1.00 13.74 ? 329  TYR A CE1 1 
ATOM   2534 C  CE2 . TYR A 1 329  ? 24.922 44.986  11.269  1.00 15.12 ? 329  TYR A CE2 1 
ATOM   2535 C  CZ  . TYR A 1 329  ? 25.641 45.332  10.120  1.00 13.75 ? 329  TYR A CZ  1 
ATOM   2536 O  OH  . TYR A 1 329  ? 25.723 46.674  9.760   1.00 15.97 ? 329  TYR A OH  1 
ATOM   2537 N  N   . ARG A 1 330  ? 24.800 38.385  9.969   1.00 15.49 ? 330  ARG A N   1 
ATOM   2538 C  CA  . ARG A 1 330  ? 24.788 36.924  9.972   1.00 15.70 ? 330  ARG A CA  1 
ATOM   2539 C  C   . ARG A 1 330  ? 25.563 36.162  11.011  1.00 17.60 ? 330  ARG A C   1 
ATOM   2540 O  O   . ARG A 1 330  ? 25.338 34.954  11.165  1.00 20.81 ? 330  ARG A O   1 
ATOM   2541 C  CB  . ARG A 1 330  ? 25.185 36.420  8.569   1.00 16.19 ? 330  ARG A CB  1 
ATOM   2542 C  CG  . ARG A 1 330  ? 24.211 36.859  7.494   1.00 17.09 ? 330  ARG A CG  1 
ATOM   2543 C  CD  . ARG A 1 330  ? 24.594 36.321  6.098   1.00 17.95 ? 330  ARG A CD  1 
ATOM   2544 N  NE  . ARG A 1 330  ? 23.600 36.858  5.186   1.00 18.84 ? 330  ARG A NE  1 
ATOM   2545 C  CZ  . ARG A 1 330  ? 23.256 36.343  4.010   1.00 23.89 ? 330  ARG A CZ  1 
ATOM   2546 N  NH1 . ARG A 1 330  ? 23.839 35.242  3.546   1.00 23.95 ? 330  ARG A NH1 1 
ATOM   2547 N  NH2 . ARG A 1 330  ? 22.301 36.939  3.299   1.00 21.92 ? 330  ARG A NH2 1 
ATOM   2548 N  N   . THR A 1 331  ? 26.489 36.808  11.708  1.00 16.28 ? 331  THR A N   1 
ATOM   2549 C  CA  . THR A 1 331  ? 27.268 36.068  12.706  1.00 14.82 ? 331  THR A CA  1 
ATOM   2550 C  C   . THR A 1 331  ? 26.872 36.498  14.098  1.00 14.86 ? 331  THR A C   1 
ATOM   2551 O  O   . THR A 1 331  ? 26.036 37.389  14.249  1.00 18.46 ? 331  THR A O   1 
ATOM   2552 C  CB  . THR A 1 331  ? 28.807 36.299  12.563  1.00 17.03 ? 331  THR A CB  1 
ATOM   2553 O  OG1 . THR A 1 331  ? 29.157 37.606  13.031  1.00 15.50 ? 331  THR A OG1 1 
ATOM   2554 C  CG2 . THR A 1 331  ? 29.266 36.129  11.066  1.00 17.35 ? 331  THR A CG2 1 
ATOM   2555 N  N   . ASN A 1 332  ? 27.483 35.855  15.093  1.00 16.72 ? 332  ASN A N   1 
ATOM   2556 C  CA  . ASN A 1 332  ? 27.264 36.215  16.495  1.00 17.69 ? 332  ASN A CA  1 
ATOM   2557 C  C   . ASN A 1 332  ? 28.350 37.157  16.991  1.00 16.87 ? 332  ASN A C   1 
ATOM   2558 O  O   . ASN A 1 332  ? 28.617 37.243  18.200  1.00 18.35 ? 332  ASN A O   1 
ATOM   2559 C  CB  . ASN A 1 332  ? 27.256 34.959  17.381  1.00 19.05 ? 332  ASN A CB  1 
ATOM   2560 C  CG  . ASN A 1 332  ? 28.630 34.287  17.507  1.00 24.76 ? 332  ASN A CG  1 
ATOM   2561 O  OD1 . ASN A 1 332  ? 29.445 34.266  16.583  1.00 24.79 ? 332  ASN A OD1 1 
ATOM   2562 N  ND2 . ASN A 1 332  ? 28.870 33.685  18.677  1.00 27.86 ? 332  ASN A ND2 1 
ATOM   2563 N  N   . VAL A 1 333  ? 28.952 37.908  16.070  1.00 15.66 ? 333  VAL A N   1 
ATOM   2564 C  CA  . VAL A 1 333  ? 30.001 38.859  16.399  1.00 14.68 ? 333  VAL A CA  1 
ATOM   2565 C  C   . VAL A 1 333  ? 29.438 40.215  15.971  1.00 14.89 ? 333  VAL A C   1 
ATOM   2566 O  O   . VAL A 1 333  ? 29.127 40.402  14.796  1.00 16.33 ? 333  VAL A O   1 
ATOM   2567 C  CB  . VAL A 1 333  ? 31.289 38.544  15.611  1.00 14.41 ? 333  VAL A CB  1 
ATOM   2568 C  CG1 . VAL A 1 333  ? 32.380 39.556  15.977  1.00 17.65 ? 333  VAL A CG1 1 
ATOM   2569 C  CG2 . VAL A 1 333  ? 31.740 37.103  15.916  1.00 17.95 ? 333  VAL A CG2 1 
ATOM   2570 N  N   . LEU A 1 334  ? 29.346 41.165  16.905  1.00 14.01 ? 334  LEU A N   1 
ATOM   2571 C  CA  . LEU A 1 334  ? 28.731 42.459  16.658  1.00 12.84 ? 334  LEU A CA  1 
ATOM   2572 C  C   . LEU A 1 334  ? 29.694 43.616  16.818  1.00 12.01 ? 334  LEU A C   1 
ATOM   2573 O  O   . LEU A 1 334  ? 30.413 43.706  17.810  1.00 15.20 ? 334  LEU A O   1 
ATOM   2574 C  CB  . LEU A 1 334  ? 27.586 42.671  17.657  1.00 13.46 ? 334  LEU A CB  1 
ATOM   2575 C  CG  . LEU A 1 334  ? 26.736 43.928  17.466  1.00 13.91 ? 334  LEU A CG  1 
ATOM   2576 C  CD1 . LEU A 1 334  ? 25.958 43.804  16.145  1.00 15.48 ? 334  LEU A CD1 1 
ATOM   2577 C  CD2 . LEU A 1 334  ? 25.766 44.089  18.676  1.00 15.34 ? 334  LEU A CD2 1 
ATOM   2578 N  N   . LEU A 1 335  ? 29.666 44.527  15.832  1.00 12.61 ? 335  LEU A N   1 
ATOM   2579 C  CA  . LEU A 1 335  ? 30.536 45.699  15.855  1.00 12.77 ? 335  LEU A CA  1 
ATOM   2580 C  C   . LEU A 1 335  ? 29.757 46.889  16.400  1.00 12.18 ? 335  LEU A C   1 
ATOM   2581 O  O   . LEU A 1 335  ? 28.712 47.234  15.869  1.00 14.16 ? 335  LEU A O   1 
ATOM   2582 C  CB  . LEU A 1 335  ? 31.001 46.027  14.427  1.00 12.74 ? 335  LEU A CB  1 
ATOM   2583 C  CG  . LEU A 1 335  ? 31.848 47.303  14.304  1.00 11.84 ? 335  LEU A CG  1 
ATOM   2584 C  CD1 . LEU A 1 335  ? 33.168 47.173  15.067  1.00 15.97 ? 335  LEU A CD1 1 
ATOM   2585 C  CD2 . LEU A 1 335  ? 32.081 47.613  12.826  1.00 14.85 ? 335  LEU A CD2 1 
ATOM   2586 N  N   . ILE A 1 336  ? 30.276 47.516  17.455  1.00 12.38 ? 336  ILE A N   1 
ATOM   2587 C  CA  . ILE A 1 336  ? 29.659 48.699  18.017  1.00 13.57 ? 336  ILE A CA  1 
ATOM   2588 C  C   . ILE A 1 336  ? 30.671 49.865  18.062  1.00 12.40 ? 336  ILE A C   1 
ATOM   2589 O  O   . ILE A 1 336  ? 31.463 49.981  19.008  1.00 13.18 ? 336  ILE A O   1 
ATOM   2590 C  CB  . ILE A 1 336  ? 29.124 48.461  19.448  1.00 15.90 ? 336  ILE A CB  1 
ATOM   2591 C  CG1 . ILE A 1 336  ? 28.089 47.326  19.456  1.00 13.52 ? 336  ILE A CG1 1 
ATOM   2592 C  CG2 . ILE A 1 336  ? 28.535 49.785  19.963  1.00 14.38 ? 336  ILE A CG2 1 
ATOM   2593 C  CD1 . ILE A 1 336  ? 26.824 47.647  18.682  1.00 14.37 ? 336  ILE A CD1 1 
ATOM   2594 N  N   . PRO A 1 337  ? 30.706 50.704  17.024  1.00 13.48 ? 337  PRO A N   1 
ATOM   2595 C  CA  . PRO A 1 337  ? 31.646 51.839  17.075  1.00 13.16 ? 337  PRO A CA  1 
ATOM   2596 C  C   . PRO A 1 337  ? 31.227 52.752  18.243  1.00 14.10 ? 337  PRO A C   1 
ATOM   2597 O  O   . PRO A 1 337  ? 30.033 52.879  18.550  1.00 15.02 ? 337  PRO A O   1 
ATOM   2598 C  CB  . PRO A 1 337  ? 31.385 52.563  15.745  1.00 13.25 ? 337  PRO A CB  1 
ATOM   2599 C  CG  . PRO A 1 337  ? 30.930 51.444  14.844  1.00 13.03 ? 337  PRO A CG  1 
ATOM   2600 C  CD  . PRO A 1 337  ? 29.961 50.685  15.746  1.00 14.55 ? 337  PRO A CD  1 
ATOM   2601 N  N   . LEU A 1 338  ? 32.213 53.391  18.880  1.00 12.36 ? 338  LEU A N   1 
ATOM   2602 C  CA  . LEU A 1 338  ? 31.939 54.323  19.971  1.00 12.66 ? 338  LEU A CA  1 
ATOM   2603 C  C   . LEU A 1 338  ? 32.750 55.600  19.745  1.00 12.65 ? 338  LEU A C   1 
ATOM   2604 O  O   . LEU A 1 338  ? 33.923 55.689  20.147  1.00 13.63 ? 338  LEU A O   1 
ATOM   2605 C  CB  . LEU A 1 338  ? 32.280 53.657  21.294  1.00 14.48 ? 338  LEU A CB  1 
ATOM   2606 C  CG  . LEU A 1 338  ? 31.912 54.560  22.487  1.00 15.72 ? 338  LEU A CG  1 
ATOM   2607 C  CD1 . LEU A 1 338  ? 30.406 54.483  22.803  1.00 17.11 ? 338  LEU A CD1 1 
ATOM   2608 C  CD2 . LEU A 1 338  ? 32.716 54.087  23.690  1.00 17.73 ? 338  LEU A CD2 1 
ATOM   2609 N  N   . GLY A 1 339  ? 32.109 56.563  19.066  1.00 12.87 ? 339  GLY A N   1 
ATOM   2610 C  CA  . GLY A 1 339  ? 32.859 57.799  18.783  1.00 12.98 ? 339  GLY A CA  1 
ATOM   2611 C  C   . GLY A 1 339  ? 32.056 58.788  17.981  1.00 13.14 ? 339  GLY A C   1 
ATOM   2612 O  O   . GLY A 1 339  ? 30.884 58.549  17.688  1.00 14.55 ? 339  GLY A O   1 
ATOM   2613 N  N   . ASP A 1 340  ? 32.715 59.908  17.623  1.00 12.80 ? 340  ASP A N   1 
ATOM   2614 C  CA  . ASP A 1 340  ? 32.078 60.978  16.892  1.00 13.05 ? 340  ASP A CA  1 
ATOM   2615 C  C   . ASP A 1 340  ? 33.208 61.930  16.485  1.00 11.88 ? 340  ASP A C   1 
ATOM   2616 O  O   . ASP A 1 340  ? 34.396 61.632  16.698  1.00 12.32 ? 340  ASP A O   1 
ATOM   2617 C  CB  . ASP A 1 340  ? 31.044 61.670  17.814  1.00 13.34 ? 340  ASP A CB  1 
ATOM   2618 C  CG  . ASP A 1 340  ? 29.930 62.388  17.057  1.00 14.99 ? 340  ASP A CG  1 
ATOM   2619 O  OD1 . ASP A 1 340  ? 30.090 62.736  15.836  1.00 15.67 ? 340  ASP A OD1 1 
ATOM   2620 O  OD2 . ASP A 1 340  ? 28.897 62.647  17.729  1.00 16.76 ? 340  ASP A OD2 1 
ATOM   2621 N  N   . ASP A 1 341  ? 32.825 63.080  15.970  1.00 13.19 ? 341  ASP A N   1 
ATOM   2622 C  CA  . ASP A 1 341  ? 33.819 64.032  15.455  1.00 13.27 ? 341  ASP A CA  1 
ATOM   2623 C  C   . ASP A 1 341  ? 34.696 64.563  16.581  1.00 14.73 ? 341  ASP A C   1 
ATOM   2624 O  O   . ASP A 1 341  ? 34.191 65.054  17.614  1.00 15.15 ? 341  ASP A O   1 
ATOM   2625 C  CB  . ASP A 1 341  ? 33.134 65.202  14.764  1.00 15.57 ? 341  ASP A CB  1 
ATOM   2626 C  CG  . ASP A 1 341  ? 32.469 64.810  13.462  1.00 15.98 ? 341  ASP A CG  1 
ATOM   2627 O  OD1 . ASP A 1 341  ? 32.403 63.603  13.142  1.00 15.96 ? 341  ASP A OD1 1 
ATOM   2628 O  OD2 . ASP A 1 341  ? 32.019 65.746  12.756  1.00 17.85 ? 341  ASP A OD2 1 
ATOM   2629 N  N   . PHE A 1 342  ? 35.997 64.476  16.372  1.00 12.47 ? 342  PHE A N   1 
ATOM   2630 C  CA  . PHE A 1 342  ? 36.990 64.980  17.318  1.00 12.35 ? 342  PHE A CA  1 
ATOM   2631 C  C   . PHE A 1 342  ? 36.721 64.591  18.781  1.00 13.57 ? 342  PHE A C   1 
ATOM   2632 O  O   . PHE A 1 342  ? 36.960 65.374  19.712  1.00 16.61 ? 342  PHE A O   1 
ATOM   2633 C  CB  . PHE A 1 342  ? 37.164 66.513  17.123  1.00 13.51 ? 342  PHE A CB  1 
ATOM   2634 C  CG  . PHE A 1 342  ? 37.738 66.892  15.773  1.00 12.95 ? 342  PHE A CG  1 
ATOM   2635 C  CD1 . PHE A 1 342  ? 39.112 66.868  15.550  1.00 12.24 ? 342  PHE A CD1 1 
ATOM   2636 C  CD2 . PHE A 1 342  ? 36.885 67.292  14.707  1.00 12.75 ? 342  PHE A CD2 1 
ATOM   2637 C  CE1 . PHE A 1 342  ? 39.655 67.232  14.308  1.00 12.14 ? 342  PHE A CE1 1 
ATOM   2638 C  CE2 . PHE A 1 342  ? 37.433 67.654  13.478  1.00 14.71 ? 342  PHE A CE2 1 
ATOM   2639 C  CZ  . PHE A 1 342  ? 38.799 67.621  13.287  1.00 13.50 ? 342  PHE A CZ  1 
ATOM   2640 N  N   . ARG A 1 343  ? 36.332 63.334  18.949  1.00 13.93 ? 343  ARG A N   1 
ATOM   2641 C  CA  . ARG A 1 343  ? 36.096 62.818  20.275  1.00 12.80 ? 343  ARG A CA  1 
ATOM   2642 C  C   . ARG A 1 343  ? 37.380 62.360  20.942  1.00 15.89 ? 343  ARG A C   1 
ATOM   2643 O  O   . ARG A 1 343  ? 38.462 62.271  20.337  1.00 14.13 ? 343  ARG A O   1 
ATOM   2644 C  CB  . ARG A 1 343  ? 35.052 61.679  20.219  1.00 12.78 ? 343  ARG A CB  1 
ATOM   2645 C  CG  . ARG A 1 343  ? 33.621 62.145  19.965  1.00 14.74 ? 343  ARG A CG  1 
ATOM   2646 C  CD  . ARG A 1 343  ? 33.169 63.105  21.104  1.00 13.45 ? 343  ARG A CD  1 
ATOM   2647 N  NE  . ARG A 1 343  ? 31.740 63.385  21.054  1.00 15.42 ? 343  ARG A NE  1 
ATOM   2648 C  CZ  . ARG A 1 343  ? 30.791 62.684  21.692  1.00 15.65 ? 343  ARG A CZ  1 
ATOM   2649 N  NH1 . ARG A 1 343  ? 31.118 61.633  22.437  1.00 15.14 ? 343  ARG A NH1 1 
ATOM   2650 N  NH2 . ARG A 1 343  ? 29.525 63.093  21.614  1.00 15.63 ? 343  ARG A NH2 1 
ATOM   2651 N  N   . PHE A 1 344  ? 37.254 62.081  22.231  1.00 15.03 ? 344  PHE A N   1 
ATOM   2652 C  CA  . PHE A 1 344  ? 38.346 61.603  23.083  1.00 15.97 ? 344  PHE A CA  1 
ATOM   2653 C  C   . PHE A 1 344  ? 39.461 62.634  23.207  1.00 16.18 ? 344  PHE A C   1 
ATOM   2654 O  O   . PHE A 1 344  ? 40.631 62.345  23.072  1.00 18.02 ? 344  PHE A O   1 
ATOM   2655 C  CB  . PHE A 1 344  ? 38.803 60.220  22.590  1.00 14.91 ? 344  PHE A CB  1 
ATOM   2656 C  CG  . PHE A 1 344  ? 37.772 59.184  22.789  1.00 15.24 ? 344  PHE A CG  1 
ATOM   2657 C  CD1 . PHE A 1 344  ? 37.568 58.643  24.063  1.00 17.42 ? 344  PHE A CD1 1 
ATOM   2658 C  CD2 . PHE A 1 344  ? 36.952 58.784  21.763  1.00 16.01 ? 344  PHE A CD2 1 
ATOM   2659 C  CE1 . PHE A 1 344  ? 36.536 57.702  24.278  1.00 17.66 ? 344  PHE A CE1 1 
ATOM   2660 C  CE2 . PHE A 1 344  ? 35.929 57.862  21.967  1.00 17.17 ? 344  PHE A CE2 1 
ATOM   2661 C  CZ  . PHE A 1 344  ? 35.724 57.320  23.235  1.00 18.07 ? 344  PHE A CZ  1 
ATOM   2662 N  N   . LYS A 1 345  ? 39.044 63.863  23.481  1.00 16.75 ? 345  LYS A N   1 
ATOM   2663 C  CA  . LYS A 1 345  ? 39.960 64.974  23.636  1.00 19.08 ? 345  LYS A CA  1 
ATOM   2664 C  C   . LYS A 1 345  ? 40.309 65.091  25.134  1.00 20.42 ? 345  LYS A C   1 
ATOM   2665 O  O   . LYS A 1 345  ? 41.380 64.695  25.561  1.00 25.47 ? 345  LYS A O   1 
ATOM   2666 C  CB  . LYS A 1 345  ? 39.273 66.252  23.145  1.00 19.34 ? 345  LYS A CB  1 
ATOM   2667 C  CG  . LYS A 1 345  ? 40.150 67.462  23.142  1.00 22.52 ? 345  LYS A CG  1 
ATOM   2668 C  CD  . LYS A 1 345  ? 39.338 68.669  22.720  1.00 27.05 ? 345  LYS A CD  1 
ATOM   2669 C  CE  . LYS A 1 345  ? 40.154 69.924  22.876  1.00 26.28 ? 345  LYS A CE  1 
ATOM   2670 N  NZ  . LYS A 1 345  ? 39.391 71.089  22.323  1.00 29.10 ? 345  LYS A NZ  1 
ATOM   2671 N  N   . GLN A 1 346  ? 39.345 65.539  25.920  1.00 20.98 ? 346  GLN A N   1 
ATOM   2672 C  CA  . GLN A 1 346  ? 39.560 65.737  27.342  1.00 21.52 ? 346  GLN A CA  1 
ATOM   2673 C  C   . GLN A 1 346  ? 39.867 64.477  28.145  1.00 19.65 ? 346  GLN A C   1 
ATOM   2674 O  O   . GLN A 1 346  ? 39.275 63.418  27.906  1.00 18.49 ? 346  GLN A O   1 
ATOM   2675 C  CB  . GLN A 1 346  ? 38.323 66.418  27.967  1.00 23.70 ? 346  GLN A CB  1 
ATOM   2676 C  CG  . GLN A 1 346  ? 37.902 67.814  27.420  1.00 29.47 ? 346  GLN A CG  1 
ATOM   2677 C  CD  . GLN A 1 346  ? 36.713 67.755  26.422  1.00 33.06 ? 346  GLN A CD  1 
ATOM   2678 O  OE1 . GLN A 1 346  ? 35.905 68.684  26.361  1.00 35.79 ? 346  GLN A OE1 1 
ATOM   2679 N  NE2 . GLN A 1 346  ? 36.620 66.673  25.636  1.00 26.10 ? 346  GLN A NE2 1 
ATOM   2680 N  N   . ASN A 1 347  ? 40.738 64.587  29.150  1.00 19.97 ? 347  ASN A N   1 
ATOM   2681 C  CA  . ASN A 1 347  ? 41.007 63.450  30.033  1.00 20.87 ? 347  ASN A CA  1 
ATOM   2682 C  C   . ASN A 1 347  ? 39.706 63.015  30.726  1.00 19.03 ? 347  ASN A C   1 
ATOM   2683 O  O   . ASN A 1 347  ? 39.427 61.823  30.848  1.00 19.61 ? 347  ASN A O   1 
ATOM   2684 C  CB  . ASN A 1 347  ? 42.024 63.857  31.102  1.00 23.35 ? 347  ASN A CB  1 
ATOM   2685 C  CG  . ASN A 1 347  ? 43.354 64.043  30.511  1.00 29.00 ? 347  ASN A CG  1 
ATOM   2686 O  OD1 . ASN A 1 347  ? 43.858 63.121  29.885  1.00 30.88 ? 347  ASN A OD1 1 
ATOM   2687 N  ND2 . ASN A 1 347  ? 43.945 65.242  30.658  1.00 32.54 ? 347  ASN A ND2 1 
ATOM   2688 N  N   . THR A 1 348  ? 38.894 63.994  31.128  1.00 18.03 ? 348  THR A N   1 
ATOM   2689 C  CA  . THR A 1 348  ? 37.625 63.698  31.767  1.00 19.36 ? 348  THR A CA  1 
ATOM   2690 C  C   . THR A 1 348  ? 36.698 62.930  30.827  1.00 18.15 ? 348  THR A C   1 
ATOM   2691 O  O   . THR A 1 348  ? 35.853 62.136  31.278  1.00 19.17 ? 348  THR A O   1 
ATOM   2692 C  CB  . THR A 1 348  ? 36.901 64.992  32.243  1.00 20.11 ? 348  THR A CB  1 
ATOM   2693 O  OG1 . THR A 1 348  ? 36.760 65.911  31.154  1.00 24.28 ? 348  THR A OG1 1 
ATOM   2694 C  CG2 . THR A 1 348  ? 37.711 65.674  33.382  1.00 21.97 ? 348  THR A CG2 1 
ATOM   2695 N  N   . GLU A 1 349  ? 36.845 63.160  29.504  1.00 16.22 ? 349  GLU A N   1 
ATOM   2696 C  CA  . GLU A 1 349  ? 36.008 62.451  28.535  1.00 16.41 ? 349  GLU A CA  1 
ATOM   2697 C  C   . GLU A 1 349  ? 36.470 60.995  28.416  1.00 16.04 ? 349  GLU A C   1 
ATOM   2698 O  O   . GLU A 1 349  ? 35.647 60.088  28.364  1.00 15.04 ? 349  GLU A O   1 
ATOM   2699 C  CB  . GLU A 1 349  ? 36.114 63.124  27.163  1.00 14.33 ? 349  GLU A CB  1 
ATOM   2700 C  CG  . GLU A 1 349  ? 35.338 62.361  26.097  1.00 15.56 ? 349  GLU A CG  1 
ATOM   2701 C  CD  . GLU A 1 349  ? 35.554 62.954  24.697  1.00 15.56 ? 349  GLU A CD  1 
ATOM   2702 O  OE1 . GLU A 1 349  ? 36.234 63.971  24.544  1.00 17.72 ? 349  GLU A OE1 1 
ATOM   2703 O  OE2 . GLU A 1 349  ? 34.991 62.379  23.765  1.00 16.30 ? 349  GLU A OE2 1 
ATOM   2704 N  N   . TRP A 1 350  ? 37.783 60.774  28.331  1.00 16.03 ? 350  TRP A N   1 
ATOM   2705 C  CA  . TRP A 1 350  ? 38.294 59.404  28.304  1.00 16.05 ? 350  TRP A CA  1 
ATOM   2706 C  C   . TRP A 1 350  ? 37.746 58.643  29.522  1.00 16.39 ? 350  TRP A C   1 
ATOM   2707 O  O   . TRP A 1 350  ? 37.237 57.529  29.392  1.00 17.34 ? 350  TRP A O   1 
ATOM   2708 C  CB  . TRP A 1 350  ? 39.806 59.357  28.348  1.00 15.85 ? 350  TRP A CB  1 
ATOM   2709 C  CG  . TRP A 1 350  ? 40.456 59.565  27.020  1.00 16.07 ? 350  TRP A CG  1 
ATOM   2710 C  CD1 . TRP A 1 350  ? 40.823 60.758  26.474  1.00 15.79 ? 350  TRP A CD1 1 
ATOM   2711 C  CD2 . TRP A 1 350  ? 40.742 58.555  26.049  1.00 15.30 ? 350  TRP A CD2 1 
ATOM   2712 N  NE1 . TRP A 1 350  ? 41.337 60.555  25.197  1.00 14.86 ? 350  TRP A NE1 1 
ATOM   2713 C  CE2 . TRP A 1 350  ? 41.284 59.219  24.910  1.00 15.05 ? 350  TRP A CE2 1 
ATOM   2714 C  CE3 . TRP A 1 350  ? 40.588 57.160  26.014  1.00 17.93 ? 350  TRP A CE3 1 
ATOM   2715 C  CZ2 . TRP A 1 350  ? 41.661 58.531  23.753  1.00 16.72 ? 350  TRP A CZ2 1 
ATOM   2716 C  CZ3 . TRP A 1 350  ? 40.982 56.479  24.833  1.00 18.13 ? 350  TRP A CZ3 1 
ATOM   2717 C  CH2 . TRP A 1 350  ? 41.501 57.175  23.732  1.00 18.39 ? 350  TRP A CH2 1 
ATOM   2718 N  N   . ASP A 1 351  ? 37.842 59.261  30.699  1.00 18.11 ? 351  ASP A N   1 
ATOM   2719 C  CA  . ASP A 1 351  ? 37.368 58.620  31.913  1.00 18.31 ? 351  ASP A CA  1 
ATOM   2720 C  C   . ASP A 1 351  ? 35.888 58.348  31.914  1.00 16.52 ? 351  ASP A C   1 
ATOM   2721 O  O   . ASP A 1 351  ? 35.467 57.235  32.247  1.00 16.76 ? 351  ASP A O   1 
ATOM   2722 C  CB  . ASP A 1 351  ? 37.651 59.495  33.134  1.00 20.04 ? 351  ASP A CB  1 
ATOM   2723 C  CG  . ASP A 1 351  ? 39.090 59.511  33.535  1.00 25.09 ? 351  ASP A CG  1 
ATOM   2724 O  OD1 . ASP A 1 351  ? 39.830 58.539  33.248  1.00 27.66 ? 351  ASP A OD1 1 
ATOM   2725 O  OD2 . ASP A 1 351  ? 39.489 60.496  34.204  1.00 29.04 ? 351  ASP A OD2 1 
ATOM   2726 N  N   . VAL A 1 352  ? 35.091 59.341  31.533  1.00 16.35 ? 352  VAL A N   1 
ATOM   2727 C  CA  . VAL A 1 352  ? 33.665 59.162  31.595  1.00 18.76 ? 352  VAL A CA  1 
ATOM   2728 C  C   . VAL A 1 352  ? 33.184 58.045  30.661  1.00 19.48 ? 352  VAL A C   1 
ATOM   2729 O  O   . VAL A 1 352  ? 32.293 57.272  31.003  1.00 19.68 ? 352  VAL A O   1 
ATOM   2730 C  CB  . VAL A 1 352  ? 32.902 60.514  31.358  1.00 21.03 ? 352  VAL A CB  1 
ATOM   2731 C  CG1 . VAL A 1 352  ? 32.628 60.763  29.900  1.00 20.13 ? 352  VAL A CG1 1 
ATOM   2732 C  CG2 . VAL A 1 352  ? 31.597 60.519  32.162  1.00 24.58 ? 352  VAL A CG2 1 
ATOM   2733 N  N   . GLN A 1 353  ? 33.795 57.918  29.485  1.00 16.27 ? 353  GLN A N   1 
ATOM   2734 C  CA  . GLN A 1 353  ? 33.342 56.859  28.601  1.00 15.90 ? 353  GLN A CA  1 
ATOM   2735 C  C   . GLN A 1 353  ? 33.881 55.515  29.099  1.00 16.03 ? 353  GLN A C   1 
ATOM   2736 O  O   . GLN A 1 353  ? 33.113 54.545  29.228  1.00 16.91 ? 353  GLN A O   1 
ATOM   2737 C  CB  . GLN A 1 353  ? 33.856 57.128  27.163  1.00 14.24 ? 353  GLN A CB  1 
ATOM   2738 C  CG  . GLN A 1 353  ? 33.319 58.426  26.489  1.00 14.81 ? 353  GLN A CG  1 
ATOM   2739 C  CD  . GLN A 1 353  ? 31.860 58.331  26.028  1.00 15.32 ? 353  GLN A CD  1 
ATOM   2740 O  OE1 . GLN A 1 353  ? 31.044 57.603  26.625  1.00 16.96 ? 353  GLN A OE1 1 
ATOM   2741 N  NE2 . GLN A 1 353  ? 31.503 59.067  24.989  1.00 15.13 ? 353  GLN A NE2 1 
ATOM   2742 N  N   . ARG A 1 354  ? 35.175 55.446  29.401  1.00 15.64 ? 354  ARG A N   1 
ATOM   2743 C  CA  . ARG A 1 354  ? 35.766 54.200  29.831  1.00 16.01 ? 354  ARG A CA  1 
ATOM   2744 C  C   . ARG A 1 354  ? 35.163 53.605  31.102  1.00 17.22 ? 354  ARG A C   1 
ATOM   2745 O  O   . ARG A 1 354  ? 34.837 52.431  31.119  1.00 17.20 ? 354  ARG A O   1 
ATOM   2746 C  CB  . ARG A 1 354  ? 37.265 54.332  30.063  1.00 15.24 ? 354  ARG A CB  1 
ATOM   2747 C  CG  . ARG A 1 354  ? 37.903 53.011  30.527  1.00 17.11 ? 354  ARG A CG  1 
ATOM   2748 C  CD  . ARG A 1 354  ? 39.420 53.183  30.758  1.00 18.69 ? 354  ARG A CD  1 
ATOM   2749 N  NE  . ARG A 1 354  ? 39.725 54.229  31.738  1.00 20.93 ? 354  ARG A NE  1 
ATOM   2750 C  CZ  . ARG A 1 354  ? 39.549 54.129  33.058  1.00 21.74 ? 354  ARG A CZ  1 
ATOM   2751 N  NH1 . ARG A 1 354  ? 39.067 53.023  33.604  1.00 21.07 ? 354  ARG A NH1 1 
ATOM   2752 N  NH2 . ARG A 1 354  ? 39.878 55.150  33.837  1.00 23.45 ? 354  ARG A NH2 1 
ATOM   2753 N  N   . VAL A 1 355  ? 35.047 54.412  32.157  1.00 18.08 ? 355  VAL A N   1 
ATOM   2754 C  CA  . VAL A 1 355  ? 34.554 53.883  33.424  1.00 18.81 ? 355  VAL A CA  1 
ATOM   2755 C  C   . VAL A 1 355  ? 33.142 53.399  33.333  1.00 18.86 ? 355  VAL A C   1 
ATOM   2756 O  O   . VAL A 1 355  ? 32.800 52.338  33.900  1.00 20.15 ? 355  VAL A O   1 
ATOM   2757 C  CB  . VAL A 1 355  ? 34.655 54.942  34.521  1.00 19.91 ? 355  VAL A CB  1 
ATOM   2758 C  CG1 . VAL A 1 355  ? 34.063 54.415  35.833  1.00 27.70 ? 355  VAL A CG1 1 
ATOM   2759 C  CG2 . VAL A 1 355  ? 36.140 55.309  34.745  1.00 22.23 ? 355  VAL A CG2 1 
ATOM   2760 N  N   . ASN A 1 356  ? 32.290 54.151  32.651  1.00 18.04 ? 356  ASN A N   1 
ATOM   2761 C  CA  . ASN A 1 356  ? 30.916 53.718  32.525  1.00 17.40 ? 356  ASN A CA  1 
ATOM   2762 C  C   . ASN A 1 356  ? 30.784 52.423  31.705  1.00 19.31 ? 356  ASN A C   1 
ATOM   2763 O  O   . ASN A 1 356  ? 30.061 51.488  32.106  1.00 17.34 ? 356  ASN A O   1 
ATOM   2764 C  CB  . ASN A 1 356  ? 30.045 54.859  32.042  1.00 17.83 ? 356  ASN A CB  1 
ATOM   2765 C  CG  . ASN A 1 356  ? 29.801 55.851  33.133  1.00 20.75 ? 356  ASN A CG  1 
ATOM   2766 O  OD1 . ASN A 1 356  ? 29.110 55.525  34.110  1.00 19.50 ? 356  ASN A OD1 1 
ATOM   2767 N  ND2 . ASN A 1 356  ? 30.401 57.046  33.035  1.00 18.84 ? 356  ASN A ND2 1 
ATOM   2768 N  N   . TYR A 1 357  ? 31.498 52.329  30.586  1.00 17.30 ? 357  TYR A N   1 
ATOM   2769 C  CA  . TYR A 1 357  ? 31.413 51.098  29.824  1.00 16.83 ? 357  TYR A CA  1 
ATOM   2770 C  C   . TYR A 1 357  ? 32.044 49.925  30.579  1.00 17.04 ? 357  TYR A C   1 
ATOM   2771 O  O   . TYR A 1 357  ? 31.551 48.793  30.495  1.00 17.25 ? 357  TYR A O   1 
ATOM   2772 C  CB  . TYR A 1 357  ? 32.051 51.280  28.425  1.00 15.37 ? 357  TYR A CB  1 
ATOM   2773 C  CG  . TYR A 1 357  ? 31.053 51.813  27.428  1.00 15.57 ? 357  TYR A CG  1 
ATOM   2774 C  CD1 . TYR A 1 357  ? 30.210 50.926  26.724  1.00 14.66 ? 357  TYR A CD1 1 
ATOM   2775 C  CD2 . TYR A 1 357  ? 30.879 53.191  27.235  1.00 15.29 ? 357  TYR A CD2 1 
ATOM   2776 C  CE1 . TYR A 1 357  ? 29.233 51.387  25.877  1.00 15.39 ? 357  TYR A CE1 1 
ATOM   2777 C  CE2 . TYR A 1 357  ? 29.883 53.670  26.375  1.00 15.74 ? 357  TYR A CE2 1 
ATOM   2778 C  CZ  . TYR A 1 357  ? 29.054 52.764  25.694  1.00 15.37 ? 357  TYR A CZ  1 
ATOM   2779 O  OH  . TYR A 1 357  ? 28.072 53.217  24.867  1.00 16.22 ? 357  TYR A OH  1 
ATOM   2780 N  N   . GLU A 1 358  ? 33.117 50.160  31.331  1.00 16.64 ? 358  GLU A N   1 
ATOM   2781 C  CA  . GLU A 1 358  ? 33.694 49.050  32.120  1.00 16.48 ? 358  GLU A CA  1 
ATOM   2782 C  C   . GLU A 1 358  ? 32.630 48.505  33.117  1.00 16.77 ? 358  GLU A C   1 
ATOM   2783 O  O   . GLU A 1 358  ? 32.544 47.305  33.310  1.00 17.38 ? 358  GLU A O   1 
ATOM   2784 C  CB  . GLU A 1 358  ? 34.888 49.549  32.941  1.00 17.62 ? 358  GLU A CB  1 
ATOM   2785 C  CG  . GLU A 1 358  ? 36.187 49.695  32.141  1.00 19.48 ? 358  GLU A CG  1 
ATOM   2786 C  CD  . GLU A 1 358  ? 37.396 50.091  33.005  1.00 25.53 ? 358  GLU A CD  1 
ATOM   2787 O  OE1 . GLU A 1 358  ? 37.344 49.974  34.252  1.00 29.87 ? 358  GLU A OE1 1 
ATOM   2788 O  OE2 . GLU A 1 358  ? 38.442 50.485  32.464  1.00 23.90 ? 358  GLU A OE2 1 
ATOM   2789 N  N   . ARG A 1 359  ? 31.827 49.391  33.710  1.00 17.92 ? 359  ARG A N   1 
ATOM   2790 C  CA  . ARG A 1 359  ? 30.796 48.918  34.655  1.00 18.51 ? 359  ARG A CA  1 
ATOM   2791 C  C   . ARG A 1 359  ? 29.725 48.127  33.919  1.00 17.49 ? 359  ARG A C   1 
ATOM   2792 O  O   . ARG A 1 359  ? 29.247 47.113  34.424  1.00 18.81 ? 359  ARG A O   1 
ATOM   2793 C  CB  . ARG A 1 359  ? 30.144 50.068  35.392  1.00 18.08 ? 359  ARG A CB  1 
ATOM   2794 C  CG  . ARG A 1 359  ? 31.034 50.780  36.364  1.00 23.36 ? 359  ARG A CG  1 
ATOM   2795 C  CD  . ARG A 1 359  ? 30.328 51.997  36.892  1.00 29.71 ? 359  ARG A CD  1 
ATOM   2796 N  NE  . ARG A 1 359  ? 31.237 52.843  37.651  1.00 32.24 ? 359  ARG A NE  1 
ATOM   2797 C  CZ  . ARG A 1 359  ? 31.316 54.165  37.510  1.00 35.07 ? 359  ARG A CZ  1 
ATOM   2798 N  NH1 . ARG A 1 359  ? 30.539 54.812  36.624  1.00 31.98 ? 359  ARG A NH1 1 
ATOM   2799 N  NH2 . ARG A 1 359  ? 32.172 54.840  38.274  1.00 38.19 ? 359  ARG A NH2 1 
ATOM   2800 N  N   . LEU A 1 360  ? 29.348 48.571  32.721  1.00 16.75 ? 360  LEU A N   1 
ATOM   2801 C  CA  . LEU A 1 360  ? 28.380 47.831  31.938  1.00 15.61 ? 360  LEU A CA  1 
ATOM   2802 C  C   . LEU A 1 360  ? 28.963 46.457  31.562  1.00 18.38 ? 360  LEU A C   1 
ATOM   2803 O  O   . LEU A 1 360  ? 28.273 45.431  31.704  1.00 18.78 ? 360  LEU A O   1 
ATOM   2804 C  CB  . LEU A 1 360  ? 27.996 48.643  30.683  1.00 17.96 ? 360  LEU A CB  1 
ATOM   2805 C  CG  . LEU A 1 360  ? 27.140 49.888  31.006  1.00 16.41 ? 360  LEU A CG  1 
ATOM   2806 C  CD1 . LEU A 1 360  ? 27.176 50.890  29.861  1.00 20.05 ? 360  LEU A CD1 1 
ATOM   2807 C  CD2 . LEU A 1 360  ? 25.670 49.499  31.232  1.00 18.65 ? 360  LEU A CD2 1 
ATOM   2808 N  N   . PHE A 1 361  ? 30.207 46.404  31.083  1.00 17.22 ? 361  PHE A N   1 
ATOM   2809 C  CA  . PHE A 1 361  ? 30.793 45.126  30.699  1.00 16.55 ? 361  PHE A CA  1 
ATOM   2810 C  C   . PHE A 1 361  ? 30.876 44.158  31.881  1.00 18.52 ? 361  PHE A C   1 
ATOM   2811 O  O   . PHE A 1 361  ? 30.576 42.977  31.723  1.00 19.29 ? 361  PHE A O   1 
ATOM   2812 C  CB  . PHE A 1 361  ? 32.225 45.283  30.132  1.00 16.02 ? 361  PHE A CB  1 
ATOM   2813 C  CG  . PHE A 1 361  ? 32.309 46.103  28.869  1.00 17.53 ? 361  PHE A CG  1 
ATOM   2814 C  CD1 . PHE A 1 361  ? 31.216 46.249  28.016  1.00 17.12 ? 361  PHE A CD1 1 
ATOM   2815 C  CD2 . PHE A 1 361  ? 33.514 46.734  28.570  1.00 16.41 ? 361  PHE A CD2 1 
ATOM   2816 C  CE1 . PHE A 1 361  ? 31.330 47.024  26.862  1.00 16.75 ? 361  PHE A CE1 1 
ATOM   2817 C  CE2 . PHE A 1 361  ? 33.641 47.528  27.403  1.00 18.02 ? 361  PHE A CE2 1 
ATOM   2818 C  CZ  . PHE A 1 361  ? 32.550 47.658  26.567  1.00 17.59 ? 361  PHE A CZ  1 
ATOM   2819 N  N   . GLU A 1 362  ? 31.319 44.643  33.049  1.00 18.57 ? 362  GLU A N   1 
ATOM   2820 C  CA  . GLU A 1 362  ? 31.431 43.722  34.171  1.00 18.96 ? 362  GLU A CA  1 
ATOM   2821 C  C   . GLU A 1 362  ? 30.054 43.118  34.512  1.00 19.86 ? 362  GLU A C   1 
ATOM   2822 O  O   . GLU A 1 362  ? 29.942 41.918  34.729  1.00 18.16 ? 362  GLU A O   1 
ATOM   2823 C  CB  . GLU A 1 362  ? 32.022 44.412  35.411  1.00 21.83 ? 362  GLU A CB  1 
ATOM   2824 C  CG  . GLU A 1 362  ? 32.157 43.366  36.529  1.00 24.13 ? 362  GLU A CG  1 
ATOM   2825 C  CD  . GLU A 1 362  ? 32.589 43.923  37.865  1.00 31.76 ? 362  GLU A CD  1 
ATOM   2826 O  OE1 . GLU A 1 362  ? 32.958 45.114  37.924  1.00 34.22 ? 362  GLU A OE1 1 
ATOM   2827 O  OE2 . GLU A 1 362  ? 32.549 43.143  38.847  1.00 32.34 ? 362  GLU A OE2 1 
ATOM   2828 N  N   . HIS A 1 363  ? 29.017 43.935  34.519  1.00 17.48 ? 363  HIS A N   1 
ATOM   2829 C  CA  . HIS A 1 363  ? 27.702 43.413  34.818  1.00 20.87 ? 363  HIS A CA  1 
ATOM   2830 C  C   . HIS A 1 363  ? 27.168 42.485  33.733  1.00 18.85 ? 363  HIS A C   1 
ATOM   2831 O  O   . HIS A 1 363  ? 26.758 41.365  34.007  1.00 21.04 ? 363  HIS A O   1 
ATOM   2832 C  CB  . HIS A 1 363  ? 26.717 44.538  35.020  1.00 21.44 ? 363  HIS A CB  1 
ATOM   2833 C  CG  . HIS A 1 363  ? 25.334 44.067  35.351  1.00 21.85 ? 363  HIS A CG  1 
ATOM   2834 N  ND1 . HIS A 1 363  ? 24.994 43.594  36.609  1.00 26.50 ? 363  HIS A ND1 1 
ATOM   2835 C  CD2 . HIS A 1 363  ? 24.222 43.964  34.593  1.00 23.90 ? 363  HIS A CD2 1 
ATOM   2836 C  CE1 . HIS A 1 363  ? 23.725 43.221  36.595  1.00 23.50 ? 363  HIS A CE1 1 
ATOM   2837 N  NE2 . HIS A 1 363  ? 23.231 43.435  35.391  1.00 25.35 ? 363  HIS A NE2 1 
ATOM   2838 N  N   . ILE A 1 364  ? 27.197 42.932  32.485  1.00 18.65 ? 364  ILE A N   1 
ATOM   2839 C  CA  . ILE A 1 364  ? 26.651 42.139  31.411  1.00 18.88 ? 364  ILE A CA  1 
ATOM   2840 C  C   . ILE A 1 364  ? 27.345 40.808  31.245  1.00 19.03 ? 364  ILE A C   1 
ATOM   2841 O  O   . ILE A 1 364  ? 26.686 39.745  31.093  1.00 19.91 ? 364  ILE A O   1 
ATOM   2842 C  CB  . ILE A 1 364  ? 26.738 42.941  30.072  1.00 18.69 ? 364  ILE A CB  1 
ATOM   2843 C  CG1 . ILE A 1 364  ? 25.743 44.108  30.078  1.00 19.06 ? 364  ILE A CG1 1 
ATOM   2844 C  CG2 . ILE A 1 364  ? 26.454 41.989  28.914  1.00 18.27 ? 364  ILE A CG2 1 
ATOM   2845 C  CD1 . ILE A 1 364  ? 26.034 45.205  29.053  1.00 20.41 ? 364  ILE A CD1 1 
ATOM   2846 N  N   . ASN A 1 365  ? 28.654 40.817  31.310  1.00 17.68 ? 365  ASN A N   1 
ATOM   2847 C  CA  . ASN A 1 365  ? 29.424 39.593  31.080  1.00 16.82 ? 365  ASN A CA  1 
ATOM   2848 C  C   . ASN A 1 365  ? 29.298 38.579  32.214  1.00 21.90 ? 365  ASN A C   1 
ATOM   2849 O  O   . ASN A 1 365  ? 29.631 37.407  32.042  1.00 22.40 ? 365  ASN A O   1 
ATOM   2850 C  CB  . ASN A 1 365  ? 30.898 39.913  30.859  1.00 18.27 ? 365  ASN A CB  1 
ATOM   2851 C  CG  . ASN A 1 365  ? 31.122 40.737  29.612  1.00 16.94 ? 365  ASN A CG  1 
ATOM   2852 O  OD1 . ASN A 1 365  ? 30.202 40.929  28.802  1.00 19.04 ? 365  ASN A OD1 1 
ATOM   2853 N  ND2 . ASN A 1 365  ? 32.349 41.239  29.464  1.00 16.54 ? 365  ASN A ND2 1 
ATOM   2854 N  N   . SER A 1 366  ? 28.821 39.057  33.359  1.00 24.31 ? 366  SER A N   1 
ATOM   2855 C  CA  . SER A 1 366  ? 28.681 38.181  34.533  1.00 27.37 ? 366  SER A CA  1 
ATOM   2856 C  C   . SER A 1 366  ? 27.258 37.681  34.719  1.00 29.01 ? 366  SER A C   1 
ATOM   2857 O  O   . SER A 1 366  ? 27.030 36.803  35.548  1.00 30.82 ? 366  SER A O   1 
ATOM   2858 C  CB  . SER A 1 366  ? 29.140 38.913  35.814  1.00 29.69 ? 366  SER A CB  1 
ATOM   2859 O  OG  . SER A 1 366  ? 28.205 39.920  36.159  1.00 31.72 ? 366  SER A OG  1 
ATOM   2860 N  N   . GLN A 1 367  ? 26.314 38.219  33.962  1.00 29.52 ? 367  GLN A N   1 
ATOM   2861 C  CA  . GLN A 1 367  ? 24.904 37.834  34.019  1.00 29.91 ? 367  GLN A CA  1 
ATOM   2862 C  C   . GLN A 1 367  ? 24.631 36.844  32.899  1.00 29.14 ? 367  GLN A C   1 
ATOM   2863 O  O   . GLN A 1 367  ? 24.279 37.233  31.774  1.00 27.93 ? 367  GLN A O   1 
ATOM   2864 C  CB  . GLN A 1 367  ? 24.005 39.054  33.807  1.00 32.12 ? 367  GLN A CB  1 
ATOM   2865 C  CG  . GLN A 1 367  ? 24.052 40.026  34.955  1.00 37.26 ? 367  GLN A CG  1 
ATOM   2866 C  CD  . GLN A 1 367  ? 23.573 39.375  36.225  1.00 40.21 ? 367  GLN A CD  1 
ATOM   2867 O  OE1 . GLN A 1 367  ? 22.411 38.961  36.312  1.00 40.74 ? 367  GLN A OE1 1 
ATOM   2868 N  NE2 . GLN A 1 367  ? 24.461 39.268  37.222  1.00 40.91 ? 367  GLN A NE2 1 
ATOM   2869 N  N   . ALA A 1 368  ? 24.738 35.557  33.215  1.00 28.76 ? 368  ALA A N   1 
ATOM   2870 C  CA  . ALA A 1 368  ? 24.534 34.531  32.198  1.00 26.94 ? 368  ALA A CA  1 
ATOM   2871 C  C   . ALA A 1 368  ? 23.287 34.682  31.338  1.00 26.62 ? 368  ALA A C   1 
ATOM   2872 O  O   . ALA A 1 368  ? 23.306 34.352  30.140  1.00 26.57 ? 368  ALA A O   1 
ATOM   2873 C  CB  . ALA A 1 368  ? 24.521 33.166  32.856  1.00 27.96 ? 368  ALA A CB  1 
ATOM   2874 N  N   . HIS A 1 369  ? 22.215 35.189  31.936  1.00 26.09 ? 369  HIS A N   1 
ATOM   2875 C  CA  . HIS A 1 369  ? 20.956 35.371  31.238  1.00 26.00 ? 369  HIS A CA  1 
ATOM   2876 C  C   . HIS A 1 369  ? 21.039 36.238  29.976  1.00 25.16 ? 369  HIS A C   1 
ATOM   2877 O  O   . HIS A 1 369  ? 20.176 36.142  29.105  1.00 26.11 ? 369  HIS A O   1 
ATOM   2878 C  CB  A HIS A 1 369  ? 19.898 35.925  32.221  0.50 27.64 ? 369  HIS A CB  1 
ATOM   2879 C  CB  B HIS A 1 369  ? 19.803 35.767  32.076  0.50 28.13 ? 369  HIS A CB  1 
ATOM   2880 C  CG  A HIS A 1 369  ? 20.204 37.294  32.755  0.50 26.87 ? 369  HIS A CG  1 
ATOM   2881 C  CG  B HIS A 1 369  ? 19.816 37.232  32.388  0.50 28.67 ? 369  HIS A CG  1 
ATOM   2882 N  ND1 A HIS A 1 369  ? 19.850 38.449  32.087  0.50 29.24 ? 369  HIS A ND1 1 
ATOM   2883 N  ND1 B HIS A 1 369  ? 19.307 38.182  31.527  0.50 30.44 ? 369  HIS A ND1 1 
ATOM   2884 C  CD2 A HIS A 1 369  ? 20.836 37.692  33.884  0.50 28.12 ? 369  HIS A CD2 1 
ATOM   2885 C  CD2 B HIS A 1 369  ? 20.307 37.911  33.450  0.50 29.69 ? 369  HIS A CD2 1 
ATOM   2886 C  CE1 A HIS A 1 369  ? 20.249 39.498  32.782  0.50 28.69 ? 369  HIS A CE1 1 
ATOM   2887 C  CE1 B HIS A 1 369  ? 19.488 39.385  32.046  0.50 28.01 ? 369  HIS A CE1 1 
ATOM   2888 N  NE2 A HIS A 1 369  ? 20.851 39.068  33.877  0.50 27.40 ? 369  HIS A NE2 1 
ATOM   2889 N  NE2 B HIS A 1 369  ? 20.093 39.249  33.212  0.50 29.87 ? 369  HIS A NE2 1 
ATOM   2890 N  N   . PHE A 1 370  ? 22.068 37.077  29.868  1.00 25.52 ? 370  PHE A N   1 
ATOM   2891 C  CA  . PHE A 1 370  ? 22.203 37.939  28.671  1.00 23.71 ? 370  PHE A CA  1 
ATOM   2892 C  C   . PHE A 1 370  ? 22.866 37.167  27.535  1.00 21.56 ? 370  PHE A C   1 
ATOM   2893 O  O   . PHE A 1 370  ? 22.649 37.464  26.370  1.00 20.80 ? 370  PHE A O   1 
ATOM   2894 C  CB  . PHE A 1 370  ? 23.090 39.172  28.930  1.00 24.82 ? 370  PHE A CB  1 
ATOM   2895 C  CG  . PHE A 1 370  ? 22.440 40.255  29.731  1.00 24.12 ? 370  PHE A CG  1 
ATOM   2896 C  CD1 . PHE A 1 370  ? 21.247 40.834  29.309  1.00 25.48 ? 370  PHE A CD1 1 
ATOM   2897 C  CD2 . PHE A 1 370  ? 23.069 40.740  30.853  1.00 25.61 ? 370  PHE A CD2 1 
ATOM   2898 C  CE1 . PHE A 1 370  ? 20.691 41.925  30.036  1.00 27.05 ? 370  PHE A CE1 1 
ATOM   2899 C  CE2 . PHE A 1 370  ? 22.527 41.814  31.572  1.00 26.07 ? 370  PHE A CE2 1 
ATOM   2900 C  CZ  . PHE A 1 370  ? 21.356 42.393  31.164  1.00 25.56 ? 370  PHE A CZ  1 
ATOM   2901 N  N   . ASN A 1 371  ? 23.691 36.195  27.900  1.00 19.53 ? 371  ASN A N   1 
ATOM   2902 C  CA  . ASN A 1 371  ? 24.452 35.402  26.945  1.00 19.04 ? 371  ASN A CA  1 
ATOM   2903 C  C   . ASN A 1 371  ? 25.233 36.301  26.004  1.00 17.53 ? 371  ASN A C   1 
ATOM   2904 O  O   . ASN A 1 371  ? 25.242 36.115  24.793  1.00 19.73 ? 371  ASN A O   1 
ATOM   2905 C  CB  . ASN A 1 371  ? 23.528 34.451  26.173  1.00 18.93 ? 371  ASN A CB  1 
ATOM   2906 C  CG  . ASN A 1 371  ? 22.887 33.414  27.093  1.00 20.21 ? 371  ASN A CG  1 
ATOM   2907 O  OD1 . ASN A 1 371  ? 23.589 32.588  27.703  1.00 22.81 ? 371  ASN A OD1 1 
ATOM   2908 N  ND2 . ASN A 1 371  ? 21.582 33.491  27.221  1.00 23.72 ? 371  ASN A ND2 1 
ATOM   2909 N  N   . VAL A 1 372  ? 25.923 37.262  26.610  1.00 16.83 ? 372  VAL A N   1 
ATOM   2910 C  CA  . VAL A 1 372  ? 26.749 38.232  25.887  1.00 17.56 ? 372  VAL A CA  1 
ATOM   2911 C  C   . VAL A 1 372  ? 28.129 38.311  26.503  1.00 18.73 ? 372  VAL A C   1 
ATOM   2912 O  O   . VAL A 1 372  ? 28.261 38.183  27.732  1.00 19.26 ? 372  VAL A O   1 
ATOM   2913 C  CB  . VAL A 1 372  ? 26.100 39.643  25.988  1.00 17.16 ? 372  VAL A CB  1 
ATOM   2914 C  CG1 . VAL A 1 372  ? 27.092 40.745  25.411  1.00 16.02 ? 372  VAL A CG1 1 
ATOM   2915 C  CG2 . VAL A 1 372  ? 24.761 39.674  25.197  1.00 18.10 ? 372  VAL A CG2 1 
ATOM   2916 N  N   . GLN A 1 373  ? 29.175 38.479  25.672  1.00 16.92 ? 373  GLN A N   1 
ATOM   2917 C  CA  . GLN A 1 373  ? 30.540 38.727  26.150  1.00 17.29 ? 373  GLN A CA  1 
ATOM   2918 C  C   . GLN A 1 373  ? 30.916 40.015  25.398  1.00 16.21 ? 373  GLN A C   1 
ATOM   2919 O  O   . GLN A 1 373  ? 31.090 39.996  24.156  1.00 17.18 ? 373  GLN A O   1 
ATOM   2920 C  CB  . GLN A 1 373  ? 31.508 37.602  25.780  1.00 17.06 ? 373  GLN A CB  1 
ATOM   2921 C  CG  . GLN A 1 373  ? 32.993 37.936  26.083  1.00 21.09 ? 373  GLN A CG  1 
ATOM   2922 C  CD  . GLN A 1 373  ? 33.245 38.274  27.552  1.00 24.85 ? 373  GLN A CD  1 
ATOM   2923 O  OE1 . GLN A 1 373  ? 32.537 37.786  28.432  1.00 25.26 ? 373  GLN A OE1 1 
ATOM   2924 N  NE2 . GLN A 1 373  ? 34.255 39.100  27.817  1.00 24.30 ? 373  GLN A NE2 1 
ATOM   2925 N  N   . ALA A 1 374  ? 30.994 41.132  26.109  1.00 15.09 ? 374  ALA A N   1 
ATOM   2926 C  CA  . ALA A 1 374  ? 31.282 42.430  25.514  1.00 15.90 ? 374  ALA A CA  1 
ATOM   2927 C  C   . ALA A 1 374  ? 32.589 43.011  25.993  1.00 15.94 ? 374  ALA A C   1 
ATOM   2928 O  O   . ALA A 1 374  ? 32.950 42.865  27.168  1.00 16.33 ? 374  ALA A O   1 
ATOM   2929 C  CB  . ALA A 1 374  ? 30.147 43.384  25.840  1.00 14.17 ? 374  ALA A CB  1 
ATOM   2930 N  N   . GLN A 1 375  ? 33.303 43.711  25.111  1.00 14.97 ? 375  GLN A N   1 
ATOM   2931 C  CA  . GLN A 1 375  ? 34.586 44.292  25.480  1.00 15.18 ? 375  GLN A CA  1 
ATOM   2932 C  C   . GLN A 1 375  ? 34.980 45.382  24.514  1.00 15.28 ? 375  GLN A C   1 
ATOM   2933 O  O   . GLN A 1 375  ? 34.434 45.466  23.426  1.00 16.89 ? 375  GLN A O   1 
ATOM   2934 C  CB  . GLN A 1 375  ? 35.688 43.227  25.404  1.00 15.66 ? 375  GLN A CB  1 
ATOM   2935 C  CG  . GLN A 1 375  ? 35.681 42.466  24.044  1.00 18.92 ? 375  GLN A CG  1 
ATOM   2936 C  CD  . GLN A 1 375  ? 34.944 41.126  24.116  1.00 25.08 ? 375  GLN A CD  1 
ATOM   2937 O  OE1 . GLN A 1 375  ? 35.323 40.248  24.918  1.00 26.30 ? 375  GLN A OE1 1 
ATOM   2938 N  NE2 . GLN A 1 375  ? 33.889 40.951  23.284  1.00 22.53 ? 375  GLN A NE2 1 
ATOM   2939 N  N   . PHE A 1 376  ? 35.932 46.212  24.931  1.00 14.36 ? 376  PHE A N   1 
ATOM   2940 C  CA  . PHE A 1 376  ? 36.498 47.184  23.980  1.00 14.59 ? 376  PHE A CA  1 
ATOM   2941 C  C   . PHE A 1 376  ? 37.291 46.339  22.978  1.00 15.28 ? 376  PHE A C   1 
ATOM   2942 O  O   . PHE A 1 376  ? 37.913 45.336  23.323  1.00 16.44 ? 376  PHE A O   1 
ATOM   2943 C  CB  . PHE A 1 376  ? 37.469 48.144  24.695  1.00 12.98 ? 376  PHE A CB  1 
ATOM   2944 C  CG  . PHE A 1 376  ? 36.796 49.064  25.638  1.00 13.63 ? 376  PHE A CG  1 
ATOM   2945 C  CD1 . PHE A 1 376  ? 35.773 49.913  25.192  1.00 14.03 ? 376  PHE A CD1 1 
ATOM   2946 C  CD2 . PHE A 1 376  ? 37.162 49.090  27.007  1.00 15.68 ? 376  PHE A CD2 1 
ATOM   2947 C  CE1 . PHE A 1 376  ? 35.125 50.766  26.106  1.00 17.31 ? 376  PHE A CE1 1 
ATOM   2948 C  CE2 . PHE A 1 376  ? 36.505 49.947  27.891  1.00 18.20 ? 376  PHE A CE2 1 
ATOM   2949 C  CZ  . PHE A 1 376  ? 35.511 50.766  27.461  1.00 18.76 ? 376  PHE A CZ  1 
ATOM   2950 N  N   . GLY A 1 377  ? 37.288 46.778  21.721  1.00 14.91 ? 377  GLY A N   1 
ATOM   2951 C  CA  . GLY A 1 377  ? 38.043 46.056  20.723  1.00 15.03 ? 377  GLY A CA  1 
ATOM   2952 C  C   . GLY A 1 377  ? 38.474 47.007  19.617  1.00 13.38 ? 377  GLY A C   1 
ATOM   2953 O  O   . GLY A 1 377  ? 38.164 48.180  19.622  1.00 15.18 ? 377  GLY A O   1 
ATOM   2954 N  N   . THR A 1 378  ? 39.217 46.447  18.662  1.00 14.70 ? 378  THR A N   1 
ATOM   2955 C  CA  . THR A 1 378  ? 39.649 47.203  17.506  1.00 15.98 ? 378  THR A CA  1 
ATOM   2956 C  C   . THR A 1 378  ? 38.890 46.664  16.298  1.00 13.74 ? 378  THR A C   1 
ATOM   2957 O  O   . THR A 1 378  ? 38.164 45.650  16.357  1.00 14.64 ? 378  THR A O   1 
ATOM   2958 C  CB  . THR A 1 378  ? 41.132 47.068  17.236  1.00 16.09 ? 378  THR A CB  1 
ATOM   2959 O  OG1 . THR A 1 378  ? 41.435 45.720  16.858  1.00 16.22 ? 378  THR A OG1 1 
ATOM   2960 C  CG2 . THR A 1 378  ? 41.944 47.415  18.492  1.00 17.82 ? 378  THR A CG2 1 
ATOM   2961 N  N   . LEU A 1 379  ? 39.053 47.363  15.175  1.00 13.73 ? 379  LEU A N   1 
ATOM   2962 C  CA  . LEU A 1 379  ? 38.357 46.944  13.943  1.00 13.32 ? 379  LEU A CA  1 
ATOM   2963 C  C   . LEU A 1 379  ? 38.850 45.594  13.443  1.00 14.18 ? 379  LEU A C   1 
ATOM   2964 O  O   . LEU A 1 379  ? 38.081 44.724  13.055  1.00 13.79 ? 379  LEU A O   1 
ATOM   2965 C  CB  . LEU A 1 379  ? 38.556 48.051  12.896  1.00 14.40 ? 379  LEU A CB  1 
ATOM   2966 C  CG  . LEU A 1 379  ? 37.812 47.825  11.565  1.00 13.46 ? 379  LEU A CG  1 
ATOM   2967 C  CD1 . LEU A 1 379  ? 36.315 47.779  11.824  1.00 15.16 ? 379  LEU A CD1 1 
ATOM   2968 C  CD2 . LEU A 1 379  ? 38.140 48.943  10.594  1.00 14.99 ? 379  LEU A CD2 1 
ATOM   2969 N  N   . GLN A 1 380  ? 40.167 45.402  13.469  1.00 13.05 ? 380  GLN A N   1 
ATOM   2970 C  CA  . GLN A 1 380  ? 40.729 44.121  13.013  1.00 13.82 ? 380  GLN A CA  1 
ATOM   2971 C  C   . GLN A 1 380  ? 40.224 42.967  13.892  1.00 14.73 ? 380  GLN A C   1 
ATOM   2972 O  O   . GLN A 1 380  ? 39.954 41.877  13.401  1.00 15.84 ? 380  GLN A O   1 
ATOM   2973 C  CB  . GLN A 1 380  ? 42.250 44.162  13.003  1.00 16.54 ? 380  GLN A CB  1 
ATOM   2974 C  CG  . GLN A 1 380  ? 42.868 42.875  12.502  1.00 17.76 ? 380  GLN A CG  1 
ATOM   2975 C  CD  . GLN A 1 380  ? 42.577 42.678  11.049  1.00 20.51 ? 380  GLN A CD  1 
ATOM   2976 O  OE1 . GLN A 1 380  ? 42.620 43.638  10.273  1.00 21.14 ? 380  GLN A OE1 1 
ATOM   2977 N  NE2 . GLN A 1 380  ? 42.270 41.428  10.658  1.00 24.60 ? 380  GLN A NE2 1 
ATOM   2978 N  N   . GLU A 1 381  ? 40.097 43.222  15.190  1.00 15.18 ? 381  GLU A N   1 
ATOM   2979 C  CA  . GLU A 1 381  ? 39.598 42.184  16.080  1.00 15.69 ? 381  GLU A CA  1 
ATOM   2980 C  C   . GLU A 1 381  ? 38.188 41.770  15.677  1.00 13.87 ? 381  GLU A C   1 
ATOM   2981 O  O   . GLU A 1 381  ? 37.855 40.592  15.710  1.00 16.05 ? 381  GLU A O   1 
ATOM   2982 C  CB  . GLU A 1 381  ? 39.521 42.700  17.508  1.00 15.87 ? 381  GLU A CB  1 
ATOM   2983 C  CG  . GLU A 1 381  ? 40.809 42.655  18.307  1.00 22.12 ? 381  GLU A CG  1 
ATOM   2984 C  CD  . GLU A 1 381  ? 40.470 42.995  19.757  1.00 26.33 ? 381  GLU A CD  1 
ATOM   2985 O  OE1 . GLU A 1 381  ? 40.386 44.173  20.045  1.00 25.13 ? 381  GLU A OE1 1 
ATOM   2986 O  OE2 . GLU A 1 381  ? 40.240 42.082  20.612  1.00 31.55 ? 381  GLU A OE2 1 
ATOM   2987 N  N   . TYR A 1 382  ? 37.332 42.749  15.363  1.00 13.24 ? 382  TYR A N   1 
ATOM   2988 C  CA  . TYR A 1 382  ? 35.993 42.450  14.900  1.00 13.06 ? 382  TYR A CA  1 
ATOM   2989 C  C   . TYR A 1 382  ? 36.034 41.548  13.664  1.00 14.09 ? 382  TYR A C   1 
ATOM   2990 O  O   . TYR A 1 382  ? 35.388 40.510  13.591  1.00 13.81 ? 382  TYR A O   1 
ATOM   2991 C  CB  . TYR A 1 382  ? 35.226 43.738  14.531  1.00 14.38 ? 382  TYR A CB  1 
ATOM   2992 C  CG  . TYR A 1 382  ? 33.924 43.440  13.848  1.00 11.82 ? 382  TYR A CG  1 
ATOM   2993 C  CD1 . TYR A 1 382  ? 32.854 42.859  14.545  1.00 14.60 ? 382  TYR A CD1 1 
ATOM   2994 C  CD2 . TYR A 1 382  ? 33.762 43.680  12.481  1.00 13.42 ? 382  TYR A CD2 1 
ATOM   2995 C  CE1 . TYR A 1 382  ? 31.665 42.530  13.880  1.00 14.40 ? 382  TYR A CE1 1 
ATOM   2996 C  CE2 . TYR A 1 382  ? 32.589 43.346  11.839  1.00 14.22 ? 382  TYR A CE2 1 
ATOM   2997 C  CZ  . TYR A 1 382  ? 31.545 42.771  12.547  1.00 14.80 ? 382  TYR A CZ  1 
ATOM   2998 O  OH  . TYR A 1 382  ? 30.354 42.419  11.936  1.00 14.22 ? 382  TYR A OH  1 
ATOM   2999 N  N   . PHE A 1 383  ? 36.777 41.984  12.645  1.00 12.90 ? 383  PHE A N   1 
ATOM   3000 C  CA  . PHE A 1 383  ? 36.826 41.187  11.420  1.00 12.98 ? 383  PHE A CA  1 
ATOM   3001 C  C   . PHE A 1 383  ? 37.409 39.804  11.627  1.00 12.43 ? 383  PHE A C   1 
ATOM   3002 O  O   . PHE A 1 383  ? 36.898 38.853  11.036  1.00 14.02 ? 383  PHE A O   1 
ATOM   3003 C  CB  . PHE A 1 383  ? 37.611 41.951  10.339  1.00 12.42 ? 383  PHE A CB  1 
ATOM   3004 C  CG  . PHE A 1 383  ? 36.827 43.086  9.709   1.00 12.60 ? 383  PHE A CG  1 
ATOM   3005 C  CD1 . PHE A 1 383  ? 35.606 42.863  9.069   1.00 14.45 ? 383  PHE A CD1 1 
ATOM   3006 C  CD2 . PHE A 1 383  ? 37.352 44.387  9.745   1.00 12.51 ? 383  PHE A CD2 1 
ATOM   3007 C  CE1 . PHE A 1 383  ? 34.895 43.934  8.450   1.00 15.34 ? 383  PHE A CE1 1 
ATOM   3008 C  CE2 . PHE A 1 383  ? 36.668 45.456  9.153   1.00 13.60 ? 383  PHE A CE2 1 
ATOM   3009 C  CZ  . PHE A 1 383  ? 35.442 45.237  8.498   1.00 14.05 ? 383  PHE A CZ  1 
ATOM   3010 N  N   . ASP A 1 384  ? 38.449 39.693  12.460  1.00 14.24 ? 384  ASP A N   1 
ATOM   3011 C  CA  . ASP A 1 384  ? 39.016 38.371  12.719  1.00 15.53 ? 384  ASP A CA  1 
ATOM   3012 C  C   . ASP A 1 384  ? 37.958 37.441  13.332  1.00 13.24 ? 384  ASP A C   1 
ATOM   3013 O  O   . ASP A 1 384  ? 37.851 36.263  12.956  1.00 16.72 ? 384  ASP A O   1 
ATOM   3014 C  CB  . ASP A 1 384  ? 40.204 38.462  13.682  1.00 15.95 ? 384  ASP A CB  1 
ATOM   3015 C  CG  . ASP A 1 384  ? 41.425 39.102  13.054  1.00 19.54 ? 384  ASP A CG  1 
ATOM   3016 O  OD1 . ASP A 1 384  ? 41.548 39.184  11.804  1.00 21.10 ? 384  ASP A OD1 1 
ATOM   3017 O  OD2 . ASP A 1 384  ? 42.276 39.516  13.867  1.00 22.79 ? 384  ASP A OD2 1 
ATOM   3018 N  N   . ALA A 1 385  ? 37.152 37.960  14.244  1.00 13.27 ? 385  ALA A N   1 
ATOM   3019 C  CA  . ALA A 1 385  ? 36.151 37.136  14.878  1.00 15.05 ? 385  ALA A CA  1 
ATOM   3020 C  C   . ALA A 1 385  ? 35.036 36.800  13.887  1.00 17.01 ? 385  ALA A C   1 
ATOM   3021 O  O   . ALA A 1 385  ? 34.522 35.688  13.885  1.00 17.57 ? 385  ALA A O   1 
ATOM   3022 C  CB  . ALA A 1 385  ? 35.624 37.873  16.127  1.00 14.81 ? 385  ALA A CB  1 
ATOM   3023 N  N   . VAL A 1 386  ? 34.653 37.750  13.026  1.00 14.21 ? 386  VAL A N   1 
ATOM   3024 C  CA  . VAL A 1 386  ? 33.639 37.436  12.031  1.00 13.92 ? 386  VAL A CA  1 
ATOM   3025 C  C   . VAL A 1 386  ? 34.107 36.286  11.121  1.00 15.81 ? 386  VAL A C   1 
ATOM   3026 O  O   . VAL A 1 386  ? 33.337 35.370  10.814  1.00 16.25 ? 386  VAL A O   1 
ATOM   3027 C  CB  . VAL A 1 386  ? 33.359 38.685  11.183  1.00 13.20 ? 386  VAL A CB  1 
ATOM   3028 C  CG1 . VAL A 1 386  ? 32.512 38.320  9.939   1.00 16.22 ? 386  VAL A CG1 1 
ATOM   3029 C  CG2 . VAL A 1 386  ? 32.604 39.687  12.007  1.00 16.24 ? 386  VAL A CG2 1 
ATOM   3030 N  N   . HIS A 1 387  ? 35.354 36.352  10.673  1.00 15.40 ? 387  HIS A N   1 
ATOM   3031 C  CA  . HIS A 1 387  ? 35.852 35.295  9.796   1.00 16.50 ? 387  HIS A CA  1 
ATOM   3032 C  C   . HIS A 1 387  ? 36.074 33.972  10.488  1.00 18.53 ? 387  HIS A C   1 
ATOM   3033 O  O   . HIS A 1 387  ? 35.977 32.930  9.836   1.00 18.08 ? 387  HIS A O   1 
ATOM   3034 C  CB  . HIS A 1 387  ? 37.098 35.772  9.033   1.00 17.68 ? 387  HIS A CB  1 
ATOM   3035 C  CG  . HIS A 1 387  ? 36.805 36.882  8.066   1.00 16.00 ? 387  HIS A CG  1 
ATOM   3036 N  ND1 . HIS A 1 387  ? 35.927 36.729  7.014   1.00 20.78 ? 387  HIS A ND1 1 
ATOM   3037 C  CD2 . HIS A 1 387  ? 37.209 38.173  8.039   1.00 18.76 ? 387  HIS A CD2 1 
ATOM   3038 C  CE1 . HIS A 1 387  ? 35.808 37.884  6.376   1.00 21.70 ? 387  HIS A CE1 1 
ATOM   3039 N  NE2 . HIS A 1 387  ? 36.573 38.775  6.981   1.00 19.46 ? 387  HIS A NE2 1 
ATOM   3040 N  N   . GLN A 1 388  ? 36.316 34.019  11.797  1.00 17.92 ? 388  GLN A N   1 
ATOM   3041 C  CA  . GLN A 1 388  ? 36.430 32.767  12.561  1.00 19.70 ? 388  GLN A CA  1 
ATOM   3042 C  C   . GLN A 1 388  ? 35.033 32.131  12.575  1.00 20.80 ? 388  GLN A C   1 
ATOM   3043 O  O   . GLN A 1 388  ? 34.904 30.920  12.446  1.00 21.50 ? 388  GLN A O   1 
ATOM   3044 C  CB  . GLN A 1 388  ? 36.930 33.083  13.959  1.00 21.60 ? 388  GLN A CB  1 
ATOM   3045 C  CG  . GLN A 1 388  ? 38.430 33.353  13.963  1.00 28.07 ? 388  GLN A CG  1 
ATOM   3046 C  CD  . GLN A 1 388  ? 38.933 34.099  15.221  1.00 35.23 ? 388  GLN A CD  1 
ATOM   3047 O  OE1 . GLN A 1 388  ? 40.118 34.512  15.295  1.00 38.94 ? 388  GLN A OE1 1 
ATOM   3048 N  NE2 . GLN A 1 388  ? 38.046 34.278  16.207  1.00 36.48 ? 388  GLN A NE2 1 
ATOM   3049 N  N   . ALA A 1 389  ? 33.986 32.944  12.693  1.00 19.38 ? 389  ALA A N   1 
ATOM   3050 C  CA  . ALA A 1 389  ? 32.583 32.464  12.693  1.00 22.43 ? 389  ALA A CA  1 
ATOM   3051 C  C   . ALA A 1 389  ? 32.239 31.862  11.332  1.00 23.59 ? 389  ALA A C   1 
ATOM   3052 O  O   . ALA A 1 389  ? 31.600 30.800  11.235  1.00 24.62 ? 389  ALA A O   1 
ATOM   3053 C  CB  . ALA A 1 389  ? 31.610 33.623  13.027  1.00 20.38 ? 389  ALA A CB  1 
ATOM   3054 N  N   . GLU A 1 390  ? 32.676 32.540  10.279  1.00 23.06 ? 390  GLU A N   1 
ATOM   3055 C  CA  . GLU A 1 390  ? 32.445 32.094  8.914   1.00 24.81 ? 390  GLU A CA  1 
ATOM   3056 C  C   . GLU A 1 390  ? 33.107 30.728  8.695   1.00 26.89 ? 390  GLU A C   1 
ATOM   3057 O  O   . GLU A 1 390  ? 32.483 29.808  8.138   1.00 27.80 ? 390  GLU A O   1 
ATOM   3058 C  CB  . GLU A 1 390  ? 33.036 33.138  7.954   1.00 22.98 ? 390  GLU A CB  1 
ATOM   3059 C  CG  . GLU A 1 390  ? 32.969 32.792  6.476   1.00 27.86 ? 390  GLU A CG  1 
ATOM   3060 C  CD  . GLU A 1 390  ? 33.725 33.806  5.629   1.00 29.35 ? 390  GLU A CD  1 
ATOM   3061 O  OE1 . GLU A 1 390  ? 34.586 34.533  6.181   1.00 28.58 ? 390  GLU A OE1 1 
ATOM   3062 O  OE2 . GLU A 1 390  ? 33.476 33.878  4.415   1.00 31.28 ? 390  GLU A OE2 1 
ATOM   3063 N  N   . ARG A 1 391  ? 34.355 30.596  9.143   1.00 25.88 ? 391  ARG A N   1 
ATOM   3064 C  CA  . ARG A 1 391  ? 35.086 29.343  8.987   1.00 28.72 ? 391  ARG A CA  1 
ATOM   3065 C  C   . ARG A 1 391  ? 34.448 28.247  9.837   1.00 27.89 ? 391  ARG A C   1 
ATOM   3066 O  O   . ARG A 1 391  ? 34.518 27.066  9.475   1.00 31.70 ? 391  ARG A O   1 
ATOM   3067 C  CB  . ARG A 1 391  ? 36.566 29.522  9.364   1.00 30.17 ? 391  ARG A CB  1 
ATOM   3068 C  CG  . ARG A 1 391  ? 37.344 30.403  8.391   1.00 33.48 ? 391  ARG A CG  1 
ATOM   3069 C  CD  . ARG A 1 391  ? 38.856 30.270  8.578   1.00 35.49 ? 391  ARG A CD  1 
ATOM   3070 N  NE  . ARG A 1 391  ? 39.307 30.699  9.901   1.00 38.26 ? 391  ARG A NE  1 
ATOM   3071 C  CZ  . ARG A 1 391  ? 39.535 31.968  10.251  1.00 39.03 ? 391  ARG A CZ  1 
ATOM   3072 N  NH1 . ARG A 1 391  ? 39.361 32.957  9.379   1.00 38.06 ? 391  ARG A NH1 1 
ATOM   3073 N  NH2 . ARG A 1 391  ? 39.936 32.245  11.483  1.00 40.20 ? 391  ARG A NH2 1 
ATOM   3074 N  N   . ALA A 1 392  ? 33.800 28.619  10.938  1.00 28.88 ? 392  ALA A N   1 
ATOM   3075 C  CA  . ALA A 1 392  ? 33.147 27.626  11.809  1.00 27.74 ? 392  ALA A CA  1 
ATOM   3076 C  C   . ALA A 1 392  ? 31.829 27.175  11.161  1.00 30.64 ? 392  ALA A C   1 
ATOM   3077 O  O   . ALA A 1 392  ? 31.069 26.377  11.747  1.00 32.73 ? 392  ALA A O   1 
ATOM   3078 C  CB  . ALA A 1 392  ? 32.883 28.214  13.180  1.00 28.14 ? 392  ALA A CB  1 
ATOM   3079 N  N   . GLY A 1 393  ? 31.572 27.691  9.956   1.00 31.15 ? 393  GLY A N   1 
ATOM   3080 C  CA  . GLY A 1 393  ? 30.371 27.351  9.215   1.00 30.36 ? 393  GLY A CA  1 
ATOM   3081 C  C   . GLY A 1 393  ? 29.116 28.030  9.702   1.00 28.94 ? 393  GLY A C   1 
ATOM   3082 O  O   . GLY A 1 393  ? 27.993 27.635  9.360   1.00 30.05 ? 393  GLY A O   1 
ATOM   3083 N  N   . GLN A 1 394  ? 29.270 29.095  10.475  1.00 28.51 ? 394  GLN A N   1 
ATOM   3084 C  CA  . GLN A 1 394  ? 28.071 29.714  10.975  1.00 29.40 ? 394  GLN A CA  1 
ATOM   3085 C  C   . GLN A 1 394  ? 27.429 30.758  10.060  1.00 27.03 ? 394  GLN A C   1 
ATOM   3086 O  O   . GLN A 1 394  ? 26.294 31.174  10.311  1.00 29.05 ? 394  GLN A O   1 
ATOM   3087 C  CB  . GLN A 1 394  ? 28.295 30.220  12.415  1.00 32.45 ? 394  GLN A CB  1 
ATOM   3088 C  CG  . GLN A 1 394  ? 28.912 31.557  12.588  1.00 36.01 ? 394  GLN A CG  1 
ATOM   3089 C  CD  . GLN A 1 394  ? 28.732 32.072  14.021  1.00 35.25 ? 394  GLN A CD  1 
ATOM   3090 O  OE1 . GLN A 1 394  ? 29.225 31.471  15.003  1.00 34.90 ? 394  GLN A OE1 1 
ATOM   3091 N  NE2 . GLN A 1 394  ? 28.030 33.188  14.146  1.00 27.90 ? 394  GLN A NE2 1 
ATOM   3092 N  N   . ALA A 1 395  ? 28.110 31.129  8.967   1.00 24.68 ? 395  ALA A N   1 
ATOM   3093 C  CA  . ALA A 1 395  ? 27.562 32.111  8.032   1.00 23.95 ? 395  ALA A CA  1 
ATOM   3094 C  C   . ALA A 1 395  ? 28.246 32.039  6.665   1.00 23.62 ? 395  ALA A C   1 
ATOM   3095 O  O   . ALA A 1 395  ? 29.407 31.660  6.571   1.00 24.65 ? 395  ALA A O   1 
ATOM   3096 C  CB  . ALA A 1 395  ? 27.735 33.540  8.626   1.00 26.23 ? 395  ALA A CB  1 
ATOM   3097 N  N   . GLU A 1 396  ? 27.509 32.370  5.607   1.00 24.27 ? 396  GLU A N   1 
ATOM   3098 C  CA  . GLU A 1 396  ? 28.073 32.456  4.267   1.00 25.35 ? 396  GLU A CA  1 
ATOM   3099 C  C   . GLU A 1 396  ? 27.672 33.880  3.850   1.00 23.51 ? 396  GLU A C   1 
ATOM   3100 O  O   . GLU A 1 396  ? 26.579 34.367  4.182   1.00 26.09 ? 396  GLU A O   1 
ATOM   3101 C  CB  . GLU A 1 396  ? 27.464 31.413  3.324   1.00 30.33 ? 396  GLU A CB  1 
ATOM   3102 C  CG  . GLU A 1 396  ? 25.984 31.591  3.102   1.00 39.19 ? 396  GLU A CG  1 
ATOM   3103 C  CD  . GLU A 1 396  ? 25.354 30.417  2.382   1.00 44.03 ? 396  GLU A CD  1 
ATOM   3104 O  OE1 . GLU A 1 396  ? 25.841 30.056  1.279   1.00 47.25 ? 396  GLU A OE1 1 
ATOM   3105 O  OE2 . GLU A 1 396  ? 24.368 29.858  2.922   1.00 47.83 ? 396  GLU A OE2 1 
ATOM   3106 N  N   . PHE A 1 397  ? 28.552 34.552  3.141   1.00 19.16 ? 397  PHE A N   1 
ATOM   3107 C  CA  . PHE A 1 397  ? 28.267 35.933  2.794   1.00 16.24 ? 397  PHE A CA  1 
ATOM   3108 C  C   . PHE A 1 397  ? 27.937 36.103  1.316   1.00 15.32 ? 397  PHE A C   1 
ATOM   3109 O  O   . PHE A 1 397  ? 28.462 35.382  0.486   1.00 19.04 ? 397  PHE A O   1 
ATOM   3110 C  CB  . PHE A 1 397  ? 29.498 36.780  3.150   1.00 17.35 ? 397  PHE A CB  1 
ATOM   3111 C  CG  . PHE A 1 397  ? 29.790 36.836  4.634   1.00 14.47 ? 397  PHE A CG  1 
ATOM   3112 C  CD1 . PHE A 1 397  ? 28.945 37.537  5.476   1.00 14.15 ? 397  PHE A CD1 1 
ATOM   3113 C  CD2 . PHE A 1 397  ? 30.861 36.142  5.158   1.00 16.74 ? 397  PHE A CD2 1 
ATOM   3114 C  CE1 . PHE A 1 397  ? 29.147 37.548  6.856   1.00 15.50 ? 397  PHE A CE1 1 
ATOM   3115 C  CE2 . PHE A 1 397  ? 31.093 36.128  6.575   1.00 17.68 ? 397  PHE A CE2 1 
ATOM   3116 C  CZ  . PHE A 1 397  ? 30.215 36.841  7.402   1.00 15.37 ? 397  PHE A CZ  1 
ATOM   3117 N  N   . PRO A 1 398  ? 27.030 37.022  1.014   1.00 14.33 ? 398  PRO A N   1 
ATOM   3118 C  CA  . PRO A 1 398  ? 26.640 37.294  -0.377  1.00 15.20 ? 398  PRO A CA  1 
ATOM   3119 C  C   . PRO A 1 398  ? 27.738 38.055  -1.125  1.00 16.10 ? 398  PRO A C   1 
ATOM   3120 O  O   . PRO A 1 398  ? 28.593 38.719  -0.518  1.00 15.21 ? 398  PRO A O   1 
ATOM   3121 C  CB  . PRO A 1 398  ? 25.379 38.133  -0.213  1.00 15.57 ? 398  PRO A CB  1 
ATOM   3122 C  CG  . PRO A 1 398  ? 25.662 38.911  1.074   1.00 16.41 ? 398  PRO A CG  1 
ATOM   3123 C  CD  . PRO A 1 398  ? 26.249 37.826  1.966   1.00 15.49 ? 398  PRO A CD  1 
ATOM   3124 N  N   . THR A 1 399  ? 27.703 37.934  -2.443  1.00 13.67 ? 399  THR A N   1 
ATOM   3125 C  CA  . THR A 1 399  ? 28.618 38.645  -3.328  1.00 12.97 ? 399  THR A CA  1 
ATOM   3126 C  C   . THR A 1 399  ? 27.843 39.868  -3.839  1.00 14.17 ? 399  THR A C   1 
ATOM   3127 O  O   . THR A 1 399  ? 26.624 39.850  -3.983  1.00 14.59 ? 399  THR A O   1 
ATOM   3128 C  CB  . THR A 1 399  ? 29.015 37.775  -4.507  1.00 13.61 ? 399  THR A CB  1 
ATOM   3129 O  OG1 . THR A 1 399  ? 27.820 37.343  -5.181  1.00 15.94 ? 399  THR A OG1 1 
ATOM   3130 C  CG2 . THR A 1 399  ? 29.820 36.564  -4.013  1.00 15.27 ? 399  THR A CG2 1 
ATOM   3131 N  N   . LEU A 1 400  ? 28.578 40.945  -4.077  1.00 12.67 ? 400  LEU A N   1 
ATOM   3132 C  CA  . LEU A 1 400  ? 27.977 42.184  -4.523  1.00 12.47 ? 400  LEU A CA  1 
ATOM   3133 C  C   . LEU A 1 400  ? 28.888 42.932  -5.476  1.00 11.59 ? 400  LEU A C   1 
ATOM   3134 O  O   . LEU A 1 400  ? 30.122 42.876  -5.364  1.00 12.51 ? 400  LEU A O   1 
ATOM   3135 C  CB  . LEU A 1 400  ? 27.709 43.097  -3.298  1.00 13.24 ? 400  LEU A CB  1 
ATOM   3136 C  CG  . LEU A 1 400  ? 27.031 44.473  -3.552  1.00 12.14 ? 400  LEU A CG  1 
ATOM   3137 C  CD1 . LEU A 1 400  ? 26.204 44.842  -2.280  1.00 13.93 ? 400  LEU A CD1 1 
ATOM   3138 C  CD2 . LEU A 1 400  ? 28.047 45.570  -3.848  1.00 12.47 ? 400  LEU A CD2 1 
ATOM   3139 N  N   . SER A 1 401  ? 28.273 43.565  -6.487  1.00 11.68 ? 401  SER A N   1 
ATOM   3140 C  CA  . SER A 1 401  ? 29.048 44.493  -7.326  1.00 12.39 ? 401  SER A CA  1 
ATOM   3141 C  C   . SER A 1 401  ? 28.185 45.731  -7.530  1.00 12.46 ? 401  SER A C   1 
ATOM   3142 O  O   . SER A 1 401  ? 26.974 45.718  -7.333  1.00 11.82 ? 401  SER A O   1 
ATOM   3143 C  CB  . SER A 1 401  ? 29.415 43.924  -8.694  1.00 13.50 ? 401  SER A CB  1 
ATOM   3144 O  OG  . SER A 1 401  ? 28.277 43.858  -9.572  1.00 13.14 ? 401  SER A OG  1 
ATOM   3145 N  N   . GLY A 1 402  ? 28.851 46.822  -7.884  1.00 11.68 ? 402  GLY A N   1 
ATOM   3146 C  CA  . GLY A 1 402  ? 28.154 48.074  -8.111  1.00 11.35 ? 402  GLY A CA  1 
ATOM   3147 C  C   . GLY A 1 402  ? 28.784 49.173  -7.251  1.00 12.12 ? 402  GLY A C   1 
ATOM   3148 O  O   . GLY A 1 402  ? 29.862 48.976  -6.627  1.00 13.89 ? 402  GLY A O   1 
ATOM   3149 N  N   . ASP A 1 403  ? 28.141 50.325  -7.208  1.00 10.63 ? 403  ASP A N   1 
ATOM   3150 C  CA  . ASP A 1 403  ? 28.651 51.442  -6.375  1.00 10.96 ? 403  ASP A CA  1 
ATOM   3151 C  C   . ASP A 1 403  ? 27.533 51.915  -5.458  1.00 13.67 ? 403  ASP A C   1 
ATOM   3152 O  O   . ASP A 1 403  ? 26.417 51.338  -5.441  1.00 12.69 ? 403  ASP A O   1 
ATOM   3153 C  CB  . ASP A 1 403  ? 29.169 52.610  -7.237  1.00 11.54 ? 403  ASP A CB  1 
ATOM   3154 C  CG  . ASP A 1 403  ? 28.047 53.379  -7.940  1.00 15.55 ? 403  ASP A CG  1 
ATOM   3155 O  OD1 . ASP A 1 403  ? 26.882 52.931  -7.981  1.00 16.21 ? 403  ASP A OD1 1 
ATOM   3156 O  OD2 . ASP A 1 403  ? 28.389 54.455  -8.454  1.00 16.87 ? 403  ASP A OD2 1 
ATOM   3157 N  N   . PHE A 1 404  ? 27.835 52.922  -4.677  1.00 11.26 ? 404  PHE A N   1 
ATOM   3158 C  CA  . PHE A 1 404  ? 26.891 53.491  -3.733  1.00 11.26 ? 404  PHE A CA  1 
ATOM   3159 C  C   . PHE A 1 404  ? 26.767 55.001  -3.882  1.00 11.99 ? 404  PHE A C   1 
ATOM   3160 O  O   . PHE A 1 404  ? 26.893 55.771  -2.917  1.00 12.16 ? 404  PHE A O   1 
ATOM   3161 C  CB  . PHE A 1 404  ? 27.253 53.103  -2.283  1.00 11.37 ? 404  PHE A CB  1 
ATOM   3162 C  CG  . PHE A 1 404  ? 27.207 51.617  -2.053  1.00 10.67 ? 404  PHE A CG  1 
ATOM   3163 C  CD1 . PHE A 1 404  ? 25.959 50.967  -1.929  1.00 11.92 ? 404  PHE A CD1 1 
ATOM   3164 C  CD2 . PHE A 1 404  ? 28.372 50.864  -2.042  1.00 11.85 ? 404  PHE A CD2 1 
ATOM   3165 C  CE1 . PHE A 1 404  ? 25.899 49.537  -1.796  1.00 11.57 ? 404  PHE A CE1 1 
ATOM   3166 C  CE2 . PHE A 1 404  ? 28.316 49.458  -1.906  1.00 12.96 ? 404  PHE A CE2 1 
ATOM   3167 C  CZ  . PHE A 1 404  ? 27.069 48.801  -1.786  1.00 11.44 ? 404  PHE A CZ  1 
ATOM   3168 N  N   . PHE A 1 405  ? 26.475 55.387  -5.121  1.00 12.79 ? 405  PHE A N   1 
ATOM   3169 C  CA  . PHE A 1 405  ? 26.186 56.790  -5.451  1.00 10.07 ? 405  PHE A CA  1 
ATOM   3170 C  C   . PHE A 1 405  ? 24.817 56.740  -6.132  1.00 12.14 ? 405  PHE A C   1 
ATOM   3171 O  O   . PHE A 1 405  ? 24.489 55.767  -6.815  1.00 14.12 ? 405  PHE A O   1 
ATOM   3172 C  CB  . PHE A 1 405  ? 27.210 57.366  -6.451  1.00 11.04 ? 405  PHE A CB  1 
ATOM   3173 C  CG  . PHE A 1 405  ? 28.597 57.494  -5.886  1.00 12.60 ? 405  PHE A CG  1 
ATOM   3174 C  CD1 . PHE A 1 405  ? 28.836 58.302  -4.774  1.00 12.65 ? 405  PHE A CD1 1 
ATOM   3175 C  CD2 . PHE A 1 405  ? 29.643 56.806  -6.472  1.00 12.95 ? 405  PHE A CD2 1 
ATOM   3176 C  CE1 . PHE A 1 405  ? 30.155 58.427  -4.239  1.00 13.86 ? 405  PHE A CE1 1 
ATOM   3177 C  CE2 . PHE A 1 405  ? 30.948 56.903  -5.959  1.00 13.20 ? 405  PHE A CE2 1 
ATOM   3178 C  CZ  . PHE A 1 405  ? 31.201 57.719  -4.836  1.00 12.35 ? 405  PHE A CZ  1 
ATOM   3179 N  N   . THR A 1 406  ? 23.994 57.778  -6.001  1.00 12.64 ? 406  THR A N   1 
ATOM   3180 C  CA  . THR A 1 406  ? 24.232 58.993  -5.241  1.00 11.77 ? 406  THR A CA  1 
ATOM   3181 C  C   . THR A 1 406  ? 23.563 58.870  -3.890  1.00 13.49 ? 406  THR A C   1 
ATOM   3182 O  O   . THR A 1 406  ? 22.421 58.438  -3.741  1.00 13.91 ? 406  THR A O   1 
ATOM   3183 C  CB  . THR A 1 406  ? 23.689 60.189  -6.024  1.00 11.89 ? 406  THR A CB  1 
ATOM   3184 O  OG1 . THR A 1 406  ? 24.594 60.418  -7.104  1.00 13.39 ? 406  THR A OG1 1 
ATOM   3185 C  CG2 . THR A 1 406  ? 23.581 61.473  -5.178  1.00 13.40 ? 406  THR A CG2 1 
ATOM   3186 N  N   . TYR A 1 407  ? 24.352 59.210  -2.877  1.00 12.27 ? 407  TYR A N   1 
ATOM   3187 C  CA  . TYR A 1 407  ? 23.918 59.105  -1.510  1.00 12.18 ? 407  TYR A CA  1 
ATOM   3188 C  C   . TYR A 1 407  ? 22.839 60.093  -1.111  1.00 13.69 ? 407  TYR A C   1 
ATOM   3189 O  O   . TYR A 1 407  ? 22.861 61.233  -1.552  1.00 15.08 ? 407  TYR A O   1 
ATOM   3190 C  CB  . TYR A 1 407  ? 25.144 59.376  -0.624  1.00 13.05 ? 407  TYR A CB  1 
ATOM   3191 C  CG  . TYR A 1 407  ? 24.895 59.540  0.844   1.00 12.57 ? 407  TYR A CG  1 
ATOM   3192 C  CD1 . TYR A 1 407  ? 24.436 58.459  1.637   1.00 13.47 ? 407  TYR A CD1 1 
ATOM   3193 C  CD2 . TYR A 1 407  ? 25.215 60.724  1.481   1.00 12.27 ? 407  TYR A CD2 1 
ATOM   3194 C  CE1 . TYR A 1 407  ? 24.317 58.594  3.031   1.00 13.43 ? 407  TYR A CE1 1 
ATOM   3195 C  CE2 . TYR A 1 407  ? 25.117 60.870  2.862   1.00 12.83 ? 407  TYR A CE2 1 
ATOM   3196 C  CZ  . TYR A 1 407  ? 24.677 59.807  3.633   1.00 13.67 ? 407  TYR A CZ  1 
ATOM   3197 O  OH  . TYR A 1 407  ? 24.685 59.943  5.008   1.00 13.85 ? 407  TYR A OH  1 
ATOM   3198 N  N   . ALA A 1 408  ? 21.870 59.625  -0.328  1.00 14.33 ? 408  ALA A N   1 
ATOM   3199 C  CA  . ALA A 1 408  ? 20.890 60.531  0.303   1.00 15.10 ? 408  ALA A CA  1 
ATOM   3200 C  C   . ALA A 1 408  ? 20.830 60.037  1.734   1.00 13.59 ? 408  ALA A C   1 
ATOM   3201 O  O   . ALA A 1 408  ? 20.712 58.815  1.990   1.00 15.29 ? 408  ALA A O   1 
ATOM   3202 C  CB  . ALA A 1 408  ? 19.475 60.432  -0.317  1.00 15.40 ? 408  ALA A CB  1 
ATOM   3203 N  N   . ASP A 1 409  ? 20.940 60.970  2.683   1.00 13.63 ? 409  ASP A N   1 
ATOM   3204 C  CA  . ASP A 1 409  ? 20.858 60.601  4.092   1.00 13.93 ? 409  ASP A CA  1 
ATOM   3205 C  C   . ASP A 1 409  ? 19.443 60.666  4.640   1.00 14.94 ? 409  ASP A C   1 
ATOM   3206 O  O   . ASP A 1 409  ? 19.159 60.031  5.679   1.00 16.04 ? 409  ASP A O   1 
ATOM   3207 C  CB  . ASP A 1 409  ? 21.824 61.443  4.966   1.00 14.18 ? 409  ASP A CB  1 
ATOM   3208 C  CG  . ASP A 1 409  ? 21.561 62.962  4.903   1.00 13.25 ? 409  ASP A CG  1 
ATOM   3209 O  OD1 . ASP A 1 409  ? 20.911 63.462  3.963   1.00 14.88 ? 409  ASP A OD1 1 
ATOM   3210 O  OD2 . ASP A 1 409  ? 22.088 63.675  5.801   1.00 16.25 ? 409  ASP A OD2 1 
ATOM   3211 N  N   . ARG A 1 410  ? 18.550 61.381  3.948   1.00 14.31 ? 410  ARG A N   1 
ATOM   3212 C  CA  . ARG A 1 410  ? 17.152 61.471  4.402   1.00 17.08 ? 410  ARG A CA  1 
ATOM   3213 C  C   . ARG A 1 410  ? 16.334 62.116  3.316   1.00 18.27 ? 410  ARG A C   1 
ATOM   3214 O  O   . ARG A 1 410  ? 16.885 62.855  2.483   1.00 17.55 ? 410  ARG A O   1 
ATOM   3215 C  CB  . ARG A 1 410  ? 17.050 62.295  5.677   1.00 17.35 ? 410  ARG A CB  1 
ATOM   3216 C  CG  . ARG A 1 410  ? 17.482 63.760  5.564   1.00 20.19 ? 410  ARG A CG  1 
ATOM   3217 C  CD  . ARG A 1 410  ? 17.474 64.304  6.963   1.00 19.67 ? 410  ARG A CD  1 
ATOM   3218 N  NE  . ARG A 1 410  ? 18.118 65.609  7.141   1.00 21.85 ? 410  ARG A NE  1 
ATOM   3219 C  CZ  . ARG A 1 410  ? 17.549 66.788  6.893   1.00 23.79 ? 410  ARG A CZ  1 
ATOM   3220 N  NH1 . ARG A 1 410  ? 16.291 66.844  6.427   1.00 23.80 ? 410  ARG A NH1 1 
ATOM   3221 N  NH2 . ARG A 1 410  ? 18.230 67.908  7.127   1.00 23.68 ? 410  ARG A NH2 1 
ATOM   3222 N  N   . SER A 1 411  ? 15.047 61.771  3.274   1.00 17.83 ? 411  SER A N   1 
ATOM   3223 C  CA  . SER A 1 411  ? 14.085 62.289  2.298   1.00 18.24 ? 411  SER A CA  1 
ATOM   3224 C  C   . SER A 1 411  ? 14.616 62.425  0.868   1.00 17.16 ? 411  SER A C   1 
ATOM   3225 O  O   . SER A 1 411  ? 15.043 61.429  0.279   1.00 18.40 ? 411  SER A O   1 
ATOM   3226 C  CB  A SER A 1 411  ? 13.466 63.609  2.812   0.50 21.37 ? 411  SER A CB  1 
ATOM   3227 C  CB  B SER A 1 411  ? 13.768 63.870  2.857   0.50 21.86 ? 411  SER A CB  1 
ATOM   3228 O  OG  A SER A 1 411  ? 14.436 64.551  3.247   0.50 22.93 ? 411  SER A OG  1 
ATOM   3229 O  OG  B SER A 1 411  ? 12.657 64.400  2.169   0.50 23.64 ? 411  SER A OG  1 
ATOM   3230 N  N   . ASP A 1 412  ? 14.577 63.630  0.295   1.00 16.03 ? 412  ASP A N   1 
ATOM   3231 C  CA  . ASP A 1 412  ? 15.064 63.819  -1.075  1.00 15.67 ? 412  ASP A CA  1 
ATOM   3232 C  C   . ASP A 1 412  ? 16.398 64.576  -1.036  1.00 14.85 ? 412  ASP A C   1 
ATOM   3233 O  O   . ASP A 1 412  ? 16.802 65.136  -2.042  1.00 15.95 ? 412  ASP A O   1 
ATOM   3234 C  CB  . ASP A 1 412  ? 14.065 64.659  -1.888  1.00 17.35 ? 412  ASP A CB  1 
ATOM   3235 C  CG  . ASP A 1 412  ? 13.871 66.082  -1.297  1.00 16.31 ? 412  ASP A CG  1 
ATOM   3236 O  OD1 . ASP A 1 412  ? 14.401 66.417  -0.204  1.00 17.38 ? 412  ASP A OD1 1 
ATOM   3237 O  OD2 . ASP A 1 412  ? 13.173 66.898  -1.960  1.00 19.37 ? 412  ASP A OD2 1 
ATOM   3238 N  N   . ASN A 1 413  ? 17.098 64.521  0.091   1.00 14.67 ? 413  ASN A N   1 
ATOM   3239 C  CA  . ASN A 1 413  ? 18.362 65.250  0.240   1.00 15.52 ? 413  ASN A CA  1 
ATOM   3240 C  C   . ASN A 1 413  ? 19.520 64.393  -0.327  1.00 13.77 ? 413  ASN A C   1 
ATOM   3241 O  O   . ASN A 1 413  ? 20.218 63.706  0.436   1.00 14.45 ? 413  ASN A O   1 
ATOM   3242 C  CB  . ASN A 1 413  ? 18.624 65.573  1.721   1.00 15.58 ? 413  ASN A CB  1 
ATOM   3243 C  CG  . ASN A 1 413  ? 17.696 66.678  2.328   1.00 16.20 ? 413  ASN A CG  1 
ATOM   3244 O  OD1 . ASN A 1 413  ? 17.964 67.148  3.430   1.00 17.49 ? 413  ASN A OD1 1 
ATOM   3245 N  ND2 . ASN A 1 413  ? 16.633 67.087  1.617   1.00 14.87 ? 413  ASN A ND2 1 
ATOM   3246 N  N   . TYR A 1 414  ? 19.691 64.460  -1.645  1.00 13.88 ? 414  TYR A N   1 
ATOM   3247 C  CA  . TYR A 1 414  ? 20.755 63.734  -2.363  1.00 13.44 ? 414  TYR A CA  1 
ATOM   3248 C  C   . TYR A 1 414  ? 21.995 64.621  -2.420  1.00 13.96 ? 414  TYR A C   1 
ATOM   3249 O  O   . TYR A 1 414  ? 21.897 65.818  -2.738  1.00 14.75 ? 414  TYR A O   1 
ATOM   3250 C  CB  . TYR A 1 414  ? 20.307 63.386  -3.781  1.00 13.21 ? 414  TYR A CB  1 
ATOM   3251 C  CG  . TYR A 1 414  ? 19.295 62.257  -3.807  1.00 14.65 ? 414  TYR A CG  1 
ATOM   3252 C  CD1 . TYR A 1 414  ? 17.942 62.500  -3.568  1.00 16.35 ? 414  TYR A CD1 1 
ATOM   3253 C  CD2 . TYR A 1 414  ? 19.725 60.927  -4.011  1.00 14.29 ? 414  TYR A CD2 1 
ATOM   3254 C  CE1 . TYR A 1 414  ? 17.017 61.420  -3.511  1.00 15.28 ? 414  TYR A CE1 1 
ATOM   3255 C  CE2 . TYR A 1 414  ? 18.790 59.848  -3.979  1.00 14.79 ? 414  TYR A CE2 1 
ATOM   3256 C  CZ  . TYR A 1 414  ? 17.470 60.129  -3.725  1.00 15.12 ? 414  TYR A CZ  1 
ATOM   3257 O  OH  . TYR A 1 414  ? 16.595 59.054  -3.726  1.00 14.37 ? 414  TYR A OH  1 
ATOM   3258 N  N   . TRP A 1 415  ? 23.141 64.009  -2.122  1.00 13.37 ? 415  TRP A N   1 
ATOM   3259 C  CA  . TRP A 1 415  ? 24.397 64.735  -2.024  1.00 12.68 ? 415  TRP A CA  1 
ATOM   3260 C  C   . TRP A 1 415  ? 25.129 64.789  -3.351  1.00 14.74 ? 415  TRP A C   1 
ATOM   3261 O  O   . TRP A 1 415  ? 26.235 64.284  -3.462  1.00 15.78 ? 415  TRP A O   1 
ATOM   3262 C  CB  . TRP A 1 415  ? 25.279 64.053  -0.975  1.00 13.27 ? 415  TRP A CB  1 
ATOM   3263 C  CG  . TRP A 1 415  ? 24.709 64.119  0.458   1.00 12.30 ? 415  TRP A CG  1 
ATOM   3264 C  CD1 . TRP A 1 415  ? 23.408 63.841  0.869   1.00 12.74 ? 415  TRP A CD1 1 
ATOM   3265 C  CD2 . TRP A 1 415  ? 25.460 64.402  1.645   1.00 12.75 ? 415  TRP A CD2 1 
ATOM   3266 N  NE1 . TRP A 1 415  ? 23.330 63.942  2.246   1.00 12.67 ? 415  TRP A NE1 1 
ATOM   3267 C  CE2 . TRP A 1 415  ? 24.566 64.278  2.751   1.00 12.14 ? 415  TRP A CE2 1 
ATOM   3268 C  CE3 . TRP A 1 415  ? 26.813 64.740  1.888   1.00 13.91 ? 415  TRP A CE3 1 
ATOM   3269 C  CZ2 . TRP A 1 415  ? 24.976 64.483  4.066   1.00 13.19 ? 415  TRP A CZ2 1 
ATOM   3270 C  CZ3 . TRP A 1 415  ? 27.217 64.937  3.168   1.00 12.46 ? 415  TRP A CZ3 1 
ATOM   3271 C  CH2 . TRP A 1 415  ? 26.309 64.810  4.267   1.00 13.54 ? 415  TRP A CH2 1 
ATOM   3272 N  N   . SER A 1 416  ? 24.475 65.337  -4.363  1.00 11.68 ? 416  SER A N   1 
ATOM   3273 C  CA  . SER A 1 416  ? 25.137 65.461  -5.659  1.00 13.69 ? 416  SER A CA  1 
ATOM   3274 C  C   . SER A 1 416  ? 25.710 66.869  -5.879  1.00 12.26 ? 416  SER A C   1 
ATOM   3275 O  O   . SER A 1 416  ? 26.389 67.087  -6.872  1.00 12.16 ? 416  SER A O   1 
ATOM   3276 C  CB  . SER A 1 416  ? 24.195 65.050  -6.803  1.00 13.23 ? 416  SER A CB  1 
ATOM   3277 O  OG  . SER A 1 416  ? 22.899 65.627  -6.630  1.00 13.59 ? 416  SER A OG  1 
ATOM   3278 N  N   . GLY A 1 417  ? 25.472 67.803  -4.958  1.00 12.07 ? 417  GLY A N   1 
ATOM   3279 C  CA  . GLY A 1 417  ? 26.035 69.138  -5.135  1.00 13.82 ? 417  GLY A CA  1 
ATOM   3280 C  C   . GLY A 1 417  ? 27.563 69.138  -5.060  1.00 11.84 ? 417  GLY A C   1 
ATOM   3281 O  O   . GLY A 1 417  ? 28.236 69.858  -5.817  1.00 12.56 ? 417  GLY A O   1 
ATOM   3282 N  N   . TYR A 1 418  ? 28.132 68.296  -4.187  1.00 11.43 ? 418  TYR A N   1 
ATOM   3283 C  CA  . TYR A 1 418  ? 29.593 68.319  -4.009  1.00 12.40 ? 418  TYR A CA  1 
ATOM   3284 C  C   . TYR A 1 418  ? 30.351 67.697  -5.162  1.00 12.59 ? 418  TYR A C   1 
ATOM   3285 O  O   . TYR A 1 418  ? 31.571 67.695  -5.198  1.00 12.35 ? 418  TYR A O   1 
ATOM   3286 C  CB  . TYR A 1 418  ? 30.001 67.681  -2.673  1.00 10.58 ? 418  TYR A CB  1 
ATOM   3287 C  CG  . TYR A 1 418  ? 30.085 66.162  -2.697  1.00 12.12 ? 418  TYR A CG  1 
ATOM   3288 C  CD1 . TYR A 1 418  ? 28.930 65.350  -2.508  1.00 11.22 ? 418  TYR A CD1 1 
ATOM   3289 C  CD2 . TYR A 1 418  ? 31.323 65.532  -2.911  1.00 12.01 ? 418  TYR A CD2 1 
ATOM   3290 C  CE1 . TYR A 1 418  ? 29.031 63.940  -2.531  1.00 11.07 ? 418  TYR A CE1 1 
ATOM   3291 C  CE2 . TYR A 1 418  ? 31.443 64.173  -2.931  1.00 11.18 ? 418  TYR A CE2 1 
ATOM   3292 C  CZ  . TYR A 1 418  ? 30.301 63.364  -2.738  1.00 9.89  ? 418  TYR A CZ  1 
ATOM   3293 O  OH  . TYR A 1 418  ? 30.510 61.992  -2.724  1.00 11.87 ? 418  TYR A OH  1 
ATOM   3294 N  N   . TYR A 1 419  ? 29.618 67.161  -6.127  1.00 10.83 ? 419  TYR A N   1 
ATOM   3295 C  CA  . TYR A 1 419  ? 30.288 66.687  -7.342  1.00 10.78 ? 419  TYR A CA  1 
ATOM   3296 C  C   . TYR A 1 419  ? 30.797 67.899  -8.130  1.00 11.33 ? 419  TYR A C   1 
ATOM   3297 O  O   . TYR A 1 419  ? 31.621 67.725  -9.033  1.00 11.80 ? 419  TYR A O   1 
ATOM   3298 C  CB  . TYR A 1 419  ? 29.326 65.904  -8.240  1.00 10.12 ? 419  TYR A CB  1 
ATOM   3299 C  CG  . TYR A 1 419  ? 28.672 64.712  -7.592  1.00 10.83 ? 419  TYR A CG  1 
ATOM   3300 C  CD1 . TYR A 1 419  ? 29.264 64.035  -6.486  1.00 11.57 ? 419  TYR A CD1 1 
ATOM   3301 C  CD2 . TYR A 1 419  ? 27.495 64.193  -8.142  1.00 10.94 ? 419  TYR A CD2 1 
ATOM   3302 C  CE1 . TYR A 1 419  ? 28.699 62.865  -5.943  1.00 11.02 ? 419  TYR A CE1 1 
ATOM   3303 C  CE2 . TYR A 1 419  ? 26.907 63.037  -7.605  1.00 11.92 ? 419  TYR A CE2 1 
ATOM   3304 C  CZ  . TYR A 1 419  ? 27.522 62.378  -6.511  1.00 11.36 ? 419  TYR A CZ  1 
ATOM   3305 O  OH  . TYR A 1 419  ? 26.911 61.255  -6.008  1.00 12.24 ? 419  TYR A OH  1 
ATOM   3306 N  N   . THR A 1 420  ? 30.307 69.108  -7.804  1.00 11.59 ? 420  THR A N   1 
ATOM   3307 C  CA  . THR A 1 420  ? 30.691 70.315  -8.518  1.00 12.02 ? 420  THR A CA  1 
ATOM   3308 C  C   . THR A 1 420  ? 31.235 71.426  -7.645  1.00 12.18 ? 420  THR A C   1 
ATOM   3309 O  O   . THR A 1 420  ? 32.015 72.239  -8.118  1.00 12.94 ? 420  THR A O   1 
ATOM   3310 C  CB  . THR A 1 420  ? 29.459 70.836  -9.296  1.00 11.68 ? 420  THR A CB  1 
ATOM   3311 O  OG1 . THR A 1 420  ? 29.016 69.802  -10.172 1.00 13.08 ? 420  THR A OG1 1 
ATOM   3312 C  CG2 . THR A 1 420  ? 29.736 72.048  -10.161 1.00 15.43 ? 420  THR A CG2 1 
ATOM   3313 N  N   . SER A 1 421  ? 30.864 71.481  -6.371  1.00 11.27 ? 421  SER A N   1 
ATOM   3314 C  CA  . SER A 1 421  ? 31.284 72.585  -5.525  1.00 12.89 ? 421  SER A CA  1 
ATOM   3315 C  C   . SER A 1 421  ? 32.765 72.902  -5.574  1.00 13.32 ? 421  SER A C   1 
ATOM   3316 O  O   . SER A 1 421  ? 33.617 72.007  -5.512  1.00 12.19 ? 421  SER A O   1 
ATOM   3317 C  CB  . SER A 1 421  ? 30.905 72.298  -4.062  1.00 12.81 ? 421  SER A CB  1 
ATOM   3318 O  OG  . SER A 1 421  ? 29.516 72.094  -3.952  1.00 13.42 ? 421  SER A OG  1 
ATOM   3319 N  N   . ARG A 1 422  ? 33.061 74.207  -5.623  1.00 12.50 ? 422  ARG A N   1 
ATOM   3320 C  CA  . ARG A 1 422  ? 34.459 74.716  -5.698  1.00 12.73 ? 422  ARG A CA  1 
ATOM   3321 C  C   . ARG A 1 422  ? 35.187 74.068  -6.872  1.00 12.94 ? 422  ARG A C   1 
ATOM   3322 O  O   . ARG A 1 422  ? 36.205 73.374  -6.731  1.00 12.90 ? 422  ARG A O   1 
ATOM   3323 C  CB  . ARG A 1 422  ? 35.210 74.483  -4.375  1.00 13.08 ? 422  ARG A CB  1 
ATOM   3324 C  CG  . ARG A 1 422  ? 34.955 75.569  -3.275  1.00 14.88 ? 422  ARG A CG  1 
ATOM   3325 C  CD  . ARG A 1 422  ? 33.503 75.683  -2.816  1.00 12.16 ? 422  ARG A CD  1 
ATOM   3326 N  NE  . ARG A 1 422  ? 33.447 76.688  -1.744  1.00 14.00 ? 422  ARG A NE  1 
ATOM   3327 C  CZ  . ARG A 1 422  ? 33.500 76.388  -0.449  1.00 14.14 ? 422  ARG A CZ  1 
ATOM   3328 N  NH1 . ARG A 1 422  ? 33.540 75.140  -0.023  1.00 14.58 ? 422  ARG A NH1 1 
ATOM   3329 N  NH2 . ARG A 1 422  ? 33.711 77.348  0.456   1.00 13.81 ? 422  ARG A NH2 1 
ATOM   3330 N  N   . PRO A 1 423  ? 34.657 74.275  -8.068  1.00 12.14 ? 423  PRO A N   1 
ATOM   3331 C  CA  . PRO A 1 423  ? 35.276 73.662  -9.244  1.00 12.23 ? 423  PRO A CA  1 
ATOM   3332 C  C   . PRO A 1 423  ? 36.677 74.121  -9.586  1.00 12.13 ? 423  PRO A C   1 
ATOM   3333 O  O   . PRO A 1 423  ? 37.419 73.387  -10.247 1.00 12.94 ? 423  PRO A O   1 
ATOM   3334 C  CB  . PRO A 1 423  ? 34.247 73.941  -10.361 1.00 10.70 ? 423  PRO A CB  1 
ATOM   3335 C  CG  . PRO A 1 423  ? 33.684 75.279  -9.943  1.00 12.63 ? 423  PRO A CG  1 
ATOM   3336 C  CD  . PRO A 1 423  ? 33.536 75.160  -8.425  1.00 12.58 ? 423  PRO A CD  1 
ATOM   3337 N  N   . TYR A 1 424  ? 37.063 75.318  -9.176  1.00 12.28 ? 424  TYR A N   1 
ATOM   3338 C  CA  . TYR A 1 424  ? 38.441 75.746  -9.419  1.00 11.98 ? 424  TYR A CA  1 
ATOM   3339 C  C   . TYR A 1 424  ? 39.423 74.754  -8.795  1.00 12.17 ? 424  TYR A C   1 
ATOM   3340 O  O   . TYR A 1 424  ? 40.377 74.324  -9.441  1.00 11.73 ? 424  TYR A O   1 
ATOM   3341 C  CB  . TYR A 1 424  ? 38.655 77.109  -8.773  1.00 12.91 ? 424  TYR A CB  1 
ATOM   3342 C  CG  . TYR A 1 424  ? 40.029 77.658  -9.033  1.00 13.20 ? 424  TYR A CG  1 
ATOM   3343 C  CD1 . TYR A 1 424  ? 41.108 77.391  -8.159  1.00 12.03 ? 424  TYR A CD1 1 
ATOM   3344 C  CD2 . TYR A 1 424  ? 40.252 78.458  -10.143 1.00 14.78 ? 424  TYR A CD2 1 
ATOM   3345 C  CE1 . TYR A 1 424  ? 42.377 77.949  -8.422  1.00 15.77 ? 424  TYR A CE1 1 
ATOM   3346 C  CE2 . TYR A 1 424  ? 41.475 78.972  -10.395 1.00 16.49 ? 424  TYR A CE2 1 
ATOM   3347 C  CZ  . TYR A 1 424  ? 42.540 78.726  -9.536  1.00 15.07 ? 424  TYR A CZ  1 
ATOM   3348 O  OH  . TYR A 1 424  ? 43.760 79.316  -9.877  1.00 21.31 ? 424  TYR A OH  1 
ATOM   3349 N  N   . HIS A 1 425  ? 39.141 74.335  -7.562  1.00 12.12 ? 425  HIS A N   1 
ATOM   3350 C  CA  . HIS A 1 425  ? 40.075 73.423  -6.889  1.00 12.16 ? 425  HIS A CA  1 
ATOM   3351 C  C   . HIS A 1 425  ? 39.950 72.007  -7.368  1.00 11.18 ? 425  HIS A C   1 
ATOM   3352 O  O   . HIS A 1 425  ? 40.921 71.238  -7.311  1.00 10.29 ? 425  HIS A O   1 
ATOM   3353 C  CB  . HIS A 1 425  ? 39.862 73.548  -5.378  1.00 11.93 ? 425  HIS A CB  1 
ATOM   3354 C  CG  . HIS A 1 425  ? 39.833 74.970  -4.944  1.00 12.94 ? 425  HIS A CG  1 
ATOM   3355 N  ND1 . HIS A 1 425  ? 40.973 75.719  -4.700  1.00 17.52 ? 425  HIS A ND1 1 
ATOM   3356 C  CD2 . HIS A 1 425  ? 38.794 75.831  -4.924  1.00 12.67 ? 425  HIS A CD2 1 
ATOM   3357 C  CE1 . HIS A 1 425  ? 40.618 76.984  -4.535  1.00 12.55 ? 425  HIS A CE1 1 
ATOM   3358 N  NE2 . HIS A 1 425  ? 39.307 77.074  -4.668  1.00 18.09 ? 425  HIS A NE2 1 
ATOM   3359 N  N   . LYS A 1 426  ? 38.748 71.631  -7.838  1.00 11.97 ? 426  LYS A N   1 
ATOM   3360 C  CA  . LYS A 1 426  ? 38.602 70.320  -8.463  1.00 11.37 ? 426  LYS A CA  1 
ATOM   3361 C  C   . LYS A 1 426  ? 39.517 70.251  -9.711  1.00 11.02 ? 426  LYS A C   1 
ATOM   3362 O  O   . LYS A 1 426  ? 40.148 69.219  -9.975  1.00 11.43 ? 426  LYS A O   1 
ATOM   3363 C  CB  . LYS A 1 426  ? 37.127 70.081  -8.871  1.00 12.23 ? 426  LYS A CB  1 
ATOM   3364 C  CG  . LYS A 1 426  ? 36.251 69.702  -7.704  1.00 11.08 ? 426  LYS A CG  1 
ATOM   3365 C  CD  . LYS A 1 426  ? 34.753 69.775  -8.075  1.00 12.62 ? 426  LYS A CD  1 
ATOM   3366 C  CE  . LYS A 1 426  ? 33.876 68.876  -7.196  1.00 12.42 ? 426  LYS A CE  1 
ATOM   3367 N  NZ  . LYS A 1 426  ? 33.855 69.329  -5.741  1.00 13.09 ? 426  LYS A NZ  1 
ATOM   3368 N  N   . ARG A 1 427  ? 39.547 71.334  -10.508 1.00 10.70 ? 427  ARG A N   1 
ATOM   3369 C  CA  . ARG A 1 427  ? 40.406 71.315  -11.678 1.00 11.15 ? 427  ARG A CA  1 
ATOM   3370 C  C   . ARG A 1 427  ? 41.879 71.334  -11.237 1.00 12.63 ? 427  ARG A C   1 
ATOM   3371 O  O   . ARG A 1 427  ? 42.712 70.643  -11.786 1.00 11.92 ? 427  ARG A O   1 
ATOM   3372 C  CB  . ARG A 1 427  ? 40.061 72.542  -12.526 1.00 11.34 ? 427  ARG A CB  1 
ATOM   3373 C  CG  . ARG A 1 427  ? 40.994 72.783  -13.707 1.00 11.17 ? 427  ARG A CG  1 
ATOM   3374 C  CD  . ARG A 1 427  ? 41.120 71.655  -14.709 1.00 13.43 ? 427  ARG A CD  1 
ATOM   3375 N  NE  . ARG A 1 427  ? 42.156 72.063  -15.670 1.00 15.45 ? 427  ARG A NE  1 
ATOM   3376 C  CZ  . ARG A 1 427  ? 42.974 71.236  -16.274 1.00 16.44 ? 427  ARG A CZ  1 
ATOM   3377 N  NH1 . ARG A 1 427  ? 42.930 69.929  -16.079 1.00 15.25 ? 427  ARG A NH1 1 
ATOM   3378 N  NH2 . ARG A 1 427  ? 43.902 71.750  -17.088 1.00 16.44 ? 427  ARG A NH2 1 
ATOM   3379 N  N   . MET A 1 428  ? 42.192 72.134  -10.221 1.00 10.44 ? 428  MET A N   1 
ATOM   3380 C  CA  . MET A 1 428  ? 43.559 72.196  -9.725  1.00 11.45 ? 428  MET A CA  1 
ATOM   3381 C  C   . MET A 1 428  ? 44.057 70.811  -9.265  1.00 10.92 ? 428  MET A C   1 
ATOM   3382 O  O   . MET A 1 428  ? 45.233 70.454  -9.491  1.00 11.18 ? 428  MET A O   1 
ATOM   3383 C  CB  . MET A 1 428  ? 43.650 73.153  -8.554  1.00 13.00 ? 428  MET A CB  1 
ATOM   3384 C  CG  . MET A 1 428  ? 45.094 73.514  -8.172  1.00 12.25 ? 428  MET A CG  1 
ATOM   3385 S  SD  . MET A 1 428  ? 44.994 74.853  -6.923  1.00 15.03 ? 428  MET A SD  1 
ATOM   3386 C  CE  . MET A 1 428  ? 46.726 75.410  -6.858  1.00 15.26 ? 428  MET A CE  1 
ATOM   3387 N  N   . ASP A 1 429  ? 43.159 70.025  -8.660  1.00 11.08 ? 429  ASP A N   1 
ATOM   3388 C  CA  . ASP A 1 429  ? 43.524 68.654  -8.268  1.00 10.79 ? 429  ASP A CA  1 
ATOM   3389 C  C   . ASP A 1 429  ? 44.108 67.839  -9.442  1.00 9.80  ? 429  ASP A C   1 
ATOM   3390 O  O   . ASP A 1 429  ? 45.096 67.123  -9.307  1.00 11.30 ? 429  ASP A O   1 
ATOM   3391 C  CB  . ASP A 1 429  ? 42.263 67.933  -7.769  1.00 11.31 ? 429  ASP A CB  1 
ATOM   3392 C  CG  . ASP A 1 429  ? 42.526 66.472  -7.470  1.00 11.55 ? 429  ASP A CG  1 
ATOM   3393 O  OD1 . ASP A 1 429  ? 43.066 66.257  -6.369  1.00 12.67 ? 429  ASP A OD1 1 
ATOM   3394 O  OD2 . ASP A 1 429  ? 42.227 65.585  -8.316  1.00 11.61 ? 429  ASP A OD2 1 
ATOM   3395 N  N   . ARG A 1 430  ? 43.468 67.934  -10.618 1.00 10.79 ? 430  ARG A N   1 
ATOM   3396 C  CA  . ARG A 1 430  ? 43.906 67.147  -11.749 1.00 10.33 ? 430  ARG A CA  1 
ATOM   3397 C  C   . ARG A 1 430  ? 45.202 67.684  -12.298 1.00 10.57 ? 430  ARG A C   1 
ATOM   3398 O  O   . ARG A 1 430  ? 46.032 66.901  -12.786 1.00 11.35 ? 430  ARG A O   1 
ATOM   3399 C  CB  . ARG A 1 430  ? 42.816 67.184  -12.840 1.00 11.14 ? 430  ARG A CB  1 
ATOM   3400 C  CG  . ARG A 1 430  ? 41.532 66.441  -12.441 1.00 11.56 ? 430  ARG A CG  1 
ATOM   3401 C  CD  . ARG A 1 430  ? 41.814 65.024  -11.976 1.00 10.05 ? 430  ARG A CD  1 
ATOM   3402 N  NE  . ARG A 1 430  ? 40.572 64.273  -12.008 1.00 11.16 ? 430  ARG A NE  1 
ATOM   3403 C  CZ  . ARG A 1 430  ? 39.861 63.931  -10.937 1.00 11.09 ? 430  ARG A CZ  1 
ATOM   3404 N  NH1 . ARG A 1 430  ? 40.271 64.264  -9.712  1.00 10.54 ? 430  ARG A NH1 1 
ATOM   3405 N  NH2 . ARG A 1 430  ? 38.727 63.236  -11.068 1.00 11.82 ? 430  ARG A NH2 1 
ATOM   3406 N  N   . VAL A 1 431  ? 45.389 69.007  -12.269 1.00 11.11 ? 431  VAL A N   1 
ATOM   3407 C  CA  . VAL A 1 431  ? 46.663 69.579  -12.728 1.00 10.44 ? 431  VAL A CA  1 
ATOM   3408 C  C   . VAL A 1 431  ? 47.819 69.082  -11.826 1.00 12.39 ? 431  VAL A C   1 
ATOM   3409 O  O   . VAL A 1 431  ? 48.848 68.600  -12.296 1.00 12.99 ? 431  VAL A O   1 
ATOM   3410 C  CB  . VAL A 1 431  ? 46.549 71.103  -12.709 1.00 11.26 ? 431  VAL A CB  1 
ATOM   3411 C  CG1 . VAL A 1 431  ? 47.909 71.743  -13.055 1.00 13.39 ? 431  VAL A CG1 1 
ATOM   3412 C  CG2 . VAL A 1 431  ? 45.459 71.556  -13.751 1.00 11.69 ? 431  VAL A CG2 1 
ATOM   3413 N  N   . LEU A 1 432  ? 47.617 69.175  -10.520 1.00 10.68 ? 432  LEU A N   1 
ATOM   3414 C  CA  . LEU A 1 432  ? 48.671 68.761  -9.595  1.00 11.41 ? 432  LEU A CA  1 
ATOM   3415 C  C   . LEU A 1 432  ? 48.861 67.249  -9.670  1.00 11.18 ? 432  LEU A C   1 
ATOM   3416 O  O   . LEU A 1 432  ? 50.002 66.760  -9.537  1.00 11.78 ? 432  LEU A O   1 
ATOM   3417 C  CB  . LEU A 1 432  ? 48.330 69.206  -8.176  1.00 12.13 ? 432  LEU A CB  1 
ATOM   3418 C  CG  . LEU A 1 432  ? 49.367 68.847  -7.084  1.00 13.32 ? 432  LEU A CG  1 
ATOM   3419 C  CD1 . LEU A 1 432  ? 50.782 69.379  -7.431  1.00 12.29 ? 432  LEU A CD1 1 
ATOM   3420 C  CD2 . LEU A 1 432  ? 48.886 69.449  -5.751  1.00 12.18 ? 432  LEU A CD2 1 
ATOM   3421 N  N   . MET A 1 433  ? 47.769 66.480  -9.892  1.00 9.80  ? 433  MET A N   1 
ATOM   3422 C  CA  . MET A 1 433  ? 47.936 65.048  -10.063 1.00 10.56 ? 433  MET A CA  1 
ATOM   3423 C  C   . MET A 1 433  ? 48.997 64.746  -11.128 1.00 10.69 ? 433  MET A C   1 
ATOM   3424 O  O   . MET A 1 433  ? 49.866 63.883  -10.956 1.00 10.88 ? 433  MET A O   1 
ATOM   3425 C  CB  . MET A 1 433  ? 46.616 64.453  -10.524 1.00 10.94 ? 433  MET A CB  1 
ATOM   3426 C  CG  . MET A 1 433  ? 46.690 62.978  -10.786 1.00 10.45 ? 433  MET A CG  1 
ATOM   3427 S  SD  . MET A 1 433  ? 45.142 62.284  -11.497 1.00 13.25 ? 433  MET A SD  1 
ATOM   3428 C  CE  . MET A 1 433  ? 45.276 62.957  -13.148 1.00 15.16 ? 433  MET A CE  1 
ATOM   3429 N  N   . HIS A 1 434  ? 48.878 65.418  -12.254 1.00 10.65 ? 434  HIS A N   1 
ATOM   3430 C  CA  . HIS A 1 434  ? 49.801 65.192  -13.340 1.00 11.26 ? 434  HIS A CA  1 
ATOM   3431 C  C   . HIS A 1 434  ? 51.198 65.727  -13.048 1.00 12.21 ? 434  HIS A C   1 
ATOM   3432 O  O   . HIS A 1 434  ? 52.192 65.078  -13.405 1.00 11.66 ? 434  HIS A O   1 
ATOM   3433 C  CB  . HIS A 1 434  ? 49.274 65.880  -14.590 1.00 12.43 ? 434  HIS A CB  1 
ATOM   3434 C  CG  . HIS A 1 434  ? 50.246 65.818  -15.729 1.00 10.25 ? 434  HIS A CG  1 
ATOM   3435 N  ND1 . HIS A 1 434  ? 51.053 66.884  -16.101 1.00 14.24 ? 434  HIS A ND1 1 
ATOM   3436 C  CD2 . HIS A 1 434  ? 50.653 64.751  -16.446 1.00 10.04 ? 434  HIS A CD2 1 
ATOM   3437 C  CE1 . HIS A 1 434  ? 51.919 66.456  -17.017 1.00 10.27 ? 434  HIS A CE1 1 
ATOM   3438 N  NE2 . HIS A 1 434  ? 51.698 65.172  -17.227 1.00 13.72 ? 434  HIS A NE2 1 
ATOM   3439 N  N   . TYR A 1 435  ? 51.282 66.884  -12.400 1.00 11.13 ? 435  TYR A N   1 
ATOM   3440 C  CA  . TYR A 1 435  ? 52.596 67.453  -12.084 1.00 11.92 ? 435  TYR A CA  1 
ATOM   3441 C  C   . TYR A 1 435  ? 53.351 66.535  -11.114 1.00 11.82 ? 435  TYR A C   1 
ATOM   3442 O  O   . TYR A 1 435  ? 54.553 66.366  -11.248 1.00 12.81 ? 435  TYR A O   1 
ATOM   3443 C  CB  A TYR A 1 435  ? 52.483 68.862  -11.449 0.50 12.89 ? 435  TYR A CB  1 
ATOM   3444 C  CB  B TYR A 1 435  ? 52.573 68.904  -11.771 0.50 12.29 ? 435  TYR A CB  1 
ATOM   3445 C  CG  A TYR A 1 435  ? 52.402 70.001  -12.436 0.50 16.52 ? 435  TYR A CG  1 
ATOM   3446 C  CG  B TYR A 1 435  ? 52.454 69.754  -13.024 0.50 14.04 ? 435  TYR A CG  1 
ATOM   3447 C  CD1 A TYR A 1 435  ? 51.443 70.010  -13.444 0.50 14.79 ? 435  TYR A CD1 1 
ATOM   3448 C  CD1 B TYR A 1 435  ? 53.465 69.741  -13.993 0.50 17.83 ? 435  TYR A CD1 1 
ATOM   3449 C  CD2 A TYR A 1 435  ? 53.245 71.102  -12.317 0.50 19.01 ? 435  TYR A CD2 1 
ATOM   3450 C  CD2 B TYR A 1 435  ? 51.336 70.551  -13.255 0.50 15.52 ? 435  TYR A CD2 1 
ATOM   3451 C  CE1 A TYR A 1 435  ? 51.318 71.092  -14.310 0.50 17.17 ? 435  TYR A CE1 1 
ATOM   3452 C  CE1 B TYR A 1 435  ? 53.363 70.509  -15.161 0.50 19.10 ? 435  TYR A CE1 1 
ATOM   3453 C  CE2 A TYR A 1 435  ? 53.132 72.190  -13.179 0.50 19.33 ? 435  TYR A CE2 1 
ATOM   3454 C  CE2 B TYR A 1 435  ? 51.229 71.321  -14.415 0.50 16.20 ? 435  TYR A CE2 1 
ATOM   3455 C  CZ  A TYR A 1 435  ? 52.166 72.175  -14.172 0.50 17.45 ? 435  TYR A CZ  1 
ATOM   3456 C  CZ  B TYR A 1 435  ? 52.247 71.297  -15.362 0.50 18.57 ? 435  TYR A CZ  1 
ATOM   3457 O  OH  A TYR A 1 435  ? 52.063 73.237  -15.043 0.50 21.96 ? 435  TYR A OH  1 
ATOM   3458 O  OH  B TYR A 1 435  ? 52.159 72.083  -16.500 0.50 17.39 ? 435  TYR A OH  1 
ATOM   3459 N  N   . VAL A 1 436  ? 52.648 65.948  -10.149 1.00 10.65 ? 436  VAL A N   1 
ATOM   3460 C  CA  . VAL A 1 436  ? 53.318 65.058  -9.203  1.00 11.14 ? 436  VAL A CA  1 
ATOM   3461 C  C   . VAL A 1 436  ? 53.822 63.840  -9.999  1.00 11.45 ? 436  VAL A C   1 
ATOM   3462 O  O   . VAL A 1 436  ? 54.969 63.401  -9.807  1.00 11.13 ? 436  VAL A O   1 
ATOM   3463 C  CB  . VAL A 1 436  ? 52.336 64.614  -8.064  1.00 12.15 ? 436  VAL A CB  1 
ATOM   3464 C  CG1 . VAL A 1 436  ? 52.854 63.366  -7.304  1.00 11.81 ? 436  VAL A CG1 1 
ATOM   3465 C  CG2 . VAL A 1 436  ? 52.176 65.770  -7.079  1.00 11.78 ? 436  VAL A CG2 1 
ATOM   3466 N  N   . ARG A 1 437  ? 52.982 63.249  -10.864 1.00 11.29 ? 437  ARG A N   1 
ATOM   3467 C  CA  . ARG A 1 437  ? 53.467 62.107  -11.621 1.00 11.15 ? 437  ARG A CA  1 
ATOM   3468 C  C   . ARG A 1 437  ? 54.703 62.474  -12.441 1.00 11.98 ? 437  ARG A C   1 
ATOM   3469 O  O   . ARG A 1 437  ? 55.690 61.719  -12.474 1.00 12.22 ? 437  ARG A O   1 
ATOM   3470 C  CB  . ARG A 1 437  ? 52.380 61.563  -12.550 1.00 11.82 ? 437  ARG A CB  1 
ATOM   3471 C  CG  . ARG A 1 437  ? 52.915 60.606  -13.610 1.00 12.77 ? 437  ARG A CG  1 
ATOM   3472 C  CD  . ARG A 1 437  ? 51.779 60.101  -14.470 1.00 11.86 ? 437  ARG A CD  1 
ATOM   3473 N  NE  . ARG A 1 437  ? 52.269 59.423  -15.679 1.00 10.70 ? 437  ARG A NE  1 
ATOM   3474 C  CZ  . ARG A 1 437  ? 51.520 58.592  -16.404 1.00 12.44 ? 437  ARG A CZ  1 
ATOM   3475 N  NH1 . ARG A 1 437  ? 50.253 58.295  -16.066 1.00 13.92 ? 437  ARG A NH1 1 
ATOM   3476 N  NH2 . ARG A 1 437  ? 52.082 58.026  -17.461 1.00 13.70 ? 437  ARG A NH2 1 
ATOM   3477 N  N   . ALA A 1 438  ? 54.624 63.603  -13.162 1.00 11.22 ? 438  ALA A N   1 
ATOM   3478 C  CA  . ALA A 1 438  ? 55.740 64.018  -14.025 1.00 10.83 ? 438  ALA A CA  1 
ATOM   3479 C  C   . ALA A 1 438  ? 57.032 64.336  -13.231 1.00 11.47 ? 438  ALA A C   1 
ATOM   3480 O  O   . ALA A 1 438  ? 58.135 63.957  -13.682 1.00 11.85 ? 438  ALA A O   1 
ATOM   3481 C  CB  . ALA A 1 438  ? 55.339 65.188  -14.875 1.00 11.72 ? 438  ALA A CB  1 
ATOM   3482 N  N   . ALA A 1 439  ? 56.900 64.969  -12.065 1.00 11.54 ? 439  ALA A N   1 
ATOM   3483 C  CA  . ALA A 1 439  ? 58.054 65.282  -11.238 1.00 11.77 ? 439  ALA A CA  1 
ATOM   3484 C  C   . ALA A 1 439  ? 58.680 63.990  -10.695 1.00 12.06 ? 439  ALA A C   1 
ATOM   3485 O  O   . ALA A 1 439  ? 59.924 63.832  -10.699 1.00 12.39 ? 439  ALA A O   1 
ATOM   3486 C  CB  . ALA A 1 439  ? 57.630 66.156  -10.119 1.00 11.93 ? 439  ALA A CB  1 
ATOM   3487 N  N   . GLU A 1 440  ? 57.840 63.061  -10.228 1.00 10.09 ? 440  GLU A N   1 
ATOM   3488 C  CA  . GLU A 1 440  ? 58.421 61.817  -9.716  1.00 10.27 ? 440  GLU A CA  1 
ATOM   3489 C  C   . GLU A 1 440  ? 59.077 61.014  -10.834 1.00 11.05 ? 440  GLU A C   1 
ATOM   3490 O  O   . GLU A 1 440  ? 60.117 60.405  -10.617 1.00 12.86 ? 440  GLU A O   1 
ATOM   3491 C  CB  . GLU A 1 440  ? 57.368 60.951  -9.022  1.00 11.16 ? 440  GLU A CB  1 
ATOM   3492 C  CG  . GLU A 1 440  ? 56.832 61.614  -7.765  1.00 13.12 ? 440  GLU A CG  1 
ATOM   3493 C  CD  . GLU A 1 440  ? 56.134 60.634  -6.826  1.00 16.61 ? 440  GLU A CD  1 
ATOM   3494 O  OE1 . GLU A 1 440  ? 55.030 60.165  -7.104  1.00 15.63 ? 440  GLU A OE1 1 
ATOM   3495 O  OE2 . GLU A 1 440  ? 56.749 60.304  -5.799  1.00 16.48 ? 440  GLU A OE2 1 
ATOM   3496 N  N   . MET A 1 441  ? 58.466 60.983  -12.014 1.00 11.96 ? 441  MET A N   1 
ATOM   3497 C  CA  . MET A 1 441  ? 59.044 60.215  -13.095 1.00 11.53 ? 441  MET A CA  1 
ATOM   3498 C  C   . MET A 1 441  ? 60.329 60.859  -13.643 1.00 12.58 ? 441  MET A C   1 
ATOM   3499 O  O   . MET A 1 441  ? 61.348 60.179  -13.774 1.00 13.08 ? 441  MET A O   1 
ATOM   3500 C  CB  . MET A 1 441  ? 57.998 60.100  -14.221 1.00 11.73 ? 441  MET A CB  1 
ATOM   3501 C  CG  . MET A 1 441  ? 58.495 59.323  -15.431 1.00 10.89 ? 441  MET A CG  1 
ATOM   3502 S  SD  . MET A 1 441  ? 57.220 59.098  -16.719 1.00 12.31 ? 441  MET A SD  1 
ATOM   3503 C  CE  . MET A 1 441  ? 56.094 57.968  -15.877 1.00 13.44 ? 441  MET A CE  1 
ATOM   3504 N  N   . LEU A 1 442  ? 60.290 62.152  -13.928 1.00 12.64 ? 442  LEU A N   1 
ATOM   3505 C  CA  . LEU A 1 442  ? 61.484 62.832  -14.456 1.00 12.66 ? 442  LEU A CA  1 
ATOM   3506 C  C   . LEU A 1 442  ? 62.702 62.726  -13.555 1.00 13.80 ? 442  LEU A C   1 
ATOM   3507 O  O   . LEU A 1 442  ? 63.803 62.480  -14.053 1.00 13.53 ? 442  LEU A O   1 
ATOM   3508 C  CB  . LEU A 1 442  ? 61.238 64.316  -14.748 1.00 12.83 ? 442  LEU A CB  1 
ATOM   3509 C  CG  . LEU A 1 442  ? 60.586 64.538  -16.118 1.00 11.57 ? 442  LEU A CG  1 
ATOM   3510 C  CD1 . LEU A 1 442  ? 59.997 65.911  -16.171 1.00 13.04 ? 442  LEU A CD1 1 
ATOM   3511 C  CD2 . LEU A 1 442  ? 61.669 64.385  -17.209 1.00 14.67 ? 442  LEU A CD2 1 
ATOM   3512 N  N   . SER A 1 443  ? 62.493 62.822  -12.241 1.00 12.29 ? 443  SER A N   1 
ATOM   3513 C  CA  . SER A 1 443  ? 63.603 62.740  -11.307 1.00 13.64 ? 443  SER A CA  1 
ATOM   3514 C  C   . SER A 1 443  ? 63.974 61.322  -10.938 1.00 13.33 ? 443  SER A C   1 
ATOM   3515 O  O   . SER A 1 443  ? 65.070 61.117  -10.417 1.00 15.71 ? 443  SER A O   1 
ATOM   3516 C  CB  . SER A 1 443  ? 63.336 63.531  -10.045 1.00 12.49 ? 443  SER A CB  1 
ATOM   3517 O  OG  . SER A 1 443  ? 62.232 62.990  -9.315  1.00 13.58 ? 443  SER A OG  1 
ATOM   3518 N  N   . ALA A 1 444  ? 63.136 60.344  -11.275 1.00 11.39 ? 444  ALA A N   1 
ATOM   3519 C  CA  . ALA A 1 444  ? 63.451 58.950  -10.948 1.00 12.51 ? 444  ALA A CA  1 
ATOM   3520 C  C   . ALA A 1 444  ? 64.619 58.398  -11.743 1.00 13.27 ? 444  ALA A C   1 
ATOM   3521 O  O   . ALA A 1 444  ? 65.229 57.422  -11.323 1.00 15.15 ? 444  ALA A O   1 
ATOM   3522 C  CB  . ALA A 1 444  ? 62.224 58.030  -11.191 1.00 13.65 ? 444  ALA A CB  1 
ATOM   3523 N  N   . TRP A 1 445  ? 64.892 58.966  -12.905 1.00 14.19 ? 445  TRP A N   1 
ATOM   3524 C  CA  . TRP A 1 445  ? 65.943 58.410  -13.777 1.00 14.76 ? 445  TRP A CA  1 
ATOM   3525 C  C   . TRP A 1 445  ? 67.320 58.474  -13.149 1.00 15.62 ? 445  TRP A C   1 
ATOM   3526 O  O   . TRP A 1 445  ? 68.192 57.705  -13.547 1.00 17.40 ? 445  TRP A O   1 
ATOM   3527 C  CB  . TRP A 1 445  ? 65.978 59.145  -15.118 1.00 14.01 ? 445  TRP A CB  1 
ATOM   3528 C  CG  . TRP A 1 445  ? 64.690 58.966  -15.899 1.00 11.69 ? 445  TRP A CG  1 
ATOM   3529 C  CD1 . TRP A 1 445  ? 63.683 59.901  -16.047 1.00 13.07 ? 445  TRP A CD1 1 
ATOM   3530 C  CD2 . TRP A 1 445  ? 64.225 57.784  -16.570 1.00 13.04 ? 445  TRP A CD2 1 
ATOM   3531 N  NE1 . TRP A 1 445  ? 62.652 59.376  -16.752 1.00 12.70 ? 445  TRP A NE1 1 
ATOM   3532 C  CE2 . TRP A 1 445  ? 62.936 58.080  -17.083 1.00 12.50 ? 445  TRP A CE2 1 
ATOM   3533 C  CE3 . TRP A 1 445  ? 64.763 56.508  -16.781 1.00 13.18 ? 445  TRP A CE3 1 
ATOM   3534 C  CZ2 . TRP A 1 445  ? 62.179 57.150  -17.785 1.00 12.92 ? 445  TRP A CZ2 1 
ATOM   3535 C  CZ3 . TRP A 1 445  ? 64.011 55.576  -17.489 1.00 14.05 ? 445  TRP A CZ3 1 
ATOM   3536 C  CH2 . TRP A 1 445  ? 62.731 55.899  -17.983 1.00 15.07 ? 445  TRP A CH2 1 
ATOM   3537 N  N   . HIS A 1 446  ? 67.512 59.410  -12.232 1.00 15.92 ? 446  HIS A N   1 
ATOM   3538 C  CA  . HIS A 1 446  ? 68.796 59.546  -11.584 1.00 17.92 ? 446  HIS A CA  1 
ATOM   3539 C  C   . HIS A 1 446  ? 68.686 59.485  -10.089 1.00 17.77 ? 446  HIS A C   1 
ATOM   3540 O  O   . HIS A 1 446  ? 67.619 59.646  -9.503  1.00 17.28 ? 446  HIS A O   1 
ATOM   3541 C  CB  . HIS A 1 446  ? 69.404 60.915  -11.835 1.00 19.61 ? 446  HIS A CB  1 
ATOM   3542 C  CG  . HIS A 1 446  ? 69.869 61.137  -13.235 1.00 21.05 ? 446  HIS A CG  1 
ATOM   3543 N  ND1 . HIS A 1 446  ? 69.124 61.826  -14.166 1.00 22.50 ? 446  HIS A ND1 1 
ATOM   3544 C  CD2 . HIS A 1 446  ? 71.025 60.791  -13.856 1.00 25.35 ? 446  HIS A CD2 1 
ATOM   3545 C  CE1 . HIS A 1 446  ? 69.798 61.899  -15.301 1.00 25.20 ? 446  HIS A CE1 1 
ATOM   3546 N  NE2 . HIS A 1 446  ? 70.950 61.279  -15.140 1.00 26.11 ? 446  HIS A NE2 1 
ATOM   3547 N  N   . SER A 1 447  ? 69.837 59.263  -9.464  1.00 17.83 ? 447  SER A N   1 
ATOM   3548 C  CA  . SER A 1 447  ? 69.956 59.301  -8.024  1.00 16.33 ? 447  SER A CA  1 
ATOM   3549 C  C   . SER A 1 447  ? 70.436 60.739  -7.808  1.00 17.75 ? 447  SER A C   1 
ATOM   3550 O  O   . SER A 1 447  ? 71.242 61.256  -8.609  1.00 19.05 ? 447  SER A O   1 
ATOM   3551 C  CB  . SER A 1 447  ? 71.004 58.301  -7.551  1.00 18.78 ? 447  SER A CB  1 
ATOM   3552 O  OG  A SER A 1 447  ? 71.159 58.407  -6.154  0.50 18.40 ? 447  SER A OG  1 
ATOM   3553 O  OG  B SER A 1 447  ? 70.654 57.584  -6.460  0.50 22.79 ? 447  SER A OG  1 
ATOM   3554 N  N   . TRP A 1 448  ? 69.908 61.419  -6.796  1.00 15.83 ? 448  TRP A N   1 
ATOM   3555 C  CA  . TRP A 1 448  ? 70.263 62.804  -6.532  1.00 16.65 ? 448  TRP A CA  1 
ATOM   3556 C  C   . TRP A 1 448  ? 70.946 63.023  -5.211  1.00 18.55 ? 448  TRP A C   1 
ATOM   3557 O  O   . TRP A 1 448  ? 70.619 62.394  -4.227  1.00 20.99 ? 448  TRP A O   1 
ATOM   3558 C  CB  . TRP A 1 448  ? 69.023 63.728  -6.572  1.00 16.09 ? 448  TRP A CB  1 
ATOM   3559 C  CG  . TRP A 1 448  ? 68.345 63.738  -7.934  1.00 16.29 ? 448  TRP A CG  1 
ATOM   3560 C  CD1 . TRP A 1 448  ? 67.510 62.794  -8.446  1.00 15.80 ? 448  TRP A CD1 1 
ATOM   3561 C  CD2 . TRP A 1 448  ? 68.494 64.742  -8.935  1.00 15.63 ? 448  TRP A CD2 1 
ATOM   3562 N  NE1 . TRP A 1 448  ? 67.120 63.147  -9.734  1.00 14.86 ? 448  TRP A NE1 1 
ATOM   3563 C  CE2 . TRP A 1 448  ? 67.710 64.344  -10.041 1.00 14.28 ? 448  TRP A CE2 1 
ATOM   3564 C  CE3 . TRP A 1 448  ? 69.217 65.949  -9.003  1.00 17.17 ? 448  TRP A CE3 1 
ATOM   3565 C  CZ2 . TRP A 1 448  ? 67.624 65.098  -11.192 1.00 16.60 ? 448  TRP A CZ2 1 
ATOM   3566 C  CZ3 . TRP A 1 448  ? 69.126 66.716  -10.184 1.00 15.28 ? 448  TRP A CZ3 1 
ATOM   3567 C  CH2 . TRP A 1 448  ? 68.328 66.264  -11.258 1.00 16.32 ? 448  TRP A CH2 1 
ATOM   3568 N  N   . ASP A 1 449  ? 71.890 63.949  -5.211  1.00 21.65 ? 449  ASP A N   1 
ATOM   3569 C  CA  . ASP A 1 449  ? 72.582 64.320  -3.993  1.00 23.82 ? 449  ASP A CA  1 
ATOM   3570 C  C   . ASP A 1 449  ? 71.559 64.946  -3.042  1.00 24.51 ? 449  ASP A C   1 
ATOM   3571 O  O   . ASP A 1 449  ? 70.646 65.645  -3.470  1.00 20.97 ? 449  ASP A O   1 
ATOM   3572 C  CB  . ASP A 1 449  ? 73.634 65.358  -4.336  1.00 28.31 ? 449  ASP A CB  1 
ATOM   3573 C  CG  . ASP A 1 449  ? 74.557 65.637  -3.192  1.00 31.18 ? 449  ASP A CG  1 
ATOM   3574 O  OD1 . ASP A 1 449  ? 74.217 66.450  -2.312  1.00 33.37 ? 449  ASP A OD1 1 
ATOM   3575 O  OD2 . ASP A 1 449  ? 75.633 65.004  -3.183  1.00 38.77 ? 449  ASP A OD2 1 
ATOM   3576 N  N   . GLY A 1 450  ? 71.738 64.724  -1.748  1.00 22.27 ? 450  GLY A N   1 
ATOM   3577 C  CA  . GLY A 1 450  ? 70.828 65.307  -0.771  1.00 22.95 ? 450  GLY A CA  1 
ATOM   3578 C  C   . GLY A 1 450  ? 70.701 66.805  -0.899  1.00 23.91 ? 450  GLY A C   1 
ATOM   3579 O  O   . GLY A 1 450  ? 69.644 67.378  -0.585  1.00 24.59 ? 450  GLY A O   1 
ATOM   3580 N  N   . MET A 1 451  ? 71.774 67.462  -1.357  1.00 21.70 ? 451  MET A N   1 
ATOM   3581 C  CA  . MET A 1 451  ? 71.751 68.910  -1.507  1.00 23.76 ? 451  MET A CA  1 
ATOM   3582 C  C   . MET A 1 451  ? 70.772 69.404  -2.560  1.00 20.55 ? 451  MET A C   1 
ATOM   3583 O  O   . MET A 1 451  ? 70.391 70.576  -2.550  1.00 23.66 ? 451  MET A O   1 
ATOM   3584 C  CB  . MET A 1 451  ? 73.145 69.436  -1.869  1.00 28.61 ? 451  MET A CB  1 
ATOM   3585 C  CG  . MET A 1 451  ? 74.161 69.334  -0.764  1.00 37.57 ? 451  MET A CG  1 
ATOM   3586 S  SD  . MET A 1 451  ? 73.666 70.249  0.745   1.00 49.88 ? 451  MET A SD  1 
ATOM   3587 C  CE  . MET A 1 451  ? 73.044 68.847  1.816   1.00 46.21 ? 451  MET A CE  1 
ATOM   3588 N  N   . ALA A 1 452  ? 70.373 68.517  -3.476  1.00 18.55 ? 452  ALA A N   1 
ATOM   3589 C  CA  . ALA A 1 452  ? 69.425 68.918  -4.517  1.00 18.05 ? 452  ALA A CA  1 
ATOM   3590 C  C   . ALA A 1 452  ? 68.003 69.054  -3.985  1.00 19.23 ? 452  ALA A C   1 
ATOM   3591 O  O   . ALA A 1 452  ? 67.137 69.582  -4.684  1.00 20.21 ? 452  ALA A O   1 
ATOM   3592 C  CB  . ALA A 1 452  ? 69.435 67.917  -5.657  1.00 17.13 ? 452  ALA A CB  1 
ATOM   3593 N  N   . ARG A 1 453  ? 67.762 68.542  -2.776  1.00 17.99 ? 453  ARG A N   1 
ATOM   3594 C  CA  . ARG A 1 453  ? 66.439 68.632  -2.142  1.00 20.41 ? 453  ARG A CA  1 
ATOM   3595 C  C   . ARG A 1 453  ? 65.309 68.049  -3.001  1.00 18.88 ? 453  ARG A C   1 
ATOM   3596 O  O   . ARG A 1 453  ? 64.181 68.520  -2.922  1.00 19.33 ? 453  ARG A O   1 
ATOM   3597 C  CB  . ARG A 1 453  ? 66.131 70.087  -1.810  1.00 20.93 ? 453  ARG A CB  1 
ATOM   3598 C  CG  . ARG A 1 453  ? 67.207 70.699  -0.901  1.00 22.48 ? 453  ARG A CG  1 
ATOM   3599 C  CD  . ARG A 1 453  ? 66.969 72.196  -0.681  1.00 25.72 ? 453  ARG A CD  1 
ATOM   3600 N  NE  . ARG A 1 453  ? 65.803 72.466  0.157   1.00 26.68 ? 453  ARG A NE  1 
ATOM   3601 C  CZ  . ARG A 1 453  ? 65.342 73.697  0.377   1.00 30.15 ? 453  ARG A CZ  1 
ATOM   3602 N  NH1 . ARG A 1 453  ? 65.961 74.752  -0.188  1.00 29.45 ? 453  ARG A NH1 1 
ATOM   3603 N  NH2 . ARG A 1 453  ? 64.274 73.874  1.150   1.00 32.23 ? 453  ARG A NH2 1 
ATOM   3604 N  N   . ILE A 1 454  ? 65.620 67.034  -3.794  1.00 15.82 ? 454  ILE A N   1 
ATOM   3605 C  CA  . ILE A 1 454  ? 64.613 66.413  -4.639  1.00 14.63 ? 454  ILE A CA  1 
ATOM   3606 C  C   . ILE A 1 454  ? 63.591 65.643  -3.781  1.00 16.97 ? 454  ILE A C   1 
ATOM   3607 O  O   . ILE A 1 454  ? 62.393 65.876  -3.911  1.00 15.40 ? 454  ILE A O   1 
ATOM   3608 C  CB  . ILE A 1 454  ? 65.272 65.468  -5.675  1.00 14.84 ? 454  ILE A CB  1 
ATOM   3609 C  CG1 . ILE A 1 454  ? 66.221 66.274  -6.587  1.00 16.60 ? 454  ILE A CG1 1 
ATOM   3610 C  CG2 . ILE A 1 454  ? 64.202 64.629  -6.395  1.00 15.60 ? 454  ILE A CG2 1 
ATOM   3611 C  CD1 . ILE A 1 454  ? 65.556 67.384  -7.400  1.00 17.98 ? 454  ILE A CD1 1 
ATOM   3612 N  N   . GLU A 1 455  ? 64.063 64.775  -2.887  1.00 15.41 ? 455  GLU A N   1 
ATOM   3613 C  CA  . GLU A 1 455  ? 63.140 64.002  -2.044  1.00 16.21 ? 455  GLU A CA  1 
ATOM   3614 C  C   . GLU A 1 455  ? 62.278 64.927  -1.210  1.00 16.18 ? 455  GLU A C   1 
ATOM   3615 O  O   . GLU A 1 455  ? 61.080 64.676  -1.027  1.00 15.99 ? 455  GLU A O   1 
ATOM   3616 C  CB  . GLU A 1 455  ? 63.913 63.042  -1.125  1.00 15.88 ? 455  GLU A CB  1 
ATOM   3617 C  CG  . GLU A 1 455  ? 64.514 61.829  -1.838  1.00 18.34 ? 455  GLU A CG  1 
ATOM   3618 C  CD  . GLU A 1 455  ? 65.887 62.124  -2.481  1.00 18.18 ? 455  GLU A CD  1 
ATOM   3619 O  OE1 . GLU A 1 455  ? 66.334 63.291  -2.400  1.00 19.51 ? 455  GLU A OE1 1 
ATOM   3620 O  OE2 . GLU A 1 455  ? 66.461 61.175  -3.038  1.00 18.56 ? 455  GLU A OE2 1 
ATOM   3621 N  N   . GLU A 1 456  ? 62.884 65.979  -0.681  1.00 16.30 ? 456  GLU A N   1 
ATOM   3622 C  CA  . GLU A 1 456  ? 62.179 66.933  0.143   1.00 15.01 ? 456  GLU A CA  1 
ATOM   3623 C  C   . GLU A 1 456  ? 61.011 67.575  -0.619  1.00 15.80 ? 456  GLU A C   1 
ATOM   3624 O  O   . GLU A 1 456  ? 59.887 67.629  -0.132  1.00 15.23 ? 456  GLU A O   1 
ATOM   3625 C  CB  . GLU A 1 456  ? 63.177 68.017  0.623   1.00 19.04 ? 456  GLU A CB  1 
ATOM   3626 C  CG  . GLU A 1 456  ? 62.546 69.149  1.392   1.00 21.07 ? 456  GLU A CG  1 
ATOM   3627 C  CD  . GLU A 1 456  ? 63.477 70.342  1.629   1.00 29.12 ? 456  GLU A CD  1 
ATOM   3628 O  OE1 . GLU A 1 456  ? 64.712 70.208  1.444   1.00 29.87 ? 456  GLU A OE1 1 
ATOM   3629 O  OE2 . GLU A 1 456  ? 62.962 71.420  2.020   1.00 28.97 ? 456  GLU A OE2 1 
ATOM   3630 N  N   . ARG A 1 457  ? 61.281 68.071  -1.828  1.00 14.86 ? 457  ARG A N   1 
ATOM   3631 C  CA  . ARG A 1 457  ? 60.214 68.742  -2.602  1.00 12.93 ? 457  ARG A CA  1 
ATOM   3632 C  C   . ARG A 1 457  ? 59.149 67.745  -3.051  1.00 14.15 ? 457  ARG A C   1 
ATOM   3633 O  O   . ARG A 1 457  ? 57.969 68.092  -3.037  1.00 14.36 ? 457  ARG A O   1 
ATOM   3634 C  CB  . ARG A 1 457  ? 60.843 69.483  -3.811  1.00 13.93 ? 457  ARG A CB  1 
ATOM   3635 C  CG  . ARG A 1 457  ? 61.165 70.952  -3.568  1.00 17.45 ? 457  ARG A CG  1 
ATOM   3636 C  CD  . ARG A 1 457  ? 62.154 71.166  -2.468  1.00 19.10 ? 457  ARG A CD  1 
ATOM   3637 N  NE  . ARG A 1 457  ? 62.384 72.598  -2.179  1.00 20.66 ? 457  ARG A NE  1 
ATOM   3638 C  CZ  . ARG A 1 457  ? 63.305 73.346  -2.792  1.00 23.45 ? 457  ARG A CZ  1 
ATOM   3639 N  NH1 . ARG A 1 457  ? 64.093 72.823  -3.735  1.00 21.00 ? 457  ARG A NH1 1 
ATOM   3640 N  NH2 . ARG A 1 457  ? 63.463 74.623  -2.445  1.00 26.40 ? 457  ARG A NH2 1 
ATOM   3641 N  N   . LEU A 1 458  ? 59.557 66.532  -3.407  1.00 12.84 ? 458  LEU A N   1 
ATOM   3642 C  CA  . LEU A 1 458  ? 58.564 65.531  -3.818  1.00 13.12 ? 458  LEU A CA  1 
ATOM   3643 C  C   . LEU A 1 458  ? 57.690 65.117  -2.651  1.00 14.27 ? 458  LEU A C   1 
ATOM   3644 O  O   . LEU A 1 458  ? 56.480 64.928  -2.841  1.00 13.82 ? 458  LEU A O   1 
ATOM   3645 C  CB  . LEU A 1 458  ? 59.244 64.317  -4.425  1.00 12.53 ? 458  LEU A CB  1 
ATOM   3646 C  CG  . LEU A 1 458  ? 59.935 64.625  -5.795  1.00 12.66 ? 458  LEU A CG  1 
ATOM   3647 C  CD1 . LEU A 1 458  ? 60.661 63.392  -6.224  1.00 16.02 ? 458  LEU A CD1 1 
ATOM   3648 C  CD2 . LEU A 1 458  ? 58.874 65.061  -6.910  1.00 14.77 ? 458  LEU A CD2 1 
ATOM   3649 N  N   . GLU A 1 459  ? 58.267 64.981  -1.442  1.00 12.57 ? 459  GLU A N   1 
ATOM   3650 C  CA  . GLU A 1 459  ? 57.431 64.592  -0.293  1.00 13.06 ? 459  GLU A CA  1 
ATOM   3651 C  C   . GLU A 1 459  ? 56.406 65.716  -0.011  1.00 13.88 ? 459  GLU A C   1 
ATOM   3652 O  O   . GLU A 1 459  ? 55.226 65.454  0.271   1.00 13.15 ? 459  GLU A O   1 
ATOM   3653 C  CB  . GLU A 1 459  ? 58.334 64.408  0.927   1.00 15.38 ? 459  GLU A CB  1 
ATOM   3654 C  CG  . GLU A 1 459  ? 57.551 64.026  2.196   1.00 18.17 ? 459  GLU A CG  1 
ATOM   3655 C  CD  . GLU A 1 459  ? 58.443 63.358  3.231   1.00 20.94 ? 459  GLU A CD  1 
ATOM   3656 O  OE1 . GLU A 1 459  ? 59.073 64.107  3.966   1.00 24.19 ? 459  GLU A OE1 1 
ATOM   3657 O  OE2 . GLU A 1 459  ? 58.531 62.110  3.290   1.00 25.55 ? 459  GLU A OE2 1 
ATOM   3658 N  N   . GLN A 1 460  ? 56.842 66.972  -0.098  1.00 12.27 ? 460  GLN A N   1 
ATOM   3659 C  CA  . GLN A 1 460  ? 55.926 68.071  0.128   1.00 12.90 ? 460  GLN A CA  1 
ATOM   3660 C  C   . GLN A 1 460  ? 54.776 68.003  -0.898  1.00 13.40 ? 460  GLN A C   1 
ATOM   3661 O  O   . GLN A 1 460  ? 53.601 68.091  -0.570  1.00 14.94 ? 460  GLN A O   1 
ATOM   3662 C  CB  . GLN A 1 460  ? 56.670 69.374  -0.052  1.00 15.95 ? 460  GLN A CB  1 
ATOM   3663 C  CG  . GLN A 1 460  ? 55.784 70.591  0.072   1.00 20.14 ? 460  GLN A CG  1 
ATOM   3664 C  CD  . GLN A 1 460  ? 56.566 71.885  -0.159  1.00 25.07 ? 460  GLN A CD  1 
ATOM   3665 O  OE1 . GLN A 1 460  ? 56.113 72.938  0.226   1.00 33.40 ? 460  GLN A OE1 1 
ATOM   3666 N  NE2 . GLN A 1 460  ? 57.708 71.796  -0.836  1.00 27.11 ? 460  GLN A NE2 1 
ATOM   3667 N  N   . ALA A 1 461  ? 55.149 67.819  -2.154  1.00 12.67 ? 461  ALA A N   1 
ATOM   3668 C  CA  . ALA A 1 461  ? 54.104 67.766  -3.173  1.00 12.82 ? 461  ALA A CA  1 
ATOM   3669 C  C   . ALA A 1 461  ? 53.124 66.614  -3.000  1.00 14.18 ? 461  ALA A C   1 
ATOM   3670 O  O   . ALA A 1 461  ? 51.915 66.819  -3.108  1.00 13.20 ? 461  ALA A O   1 
ATOM   3671 C  CB  . ALA A 1 461  ? 54.753 67.730  -4.573  1.00 13.94 ? 461  ALA A CB  1 
ATOM   3672 N  N   . ARG A 1 462  ? 53.641 65.419  -2.705  1.00 12.39 ? 462  ARG A N   1 
ATOM   3673 C  CA  . ARG A 1 462  ? 52.771 64.271  -2.518  1.00 11.67 ? 462  ARG A CA  1 
ATOM   3674 C  C   . ARG A 1 462  ? 51.852 64.517  -1.316  1.00 12.46 ? 462  ARG A C   1 
ATOM   3675 O  O   . ARG A 1 462  ? 50.674 64.157  -1.351  1.00 12.13 ? 462  ARG A O   1 
ATOM   3676 C  CB  . ARG A 1 462  ? 53.551 62.991  -2.228  1.00 11.92 ? 462  ARG A CB  1 
ATOM   3677 C  CG  . ARG A 1 462  ? 54.301 62.430  -3.461  1.00 11.82 ? 462  ARG A CG  1 
ATOM   3678 C  CD  . ARG A 1 462  ? 54.767 61.009  -3.219  1.00 11.90 ? 462  ARG A CD  1 
ATOM   3679 N  NE  . ARG A 1 462  ? 55.694 60.964  -2.057  1.00 11.69 ? 462  ARG A NE  1 
ATOM   3680 C  CZ  . ARG A 1 462  ? 57.017 61.103  -2.146  1.00 14.70 ? 462  ARG A CZ  1 
ATOM   3681 N  NH1 . ARG A 1 462  ? 57.635 61.269  -3.316  1.00 14.07 ? 462  ARG A NH1 1 
ATOM   3682 N  NH2 . ARG A 1 462  ? 57.761 61.119  -1.050  1.00 17.55 ? 462  ARG A NH2 1 
ATOM   3683 N  N   . ARG A 1 463  ? 52.380 65.145  -0.262  1.00 12.31 ? 463  ARG A N   1 
ATOM   3684 C  CA  . ARG A 1 463  ? 51.555 65.317  0.928   1.00 12.24 ? 463  ARG A CA  1 
ATOM   3685 C  C   . ARG A 1 463  ? 50.495 66.369  0.749   1.00 12.02 ? 463  ARG A C   1 
ATOM   3686 O  O   . ARG A 1 463  ? 49.379 66.182  1.269   1.00 13.13 ? 463  ARG A O   1 
ATOM   3687 C  CB  . ARG A 1 463  ? 52.441 65.607  2.156   1.00 12.42 ? 463  ARG A CB  1 
ATOM   3688 C  CG  . ARG A 1 463  ? 53.165 64.351  2.557   1.00 12.91 ? 463  ARG A CG  1 
ATOM   3689 C  CD  . ARG A 1 463  ? 54.184 64.574  3.652   1.00 15.21 ? 463  ARG A CD  1 
ATOM   3690 N  NE  . ARG A 1 463  ? 54.672 63.246  4.009   1.00 15.76 ? 463  ARG A NE  1 
ATOM   3691 C  CZ  . ARG A 1 463  ? 55.432 62.984  5.071   1.00 19.16 ? 463  ARG A CZ  1 
ATOM   3692 N  NH1 . ARG A 1 463  ? 55.798 63.975  5.848   1.00 19.72 ? 463  ARG A NH1 1 
ATOM   3693 N  NH2 . ARG A 1 463  ? 55.758 61.724  5.358   1.00 20.25 ? 463  ARG A NH2 1 
ATOM   3694 N  N   . GLU A 1 464  ? 50.762 67.450  0.010   1.00 12.12 ? 464  GLU A N   1 
ATOM   3695 C  CA  . GLU A 1 464  ? 49.716 68.455  -0.126  1.00 13.09 ? 464  GLU A CA  1 
ATOM   3696 C  C   . GLU A 1 464  ? 48.623 67.933  -1.053  1.00 12.85 ? 464  GLU A C   1 
ATOM   3697 O  O   . GLU A 1 464  ? 47.435 68.170  -0.801  1.00 13.67 ? 464  GLU A O   1 
ATOM   3698 C  CB  . GLU A 1 464  ? 50.251 69.803  -0.680  1.00 14.85 ? 464  GLU A CB  1 
ATOM   3699 C  CG  . GLU A 1 464  ? 51.462 70.390  0.115   1.00 18.04 ? 464  GLU A CG  1 
ATOM   3700 C  CD  . GLU A 1 464  ? 51.156 70.849  1.529   1.00 23.10 ? 464  GLU A CD  1 
ATOM   3701 O  OE1 . GLU A 1 464  ? 50.166 70.417  2.114   1.00 20.71 ? 464  GLU A OE1 1 
ATOM   3702 O  OE2 . GLU A 1 464  ? 51.963 71.648  2.067   1.00 25.93 ? 464  GLU A OE2 1 
ATOM   3703 N  N   . LEU A 1 465  ? 49.009 67.223  -2.115  1.00 12.63 ? 465  LEU A N   1 
ATOM   3704 C  CA  . LEU A 1 465  ? 47.965 66.665  -2.995  1.00 11.88 ? 465  LEU A CA  1 
ATOM   3705 C  C   . LEU A 1 465  ? 47.177 65.591  -2.206  1.00 12.04 ? 465  LEU A C   1 
ATOM   3706 O  O   . LEU A 1 465  ? 45.958 65.477  -2.331  1.00 12.11 ? 465  LEU A O   1 
ATOM   3707 C  CB  . LEU A 1 465  ? 48.612 66.013  -4.223  1.00 11.85 ? 465  LEU A CB  1 
ATOM   3708 C  CG  . LEU A 1 465  ? 47.634 65.377  -5.230  1.00 11.10 ? 465  LEU A CG  1 
ATOM   3709 C  CD1 . LEU A 1 465  ? 46.557 66.391  -5.710  1.00 11.80 ? 465  LEU A CD1 1 
ATOM   3710 C  CD2 . LEU A 1 465  ? 48.429 64.843  -6.437  1.00 13.23 ? 465  LEU A CD2 1 
ATOM   3711 N  N   . SER A 1 466  ? 47.889 64.777  -1.399  1.00 10.66 ? 466  SER A N   1 
ATOM   3712 C  CA  . SER A 1 466  ? 47.216 63.721  -0.643  1.00 10.06 ? 466  SER A CA  1 
ATOM   3713 C  C   . SER A 1 466  ? 46.212 64.321  0.361   1.00 10.46 ? 466  SER A C   1 
ATOM   3714 O  O   . SER A 1 466  ? 45.090 63.801  0.519   1.00 11.03 ? 466  SER A O   1 
ATOM   3715 C  CB  . SER A 1 466  ? 48.232 62.894  0.130   1.00 10.21 ? 466  SER A CB  1 
ATOM   3716 O  OG  . SER A 1 466  ? 48.990 62.081  -0.761  1.00 12.21 ? 466  SER A OG  1 
ATOM   3717 N  N   . LEU A 1 467  ? 46.617 65.411  1.021   1.00 10.38 ? 467  LEU A N   1 
ATOM   3718 C  CA  . LEU A 1 467  ? 45.755 66.079  1.983   1.00 11.72 ? 467  LEU A CA  1 
ATOM   3719 C  C   . LEU A 1 467  ? 44.453 66.526  1.288   1.00 10.54 ? 467  LEU A C   1 
ATOM   3720 O  O   . LEU A 1 467  ? 43.356 66.376  1.831   1.00 10.52 ? 467  LEU A O   1 
ATOM   3721 C  CB  . LEU A 1 467  ? 46.499 67.285  2.566   1.00 11.72 ? 467  LEU A CB  1 
ATOM   3722 C  CG  . LEU A 1 467  ? 45.629 68.064  3.570   1.00 15.86 ? 467  LEU A CG  1 
ATOM   3723 C  CD1 . LEU A 1 467  ? 45.407 67.269  4.822   1.00 22.27 ? 467  LEU A CD1 1 
ATOM   3724 C  CD2 . LEU A 1 467  ? 46.298 69.405  3.894   1.00 17.15 ? 467  LEU A CD2 1 
ATOM   3725 N  N   . PHE A 1 468  ? 44.578 67.003  0.051   1.00 10.82 ? 468  PHE A N   1 
ATOM   3726 C  CA  . PHE A 1 468  ? 43.400 67.536  -0.657  1.00 10.77 ? 468  PHE A CA  1 
ATOM   3727 C  C   . PHE A 1 468  ? 42.416 66.441  -1.036  1.00 10.14 ? 468  PHE A C   1 
ATOM   3728 O  O   . PHE A 1 468  ? 41.281 66.725  -1.363  1.00 12.09 ? 468  PHE A O   1 
ATOM   3729 C  CB  . PHE A 1 468  ? 43.821 68.329  -1.910  1.00 10.53 ? 468  PHE A CB  1 
ATOM   3730 C  CG  . PHE A 1 468  ? 42.697 69.176  -2.462  1.00 9.66  ? 468  PHE A CG  1 
ATOM   3731 C  CD1 . PHE A 1 468  ? 42.035 70.110  -1.680  1.00 11.69 ? 468  PHE A CD1 1 
ATOM   3732 C  CD2 . PHE A 1 468  ? 42.261 68.985  -3.779  1.00 10.00 ? 468  PHE A CD2 1 
ATOM   3733 C  CE1 . PHE A 1 468  ? 40.941 70.859  -2.173  1.00 11.53 ? 468  PHE A CE1 1 
ATOM   3734 C  CE2 . PHE A 1 468  ? 41.172 69.720  -4.293  1.00 10.30 ? 468  PHE A CE2 1 
ATOM   3735 C  CZ  . PHE A 1 468  ? 40.501 70.658  -3.497  1.00 11.69 ? 468  PHE A CZ  1 
ATOM   3736 N  N   . GLN A 1 469  ? 42.865 65.189  -1.028  1.00 9.16  ? 469  GLN A N   1 
ATOM   3737 C  CA  . GLN A 1 469  ? 41.906 64.121  -1.264  1.00 9.43  ? 469  GLN A CA  1 
ATOM   3738 C  C   . GLN A 1 469  ? 40.871 63.926  -0.170  1.00 10.47 ? 469  GLN A C   1 
ATOM   3739 O  O   . GLN A 1 469  ? 39.909 63.155  -0.329  1.00 11.21 ? 469  GLN A O   1 
ATOM   3740 C  CB  . GLN A 1 469  ? 42.640 62.793  -1.436  1.00 10.99 ? 469  GLN A CB  1 
ATOM   3741 C  CG  . GLN A 1 469  ? 43.725 62.849  -2.584  1.00 9.58  ? 469  GLN A CG  1 
ATOM   3742 C  CD  . GLN A 1 469  ? 43.252 63.532  -3.846  1.00 11.34 ? 469  GLN A CD  1 
ATOM   3743 O  OE1 . GLN A 1 469  ? 43.814 64.571  -4.315  1.00 13.77 ? 469  GLN A OE1 1 
ATOM   3744 N  NE2 . GLN A 1 469  ? 42.212 63.004  -4.388  1.00 8.90  ? 469  GLN A NE2 1 
ATOM   3745 N  N   . HIS A 1 470  ? 41.110 64.573  0.960   1.00 9.75  ? 470  HIS A N   1 
ATOM   3746 C  CA  . HIS A 1 470  ? 40.157 64.534  2.080   1.00 11.34 ? 470  HIS A CA  1 
ATOM   3747 C  C   . HIS A 1 470  ? 38.734 64.781  1.578   1.00 11.33 ? 470  HIS A C   1 
ATOM   3748 O  O   . HIS A 1 470  ? 38.512 65.562  0.632   1.00 11.00 ? 470  HIS A O   1 
ATOM   3749 C  CB  . HIS A 1 470  ? 40.529 65.622  3.096   1.00 10.21 ? 470  HIS A CB  1 
ATOM   3750 C  CG  . HIS A 1 470  ? 39.538 65.751  4.200   1.00 11.44 ? 470  HIS A CG  1 
ATOM   3751 N  ND1 . HIS A 1 470  ? 39.046 66.942  4.667   1.00 14.61 ? 470  HIS A ND1 1 
ATOM   3752 C  CD2 . HIS A 1 470  ? 38.908 64.779  4.903   1.00 9.59  ? 470  HIS A CD2 1 
ATOM   3753 C  CE1 . HIS A 1 470  ? 38.146 66.701  5.617   1.00 10.06 ? 470  HIS A CE1 1 
ATOM   3754 N  NE2 . HIS A 1 470  ? 38.054 65.394  5.775   1.00 15.72 ? 470  HIS A NE2 1 
ATOM   3755 N  N   . HIS A 1 471  ? 37.762 64.155  2.252   1.00 10.88 ? 471  HIS A N   1 
ATOM   3756 C  CA  . HIS A 1 471  ? 36.360 64.302  1.892   1.00 11.61 ? 471  HIS A CA  1 
ATOM   3757 C  C   . HIS A 1 471  ? 35.715 65.676  2.162   1.00 11.09 ? 471  HIS A C   1 
ATOM   3758 O  O   . HIS A 1 471  ? 34.523 65.785  1.959   1.00 12.94 ? 471  HIS A O   1 
ATOM   3759 C  CB  . HIS A 1 471  ? 35.514 63.152  2.505   1.00 11.77 ? 471  HIS A CB  1 
ATOM   3760 C  CG  . HIS A 1 471  ? 35.585 63.056  3.994   1.00 10.59 ? 471  HIS A CG  1 
ATOM   3761 N  ND1 . HIS A 1 471  ? 36.566 62.336  4.646   1.00 10.45 ? 471  HIS A ND1 1 
ATOM   3762 C  CD2 . HIS A 1 471  ? 34.837 63.655  4.957   1.00 12.23 ? 471  HIS A CD2 1 
ATOM   3763 C  CE1 . HIS A 1 471  ? 36.422 62.503  5.953   1.00 10.72 ? 471  HIS A CE1 1 
ATOM   3764 N  NE2 . HIS A 1 471  ? 35.387 63.294  6.171   1.00 9.32  ? 471  HIS A NE2 1 
ATOM   3765 N  N   . ASP A 1 472  ? 36.508 66.678  2.624   1.00 12.14 ? 472  ASP A N   1 
ATOM   3766 C  CA  . ASP A 1 472  ? 36.041 68.068  2.621   1.00 13.25 ? 472  ASP A CA  1 
ATOM   3767 C  C   . ASP A 1 472  ? 37.044 68.904  1.827   1.00 13.58 ? 472  ASP A C   1 
ATOM   3768 O  O   . ASP A 1 472  ? 36.922 70.129  1.840   1.00 14.39 ? 472  ASP A O   1 
ATOM   3769 C  CB  . ASP A 1 472  ? 35.880 68.673  4.012   1.00 13.48 ? 472  ASP A CB  1 
ATOM   3770 C  CG  . ASP A 1 472  ? 34.783 67.968  4.824   1.00 12.84 ? 472  ASP A CG  1 
ATOM   3771 O  OD1 . ASP A 1 472  ? 33.589 68.046  4.428   1.00 13.34 ? 472  ASP A OD1 1 
ATOM   3772 O  OD2 . ASP A 1 472  ? 35.196 67.317  5.800   1.00 13.13 ? 472  ASP A OD2 1 
ATOM   3773 N  N   . GLY A 1 473  ? 37.973 68.270  1.110   1.00 10.52 ? 473  GLY A N   1 
ATOM   3774 C  CA  . GLY A 1 473  ? 38.940 69.027  0.311   1.00 12.70 ? 473  GLY A CA  1 
ATOM   3775 C  C   . GLY A 1 473  ? 38.437 69.101  -1.122  1.00 11.69 ? 473  GLY A C   1 
ATOM   3776 O  O   . GLY A 1 473  ? 37.718 70.034  -1.511  1.00 11.74 ? 473  GLY A O   1 
ATOM   3777 N  N   . ILE A 1 474  ? 38.757 68.061  -1.894  1.00 10.89 ? 474  ILE A N   1 
ATOM   3778 C  CA  . ILE A 1 474  ? 38.343 68.050  -3.286  1.00 12.48 ? 474  ILE A CA  1 
ATOM   3779 C  C   . ILE A 1 474  ? 36.841 68.173  -3.467  1.00 11.99 ? 474  ILE A C   1 
ATOM   3780 O  O   . ILE A 1 474  ? 36.376 68.662  -4.520  1.00 11.95 ? 474  ILE A O   1 
ATOM   3781 C  CB  . ILE A 1 474  ? 38.934 66.793  -3.990  1.00 11.16 ? 474  ILE A CB  1 
ATOM   3782 C  CG1 . ILE A 1 474  ? 38.677 66.875  -5.474  1.00 12.23 ? 474  ILE A CG1 1 
ATOM   3783 C  CG2 . ILE A 1 474  ? 38.356 65.481  -3.370  1.00 11.98 ? 474  ILE A CG2 1 
ATOM   3784 C  CD1 . ILE A 1 474  ? 39.428 65.726  -6.252  1.00 13.22 ? 474  ILE A CD1 1 
ATOM   3785 N  N   . THR A 1 475  ? 36.069 67.748  -2.462  1.00 10.99 ? 475  THR A N   1 
ATOM   3786 C  CA  . THR A 1 475  ? 34.616 67.832  -2.495  1.00 11.81 ? 475  THR A CA  1 
ATOM   3787 C  C   . THR A 1 475  ? 34.060 69.273  -2.512  1.00 11.05 ? 475  THR A C   1 
ATOM   3788 O  O   . THR A 1 475  ? 32.899 69.493  -2.850  1.00 11.97 ? 475  THR A O   1 
ATOM   3789 C  CB  . THR A 1 475  ? 34.039 67.176  -1.227  1.00 12.99 ? 475  THR A CB  1 
ATOM   3790 O  OG1 . THR A 1 475  ? 34.579 67.895  -0.103  1.00 13.09 ? 475  THR A OG1 1 
ATOM   3791 C  CG2 . THR A 1 475  ? 34.411 65.692  -1.143  1.00 12.90 ? 475  THR A CG2 1 
ATOM   3792 N  N   . GLY A 1 476  ? 34.885 70.245  -2.133  1.00 10.65 ? 476  GLY A N   1 
ATOM   3793 C  CA  . GLY A 1 476  ? 34.414 71.618  -2.117  1.00 11.26 ? 476  GLY A CA  1 
ATOM   3794 C  C   . GLY A 1 476  ? 33.444 71.882  -0.965  1.00 11.51 ? 476  GLY A C   1 
ATOM   3795 O  O   . GLY A 1 476  ? 32.560 72.734  -1.116  1.00 13.08 ? 476  GLY A O   1 
ATOM   3796 N  N   . THR A 1 477  ? 33.606 71.173  0.156   1.00 11.85 ? 477  THR A N   1 
ATOM   3797 C  CA  . THR A 1 477  ? 32.713 71.322  1.282   1.00 11.78 ? 477  THR A CA  1 
ATOM   3798 C  C   . THR A 1 477  ? 33.344 71.906  2.525   1.00 13.00 ? 477  THR A C   1 
ATOM   3799 O  O   . THR A 1 477  ? 32.807 71.741  3.616   1.00 15.27 ? 477  THR A O   1 
ATOM   3800 C  CB  . THR A 1 477  ? 32.037 69.977  1.608   1.00 12.13 ? 477  THR A CB  1 
ATOM   3801 O  OG1 . THR A 1 477  ? 33.030 68.961  1.846   1.00 13.70 ? 477  THR A OG1 1 
ATOM   3802 C  CG2 . THR A 1 477  ? 31.187 69.534  0.386   1.00 12.67 ? 477  THR A CG2 1 
ATOM   3803 N  N   . ALA A 1 478  ? 34.430 72.660  2.380   1.00 12.70 ? 478  ALA A N   1 
ATOM   3804 C  CA  . ALA A 1 478  ? 35.089 73.267  3.552   1.00 12.79 ? 478  ALA A CA  1 
ATOM   3805 C  C   . ALA A 1 478  ? 34.791 74.762  3.624   1.00 13.45 ? 478  ALA A C   1 
ATOM   3806 O  O   . ALA A 1 478  ? 34.287 75.379  2.690   1.00 13.87 ? 478  ALA A O   1 
ATOM   3807 C  CB  . ALA A 1 478  ? 36.627 73.020  3.488   1.00 14.82 ? 478  ALA A CB  1 
ATOM   3808 N  N   . LYS A 1 479  ? 35.092 75.356  4.769   1.00 14.43 ? 479  LYS A N   1 
ATOM   3809 C  CA  . LYS A 1 479  ? 34.848 76.800  4.878   1.00 13.81 ? 479  LYS A CA  1 
ATOM   3810 C  C   . LYS A 1 479  ? 35.811 77.551  3.945   1.00 13.63 ? 479  LYS A C   1 
ATOM   3811 O  O   . LYS A 1 479  ? 36.882 77.052  3.566   1.00 13.29 ? 479  LYS A O   1 
ATOM   3812 C  CB  . LYS A 1 479  ? 35.048 77.249  6.326   1.00 14.75 ? 479  LYS A CB  1 
ATOM   3813 C  CG  . LYS A 1 479  ? 33.793 76.947  7.213   1.00 20.02 ? 479  LYS A CG  1 
ATOM   3814 C  CD  . LYS A 1 479  ? 33.890 77.648  8.557   1.00 23.49 ? 479  LYS A CD  1 
ATOM   3815 C  CE  . LYS A 1 479  ? 32.567 77.551  9.351   1.00 23.64 ? 479  LYS A CE  1 
ATOM   3816 N  NZ  . LYS A 1 479  ? 31.393 78.273  8.731   1.00 23.96 ? 479  LYS A NZ  1 
ATOM   3817 N  N   . THR A 1 480  ? 35.424 78.769  3.596   1.00 14.20 ? 480  THR A N   1 
ATOM   3818 C  CA  . THR A 1 480  ? 36.224 79.582  2.709   1.00 13.82 ? 480  THR A CA  1 
ATOM   3819 C  C   . THR A 1 480  ? 37.706 79.672  3.066   1.00 14.55 ? 480  THR A C   1 
ATOM   3820 O  O   . THR A 1 480  ? 38.572 79.451  2.194   1.00 15.14 ? 480  THR A O   1 
ATOM   3821 C  CB  . THR A 1 480  ? 35.632 80.992  2.660   1.00 17.90 ? 480  THR A CB  1 
ATOM   3822 O  OG1 . THR A 1 480  ? 34.292 80.889  2.196   1.00 21.06 ? 480  THR A OG1 1 
ATOM   3823 C  CG2 . THR A 1 480  ? 36.413 81.890  1.673   1.00 18.86 ? 480  THR A CG2 1 
ATOM   3824 N  N   . HIS A 1 481  ? 38.040 79.967  4.323   1.00 14.37 ? 481  HIS A N   1 
ATOM   3825 C  CA  . HIS A 1 481  ? 39.454 80.067  4.648   1.00 13.99 ? 481  HIS A CA  1 
ATOM   3826 C  C   . HIS A 1 481  ? 40.214 78.738  4.605   1.00 14.11 ? 481  HIS A C   1 
ATOM   3827 O  O   . HIS A 1 481  ? 41.452 78.708  4.436   1.00 14.68 ? 481  HIS A O   1 
ATOM   3828 C  CB  . HIS A 1 481  ? 39.646 80.776  6.015   1.00 15.04 ? 481  HIS A CB  1 
ATOM   3829 C  CG  . HIS A 1 481  ? 39.495 79.883  7.209   1.00 14.62 ? 481  HIS A CG  1 
ATOM   3830 N  ND1 . HIS A 1 481  ? 38.276 79.412  7.666   1.00 18.15 ? 481  HIS A ND1 1 
ATOM   3831 C  CD2 . HIS A 1 481  ? 40.433 79.388  8.059   1.00 15.97 ? 481  HIS A CD2 1 
ATOM   3832 C  CE1 . HIS A 1 481  ? 38.480 78.674  8.743   1.00 16.97 ? 481  HIS A CE1 1 
ATOM   3833 N  NE2 . HIS A 1 481  ? 39.776 78.649  9.002   1.00 18.66 ? 481  HIS A NE2 1 
ATOM   3834 N  N   . VAL A 1 482  ? 39.466 77.629  4.704   1.00 12.52 ? 482  VAL A N   1 
ATOM   3835 C  CA  . VAL A 1 482  ? 40.071 76.298  4.627   1.00 13.43 ? 482  VAL A CA  1 
ATOM   3836 C  C   . VAL A 1 482  ? 40.345 75.986  3.156   1.00 12.05 ? 482  VAL A C   1 
ATOM   3837 O  O   . VAL A 1 482  ? 41.404 75.444  2.842   1.00 13.35 ? 482  VAL A O   1 
ATOM   3838 C  CB  . VAL A 1 482  ? 39.117 75.267  5.266   1.00 10.57 ? 482  VAL A CB  1 
ATOM   3839 C  CG1 . VAL A 1 482  ? 39.773 73.844  5.233   1.00 13.24 ? 482  VAL A CG1 1 
ATOM   3840 C  CG2 . VAL A 1 482  ? 38.890 75.640  6.768   1.00 12.44 ? 482  VAL A CG2 1 
ATOM   3841 N  N   . VAL A 1 483  ? 39.413 76.348  2.273   1.00 12.39 ? 483  VAL A N   1 
ATOM   3842 C  CA  . VAL A 1 483  ? 39.652 76.168  0.852   1.00 12.17 ? 483  VAL A CA  1 
ATOM   3843 C  C   . VAL A 1 483  ? 40.901 76.976  0.453   1.00 12.91 ? 483  VAL A C   1 
ATOM   3844 O  O   . VAL A 1 483  ? 41.721 76.492  -0.340  1.00 14.06 ? 483  VAL A O   1 
ATOM   3845 C  CB  . VAL A 1 483  ? 38.450 76.681  0.031   1.00 11.09 ? 483  VAL A CB  1 
ATOM   3846 C  CG1 . VAL A 1 483  ? 38.750 76.644  -1.473  1.00 14.35 ? 483  VAL A CG1 1 
ATOM   3847 C  CG2 . VAL A 1 483  ? 37.230 75.826  0.338   1.00 14.54 ? 483  VAL A CG2 1 
ATOM   3848 N  N   . VAL A 1 484  ? 41.079 78.182  1.028   1.00 14.45 ? 484  VAL A N   1 
ATOM   3849 C  CA  . VAL A 1 484  ? 42.260 78.998  0.736   1.00 14.36 ? 484  VAL A CA  1 
ATOM   3850 C  C   . VAL A 1 484  ? 43.509 78.270  1.193   1.00 14.97 ? 484  VAL A C   1 
ATOM   3851 O  O   . VAL A 1 484  ? 44.519 78.235  0.461   1.00 15.64 ? 484  VAL A O   1 
ATOM   3852 C  CB  . VAL A 1 484  ? 42.145 80.348  1.416   1.00 14.87 ? 484  VAL A CB  1 
ATOM   3853 C  CG1 . VAL A 1 484  ? 43.518 81.074  1.356   1.00 17.44 ? 484  VAL A CG1 1 
ATOM   3854 C  CG2 . VAL A 1 484  ? 41.039 81.142  0.714   1.00 17.47 ? 484  VAL A CG2 1 
ATOM   3855 N  N   . ASP A 1 485  ? 43.440 77.649  2.362   1.00 13.55 ? 485  ASP A N   1 
ATOM   3856 C  CA  . ASP A 1 485  ? 44.598 76.893  2.846   1.00 13.65 ? 485  ASP A CA  1 
ATOM   3857 C  C   . ASP A 1 485  ? 44.939 75.743  1.908   1.00 14.13 ? 485  ASP A C   1 
ATOM   3858 O  O   . ASP A 1 485  ? 46.111 75.528  1.558   1.00 12.73 ? 485  ASP A O   1 
ATOM   3859 C  CB  . ASP A 1 485  ? 44.325 76.367  4.262   1.00 14.59 ? 485  ASP A CB  1 
ATOM   3860 C  CG  . ASP A 1 485  ? 45.560 75.718  4.865   1.00 14.47 ? 485  ASP A CG  1 
ATOM   3861 O  OD1 . ASP A 1 485  ? 46.595 76.413  4.989   1.00 18.84 ? 485  ASP A OD1 1 
ATOM   3862 O  OD2 . ASP A 1 485  ? 45.526 74.541  5.224   1.00 15.15 ? 485  ASP A OD2 1 
ATOM   3863 N  N   . TYR A 1 486  ? 43.941 74.979  1.471   1.00 12.06 ? 486  TYR A N   1 
ATOM   3864 C  CA  . TYR A 1 486  ? 44.242 73.892  0.529   1.00 11.90 ? 486  TYR A CA  1 
ATOM   3865 C  C   . TYR A 1 486  ? 44.830 74.432  -0.775  1.00 12.77 ? 486  TYR A C   1 
ATOM   3866 O  O   . TYR A 1 486  ? 45.741 73.786  -1.315  1.00 12.98 ? 486  TYR A O   1 
ATOM   3867 C  CB  . TYR A 1 486  ? 42.981 73.124  0.161   1.00 12.81 ? 486  TYR A CB  1 
ATOM   3868 C  CG  . TYR A 1 486  ? 42.362 72.292  1.287   1.00 11.61 ? 486  TYR A CG  1 
ATOM   3869 C  CD1 . TYR A 1 486  ? 43.152 71.432  2.076   1.00 13.51 ? 486  TYR A CD1 1 
ATOM   3870 C  CD2 . TYR A 1 486  ? 40.997 72.343  1.487   1.00 12.92 ? 486  TYR A CD2 1 
ATOM   3871 C  CE1 . TYR A 1 486  ? 42.536 70.605  3.072   1.00 14.59 ? 486  TYR A CE1 1 
ATOM   3872 C  CE2 . TYR A 1 486  ? 40.367 71.530  2.465   1.00 11.73 ? 486  TYR A CE2 1 
ATOM   3873 C  CZ  . TYR A 1 486  ? 41.157 70.686  3.225   1.00 13.28 ? 486  TYR A CZ  1 
ATOM   3874 O  OH  . TYR A 1 486  ? 40.508 69.882  4.167   1.00 14.31 ? 486  TYR A OH  1 
ATOM   3875 N  N   . GLU A 1 487  ? 44.298 75.558  -1.276  1.00 12.98 ? 487  GLU A N   1 
ATOM   3876 C  CA  . GLU A 1 487  ? 44.817 76.135  -2.518  1.00 13.48 ? 487  GLU A CA  1 
ATOM   3877 C  C   . GLU A 1 487  ? 46.278 76.572  -2.337  1.00 14.84 ? 487  GLU A C   1 
ATOM   3878 O  O   . GLU A 1 487  ? 47.133 76.320  -3.206  1.00 14.13 ? 487  GLU A O   1 
ATOM   3879 C  CB  . GLU A 1 487  ? 43.956 77.329  -2.933  1.00 13.77 ? 487  GLU A CB  1 
ATOM   3880 C  CG  . GLU A 1 487  ? 44.412 77.906  -4.275  1.00 16.00 ? 487  GLU A CG  1 
ATOM   3881 C  CD  . GLU A 1 487  ? 43.589 79.061  -4.744  1.00 22.00 ? 487  GLU A CD  1 
ATOM   3882 O  OE1 . GLU A 1 487  ? 42.423 79.217  -4.344  1.00 22.49 ? 487  GLU A OE1 1 
ATOM   3883 O  OE2 . GLU A 1 487  ? 44.155 79.836  -5.552  1.00 26.54 ? 487  GLU A OE2 1 
ATOM   3884 N  N   . GLN A 1 488  ? 46.573 77.213  -1.218  1.00 15.07 ? 488  GLN A N   1 
ATOM   3885 C  CA  . GLN A 1 488  ? 47.959 77.668  -0.950  1.00 16.40 ? 488  GLN A CA  1 
ATOM   3886 C  C   . GLN A 1 488  ? 48.888 76.488  -0.901  1.00 15.54 ? 488  GLN A C   1 
ATOM   3887 O  O   . GLN A 1 488  ? 49.962 76.515  -1.489  1.00 14.20 ? 488  GLN A O   1 
ATOM   3888 C  CB  . GLN A 1 488  ? 48.047 78.409  0.404   1.00 20.89 ? 488  GLN A CB  1 
ATOM   3889 C  CG  . GLN A 1 488  ? 47.323 79.719  0.379   1.00 28.51 ? 488  GLN A CG  1 
ATOM   3890 C  CD  . GLN A 1 488  ? 47.328 80.434  1.717   1.00 34.88 ? 488  GLN A CD  1 
ATOM   3891 O  OE1 . GLN A 1 488  ? 46.897 81.580  1.802   1.00 39.88 ? 488  GLN A OE1 1 
ATOM   3892 N  NE2 . GLN A 1 488  ? 47.807 79.762  2.772   1.00 38.18 ? 488  GLN A NE2 1 
ATOM   3893 N  N   . ARG A 1 489  ? 48.485 75.429  -0.209  1.00 13.18 ? 489  ARG A N   1 
ATOM   3894 C  CA  . ARG A 1 489  ? 49.286 74.214  -0.127  1.00 12.52 ? 489  ARG A CA  1 
ATOM   3895 C  C   . ARG A 1 489  ? 49.503 73.624  -1.512  1.00 12.12 ? 489  ARG A C   1 
ATOM   3896 O  O   . ARG A 1 489  ? 50.624 73.208  -1.861  1.00 13.46 ? 489  ARG A O   1 
ATOM   3897 C  CB  . ARG A 1 489  ? 48.575 73.206  0.759   1.00 13.72 ? 489  ARG A CB  1 
ATOM   3898 C  CG  . ARG A 1 489  ? 48.679 73.565  2.208   1.00 13.14 ? 489  ARG A CG  1 
ATOM   3899 C  CD  . ARG A 1 489  ? 47.687 72.642  2.996   1.00 15.49 ? 489  ARG A CD  1 
ATOM   3900 N  NE  . ARG A 1 489  ? 47.777 72.805  4.465   1.00 13.50 ? 489  ARG A NE  1 
ATOM   3901 C  CZ  . ARG A 1 489  ? 48.652 72.167  5.253   1.00 16.58 ? 489  ARG A CZ  1 
ATOM   3902 N  NH1 . ARG A 1 489  ? 49.525 71.316  4.762   1.00 17.42 ? 489  ARG A NH1 1 
ATOM   3903 N  NH2 . ARG A 1 489  ? 48.637 72.399  6.555   1.00 16.14 ? 489  ARG A NH2 1 
ATOM   3904 N  N   . MET A 1 490  ? 48.437 73.580  -2.334  1.00 12.24 ? 490  MET A N   1 
ATOM   3905 C  CA  . MET A 1 490  ? 48.626 73.016  -3.664  1.00 12.31 ? 490  MET A CA  1 
ATOM   3906 C  C   . MET A 1 490  ? 49.512 73.885  -4.544  1.00 12.44 ? 490  MET A C   1 
ATOM   3907 O  O   . MET A 1 490  ? 50.200 73.353  -5.419  1.00 12.89 ? 490  MET A O   1 
ATOM   3908 C  CB  . MET A 1 490  ? 47.290 72.725  -4.359  1.00 13.23 ? 490  MET A CB  1 
ATOM   3909 C  CG  . MET A 1 490  ? 46.534 71.522  -3.688  1.00 13.36 ? 490  MET A CG  1 
ATOM   3910 S  SD  . MET A 1 490  ? 45.229 70.839  -4.783  1.00 15.94 ? 490  MET A SD  1 
ATOM   3911 C  CE  . MET A 1 490  ? 43.961 72.083  -4.397  1.00 17.39 ? 490  MET A CE  1 
ATOM   3912 N  N   . GLN A 1 491  ? 49.487 75.201  -4.365  1.00 13.60 ? 491  GLN A N   1 
ATOM   3913 C  CA  . GLN A 1 491  ? 50.357 76.066  -5.167  1.00 13.62 ? 491  GLN A CA  1 
ATOM   3914 C  C   . GLN A 1 491  ? 51.805 75.774  -4.797  1.00 14.02 ? 491  GLN A C   1 
ATOM   3915 O  O   A GLN A 1 491  ? 52.686 75.639  -5.660  0.50 13.21 ? 491  GLN A O   1 
ATOM   3916 O  O   B GLN A 1 491  ? 52.584 75.900  -5.688  0.50 14.78 ? 491  GLN A O   1 
ATOM   3917 C  CB  A GLN A 1 491  ? 50.051 77.532  -4.887  0.50 16.01 ? 491  GLN A CB  1 
ATOM   3918 C  CB  B GLN A 1 491  ? 49.855 77.540  -4.811  0.50 17.44 ? 491  GLN A CB  1 
ATOM   3919 C  CG  A GLN A 1 491  ? 50.870 78.503  -5.734  0.50 19.94 ? 491  GLN A CG  1 
ATOM   3920 C  CG  B GLN A 1 491  ? 48.958 78.072  -5.900  0.50 23.12 ? 491  GLN A CG  1 
ATOM   3921 C  CD  A GLN A 1 491  ? 50.580 78.380  -7.220  0.50 25.50 ? 491  GLN A CD  1 
ATOM   3922 C  CD  B GLN A 1 491  ? 49.714 78.211  -7.214  0.50 25.44 ? 491  GLN A CD  1 
ATOM   3923 O  OE1 A GLN A 1 491  ? 51.265 77.652  -7.949  0.50 28.02 ? 491  GLN A OE1 1 
ATOM   3924 O  OE1 B GLN A 1 491  ? 50.120 77.223  -7.814  0.50 28.47 ? 491  GLN A OE1 1 
ATOM   3925 N  NE2 A GLN A 1 491  ? 49.552 79.090  -7.677  0.50 32.84 ? 491  GLN A NE2 1 
ATOM   3926 N  NE2 B GLN A 1 491  ? 49.925 79.453  -7.651  0.50 32.10 ? 491  GLN A NE2 1 
ATOM   3927 N  N   . GLU A 1 492  ? 52.056 75.630  -3.508  1.00 14.50 ? 492  GLU A N   1 
ATOM   3928 C  CA  . GLU A 1 492  ? 53.414 75.320  -3.084  1.00 15.64 ? 492  GLU A CA  1 
ATOM   3929 C  C   . GLU A 1 492  ? 53.831 73.964  -3.674  1.00 14.63 ? 492  GLU A C   1 
ATOM   3930 O  O   . GLU A 1 492  ? 54.970 73.768  -4.131  1.00 15.90 ? 492  GLU A O   1 
ATOM   3931 C  CB  . GLU A 1 492  ? 53.512 75.287  -1.560  1.00 18.71 ? 492  GLU A CB  1 
ATOM   3932 C  CG  . GLU A 1 492  ? 53.464 76.695  -0.918  1.00 25.46 ? 492  GLU A CG  1 
ATOM   3933 C  CD  . GLU A 1 492  ? 54.484 77.668  -1.497  1.00 31.67 ? 492  GLU A CD  1 
ATOM   3934 O  OE1 . GLU A 1 492  ? 55.695 77.328  -1.556  1.00 35.57 ? 492  GLU A OE1 1 
ATOM   3935 O  OE2 . GLU A 1 492  ? 54.078 78.791  -1.899  1.00 38.30 ? 492  GLU A OE2 1 
ATOM   3936 N  N   . ALA A 1 493  ? 52.894 73.019  -3.727  1.00 13.24 ? 493  ALA A N   1 
ATOM   3937 C  CA  . ALA A 1 493  ? 53.228 71.727  -4.319  1.00 11.94 ? 493  ALA A CA  1 
ATOM   3938 C  C   . ALA A 1 493  ? 53.533 71.852  -5.825  1.00 12.95 ? 493  ALA A C   1 
ATOM   3939 O  O   . ALA A 1 493  ? 54.405 71.137  -6.326  1.00 11.92 ? 493  ALA A O   1 
ATOM   3940 C  CB  . ALA A 1 493  ? 52.064 70.750  -4.113  1.00 13.98 ? 493  ALA A CB  1 
ATOM   3941 N  N   . LEU A 1 494  ? 52.757 72.688  -6.545  1.00 12.83 ? 494  LEU A N   1 
ATOM   3942 C  CA  . LEU A 1 494  ? 53.024 72.883  -7.974  1.00 12.77 ? 494  LEU A CA  1 
ATOM   3943 C  C   . LEU A 1 494  ? 54.421 73.477  -8.137  1.00 12.34 ? 494  LEU A C   1 
ATOM   3944 O  O   . LEU A 1 494  ? 55.144 73.046  -9.029  1.00 13.65 ? 494  LEU A O   1 
ATOM   3945 C  CB  . LEU A 1 494  ? 51.958 73.815  -8.581  1.00 12.20 ? 494  LEU A CB  1 
ATOM   3946 C  CG  . LEU A 1 494  ? 50.604 73.136  -8.831  1.00 14.43 ? 494  LEU A CG  1 
ATOM   3947 C  CD1 . LEU A 1 494  ? 49.589 74.250  -9.127  1.00 16.90 ? 494  LEU A CD1 1 
ATOM   3948 C  CD2 . LEU A 1 494  ? 50.700 72.085  -9.907  1.00 15.50 ? 494  LEU A CD2 1 
ATOM   3949 N  N   . LYS A 1 495  ? 54.805 74.433  -7.292  1.00 14.17 ? 495  LYS A N   1 
ATOM   3950 C  CA  . LYS A 1 495  ? 56.155 75.058  -7.401  1.00 13.78 ? 495  LYS A CA  1 
ATOM   3951 C  C   . LYS A 1 495  ? 57.238 74.003  -7.092  1.00 14.51 ? 495  LYS A C   1 
ATOM   3952 O  O   . LYS A 1 495  ? 58.272 73.935  -7.775  1.00 14.31 ? 495  LYS A O   1 
ATOM   3953 C  CB  . LYS A 1 495  ? 56.266 76.228  -6.449  1.00 17.01 ? 495  LYS A CB  1 
ATOM   3954 C  CG  . LYS A 1 495  ? 55.359 77.368  -6.842  1.00 22.35 ? 495  LYS A CG  1 
ATOM   3955 C  CD  . LYS A 1 495  ? 55.583 78.650  -6.033  1.00 29.78 ? 495  LYS A CD  1 
ATOM   3956 C  CE  . LYS A 1 495  ? 55.221 78.531  -4.581  1.00 35.44 ? 495  LYS A CE  1 
ATOM   3957 N  NZ  . LYS A 1 495  ? 55.253 79.897  -3.903  1.00 39.08 ? 495  LYS A NZ  1 
ATOM   3958 N  N   . ALA A 1 496  ? 56.979 73.111  -6.143  1.00 12.20 ? 496  ALA A N   1 
ATOM   3959 C  CA  . ALA A 1 496  ? 57.934 72.058  -5.853  1.00 12.49 ? 496  ALA A CA  1 
ATOM   3960 C  C   . ALA A 1 496  ? 58.098 71.113  -7.054  1.00 13.64 ? 496  ALA A C   1 
ATOM   3961 O  O   . ALA A 1 496  ? 59.208 70.683  -7.421  1.00 12.15 ? 496  ALA A O   1 
ATOM   3962 C  CB  . ALA A 1 496  ? 57.441 71.285  -4.582  1.00 12.36 ? 496  ALA A CB  1 
ATOM   3963 N  N   . CYS A 1 497  ? 56.978 70.755  -7.690  1.00 11.82 ? 497  CYS A N   1 
ATOM   3964 C  CA  . CYS A 1 497  ? 57.027 69.879  -8.846  1.00 12.35 ? 497  CYS A CA  1 
ATOM   3965 C  C   . CYS A 1 497  ? 57.815 70.561  -9.966  1.00 13.41 ? 497  CYS A C   1 
ATOM   3966 O  O   . CYS A 1 497  ? 58.621 69.921  -10.640 1.00 12.79 ? 497  CYS A O   1 
ATOM   3967 C  CB  . CYS A 1 497  ? 55.617 69.560  -9.346  1.00 10.85 ? 497  CYS A CB  1 
ATOM   3968 S  SG  . CYS A 1 497  ? 54.710 68.405  -8.278  1.00 13.93 ? 497  CYS A SG  1 
ATOM   3969 N  N   . GLN A 1 498  ? 57.511 71.823  -10.220 1.00 11.84 ? 498  GLN A N   1 
ATOM   3970 C  CA  . GLN A 1 498  ? 58.230 72.546  -11.291 1.00 13.00 ? 498  GLN A CA  1 
ATOM   3971 C  C   . GLN A 1 498  ? 59.714 72.526  -11.019 1.00 15.09 ? 498  GLN A C   1 
ATOM   3972 O  O   . GLN A 1 498  ? 60.523 72.280  -11.949 1.00 14.14 ? 498  GLN A O   1 
ATOM   3973 C  CB  . GLN A 1 498  ? 57.754 74.007  -11.363 1.00 13.53 ? 498  GLN A CB  1 
ATOM   3974 C  CG  . GLN A 1 498  ? 58.605 74.830  -12.337 1.00 20.01 ? 498  GLN A CG  1 
ATOM   3975 C  CD  . GLN A 1 498  ? 58.165 76.290  -12.446 1.00 23.29 ? 498  GLN A CD  1 
ATOM   3976 O  OE1 . GLN A 1 498  ? 58.090 77.029  -11.438 1.00 26.91 ? 498  GLN A OE1 1 
ATOM   3977 N  NE2 . GLN A 1 498  ? 57.898 76.728  -13.670 1.00 19.12 ? 498  GLN A NE2 1 
ATOM   3978 N  N   . MET A 1 499  ? 60.112 72.789  -9.777  1.00 13.06 ? 499  MET A N   1 
ATOM   3979 C  CA  . MET A 1 499  ? 61.537 72.783  -9.483  1.00 14.07 ? 499  MET A CA  1 
ATOM   3980 C  C   . MET A 1 499  ? 62.184 71.448  -9.775  1.00 12.72 ? 499  MET A C   1 
ATOM   3981 O  O   . MET A 1 499  ? 63.207 71.387  -10.456 1.00 14.03 ? 499  MET A O   1 
ATOM   3982 C  CB  . MET A 1 499  ? 61.756 73.204  -8.024  1.00 13.61 ? 499  MET A CB  1 
ATOM   3983 C  CG  . MET A 1 499  ? 63.174 73.023  -7.458  1.00 16.54 ? 499  MET A CG  1 
ATOM   3984 S  SD  . MET A 1 499  ? 64.445 73.977  -8.310  1.00 21.32 ? 499  MET A SD  1 
ATOM   3985 C  CE  . MET A 1 499  ? 63.937 75.623  -7.854  1.00 19.35 ? 499  MET A CE  1 
ATOM   3986 N  N   . VAL A 1 500  ? 61.549 70.366  -9.331  1.00 12.18 ? 500  VAL A N   1 
ATOM   3987 C  CA  . VAL A 1 500  ? 62.097 69.050  -9.548  1.00 10.77 ? 500  VAL A CA  1 
ATOM   3988 C  C   . VAL A 1 500  ? 62.128 68.739  -11.035 1.00 12.47 ? 500  VAL A C   1 
ATOM   3989 O  O   . VAL A 1 500  ? 63.114 68.187  -11.546 1.00 13.24 ? 500  VAL A O   1 
ATOM   3990 C  CB  . VAL A 1 500  ? 61.300 67.988  -8.743  1.00 13.58 ? 500  VAL A CB  1 
ATOM   3991 C  CG1 . VAL A 1 500  ? 61.725 66.586  -9.136  1.00 13.87 ? 500  VAL A CG1 1 
ATOM   3992 C  CG2 . VAL A 1 500  ? 61.586 68.236  -7.263  1.00 14.73 ? 500  VAL A CG2 1 
ATOM   3993 N  N   . MET A 1 501  ? 61.037 69.037  -11.730 1.00 13.15 ? 501  MET A N   1 
ATOM   3994 C  CA  . MET A 1 501  ? 60.970 68.732  -13.154 1.00 13.02 ? 501  MET A CA  1 
ATOM   3995 C  C   . MET A 1 501  ? 62.053 69.463  -13.930 1.00 12.26 ? 501  MET A C   1 
ATOM   3996 O  O   . MET A 1 501  ? 62.727 68.817  -14.766 1.00 12.39 ? 501  MET A O   1 
ATOM   3997 C  CB  . MET A 1 501  ? 59.599 69.113  -13.726 1.00 13.53 ? 501  MET A CB  1 
ATOM   3998 C  CG  . MET A 1 501  ? 58.471 68.168  -13.231 1.00 14.43 ? 501  MET A CG  1 
ATOM   3999 S  SD  . MET A 1 501  ? 56.850 68.839  -13.506 1.00 17.58 ? 501  MET A SD  1 
ATOM   4000 C  CE  . MET A 1 501  ? 56.662 68.604  -15.269 1.00 17.02 ? 501  MET A CE  1 
ATOM   4001 N  N   . GLN A 1 502  ? 62.211 70.765  -13.686 1.00 13.68 ? 502  GLN A N   1 
ATOM   4002 C  CA  . GLN A 1 502  ? 63.176 71.503  -14.507 1.00 13.39 ? 502  GLN A CA  1 
ATOM   4003 C  C   . GLN A 1 502  ? 64.616 71.120  -14.172 1.00 14.50 ? 502  GLN A C   1 
ATOM   4004 O  O   . GLN A 1 502  ? 65.445 71.040  -15.096 1.00 14.24 ? 502  GLN A O   1 
ATOM   4005 C  CB  . GLN A 1 502  ? 62.890 73.000  -14.447 1.00 15.64 ? 502  GLN A CB  1 
ATOM   4006 C  CG  . GLN A 1 502  ? 63.069 73.633  -13.085 1.00 15.05 ? 502  GLN A CG  1 
ATOM   4007 C  CD  . GLN A 1 502  ? 64.487 74.163  -12.858 1.00 18.65 ? 502  GLN A CD  1 
ATOM   4008 O  OE1 . GLN A 1 502  ? 65.286 74.268  -13.805 1.00 16.37 ? 502  GLN A OE1 1 
ATOM   4009 N  NE2 . GLN A 1 502  ? 64.803 74.518  -11.626 1.00 17.54 ? 502  GLN A NE2 1 
ATOM   4010 N  N   . GLN A 1 503  ? 64.919 70.834  -12.915 1.00 13.62 ? 503  GLN A N   1 
ATOM   4011 C  CA  . GLN A 1 503  ? 66.282 70.334  -12.624 1.00 14.39 ? 503  GLN A CA  1 
ATOM   4012 C  C   . GLN A 1 503  ? 66.512 69.005  -13.341 1.00 14.10 ? 503  GLN A C   1 
ATOM   4013 O  O   . GLN A 1 503  ? 67.618 68.730  -13.847 1.00 15.64 ? 503  GLN A O   1 
ATOM   4014 C  CB  . GLN A 1 503  ? 66.470 70.104  -11.119 1.00 14.79 ? 503  GLN A CB  1 
ATOM   4015 C  CG  . GLN A 1 503  ? 66.588 71.391  -10.335 1.00 15.97 ? 503  GLN A CG  1 
ATOM   4016 C  CD  . GLN A 1 503  ? 67.963 72.060  -10.468 1.00 17.07 ? 503  GLN A CD  1 
ATOM   4017 O  OE1 . GLN A 1 503  ? 68.942 71.397  -10.771 1.00 20.20 ? 503  GLN A OE1 1 
ATOM   4018 N  NE2 . GLN A 1 503  ? 68.027 73.353  -10.198 1.00 19.40 ? 503  GLN A NE2 1 
ATOM   4019 N  N   . SER A 1 504  ? 65.488 68.138  -13.386 1.00 13.62 ? 504  SER A N   1 
ATOM   4020 C  CA  . SER A 1 504  ? 65.634 66.855  -14.043 1.00 14.64 ? 504  SER A CA  1 
ATOM   4021 C  C   . SER A 1 504  ? 65.857 66.999  -15.554 1.00 13.83 ? 504  SER A C   1 
ATOM   4022 O  O   . SER A 1 504  ? 66.711 66.296  -16.136 1.00 14.56 ? 504  SER A O   1 
ATOM   4023 C  CB  . SER A 1 504  ? 64.394 65.962  -13.793 1.00 15.43 ? 504  SER A CB  1 
ATOM   4024 O  OG  . SER A 1 504  ? 64.224 65.725  -12.382 1.00 14.14 ? 504  SER A OG  1 
ATOM   4025 N  N   . VAL A 1 505  ? 65.071 67.865  -16.205 1.00 13.68 ? 505  VAL A N   1 
ATOM   4026 C  CA  . VAL A 1 505  ? 65.230 68.066  -17.654 1.00 14.28 ? 505  VAL A CA  1 
ATOM   4027 C  C   . VAL A 1 505  ? 66.660 68.587  -17.960 1.00 13.42 ? 505  VAL A C   1 
ATOM   4028 O  O   . VAL A 1 505  ? 67.330 68.120  -18.893 1.00 14.95 ? 505  VAL A O   1 
ATOM   4029 C  CB  . VAL A 1 505  ? 64.156 69.065  -18.155 1.00 13.80 ? 505  VAL A CB  1 
ATOM   4030 C  CG1 . VAL A 1 505  ? 64.498 69.553  -19.582 1.00 14.41 ? 505  VAL A CG1 1 
ATOM   4031 C  CG2 . VAL A 1 505  ? 62.771 68.400  -18.109 1.00 14.47 ? 505  VAL A CG2 1 
ATOM   4032 N  N   . TYR A 1 506  ? 67.141 69.498  -17.156 1.00 13.77 ? 506  TYR A N   1 
ATOM   4033 C  CA  . TYR A 1 506  ? 68.473 70.031  -17.377 1.00 14.83 ? 506  TYR A CA  1 
ATOM   4034 C  C   . TYR A 1 506  ? 69.520 68.901  -17.268 1.00 16.79 ? 506  TYR A C   1 
ATOM   4035 O  O   . TYR A 1 506  ? 70.440 68.790  -18.086 1.00 16.69 ? 506  TYR A O   1 
ATOM   4036 C  CB  . TYR A 1 506  ? 68.769 71.130  -16.366 1.00 16.01 ? 506  TYR A CB  1 
ATOM   4037 C  CG  . TYR A 1 506  ? 70.041 71.839  -16.662 1.00 20.78 ? 506  TYR A CG  1 
ATOM   4038 C  CD1 . TYR A 1 506  ? 70.213 72.450  -17.907 1.00 23.66 ? 506  TYR A CD1 1 
ATOM   4039 C  CD2 . TYR A 1 506  ? 71.067 71.874  -15.732 1.00 20.77 ? 506  TYR A CD2 1 
ATOM   4040 C  CE1 . TYR A 1 506  ? 71.375 73.078  -18.219 1.00 26.76 ? 506  TYR A CE1 1 
ATOM   4041 C  CE2 . TYR A 1 506  ? 72.278 72.517  -16.043 1.00 25.87 ? 506  TYR A CE2 1 
ATOM   4042 C  CZ  . TYR A 1 506  ? 72.395 73.112  -17.294 1.00 25.60 ? 506  TYR A CZ  1 
ATOM   4043 O  OH  . TYR A 1 506  ? 73.507 73.827  -17.664 1.00 29.85 ? 506  TYR A OH  1 
ATOM   4044 N  N   . ARG A 1 507  ? 69.348 68.010  -16.303 1.00 16.23 ? 507  ARG A N   1 
ATOM   4045 C  CA  . ARG A 1 507  ? 70.301 66.906  -16.143 1.00 15.91 ? 507  ARG A CA  1 
ATOM   4046 C  C   . ARG A 1 507  ? 70.181 65.870  -17.256 1.00 16.70 ? 507  ARG A C   1 
ATOM   4047 O  O   . ARG A 1 507  ? 71.197 65.326  -17.747 1.00 16.63 ? 507  ARG A O   1 
ATOM   4048 C  CB  . ARG A 1 507  ? 70.075 66.242  -14.787 1.00 16.38 ? 507  ARG A CB  1 
ATOM   4049 C  CG  . ARG A 1 507  ? 71.148 65.199  -14.457 1.00 16.85 ? 507  ARG A CG  1 
ATOM   4050 C  CD  . ARG A 1 507  ? 71.035 64.789  -12.999 1.00 18.29 ? 507  ARG A CD  1 
ATOM   4051 N  NE  . ARG A 1 507  ? 72.063 63.795  -12.651 1.00 21.88 ? 507  ARG A NE  1 
ATOM   4052 C  CZ  . ARG A 1 507  ? 72.129 63.196  -11.455 1.00 22.26 ? 507  ARG A CZ  1 
ATOM   4053 N  NH1 . ARG A 1 507  ? 71.251 63.486  -10.502 1.00 22.19 ? 507  ARG A NH1 1 
ATOM   4054 N  NH2 . ARG A 1 507  ? 73.048 62.266  -11.217 1.00 23.02 ? 507  ARG A NH2 1 
ATOM   4055 N  N   . LEU A 1 508  ? 68.946 65.582  -17.671 1.00 15.02 ? 508  LEU A N   1 
ATOM   4056 C  CA  . LEU A 1 508  ? 68.742 64.599  -18.695 1.00 14.98 ? 508  LEU A CA  1 
ATOM   4057 C  C   . LEU A 1 508  ? 69.168 65.005  -20.102 1.00 14.20 ? 508  LEU A C   1 
ATOM   4058 O  O   . LEU A 1 508  ? 69.412 64.145  -20.952 1.00 17.60 ? 508  LEU A O   1 
ATOM   4059 C  CB  . LEU A 1 508  ? 67.275 64.176  -18.738 1.00 14.74 ? 508  LEU A CB  1 
ATOM   4060 C  CG  . LEU A 1 508  ? 66.799 63.378  -17.517 1.00 15.19 ? 508  LEU A CG  1 
ATOM   4061 C  CD1 . LEU A 1 508  ? 65.249 63.501  -17.421 1.00 15.09 ? 508  LEU A CD1 1 
ATOM   4062 C  CD2 . LEU A 1 508  ? 67.258 61.925  -17.670 1.00 16.25 ? 508  LEU A CD2 1 
ATOM   4063 N  N   . LEU A 1 509  ? 69.231 66.317  -20.336 1.00 15.71 ? 509  LEU A N   1 
ATOM   4064 C  CA  . LEU A 1 509  ? 69.533 66.812  -21.669 1.00 15.95 ? 509  LEU A CA  1 
ATOM   4065 C  C   . LEU A 1 509  ? 70.803 67.638  -21.763 1.00 17.20 ? 509  LEU A C   1 
ATOM   4066 O  O   . LEU A 1 509  ? 70.961 68.401  -22.721 1.00 17.09 ? 509  LEU A O   1 
ATOM   4067 C  CB  . LEU A 1 509  ? 68.318 67.605  -22.193 1.00 15.68 ? 509  LEU A CB  1 
ATOM   4068 C  CG  . LEU A 1 509  ? 67.098 66.744  -22.526 1.00 13.63 ? 509  LEU A CG  1 
ATOM   4069 C  CD1 . LEU A 1 509  ? 65.970 67.711  -22.930 1.00 13.27 ? 509  LEU A CD1 1 
ATOM   4070 C  CD2 . LEU A 1 509  ? 67.351 65.733  -23.674 1.00 16.64 ? 509  LEU A CD2 1 
ATOM   4071 N  N   . THR A 1 510  ? 71.715 67.511  -20.812 1.00 15.61 ? 510  THR A N   1 
ATOM   4072 C  CA  . THR A 1 510  ? 72.958 68.261  -20.910 1.00 17.18 ? 510  THR A CA  1 
ATOM   4073 C  C   . THR A 1 510  ? 74.123 67.273  -20.910 1.00 17.56 ? 510  THR A C   1 
ATOM   4074 O  O   . THR A 1 510  ? 74.120 66.300  -20.159 1.00 17.41 ? 510  THR A O   1 
ATOM   4075 C  CB  . THR A 1 510  ? 73.099 69.231  -19.750 1.00 15.52 ? 510  THR A CB  1 
ATOM   4076 O  OG1 . THR A 1 510  ? 71.995 70.150  -19.780 1.00 16.23 ? 510  THR A OG1 1 
ATOM   4077 C  CG2 . THR A 1 510  ? 74.423 70.070  -19.841 1.00 17.62 ? 510  THR A CG2 1 
ATOM   4078 N  N   . LYS A 1 511  ? 75.084 67.501  -21.807 1.00 18.31 ? 511  LYS A N   1 
ATOM   4079 C  CA  . LYS A 1 511  ? 76.243 66.625  -21.898 1.00 19.29 ? 511  LYS A CA  1 
ATOM   4080 C  C   . LYS A 1 511  ? 76.766 66.470  -20.484 1.00 19.31 ? 511  LYS A C   1 
ATOM   4081 O  O   . LYS A 1 511  ? 77.024 67.438  -19.767 1.00 19.55 ? 511  LYS A O   1 
ATOM   4082 C  CB  . LYS A 1 511  ? 77.316 67.260  -22.798 1.00 21.99 ? 511  LYS A CB  1 
ATOM   4083 C  CG  . LYS A 1 511  ? 78.562 66.403  -22.819 1.00 27.23 ? 511  LYS A CG  1 
ATOM   4084 C  CD  . LYS A 1 511  ? 79.539 66.768  -23.905 1.00 31.92 ? 511  LYS A CD  1 
ATOM   4085 C  CE  . LYS A 1 511  ? 80.634 65.684  -23.947 1.00 36.46 ? 511  LYS A CE  1 
ATOM   4086 N  NZ  . LYS A 1 511  ? 81.806 66.047  -24.798 1.00 38.12 ? 511  LYS A NZ  1 
ATOM   4087 N  N   . PRO A 1 512  ? 76.966 65.217  -20.059 1.00 20.50 ? 512  PRO A N   1 
ATOM   4088 C  CA  . PRO A 1 512  ? 77.443 64.941  -18.713 1.00 22.26 ? 512  PRO A CA  1 
ATOM   4089 C  C   . PRO A 1 512  ? 78.669 65.680  -18.216 1.00 20.44 ? 512  PRO A C   1 
ATOM   4090 O  O   . PRO A 1 512  ? 78.679 66.171  -17.091 1.00 20.15 ? 512  PRO A O   1 
ATOM   4091 C  CB  . PRO A 1 512  ? 77.639 63.428  -18.731 1.00 24.06 ? 512  PRO A CB  1 
ATOM   4092 C  CG  . PRO A 1 512  ? 76.600 62.980  -19.662 1.00 25.84 ? 512  PRO A CG  1 
ATOM   4093 C  CD  . PRO A 1 512  ? 76.687 63.971  -20.790 1.00 23.11 ? 512  PRO A CD  1 
ATOM   4094 N  N   . SER A 1 513  ? 79.697 65.786  -19.060 1.00 21.41 ? 513  SER A N   1 
ATOM   4095 C  CA  . SER A 1 513  ? 80.921 66.465  -18.613 1.00 21.76 ? 513  SER A CA  1 
ATOM   4096 C  C   . SER A 1 513  ? 80.793 67.972  -18.565 1.00 20.32 ? 513  SER A C   1 
ATOM   4097 O  O   . SER A 1 513  ? 81.734 68.653  -18.135 1.00 23.21 ? 513  SER A O   1 
ATOM   4098 C  CB  . SER A 1 513  ? 82.117 66.071  -19.498 1.00 20.96 ? 513  SER A CB  1 
ATOM   4099 O  OG  . SER A 1 513  ? 81.813 66.300  -20.847 1.00 23.96 ? 513  SER A OG  1 
ATOM   4100 N  N   . ILE A 1 514  ? 79.648 68.512  -18.990 1.00 20.20 ? 514  ILE A N   1 
ATOM   4101 C  CA  . ILE A 1 514  ? 79.402 69.955  -18.958 1.00 20.47 ? 514  ILE A CA  1 
ATOM   4102 C  C   . ILE A 1 514  ? 78.405 70.301  -17.830 1.00 19.55 ? 514  ILE A C   1 
ATOM   4103 O  O   . ILE A 1 514  ? 78.427 71.392  -17.260 1.00 19.77 ? 514  ILE A O   1 
ATOM   4104 C  CB  . ILE A 1 514  ? 78.784 70.433  -20.307 1.00 22.61 ? 514  ILE A CB  1 
ATOM   4105 C  CG1 . ILE A 1 514  ? 79.835 70.367  -21.420 1.00 25.34 ? 514  ILE A CG1 1 
ATOM   4106 C  CG2 . ILE A 1 514  ? 78.176 71.863  -20.154 1.00 22.76 ? 514  ILE A CG2 1 
ATOM   4107 C  CD1 . ILE A 1 514  ? 79.293 70.752  -22.768 1.00 27.99 ? 514  ILE A CD1 1 
ATOM   4108 N  N   . TYR A 1 515  ? 77.531 69.344  -17.512 1.00 18.88 ? 515  TYR A N   1 
ATOM   4109 C  CA  . TYR A 1 515  ? 76.491 69.551  -16.491 1.00 16.81 ? 515  TYR A CA  1 
ATOM   4110 C  C   . TYR A 1 515  ? 77.043 70.122  -15.194 1.00 18.31 ? 515  TYR A C   1 
ATOM   4111 O  O   . TYR A 1 515  ? 77.896 69.497  -14.572 1.00 19.10 ? 515  TYR A O   1 
ATOM   4112 C  CB  . TYR A 1 515  ? 75.785 68.200  -16.287 1.00 17.67 ? 515  TYR A CB  1 
ATOM   4113 C  CG  . TYR A 1 515  ? 74.761 68.189  -15.203 1.00 18.68 ? 515  TYR A CG  1 
ATOM   4114 C  CD1 . TYR A 1 515  ? 73.592 68.936  -15.301 1.00 17.26 ? 515  TYR A CD1 1 
ATOM   4115 C  CD2 . TYR A 1 515  ? 74.955 67.394  -14.098 1.00 18.97 ? 515  TYR A CD2 1 
ATOM   4116 C  CE1 . TYR A 1 515  ? 72.612 68.880  -14.295 1.00 18.69 ? 515  TYR A CE1 1 
ATOM   4117 C  CE2 . TYR A 1 515  ? 74.005 67.325  -13.083 1.00 17.80 ? 515  TYR A CE2 1 
ATOM   4118 C  CZ  . TYR A 1 515  ? 72.839 68.071  -13.198 1.00 18.93 ? 515  TYR A CZ  1 
ATOM   4119 O  OH  . TYR A 1 515  ? 71.887 67.961  -12.224 1.00 18.25 ? 515  TYR A OH  1 
ATOM   4120 N  N   . SER A 1 516  ? 76.570 71.299  -14.773 1.00 18.19 ? 516  SER A N   1 
ATOM   4121 C  CA  . SER A 1 516  ? 77.088 71.965  -13.557 1.00 19.18 ? 516  SER A CA  1 
ATOM   4122 C  C   . SER A 1 516  ? 75.913 72.621  -12.833 1.00 19.50 ? 516  SER A C   1 
ATOM   4123 O  O   . SER A 1 516  ? 75.753 73.854  -12.813 1.00 22.02 ? 516  SER A O   1 
ATOM   4124 C  CB  . SER A 1 516  ? 78.113 73.048  -13.959 1.00 20.60 ? 516  SER A CB  1 
ATOM   4125 O  OG  . SER A 1 516  ? 78.810 73.490  -12.802 1.00 25.39 ? 516  SER A OG  1 
ATOM   4126 N  N   . PRO A 1 517  ? 75.096 71.800  -12.167 1.00 20.38 ? 517  PRO A N   1 
ATOM   4127 C  CA  . PRO A 1 517  ? 73.937 72.371  -11.500 1.00 21.75 ? 517  PRO A CA  1 
ATOM   4128 C  C   . PRO A 1 517  ? 74.029 73.213  -10.268 1.00 20.94 ? 517  PRO A C   1 
ATOM   4129 O  O   . PRO A 1 517  ? 74.856 72.974  -9.393  1.00 25.37 ? 517  PRO A O   1 
ATOM   4130 C  CB  . PRO A 1 517  ? 73.065 71.145  -11.240 1.00 20.83 ? 517  PRO A CB  1 
ATOM   4131 C  CG  . PRO A 1 517  ? 74.100 70.126  -10.877 1.00 21.64 ? 517  PRO A CG  1 
ATOM   4132 C  CD  . PRO A 1 517  ? 75.199 70.353  -11.942 1.00 21.11 ? 517  PRO A CD  1 
ATOM   4133 N  N   . ASP A 1 518  ? 73.182 74.230  -10.225 1.00 22.42 ? 518  ASP A N   1 
ATOM   4134 C  CA  . ASP A 1 518  ? 72.997 75.042  -9.033  1.00 23.51 ? 518  ASP A CA  1 
ATOM   4135 C  C   . ASP A 1 518  ? 71.555 74.577  -8.733  1.00 22.53 ? 518  ASP A C   1 
ATOM   4136 O  O   . ASP A 1 518  ? 70.600 74.890  -9.486  1.00 21.99 ? 518  ASP A O   1 
ATOM   4137 C  CB  . ASP A 1 518  ? 73.015 76.526  -9.350  1.00 25.39 ? 518  ASP A CB  1 
ATOM   4138 C  CG  . ASP A 1 518  ? 72.510 77.370  -8.198  1.00 29.30 ? 518  ASP A CG  1 
ATOM   4139 O  OD1 . ASP A 1 518  ? 71.918 76.826  -7.229  1.00 25.93 ? 518  ASP A OD1 1 
ATOM   4140 O  OD2 . ASP A 1 518  ? 72.684 78.597  -8.275  1.00 31.63 ? 518  ASP A OD2 1 
ATOM   4141 N  N   . PHE A 1 519  ? 71.421 73.804  -7.661  1.00 22.55 ? 519  PHE A N   1 
ATOM   4142 C  CA  . PHE A 1 519  ? 70.126 73.221  -7.327  1.00 21.10 ? 519  PHE A CA  1 
ATOM   4143 C  C   . PHE A 1 519  ? 69.046 74.190  -6.922  1.00 21.07 ? 519  PHE A C   1 
ATOM   4144 O  O   . PHE A 1 519  ? 67.911 73.785  -6.736  1.00 22.94 ? 519  PHE A O   1 
ATOM   4145 C  CB  . PHE A 1 519  ? 70.304 72.146  -6.279  1.00 20.26 ? 519  PHE A CB  1 
ATOM   4146 C  CG  . PHE A 1 519  ? 71.171 71.007  -6.724  1.00 19.84 ? 519  PHE A CG  1 
ATOM   4147 C  CD1 . PHE A 1 519  ? 70.884 70.314  -7.897  1.00 19.99 ? 519  PHE A CD1 1 
ATOM   4148 C  CD2 . PHE A 1 519  ? 72.276 70.628  -5.959  1.00 19.83 ? 519  PHE A CD2 1 
ATOM   4149 C  CE1 . PHE A 1 519  ? 71.677 69.261  -8.317  1.00 20.22 ? 519  PHE A CE1 1 
ATOM   4150 C  CE2 . PHE A 1 519  ? 73.081 69.579  -6.353  1.00 18.85 ? 519  PHE A CE2 1 
ATOM   4151 C  CZ  . PHE A 1 519  ? 72.792 68.884  -7.532  1.00 20.90 ? 519  PHE A CZ  1 
ATOM   4152 N  N   . SER A 1 520  ? 69.381 75.466  -6.785  1.00 20.02 ? 520  SER A N   1 
ATOM   4153 C  CA  . SER A 1 520  ? 68.391 76.481  -6.437  1.00 20.71 ? 520  SER A CA  1 
ATOM   4154 C  C   . SER A 1 520  ? 68.025 77.292  -7.712  1.00 22.10 ? 520  SER A C   1 
ATOM   4155 O  O   . SER A 1 520  ? 67.097 78.089  -7.699  1.00 21.91 ? 520  SER A O   1 
ATOM   4156 C  CB  . SER A 1 520  ? 68.979 77.449  -5.411  1.00 22.94 ? 520  SER A CB  1 
ATOM   4157 O  OG  . SER A 1 520  ? 70.020 78.223  -6.006  1.00 27.30 ? 520  SER A OG  1 
ATOM   4158 N  N   . PHE A 1 521  ? 68.722 77.032  -8.816  1.00 21.34 ? 521  PHE A N   1 
ATOM   4159 C  CA  . PHE A 1 521  ? 68.509 77.807  -10.034 1.00 22.35 ? 521  PHE A CA  1 
ATOM   4160 C  C   . PHE A 1 521  ? 67.391 77.308  -10.949 1.00 20.83 ? 521  PHE A C   1 
ATOM   4161 O  O   . PHE A 1 521  ? 67.129 76.113  -11.019 1.00 21.13 ? 521  PHE A O   1 
ATOM   4162 C  CB  . PHE A 1 521  ? 69.841 77.829  -10.802 1.00 23.24 ? 521  PHE A CB  1 
ATOM   4163 C  CG  . PHE A 1 521  ? 69.859 78.779  -11.981 1.00 25.23 ? 521  PHE A CG  1 
ATOM   4164 C  CD1 . PHE A 1 521  ? 70.063 80.140  -11.784 1.00 28.29 ? 521  PHE A CD1 1 
ATOM   4165 C  CD2 . PHE A 1 521  ? 69.644 78.308  -13.279 1.00 26.04 ? 521  PHE A CD2 1 
ATOM   4166 C  CE1 . PHE A 1 521  ? 70.042 81.024  -12.865 1.00 29.70 ? 521  PHE A CE1 1 
ATOM   4167 C  CE2 . PHE A 1 521  ? 69.625 79.183  -14.358 1.00 27.45 ? 521  PHE A CE2 1 
ATOM   4168 C  CZ  . PHE A 1 521  ? 69.822 80.545  -14.154 1.00 29.33 ? 521  PHE A CZ  1 
ATOM   4169 N  N   . SER A 1 522  ? 66.775 78.239  -11.673 1.00 20.79 ? 522  SER A N   1 
ATOM   4170 C  CA  . SER A 1 522  ? 65.721 77.905  -12.612 1.00 20.93 ? 522  SER A CA  1 
ATOM   4171 C  C   . SER A 1 522  ? 66.277 77.823  -14.025 1.00 19.62 ? 522  SER A C   1 
ATOM   4172 O  O   . SER A 1 522  ? 66.352 78.818  -14.711 1.00 21.59 ? 522  SER A O   1 
ATOM   4173 C  CB  . SER A 1 522  ? 64.620 78.964  -12.574 1.00 24.71 ? 522  SER A CB  1 
ATOM   4174 O  OG  . SER A 1 522  ? 63.810 78.736  -11.431 1.00 33.90 ? 522  SER A OG  1 
ATOM   4175 N  N   . TYR A 1 523  ? 66.630 76.632  -14.461 1.00 15.31 ? 523  TYR A N   1 
ATOM   4176 C  CA  . TYR A 1 523  ? 67.154 76.443  -15.810 1.00 14.52 ? 523  TYR A CA  1 
ATOM   4177 C  C   . TYR A 1 523  ? 66.019 76.500  -16.825 1.00 17.11 ? 523  TYR A C   1 
ATOM   4178 O  O   . TYR A 1 523  ? 66.243 76.889  -17.962 1.00 15.81 ? 523  TYR A O   1 
ATOM   4179 C  CB  . TYR A 1 523  ? 67.842 75.088  -15.918 1.00 16.53 ? 523  TYR A CB  1 
ATOM   4180 C  CG  . TYR A 1 523  ? 69.103 75.061  -15.131 1.00 19.08 ? 523  TYR A CG  1 
ATOM   4181 C  CD1 . TYR A 1 523  ? 70.265 75.686  -15.621 1.00 20.36 ? 523  TYR A CD1 1 
ATOM   4182 C  CD2 . TYR A 1 523  ? 69.135 74.486  -13.871 1.00 17.57 ? 523  TYR A CD2 1 
ATOM   4183 C  CE1 . TYR A 1 523  ? 71.420 75.732  -14.857 1.00 21.86 ? 523  TYR A CE1 1 
ATOM   4184 C  CE2 . TYR A 1 523  ? 70.280 74.529  -13.118 1.00 20.78 ? 523  TYR A CE2 1 
ATOM   4185 C  CZ  . TYR A 1 523  ? 71.412 75.159  -13.622 1.00 24.55 ? 523  TYR A CZ  1 
ATOM   4186 O  OH  . TYR A 1 523  ? 72.568 75.232  -12.874 1.00 24.57 ? 523  TYR A OH  1 
ATOM   4187 N  N   . PHE A 1 524  ? 64.812 76.103  -16.413 1.00 15.20 ? 524  PHE A N   1 
ATOM   4188 C  CA  . PHE A 1 524  ? 63.635 76.143  -17.285 1.00 14.60 ? 524  PHE A CA  1 
ATOM   4189 C  C   . PHE A 1 524  ? 62.436 76.586  -16.485 1.00 17.65 ? 524  PHE A C   1 
ATOM   4190 O  O   . PHE A 1 524  ? 62.396 76.392  -15.281 1.00 17.56 ? 524  PHE A O   1 
ATOM   4191 C  CB  . PHE A 1 524  ? 63.235 74.768  -17.838 1.00 14.91 ? 524  PHE A CB  1 
ATOM   4192 C  CG  . PHE A 1 524  ? 64.271 74.115  -18.690 1.00 14.32 ? 524  PHE A CG  1 
ATOM   4193 C  CD1 . PHE A 1 524  ? 65.307 73.367  -18.102 1.00 16.06 ? 524  PHE A CD1 1 
ATOM   4194 C  CD2 . PHE A 1 524  ? 64.236 74.232  -20.078 1.00 15.24 ? 524  PHE A CD2 1 
ATOM   4195 C  CE1 . PHE A 1 524  ? 66.278 72.768  -18.908 1.00 16.46 ? 524  PHE A CE1 1 
ATOM   4196 C  CE2 . PHE A 1 524  ? 65.200 73.632  -20.875 1.00 15.13 ? 524  PHE A CE2 1 
ATOM   4197 C  CZ  . PHE A 1 524  ? 66.232 72.896  -20.277 1.00 16.14 ? 524  PHE A CZ  1 
ATOM   4198 N  N   . THR A 1 525  ? 61.489 77.208  -17.154 1.00 17.71 ? 525  THR A N   1 
ATOM   4199 C  CA  . THR A 1 525  ? 60.237 77.478  -16.471 1.00 20.09 ? 525  THR A CA  1 
ATOM   4200 C  C   . THR A 1 525  ? 59.194 76.685  -17.247 1.00 17.02 ? 525  THR A C   1 
ATOM   4201 O  O   . THR A 1 525  ? 59.281 76.506  -18.487 1.00 20.20 ? 525  THR A O   1 
ATOM   4202 C  CB  . THR A 1 525  ? 59.826 78.924  -16.487 1.00 23.37 ? 525  THR A CB  1 
ATOM   4203 O  OG1 . THR A 1 525  ? 59.773 79.362  -17.825 1.00 25.09 ? 525  THR A OG1 1 
ATOM   4204 C  CG2 . THR A 1 525  ? 60.832 79.805  -15.729 1.00 25.08 ? 525  THR A CG2 1 
ATOM   4205 N  N   . LEU A 1 526  ? 58.221 76.163  -16.526 1.00 16.56 ? 526  LEU A N   1 
ATOM   4206 C  CA  . LEU A 1 526  ? 57.136 75.439  -17.144 1.00 16.99 ? 526  LEU A CA  1 
ATOM   4207 C  C   . LEU A 1 526  ? 56.166 76.413  -17.811 1.00 18.04 ? 526  LEU A C   1 
ATOM   4208 O  O   . LEU A 1 526  ? 55.924 77.515  -17.305 1.00 21.38 ? 526  LEU A O   1 
ATOM   4209 C  CB  . LEU A 1 526  ? 56.374 74.629  -16.087 1.00 21.82 ? 526  LEU A CB  1 
ATOM   4210 C  CG  . LEU A 1 526  ? 56.900 73.258  -15.699 1.00 20.75 ? 526  LEU A CG  1 
ATOM   4211 C  CD1 . LEU A 1 526  ? 56.070 72.756  -14.520 1.00 25.42 ? 526  LEU A CD1 1 
ATOM   4212 C  CD2 . LEU A 1 526  ? 56.804 72.295  -16.871 1.00 22.01 ? 526  LEU A CD2 1 
ATOM   4213 N  N   . ASP A 1 527  ? 55.634 76.020  -18.951 1.00 15.18 ? 527  ASP A N   1 
ATOM   4214 C  CA  . ASP A 1 527  ? 54.633 76.822  -19.655 1.00 15.56 ? 527  ASP A CA  1 
ATOM   4215 C  C   . ASP A 1 527  ? 53.394 75.930  -19.710 1.00 15.95 ? 527  ASP A C   1 
ATOM   4216 O  O   . ASP A 1 527  ? 53.453 74.808  -20.183 1.00 19.65 ? 527  ASP A O   1 
ATOM   4217 C  CB  . ASP A 1 527  ? 55.085 77.198  -21.081 1.00 18.24 ? 527  ASP A CB  1 
ATOM   4218 C  CG  . ASP A 1 527  ? 54.046 78.047  -21.804 1.00 19.59 ? 527  ASP A CG  1 
ATOM   4219 O  OD1 . ASP A 1 527  ? 53.796 79.171  -21.365 1.00 21.78 ? 527  ASP A OD1 1 
ATOM   4220 O  OD2 . ASP A 1 527  ? 53.479 77.561  -22.799 1.00 21.81 ? 527  ASP A OD2 1 
ATOM   4221 N  N   . ASP A 1 528  ? 52.301 76.409  -19.134 1.00 15.56 ? 528  ASP A N   1 
ATOM   4222 C  CA  . ASP A 1 528  ? 51.072 75.611  -19.107 1.00 15.23 ? 528  ASP A CA  1 
ATOM   4223 C  C   . ASP A 1 528  ? 49.969 76.469  -19.711 1.00 16.78 ? 528  ASP A C   1 
ATOM   4224 O  O   . ASP A 1 528  ? 49.643 77.541  -19.184 1.00 17.54 ? 528  ASP A O   1 
ATOM   4225 C  CB  . ASP A 1 528  ? 50.738 75.237  -17.655 1.00 16.04 ? 528  ASP A CB  1 
ATOM   4226 C  CG  . ASP A 1 528  ? 49.683 74.129  -17.566 1.00 18.07 ? 528  ASP A CG  1 
ATOM   4227 O  OD1 . ASP A 1 528  ? 48.661 74.169  -18.289 1.00 17.00 ? 528  ASP A OD1 1 
ATOM   4228 O  OD2 . ASP A 1 528  ? 49.884 73.170  -16.780 1.00 18.82 ? 528  ASP A OD2 1 
ATOM   4229 N  N   . SER A 1 529  ? 49.431 75.979  -20.820 1.00 17.74 ? 529  SER A N   1 
ATOM   4230 C  CA  . SER A 1 529  ? 48.369 76.672  -21.567 1.00 17.55 ? 529  SER A CA  1 
ATOM   4231 C  C   . SER A 1 529  ? 46.992 76.546  -20.976 1.00 19.92 ? 529  SER A C   1 
ATOM   4232 O  O   . SER A 1 529  ? 46.112 77.300  -21.338 1.00 23.42 ? 529  SER A O   1 
ATOM   4233 C  CB  . SER A 1 529  ? 48.255 76.126  -22.998 1.00 23.07 ? 529  SER A CB  1 
ATOM   4234 O  OG  . SER A 1 529  ? 49.489 76.229  -23.636 1.00 25.36 ? 529  SER A OG  1 
ATOM   4235 N  N   . ARG A 1 530  ? 46.788 75.596  -20.072 1.00 16.91 ? 530  ARG A N   1 
ATOM   4236 C  CA  . ARG A 1 530  ? 45.452 75.393  -19.551 1.00 19.02 ? 530  ARG A CA  1 
ATOM   4237 C  C   . ARG A 1 530  ? 45.316 75.532  -18.071 1.00 20.41 ? 530  ARG A C   1 
ATOM   4238 O  O   . ARG A 1 530  ? 44.254 75.205  -17.513 1.00 24.09 ? 530  ARG A O   1 
ATOM   4239 C  CB  . ARG A 1 530  ? 44.932 74.027  -19.993 1.00 17.17 ? 530  ARG A CB  1 
ATOM   4240 C  CG  . ARG A 1 530  ? 44.950 73.925  -21.507 1.00 19.96 ? 530  ARG A CG  1 
ATOM   4241 C  CD  . ARG A 1 530  ? 44.289 72.687  -22.069 1.00 21.04 ? 530  ARG A CD  1 
ATOM   4242 N  NE  . ARG A 1 530  ? 44.979 71.495  -21.610 1.00 20.77 ? 530  ARG A NE  1 
ATOM   4243 C  CZ  . ARG A 1 530  ? 44.789 70.304  -22.155 1.00 21.95 ? 530  ARG A CZ  1 
ATOM   4244 N  NH1 . ARG A 1 530  ? 43.933 70.178  -23.171 1.00 22.03 ? 530  ARG A NH1 1 
ATOM   4245 N  NH2 . ARG A 1 530  ? 45.443 69.267  -21.688 1.00 19.77 ? 530  ARG A NH2 1 
ATOM   4246 N  N   . TRP A 1 531  ? 46.376 75.952  -17.389 1.00 17.07 ? 531  TRP A N   1 
ATOM   4247 C  CA  . TRP A 1 531  ? 46.224 76.170  -15.935 1.00 16.11 ? 531  TRP A CA  1 
ATOM   4248 C  C   . TRP A 1 531  ? 47.155 77.302  -15.515 1.00 16.55 ? 531  TRP A C   1 
ATOM   4249 O  O   . TRP A 1 531  ? 48.343 77.219  -15.751 1.00 18.26 ? 531  TRP A O   1 
ATOM   4250 C  CB  . TRP A 1 531  ? 46.600 74.925  -15.108 1.00 17.46 ? 531  TRP A CB  1 
ATOM   4251 C  CG  . TRP A 1 531  ? 46.501 75.262  -13.641 1.00 18.74 ? 531  TRP A CG  1 
ATOM   4252 C  CD1 . TRP A 1 531  ? 47.523 75.714  -12.812 1.00 20.52 ? 531  TRP A CD1 1 
ATOM   4253 C  CD2 . TRP A 1 531  ? 45.302 75.352  -12.879 1.00 21.89 ? 531  TRP A CD2 1 
ATOM   4254 N  NE1 . TRP A 1 531  ? 47.004 76.078  -11.608 1.00 24.72 ? 531  TRP A NE1 1 
ATOM   4255 C  CE2 . TRP A 1 531  ? 45.651 75.868  -11.615 1.00 20.07 ? 531  TRP A CE2 1 
ATOM   4256 C  CE3 . TRP A 1 531  ? 43.976 75.052  -13.139 1.00 22.44 ? 531  TRP A CE3 1 
ATOM   4257 C  CZ2 . TRP A 1 531  ? 44.698 76.087  -10.595 1.00 23.68 ? 531  TRP A CZ2 1 
ATOM   4258 C  CZ3 . TRP A 1 531  ? 43.009 75.269  -12.125 1.00 23.44 ? 531  TRP A CZ3 1 
ATOM   4259 C  CH2 . TRP A 1 531  ? 43.390 75.781  -10.875 1.00 24.36 ? 531  TRP A CH2 1 
ATOM   4260 N  N   . PRO A 1 532  ? 46.637 78.328  -14.830 1.00 18.37 ? 532  PRO A N   1 
ATOM   4261 C  CA  . PRO A 1 532  ? 45.249 78.526  -14.405 1.00 19.51 ? 532  PRO A CA  1 
ATOM   4262 C  C   . PRO A 1 532  ? 44.358 78.785  -15.610 1.00 21.77 ? 532  PRO A C   1 
ATOM   4263 O  O   . PRO A 1 532  ? 43.140 78.621  -15.554 1.00 22.74 ? 532  PRO A O   1 
ATOM   4264 C  CB  . PRO A 1 532  ? 45.329 79.749  -13.483 1.00 20.56 ? 532  PRO A CB  1 
ATOM   4265 C  CG  . PRO A 1 532  ? 46.709 79.638  -12.883 1.00 22.53 ? 532  PRO A CG  1 
ATOM   4266 C  CD  . PRO A 1 532  ? 47.539 79.263  -14.115 1.00 18.17 ? 532  PRO A CD  1 
ATOM   4267 N  N   . GLY A 1 533  ? 44.984 79.162  -16.717 1.00 21.73 ? 533  GLY A N   1 
ATOM   4268 C  CA  . GLY A 1 533  ? 44.219 79.401  -17.923 1.00 22.74 ? 533  GLY A CA  1 
ATOM   4269 C  C   . GLY A 1 533  ? 44.114 80.844  -18.331 1.00 27.24 ? 533  GLY A C   1 
ATOM   4270 O  O   . GLY A 1 533  ? 44.218 81.766  -17.498 1.00 26.33 ? 533  GLY A O   1 
ATOM   4271 N  N   . SER A 1 534  ? 43.925 81.021  -19.642 1.00 31.58 ? 534  SER A N   1 
ATOM   4272 C  CA  . SER A 1 534  ? 43.773 82.343  -20.226 1.00 35.31 ? 534  SER A CA  1 
ATOM   4273 C  C   . SER A 1 534  ? 42.478 82.854  -19.656 1.00 35.04 ? 534  SER A C   1 
ATOM   4274 O  O   . SER A 1 534  ? 41.449 82.141  -19.663 1.00 35.97 ? 534  SER A O   1 
ATOM   4275 C  CB  . SER A 1 534  ? 43.673 82.282  -21.762 1.00 38.84 ? 534  SER A CB  1 
ATOM   4276 O  OG  . SER A 1 534  ? 43.544 83.591  -22.319 1.00 41.76 ? 534  SER A OG  1 
ATOM   4277 N  N   . GLY A 1 535  ? 42.523 84.079  -19.159 1.00 33.61 ? 535  GLY A N   1 
ATOM   4278 C  CA  . GLY A 1 535  ? 41.325 84.661  -18.591 1.00 31.83 ? 535  GLY A CA  1 
ATOM   4279 C  C   . GLY A 1 535  ? 41.208 84.381  -17.111 1.00 31.45 ? 535  GLY A C   1 
ATOM   4280 O  O   . GLY A 1 535  ? 40.346 84.945  -16.424 1.00 32.98 ? 535  GLY A O   1 
ATOM   4281 N  N   . VAL A 1 536  ? 42.061 83.497  -16.596 1.00 30.81 ? 536  VAL A N   1 
ATOM   4282 C  CA  . VAL A 1 536  ? 42.012 83.206  -15.168 1.00 29.83 ? 536  VAL A CA  1 
ATOM   4283 C  C   . VAL A 1 536  ? 43.186 83.918  -14.498 1.00 32.44 ? 536  VAL A C   1 
ATOM   4284 O  O   . VAL A 1 536  ? 43.018 84.624  -13.515 1.00 31.70 ? 536  VAL A O   1 
ATOM   4285 C  CB  . VAL A 1 536  ? 42.051 81.667  -14.904 1.00 29.63 ? 536  VAL A CB  1 
ATOM   4286 C  CG1 . VAL A 1 536  ? 41.952 81.364  -13.393 1.00 29.94 ? 536  VAL A CG1 1 
ATOM   4287 C  CG2 . VAL A 1 536  ? 40.848 81.003  -15.630 1.00 29.38 ? 536  VAL A CG2 1 
ATOM   4288 N  N   . GLU A 1 537  ? 44.376 83.755  -15.057 1.00 34.28 ? 537  GLU A N   1 
ATOM   4289 C  CA  . GLU A 1 537  ? 45.564 84.407  -14.525 1.00 36.45 ? 537  GLU A CA  1 
ATOM   4290 C  C   . GLU A 1 537  ? 46.477 84.653  -15.734 1.00 37.66 ? 537  GLU A C   1 
ATOM   4291 O  O   . GLU A 1 537  ? 46.719 83.733  -16.525 1.00 37.57 ? 537  GLU A O   1 
ATOM   4292 C  CB  . GLU A 1 537  ? 46.251 83.477  -13.518 1.00 39.01 ? 537  GLU A CB  1 
ATOM   4293 C  CG  . GLU A 1 537  ? 47.440 84.067  -12.780 1.00 44.01 ? 537  GLU A CG  1 
ATOM   4294 C  CD  . GLU A 1 537  ? 48.043 83.091  -11.768 1.00 47.70 ? 537  GLU A CD  1 
ATOM   4295 O  OE1 . GLU A 1 537  ? 47.481 82.970  -10.647 1.00 48.64 ? 537  GLU A OE1 1 
ATOM   4296 O  OE2 . GLU A 1 537  ? 49.067 82.434  -12.100 1.00 49.03 ? 537  GLU A OE2 1 
ATOM   4297 N  N   . ASP A 1 538  ? 46.954 85.882  -15.920 1.00 40.26 ? 538  ASP A N   1 
ATOM   4298 C  CA  . ASP A 1 538  ? 47.864 86.128  -17.051 1.00 43.10 ? 538  ASP A CA  1 
ATOM   4299 C  C   . ASP A 1 538  ? 49.227 85.788  -16.432 1.00 42.32 ? 538  ASP A C   1 
ATOM   4300 O  O   . ASP A 1 538  ? 49.921 86.661  -15.900 1.00 43.92 ? 538  ASP A O   1 
ATOM   4301 C  CB  . ASP A 1 538  ? 47.810 87.602  -17.495 1.00 46.23 ? 538  ASP A CB  1 
ATOM   4302 C  CG  . ASP A 1 538  ? 48.650 87.877  -18.761 1.00 50.86 ? 538  ASP A CG  1 
ATOM   4303 O  OD1 . ASP A 1 538  ? 49.804 87.382  -18.830 1.00 52.37 ? 538  ASP A OD1 1 
ATOM   4304 O  OD2 . ASP A 1 538  ? 48.168 88.597  -19.683 1.00 51.38 ? 538  ASP A OD2 1 
ATOM   4305 N  N   . SER A 1 539  ? 49.606 84.516  -16.464 1.00 38.59 ? 539  SER A N   1 
ATOM   4306 C  CA  . SER A 1 539  ? 50.870 84.133  -15.843 1.00 36.88 ? 539  SER A CA  1 
ATOM   4307 C  C   . SER A 1 539  ? 51.884 83.457  -16.761 1.00 34.48 ? 539  SER A C   1 
ATOM   4308 O  O   . SER A 1 539  ? 52.994 83.145  -16.322 1.00 34.48 ? 539  SER A O   1 
ATOM   4309 C  CB  . SER A 1 539  ? 50.601 83.225  -14.642 1.00 37.90 ? 539  SER A CB  1 
ATOM   4310 O  OG  . SER A 1 539  ? 50.171 81.935  -15.054 1.00 37.87 ? 539  SER A OG  1 
ATOM   4311 N  N   . ARG A 1 540  ? 51.497 83.224  -18.011 1.00 31.02 ? 540  ARG A N   1 
ATOM   4312 C  CA  . ARG A 1 540  ? 52.396 82.587  -18.959 1.00 28.60 ? 540  ARG A CA  1 
ATOM   4313 C  C   . ARG A 1 540  ? 53.476 83.565  -19.354 1.00 28.21 ? 540  ARG A C   1 
ATOM   4314 O  O   . ARG A 1 540  ? 53.201 84.738  -19.555 1.00 30.95 ? 540  ARG A O   1 
ATOM   4315 C  CB  . ARG A 1 540  ? 51.641 82.155  -20.204 1.00 27.27 ? 540  ARG A CB  1 
ATOM   4316 C  CG  . ARG A 1 540  ? 50.790 80.923  -19.941 1.00 25.31 ? 540  ARG A CG  1 
ATOM   4317 C  CD  . ARG A 1 540  ? 50.074 80.478  -21.162 1.00 22.48 ? 540  ARG A CD  1 
ATOM   4318 N  NE  . ARG A 1 540  ? 50.969 79.798  -22.091 1.00 20.49 ? 540  ARG A NE  1 
ATOM   4319 C  CZ  . ARG A 1 540  ? 50.588 79.396  -23.295 1.00 20.18 ? 540  ARG A CZ  1 
ATOM   4320 N  NH1 . ARG A 1 540  ? 49.332 79.606  -23.719 1.00 21.37 ? 540  ARG A NH1 1 
ATOM   4321 N  NH2 . ARG A 1 540  ? 51.466 78.795  -24.078 1.00 19.30 ? 540  ARG A NH2 1 
ATOM   4322 N  N   . THR A 1 541  ? 54.704 83.072  -19.472 1.00 25.77 ? 541  THR A N   1 
ATOM   4323 C  CA  . THR A 1 541  ? 55.790 83.948  -19.859 1.00 25.71 ? 541  THR A CA  1 
ATOM   4324 C  C   . THR A 1 541  ? 55.894 83.984  -21.386 1.00 22.48 ? 541  THR A C   1 
ATOM   4325 O  O   . THR A 1 541  ? 55.693 82.986  -22.059 1.00 26.07 ? 541  THR A O   1 
ATOM   4326 C  CB  . THR A 1 541  ? 57.117 83.448  -19.284 1.00 28.24 ? 541  THR A CB  1 
ATOM   4327 O  OG1 . THR A 1 541  ? 57.609 82.407  -20.113 1.00 31.55 ? 541  THR A OG1 1 
ATOM   4328 C  CG2 . THR A 1 541  ? 56.929 82.889  -17.896 1.00 27.52 ? 541  THR A CG2 1 
ATOM   4329 N  N   . THR A 1 542  ? 56.181 85.158  -21.912 1.00 21.08 ? 542  THR A N   1 
ATOM   4330 C  CA  . THR A 1 542  ? 56.376 85.298  -23.339 1.00 18.74 ? 542  THR A CA  1 
ATOM   4331 C  C   . THR A 1 542  ? 57.850 85.035  -23.639 1.00 16.26 ? 542  THR A C   1 
ATOM   4332 O  O   . THR A 1 542  ? 58.744 85.483  -22.893 1.00 18.84 ? 542  THR A O   1 
ATOM   4333 C  CB  . THR A 1 542  ? 56.039 86.726  -23.770 1.00 20.82 ? 542  THR A CB  1 
ATOM   4334 O  OG1 . THR A 1 542  ? 54.682 86.985  -23.429 1.00 22.41 ? 542  THR A OG1 1 
ATOM   4335 C  CG2 . THR A 1 542  ? 56.223 86.924  -25.262 1.00 21.16 ? 542  THR A CG2 1 
ATOM   4336 N  N   . ILE A 1 543  ? 58.104 84.296  -24.708 1.00 15.99 ? 543  ILE A N   1 
ATOM   4337 C  CA  . ILE A 1 543  ? 59.480 84.056  -25.140 1.00 15.72 ? 543  ILE A CA  1 
ATOM   4338 C  C   . ILE A 1 543  ? 59.837 85.353  -25.925 1.00 16.68 ? 543  ILE A C   1 
ATOM   4339 O  O   . ILE A 1 543  ? 59.229 85.664  -26.975 1.00 16.66 ? 543  ILE A O   1 
ATOM   4340 C  CB  . ILE A 1 543  ? 59.548 82.828  -26.017 1.00 16.09 ? 543  ILE A CB  1 
ATOM   4341 C  CG1 . ILE A 1 543  ? 59.217 81.565  -25.155 1.00 16.88 ? 543  ILE A CG1 1 
ATOM   4342 C  CG2 . ILE A 1 543  ? 60.927 82.765  -26.720 1.00 16.45 ? 543  ILE A CG2 1 
ATOM   4343 C  CD1 . ILE A 1 543  ? 59.132 80.297  -25.969 1.00 16.51 ? 543  ILE A CD1 1 
ATOM   4344 N  N   . ILE A 1 544  ? 60.778 86.106  -25.367 1.00 16.29 ? 544  ILE A N   1 
ATOM   4345 C  CA  . ILE A 1 544  ? 61.179 87.384  -25.937 1.00 17.43 ? 544  ILE A CA  1 
ATOM   4346 C  C   . ILE A 1 544  ? 62.386 87.236  -26.862 1.00 18.49 ? 544  ILE A C   1 
ATOM   4347 O  O   . ILE A 1 544  ? 63.494 86.891  -26.423 1.00 17.96 ? 544  ILE A O   1 
ATOM   4348 C  CB  . ILE A 1 544  ? 61.421 88.370  -24.785 1.00 20.31 ? 544  ILE A CB  1 
ATOM   4349 C  CG1 . ILE A 1 544  ? 60.092 88.596  -24.043 1.00 25.01 ? 544  ILE A CG1 1 
ATOM   4350 C  CG2 . ILE A 1 544  ? 61.970 89.677  -25.309 1.00 23.41 ? 544  ILE A CG2 1 
ATOM   4351 C  CD1 . ILE A 1 544  ? 60.155 89.554  -22.841 1.00 28.64 ? 544  ILE A CD1 1 
ATOM   4352 N  N   . LEU A 1 545  ? 62.124 87.432  -28.150 1.00 17.80 ? 545  LEU A N   1 
ATOM   4353 C  CA  . LEU A 1 545  ? 63.163 87.302  -29.170 1.00 16.97 ? 545  LEU A CA  1 
ATOM   4354 C  C   . LEU A 1 545  ? 63.298 88.660  -29.853 1.00 19.58 ? 545  LEU A C   1 
ATOM   4355 O  O   . LEU A 1 545  ? 62.362 89.448  -29.877 1.00 20.84 ? 545  LEU A O   1 
ATOM   4356 C  CB  . LEU A 1 545  ? 62.780 86.229  -30.200 1.00 18.17 ? 545  LEU A CB  1 
ATOM   4357 C  CG  . LEU A 1 545  ? 62.548 84.818  -29.638 1.00 17.98 ? 545  LEU A CG  1 
ATOM   4358 C  CD1 . LEU A 1 545  ? 62.078 83.875  -30.716 1.00 20.73 ? 545  LEU A CD1 1 
ATOM   4359 C  CD2 . LEU A 1 545  ? 63.848 84.287  -29.061 1.00 17.94 ? 545  LEU A CD2 1 
ATOM   4360 N  N   . GLY A 1 546  ? 64.456 88.921  -30.425 1.00 19.12 ? 546  GLY A N   1 
ATOM   4361 C  CA  . GLY A 1 546  ? 64.661 90.205  -31.077 1.00 20.26 ? 546  GLY A CA  1 
ATOM   4362 C  C   . GLY A 1 546  ? 66.067 90.253  -31.617 1.00 18.42 ? 546  GLY A C   1 
ATOM   4363 O  O   . GLY A 1 546  ? 67.007 89.743  -31.009 1.00 18.42 ? 546  GLY A O   1 
ATOM   4364 N  N   . GLU A 1 547  ? 66.227 90.900  -32.756 1.00 19.89 ? 547  GLU A N   1 
ATOM   4365 C  CA  . GLU A 1 547  ? 67.555 91.005  -33.358 1.00 25.11 ? 547  GLU A CA  1 
ATOM   4366 C  C   . GLU A 1 547  ? 68.599 91.650  -32.441 1.00 25.35 ? 547  GLU A C   1 
ATOM   4367 O  O   . GLU A 1 547  ? 69.776 91.324  -32.498 1.00 27.95 ? 547  GLU A O   1 
ATOM   4368 C  CB  . GLU A 1 547  ? 67.480 91.815  -34.645 1.00 29.60 ? 547  GLU A CB  1 
ATOM   4369 C  CG  . GLU A 1 547  ? 68.804 91.780  -35.410 1.00 39.59 ? 547  GLU A CG  1 
ATOM   4370 C  CD  . GLU A 1 547  ? 68.794 92.637  -36.667 1.00 44.41 ? 547  GLU A CD  1 
ATOM   4371 O  OE1 . GLU A 1 547  ? 67.743 92.681  -37.359 1.00 47.09 ? 547  GLU A OE1 1 
ATOM   4372 O  OE2 . GLU A 1 547  ? 69.849 93.254  -36.971 1.00 48.28 ? 547  GLU A OE2 1 
ATOM   4373 N  N   . ASP A 1 548  ? 68.130 92.554  -31.590 1.00 23.34 ? 548  ASP A N   1 
ATOM   4374 C  CA  . ASP A 1 548  ? 69.001 93.265  -30.666 1.00 23.89 ? 548  ASP A CA  1 
ATOM   4375 C  C   . ASP A 1 548  ? 68.953 92.681  -29.264 1.00 25.82 ? 548  ASP A C   1 
ATOM   4376 O  O   . ASP A 1 548  ? 69.314 93.355  -28.286 1.00 28.54 ? 548  ASP A O   1 
ATOM   4377 C  CB  . ASP A 1 548  ? 68.596 94.746  -30.615 1.00 25.01 ? 548  ASP A CB  1 
ATOM   4378 C  CG  . ASP A 1 548  ? 68.798 95.445  -31.942 1.00 27.13 ? 548  ASP A CG  1 
ATOM   4379 O  OD1 . ASP A 1 548  ? 69.953 95.504  -32.403 1.00 30.08 ? 548  ASP A OD1 1 
ATOM   4380 O  OD2 . ASP A 1 548  ? 67.816 95.938  -32.517 1.00 30.28 ? 548  ASP A OD2 1 
ATOM   4381 N  N   . ILE A 1 549  ? 68.500 91.440  -29.120 1.00 21.96 ? 549  ILE A N   1 
ATOM   4382 C  CA  . ILE A 1 549  ? 68.501 90.891  -27.774 1.00 22.07 ? 549  ILE A CA  1 
ATOM   4383 C  C   . ILE A 1 549  ? 68.716 89.378  -27.732 1.00 21.92 ? 549  ILE A C   1 
ATOM   4384 O  O   . ILE A 1 549  ? 69.538 88.908  -26.975 1.00 21.83 ? 549  ILE A O   1 
ATOM   4385 C  CB  . ILE A 1 549  ? 67.187 91.257  -26.965 1.00 21.83 ? 549  ILE A CB  1 
ATOM   4386 C  CG1 . ILE A 1 549  ? 67.303 90.684  -25.527 1.00 25.89 ? 549  ILE A CG1 1 
ATOM   4387 C  CG2 . ILE A 1 549  ? 65.922 90.762  -27.689 1.00 21.88 ? 549  ILE A CG2 1 
ATOM   4388 C  CD1 . ILE A 1 549  ? 66.094 90.948  -24.603 1.00 27.83 ? 549  ILE A CD1 1 
ATOM   4389 N  N   . LEU A 1 550  ? 67.999 88.633  -28.559 1.00 19.29 ? 550  LEU A N   1 
ATOM   4390 C  CA  . LEU A 1 550  ? 68.096 87.174  -28.497 1.00 19.34 ? 550  LEU A CA  1 
ATOM   4391 C  C   . LEU A 1 550  ? 67.465 86.604  -29.745 1.00 18.00 ? 550  LEU A C   1 
ATOM   4392 O  O   . LEU A 1 550  ? 66.263 86.728  -29.979 1.00 19.31 ? 550  LEU A O   1 
ATOM   4393 C  CB  . LEU A 1 550  ? 67.336 86.657  -27.267 1.00 20.65 ? 550  LEU A CB  1 
ATOM   4394 C  CG  . LEU A 1 550  ? 67.415 85.132  -27.041 1.00 20.25 ? 550  LEU A CG  1 
ATOM   4395 C  CD1 . LEU A 1 550  ? 68.843 84.705  -26.851 1.00 21.23 ? 550  LEU A CD1 1 
ATOM   4396 C  CD2 . LEU A 1 550  ? 66.588 84.757  -25.818 1.00 21.07 ? 550  LEU A CD2 1 
ATOM   4397 N  N   . PRO A 1 551  ? 68.261 85.941  -30.567 1.00 19.39 ? 551  PRO A N   1 
ATOM   4398 C  CA  . PRO A 1 551  ? 67.696 85.387  -31.793 1.00 18.51 ? 551  PRO A CA  1 
ATOM   4399 C  C   . PRO A 1 551  ? 66.809 84.154  -31.658 1.00 18.56 ? 551  PRO A C   1 
ATOM   4400 O  O   . PRO A 1 551  ? 65.895 83.950  -32.475 1.00 19.64 ? 551  PRO A O   1 
ATOM   4401 C  CB  . PRO A 1 551  ? 68.932 85.028  -32.641 1.00 19.02 ? 551  PRO A CB  1 
ATOM   4402 C  CG  . PRO A 1 551  ? 70.043 85.796  -32.041 1.00 24.48 ? 551  PRO A CG  1 
ATOM   4403 C  CD  . PRO A 1 551  ? 69.733 85.877  -30.554 1.00 20.74 ? 551  PRO A CD  1 
ATOM   4404 N  N   . SER A 1 552  ? 67.101 83.328  -30.656 1.00 17.40 ? 552  SER A N   1 
ATOM   4405 C  CA  . SER A 1 552  ? 66.381 82.066  -30.577 1.00 16.76 ? 552  SER A CA  1 
ATOM   4406 C  C   . SER A 1 552  ? 66.268 81.563  -29.168 1.00 16.86 ? 552  SER A C   1 
ATOM   4407 O  O   . SER A 1 552  ? 66.937 82.026  -28.281 1.00 16.54 ? 552  SER A O   1 
ATOM   4408 C  CB  . SER A 1 552  ? 67.096 81.012  -31.406 1.00 18.76 ? 552  SER A CB  1 
ATOM   4409 O  OG  . SER A 1 552  ? 68.371 80.706  -30.894 1.00 21.58 ? 552  SER A OG  1 
ATOM   4410 N  N   . LYS A 1 553  ? 65.437 80.544  -29.004 1.00 15.53 ? 553  LYS A N   1 
ATOM   4411 C  CA  . LYS A 1 553  ? 65.169 79.990  -27.675 1.00 14.83 ? 553  LYS A CA  1 
ATOM   4412 C  C   . LYS A 1 553  ? 64.857 78.505  -27.793 1.00 14.60 ? 553  LYS A C   1 
ATOM   4413 O  O   . LYS A 1 553  ? 64.064 78.060  -28.642 1.00 14.69 ? 553  LYS A O   1 
ATOM   4414 C  CB  . LYS A 1 553  ? 63.915 80.698  -27.113 1.00 16.51 ? 553  LYS A CB  1 
ATOM   4415 C  CG  . LYS A 1 553  ? 63.366 80.050  -25.802 1.00 18.10 ? 553  LYS A CG  1 
ATOM   4416 C  CD  . LYS A 1 553  ? 64.378 80.178  -24.682 1.00 17.43 ? 553  LYS A CD  1 
ATOM   4417 C  CE  . LYS A 1 553  ? 64.687 81.642  -24.325 1.00 18.01 ? 553  LYS A CE  1 
ATOM   4418 N  NZ  . LYS A 1 553  ? 65.856 81.764  -23.355 1.00 19.10 ? 553  LYS A NZ  1 
ATOM   4419 N  N   . HIS A 1 554  ? 65.487 77.746  -26.904 1.00 14.71 ? 554  HIS A N   1 
ATOM   4420 C  CA  . HIS A 1 554  ? 65.215 76.312  -26.804 1.00 14.39 ? 554  HIS A CA  1 
ATOM   4421 C  C   . HIS A 1 554  ? 64.018 76.040  -25.880 1.00 14.57 ? 554  HIS A C   1 
ATOM   4422 O  O   . HIS A 1 554  ? 63.866 76.673  -24.827 1.00 14.92 ? 554  HIS A O   1 
ATOM   4423 C  CB  . HIS A 1 554  ? 66.421 75.574  -26.190 1.00 17.26 ? 554  HIS A CB  1 
ATOM   4424 C  CG  . HIS A 1 554  ? 67.570 75.451  -27.126 1.00 19.34 ? 554  HIS A CG  1 
ATOM   4425 N  ND1 . HIS A 1 554  ? 68.219 74.265  -27.389 1.00 25.88 ? 554  HIS A ND1 1 
ATOM   4426 C  CD2 . HIS A 1 554  ? 68.205 76.400  -27.864 1.00 23.73 ? 554  HIS A CD2 1 
ATOM   4427 C  CE1 . HIS A 1 554  ? 69.213 74.491  -28.232 1.00 21.25 ? 554  HIS A CE1 1 
ATOM   4428 N  NE2 . HIS A 1 554  ? 69.225 75.775  -28.534 1.00 27.91 ? 554  HIS A NE2 1 
ATOM   4429 N  N   . VAL A 1 555  ? 63.180 75.123  -26.330 1.00 12.55 ? 555  VAL A N   1 
ATOM   4430 C  CA  . VAL A 1 555  ? 62.038 74.636  -25.542 1.00 13.41 ? 555  VAL A CA  1 
ATOM   4431 C  C   . VAL A 1 555  ? 62.126 73.125  -25.534 1.00 13.35 ? 555  VAL A C   1 
ATOM   4432 O  O   . VAL A 1 555  ? 62.655 72.513  -26.469 1.00 14.33 ? 555  VAL A O   1 
ATOM   4433 C  CB  . VAL A 1 555  ? 60.652 75.096  -26.099 1.00 13.29 ? 555  VAL A CB  1 
ATOM   4434 C  CG1 . VAL A 1 555  ? 60.574 76.617  -26.015 1.00 14.29 ? 555  VAL A CG1 1 
ATOM   4435 C  CG2 . VAL A 1 555  ? 60.433 74.605  -27.515 1.00 14.18 ? 555  VAL A CG2 1 
ATOM   4436 N  N   . VAL A 1 556  ? 61.595 72.498  -24.471 1.00 12.77 ? 556  VAL A N   1 
ATOM   4437 C  CA  . VAL A 1 556  ? 61.655 71.044  -24.324 1.00 13.16 ? 556  VAL A CA  1 
ATOM   4438 C  C   . VAL A 1 556  ? 60.288 70.538  -23.906 1.00 11.48 ? 556  VAL A C   1 
ATOM   4439 O  O   . VAL A 1 556  ? 59.636 71.153  -23.030 1.00 13.28 ? 556  VAL A O   1 
ATOM   4440 C  CB  . VAL A 1 556  ? 62.660 70.640  -23.210 1.00 12.64 ? 556  VAL A CB  1 
ATOM   4441 C  CG1 . VAL A 1 556  ? 62.586 69.154  -22.950 1.00 12.31 ? 556  VAL A CG1 1 
ATOM   4442 C  CG2 . VAL A 1 556  ? 64.054 71.048  -23.632 1.00 13.48 ? 556  VAL A CG2 1 
ATOM   4443 N  N   . MET A 1 557  ? 59.855 69.459  -24.522 1.00 12.58 ? 557  MET A N   1 
ATOM   4444 C  CA  . MET A 1 557  ? 58.593 68.810  -24.154 1.00 12.13 ? 557  MET A CA  1 
ATOM   4445 C  C   . MET A 1 557  ? 58.892 67.489  -23.491 1.00 13.63 ? 557  MET A C   1 
ATOM   4446 O  O   . MET A 1 557  ? 59.778 66.757  -23.907 1.00 13.02 ? 557  MET A O   1 
ATOM   4447 C  CB  . MET A 1 557  ? 57.698 68.511  -25.389 1.00 12.86 ? 557  MET A CB  1 
ATOM   4448 C  CG  . MET A 1 557  ? 56.699 69.641  -25.702 1.00 14.11 ? 557  MET A CG  1 
ATOM   4449 S  SD  . MET A 1 557  ? 57.381 71.273  -25.930 1.00 15.04 ? 557  MET A SD  1 
ATOM   4450 C  CE  . MET A 1 557  ? 58.406 70.980  -27.395 1.00 15.87 ? 557  MET A CE  1 
ATOM   4451 N  N   . HIS A 1 558  ? 58.127 67.187  -22.438 1.00 11.26 ? 558  HIS A N   1 
ATOM   4452 C  CA  . HIS A 1 558  ? 58.206 65.880  -21.775 1.00 11.61 ? 558  HIS A CA  1 
ATOM   4453 C  C   . HIS A 1 558  ? 56.893 65.107  -21.985 1.00 11.75 ? 558  HIS A C   1 
ATOM   4454 O  O   . HIS A 1 558  ? 55.798 65.681  -21.973 1.00 12.13 ? 558  HIS A O   1 
ATOM   4455 C  CB  . HIS A 1 558  ? 58.385 66.064  -20.256 1.00 11.31 ? 558  HIS A CB  1 
ATOM   4456 C  CG  . HIS A 1 558  ? 58.252 64.798  -19.477 1.00 10.62 ? 558  HIS A CG  1 
ATOM   4457 N  ND1 . HIS A 1 558  ? 57.292 64.643  -18.486 1.00 12.40 ? 558  HIS A ND1 1 
ATOM   4458 C  CD2 . HIS A 1 558  ? 58.981 63.659  -19.486 1.00 10.55 ? 558  HIS A CD2 1 
ATOM   4459 C  CE1 . HIS A 1 558  ? 57.453 63.456  -17.917 1.00 12.43 ? 558  HIS A CE1 1 
ATOM   4460 N  NE2 . HIS A 1 558  ? 58.464 62.833  -18.506 1.00 12.31 ? 558  HIS A NE2 1 
ATOM   4461 N  N   . ASN A 1 559  ? 57.018 63.797  -22.208 1.00 10.85 ? 559  ASN A N   1 
ATOM   4462 C  CA  . ASN A 1 559  ? 55.871 62.943  -22.395 1.00 10.64 ? 559  ASN A CA  1 
ATOM   4463 C  C   . ASN A 1 559  ? 55.876 61.870  -21.320 1.00 12.38 ? 559  ASN A C   1 
ATOM   4464 O  O   . ASN A 1 559  ? 56.587 60.914  -21.439 1.00 12.80 ? 559  ASN A O   1 
ATOM   4465 C  CB  . ASN A 1 559  ? 55.945 62.287  -23.796 1.00 12.47 ? 559  ASN A CB  1 
ATOM   4466 C  CG  . ASN A 1 559  ? 54.948 61.202  -23.985 1.00 12.23 ? 559  ASN A CG  1 
ATOM   4467 O  OD1 . ASN A 1 559  ? 53.859 61.179  -23.396 1.00 13.13 ? 559  ASN A OD1 1 
ATOM   4468 N  ND2 . ASN A 1 559  ? 55.288 60.274  -24.871 1.00 13.50 ? 559  ASN A ND2 1 
ATOM   4469 N  N   . THR A 1 560  ? 55.009 62.004  -20.321 1.00 10.87 ? 560  THR A N   1 
ATOM   4470 C  CA  . THR A 1 560  ? 55.029 61.006  -19.222 1.00 11.53 ? 560  THR A CA  1 
ATOM   4471 C  C   . THR A 1 560  ? 54.411 59.652  -19.618 1.00 12.43 ? 560  THR A C   1 
ATOM   4472 O  O   . THR A 1 560  ? 54.588 58.677  -18.892 1.00 13.28 ? 560  THR A O   1 
ATOM   4473 C  CB  . THR A 1 560  ? 54.259 61.615  -18.041 1.00 12.46 ? 560  THR A CB  1 
ATOM   4474 O  OG1 . THR A 1 560  ? 54.554 60.880  -16.841 1.00 12.56 ? 560  THR A OG1 1 
ATOM   4475 C  CG2 . THR A 1 560  ? 52.787 61.611  -18.280 1.00 12.77 ? 560  THR A CG2 1 
ATOM   4476 N  N   . LEU A 1 561  ? 53.677 59.574  -20.740 1.00 12.26 ? 561  LEU A N   1 
ATOM   4477 C  CA  . LEU A 1 561  ? 53.066 58.330  -21.156 1.00 12.75 ? 561  LEU A CA  1 
ATOM   4478 C  C   . LEU A 1 561  ? 54.072 57.410  -21.838 1.00 12.60 ? 561  LEU A C   1 
ATOM   4479 O  O   . LEU A 1 561  ? 54.955 57.869  -22.562 1.00 12.06 ? 561  LEU A O   1 
ATOM   4480 C  CB  . LEU A 1 561  ? 51.921 58.621  -22.165 1.00 13.37 ? 561  LEU A CB  1 
ATOM   4481 C  CG  . LEU A 1 561  ? 50.798 59.543  -21.609 1.00 13.16 ? 561  LEU A CG  1 
ATOM   4482 C  CD1 . LEU A 1 561  ? 49.675 59.676  -22.677 1.00 15.47 ? 561  LEU A CD1 1 
ATOM   4483 C  CD2 . LEU A 1 561  ? 50.156 58.913  -20.388 1.00 13.77 ? 561  LEU A CD2 1 
ATOM   4484 N  N   . PRO A 1 562  ? 53.896 56.100  -21.675 1.00 12.74 ? 562  PRO A N   1 
ATOM   4485 C  CA  . PRO A 1 562  ? 54.807 55.124  -22.267 1.00 13.33 ? 562  PRO A CA  1 
ATOM   4486 C  C   . PRO A 1 562  ? 54.633 54.772  -23.716 1.00 15.01 ? 562  PRO A C   1 
ATOM   4487 O  O   . PRO A 1 562  ? 54.767 53.612  -24.095 1.00 14.95 ? 562  PRO A O   1 
ATOM   4488 C  CB  . PRO A 1 562  ? 54.654 53.933  -21.326 1.00 13.57 ? 562  PRO A CB  1 
ATOM   4489 C  CG  . PRO A 1 562  ? 53.189 53.960  -20.998 1.00 13.45 ? 562  PRO A CG  1 
ATOM   4490 C  CD  . PRO A 1 562  ? 52.889 55.448  -20.813 1.00 12.89 ? 562  PRO A CD  1 
ATOM   4491 N  N   . HIS A 1 563  ? 54.311 55.775  -24.527 1.00 14.50 ? 563  HIS A N   1 
ATOM   4492 C  CA  . HIS A 1 563  ? 54.236 55.543  -25.970 1.00 15.24 ? 563  HIS A CA  1 
ATOM   4493 C  C   . HIS A 1 563  ? 54.605 56.829  -26.634 1.00 15.42 ? 563  HIS A C   1 
ATOM   4494 O  O   . HIS A 1 563  ? 54.467 57.915  -26.060 1.00 15.91 ? 563  HIS A O   1 
ATOM   4495 C  CB  . HIS A 1 563  ? 52.841 55.068  -26.439 1.00 14.91 ? 563  HIS A CB  1 
ATOM   4496 C  CG  . HIS A 1 563  ? 51.703 55.930  -25.971 1.00 15.98 ? 563  HIS A CG  1 
ATOM   4497 N  ND1 . HIS A 1 563  ? 50.907 55.570  -24.907 1.00 15.20 ? 563  HIS A ND1 1 
ATOM   4498 C  CD2 . HIS A 1 563  ? 51.158 57.064  -26.483 1.00 15.27 ? 563  HIS A CD2 1 
ATOM   4499 C  CE1 . HIS A 1 563  ? 49.911 56.439  -24.786 1.00 16.68 ? 563  HIS A CE1 1 
ATOM   4500 N  NE2 . HIS A 1 563  ? 50.042 57.361  -25.727 1.00 16.50 ? 563  HIS A NE2 1 
ATOM   4501 N  N   . TRP A 1 564  ? 55.153 56.721  -27.847 1.00 15.25 ? 564  TRP A N   1 
ATOM   4502 C  CA  . TRP A 1 564  ? 55.471 57.918  -28.614 1.00 14.34 ? 564  TRP A CA  1 
ATOM   4503 C  C   . TRP A 1 564  ? 54.212 58.759  -28.755 1.00 14.96 ? 564  TRP A C   1 
ATOM   4504 O  O   . TRP A 1 564  ? 53.092 58.252  -28.968 1.00 15.84 ? 564  TRP A O   1 
ATOM   4505 C  CB  . TRP A 1 564  ? 55.924 57.533  -30.038 1.00 16.47 ? 564  TRP A CB  1 
ATOM   4506 C  CG  . TRP A 1 564  ? 57.320 57.088  -30.129 1.00 16.11 ? 564  TRP A CG  1 
ATOM   4507 C  CD1 . TRP A 1 564  ? 57.799 55.799  -29.998 1.00 16.79 ? 564  TRP A CD1 1 
ATOM   4508 C  CD2 . TRP A 1 564  ? 58.467 57.928  -30.279 1.00 15.74 ? 564  TRP A CD2 1 
ATOM   4509 N  NE1 . TRP A 1 564  ? 59.165 55.805  -30.048 1.00 17.76 ? 564  TRP A NE1 1 
ATOM   4510 C  CE2 . TRP A 1 564  ? 59.613 57.091  -30.223 1.00 16.95 ? 564  TRP A CE2 1 
ATOM   4511 C  CE3 . TRP A 1 564  ? 58.640 59.317  -30.453 1.00 15.60 ? 564  TRP A CE3 1 
ATOM   4512 C  CZ2 . TRP A 1 564  ? 60.930 57.598  -30.332 1.00 15.90 ? 564  TRP A CZ2 1 
ATOM   4513 C  CZ3 . TRP A 1 564  ? 59.955 59.830  -30.560 1.00 16.05 ? 564  TRP A CZ3 1 
ATOM   4514 C  CH2 . TRP A 1 564  ? 61.080 58.965  -30.498 1.00 17.71 ? 564  TRP A CH2 1 
ATOM   4515 N  N   . ARG A 1 565  ? 54.382 60.061  -28.615 1.00 14.60 ? 565  ARG A N   1 
ATOM   4516 C  CA  . ARG A 1 565  ? 53.238 60.909  -28.768 1.00 16.29 ? 565  ARG A CA  1 
ATOM   4517 C  C   . ARG A 1 565  ? 53.571 62.137  -29.593 1.00 16.49 ? 565  ARG A C   1 
ATOM   4518 O  O   . ARG A 1 565  ? 54.651 62.718  -29.461 1.00 18.84 ? 565  ARG A O   1 
ATOM   4519 C  CB  . ARG A 1 565  ? 52.748 61.347  -27.374 1.00 19.88 ? 565  ARG A CB  1 
ATOM   4520 C  CG  . ARG A 1 565  ? 51.391 61.974  -27.348 1.00 25.06 ? 565  ARG A CG  1 
ATOM   4521 C  CD  . ARG A 1 565  ? 50.585 61.630  -26.033 1.00 22.52 ? 565  ARG A CD  1 
ATOM   4522 N  NE  . ARG A 1 565  ? 51.339 61.981  -24.835 1.00 22.11 ? 565  ARG A NE  1 
ATOM   4523 C  CZ  . ARG A 1 565  ? 50.817 62.626  -23.798 1.00 16.01 ? 565  ARG A CZ  1 
ATOM   4524 N  NH1 . ARG A 1 565  ? 49.528 63.012  -23.789 1.00 16.32 ? 565  ARG A NH1 1 
ATOM   4525 N  NH2 . ARG A 1 565  ? 51.620 62.913  -22.763 1.00 15.87 ? 565  ARG A NH2 1 
ATOM   4526 N  N   . GLU A 1 566  ? 52.660 62.482  -30.481 1.00 19.25 ? 566  GLU A N   1 
ATOM   4527 C  CA  . GLU A 1 566  ? 52.765 63.742  -31.194 1.00 21.51 ? 566  GLU A CA  1 
ATOM   4528 C  C   . GLU A 1 566  ? 51.582 64.515  -30.603 1.00 24.60 ? 566  GLU A C   1 
ATOM   4529 O  O   . GLU A 1 566  ? 50.542 63.920  -30.261 1.00 27.28 ? 566  GLU A O   1 
ATOM   4530 C  CB  . GLU A 1 566  ? 52.532 63.589  -32.666 1.00 27.25 ? 566  GLU A CB  1 
ATOM   4531 C  CG  . GLU A 1 566  ? 53.620 62.936  -33.345 1.00 25.56 ? 566  GLU A CG  1 
ATOM   4532 C  CD  . GLU A 1 566  ? 53.349 62.901  -34.826 1.00 33.10 ? 566  GLU A CD  1 
ATOM   4533 O  OE1 . GLU A 1 566  ? 52.195 62.557  -35.202 1.00 36.50 ? 566  GLU A OE1 1 
ATOM   4534 O  OE2 . GLU A 1 566  ? 54.284 63.225  -35.590 1.00 32.54 ? 566  GLU A OE2 1 
ATOM   4535 N  N   . GLN A 1 567  ? 51.716 65.825  -30.479 1.00 20.18 ? 567  GLN A N   1 
ATOM   4536 C  CA  . GLN A 1 567  ? 50.633 66.644  -29.914 1.00 20.67 ? 567  GLN A CA  1 
ATOM   4537 C  C   . GLN A 1 567  ? 51.020 68.084  -30.264 1.00 18.86 ? 567  GLN A C   1 
ATOM   4538 O  O   . GLN A 1 567  ? 52.210 68.441  -30.265 1.00 17.31 ? 567  GLN A O   1 
ATOM   4539 C  CB  . GLN A 1 567  ? 50.546 66.494  -28.356 1.00 22.42 ? 567  GLN A CB  1 
ATOM   4540 C  CG  . GLN A 1 567  ? 49.424 67.359  -27.601 1.00 23.07 ? 567  GLN A CG  1 
ATOM   4541 C  CD  . GLN A 1 567  ? 49.823 67.843  -26.144 1.00 25.17 ? 567  GLN A CD  1 
ATOM   4542 O  OE1 . GLN A 1 567  ? 49.815 67.050  -25.168 1.00 18.98 ? 567  GLN A OE1 1 
ATOM   4543 N  NE2 . GLN A 1 567  ? 50.186 69.146  -26.018 1.00 24.41 ? 567  GLN A NE2 1 
ATOM   4544 N  N   . LEU A 1 568  ? 50.032 68.898  -30.616 1.00 16.20 ? 568  LEU A N   1 
ATOM   4545 C  CA  . LEU A 1 568  ? 50.337 70.306  -30.860 1.00 15.90 ? 568  LEU A CA  1 
ATOM   4546 C  C   . LEU A 1 568  ? 50.640 70.938  -29.516 1.00 14.77 ? 568  LEU A C   1 
ATOM   4547 O  O   . LEU A 1 568  ? 49.965 70.655  -28.486 1.00 17.05 ? 568  LEU A O   1 
ATOM   4548 C  CB  . LEU A 1 568  ? 49.140 71.055  -31.456 1.00 18.44 ? 568  LEU A CB  1 
ATOM   4549 C  CG  . LEU A 1 568  ? 48.798 70.747  -32.913 1.00 20.48 ? 568  LEU A CG  1 
ATOM   4550 C  CD1 . LEU A 1 568  ? 47.751 71.766  -33.392 1.00 21.59 ? 568  LEU A CD1 1 
ATOM   4551 C  CD2 . LEU A 1 568  ? 50.031 70.872  -33.778 1.00 23.25 ? 568  LEU A CD2 1 
ATOM   4552 N  N   . VAL A 1 569  ? 51.649 71.778  -29.540 1.00 13.05 ? 569  VAL A N   1 
ATOM   4553 C  CA  . VAL A 1 569  ? 52.034 72.570  -28.371 1.00 12.80 ? 569  VAL A CA  1 
ATOM   4554 C  C   . VAL A 1 569  ? 52.084 74.029  -28.765 1.00 14.82 ? 569  VAL A C   1 
ATOM   4555 O  O   . VAL A 1 569  ? 52.319 74.380  -29.927 1.00 16.25 ? 569  VAL A O   1 
ATOM   4556 C  CB  . VAL A 1 569  ? 53.410 72.192  -27.759 1.00 13.68 ? 569  VAL A CB  1 
ATOM   4557 C  CG1 . VAL A 1 569  ? 53.318 70.779  -27.127 1.00 14.63 ? 569  VAL A CG1 1 
ATOM   4558 C  CG2 . VAL A 1 569  ? 54.538 72.239  -28.814 1.00 14.47 ? 569  VAL A CG2 1 
ATOM   4559 N  N   . ASP A 1 570  ? 51.852 74.906  -27.823 1.00 14.12 ? 570  ASP A N   1 
ATOM   4560 C  CA  . ASP A 1 570  ? 51.898 76.320  -28.136 1.00 16.89 ? 570  ASP A CA  1 
ATOM   4561 C  C   . ASP A 1 570  ? 52.668 77.108  -27.101 1.00 16.47 ? 570  ASP A C   1 
ATOM   4562 O  O   . ASP A 1 570  ? 52.741 76.726  -25.919 1.00 17.82 ? 570  ASP A O   1 
ATOM   4563 C  CB  . ASP A 1 570  ? 50.488 76.915  -28.303 1.00 19.24 ? 570  ASP A CB  1 
ATOM   4564 C  CG  . ASP A 1 570  ? 49.687 76.976  -26.992 1.00 26.03 ? 570  ASP A CG  1 
ATOM   4565 O  OD1 . ASP A 1 570  ? 49.368 75.919  -26.428 1.00 30.72 ? 570  ASP A OD1 1 
ATOM   4566 O  OD2 . ASP A 1 570  ? 49.376 78.082  -26.523 1.00 28.33 ? 570  ASP A OD2 1 
ATOM   4567 N  N   . PHE A 1 571  ? 53.271 78.198  -27.556 1.00 14.94 ? 571  PHE A N   1 
ATOM   4568 C  CA  . PHE A 1 571  ? 54.017 79.111  -26.714 1.00 15.14 ? 571  PHE A CA  1 
ATOM   4569 C  C   . PHE A 1 571  ? 53.685 80.540  -27.101 1.00 14.90 ? 571  PHE A C   1 
ATOM   4570 O  O   . PHE A 1 571  ? 53.289 80.796  -28.256 1.00 16.46 ? 571  PHE A O   1 
ATOM   4571 C  CB  . PHE A 1 571  ? 55.537 78.921  -26.933 1.00 15.27 ? 571  PHE A CB  1 
ATOM   4572 C  CG  . PHE A 1 571  ? 56.040 77.575  -26.526 1.00 13.73 ? 571  PHE A CG  1 
ATOM   4573 C  CD1 . PHE A 1 571  ? 55.999 76.510  -27.390 1.00 14.73 ? 571  PHE A CD1 1 
ATOM   4574 C  CD2 . PHE A 1 571  ? 56.553 77.402  -25.240 1.00 15.32 ? 571  PHE A CD2 1 
ATOM   4575 C  CE1 . PHE A 1 571  ? 56.457 75.259  -26.991 1.00 15.40 ? 571  PHE A CE1 1 
ATOM   4576 C  CE2 . PHE A 1 571  ? 57.008 76.142  -24.840 1.00 13.16 ? 571  PHE A CE2 1 
ATOM   4577 C  CZ  . PHE A 1 571  ? 56.955 75.083  -25.707 1.00 16.09 ? 571  PHE A CZ  1 
ATOM   4578 N  N   . TYR A 1 572  ? 53.836 81.451  -26.148 1.00 14.87 ? 572  TYR A N   1 
ATOM   4579 C  CA  . TYR A 1 572  ? 53.693 82.882  -26.441 1.00 15.39 ? 572  TYR A CA  1 
ATOM   4580 C  C   . TYR A 1 572  ? 55.074 83.377  -26.875 1.00 17.38 ? 572  TYR A C   1 
ATOM   4581 O  O   . TYR A 1 572  ? 56.101 83.045  -26.246 1.00 16.06 ? 572  TYR A O   1 
ATOM   4582 C  CB  . TYR A 1 572  ? 53.257 83.674  -25.209 1.00 16.32 ? 572  TYR A CB  1 
ATOM   4583 C  CG  . TYR A 1 572  ? 51.807 83.569  -24.827 1.00 20.07 ? 572  TYR A CG  1 
ATOM   4584 C  CD1 . TYR A 1 572  ? 50.907 82.843  -25.593 1.00 19.93 ? 572  TYR A CD1 1 
ATOM   4585 C  CD2 . TYR A 1 572  ? 51.340 84.196  -23.671 1.00 23.16 ? 572  TYR A CD2 1 
ATOM   4586 C  CE1 . TYR A 1 572  ? 49.561 82.725  -25.231 1.00 23.17 ? 572  TYR A CE1 1 
ATOM   4587 C  CE2 . TYR A 1 572  ? 49.992 84.088  -23.301 1.00 24.94 ? 572  TYR A CE2 1 
ATOM   4588 C  CZ  . TYR A 1 572  ? 49.118 83.352  -24.092 1.00 22.47 ? 572  TYR A CZ  1 
ATOM   4589 O  OH  . TYR A 1 572  ? 47.778 83.236  -23.742 1.00 28.78 ? 572  TYR A OH  1 
ATOM   4590 N  N   . VAL A 1 573  ? 55.103 84.183  -27.941 1.00 15.47 ? 573  VAL A N   1 
ATOM   4591 C  CA  . VAL A 1 573  ? 56.370 84.736  -28.457 1.00 16.24 ? 573  VAL A CA  1 
ATOM   4592 C  C   . VAL A 1 573  ? 56.140 86.203  -28.737 1.00 15.47 ? 573  VAL A C   1 
ATOM   4593 O  O   . VAL A 1 573  ? 55.011 86.621  -28.990 1.00 17.53 ? 573  VAL A O   1 
ATOM   4594 C  CB  . VAL A 1 573  ? 56.830 84.053  -29.756 1.00 16.06 ? 573  VAL A CB  1 
ATOM   4595 C  CG1 . VAL A 1 573  ? 57.399 82.684  -29.427 1.00 17.64 ? 573  VAL A CG1 1 
ATOM   4596 C  CG2 . VAL A 1 573  ? 55.682 83.929  -30.740 1.00 17.13 ? 573  VAL A CG2 1 
ATOM   4597 N  N   . SER A 1 574  ? 57.219 86.980  -28.743 1.00 17.33 ? 574  SER A N   1 
ATOM   4598 C  CA  . SER A 1 574  ? 57.104 88.438  -28.906 1.00 18.85 ? 574  SER A CA  1 
ATOM   4599 C  C   . SER A 1 574  ? 57.063 88.955  -30.332 1.00 20.58 ? 574  SER A C   1 
ATOM   4600 O  O   . SER A 1 574  ? 57.009 90.188  -30.557 1.00 24.14 ? 574  SER A O   1 
ATOM   4601 C  CB  . SER A 1 574  ? 58.230 89.119  -28.128 1.00 20.26 ? 574  SER A CB  1 
ATOM   4602 O  OG  . SER A 1 574  ? 59.502 88.788  -28.650 1.00 18.84 ? 574  SER A OG  1 
ATOM   4603 N  N   . SER A 1 575  ? 57.058 88.038  -31.286 1.00 20.89 ? 575  SER A N   1 
ATOM   4604 C  CA  . SER A 1 575  ? 56.989 88.389  -32.691 1.00 20.37 ? 575  SER A CA  1 
ATOM   4605 C  C   . SER A 1 575  ? 56.242 87.304  -33.437 1.00 20.80 ? 575  SER A C   1 
ATOM   4606 O  O   . SER A 1 575  ? 56.292 86.124  -33.065 1.00 17.78 ? 575  SER A O   1 
ATOM   4607 C  CB  . SER A 1 575  ? 58.407 88.471  -33.278 1.00 21.35 ? 575  SER A CB  1 
ATOM   4608 O  OG  . SER A 1 575  ? 58.407 88.566  -34.709 1.00 22.24 ? 575  SER A OG  1 
ATOM   4609 N  N   . PRO A 1 576  ? 55.535 87.673  -34.507 1.00 19.17 ? 576  PRO A N   1 
ATOM   4610 C  CA  . PRO A 1 576  ? 54.818 86.661  -35.281 1.00 19.31 ? 576  PRO A CA  1 
ATOM   4611 C  C   . PRO A 1 576  ? 55.768 85.982  -36.272 1.00 18.75 ? 576  PRO A C   1 
ATOM   4612 O  O   . PRO A 1 576  ? 55.419 84.982  -36.883 1.00 20.92 ? 576  PRO A O   1 
ATOM   4613 C  CB  . PRO A 1 576  ? 53.725 87.457  -35.984 1.00 20.27 ? 576  PRO A CB  1 
ATOM   4614 C  CG  . PRO A 1 576  ? 54.331 88.830  -36.133 1.00 23.86 ? 576  PRO A CG  1 
ATOM   4615 C  CD  . PRO A 1 576  ? 55.216 89.051  -34.928 1.00 19.83 ? 576  PRO A CD  1 
ATOM   4616 N  N   . PHE A 1 577  ? 56.990 86.516  -36.419 1.00 18.75 ? 577  PHE A N   1 
ATOM   4617 C  CA  . PHE A 1 577  ? 57.896 85.962  -37.427 1.00 19.73 ? 577  PHE A CA  1 
ATOM   4618 C  C   . PHE A 1 577  ? 58.842 85.001  -36.762 1.00 20.17 ? 577  PHE A C   1 
ATOM   4619 O  O   . PHE A 1 577  ? 60.010 85.298  -36.550 1.00 20.03 ? 577  PHE A O   1 
ATOM   4620 C  CB  . PHE A 1 577  ? 58.656 87.099  -38.122 1.00 19.65 ? 577  PHE A CB  1 
ATOM   4621 C  CG  . PHE A 1 577  ? 57.738 88.147  -38.715 1.00 24.98 ? 577  PHE A CG  1 
ATOM   4622 C  CD1 . PHE A 1 577  ? 56.681 87.770  -39.523 1.00 21.79 ? 577  PHE A CD1 1 
ATOM   4623 C  CD2 . PHE A 1 577  ? 57.978 89.509  -38.496 1.00 26.96 ? 577  PHE A CD2 1 
ATOM   4624 C  CE1 . PHE A 1 577  ? 55.855 88.743  -40.129 1.00 26.24 ? 577  PHE A CE1 1 
ATOM   4625 C  CE2 . PHE A 1 577  ? 57.171 90.481  -39.091 1.00 29.09 ? 577  PHE A CE2 1 
ATOM   4626 C  CZ  . PHE A 1 577  ? 56.115 90.084  -39.905 1.00 28.50 ? 577  PHE A CZ  1 
ATOM   4627 N  N   . VAL A 1 578  ? 58.292 83.830  -36.421 1.00 18.96 ? 578  VAL A N   1 
ATOM   4628 C  CA  . VAL A 1 578  ? 59.073 82.809  -35.725 1.00 17.72 ? 578  VAL A CA  1 
ATOM   4629 C  C   . VAL A 1 578  ? 58.930 81.476  -36.425 1.00 17.82 ? 578  VAL A C   1 
ATOM   4630 O  O   . VAL A 1 578  ? 57.865 81.147  -36.912 1.00 21.05 ? 578  VAL A O   1 
ATOM   4631 C  CB  . VAL A 1 578  ? 58.586 82.701  -34.213 1.00 16.68 ? 578  VAL A CB  1 
ATOM   4632 C  CG1 . VAL A 1 578  ? 59.364 81.568  -33.472 1.00 16.55 ? 578  VAL A CG1 1 
ATOM   4633 C  CG2 . VAL A 1 578  ? 58.845 83.984  -33.510 1.00 17.80 ? 578  VAL A CG2 1 
ATOM   4634 N  N   . SER A 1 579  ? 60.021 80.732  -36.515 1.00 20.33 ? 579  SER A N   1 
ATOM   4635 C  CA  . SER A 1 579  ? 59.950 79.422  -37.122 1.00 20.03 ? 579  SER A CA  1 
ATOM   4636 C  C   . SER A 1 579  ? 60.519 78.420  -36.153 1.00 18.70 ? 579  SER A C   1 
ATOM   4637 O  O   . SER A 1 579  ? 61.271 78.767  -35.250 1.00 19.14 ? 579  SER A O   1 
ATOM   4638 C  CB  . SER A 1 579  ? 60.653 79.397  -38.479 1.00 26.20 ? 579  SER A CB  1 
ATOM   4639 O  OG  . SER A 1 579  ? 61.911 79.986  -38.375 1.00 27.28 ? 579  SER A OG  1 
ATOM   4640 N  N   . VAL A 1 580  ? 60.150 77.175  -36.355 1.00 16.51 ? 580  VAL A N   1 
ATOM   4641 C  CA  . VAL A 1 580  ? 60.563 76.122  -35.448 1.00 15.22 ? 580  VAL A CA  1 
ATOM   4642 C  C   . VAL A 1 580  ? 61.440 75.095  -36.121 1.00 16.16 ? 580  VAL A C   1 
ATOM   4643 O  O   . VAL A 1 580  ? 61.193 74.729  -37.278 1.00 18.78 ? 580  VAL A O   1 
ATOM   4644 C  CB  . VAL A 1 580  ? 59.288 75.408  -34.924 1.00 16.25 ? 580  VAL A CB  1 
ATOM   4645 C  CG1 . VAL A 1 580  ? 59.650 74.355  -33.892 1.00 16.68 ? 580  VAL A CG1 1 
ATOM   4646 C  CG2 . VAL A 1 580  ? 58.309 76.443  -34.300 1.00 16.54 ? 580  VAL A CG2 1 
ATOM   4647 N  N   . THR A 1 581  ? 62.412 74.590  -35.365 1.00 16.46 ? 581  THR A N   1 
ATOM   4648 C  CA  . THR A 1 581  ? 63.275 73.517  -35.852 1.00 16.48 ? 581  THR A CA  1 
ATOM   4649 C  C   . THR A 1 581  ? 63.455 72.505  -34.726 1.00 17.13 ? 581  THR A C   1 
ATOM   4650 O  O   . THR A 1 581  ? 63.217 72.838  -33.579 1.00 16.82 ? 581  THR A O   1 
ATOM   4651 C  CB  . THR A 1 581  ? 64.715 74.005  -36.272 1.00 19.55 ? 581  THR A CB  1 
ATOM   4652 O  OG1 . THR A 1 581  ? 65.267 74.896  -35.299 1.00 21.34 ? 581  THR A OG1 1 
ATOM   4653 C  CG2 . THR A 1 581  ? 64.661 74.755  -37.604 1.00 17.98 ? 581  THR A CG2 1 
ATOM   4654 N  N   . ASP A 1 582  ? 63.754 71.263  -35.064 1.00 16.53 ? 582  ASP A N   1 
ATOM   4655 C  CA  . ASP A 1 582  ? 64.075 70.248  -34.061 1.00 17.96 ? 582  ASP A CA  1 
ATOM   4656 C  C   . ASP A 1 582  ? 65.600 70.359  -33.771 1.00 20.80 ? 582  ASP A C   1 
ATOM   4657 O  O   . ASP A 1 582  ? 66.265 71.230  -34.334 1.00 18.67 ? 582  ASP A O   1 
ATOM   4658 C  CB  . ASP A 1 582  ? 63.610 68.855  -34.520 1.00 20.90 ? 582  ASP A CB  1 
ATOM   4659 C  CG  . ASP A 1 582  ? 64.347 68.308  -35.748 1.00 20.09 ? 582  ASP A CG  1 
ATOM   4660 O  OD1 . ASP A 1 582  ? 65.403 68.835  -36.133 1.00 20.11 ? 582  ASP A OD1 1 
ATOM   4661 O  OD2 . ASP A 1 582  ? 63.829 67.296  -36.275 1.00 22.88 ? 582  ASP A OD2 1 
ATOM   4662 N  N   . LEU A 1 583  ? 66.198 69.535  -32.899 1.00 25.44 ? 583  LEU A N   1 
ATOM   4663 C  CA  . LEU A 1 583  ? 67.619 69.818  -32.695 1.00 27.28 ? 583  LEU A CA  1 
ATOM   4664 C  C   . LEU A 1 583  ? 68.544 69.294  -33.788 1.00 28.70 ? 583  LEU A C   1 
ATOM   4665 O  O   . LEU A 1 583  ? 69.769 69.418  -33.664 1.00 31.62 ? 583  LEU A O   1 
ATOM   4666 C  CB  . LEU A 1 583  ? 68.133 69.434  -31.272 1.00 28.22 ? 583  LEU A CB  1 
ATOM   4667 C  CG  . LEU A 1 583  ? 69.106 70.481  -30.630 1.00 25.15 ? 583  LEU A CG  1 
ATOM   4668 C  CD1 . LEU A 1 583  ? 68.431 71.842  -30.559 1.00 27.82 ? 583  LEU A CD1 1 
ATOM   4669 C  CD2 . LEU A 1 583  ? 69.529 70.111  -29.204 1.00 29.10 ? 583  LEU A CD2 1 
ATOM   4670 N  N   . ALA A 1 584  ? 67.977 68.730  -34.864 1.00 24.80 ? 584  ALA A N   1 
ATOM   4671 C  CA  . ALA A 1 584  ? 68.822 68.357  -36.001 1.00 21.46 ? 584  ALA A CA  1 
ATOM   4672 C  C   . ALA A 1 584  ? 68.643 69.488  -37.030 1.00 20.21 ? 584  ALA A C   1 
ATOM   4673 O  O   . ALA A 1 584  ? 69.080 69.384  -38.187 1.00 19.90 ? 584  ALA A O   1 
ATOM   4674 C  CB  . ALA A 1 584  ? 68.405 67.020  -36.607 1.00 21.54 ? 584  ALA A CB  1 
ATOM   4675 N  N   . ASN A 1 585  ? 67.992 70.574  -36.617 1.00 20.13 ? 585  ASN A N   1 
ATOM   4676 C  CA  . ASN A 1 585  ? 67.764 71.728  -37.482 1.00 21.06 ? 585  ASN A CA  1 
ATOM   4677 C  C   . ASN A 1 585  ? 66.760 71.453  -38.604 1.00 21.80 ? 585  ASN A C   1 
ATOM   4678 O  O   . ASN A 1 585  ? 66.720 72.175  -39.599 1.00 24.05 ? 585  ASN A O   1 
ATOM   4679 C  CB  . ASN A 1 585  ? 69.091 72.211  -38.089 1.00 24.21 ? 585  ASN A CB  1 
ATOM   4680 C  CG  A ASN A 1 585  ? 69.484 73.587  -37.617 0.50 27.41 ? 585  ASN A CG  1 
ATOM   4681 C  CG  B ASN A 1 585  ? 68.988 73.654  -38.529 0.50 23.58 ? 585  ASN A CG  1 
ATOM   4682 O  OD1 A ASN A 1 585  ? 68.692 74.533  -37.685 0.50 27.09 ? 585  ASN A OD1 1 
ATOM   4683 O  OD1 B ASN A 1 585  ? 69.733 74.020  -39.436 0.50 25.91 ? 585  ASN A OD1 1 
ATOM   4684 N  ND2 A ASN A 1 585  ? 70.714 73.716  -37.139 0.50 31.45 ? 585  ASN A ND2 1 
ATOM   4685 N  ND2 B ASN A 1 585  ? 68.076 74.451  -37.984 0.50 23.59 ? 585  ASN A ND2 1 
ATOM   4686 N  N   . ASN A 1 586  ? 65.945 70.420  -38.454 1.00 19.06 ? 586  ASN A N   1 
ATOM   4687 C  CA  . ASN A 1 586  ? 64.936 70.105  -39.474 1.00 20.33 ? 586  ASN A CA  1 
ATOM   4688 C  C   . ASN A 1 586  ? 63.783 71.075  -39.221 1.00 21.10 ? 586  ASN A C   1 
ATOM   4689 O  O   . ASN A 1 586  ? 63.338 71.235  -38.098 1.00 19.27 ? 586  ASN A O   1 
ATOM   4690 C  CB  . ASN A 1 586  ? 64.346 68.705  -39.312 1.00 21.08 ? 586  ASN A CB  1 
ATOM   4691 C  CG  . ASN A 1 586  ? 65.366 67.624  -39.438 1.00 20.57 ? 586  ASN A CG  1 
ATOM   4692 O  OD1 . ASN A 1 586  ? 66.243 67.677  -40.314 1.00 22.18 ? 586  ASN A OD1 1 
ATOM   4693 N  ND2 . ASN A 1 586  ? 65.267 66.613  -38.572 1.00 22.51 ? 586  ASN A ND2 1 
ATOM   4694 N  N   . PRO A 1 587  ? 63.259 71.717  -40.260 1.00 20.51 ? 587  PRO A N   1 
ATOM   4695 C  CA  . PRO A 1 587  ? 62.141 72.641  -40.054 1.00 19.63 ? 587  PRO A CA  1 
ATOM   4696 C  C   . PRO A 1 587  ? 60.897 71.883  -39.598 1.00 17.93 ? 587  PRO A C   1 
ATOM   4697 O  O   . PRO A 1 587  ? 60.655 70.742  -40.002 1.00 21.73 ? 587  PRO A O   1 
ATOM   4698 C  CB  . PRO A 1 587  ? 61.934 73.269  -41.435 1.00 22.61 ? 587  PRO A CB  1 
ATOM   4699 C  CG  . PRO A 1 587  ? 63.272 73.107  -42.116 1.00 27.08 ? 587  PRO A CG  1 
ATOM   4700 C  CD  . PRO A 1 587  ? 63.744 71.741  -41.650 1.00 22.88 ? 587  PRO A CD  1 
ATOM   4701 N  N   . VAL A 1 588  ? 60.087 72.533  -38.754 1.00 17.65 ? 588  VAL A N   1 
ATOM   4702 C  CA  . VAL A 1 588  ? 58.862 71.944  -38.251 1.00 17.95 ? 588  VAL A CA  1 
ATOM   4703 C  C   . VAL A 1 588  ? 57.750 72.936  -38.615 1.00 15.72 ? 588  VAL A C   1 
ATOM   4704 O  O   . VAL A 1 588  ? 57.882 74.144  -38.350 1.00 18.70 ? 588  VAL A O   1 
ATOM   4705 C  CB  . VAL A 1 588  ? 58.944 71.803  -36.711 1.00 16.98 ? 588  VAL A CB  1 
ATOM   4706 C  CG1 . VAL A 1 588  ? 57.622 71.325  -36.135 1.00 17.99 ? 588  VAL A CG1 1 
ATOM   4707 C  CG2 . VAL A 1 588  ? 60.094 70.852  -36.329 1.00 16.35 ? 588  VAL A CG2 1 
ATOM   4708 N  N   . GLU A 1 589  ? 56.693 72.438  -39.246 1.00 16.80 ? 589  GLU A N   1 
ATOM   4709 C  CA  . GLU A 1 589  ? 55.598 73.290  -39.656 1.00 17.67 ? 589  GLU A CA  1 
ATOM   4710 C  C   . GLU A 1 589  ? 54.968 73.920  -38.427 1.00 18.62 ? 589  GLU A C   1 
ATOM   4711 O  O   . GLU A 1 589  ? 54.707 73.228  -37.435 1.00 19.25 ? 589  GLU A O   1 
ATOM   4712 C  CB  . GLU A 1 589  ? 54.543 72.481  -40.401 1.00 22.63 ? 589  GLU A CB  1 
ATOM   4713 C  CG  . GLU A 1 589  ? 53.428 73.343  -40.895 1.00 33.21 ? 589  GLU A CG  1 
ATOM   4714 C  CD  . GLU A 1 589  ? 52.486 72.632  -41.839 1.00 39.43 ? 589  GLU A CD  1 
ATOM   4715 O  OE1 . GLU A 1 589  ? 52.962 71.804  -42.656 1.00 44.52 ? 589  GLU A OE1 1 
ATOM   4716 O  OE2 . GLU A 1 589  ? 51.266 72.931  -41.784 1.00 42.25 ? 589  GLU A OE2 1 
ATOM   4717 N  N   . ALA A 1 590  ? 54.699 75.210  -38.485 1.00 16.98 ? 590  ALA A N   1 
ATOM   4718 C  CA  . ALA A 1 590  ? 54.117 75.917  -37.360 1.00 15.86 ? 590  ALA A CA  1 
ATOM   4719 C  C   . ALA A 1 590  ? 53.018 76.838  -37.815 1.00 18.13 ? 590  ALA A C   1 
ATOM   4720 O  O   . ALA A 1 590  ? 52.947 77.169  -39.008 1.00 18.11 ? 590  ALA A O   1 
ATOM   4721 C  CB  . ALA A 1 590  ? 55.161 76.721  -36.635 1.00 17.76 ? 590  ALA A CB  1 
ATOM   4722 N  N   . GLN A 1 591  ? 52.186 77.253  -36.877 1.00 16.65 ? 591  GLN A N   1 
ATOM   4723 C  CA  . GLN A 1 591  ? 51.078 78.179  -37.142 1.00 15.77 ? 591  GLN A CA  1 
ATOM   4724 C  C   . GLN A 1 591  ? 51.149 79.250  -36.089 1.00 16.89 ? 591  GLN A C   1 
ATOM   4725 O  O   . GLN A 1 591  ? 51.393 78.964  -34.899 1.00 17.15 ? 591  GLN A O   1 
ATOM   4726 C  CB  . GLN A 1 591  ? 49.717 77.477  -37.047 1.00 16.43 ? 591  GLN A CB  1 
ATOM   4727 C  CG  . GLN A 1 591  ? 48.532 78.455  -37.041 1.00 15.55 ? 591  GLN A CG  1 
ATOM   4728 C  CD  . GLN A 1 591  ? 47.190 77.741  -36.795 1.00 15.45 ? 591  GLN A CD  1 
ATOM   4729 O  OE1 . GLN A 1 591  ? 46.942 76.664  -37.349 1.00 16.84 ? 591  GLN A OE1 1 
ATOM   4730 N  NE2 . GLN A 1 591  ? 46.342 78.338  -35.980 1.00 16.58 ? 591  GLN A NE2 1 
ATOM   4731 N  N   . VAL A 1 592  ? 50.978 80.499  -36.500 1.00 14.71 ? 592  VAL A N   1 
ATOM   4732 C  CA  . VAL A 1 592  ? 50.949 81.597  -35.558 1.00 14.50 ? 592  VAL A CA  1 
ATOM   4733 C  C   . VAL A 1 592  ? 49.548 82.185  -35.552 1.00 16.50 ? 592  VAL A C   1 
ATOM   4734 O  O   . VAL A 1 592  ? 48.898 82.298  -36.611 1.00 17.03 ? 592  VAL A O   1 
ATOM   4735 C  CB  . VAL A 1 592  ? 52.012 82.677  -35.894 1.00 15.55 ? 592  VAL A CB  1 
ATOM   4736 C  CG1 . VAL A 1 592  ? 51.747 83.924  -35.079 1.00 16.03 ? 592  VAL A CG1 1 
ATOM   4737 C  CG2 . VAL A 1 592  ? 53.426 82.160  -35.549 1.00 17.17 ? 592  VAL A CG2 1 
ATOM   4738 N  N   . SER A 1 593  ? 49.045 82.478  -34.363 1.00 17.78 ? 593  SER A N   1 
ATOM   4739 C  CA  . SER A 1 593  ? 47.711 83.049  -34.153 1.00 17.51 ? 593  SER A CA  1 
ATOM   4740 C  C   . SER A 1 593  ? 47.869 84.157  -33.170 1.00 17.68 ? 593  SER A C   1 
ATOM   4741 O  O   . SER A 1 593  ? 48.875 84.257  -32.432 1.00 19.44 ? 593  SER A O   1 
ATOM   4742 C  CB  . SER A 1 593  ? 46.720 82.024  -33.523 1.00 18.39 ? 593  SER A CB  1 
ATOM   4743 O  OG  . SER A 1 593  ? 46.565 80.841  -34.304 1.00 18.93 ? 593  SER A OG  1 
ATOM   4744 N  N   . PRO A 1 594  ? 46.873 85.017  -33.092 1.00 18.67 ? 594  PRO A N   1 
ATOM   4745 C  CA  . PRO A 1 594  ? 46.949 86.116  -32.129 1.00 16.62 ? 594  PRO A CA  1 
ATOM   4746 C  C   . PRO A 1 594  ? 46.699 85.599  -30.697 1.00 18.63 ? 594  PRO A C   1 
ATOM   4747 O  O   . PRO A 1 594  ? 46.266 84.446  -30.500 1.00 17.44 ? 594  PRO A O   1 
ATOM   4748 C  CB  . PRO A 1 594  ? 45.804 87.054  -32.554 1.00 17.36 ? 594  PRO A CB  1 
ATOM   4749 C  CG  . PRO A 1 594  ? 45.466 86.594  -33.991 1.00 16.07 ? 594  PRO A CG  1 
ATOM   4750 C  CD  . PRO A 1 594  ? 45.679 85.134  -33.958 1.00 16.26 ? 594  PRO A CD  1 
ATOM   4751 N  N   . VAL A 1 595  ? 47.006 86.442  -29.705 1.00 16.05 ? 595  VAL A N   1 
ATOM   4752 C  CA  . VAL A 1 595  ? 46.676 86.118  -28.329 1.00 17.82 ? 595  VAL A CA  1 
ATOM   4753 C  C   . VAL A 1 595  ? 45.399 86.913  -28.079 1.00 16.95 ? 595  VAL A C   1 
ATOM   4754 O  O   . VAL A 1 595  ? 45.403 88.144  -28.045 1.00 19.25 ? 595  VAL A O   1 
ATOM   4755 C  CB  . VAL A 1 595  ? 47.768 86.564  -27.343 1.00 17.38 ? 595  VAL A CB  1 
ATOM   4756 C  CG1 . VAL A 1 595  ? 47.245 86.352  -25.927 1.00 18.43 ? 595  VAL A CG1 1 
ATOM   4757 C  CG2 . VAL A 1 595  ? 49.060 85.734  -27.574 1.00 18.57 ? 595  VAL A CG2 1 
ATOM   4758 N  N   . TRP A 1 596  ? 44.274 86.208  -27.932 1.00 16.84 ? 596  TRP A N   1 
ATOM   4759 C  CA  . TRP A 1 596  ? 42.988 86.845  -27.705 1.00 18.38 ? 596  TRP A CA  1 
ATOM   4760 C  C   . TRP A 1 596  ? 42.562 86.733  -26.257 1.00 20.09 ? 596  TRP A C   1 
ATOM   4761 O  O   . TRP A 1 596  ? 42.652 85.652  -25.667 1.00 20.99 ? 596  TRP A O   1 
ATOM   4762 C  CB  . TRP A 1 596  ? 41.891 86.160  -28.555 1.00 18.80 ? 596  TRP A CB  1 
ATOM   4763 C  CG  . TRP A 1 596  ? 42.031 86.314  -30.023 1.00 17.94 ? 596  TRP A CG  1 
ATOM   4764 C  CD1 . TRP A 1 596  ? 42.444 85.365  -30.938 1.00 17.51 ? 596  TRP A CD1 1 
ATOM   4765 C  CD2 . TRP A 1 596  ? 41.747 87.487  -30.773 1.00 18.25 ? 596  TRP A CD2 1 
ATOM   4766 N  NE1 . TRP A 1 596  ? 42.429 85.891  -32.210 1.00 19.15 ? 596  TRP A NE1 1 
ATOM   4767 C  CE2 . TRP A 1 596  ? 42.005 87.190  -32.133 1.00 18.95 ? 596  TRP A CE2 1 
ATOM   4768 C  CE3 . TRP A 1 596  ? 41.295 88.774  -30.428 1.00 19.73 ? 596  TRP A CE3 1 
ATOM   4769 C  CZ2 . TRP A 1 596  ? 41.827 88.129  -33.143 1.00 20.03 ? 596  TRP A CZ2 1 
ATOM   4770 C  CZ3 . TRP A 1 596  ? 41.118 89.708  -31.461 1.00 20.43 ? 596  TRP A CZ3 1 
ATOM   4771 C  CH2 . TRP A 1 596  ? 41.386 89.371  -32.777 1.00 20.68 ? 596  TRP A CH2 1 
ATOM   4772 N  N   . SER A 1 597  ? 42.101 87.834  -25.685 1.00 19.80 ? 597  SER A N   1 
ATOM   4773 C  CA  . SER A 1 597  ? 41.583 87.800  -24.329 1.00 21.15 ? 597  SER A CA  1 
ATOM   4774 C  C   . SER A 1 597  ? 40.174 88.401  -24.352 1.00 21.29 ? 597  SER A C   1 
ATOM   4775 O  O   . SER A 1 597  ? 39.876 89.329  -25.125 1.00 24.01 ? 597  SER A O   1 
ATOM   4776 C  CB  . SER A 1 597  ? 42.494 88.573  -23.372 1.00 25.02 ? 597  SER A CB  1 
ATOM   4777 O  OG  . SER A 1 597  ? 42.611 89.885  -23.813 1.00 29.81 ? 597  SER A OG  1 
ATOM   4778 N  N   . TRP A 1 598  ? 39.300 87.889  -23.500 1.00 21.43 ? 598  TRP A N   1 
ATOM   4779 C  CA  . TRP A 1 598  ? 37.928 88.361  -23.481 1.00 20.25 ? 598  TRP A CA  1 
ATOM   4780 C  C   . TRP A 1 598  ? 37.687 89.310  -22.321 1.00 23.83 ? 598  TRP A C   1 
ATOM   4781 O  O   . TRP A 1 598  ? 38.202 89.117  -21.241 1.00 25.92 ? 598  TRP A O   1 
ATOM   4782 C  CB  . TRP A 1 598  ? 36.943 87.171  -23.409 1.00 20.32 ? 598  TRP A CB  1 
ATOM   4783 C  CG  . TRP A 1 598  ? 36.898 86.410  -24.703 1.00 17.52 ? 598  TRP A CG  1 
ATOM   4784 C  CD1 . TRP A 1 598  ? 37.801 85.520  -25.142 1.00 17.50 ? 598  TRP A CD1 1 
ATOM   4785 C  CD2 . TRP A 1 598  ? 35.888 86.492  -25.701 1.00 17.19 ? 598  TRP A CD2 1 
ATOM   4786 N  NE1 . TRP A 1 598  ? 37.429 85.018  -26.363 1.00 16.82 ? 598  TRP A NE1 1 
ATOM   4787 C  CE2 . TRP A 1 598  ? 36.250 85.595  -26.730 1.00 15.51 ? 598  TRP A CE2 1 
ATOM   4788 C  CE3 . TRP A 1 598  ? 34.705 87.231  -25.824 1.00 16.62 ? 598  TRP A CE3 1 
ATOM   4789 C  CZ2 . TRP A 1 598  ? 35.472 85.411  -27.875 1.00 17.29 ? 598  TRP A CZ2 1 
ATOM   4790 C  CZ3 . TRP A 1 598  ? 33.922 87.050  -26.961 1.00 15.46 ? 598  TRP A CZ3 1 
ATOM   4791 C  CH2 . TRP A 1 598  ? 34.318 86.142  -27.974 1.00 17.50 ? 598  TRP A CH2 1 
ATOM   4792 N  N   . HIS A 1 599  ? 36.891 90.333  -22.563 1.00 26.84 ? 599  HIS A N   1 
ATOM   4793 C  CA  . HIS A 1 599  ? 36.654 91.329  -21.533 1.00 31.02 ? 599  HIS A CA  1 
ATOM   4794 C  C   . HIS A 1 599  ? 35.196 91.663  -21.436 1.00 31.83 ? 599  HIS A C   1 
ATOM   4795 O  O   . HIS A 1 599  ? 34.504 91.730  -22.459 1.00 29.90 ? 599  HIS A O   1 
ATOM   4796 C  CB  . HIS A 1 599  ? 37.422 92.603  -21.873 1.00 34.32 ? 599  HIS A CB  1 
ATOM   4797 C  CG  . HIS A 1 599  ? 38.902 92.401  -21.938 1.00 38.21 ? 599  HIS A CG  1 
ATOM   4798 N  ND1 . HIS A 1 599  ? 39.666 92.140  -20.820 1.00 39.85 ? 599  HIS A ND1 1 
ATOM   4799 C  CD2 . HIS A 1 599  ? 39.748 92.344  -22.995 1.00 40.52 ? 599  HIS A CD2 1 
ATOM   4800 C  CE1 . HIS A 1 599  ? 40.918 91.926  -21.186 1.00 40.18 ? 599  HIS A CE1 1 
ATOM   4801 N  NE2 . HIS A 1 599  ? 40.995 92.044  -22.501 1.00 39.92 ? 599  HIS A NE2 1 
ATOM   4802 N  N   . HIS A 1 600  ? 34.722 91.851  -20.212 1.00 35.41 ? 600  HIS A N   1 
ATOM   4803 C  CA  . HIS A 1 600  ? 33.340 92.245  -20.035 1.00 38.92 ? 600  HIS A CA  1 
ATOM   4804 C  C   . HIS A 1 600  ? 33.455 93.743  -19.983 1.00 39.39 ? 600  HIS A C   1 
ATOM   4805 O  O   . HIS A 1 600  ? 33.831 94.312  -18.955 1.00 40.89 ? 600  HIS A O   1 
ATOM   4806 C  CB  . HIS A 1 600  ? 32.716 91.739  -18.730 1.00 43.02 ? 600  HIS A CB  1 
ATOM   4807 C  CG  . HIS A 1 600  ? 31.370 92.343  -18.460 1.00 48.43 ? 600  HIS A CG  1 
ATOM   4808 N  ND1 . HIS A 1 600  ? 30.406 92.468  -19.442 1.00 51.24 ? 600  HIS A ND1 1 
ATOM   4809 C  CD2 . HIS A 1 600  ? 30.849 92.923  -17.350 1.00 50.80 ? 600  HIS A CD2 1 
ATOM   4810 C  CE1 . HIS A 1 600  ? 29.354 93.101  -18.953 1.00 51.61 ? 600  HIS A CE1 1 
ATOM   4811 N  NE2 . HIS A 1 600  ? 29.597 93.390  -17.685 1.00 52.00 ? 600  HIS A NE2 1 
ATOM   4812 N  N   . ASP A 1 601  ? 33.156 94.361  -21.117 1.00 39.66 ? 601  ASP A N   1 
ATOM   4813 C  CA  . ASP A 1 601  ? 33.226 95.794  -21.292 1.00 41.09 ? 601  ASP A CA  1 
ATOM   4814 C  C   . ASP A 1 601  ? 32.079 96.461  -20.504 1.00 42.29 ? 601  ASP A C   1 
ATOM   4815 O  O   . ASP A 1 601  ? 30.916 96.323  -20.876 1.00 40.30 ? 601  ASP A O   1 
ATOM   4816 C  CB  . ASP A 1 601  ? 33.100 96.097  -22.788 1.00 41.97 ? 601  ASP A CB  1 
ATOM   4817 C  CG  . ASP A 1 601  ? 33.411 97.541  -23.126 1.00 45.19 ? 601  ASP A CG  1 
ATOM   4818 O  OD1 . ASP A 1 601  ? 32.982 98.442  -22.375 1.00 44.82 ? 601  ASP A OD1 1 
ATOM   4819 O  OD2 . ASP A 1 601  ? 34.069 97.792  -24.161 1.00 47.06 ? 601  ASP A OD2 1 
ATOM   4820 N  N   . THR A 1 602  ? 32.405 97.166  -19.419 1.00 43.57 ? 602  THR A N   1 
ATOM   4821 C  CA  . THR A 1 602  ? 31.368 97.837  -18.629 1.00 45.64 ? 602  THR A CA  1 
ATOM   4822 C  C   . THR A 1 602  ? 30.835 99.081  -19.324 1.00 44.87 ? 602  THR A C   1 
ATOM   4823 O  O   . THR A 1 602  ? 29.812 99.630  -18.905 1.00 46.82 ? 602  THR A O   1 
ATOM   4824 C  CB  . THR A 1 602  ? 31.855 98.238  -17.203 1.00 47.95 ? 602  THR A CB  1 
ATOM   4825 O  OG1 . THR A 1 602  ? 33.089 98.971  -17.293 1.00 50.34 ? 602  THR A OG1 1 
ATOM   4826 C  CG2 . THR A 1 602  ? 32.026 96.989  -16.319 1.00 48.17 ? 602  THR A CG2 1 
ATOM   4827 N  N   . LEU A 1 603  ? 31.507 99.522  -20.384 1.00 43.29 ? 603  LEU A N   1 
ATOM   4828 C  CA  . LEU A 1 603  ? 31.046 100.692 -21.128 1.00 42.63 ? 603  LEU A CA  1 
ATOM   4829 C  C   . LEU A 1 603  ? 29.969 100.325 -22.141 1.00 40.61 ? 603  LEU A C   1 
ATOM   4830 O  O   . LEU A 1 603  ? 28.919 100.952 -22.199 1.00 41.77 ? 603  LEU A O   1 
ATOM   4831 C  CB  . LEU A 1 603  ? 32.210 101.389 -21.857 1.00 44.43 ? 603  LEU A CB  1 
ATOM   4832 C  CG  . LEU A 1 603  ? 33.272 102.101 -21.007 1.00 46.38 ? 603  LEU A CG  1 
ATOM   4833 C  CD1 . LEU A 1 603  ? 32.585 103.009 -19.975 1.00 48.50 ? 603  LEU A CD1 1 
ATOM   4834 C  CD2 . LEU A 1 603  ? 34.138 101.071 -20.296 1.00 47.69 ? 603  LEU A CD2 1 
ATOM   4835 N  N   . THR A 1 604  ? 30.222 99.298  -22.938 1.00 36.23 ? 604  THR A N   1 
ATOM   4836 C  CA  . THR A 1 604  ? 29.263 98.874  -23.948 1.00 33.30 ? 604  THR A CA  1 
ATOM   4837 C  C   . THR A 1 604  ? 28.333 97.768  -23.440 1.00 30.21 ? 604  THR A C   1 
ATOM   4838 O  O   . THR A 1 604  ? 27.364 97.428  -24.116 1.00 29.93 ? 604  THR A O   1 
ATOM   4839 C  CB  . THR A 1 604  ? 29.989 98.333  -25.170 1.00 34.69 ? 604  THR A CB  1 
ATOM   4840 O  OG1 . THR A 1 604  ? 30.818 97.231  -24.761 1.00 37.01 ? 604  THR A OG1 1 
ATOM   4841 C  CG2 . THR A 1 604  ? 30.876 99.421  -25.795 1.00 36.14 ? 604  THR A CG2 1 
ATOM   4842 N  N   . LYS A 1 605  ? 28.631 97.215  -22.266 1.00 29.31 ? 605  LYS A N   1 
ATOM   4843 C  CA  . LYS A 1 605  ? 27.833 96.121  -21.692 1.00 29.51 ? 605  LYS A CA  1 
ATOM   4844 C  C   . LYS A 1 605  ? 27.827 94.913  -22.620 1.00 30.29 ? 605  LYS A C   1 
ATOM   4845 O  O   . LYS A 1 605  ? 26.773 94.332  -22.885 1.00 29.28 ? 605  LYS A O   1 
ATOM   4846 C  CB  . LYS A 1 605  ? 26.379 96.544  -21.442 1.00 29.55 ? 605  LYS A CB  1 
ATOM   4847 C  CG  . LYS A 1 605  ? 26.215 97.618  -20.415 1.00 32.39 ? 605  LYS A CG  1 
ATOM   4848 C  CD  . LYS A 1 605  ? 26.722 97.195  -19.027 1.00 34.03 ? 605  LYS A CD  1 
ATOM   4849 C  CE  . LYS A 1 605  ? 26.602 98.380  -18.045 1.00 34.79 ? 605  LYS A CE  1 
ATOM   4850 N  NZ  . LYS A 1 605  ? 27.015 98.051  -16.659 1.00 40.63 ? 605  LYS A NZ  1 
ATOM   4851 N  N   . THR A 1 606  ? 29.000 94.579  -23.147 1.00 27.65 ? 606  THR A N   1 
ATOM   4852 C  CA  . THR A 1 606  ? 29.175 93.410  -24.022 1.00 27.21 ? 606  THR A CA  1 
ATOM   4853 C  C   . THR A 1 606  ? 30.411 92.660  -23.565 1.00 26.30 ? 606  THR A C   1 
ATOM   4854 O  O   . THR A 1 606  ? 31.262 93.209  -22.862 1.00 26.22 ? 606  THR A O   1 
ATOM   4855 C  CB  . THR A 1 606  ? 29.444 93.793  -25.482 1.00 29.85 ? 606  THR A CB  1 
ATOM   4856 O  OG1 . THR A 1 606  ? 30.600 94.649  -25.535 1.00 31.56 ? 606  THR A OG1 1 
ATOM   4857 C  CG2 . THR A 1 606  ? 28.227 94.463  -26.108 1.00 30.11 ? 606  THR A CG2 1 
ATOM   4858 N  N   . ILE A 1 607  ? 30.498 91.392  -23.960 1.00 23.94 ? 607  ILE A N   1 
ATOM   4859 C  CA  . ILE A 1 607  ? 31.662 90.566  -23.664 1.00 22.34 ? 607  ILE A CA  1 
ATOM   4860 C  C   . ILE A 1 607  ? 32.323 90.353  -25.043 1.00 21.10 ? 607  ILE A C   1 
ATOM   4861 O  O   . ILE A 1 607  ? 31.747 89.743  -25.958 1.00 22.12 ? 607  ILE A O   1 
ATOM   4862 C  CB  . ILE A 1 607  ? 31.219 89.246  -23.070 1.00 20.82 ? 607  ILE A CB  1 
ATOM   4863 C  CG1 . ILE A 1 607  ? 30.357 89.508  -21.821 1.00 23.40 ? 607  ILE A CG1 1 
ATOM   4864 C  CG2 . ILE A 1 607  ? 32.454 88.379  -22.720 1.00 22.47 ? 607  ILE A CG2 1 
ATOM   4865 C  CD1 . ILE A 1 607  ? 29.603 88.290  -21.353 1.00 25.93 ? 607  ILE A CD1 1 
ATOM   4866 N  N   . HIS A 1 608  ? 33.535 90.868  -25.212 1.00 22.26 ? 608  HIS A N   1 
ATOM   4867 C  CA  . HIS A 1 608  ? 34.166 90.763  -26.516 1.00 21.59 ? 608  HIS A CA  1 
ATOM   4868 C  C   . HIS A 1 608  ? 35.657 90.566  -26.413 1.00 20.74 ? 608  HIS A C   1 
ATOM   4869 O  O   . HIS A 1 608  ? 36.246 90.838  -25.373 1.00 23.40 ? 608  HIS A O   1 
ATOM   4870 C  CB  . HIS A 1 608  ? 33.828 92.003  -27.336 1.00 27.19 ? 608  HIS A CB  1 
ATOM   4871 C  CG  . HIS A 1 608  ? 34.420 93.257  -26.792 1.00 29.33 ? 608  HIS A CG  1 
ATOM   4872 N  ND1 . HIS A 1 608  ? 34.287 93.645  -25.474 1.00 35.37 ? 608  HIS A ND1 1 
ATOM   4873 C  CD2 . HIS A 1 608  ? 35.152 94.222  -27.398 1.00 35.33 ? 608  HIS A CD2 1 
ATOM   4874 C  CE1 . HIS A 1 608  ? 34.909 94.798  -25.292 1.00 35.42 ? 608  HIS A CE1 1 
ATOM   4875 N  NE2 . HIS A 1 608  ? 35.441 95.171  -26.443 1.00 35.93 ? 608  HIS A NE2 1 
ATOM   4876 N  N   . PRO A 1 609  ? 36.296 90.110  -27.501 1.00 19.65 ? 609  PRO A N   1 
ATOM   4877 C  CA  . PRO A 1 609  ? 37.729 89.860  -27.478 1.00 20.91 ? 609  PRO A CA  1 
ATOM   4878 C  C   . PRO A 1 609  ? 38.620 90.999  -27.890 1.00 23.02 ? 609  PRO A C   1 
ATOM   4879 O  O   . PRO A 1 609  ? 38.274 91.757  -28.802 1.00 24.72 ? 609  PRO A O   1 
ATOM   4880 C  CB  . PRO A 1 609  ? 37.869 88.680  -28.427 1.00 20.53 ? 609  PRO A CB  1 
ATOM   4881 C  CG  . PRO A 1 609  ? 36.883 89.023  -29.504 1.00 21.03 ? 609  PRO A CG  1 
ATOM   4882 C  CD  . PRO A 1 609  ? 35.707 89.699  -28.785 1.00 19.65 ? 609  PRO A CD  1 
ATOM   4883 N  N   . GLN A 1 610  ? 39.766 91.080  -27.218 1.00 21.63 ? 610  GLN A N   1 
ATOM   4884 C  CA  . GLN A 1 610  ? 40.808 92.060  -27.511 1.00 23.78 ? 610  GLN A CA  1 
ATOM   4885 C  C   . GLN A 1 610  ? 42.040 91.257  -27.895 1.00 21.27 ? 610  GLN A C   1 
ATOM   4886 O  O   . GLN A 1 610  ? 42.341 90.258  -27.241 1.00 21.20 ? 610  GLN A O   1 
ATOM   4887 C  CB  . GLN A 1 610  ? 41.126 92.912  -26.279 1.00 29.04 ? 610  GLN A CB  1 
ATOM   4888 C  CG  . GLN A 1 610  ? 39.942 93.764  -25.796 1.00 38.68 ? 610  GLN A CG  1 
ATOM   4889 C  CD  . GLN A 1 610  ? 39.569 94.901  -26.754 1.00 42.50 ? 610  GLN A CD  1 
ATOM   4890 O  OE1 . GLN A 1 610  ? 38.977 94.686  -27.828 1.00 44.72 ? 610  GLN A OE1 1 
ATOM   4891 N  NE2 . GLN A 1 610  ? 39.923 96.126  -26.364 1.00 45.05 ? 610  GLN A NE2 1 
ATOM   4892 N  N   . GLY A 1 611  ? 42.735 91.679  -28.944 1.00 19.71 ? 611  GLY A N   1 
ATOM   4893 C  CA  . GLY A 1 611  ? 43.924 90.961  -29.368 1.00 20.45 ? 611  GLY A CA  1 
ATOM   4894 C  C   . GLY A 1 611  ? 45.188 91.687  -28.912 1.00 21.98 ? 611  GLY A C   1 
ATOM   4895 O  O   . GLY A 1 611  ? 45.222 92.926  -28.842 1.00 21.94 ? 611  GLY A O   1 
ATOM   4896 N  N   . SER A 1 612  ? 46.230 90.923  -28.597 1.00 22.67 ? 612  SER A N   1 
ATOM   4897 C  CA  . SER A 1 612  ? 47.477 91.553  -28.198 1.00 22.14 ? 612  SER A CA  1 
ATOM   4898 C  C   . SER A 1 612  ? 48.194 92.133  -29.398 1.00 20.12 ? 612  SER A C   1 
ATOM   4899 O  O   . SER A 1 612  ? 48.159 91.577  -30.490 1.00 22.61 ? 612  SER A O   1 
ATOM   4900 C  CB  . SER A 1 612  ? 48.416 90.533  -27.556 1.00 20.43 ? 612  SER A CB  1 
ATOM   4901 O  OG  . SER A 1 612  ? 49.670 91.147  -27.344 1.00 21.04 ? 612  SER A OG  1 
ATOM   4902 N  N   . THR A 1 613  ? 48.874 93.262  -29.205 1.00 26.65 ? 613  THR A N   1 
ATOM   4903 C  CA  . THR A 1 613  ? 49.633 93.817  -30.315 1.00 27.85 ? 613  THR A CA  1 
ATOM   4904 C  C   . THR A 1 613  ? 51.138 93.585  -30.058 1.00 29.27 ? 613  THR A C   1 
ATOM   4905 O  O   . THR A 1 613  ? 51.982 94.033  -30.847 1.00 31.61 ? 613  THR A O   1 
ATOM   4906 C  CB  . THR A 1 613  ? 49.380 95.319  -30.466 1.00 30.75 ? 613  THR A CB  1 
ATOM   4907 O  OG1 . THR A 1 613  ? 49.782 95.982  -29.264 1.00 30.33 ? 613  THR A OG1 1 
ATOM   4908 C  CG2 . THR A 1 613  ? 47.886 95.587  -30.682 1.00 31.47 ? 613  THR A CG2 1 
ATOM   4909 N  N   . THR A 1 614  ? 51.446 92.853  -28.981 1.00 27.58 ? 614  THR A N   1 
ATOM   4910 C  CA  . THR A 1 614  ? 52.828 92.571  -28.589 1.00 29.56 ? 614  THR A CA  1 
ATOM   4911 C  C   . THR A 1 614  ? 53.236 91.108  -28.360 1.00 29.66 ? 614  THR A C   1 
ATOM   4912 O  O   . THR A 1 614  ? 54.434 90.807  -28.289 1.00 30.36 ? 614  THR A O   1 
ATOM   4913 C  CB  . THR A 1 614  ? 53.175 93.336  -27.306 1.00 29.40 ? 614  THR A CB  1 
ATOM   4914 O  OG1 . THR A 1 614  ? 52.248 93.008  -26.267 1.00 34.49 ? 614  THR A OG1 1 
ATOM   4915 C  CG2 . THR A 1 614  ? 53.166 94.854  -27.575 1.00 34.79 ? 614  THR A CG2 1 
ATOM   4916 N  N   . LYS A 1 615  ? 52.259 90.212  -28.223 1.00 24.94 ? 615  LYS A N   1 
ATOM   4917 C  CA  . LYS A 1 615  ? 52.514 88.786  -27.976 1.00 23.35 ? 615  LYS A CA  1 
ATOM   4918 C  C   . LYS A 1 615  ? 51.684 88.018  -28.977 1.00 21.19 ? 615  LYS A C   1 
ATOM   4919 O  O   . LYS A 1 615  ? 50.583 88.446  -29.323 1.00 21.09 ? 615  LYS A O   1 
ATOM   4920 C  CB  . LYS A 1 615  ? 52.013 88.323  -26.598 1.00 26.37 ? 615  LYS A CB  1 
ATOM   4921 C  CG  . LYS A 1 615  ? 52.455 89.063  -25.394 1.00 31.87 ? 615  LYS A CG  1 
ATOM   4922 C  CD  . LYS A 1 615  ? 52.119 88.258  -24.131 1.00 31.41 ? 615  LYS A CD  1 
ATOM   4923 C  CE  . LYS A 1 615  ? 50.651 87.975  -23.930 1.00 30.68 ? 615  LYS A CE  1 
ATOM   4924 N  NZ  . LYS A 1 615  ? 50.437 87.771  -22.456 1.00 32.15 ? 615  LYS A NZ  1 
ATOM   4925 N  N   . TYR A 1 616  ? 52.174 86.851  -29.389 1.00 18.94 ? 616  TYR A N   1 
ATOM   4926 C  CA  . TYR A 1 616  ? 51.493 86.015  -30.359 1.00 17.89 ? 616  TYR A CA  1 
ATOM   4927 C  C   . TYR A 1 616  ? 51.637 84.577  -29.938 1.00 17.58 ? 616  TYR A C   1 
ATOM   4928 O  O   . TYR A 1 616  ? 52.536 84.254  -29.152 1.00 19.03 ? 616  TYR A O   1 
ATOM   4929 C  CB  . TYR A 1 616  ? 52.157 86.202  -31.742 1.00 17.46 ? 616  TYR A CB  1 
ATOM   4930 C  CG  . TYR A 1 616  ? 52.177 87.651  -32.114 1.00 21.32 ? 616  TYR A CG  1 
ATOM   4931 C  CD1 . TYR A 1 616  ? 51.068 88.226  -32.751 1.00 23.73 ? 616  TYR A CD1 1 
ATOM   4932 C  CD2 . TYR A 1 616  ? 53.239 88.474  -31.726 1.00 21.47 ? 616  TYR A CD2 1 
ATOM   4933 C  CE1 . TYR A 1 616  ? 51.011 89.572  -32.978 1.00 26.29 ? 616  TYR A CE1 1 
ATOM   4934 C  CE2 . TYR A 1 616  ? 53.195 89.837  -31.955 1.00 25.15 ? 616  TYR A CE2 1 
ATOM   4935 C  CZ  . TYR A 1 616  ? 52.078 90.373  -32.574 1.00 23.93 ? 616  TYR A CZ  1 
ATOM   4936 O  OH  . TYR A 1 616  ? 52.024 91.736  -32.784 1.00 32.32 ? 616  TYR A OH  1 
ATOM   4937 N  N   . ARG A 1 617  ? 50.783 83.707  -30.449 1.00 16.83 ? 617  ARG A N   1 
ATOM   4938 C  CA  . ARG A 1 617  ? 50.896 82.299  -30.108 1.00 17.64 ? 617  ARG A CA  1 
ATOM   4939 C  C   . ARG A 1 617  ? 51.521 81.526  -31.254 1.00 19.02 ? 617  ARG A C   1 
ATOM   4940 O  O   . ARG A 1 617  ? 51.064 81.673  -32.383 1.00 19.31 ? 617  ARG A O   1 
ATOM   4941 C  CB  . ARG A 1 617  ? 49.524 81.685  -29.857 1.00 21.54 ? 617  ARG A CB  1 
ATOM   4942 C  CG  . ARG A 1 617  ? 48.848 82.030  -28.554 1.00 26.77 ? 617  ARG A CG  1 
ATOM   4943 C  CD  . ARG A 1 617  ? 47.446 81.373  -28.474 1.00 26.88 ? 617  ARG A CD  1 
ATOM   4944 N  NE  . ARG A 1 617  ? 47.496 79.911  -28.539 1.00 25.71 ? 617  ARG A NE  1 
ATOM   4945 C  CZ  . ARG A 1 617  ? 46.816 79.166  -29.412 1.00 27.00 ? 617  ARG A CZ  1 
ATOM   4946 N  NH1 . ARG A 1 617  ? 46.022 79.734  -30.312 1.00 26.40 ? 617  ARG A NH1 1 
ATOM   4947 N  NH2 . ARG A 1 617  ? 46.921 77.852  -29.393 1.00 25.60 ? 617  ARG A NH2 1 
ATOM   4948 N  N   . ILE A 1 618  ? 52.555 80.717  -31.001 1.00 15.68 ? 618  ILE A N   1 
ATOM   4949 C  CA  . ILE A 1 618  ? 53.074 79.855  -32.046 1.00 18.47 ? 618  ILE A CA  1 
ATOM   4950 C  C   . ILE A 1 618  ? 52.724 78.432  -31.653 1.00 17.00 ? 618  ILE A C   1 
ATOM   4951 O  O   . ILE A 1 618  ? 52.897 78.035  -30.494 1.00 16.95 ? 618  ILE A O   1 
ATOM   4952 C  CB  . ILE A 1 618  ? 54.562 80.030  -32.299 1.00 17.30 ? 618  ILE A CB  1 
ATOM   4953 C  CG1 . ILE A 1 618  ? 54.938 79.152  -33.483 1.00 19.49 ? 618  ILE A CG1 1 
ATOM   4954 C  CG2 . ILE A 1 618  ? 55.412 79.715  -31.040 1.00 17.67 ? 618  ILE A CG2 1 
ATOM   4955 C  CD1 . ILE A 1 618  ? 56.163 79.601  -34.192 1.00 19.86 ? 618  ILE A CD1 1 
ATOM   4956 N  N   . ILE A 1 619  ? 52.240 77.662  -32.617 1.00 17.09 ? 619  ILE A N   1 
ATOM   4957 C  CA  . ILE A 1 619  ? 51.770 76.304  -32.415 1.00 16.71 ? 619  ILE A CA  1 
ATOM   4958 C  C   . ILE A 1 619  ? 52.481 75.352  -33.353 1.00 17.33 ? 619  ILE A C   1 
ATOM   4959 O  O   . ILE A 1 619  ? 52.650 75.672  -34.525 1.00 16.70 ? 619  ILE A O   1 
ATOM   4960 C  CB  . ILE A 1 619  ? 50.263 76.276  -32.746 1.00 19.99 ? 619  ILE A CB  1 
ATOM   4961 C  CG1 . ILE A 1 619  ? 49.590 77.392  -31.947 1.00 21.54 ? 619  ILE A CG1 1 
ATOM   4962 C  CG2 . ILE A 1 619  ? 49.657 74.914  -32.542 1.00 23.03 ? 619  ILE A CG2 1 
ATOM   4963 C  CD1 . ILE A 1 619  ? 48.437 78.084  -32.731 1.00 24.90 ? 619  ILE A CD1 1 
ATOM   4964 N  N   . PHE A 1 620  ? 52.879 74.170  -32.896 1.00 13.90 ? 620  PHE A N   1 
ATOM   4965 C  CA  . PHE A 1 620  ? 53.533 73.221  -33.789 1.00 14.09 ? 620  PHE A CA  1 
ATOM   4966 C  C   . PHE A 1 620  ? 53.417 71.840  -33.177 1.00 15.06 ? 620  PHE A C   1 
ATOM   4967 O  O   . PHE A 1 620  ? 53.164 71.718  -31.973 1.00 16.69 ? 620  PHE A O   1 
ATOM   4968 C  CB  . PHE A 1 620  ? 55.020 73.589  -33.985 1.00 14.93 ? 620  PHE A CB  1 
ATOM   4969 C  CG  . PHE A 1 620  ? 55.863 73.504  -32.729 1.00 13.97 ? 620  PHE A CG  1 
ATOM   4970 C  CD1 . PHE A 1 620  ? 56.528 72.318  -32.404 1.00 14.52 ? 620  PHE A CD1 1 
ATOM   4971 C  CD2 . PHE A 1 620  ? 56.033 74.621  -31.921 1.00 13.87 ? 620  PHE A CD2 1 
ATOM   4972 C  CE1 . PHE A 1 620  ? 57.388 72.248  -31.266 1.00 13.93 ? 620  PHE A CE1 1 
ATOM   4973 C  CE2 . PHE A 1 620  ? 56.891 74.567  -30.776 1.00 14.17 ? 620  PHE A CE2 1 
ATOM   4974 C  CZ  . PHE A 1 620  ? 57.552 73.375  -30.480 1.00 15.95 ? 620  PHE A CZ  1 
ATOM   4975 N  N   . LYS A 1 621  ? 53.619 70.814  -33.977 1.00 14.95 ? 621  LYS A N   1 
ATOM   4976 C  CA  . LYS A 1 621  ? 53.523 69.478  -33.455 1.00 16.90 ? 621  LYS A CA  1 
ATOM   4977 C  C   . LYS A 1 621  ? 54.847 69.022  -32.840 1.00 16.92 ? 621  LYS A C   1 
ATOM   4978 O  O   . LYS A 1 621  ? 55.901 69.054  -33.490 1.00 18.26 ? 621  LYS A O   1 
ATOM   4979 C  CB  . LYS A 1 621  ? 53.116 68.533  -34.611 1.00 19.00 ? 621  LYS A CB  1 
ATOM   4980 C  CG  . LYS A 1 621  ? 52.726 67.162  -34.124 1.00 24.37 ? 621  LYS A CG  1 
ATOM   4981 C  CD  . LYS A 1 621  ? 51.814 66.476  -35.129 1.00 31.71 ? 621  LYS A CD  1 
ATOM   4982 C  CE  . LYS A 1 621  ? 52.424 66.477  -36.515 1.00 33.33 ? 621  LYS A CE  1 
ATOM   4983 N  NZ  . LYS A 1 621  ? 51.593 65.644  -37.462 1.00 37.52 ? 621  LYS A NZ  1 
ATOM   4984 N  N   . ALA A 1 622  ? 54.802 68.598  -31.570 1.00 15.12 ? 622  ALA A N   1 
ATOM   4985 C  CA  . ALA A 1 622  ? 56.004 68.052  -30.944 1.00 15.40 ? 622  ALA A CA  1 
ATOM   4986 C  C   . ALA A 1 622  ? 55.889 66.521  -30.918 1.00 15.19 ? 622  ALA A C   1 
ATOM   4987 O  O   . ALA A 1 622  ? 54.813 65.969  -30.655 1.00 17.95 ? 622  ALA A O   1 
ATOM   4988 C  CB  . ALA A 1 622  ? 56.146 68.567  -29.513 1.00 14.95 ? 622  ALA A CB  1 
ATOM   4989 N  N   . ARG A 1 623  ? 56.966 65.844  -31.285 1.00 14.35 ? 623  ARG A N   1 
ATOM   4990 C  CA  . ARG A 1 623  ? 56.986 64.380  -31.290 1.00 15.53 ? 623  ARG A CA  1 
ATOM   4991 C  C   . ARG A 1 623  ? 57.968 64.012  -30.188 1.00 14.82 ? 623  ARG A C   1 
ATOM   4992 O  O   . ARG A 1 623  ? 59.143 64.359  -30.231 1.00 16.95 ? 623  ARG A O   1 
ATOM   4993 C  CB  . ARG A 1 623  ? 57.445 63.892  -32.665 1.00 17.73 ? 623  ARG A CB  1 
ATOM   4994 C  CG  . ARG A 1 623  ? 57.621 62.397  -32.735 1.00 21.15 ? 623  ARG A CG  1 
ATOM   4995 C  CD  . ARG A 1 623  ? 57.772 61.877  -34.195 1.00 22.49 ? 623  ARG A CD  1 
ATOM   4996 N  NE  . ARG A 1 623  ? 57.883 60.411  -34.169 1.00 25.58 ? 623  ARG A NE  1 
ATOM   4997 C  CZ  . ARG A 1 623  ? 59.035 59.766  -33.999 1.00 27.18 ? 623  ARG A CZ  1 
ATOM   4998 N  NH1 . ARG A 1 623  ? 60.184 60.440  -33.870 1.00 30.49 ? 623  ARG A NH1 1 
ATOM   4999 N  NH2 . ARG A 1 623  ? 59.034 58.445  -33.856 1.00 30.68 ? 623  ARG A NH2 1 
ATOM   5000 N  N   . VAL A 1 624  ? 57.443 63.303  -29.185 1.00 14.35 ? 624  VAL A N   1 
ATOM   5001 C  CA  . VAL A 1 624  ? 58.219 63.017  -27.974 1.00 13.72 ? 624  VAL A CA  1 
ATOM   5002 C  C   . VAL A 1 624  ? 58.256 61.533  -27.668 1.00 12.91 ? 624  VAL A C   1 
ATOM   5003 O  O   . VAL A 1 624  ? 57.239 60.876  -27.735 1.00 13.72 ? 624  VAL A O   1 
ATOM   5004 C  CB  . VAL A 1 624  ? 57.547 63.782  -26.814 1.00 14.11 ? 624  VAL A CB  1 
ATOM   5005 C  CG1 . VAL A 1 624  ? 58.466 63.780  -25.605 1.00 14.87 ? 624  VAL A CG1 1 
ATOM   5006 C  CG2 . VAL A 1 624  ? 57.230 65.245  -27.241 1.00 14.91 ? 624  VAL A CG2 1 
ATOM   5007 N  N   . PRO A 1 625  ? 59.453 61.009  -27.294 1.00 13.92 ? 625  PRO A N   1 
ATOM   5008 C  CA  . PRO A 1 625  ? 59.559 59.577  -26.997 1.00 13.59 ? 625  PRO A CA  1 
ATOM   5009 C  C   . PRO A 1 625  ? 58.731 59.123  -25.799 1.00 14.80 ? 625  PRO A C   1 
ATOM   5010 O  O   . PRO A 1 625  ? 58.294 59.936  -24.977 1.00 13.41 ? 625  PRO A O   1 
ATOM   5011 C  CB  . PRO A 1 625  ? 61.037 59.368  -26.668 1.00 16.29 ? 625  PRO A CB  1 
ATOM   5012 C  CG  . PRO A 1 625  ? 61.761 60.552  -27.308 1.00 15.93 ? 625  PRO A CG  1 
ATOM   5013 C  CD  . PRO A 1 625  ? 60.753 61.693  -27.157 1.00 14.77 ? 625  PRO A CD  1 
ATOM   5014 N  N   . PRO A 1 626  ? 58.536 57.818  -25.681 1.00 13.94 ? 626  PRO A N   1 
ATOM   5015 C  CA  . PRO A 1 626  ? 57.773 57.284  -24.528 1.00 14.44 ? 626  PRO A CA  1 
ATOM   5016 C  C   . PRO A 1 626  ? 58.575 57.710  -23.271 1.00 14.49 ? 626  PRO A C   1 
ATOM   5017 O  O   . PRO A 1 626  ? 59.816 57.532  -23.189 1.00 14.92 ? 626  PRO A O   1 
ATOM   5018 C  CB  . PRO A 1 626  ? 57.892 55.764  -24.689 1.00 13.47 ? 626  PRO A CB  1 
ATOM   5019 C  CG  . PRO A 1 626  ? 58.194 55.574  -26.231 1.00 14.01 ? 626  PRO A CG  1 
ATOM   5020 C  CD  . PRO A 1 626  ? 59.083 56.738  -26.546 1.00 14.70 ? 626  PRO A CD  1 
ATOM   5021 N  N   . MET A 1 627  ? 57.871 58.266  -22.271 1.00 12.04 ? 627  MET A N   1 
ATOM   5022 C  CA  . MET A 1 627  ? 58.499 58.681  -20.993 1.00 12.33 ? 627  MET A CA  1 
ATOM   5023 C  C   . MET A 1 627  ? 59.791 59.429  -21.256 1.00 12.47 ? 627  MET A C   1 
ATOM   5024 O  O   . MET A 1 627  ? 60.798 59.282  -20.555 1.00 13.18 ? 627  MET A O   1 
ATOM   5025 C  CB  . MET A 1 627  ? 58.775 57.442  -20.122 1.00 13.38 ? 627  MET A CB  1 
ATOM   5026 C  CG  . MET A 1 627  ? 57.501 56.747  -19.736 1.00 12.68 ? 627  MET A CG  1 
ATOM   5027 S  SD  . MET A 1 627  ? 57.697 55.049  -19.080 1.00 15.86 ? 627  MET A SD  1 
ATOM   5028 C  CE  . MET A 1 627  ? 58.596 55.372  -17.660 1.00 16.05 ? 627  MET A CE  1 
ATOM   5029 N  N   . GLY A 1 628  ? 59.722 60.308  -22.263 1.00 12.99 ? 628  GLY A N   1 
ATOM   5030 C  CA  . GLY A 1 628  ? 60.926 60.982  -22.706 1.00 13.94 ? 628  GLY A CA  1 
ATOM   5031 C  C   . GLY A 1 628  ? 60.819 62.480  -22.925 1.00 13.90 ? 628  GLY A C   1 
ATOM   5032 O  O   . GLY A 1 628  ? 59.826 63.112  -22.539 1.00 12.62 ? 628  GLY A O   1 
ATOM   5033 N  N   . LEU A 1 629  ? 61.851 63.019  -23.583 1.00 13.53 ? 629  LEU A N   1 
ATOM   5034 C  CA  . LEU A 1 629  ? 61.974 64.468  -23.809 1.00 13.00 ? 629  LEU A CA  1 
ATOM   5035 C  C   . LEU A 1 629  ? 62.408 64.758  -25.219 1.00 14.72 ? 629  LEU A C   1 
ATOM   5036 O  O   . LEU A 1 629  ? 63.177 63.980  -25.823 1.00 14.86 ? 629  LEU A O   1 
ATOM   5037 C  CB  . LEU A 1 629  ? 63.049 65.051  -22.902 1.00 12.31 ? 629  LEU A CB  1 
ATOM   5038 C  CG  . LEU A 1 629  ? 62.821 64.888  -21.395 1.00 12.92 ? 629  LEU A CG  1 
ATOM   5039 C  CD1 . LEU A 1 629  ? 64.097 65.181  -20.650 1.00 13.80 ? 629  LEU A CD1 1 
ATOM   5040 C  CD2 . LEU A 1 629  ? 61.717 65.861  -20.955 1.00 14.36 ? 629  LEU A CD2 1 
ATOM   5041 N  N   . ALA A 1 630  ? 61.934 65.881  -25.742 1.00 13.26 ? 630  ALA A N   1 
ATOM   5042 C  CA  . ALA A 1 630  ? 62.307 66.292  -27.110 1.00 14.49 ? 630  ALA A CA  1 
ATOM   5043 C  C   . ALA A 1 630  ? 62.538 67.793  -27.070 1.00 15.47 ? 630  ALA A C   1 
ATOM   5044 O  O   . ALA A 1 630  ? 61.757 68.554  -26.501 1.00 14.87 ? 630  ALA A O   1 
ATOM   5045 C  CB  . ALA A 1 630  ? 61.207 65.941  -28.102 1.00 15.48 ? 630  ALA A CB  1 
ATOM   5046 N  N   . THR A 1 631  ? 63.614 68.215  -27.726 1.00 13.98 ? 631  THR A N   1 
ATOM   5047 C  CA  . THR A 1 631  ? 64.000 69.636  -27.755 1.00 15.78 ? 631  THR A CA  1 
ATOM   5048 C  C   . THR A 1 631  ? 63.739 70.288  -29.097 1.00 14.95 ? 631  THR A C   1 
ATOM   5049 O  O   . THR A 1 631  ? 64.024 69.688  -30.155 1.00 16.94 ? 631  THR A O   1 
ATOM   5050 C  CB  . THR A 1 631  ? 65.509 69.768  -27.467 1.00 16.11 ? 631  THR A CB  1 
ATOM   5051 O  OG1 . THR A 1 631  ? 65.815 69.041  -26.260 1.00 15.87 ? 631  THR A OG1 1 
ATOM   5052 C  CG2 . THR A 1 631  ? 65.940 71.244  -27.301 1.00 17.81 ? 631  THR A CG2 1 
ATOM   5053 N  N   . TYR A 1 632  ? 63.215 71.504  -29.048 1.00 14.79 ? 632  TYR A N   1 
ATOM   5054 C  CA  . TYR A 1 632  ? 62.966 72.300  -30.252 1.00 14.90 ? 632  TYR A CA  1 
ATOM   5055 C  C   . TYR A 1 632  ? 63.540 73.689  -30.075 1.00 15.71 ? 632  TYR A C   1 
ATOM   5056 O  O   . TYR A 1 632  ? 63.879 74.122  -28.979 1.00 15.40 ? 632  TYR A O   1 
ATOM   5057 C  CB  . TYR A 1 632  ? 61.469 72.375  -30.559 1.00 15.21 ? 632  TYR A CB  1 
ATOM   5058 C  CG  . TYR A 1 632  ? 60.873 71.057  -30.960 1.00 15.68 ? 632  TYR A CG  1 
ATOM   5059 C  CD1 . TYR A 1 632  ? 60.542 70.094  -29.995 1.00 16.17 ? 632  TYR A CD1 1 
ATOM   5060 C  CD2 . TYR A 1 632  ? 60.632 70.757  -32.314 1.00 15.60 ? 632  TYR A CD2 1 
ATOM   5061 C  CE1 . TYR A 1 632  ? 59.999 68.880  -30.368 1.00 16.68 ? 632  TYR A CE1 1 
ATOM   5062 C  CE2 . TYR A 1 632  ? 60.096 69.534  -32.701 1.00 17.31 ? 632  TYR A CE2 1 
ATOM   5063 C  CZ  . TYR A 1 632  ? 59.781 68.591  -31.719 1.00 15.90 ? 632  TYR A CZ  1 
ATOM   5064 O  OH  . TYR A 1 632  ? 59.302 67.366  -32.111 1.00 19.13 ? 632  TYR A OH  1 
ATOM   5065 N  N   . VAL A 1 633  ? 63.700 74.393  -31.202 1.00 14.22 ? 633  VAL A N   1 
ATOM   5066 C  CA  . VAL A 1 633  ? 64.248 75.740  -31.181 1.00 14.20 ? 633  VAL A CA  1 
ATOM   5067 C  C   . VAL A 1 633  ? 63.305 76.705  -31.913 1.00 13.33 ? 633  VAL A C   1 
ATOM   5068 O  O   . VAL A 1 633  ? 62.815 76.375  -32.993 1.00 15.36 ? 633  VAL A O   1 
ATOM   5069 C  CB  . VAL A 1 633  ? 65.642 75.779  -31.880 1.00 15.10 ? 633  VAL A CB  1 
ATOM   5070 C  CG1 . VAL A 1 633  ? 66.226 77.174  -31.838 1.00 17.99 ? 633  VAL A CG1 1 
ATOM   5071 C  CG2 . VAL A 1 633  ? 66.578 74.788  -31.195 1.00 18.71 ? 633  VAL A CG2 1 
ATOM   5072 N  N   . LEU A 1 634  ? 63.029 77.847  -31.310 1.00 14.43 ? 634  LEU A N   1 
ATOM   5073 C  CA  . LEU A 1 634  ? 62.181 78.891  -31.917 1.00 15.78 ? 634  LEU A CA  1 
ATOM   5074 C  C   . LEU A 1 634  ? 63.136 80.009  -32.295 1.00 16.63 ? 634  LEU A C   1 
ATOM   5075 O  O   . LEU A 1 634  ? 63.913 80.481  -31.441 1.00 15.18 ? 634  LEU A O   1 
ATOM   5076 C  CB  . LEU A 1 634  ? 61.163 79.447  -30.913 1.00 16.45 ? 634  LEU A CB  1 
ATOM   5077 C  CG  . LEU A 1 634  ? 60.240 78.444  -30.207 1.00 24.01 ? 634  LEU A CG  1 
ATOM   5078 C  CD1 . LEU A 1 634  ? 59.016 79.189  -29.633 1.00 21.88 ? 634  LEU A CD1 1 
ATOM   5079 C  CD2 . LEU A 1 634  ? 59.816 77.338  -31.095 1.00 25.74 ? 634  LEU A CD2 1 
ATOM   5080 N  N   . THR A 1 635  ? 63.083 80.435  -33.573 1.00 16.10 ? 635  THR A N   1 
ATOM   5081 C  CA  . THR A 1 635  ? 64.020 81.445  -34.071 1.00 15.93 ? 635  THR A CA  1 
ATOM   5082 C  C   . THR A 1 635  ? 63.247 82.579  -34.742 1.00 16.41 ? 635  THR A C   1 
ATOM   5083 O  O   . THR A 1 635  ? 62.312 82.354  -35.527 1.00 17.91 ? 635  THR A O   1 
ATOM   5084 C  CB  . THR A 1 635  ? 64.961 80.806  -35.105 1.00 17.82 ? 635  THR A CB  1 
ATOM   5085 O  OG1 . THR A 1 635  ? 65.635 79.672  -34.524 1.00 18.05 ? 635  THR A OG1 1 
ATOM   5086 C  CG2 . THR A 1 635  ? 65.984 81.833  -35.608 1.00 18.00 ? 635  THR A CG2 1 
ATOM   5087 N  N   . ILE A 1 636  ? 63.668 83.801  -34.450 1.00 17.56 ? 636  ILE A N   1 
ATOM   5088 C  CA  . ILE A 1 636  ? 62.972 84.948  -35.050 1.00 18.83 ? 636  ILE A CA  1 
ATOM   5089 C  C   . ILE A 1 636  ? 63.591 85.309  -36.397 1.00 22.45 ? 636  ILE A C   1 
ATOM   5090 O  O   . ILE A 1 636  ? 64.766 85.016  -36.653 1.00 21.91 ? 636  ILE A O   1 
ATOM   5091 C  CB  . ILE A 1 636  ? 63.035 86.166  -34.109 1.00 18.85 ? 636  ILE A CB  1 
ATOM   5092 C  CG1 . ILE A 1 636  ? 62.116 87.283  -34.619 1.00 20.18 ? 636  ILE A CG1 1 
ATOM   5093 C  CG2 . ILE A 1 636  ? 64.470 86.722  -34.006 1.00 20.46 ? 636  ILE A CG2 1 
ATOM   5094 C  CD1 . ILE A 1 636  ? 62.045 88.448  -33.638 1.00 22.14 ? 636  ILE A CD1 1 
ATOM   5095 N  N   . SER A 1 637  ? 62.762 85.853  -37.286 1.00 21.99 ? 637  SER A N   1 
ATOM   5096 C  CA  . SER A 1 637  ? 63.260 86.339  -38.577 1.00 25.30 ? 637  SER A CA  1 
ATOM   5097 C  C   . SER A 1 637  ? 62.630 87.707  -38.821 1.00 27.98 ? 637  SER A C   1 
ATOM   5098 O  O   . SER A 1 637  ? 61.709 88.099  -38.126 1.00 25.90 ? 637  SER A O   1 
ATOM   5099 C  CB  . SER A 1 637  ? 62.948 85.370  -39.727 1.00 30.95 ? 637  SER A CB  1 
ATOM   5100 O  OG  . SER A 1 637  ? 61.575 85.072  -39.791 1.00 35.46 ? 637  SER A OG  1 
ATOM   5101 N  N   . ASP A 1 638  ? 63.139 88.454  -39.800 1.00 31.01 ? 638  ASP A N   1 
ATOM   5102 C  CA  . ASP A 1 638  ? 62.584 89.783  -40.018 1.00 34.56 ? 638  ASP A CA  1 
ATOM   5103 C  C   . ASP A 1 638  ? 61.262 89.764  -40.798 1.00 34.44 ? 638  ASP A C   1 
ATOM   5104 O  O   . ASP A 1 638  ? 60.522 90.755  -40.794 1.00 35.99 ? 638  ASP A O   1 
ATOM   5105 C  CB  . ASP A 1 638  ? 63.629 90.692  -40.695 1.00 39.13 ? 638  ASP A CB  1 
ATOM   5106 C  CG  . ASP A 1 638  ? 63.757 90.438  -42.174 1.00 43.62 ? 638  ASP A CG  1 
ATOM   5107 O  OD1 . ASP A 1 638  ? 63.862 89.253  -42.574 1.00 45.28 ? 638  ASP A OD1 1 
ATOM   5108 O  OD2 . ASP A 1 638  ? 63.756 91.437  -42.945 1.00 48.46 ? 638  ASP A OD2 1 
ATOM   5109 N  N   . SER A 1 639  ? 60.949 88.622  -41.413 1.00 31.93 ? 639  SER A N   1 
ATOM   5110 C  CA  . SER A 1 639  ? 59.729 88.478  -42.194 1.00 31.69 ? 639  SER A CA  1 
ATOM   5111 C  C   . SER A 1 639  ? 59.135 87.074  -42.085 1.00 30.53 ? 639  SER A C   1 
ATOM   5112 O  O   . SER A 1 639  ? 59.732 86.184  -41.472 1.00 27.16 ? 639  SER A O   1 
ATOM   5113 C  CB  . SER A 1 639  ? 60.014 88.791  -43.669 1.00 31.29 ? 639  SER A CB  1 
ATOM   5114 O  OG  . SER A 1 639  ? 61.017 87.918  -44.158 1.00 34.33 ? 639  SER A OG  1 
ATOM   5115 N  N   . LYS A 1 640  ? 57.958 86.890  -42.674 1.00 28.83 ? 640  LYS A N   1 
ATOM   5116 C  CA  . LYS A 1 640  ? 57.282 85.597  -42.649 1.00 29.38 ? 640  LYS A CA  1 
ATOM   5117 C  C   . LYS A 1 640  ? 58.203 84.432  -43.041 1.00 28.18 ? 640  LYS A C   1 
ATOM   5118 O  O   . LYS A 1 640  ? 58.747 84.385  -44.160 1.00 29.02 ? 640  LYS A O   1 
ATOM   5119 C  CB  . LYS A 1 640  ? 56.072 85.585  -43.595 1.00 30.28 ? 640  LYS A CB  1 
ATOM   5120 C  CG  . LYS A 1 640  ? 54.936 86.549  -43.274 1.00 35.99 ? 640  LYS A CG  1 
ATOM   5121 C  CD  . LYS A 1 640  ? 53.627 86.106  -43.970 1.00 38.91 ? 640  LYS A CD  1 
ATOM   5122 C  CE  . LYS A 1 640  ? 53.741 86.033  -45.492 1.00 41.17 ? 640  LYS A CE  1 
ATOM   5123 N  NZ  . LYS A 1 640  ? 53.641 87.369  -46.148 1.00 43.20 ? 640  LYS A NZ  1 
ATOM   5124 N  N   . PRO A 1 641  ? 58.390 83.461  -42.123 1.00 26.11 ? 641  PRO A N   1 
ATOM   5125 C  CA  . PRO A 1 641  ? 59.216 82.264  -42.300 1.00 25.63 ? 641  PRO A CA  1 
ATOM   5126 C  C   . PRO A 1 641  ? 58.532 81.321  -43.274 1.00 25.52 ? 641  PRO A C   1 
ATOM   5127 O  O   . PRO A 1 641  ? 57.300 81.233  -43.318 1.00 23.84 ? 641  PRO A O   1 
ATOM   5128 C  CB  . PRO A 1 641  ? 59.224 81.622  -40.908 1.00 27.47 ? 641  PRO A CB  1 
ATOM   5129 C  CG  . PRO A 1 641  ? 58.948 82.773  -40.004 1.00 26.22 ? 641  PRO A CG  1 
ATOM   5130 C  CD  . PRO A 1 641  ? 57.919 83.571  -40.731 1.00 25.89 ? 641  PRO A CD  1 
ATOM   5131 N  N   . GLU A 1 642  ? 59.330 80.569  -44.010 1.00 24.95 ? 642  GLU A N   1 
ATOM   5132 C  CA  . GLU A 1 642  ? 58.795 79.631  -44.971 1.00 25.47 ? 642  GLU A CA  1 
ATOM   5133 C  C   . GLU A 1 642  ? 57.885 78.545  -44.401 1.00 26.54 ? 642  GLU A C   1 
ATOM   5134 O  O   . GLU A 1 642  ? 56.914 78.147  -45.032 1.00 27.54 ? 642  GLU A O   1 
ATOM   5135 C  CB  . GLU A 1 642  ? 59.959 78.960  -45.714 1.00 28.94 ? 642  GLU A CB  1 
ATOM   5136 C  CG  . GLU A 1 642  ? 59.549 77.862  -46.643 1.00 34.70 ? 642  GLU A CG  1 
ATOM   5137 C  CD  . GLU A 1 642  ? 60.743 77.288  -47.395 1.00 40.07 ? 642  GLU A CD  1 
ATOM   5138 O  OE1 . GLU A 1 642  ? 61.845 77.900  -47.319 1.00 43.05 ? 642  GLU A OE1 1 
ATOM   5139 O  OE2 . GLU A 1 642  ? 60.575 76.229  -48.052 1.00 42.97 ? 642  GLU A OE2 1 
ATOM   5140 N  N   . HIS A 1 643  ? 58.191 78.088  -43.188 1.00 24.46 ? 643  HIS A N   1 
ATOM   5141 C  CA  . HIS A 1 643  ? 57.435 76.984  -42.596 1.00 22.49 ? 643  HIS A CA  1 
ATOM   5142 C  C   . HIS A 1 643  ? 56.446 77.361  -41.509 1.00 22.27 ? 643  HIS A C   1 
ATOM   5143 O  O   . HIS A 1 643  ? 56.043 76.497  -40.730 1.00 20.33 ? 643  HIS A O   1 
ATOM   5144 C  CB  . HIS A 1 643  ? 58.411 75.941  -42.059 1.00 23.02 ? 643  HIS A CB  1 
ATOM   5145 C  CG  . HIS A 1 643  ? 59.279 75.362  -43.129 1.00 22.26 ? 643  HIS A CG  1 
ATOM   5146 N  ND1 . HIS A 1 643  ? 58.840 74.366  -43.965 1.00 29.06 ? 643  HIS A ND1 1 
ATOM   5147 C  CD2 . HIS A 1 643  ? 60.532 75.673  -43.531 1.00 23.93 ? 643  HIS A CD2 1 
ATOM   5148 C  CE1 . HIS A 1 643  ? 59.790 74.081  -44.841 1.00 27.23 ? 643  HIS A CE1 1 
ATOM   5149 N  NE2 . HIS A 1 643  ? 60.827 74.860  -44.595 1.00 25.78 ? 643  HIS A NE2 1 
ATOM   5150 N  N   . THR A 1 644  ? 56.099 78.638  -41.455 1.00 18.91 ? 644  THR A N   1 
ATOM   5151 C  CA  . THR A 1 644  ? 55.135 79.158  -40.510 1.00 19.15 ? 644  THR A CA  1 
ATOM   5152 C  C   . THR A 1 644  ? 53.992 79.814  -41.276 1.00 20.61 ? 644  THR A C   1 
ATOM   5153 O  O   . THR A 1 644  ? 54.230 80.639  -42.177 1.00 21.02 ? 644  THR A O   1 
ATOM   5154 C  CB  . THR A 1 644  ? 55.772 80.184  -39.571 1.00 19.04 ? 644  THR A CB  1 
ATOM   5155 O  OG1 . THR A 1 644  ? 56.834 79.527  -38.829 1.00 20.35 ? 644  THR A OG1 1 
ATOM   5156 C  CG2 . THR A 1 644  ? 54.727 80.764  -38.556 1.00 19.88 ? 644  THR A CG2 1 
ATOM   5157 N  N   . SER A 1 645  ? 52.771 79.396  -40.953 1.00 18.28 ? 645  SER A N   1 
ATOM   5158 C  CA  . SER A 1 645  ? 51.554 79.937  -41.545 1.00 18.27 ? 645  SER A CA  1 
ATOM   5159 C  C   . SER A 1 645  ? 50.856 80.796  -40.491 1.00 18.21 ? 645  SER A C   1 
ATOM   5160 O  O   . SER A 1 645  ? 51.197 80.732  -39.313 1.00 19.19 ? 645  SER A O   1 
ATOM   5161 C  CB  . SER A 1 645  ? 50.614 78.830  -42.006 1.00 20.61 ? 645  SER A CB  1 
ATOM   5162 O  OG  . SER A 1 645  ? 50.078 78.114  -40.877 1.00 21.10 ? 645  SER A OG  1 
ATOM   5163 N  N   . TYR A 1 646  ? 49.883 81.588  -40.910 1.00 16.68 ? 646  TYR A N   1 
ATOM   5164 C  CA  . TYR A 1 646  ? 49.165 82.494  -40.025 1.00 16.95 ? 646  TYR A CA  1 
ATOM   5165 C  C   . TYR A 1 646  ? 47.670 82.299  -40.112 1.00 18.52 ? 646  TYR A C   1 
ATOM   5166 O  O   . TYR A 1 646  ? 47.107 82.237  -41.195 1.00 20.91 ? 646  TYR A O   1 
ATOM   5167 C  CB  . TYR A 1 646  ? 49.505 83.933  -40.426 1.00 19.13 ? 646  TYR A CB  1 
ATOM   5168 C  CG  . TYR A 1 646  ? 50.975 84.209  -40.221 1.00 19.32 ? 646  TYR A CG  1 
ATOM   5169 C  CD1 . TYR A 1 646  ? 51.913 83.909  -41.207 1.00 19.69 ? 646  TYR A CD1 1 
ATOM   5170 C  CD2 . TYR A 1 646  ? 51.433 84.648  -38.987 1.00 19.78 ? 646  TYR A CD2 1 
ATOM   5171 C  CE1 . TYR A 1 646  ? 53.275 84.032  -40.963 1.00 21.84 ? 646  TYR A CE1 1 
ATOM   5172 C  CE2 . TYR A 1 646  ? 52.772 84.777  -38.734 1.00 19.78 ? 646  TYR A CE2 1 
ATOM   5173 C  CZ  . TYR A 1 646  ? 53.698 84.463  -39.723 1.00 20.24 ? 646  TYR A CZ  1 
ATOM   5174 O  OH  . TYR A 1 646  ? 55.042 84.535  -39.422 1.00 22.94 ? 646  TYR A OH  1 
ATOM   5175 N  N   . ALA A 1 647  ? 47.012 82.171  -38.955 1.00 16.81 ? 647  ALA A N   1 
ATOM   5176 C  CA  . ALA A 1 647  ? 45.590 81.979  -38.935 1.00 16.05 ? 647  ALA A CA  1 
ATOM   5177 C  C   . ALA A 1 647  ? 44.817 83.203  -39.375 1.00 16.16 ? 647  ALA A C   1 
ATOM   5178 O  O   . ALA A 1 647  ? 45.253 84.340  -39.215 1.00 17.65 ? 647  ALA A O   1 
ATOM   5179 C  CB  . ALA A 1 647  ? 45.127 81.586  -37.528 1.00 17.53 ? 647  ALA A CB  1 
ATOM   5180 N  N   . SER A 1 648  ? 43.669 82.949  -39.979 1.00 16.19 ? 648  SER A N   1 
ATOM   5181 C  CA  . SER A 1 648  ? 42.800 84.067  -40.295 1.00 15.90 ? 648  SER A CA  1 
ATOM   5182 C  C   . SER A 1 648  ? 41.911 84.248  -39.043 1.00 16.59 ? 648  SER A C   1 
ATOM   5183 O  O   . SER A 1 648  ? 41.728 83.311  -38.248 1.00 16.65 ? 648  SER A O   1 
ATOM   5184 C  CB  . SER A 1 648  ? 41.933 83.726  -41.513 1.00 19.68 ? 648  SER A CB  1 
ATOM   5185 O  OG  . SER A 1 648  ? 41.093 82.625  -41.255 1.00 24.87 ? 648  SER A OG  1 
ATOM   5186 N  N   . ASN A 1 649  ? 41.304 85.417  -38.888 1.00 15.44 ? 649  ASN A N   1 
ATOM   5187 C  CA  . ASN A 1 649  ? 40.437 85.696  -37.740 1.00 15.92 ? 649  ASN A CA  1 
ATOM   5188 C  C   . ASN A 1 649  ? 39.219 86.445  -38.203 1.00 16.86 ? 649  ASN A C   1 
ATOM   5189 O  O   . ASN A 1 649  ? 39.344 87.427  -38.960 1.00 17.56 ? 649  ASN A O   1 
ATOM   5190 C  CB  . ASN A 1 649  ? 41.157 86.510  -36.677 1.00 17.50 ? 649  ASN A CB  1 
ATOM   5191 C  CG  . ASN A 1 649  ? 42.354 85.757  -36.090 1.00 17.52 ? 649  ASN A CG  1 
ATOM   5192 O  OD1 . ASN A 1 649  ? 42.213 84.972  -35.136 1.00 16.97 ? 649  ASN A OD1 1 
ATOM   5193 N  ND2 . ASN A 1 649  ? 43.520 85.929  -36.710 1.00 17.63 ? 649  ASN A ND2 1 
ATOM   5194 N  N   . LEU A 1 650  ? 38.058 86.003  -37.749 1.00 16.10 ? 650  LEU A N   1 
ATOM   5195 C  CA  . LEU A 1 650  ? 36.772 86.586  -38.153 1.00 16.93 ? 650  LEU A CA  1 
ATOM   5196 C  C   . LEU A 1 650  ? 35.942 86.861  -36.908 1.00 17.43 ? 650  LEU A C   1 
ATOM   5197 O  O   . LEU A 1 650  ? 35.621 85.947  -36.143 1.00 17.94 ? 650  LEU A O   1 
ATOM   5198 C  CB  . LEU A 1 650  ? 36.038 85.609  -39.070 1.00 17.60 ? 650  LEU A CB  1 
ATOM   5199 C  CG  . LEU A 1 650  ? 34.577 85.910  -39.400 1.00 17.39 ? 650  LEU A CG  1 
ATOM   5200 C  CD1 . LEU A 1 650  ? 34.496 87.190  -40.274 1.00 18.22 ? 650  LEU A CD1 1 
ATOM   5201 C  CD2 . LEU A 1 650  ? 34.010 84.751  -40.209 1.00 20.64 ? 650  LEU A CD2 1 
ATOM   5202 N  N   . LEU A 1 651  ? 35.626 88.122  -36.669 1.00 17.08 ? 651  LEU A N   1 
ATOM   5203 C  CA  . LEU A 1 651  ? 34.816 88.560  -35.529 1.00 17.65 ? 651  LEU A CA  1 
ATOM   5204 C  C   . LEU A 1 651  ? 33.388 88.766  -36.003 1.00 19.72 ? 651  LEU A C   1 
ATOM   5205 O  O   . LEU A 1 651  ? 33.135 89.577  -36.896 1.00 20.63 ? 651  LEU A O   1 
ATOM   5206 C  CB  . LEU A 1 651  ? 35.377 89.864  -34.961 1.00 21.61 ? 651  LEU A CB  1 
ATOM   5207 C  CG  . LEU A 1 651  ? 35.141 90.296  -33.500 1.00 27.38 ? 651  LEU A CG  1 
ATOM   5208 C  CD1 . LEU A 1 651  ? 34.047 91.346  -33.429 1.00 30.88 ? 651  LEU A CD1 1 
ATOM   5209 C  CD2 . LEU A 1 651  ? 34.905 89.096  -32.604 1.00 26.58 ? 651  LEU A CD2 1 
ATOM   5210 N  N   . LEU A 1 652  ? 32.451 88.011  -35.441 1.00 20.29 ? 652  LEU A N   1 
ATOM   5211 C  CA  . LEU A 1 652  ? 31.073 88.100  -35.828 1.00 20.44 ? 652  LEU A CA  1 
ATOM   5212 C  C   . LEU A 1 652  ? 30.267 88.816  -34.769 1.00 22.91 ? 652  LEU A C   1 
ATOM   5213 O  O   . LEU A 1 652  ? 30.108 88.337  -33.632 1.00 22.06 ? 652  LEU A O   1 
ATOM   5214 C  CB  . LEU A 1 652  ? 30.500 86.696  -36.092 1.00 19.27 ? 652  LEU A CB  1 
ATOM   5215 C  CG  . LEU A 1 652  ? 31.244 85.922  -37.177 1.00 19.43 ? 652  LEU A CG  1 
ATOM   5216 C  CD1 . LEU A 1 652  ? 30.718 84.472  -37.303 1.00 19.80 ? 652  LEU A CD1 1 
ATOM   5217 C  CD2 . LEU A 1 652  ? 31.127 86.677  -38.523 1.00 20.75 ? 652  LEU A CD2 1 
ATOM   5218 N  N   . ARG A 1 653  ? 29.752 89.983  -35.134 1.00 22.06 ? 653  ARG A N   1 
ATOM   5219 C  CA  . ARG A 1 653  ? 28.939 90.784  -34.249 1.00 27.06 ? 653  ARG A CA  1 
ATOM   5220 C  C   . ARG A 1 653  ? 28.455 91.973  -35.062 1.00 27.07 ? 653  ARG A C   1 
ATOM   5221 O  O   . ARG A 1 653  ? 29.119 92.401  -36.001 1.00 26.44 ? 653  ARG A O   1 
ATOM   5222 C  CB  . ARG A 1 653  ? 29.749 91.292  -33.060 1.00 28.65 ? 653  ARG A CB  1 
ATOM   5223 C  CG  . ARG A 1 653  ? 30.903 92.172  -33.436 1.00 32.34 ? 653  ARG A CG  1 
ATOM   5224 C  CD  . ARG A 1 653  ? 30.799 93.488  -32.699 1.00 38.63 ? 653  ARG A CD  1 
ATOM   5225 N  NE  . ARG A 1 653  ? 31.097 93.395  -31.277 1.00 39.51 ? 653  ARG A NE  1 
ATOM   5226 C  CZ  . ARG A 1 653  ? 30.780 94.325  -30.380 1.00 40.82 ? 653  ARG A CZ  1 
ATOM   5227 N  NH1 . ARG A 1 653  ? 30.141 95.427  -30.750 1.00 44.47 ? 653  ARG A NH1 1 
ATOM   5228 N  NH2 . ARG A 1 653  ? 31.111 94.173  -29.112 1.00 43.84 ? 653  ARG A NH2 1 
ATOM   5229 N  N   . LYS A 1 654  ? 27.289 92.486  -34.717 1.00 29.36 ? 654  LYS A N   1 
ATOM   5230 C  CA  . LYS A 1 654  ? 26.816 93.664  -35.415 1.00 32.46 ? 654  LYS A CA  1 
ATOM   5231 C  C   . LYS A 1 654  ? 27.534 94.832  -34.730 1.00 33.24 ? 654  LYS A C   1 
ATOM   5232 O  O   . LYS A 1 654  ? 27.924 94.736  -33.571 1.00 34.33 ? 654  LYS A O   1 
ATOM   5233 C  CB  . LYS A 1 654  ? 25.298 93.763  -35.293 1.00 34.00 ? 654  LYS A CB  1 
ATOM   5234 C  CG  . LYS A 1 654  ? 24.594 92.643  -36.062 1.00 38.94 ? 654  LYS A CG  1 
ATOM   5235 C  CD  . LYS A 1 654  ? 23.188 93.025  -36.491 1.00 43.83 ? 654  LYS A CD  1 
ATOM   5236 C  CE  . LYS A 1 654  ? 23.215 94.183  -37.482 1.00 47.00 ? 654  LYS A CE  1 
ATOM   5237 N  NZ  . LYS A 1 654  ? 21.841 94.555  -37.936 1.00 49.82 ? 654  LYS A NZ  1 
ATOM   5238 N  N   . ASN A 1 655  ? 27.751 95.927  -35.435 1.00 35.76 ? 655  ASN A N   1 
ATOM   5239 C  CA  . ASN A 1 655  ? 28.411 97.056  -34.784 1.00 35.09 ? 655  ASN A CA  1 
ATOM   5240 C  C   . ASN A 1 655  ? 29.830 96.734  -34.314 1.00 32.90 ? 655  ASN A C   1 
ATOM   5241 O  O   . ASN A 1 655  ? 30.178 96.960  -33.156 1.00 33.11 ? 655  ASN A O   1 
ATOM   5242 C  CB  . ASN A 1 655  ? 27.582 97.500  -33.577 1.00 39.84 ? 655  ASN A CB  1 
ATOM   5243 C  CG  . ASN A 1 655  ? 27.900 98.915  -33.140 1.00 46.16 ? 655  ASN A CG  1 
ATOM   5244 O  OD1 . ASN A 1 655  ? 28.430 99.142  -32.037 1.00 47.41 ? 655  ASN A OD1 1 
ATOM   5245 N  ND2 . ASN A 1 655  ? 27.575 99.891  -34.004 1.00 48.71 ? 655  ASN A ND2 1 
ATOM   5246 N  N   . PRO A 1 656  ? 30.674 96.204  -35.210 1.00 28.29 ? 656  PRO A N   1 
ATOM   5247 C  CA  . PRO A 1 656  ? 32.040 95.887  -34.788 1.00 26.58 ? 656  PRO A CA  1 
ATOM   5248 C  C   . PRO A 1 656  ? 32.914 97.134  -34.782 1.00 25.68 ? 656  PRO A C   1 
ATOM   5249 O  O   . PRO A 1 656  ? 32.562 98.164  -35.370 1.00 25.25 ? 656  PRO A O   1 
ATOM   5250 C  CB  . PRO A 1 656  ? 32.511 94.917  -35.859 1.00 26.09 ? 656  PRO A CB  1 
ATOM   5251 C  CG  . PRO A 1 656  ? 31.806 95.471  -37.117 1.00 25.59 ? 656  PRO A CG  1 
ATOM   5252 C  CD  . PRO A 1 656  ? 30.423 95.787  -36.608 1.00 27.54 ? 656  PRO A CD  1 
ATOM   5253 N  N   . THR A 1 657  ? 34.042 97.019  -34.094 1.00 25.15 ? 657  THR A N   1 
ATOM   5254 C  CA  . THR A 1 657  ? 35.048 98.061  -34.073 1.00 24.61 ? 657  THR A CA  1 
ATOM   5255 C  C   . THR A 1 657  ? 36.328 97.315  -34.428 1.00 23.45 ? 657  THR A C   1 
ATOM   5256 O  O   . THR A 1 657  ? 36.398 96.072  -34.304 1.00 24.20 ? 657  THR A O   1 
ATOM   5257 C  CB  . THR A 1 657  ? 35.162 98.728  -32.707 1.00 26.79 ? 657  THR A CB  1 
ATOM   5258 O  OG1 . THR A 1 657  ? 35.254 97.727  -31.689 1.00 27.41 ? 657  THR A OG1 1 
ATOM   5259 C  CG2 . THR A 1 657  ? 33.930 99.602  -32.457 1.00 26.10 ? 657  THR A CG2 1 
ATOM   5260 N  N   . SER A 1 658  ? 37.336 98.063  -34.866 1.00 22.59 ? 658  SER A N   1 
ATOM   5261 C  CA  . SER A 1 658  ? 38.605 97.510  -35.331 1.00 22.38 ? 658  SER A CA  1 
ATOM   5262 C  C   . SER A 1 658  ? 39.338 96.686  -34.264 1.00 22.62 ? 658  SER A C   1 
ATOM   5263 O  O   . SER A 1 658  ? 39.097 96.854  -33.068 1.00 24.54 ? 658  SER A O   1 
ATOM   5264 C  CB  . SER A 1 658  ? 39.496 98.645  -35.797 1.00 24.23 ? 658  SER A CB  1 
ATOM   5265 O  OG  . SER A 1 658  ? 39.829 99.454  -34.668 1.00 27.52 ? 658  SER A OG  1 
ATOM   5266 N  N   . LEU A 1 659  ? 40.196 95.785  -34.728 1.00 23.12 ? 659  LEU A N   1 
ATOM   5267 C  CA  . LEU A 1 659  ? 40.976 94.897  -33.837 1.00 24.12 ? 659  LEU A CA  1 
ATOM   5268 C  C   . LEU A 1 659  ? 42.382 94.825  -34.388 1.00 24.57 ? 659  LEU A C   1 
ATOM   5269 O  O   . LEU A 1 659  ? 42.727 93.896  -35.121 1.00 25.41 ? 659  LEU A O   1 
ATOM   5270 C  CB  . LEU A 1 659  ? 40.363 93.476  -33.822 1.00 24.60 ? 659  LEU A CB  1 
ATOM   5271 C  CG  . LEU A 1 659  ? 39.018 93.336  -33.102 1.00 26.06 ? 659  LEU A CG  1 
ATOM   5272 C  CD1 . LEU A 1 659  ? 38.467 91.904  -33.258 1.00 26.63 ? 659  LEU A CD1 1 
ATOM   5273 C  CD2 . LEU A 1 659  ? 39.189 93.711  -31.644 1.00 27.67 ? 659  LEU A CD2 1 
ATOM   5274 N  N   . PRO A 1 660  ? 43.207 95.839  -34.084 1.00 24.54 ? 660  PRO A N   1 
ATOM   5275 C  CA  . PRO A 1 660  ? 44.586 95.867  -34.571 1.00 23.86 ? 660  PRO A CA  1 
ATOM   5276 C  C   . PRO A 1 660  ? 45.379 94.769  -33.860 1.00 23.49 ? 660  PRO A C   1 
ATOM   5277 O  O   . PRO A 1 660  ? 45.089 94.451  -32.721 1.00 24.37 ? 660  PRO A O   1 
ATOM   5278 C  CB  . PRO A 1 660  ? 45.052 97.280  -34.209 1.00 23.84 ? 660  PRO A CB  1 
ATOM   5279 C  CG  . PRO A 1 660  ? 44.286 97.599  -32.981 1.00 28.05 ? 660  PRO A CG  1 
ATOM   5280 C  CD  . PRO A 1 660  ? 42.889 97.037  -33.292 1.00 24.45 ? 660  PRO A CD  1 
ATOM   5281 N  N   . LEU A 1 661  ? 46.357 94.213  -34.556 1.00 26.39 ? 661  LEU A N   1 
ATOM   5282 C  CA  . LEU A 1 661  ? 47.154 93.111  -33.982 1.00 27.20 ? 661  LEU A CA  1 
ATOM   5283 C  C   . LEU A 1 661  ? 48.681 93.313  -34.106 1.00 28.10 ? 661  LEU A C   1 
ATOM   5284 O  O   . LEU A 1 661  ? 49.416 92.344  -34.304 1.00 25.39 ? 661  LEU A O   1 
ATOM   5285 C  CB  . LEU A 1 661  ? 46.763 91.813  -34.684 1.00 26.62 ? 661  LEU A CB  1 
ATOM   5286 C  CG  . LEU A 1 661  ? 45.319 91.339  -34.497 1.00 23.15 ? 661  LEU A CG  1 
ATOM   5287 C  CD1 . LEU A 1 661  ? 45.089 90.042  -35.312 1.00 24.12 ? 661  LEU A CD1 1 
ATOM   5288 C  CD2 . LEU A 1 661  ? 45.055 91.103  -33.012 1.00 26.74 ? 661  LEU A CD2 1 
ATOM   5289 N  N   . GLY A 1 662  ? 49.157 94.558  -34.007 1.00 30.32 ? 662  GLY A N   1 
ATOM   5290 C  CA  . GLY A 1 662  ? 50.597 94.822  -34.125 1.00 28.60 ? 662  GLY A CA  1 
ATOM   5291 C  C   . GLY A 1 662  ? 51.188 94.283  -35.419 1.00 29.98 ? 662  GLY A C   1 
ATOM   5292 O  O   . GLY A 1 662  ? 50.681 94.542  -36.514 1.00 30.83 ? 662  GLY A O   1 
ATOM   5293 N  N   . GLN A 1 663  ? 52.244 93.477  -35.316 1.00 28.89 ? 663  GLN A N   1 
ATOM   5294 C  CA  . GLN A 1 663  ? 52.856 92.944  -36.520 1.00 28.54 ? 663  GLN A CA  1 
ATOM   5295 C  C   . GLN A 1 663  ? 52.161 91.734  -37.164 1.00 25.10 ? 663  GLN A C   1 
ATOM   5296 O  O   . GLN A 1 663  ? 52.572 91.291  -38.226 1.00 28.72 ? 663  GLN A O   1 
ATOM   5297 C  CB  . GLN A 1 663  ? 54.309 92.552  -36.247 1.00 32.38 ? 663  GLN A CB  1 
ATOM   5298 C  CG  . GLN A 1 663  ? 55.110 93.512  -35.355 1.00 35.94 ? 663  GLN A CG  1 
ATOM   5299 C  CD  . GLN A 1 663  ? 56.438 92.880  -34.960 1.00 37.54 ? 663  GLN A CD  1 
ATOM   5300 O  OE1 . GLN A 1 663  ? 57.303 92.649  -35.827 1.00 34.75 ? 663  GLN A OE1 1 
ATOM   5301 N  NE2 . GLN A 1 663  ? 56.598 92.565  -33.665 1.00 37.87 ? 663  GLN A NE2 1 
ATOM   5302 N  N   . TYR A 1 664  ? 51.113 91.203  -36.542 1.00 26.54 ? 664  TYR A N   1 
ATOM   5303 C  CA  . TYR A 1 664  ? 50.437 90.032  -37.113 1.00 25.83 ? 664  TYR A CA  1 
ATOM   5304 C  C   . TYR A 1 664  ? 50.148 90.348  -38.573 1.00 23.70 ? 664  TYR A C   1 
ATOM   5305 O  O   . TYR A 1 664  ? 49.468 91.329  -38.854 1.00 25.50 ? 664  TYR A O   1 
ATOM   5306 C  CB  . TYR A 1 664  ? 49.160 89.777  -36.324 1.00 23.39 ? 664  TYR A CB  1 
ATOM   5307 C  CG  . TYR A 1 664  ? 48.574 88.432  -36.591 1.00 20.76 ? 664  TYR A CG  1 
ATOM   5308 C  CD1 . TYR A 1 664  ? 49.114 87.289  -35.985 1.00 18.94 ? 664  TYR A CD1 1 
ATOM   5309 C  CD2 . TYR A 1 664  ? 47.477 88.284  -37.451 1.00 18.85 ? 664  TYR A CD2 1 
ATOM   5310 C  CE1 . TYR A 1 664  ? 48.562 86.042  -36.222 1.00 20.00 ? 664  TYR A CE1 1 
ATOM   5311 C  CE2 . TYR A 1 664  ? 46.923 87.041  -37.711 1.00 18.67 ? 664  TYR A CE2 1 
ATOM   5312 C  CZ  . TYR A 1 664  ? 47.477 85.916  -37.078 1.00 18.42 ? 664  TYR A CZ  1 
ATOM   5313 O  OH  . TYR A 1 664  ? 46.900 84.710  -37.297 1.00 18.76 ? 664  TYR A OH  1 
ATOM   5314 N  N   . PRO A 1 665  ? 50.606 89.500  -39.511 1.00 26.90 ? 665  PRO A N   1 
ATOM   5315 C  CA  . PRO A 1 665  ? 50.407 89.747  -40.947 1.00 27.63 ? 665  PRO A CA  1 
ATOM   5316 C  C   . PRO A 1 665  ? 49.066 89.612  -41.633 1.00 29.32 ? 665  PRO A C   1 
ATOM   5317 O  O   . PRO A 1 665  ? 48.975 89.866  -42.832 1.00 32.69 ? 665  PRO A O   1 
ATOM   5318 C  CB  . PRO A 1 665  ? 51.445 88.832  -41.594 1.00 27.95 ? 665  PRO A CB  1 
ATOM   5319 C  CG  . PRO A 1 665  ? 51.388 87.628  -40.683 1.00 27.53 ? 665  PRO A CG  1 
ATOM   5320 C  CD  . PRO A 1 665  ? 51.370 88.254  -39.303 1.00 25.34 ? 665  PRO A CD  1 
ATOM   5321 N  N   . GLU A 1 666  ? 48.027 89.230  -40.912 1.00 27.49 ? 666  GLU A N   1 
ATOM   5322 C  CA  . GLU A 1 666  ? 46.724 89.058  -41.551 1.00 25.73 ? 666  GLU A CA  1 
ATOM   5323 C  C   . GLU A 1 666  ? 45.707 89.931  -40.821 1.00 24.67 ? 666  GLU A C   1 
ATOM   5324 O  O   . GLU A 1 666  ? 45.571 89.842  -39.604 1.00 24.32 ? 666  GLU A O   1 
ATOM   5325 C  CB  . GLU A 1 666  ? 46.328 87.585  -41.468 1.00 30.13 ? 666  GLU A CB  1 
ATOM   5326 C  CG  . GLU A 1 666  ? 44.895 87.346  -41.797 1.00 35.96 ? 666  GLU A CG  1 
ATOM   5327 C  CD  . GLU A 1 666  ? 44.689 86.769  -43.182 1.00 39.10 ? 666  GLU A CD  1 
ATOM   5328 O  OE1 . GLU A 1 666  ? 45.657 86.815  -44.003 1.00 40.57 ? 666  GLU A OE1 1 
ATOM   5329 O  OE2 . GLU A 1 666  ? 43.554 86.280  -43.428 1.00 37.84 ? 666  GLU A OE2 1 
ATOM   5330 N  N   . ASP A 1 667  ? 44.995 90.804  -41.549 1.00 23.02 ? 667  ASP A N   1 
ATOM   5331 C  CA  . ASP A 1 667  ? 44.003 91.668  -40.913 1.00 22.98 ? 667  ASP A CA  1 
ATOM   5332 C  C   . ASP A 1 667  ? 42.753 90.895  -40.454 1.00 18.13 ? 667  ASP A C   1 
ATOM   5333 O  O   . ASP A 1 667  ? 42.275 90.008  -41.161 1.00 18.94 ? 667  ASP A O   1 
ATOM   5334 C  CB  . ASP A 1 667  ? 43.504 92.761  -41.896 1.00 26.13 ? 667  ASP A CB  1 
ATOM   5335 C  CG  . ASP A 1 667  ? 44.593 93.746  -42.292 1.00 31.34 ? 667  ASP A CG  1 
ATOM   5336 O  OD1 . ASP A 1 667  ? 45.539 93.965  -41.499 1.00 33.74 ? 667  ASP A OD1 1 
ATOM   5337 O  OD2 . ASP A 1 667  ? 44.491 94.328  -43.395 1.00 33.71 ? 667  ASP A OD2 1 
ATOM   5338 N  N   . VAL A 1 668  ? 42.238 91.248  -39.291 1.00 20.10 ? 668  VAL A N   1 
ATOM   5339 C  CA  . VAL A 1 668  ? 41.002 90.643  -38.795 1.00 19.05 ? 668  VAL A CA  1 
ATOM   5340 C  C   . VAL A 1 668  ? 39.839 91.033  -39.733 1.00 19.75 ? 668  VAL A C   1 
ATOM   5341 O  O   . VAL A 1 668  ? 39.768 92.186  -40.200 1.00 22.51 ? 668  VAL A O   1 
ATOM   5342 C  CB  . VAL A 1 668  ? 40.653 91.148  -37.361 1.00 18.75 ? 668  VAL A CB  1 
ATOM   5343 C  CG1 . VAL A 1 668  ? 39.303 90.557  -36.890 1.00 19.34 ? 668  VAL A CG1 1 
ATOM   5344 C  CG2 . VAL A 1 668  ? 41.761 90.701  -36.390 1.00 20.47 ? 668  VAL A CG2 1 
ATOM   5345 N  N   . LYS A 1 669  ? 38.953 90.076  -39.993 1.00 17.90 ? 669  LYS A N   1 
ATOM   5346 C  CA  . LYS A 1 669  ? 37.749 90.242  -40.827 1.00 18.18 ? 669  LYS A CA  1 
ATOM   5347 C  C   . LYS A 1 669  ? 36.528 90.344  -39.916 1.00 20.05 ? 669  LYS A C   1 
ATOM   5348 O  O   . LYS A 1 669  ? 36.508 89.761  -38.806 1.00 19.35 ? 669  LYS A O   1 
ATOM   5349 C  CB  . LYS A 1 669  ? 37.590 89.061  -41.771 1.00 22.36 ? 669  LYS A CB  1 
ATOM   5350 C  CG  . LYS A 1 669  ? 38.263 89.223  -43.125 1.00 32.86 ? 669  LYS A CG  1 
ATOM   5351 C  CD  . LYS A 1 669  ? 39.764 89.059  -43.066 1.00 36.33 ? 669  LYS A CD  1 
ATOM   5352 C  CE  . LYS A 1 669  ? 40.443 89.749  -44.267 1.00 36.63 ? 669  LYS A CE  1 
ATOM   5353 N  NZ  . LYS A 1 669  ? 41.928 89.736  -44.096 1.00 34.94 ? 669  LYS A NZ  1 
ATOM   5354 N  N   . PHE A 1 670  ? 35.490 91.042  -40.380 1.00 18.41 ? 670  PHE A N   1 
ATOM   5355 C  CA  . PHE A 1 670  ? 34.292 91.252  -39.579 1.00 18.32 ? 670  PHE A CA  1 
ATOM   5356 C  C   . PHE A 1 670  ? 33.053 90.825  -40.334 1.00 20.24 ? 670  PHE A C   1 
ATOM   5357 O  O   . PHE A 1 670  ? 33.072 90.754  -41.543 1.00 20.19 ? 670  PHE A O   1 
ATOM   5358 C  CB  . PHE A 1 670  ? 34.143 92.715  -39.157 1.00 19.00 ? 670  PHE A CB  1 
ATOM   5359 C  CG  . PHE A 1 670  ? 35.290 93.212  -38.346 1.00 18.73 ? 670  PHE A CG  1 
ATOM   5360 C  CD1 . PHE A 1 670  ? 36.444 93.669  -38.987 1.00 20.85 ? 670  PHE A CD1 1 
ATOM   5361 C  CD2 . PHE A 1 670  ? 35.264 93.143  -36.957 1.00 20.80 ? 670  PHE A CD2 1 
ATOM   5362 C  CE1 . PHE A 1 670  ? 37.568 94.049  -38.234 1.00 22.47 ? 670  PHE A CE1 1 
ATOM   5363 C  CE2 . PHE A 1 670  ? 36.371 93.517  -36.206 1.00 24.46 ? 670  PHE A CE2 1 
ATOM   5364 C  CZ  . PHE A 1 670  ? 37.532 93.975  -36.863 1.00 22.19 ? 670  PHE A CZ  1 
ATOM   5365 N  N   . GLY A 1 671  ? 31.971 90.533  -39.608 1.00 20.83 ? 671  GLY A N   1 
ATOM   5366 C  CA  . GLY A 1 671  ? 30.739 90.112  -40.269 1.00 19.57 ? 671  GLY A CA  1 
ATOM   5367 C  C   . GLY A 1 671  ? 29.604 90.058  -39.265 1.00 20.50 ? 671  GLY A C   1 
ATOM   5368 O  O   . GLY A 1 671  ? 29.823 90.049  -38.051 1.00 19.57 ? 671  GLY A O   1 
ATOM   5369 N  N   . ASP A 1 672  ? 28.375 90.047  -39.755 1.00 19.89 ? 672  ASP A N   1 
ATOM   5370 C  CA  . ASP A 1 672  ? 27.237 89.927  -38.870 1.00 21.66 ? 672  ASP A CA  1 
ATOM   5371 C  C   . ASP A 1 672  ? 27.190 88.460  -38.418 1.00 21.31 ? 672  ASP A C   1 
ATOM   5372 O  O   . ASP A 1 672  ? 27.691 87.585  -39.125 1.00 19.99 ? 672  ASP A O   1 
ATOM   5373 C  CB  . ASP A 1 672  ? 25.935 90.214  -39.638 1.00 24.02 ? 672  ASP A CB  1 
ATOM   5374 C  CG  . ASP A 1 672  ? 25.644 91.698  -39.796 1.00 28.41 ? 672  ASP A CG  1 
ATOM   5375 O  OD1 . ASP A 1 672  ? 26.454 92.541  -39.379 1.00 29.58 ? 672  ASP A OD1 1 
ATOM   5376 O  OD2 . ASP A 1 672  ? 24.565 92.005  -40.347 1.00 33.83 ? 672  ASP A OD2 1 
ATOM   5377 N  N   . PRO A 1 673  ? 26.602 88.189  -37.239 1.00 22.19 ? 673  PRO A N   1 
ATOM   5378 C  CA  . PRO A 1 673  ? 26.505 86.802  -36.754 1.00 23.63 ? 673  PRO A CA  1 
ATOM   5379 C  C   . PRO A 1 673  ? 25.910 85.915  -37.851 1.00 22.74 ? 673  PRO A C   1 
ATOM   5380 O  O   . PRO A 1 673  ? 24.991 86.328  -38.588 1.00 24.71 ? 673  PRO A O   1 
ATOM   5381 C  CB  . PRO A 1 673  ? 25.576 86.935  -35.555 1.00 24.54 ? 673  PRO A CB  1 
ATOM   5382 C  CG  . PRO A 1 673  ? 25.940 88.261  -34.987 1.00 26.73 ? 673  PRO A CG  1 
ATOM   5383 C  CD  . PRO A 1 673  ? 26.112 89.140  -36.218 1.00 23.78 ? 673  PRO A CD  1 
ATOM   5384 N  N   . ARG A 1 674  ? 26.417 84.694  -37.967 1.00 21.13 ? 674  ARG A N   1 
ATOM   5385 C  CA  . ARG A 1 674  ? 25.939 83.765  -38.981 1.00 22.23 ? 674  ARG A CA  1 
ATOM   5386 C  C   . ARG A 1 674  ? 26.406 82.359  -38.650 1.00 23.52 ? 674  ARG A C   1 
ATOM   5387 O  O   . ARG A 1 674  ? 27.331 82.180  -37.856 1.00 22.74 ? 674  ARG A O   1 
ATOM   5388 C  CB  . ARG A 1 674  ? 26.482 84.161  -40.365 1.00 22.52 ? 674  ARG A CB  1 
ATOM   5389 C  CG  . ARG A 1 674  ? 27.989 84.079  -40.534 1.00 26.04 ? 674  ARG A CG  1 
ATOM   5390 C  CD  . ARG A 1 674  ? 28.313 84.142  -42.034 1.00 28.46 ? 674  ARG A CD  1 
ATOM   5391 N  NE  . ARG A 1 674  ? 29.695 83.834  -42.367 1.00 30.21 ? 674  ARG A NE  1 
ATOM   5392 C  CZ  . ARG A 1 674  ? 30.672 84.730  -42.469 1.00 29.88 ? 674  ARG A CZ  1 
ATOM   5393 N  NH1 . ARG A 1 674  ? 30.438 86.030  -42.258 1.00 33.55 ? 674  ARG A NH1 1 
ATOM   5394 N  NH2 . ARG A 1 674  ? 31.883 84.322  -42.831 1.00 29.52 ? 674  ARG A NH2 1 
ATOM   5395 N  N   . GLU A 1 675  ? 25.757 81.355  -39.223 1.00 21.93 ? 675  GLU A N   1 
ATOM   5396 C  CA  . GLU A 1 675  ? 26.194 79.996  -38.986 1.00 22.82 ? 675  GLU A CA  1 
ATOM   5397 C  C   . GLU A 1 675  ? 27.518 79.776  -39.697 1.00 24.26 ? 675  GLU A C   1 
ATOM   5398 O  O   . GLU A 1 675  ? 27.787 80.350  -40.770 1.00 25.72 ? 675  GLU A O   1 
ATOM   5399 C  CB  . GLU A 1 675  ? 25.125 79.003  -39.472 1.00 25.14 ? 675  GLU A CB  1 
ATOM   5400 C  CG  . GLU A 1 675  ? 23.843 79.204  -38.707 1.00 29.18 ? 675  GLU A CG  1 
ATOM   5401 C  CD  . GLU A 1 675  ? 22.959 77.987  -38.702 1.00 33.93 ? 675  GLU A CD  1 
ATOM   5402 O  OE1 . GLU A 1 675  ? 23.040 77.224  -39.694 1.00 36.26 ? 675  GLU A OE1 1 
ATOM   5403 O  OE2 . GLU A 1 675  ? 22.183 77.809  -37.713 1.00 37.93 ? 675  GLU A OE2 1 
ATOM   5404 N  N   . ILE A 1 676  ? 28.383 78.951  -39.119 1.00 22.53 ? 676  ILE A N   1 
ATOM   5405 C  CA  . ILE A 1 676  ? 29.661 78.713  -39.749 1.00 23.50 ? 676  ILE A CA  1 
ATOM   5406 C  C   . ILE A 1 676  ? 30.046 77.248  -39.632 1.00 22.40 ? 676  ILE A C   1 
ATOM   5407 O  O   . ILE A 1 676  ? 29.573 76.551  -38.744 1.00 21.53 ? 676  ILE A O   1 
ATOM   5408 C  CB  . ILE A 1 676  ? 30.755 79.554  -39.107 1.00 28.24 ? 676  ILE A CB  1 
ATOM   5409 C  CG1 . ILE A 1 676  ? 31.234 78.885  -37.836 1.00 28.74 ? 676  ILE A CG1 1 
ATOM   5410 C  CG2 . ILE A 1 676  ? 30.228 80.900  -38.705 1.00 31.96 ? 676  ILE A CG2 1 
ATOM   5411 C  CD1 . ILE A 1 676  ? 32.472 79.504  -37.247 1.00 32.61 ? 676  ILE A CD1 1 
ATOM   5412 N  N   . SER A 1 677  ? 30.908 76.804  -40.535 1.00 22.10 ? 677  SER A N   1 
ATOM   5413 C  CA  . SER A 1 677  ? 31.390 75.429  -40.591 1.00 22.36 ? 677  SER A CA  1 
ATOM   5414 C  C   . SER A 1 677  ? 32.921 75.418  -40.670 1.00 22.35 ? 677  SER A C   1 
ATOM   5415 O  O   . SER A 1 677  ? 33.515 76.217  -41.398 1.00 22.91 ? 677  SER A O   1 
ATOM   5416 C  CB  A SER A 1 677  ? 30.808 74.737  -41.832 0.50 23.56 ? 677  SER A CB  1 
ATOM   5417 C  CB  B SER A 1 677  ? 30.769 74.555  -41.606 0.50 23.72 ? 677  SER A CB  1 
ATOM   5418 O  OG  A SER A 1 677  ? 31.277 73.414  -41.944 0.50 25.41 ? 677  SER A OG  1 
ATOM   5419 O  OG  B SER A 1 677  ? 29.425 74.241  -41.297 0.50 26.43 ? 677  SER A OG  1 
ATOM   5420 N  N   . LEU A 1 678  ? 33.565 74.512  -39.934 1.00 20.81 ? 678  LEU A N   1 
ATOM   5421 C  CA  . LEU A 1 678  ? 35.009 74.426  -39.939 1.00 21.33 ? 678  LEU A CA  1 
ATOM   5422 C  C   . LEU A 1 678  ? 35.476 72.999  -40.011 1.00 20.49 ? 678  LEU A C   1 
ATOM   5423 O  O   . LEU A 1 678  ? 34.796 72.087  -39.504 1.00 20.35 ? 678  LEU A O   1 
ATOM   5424 C  CB  . LEU A 1 678  ? 35.599 74.983  -38.638 1.00 22.06 ? 678  LEU A CB  1 
ATOM   5425 C  CG  . LEU A 1 678  ? 35.653 76.473  -38.379 1.00 23.47 ? 678  LEU A CG  1 
ATOM   5426 C  CD1 . LEU A 1 678  ? 36.146 76.721  -36.949 1.00 22.67 ? 678  LEU A CD1 1 
ATOM   5427 C  CD2 . LEU A 1 678  ? 36.629 77.097  -39.344 1.00 25.93 ? 678  LEU A CD2 1 
ATOM   5428 N  N   . ARG A 1 679  ? 36.629 72.816  -40.631 1.00 20.50 ? 679  ARG A N   1 
ATOM   5429 C  CA  . ARG A 1 679  ? 37.234 71.499  -40.731 1.00 22.70 ? 679  ARG A CA  1 
ATOM   5430 C  C   . ARG A 1 679  ? 38.751 71.655  -40.708 1.00 23.63 ? 679  ARG A C   1 
ATOM   5431 O  O   . ARG A 1 679  ? 39.332 72.424  -41.484 1.00 23.92 ? 679  ARG A O   1 
ATOM   5432 C  CB  . ARG A 1 679  ? 36.793 70.796  -42.024 1.00 25.05 ? 679  ARG A CB  1 
ATOM   5433 C  CG  . ARG A 1 679  ? 37.259 69.348  -42.060 1.00 25.59 ? 679  ARG A CG  1 
ATOM   5434 C  CD  . ARG A 1 679  ? 37.116 68.752  -43.453 1.00 29.31 ? 679  ARG A CD  1 
ATOM   5435 N  NE  . ARG A 1 679  ? 37.498 67.352  -43.409 1.00 35.59 ? 679  ARG A NE  1 
ATOM   5436 C  CZ  . ARG A 1 679  ? 37.660 66.587  -44.478 1.00 39.26 ? 679  ARG A CZ  1 
ATOM   5437 N  NH1 . ARG A 1 679  ? 37.474 67.095  -45.694 1.00 41.20 ? 679  ARG A NH1 1 
ATOM   5438 N  NH2 . ARG A 1 679  ? 38.001 65.315  -44.322 1.00 41.69 ? 679  ARG A NH2 1 
ATOM   5439 N  N   . VAL A 1 680  ? 39.409 70.974  -39.781 1.00 22.44 ? 680  VAL A N   1 
ATOM   5440 C  CA  . VAL A 1 680  ? 40.842 71.005  -39.723 1.00 20.69 ? 680  VAL A CA  1 
ATOM   5441 C  C   . VAL A 1 680  ? 41.368 69.644  -40.189 1.00 23.95 ? 680  VAL A C   1 
ATOM   5442 O  O   . VAL A 1 680  ? 40.836 68.582  -39.794 1.00 23.81 ? 680  VAL A O   1 
ATOM   5443 C  CB  . VAL A 1 680  ? 41.316 71.299  -38.280 1.00 19.22 ? 680  VAL A CB  1 
ATOM   5444 C  CG1 . VAL A 1 680  ? 42.808 71.129  -38.183 1.00 22.31 ? 680  VAL A CG1 1 
ATOM   5445 C  CG2 . VAL A 1 680  ? 40.896 72.729  -37.876 1.00 19.62 ? 680  VAL A CG2 1 
ATOM   5446 N  N   . GLY A 1 681  ? 42.381 69.683  -41.054 1.00 25.19 ? 681  GLY A N   1 
ATOM   5447 C  CA  . GLY A 1 681  ? 42.948 68.448  -41.576 1.00 29.66 ? 681  GLY A CA  1 
ATOM   5448 C  C   . GLY A 1 681  ? 41.891 67.641  -42.327 1.00 31.73 ? 681  GLY A C   1 
ATOM   5449 O  O   . GLY A 1 681  ? 41.067 68.209  -43.063 1.00 32.95 ? 681  GLY A O   1 
ATOM   5450 N  N   . ASN A 1 682  ? 41.927 66.317  -42.137 1.00 35.97 ? 682  ASN A N   1 
ATOM   5451 C  CA  . ASN A 1 682  ? 40.968 65.393  -42.753 1.00 37.24 ? 682  ASN A CA  1 
ATOM   5452 C  C   . ASN A 1 682  ? 39.993 65.000  -41.654 1.00 36.89 ? 682  ASN A C   1 
ATOM   5453 O  O   . ASN A 1 682  ? 39.199 64.062  -41.800 1.00 38.54 ? 682  ASN A O   1 
ATOM   5454 C  CB  . ASN A 1 682  ? 41.658 64.120  -43.243 1.00 41.14 ? 682  ASN A CB  1 
ATOM   5455 C  CG  . ASN A 1 682  ? 42.906 64.404  -44.035 1.00 43.94 ? 682  ASN A CG  1 
ATOM   5456 O  OD1 . ASN A 1 682  ? 42.865 65.083  -45.064 1.00 46.99 ? 682  ASN A OD1 1 
ATOM   5457 N  ND2 . ASN A 1 682  ? 44.037 63.882  -43.561 1.00 46.37 ? 682  ASN A ND2 1 
ATOM   5458 N  N   . GLY A 1 683  ? 40.053 65.736  -40.552 1.00 34.57 ? 683  GLY A N   1 
ATOM   5459 C  CA  . GLY A 1 683  ? 39.206 65.451  -39.418 1.00 32.48 ? 683  GLY A CA  1 
ATOM   5460 C  C   . GLY A 1 683  ? 37.741 65.750  -39.627 1.00 29.96 ? 683  GLY A C   1 
ATOM   5461 O  O   . GLY A 1 683  ? 37.288 65.954  -40.753 1.00 29.39 ? 683  GLY A O   1 
ATOM   5462 N  N   . PRO A 1 684  ? 36.967 65.808  -38.535 1.00 26.50 ? 684  PRO A N   1 
ATOM   5463 C  CA  . PRO A 1 684  ? 35.531 66.086  -38.655 1.00 24.29 ? 684  PRO A CA  1 
ATOM   5464 C  C   . PRO A 1 684  ? 35.195 67.522  -39.053 1.00 22.90 ? 684  PRO A C   1 
ATOM   5465 O  O   . PRO A 1 684  ? 35.998 68.409  -38.878 1.00 22.11 ? 684  PRO A O   1 
ATOM   5466 C  CB  . PRO A 1 684  ? 34.982 65.731  -37.272 1.00 24.57 ? 684  PRO A CB  1 
ATOM   5467 C  CG  . PRO A 1 684  ? 36.189 66.063  -36.331 1.00 24.80 ? 684  PRO A CG  1 
ATOM   5468 C  CD  . PRO A 1 684  ? 37.384 65.609  -37.134 1.00 27.37 ? 684  PRO A CD  1 
ATOM   5469 N  N   . THR A 1 685  ? 34.014 67.714  -39.617 1.00 21.56 ? 685  THR A N   1 
ATOM   5470 C  CA  . THR A 1 685  ? 33.556 69.043  -39.988 1.00 21.25 ? 685  THR A CA  1 
ATOM   5471 C  C   . THR A 1 685  ? 32.507 69.403  -38.946 1.00 22.36 ? 685  THR A C   1 
ATOM   5472 O  O   . THR A 1 685  ? 31.543 68.666  -38.715 1.00 21.98 ? 685  THR A O   1 
ATOM   5473 C  CB  . THR A 1 685  ? 32.934 69.071  -41.394 1.00 22.64 ? 685  THR A CB  1 
ATOM   5474 O  OG1 . THR A 1 685  ? 33.956 68.773  -42.348 1.00 23.26 ? 685  THR A OG1 1 
ATOM   5475 C  CG2 . THR A 1 685  ? 32.334 70.442  -41.678 1.00 21.60 ? 685  THR A CG2 1 
ATOM   5476 N  N   . LEU A 1 686  ? 32.694 70.563  -38.315 1.00 18.89 ? 686  LEU A N   1 
ATOM   5477 C  CA  . LEU A 1 686  ? 31.800 70.996  -37.283 1.00 20.52 ? 686  LEU A CA  1 
ATOM   5478 C  C   . LEU A 1 686  ? 31.026 72.217  -37.724 1.00 18.89 ? 686  LEU A C   1 
ATOM   5479 O  O   . LEU A 1 686  ? 31.616 73.154  -38.259 1.00 21.04 ? 686  LEU A O   1 
ATOM   5480 C  CB  . LEU A 1 686  ? 32.582 71.383  -36.010 1.00 19.53 ? 686  LEU A CB  1 
ATOM   5481 C  CG  . LEU A 1 686  ? 33.557 70.408  -35.336 1.00 26.08 ? 686  LEU A CG  1 
ATOM   5482 C  CD1 . LEU A 1 686  ? 33.738 70.843  -33.883 1.00 22.31 ? 686  LEU A CD1 1 
ATOM   5483 C  CD2 . LEU A 1 686  ? 33.126 69.001  -35.435 1.00 21.91 ? 686  LEU A CD2 1 
ATOM   5484 N  N   . ALA A 1 687  ? 29.744 72.213  -37.442 1.00 17.81 ? 687  ALA A N   1 
ATOM   5485 C  CA  . ALA A 1 687  ? 28.876 73.345  -37.740 1.00 17.85 ? 687  ALA A CA  1 
ATOM   5486 C  C   . ALA A 1 687  ? 28.423 74.020  -36.463 1.00 20.16 ? 687  ALA A C   1 
ATOM   5487 O  O   . ALA A 1 687  ? 28.067 73.354  -35.483 1.00 19.91 ? 687  ALA A O   1 
ATOM   5488 C  CB  . ALA A 1 687  ? 27.640 72.868  -38.543 1.00 20.31 ? 687  ALA A CB  1 
ATOM   5489 N  N   . PHE A 1 688  ? 28.404 75.351  -36.484 1.00 17.32 ? 688  PHE A N   1 
ATOM   5490 C  CA  . PHE A 1 688  ? 28.045 76.166  -35.355 1.00 16.67 ? 688  PHE A CA  1 
ATOM   5491 C  C   . PHE A 1 688  ? 26.871 77.080  -35.636 1.00 16.41 ? 688  PHE A C   1 
ATOM   5492 O  O   . PHE A 1 688  ? 26.691 77.544  -36.780 1.00 20.31 ? 688  PHE A O   1 
ATOM   5493 C  CB  . PHE A 1 688  ? 29.230 77.056  -34.944 1.00 16.51 ? 688  PHE A CB  1 
ATOM   5494 C  CG  . PHE A 1 688  ? 30.459 76.292  -34.614 1.00 15.54 ? 688  PHE A CG  1 
ATOM   5495 C  CD1 . PHE A 1 688  ? 31.288 75.803  -35.590 1.00 15.56 ? 688  PHE A CD1 1 
ATOM   5496 C  CD2 . PHE A 1 688  ? 30.744 76.017  -33.283 1.00 15.62 ? 688  PHE A CD2 1 
ATOM   5497 C  CE1 . PHE A 1 688  ? 32.412 75.029  -35.296 1.00 15.73 ? 688  PHE A CE1 1 
ATOM   5498 C  CE2 . PHE A 1 688  ? 31.852 75.253  -32.953 1.00 14.98 ? 688  PHE A CE2 1 
ATOM   5499 C  CZ  . PHE A 1 688  ? 32.692 74.753  -33.941 1.00 14.69 ? 688  PHE A CZ  1 
ATOM   5500 N  N   . SER A 1 689  ? 26.095 77.356  -34.606 1.00 16.91 ? 689  SER A N   1 
ATOM   5501 C  CA  . SER A 1 689  ? 24.957 78.289  -34.679 1.00 17.07 ? 689  SER A CA  1 
ATOM   5502 C  C   . SER A 1 689  ? 25.507 79.712  -34.755 1.00 19.66 ? 689  SER A C   1 
ATOM   5503 O  O   . SER A 1 689  ? 26.706 79.933  -34.561 1.00 18.67 ? 689  SER A O   1 
ATOM   5504 C  CB  . SER A 1 689  ? 24.081 78.175  -33.438 1.00 20.24 ? 689  SER A CB  1 
ATOM   5505 O  OG  . SER A 1 689  ? 24.722 78.733  -32.317 1.00 21.17 ? 689  SER A OG  1 
ATOM   5506 N  N   . GLU A 1 690  ? 24.630 80.674  -35.031 1.00 21.19 ? 690  GLU A N   1 
ATOM   5507 C  CA  . GLU A 1 690  ? 25.065 82.059  -35.087 1.00 22.48 ? 690  GLU A CA  1 
ATOM   5508 C  C   . GLU A 1 690  ? 25.432 82.565  -33.689 1.00 22.23 ? 690  GLU A C   1 
ATOM   5509 O  O   . GLU A 1 690  ? 25.988 83.663  -33.535 1.00 20.46 ? 690  GLU A O   1 
ATOM   5510 C  CB  . GLU A 1 690  ? 23.970 82.931  -35.727 1.00 25.07 ? 690  GLU A CB  1 
ATOM   5511 C  CG  . GLU A 1 690  ? 22.803 83.252  -34.874 1.00 28.51 ? 690  GLU A CG  1 
ATOM   5512 C  CD  . GLU A 1 690  ? 21.910 84.300  -35.552 1.00 33.96 ? 690  GLU A CD  1 
ATOM   5513 O  OE1 . GLU A 1 690  ? 21.376 83.993  -36.649 1.00 36.18 ? 690  GLU A OE1 1 
ATOM   5514 O  OE2 . GLU A 1 690  ? 21.761 85.420  -35.000 1.00 36.61 ? 690  GLU A OE2 1 
ATOM   5515 N  N   . GLN A 1 691  ? 25.134 81.772  -32.660 1.00 20.80 ? 691  GLN A N   1 
ATOM   5516 C  CA  . GLN A 1 691  ? 25.544 82.158  -31.305 1.00 20.40 ? 691  GLN A CA  1 
ATOM   5517 C  C   . GLN A 1 691  ? 26.882 81.495  -30.923 1.00 19.48 ? 691  GLN A C   1 
ATOM   5518 O  O   . GLN A 1 691  ? 27.289 81.579  -29.779 1.00 21.80 ? 691  GLN A O   1 
ATOM   5519 C  CB  . GLN A 1 691  ? 24.510 81.791  -30.240 1.00 23.03 ? 691  GLN A CB  1 
ATOM   5520 C  CG  . GLN A 1 691  ? 23.278 82.600  -30.315 1.00 27.59 ? 691  GLN A CG  1 
ATOM   5521 C  CD  . GLN A 1 691  ? 22.142 81.693  -30.499 1.00 35.63 ? 691  GLN A CD  1 
ATOM   5522 O  OE1 . GLN A 1 691  ? 21.642 81.081  -29.525 1.00 37.30 ? 691  GLN A OE1 1 
ATOM   5523 N  NE2 . GLN A 1 691  ? 21.728 81.535  -31.747 1.00 36.14 ? 691  GLN A NE2 1 
ATOM   5524 N  N   . GLY A 1 692  ? 27.541 80.850  -31.873 1.00 18.32 ? 692  GLY A N   1 
ATOM   5525 C  CA  . GLY A 1 692  ? 28.856 80.256  -31.638 1.00 19.19 ? 692  GLY A CA  1 
ATOM   5526 C  C   . GLY A 1 692  ? 28.871 78.901  -30.969 1.00 18.78 ? 692  GLY A C   1 
ATOM   5527 O  O   . GLY A 1 692  ? 29.926 78.467  -30.508 1.00 18.94 ? 692  GLY A O   1 
ATOM   5528 N  N   . LEU A 1 693  ? 27.730 78.224  -30.925 1.00 18.47 ? 693  LEU A N   1 
ATOM   5529 C  CA  . LEU A 1 693  ? 27.637 76.901  -30.281 1.00 18.91 ? 693  LEU A CA  1 
ATOM   5530 C  C   . LEU A 1 693  ? 27.493 75.785  -31.281 1.00 18.10 ? 693  LEU A C   1 
ATOM   5531 O  O   . LEU A 1 693  ? 26.766 75.914  -32.287 1.00 18.12 ? 693  LEU A O   1 
ATOM   5532 C  CB  . LEU A 1 693  ? 26.449 76.888  -29.333 1.00 21.15 ? 693  LEU A CB  1 
ATOM   5533 C  CG  . LEU A 1 693  ? 26.564 77.883  -28.182 1.00 23.99 ? 693  LEU A CG  1 
ATOM   5534 C  CD1 . LEU A 1 693  ? 25.170 78.387  -27.838 1.00 28.12 ? 693  LEU A CD1 1 
ATOM   5535 C  CD2 . LEU A 1 693  ? 27.213 77.238  -26.976 1.00 24.36 ? 693  LEU A CD2 1 
ATOM   5536 N  N   . LEU A 1 694  ? 28.161 74.671  -31.025 1.00 15.56 ? 694  LEU A N   1 
ATOM   5537 C  CA  . LEU A 1 694  ? 28.094 73.519  -31.886 1.00 15.44 ? 694  LEU A CA  1 
ATOM   5538 C  C   . LEU A 1 694  ? 26.652 73.121  -32.164 1.00 16.04 ? 694  LEU A C   1 
ATOM   5539 O  O   . LEU A 1 694  ? 25.784 73.138  -31.262 1.00 16.36 ? 694  LEU A O   1 
ATOM   5540 C  CB  . LEU A 1 694  ? 28.827 72.343  -31.212 1.00 16.79 ? 694  LEU A CB  1 
ATOM   5541 C  CG  . LEU A 1 694  ? 28.981 71.120  -32.103 1.00 17.32 ? 694  LEU A CG  1 
ATOM   5542 C  CD1 . LEU A 1 694  ? 29.933 71.385  -33.235 1.00 17.32 ? 694  LEU A CD1 1 
ATOM   5543 C  CD2 . LEU A 1 694  ? 29.577 69.972  -31.222 1.00 17.99 ? 694  LEU A CD2 1 
ATOM   5544 N  N   . LYS A 1 695  ? 26.413 72.779  -33.427 1.00 19.10 ? 695  LYS A N   1 
ATOM   5545 C  CA  . LYS A 1 695  ? 25.109 72.360  -33.915 1.00 21.21 ? 695  LYS A CA  1 
ATOM   5546 C  C   . LYS A 1 695  ? 25.179 70.949  -34.488 1.00 19.90 ? 695  LYS A C   1 
ATOM   5547 O  O   . LYS A 1 695  ? 24.235 70.175  -34.331 1.00 22.16 ? 695  LYS A O   1 
ATOM   5548 C  CB  . LYS A 1 695  ? 24.657 73.347  -35.004 1.00 25.20 ? 695  LYS A CB  1 
ATOM   5549 C  CG  A LYS A 1 695  ? 23.241 73.215  -35.481 0.50 32.56 ? 695  LYS A CG  1 
ATOM   5550 C  CG  B LYS A 1 695  ? 23.302 72.967  -35.648 0.50 32.07 ? 695  LYS A CG  1 
ATOM   5551 C  CD  A LYS A 1 695  ? 22.986 74.268  -36.568 0.50 34.04 ? 695  LYS A CD  1 
ATOM   5552 C  CD  B LYS A 1 695  ? 22.834 74.154  -36.498 0.50 34.39 ? 695  LYS A CD  1 
ATOM   5553 C  CE  A LYS A 1 695  ? 21.542 74.254  -37.045 0.50 35.52 ? 695  LYS A CE  1 
ATOM   5554 C  CE  B LYS A 1 695  ? 22.445 75.338  -35.621 0.50 35.37 ? 695  LYS A CE  1 
ATOM   5555 N  NZ  A LYS A 1 695  ? 21.371 75.131  -38.224 0.50 35.10 ? 695  LYS A NZ  1 
ATOM   5556 N  NZ  B LYS A 1 695  ? 21.203 75.068  -34.852 0.50 36.91 ? 695  LYS A NZ  1 
ATOM   5557 N  N   . SER A 1 696  ? 26.276 70.608  -35.152 1.00 19.60 ? 696  SER A N   1 
ATOM   5558 C  CA  . SER A 1 696  ? 26.406 69.285  -35.758 1.00 17.99 ? 696  SER A CA  1 
ATOM   5559 C  C   . SER A 1 696  ? 27.839 68.895  -36.003 1.00 17.74 ? 696  SER A C   1 
ATOM   5560 O  O   . SER A 1 696  ? 28.752 69.752  -36.059 1.00 18.87 ? 696  SER A O   1 
ATOM   5561 C  CB  . SER A 1 696  ? 25.601 69.226  -37.085 1.00 22.50 ? 696  SER A CB  1 
ATOM   5562 O  OG  . SER A 1 696  ? 26.243 69.967  -38.092 1.00 24.61 ? 696  SER A OG  1 
ATOM   5563 N  N   . ILE A 1 697  ? 28.066 67.585  -36.146 1.00 18.36 ? 697  ILE A N   1 
ATOM   5564 C  CA  . ILE A 1 697  ? 29.368 67.050  -36.433 1.00 17.33 ? 697  ILE A CA  1 
ATOM   5565 C  C   . ILE A 1 697  ? 29.234 66.085  -37.598 1.00 22.40 ? 697  ILE A C   1 
ATOM   5566 O  O   . ILE A 1 697  ? 28.356 65.226  -37.547 1.00 22.29 ? 697  ILE A O   1 
ATOM   5567 C  CB  . ILE A 1 697  ? 29.946 66.252  -35.231 1.00 18.62 ? 697  ILE A CB  1 
ATOM   5568 C  CG1 . ILE A 1 697  ? 30.079 67.155  -34.019 1.00 19.15 ? 697  ILE A CG1 1 
ATOM   5569 C  CG2 . ILE A 1 697  ? 31.269 65.687  -35.608 1.00 19.50 ? 697  ILE A CG2 1 
ATOM   5570 C  CD1 . ILE A 1 697  ? 30.523 66.375  -32.759 1.00 19.07 ? 697  ILE A CD1 1 
ATOM   5571 N  N   . GLN A 1 698  ? 30.086 66.243  -38.612 1.00 20.32 ? 698  GLN A N   1 
ATOM   5572 C  CA  . GLN A 1 698  ? 30.095 65.362  -39.777 1.00 22.18 ? 698  GLN A CA  1 
ATOM   5573 C  C   . GLN A 1 698  ? 31.439 64.692  -39.721 1.00 21.95 ? 698  GLN A C   1 
ATOM   5574 O  O   . GLN A 1 698  ? 32.489 65.323  -39.907 1.00 23.62 ? 698  GLN A O   1 
ATOM   5575 C  CB  . GLN A 1 698  ? 29.945 66.163  -41.075 1.00 24.98 ? 698  GLN A CB  1 
ATOM   5576 C  CG  . GLN A 1 698  ? 30.015 65.252  -42.304 1.00 27.88 ? 698  GLN A CG  1 
ATOM   5577 C  CD  . GLN A 1 698  ? 30.056 66.048  -43.577 1.00 31.27 ? 698  GLN A CD  1 
ATOM   5578 O  OE1 . GLN A 1 698  ? 29.188 65.903  -44.432 1.00 34.72 ? 698  GLN A OE1 1 
ATOM   5579 N  NE2 . GLN A 1 698  ? 31.054 66.904  -43.705 1.00 29.88 ? 698  GLN A NE2 1 
ATOM   5580 N  N   . LEU A 1 699  ? 31.439 63.389  -39.465 1.00 23.55 ? 699  LEU A N   1 
ATOM   5581 C  CA  . LEU A 1 699  ? 32.693 62.679  -39.310 1.00 27.26 ? 699  LEU A CA  1 
ATOM   5582 C  C   . LEU A 1 699  ? 33.579 62.597  -40.533 1.00 29.50 ? 699  LEU A C   1 
ATOM   5583 O  O   . LEU A 1 699  ? 34.798 62.719  -40.425 1.00 29.11 ? 699  LEU A O   1 
ATOM   5584 C  CB  . LEU A 1 699  ? 32.437 61.262  -38.770 1.00 28.12 ? 699  LEU A CB  1 
ATOM   5585 C  CG  . LEU A 1 699  ? 31.774 61.179  -37.386 1.00 27.74 ? 699  LEU A CG  1 
ATOM   5586 C  CD1 . LEU A 1 699  ? 31.696 59.706  -36.933 1.00 28.25 ? 699  LEU A CD1 1 
ATOM   5587 C  CD2 . LEU A 1 699  ? 32.574 61.992  -36.407 1.00 28.52 ? 699  LEU A CD2 1 
ATOM   5588 N  N   . THR A 1 700  ? 32.972 62.404  -41.698 1.00 32.56 ? 700  THR A N   1 
ATOM   5589 C  CA  . THR A 1 700  ? 33.730 62.266  -42.936 1.00 37.44 ? 700  THR A CA  1 
ATOM   5590 C  C   . THR A 1 700  ? 33.012 62.995  -44.061 1.00 38.99 ? 700  THR A C   1 
ATOM   5591 O  O   . THR A 1 700  ? 31.848 63.353  -43.922 1.00 40.13 ? 700  THR A O   1 
ATOM   5592 C  CB  . THR A 1 700  ? 33.883 60.768  -43.336 1.00 36.94 ? 700  THR A CB  1 
ATOM   5593 O  OG1 . THR A 1 700  ? 32.584 60.198  -43.581 1.00 38.62 ? 700  THR A OG1 1 
ATOM   5594 C  CG2 . THR A 1 700  ? 34.552 59.982  -42.223 1.00 37.54 ? 700  THR A CG2 1 
ATOM   5595 N  N   . GLN A 1 701  ? 33.718 63.201  -45.173 1.00 43.70 ? 701  GLN A N   1 
ATOM   5596 C  CA  . GLN A 1 701  ? 33.173 63.883  -46.345 1.00 47.52 ? 701  GLN A CA  1 
ATOM   5597 C  C   . GLN A 1 701  ? 31.760 63.454  -46.721 1.00 48.01 ? 701  GLN A C   1 
ATOM   5598 O  O   . GLN A 1 701  ? 30.874 64.298  -46.915 1.00 49.45 ? 701  GLN A O   1 
ATOM   5599 C  CB  . GLN A 1 701  ? 34.088 63.661  -47.556 1.00 50.54 ? 701  GLN A CB  1 
ATOM   5600 C  CG  . GLN A 1 701  ? 35.355 64.508  -47.563 1.00 54.58 ? 701  GLN A CG  1 
ATOM   5601 C  CD  . GLN A 1 701  ? 35.067 65.988  -47.796 1.00 57.84 ? 701  GLN A CD  1 
ATOM   5602 O  OE1 . GLN A 1 701  ? 35.989 66.815  -47.838 1.00 59.39 ? 701  GLN A OE1 1 
ATOM   5603 N  NE2 . GLN A 1 701  ? 33.784 66.332  -47.948 1.00 59.56 ? 701  GLN A NE2 1 
ATOM   5604 N  N   . ASP A 1 702  ? 31.548 62.148  -46.816 1.00 48.38 ? 702  ASP A N   1 
ATOM   5605 C  CA  . ASP A 1 702  ? 30.240 61.611  -47.190 1.00 50.33 ? 702  ASP A CA  1 
ATOM   5606 C  C   . ASP A 1 702  ? 29.161 61.632  -46.102 1.00 49.45 ? 702  ASP A C   1 
ATOM   5607 O  O   . ASP A 1 702  ? 28.027 62.086  -46.340 1.00 49.64 ? 702  ASP A O   1 
ATOM   5608 C  CB  . ASP A 1 702  ? 30.403 60.172  -47.712 1.00 53.18 ? 702  ASP A CB  1 
ATOM   5609 C  CG  . ASP A 1 702  ? 31.068 59.246  -46.696 1.00 55.78 ? 702  ASP A CG  1 
ATOM   5610 O  OD1 . ASP A 1 702  ? 32.242 59.500  -46.328 1.00 56.93 ? 702  ASP A OD1 1 
ATOM   5611 O  OD2 . ASP A 1 702  ? 30.414 58.263  -46.268 1.00 57.27 ? 702  ASP A OD2 1 
ATOM   5612 N  N   . SER A 1 703  ? 29.534 61.149  -44.916 1.00 46.53 ? 703  SER A N   1 
ATOM   5613 C  CA  . SER A 1 703  ? 28.649 61.033  -43.759 1.00 43.00 ? 703  SER A CA  1 
ATOM   5614 C  C   . SER A 1 703  ? 27.718 62.192  -43.462 1.00 40.25 ? 703  SER A C   1 
ATOM   5615 O  O   . SER A 1 703  ? 27.963 63.323  -43.867 1.00 40.44 ? 703  SER A O   1 
ATOM   5616 C  CB  . SER A 1 703  ? 29.483 60.720  -42.508 1.00 43.99 ? 703  SER A CB  1 
ATOM   5617 O  OG  . SER A 1 703  ? 30.365 61.783  -42.179 1.00 41.89 ? 703  SER A OG  1 
ATOM   5618 N  N   . PRO A 1 704  ? 26.631 61.918  -42.719 1.00 38.47 ? 704  PRO A N   1 
ATOM   5619 C  CA  . PRO A 1 704  ? 25.664 62.946  -42.361 1.00 36.85 ? 704  PRO A CA  1 
ATOM   5620 C  C   . PRO A 1 704  ? 26.146 63.926  -41.295 1.00 35.81 ? 704  PRO A C   1 
ATOM   5621 O  O   . PRO A 1 704  ? 27.106 63.677  -40.550 1.00 32.61 ? 704  PRO A O   1 
ATOM   5622 C  CB  . PRO A 1 704  ? 24.468 62.141  -41.875 1.00 38.86 ? 704  PRO A CB  1 
ATOM   5623 C  CG  . PRO A 1 704  ? 25.093 60.945  -41.281 1.00 39.42 ? 704  PRO A CG  1 
ATOM   5624 C  CD  . PRO A 1 704  ? 26.168 60.592  -42.269 1.00 38.74 ? 704  PRO A CD  1 
ATOM   5625 N  N   . HIS A 1 705  ? 25.449 65.050  -41.246 1.00 34.22 ? 705  HIS A N   1 
ATOM   5626 C  CA  . HIS A 1 705  ? 25.728 66.080  -40.263 1.00 31.95 ? 705  HIS A CA  1 
ATOM   5627 C  C   . HIS A 1 705  ? 24.871 65.684  -39.065 1.00 29.36 ? 705  HIS A C   1 
ATOM   5628 O  O   . HIS A 1 705  ? 23.692 65.996  -38.982 1.00 29.24 ? 705  HIS A O   1 
ATOM   5629 C  CB  . HIS A 1 705  ? 25.349 67.461  -40.831 1.00 34.70 ? 705  HIS A CB  1 
ATOM   5630 C  CG  . HIS A 1 705  ? 26.234 67.898  -41.967 1.00 36.50 ? 705  HIS A CG  1 
ATOM   5631 N  ND1 . HIS A 1 705  ? 27.449 68.521  -41.766 1.00 36.23 ? 705  HIS A ND1 1 
ATOM   5632 C  CD2 . HIS A 1 705  ? 26.140 67.688  -43.304 1.00 36.91 ? 705  HIS A CD2 1 
ATOM   5633 C  CE1 . HIS A 1 705  ? 28.072 68.662  -42.924 1.00 38.78 ? 705  HIS A CE1 1 
ATOM   5634 N  NE2 . HIS A 1 705  ? 27.298 68.163  -43.875 1.00 38.03 ? 705  HIS A NE2 1 
ATOM   5635 N  N   . VAL A 1 706  ? 25.510 65.014  -38.102 1.00 25.06 ? 706  VAL A N   1 
ATOM   5636 C  CA  . VAL A 1 706  ? 24.843 64.526  -36.906 1.00 22.41 ? 706  VAL A CA  1 
ATOM   5637 C  C   . VAL A 1 706  ? 24.522 65.629  -35.917 1.00 21.22 ? 706  VAL A C   1 
ATOM   5638 O  O   . VAL A 1 706  ? 25.423 66.326  -35.446 1.00 21.44 ? 706  VAL A O   1 
ATOM   5639 C  CB  . VAL A 1 706  ? 25.768 63.469  -36.214 1.00 22.01 ? 706  VAL A CB  1 
ATOM   5640 C  CG1 . VAL A 1 706  ? 25.073 62.867  -35.007 1.00 24.47 ? 706  VAL A CG1 1 
ATOM   5641 C  CG2 . VAL A 1 706  ? 26.191 62.413  -37.224 1.00 22.84 ? 706  VAL A CG2 1 
ATOM   5642 N  N   . PRO A 1 707  ? 23.256 65.814  -35.574 1.00 21.37 ? 707  PRO A N   1 
ATOM   5643 C  CA  . PRO A 1 707  ? 22.924 66.866  -34.620 1.00 20.40 ? 707  PRO A CA  1 
ATOM   5644 C  C   . PRO A 1 707  ? 23.620 66.608  -33.270 1.00 20.94 ? 707  PRO A C   1 
ATOM   5645 O  O   . PRO A 1 707  ? 23.469 65.527  -32.676 1.00 23.14 ? 707  PRO A O   1 
ATOM   5646 C  CB  . PRO A 1 707  ? 21.403 66.766  -34.494 1.00 22.82 ? 707  PRO A CB  1 
ATOM   5647 C  CG  . PRO A 1 707  ? 20.981 66.098  -35.791 1.00 24.21 ? 707  PRO A CG  1 
ATOM   5648 C  CD  . PRO A 1 707  ? 22.039 65.080  -35.998 1.00 21.34 ? 707  PRO A CD  1 
ATOM   5649 N  N   . VAL A 1 708  ? 24.373 67.605  -32.802 1.00 20.35 ? 708  VAL A N   1 
ATOM   5650 C  CA  . VAL A 1 708  ? 25.095 67.565  -31.507 1.00 16.86 ? 708  VAL A CA  1 
ATOM   5651 C  C   . VAL A 1 708  ? 25.044 69.042  -31.147 1.00 17.08 ? 708  VAL A C   1 
ATOM   5652 O  O   . VAL A 1 708  ? 25.807 69.861  -31.693 1.00 21.16 ? 708  VAL A O   1 
ATOM   5653 C  CB  . VAL A 1 708  ? 26.536 67.082  -31.654 1.00 17.84 ? 708  VAL A CB  1 
ATOM   5654 C  CG1 . VAL A 1 708  ? 27.208 67.102  -30.273 1.00 17.56 ? 708  VAL A CG1 1 
ATOM   5655 C  CG2 . VAL A 1 708  ? 26.564 65.622  -32.176 1.00 19.79 ? 708  VAL A CG2 1 
ATOM   5656 N  N   . HIS A 1 709  ? 24.143 69.395  -30.242 1.00 16.22 ? 709  HIS A N   1 
ATOM   5657 C  CA  . HIS A 1 709  ? 23.932 70.800  -29.879 1.00 17.75 ? 709  HIS A CA  1 
ATOM   5658 C  C   . HIS A 1 709  ? 24.323 71.178  -28.450 1.00 17.88 ? 709  HIS A C   1 
ATOM   5659 O  O   A HIS A 1 709  ? 23.765 70.631  -27.484 0.50 17.94 ? 709  HIS A O   1 
ATOM   5660 O  O   B HIS A 1 709  ? 24.039 70.365  -27.585 0.50 18.78 ? 709  HIS A O   1 
ATOM   5661 C  CB  . HIS A 1 709  ? 22.448 71.177  -30.067 1.00 20.74 ? 709  HIS A CB  1 
ATOM   5662 C  CG  A HIS A 1 709  ? 21.972 71.164  -31.487 0.50 23.21 ? 709  HIS A CG  1 
ATOM   5663 C  CG  B HIS A 1 709  ? 22.299 72.670  -29.861 0.50 23.29 ? 709  HIS A CG  1 
ATOM   5664 N  ND1 A HIS A 1 709  ? 21.316 72.237  -32.056 0.50 26.83 ? 709  HIS A ND1 1 
ATOM   5665 N  ND1 B HIS A 1 709  ? 23.065 73.705  -30.358 0.50 25.59 ? 709  HIS A ND1 1 
ATOM   5666 C  CD2 A HIS A 1 709  ? 22.006 70.200  -32.437 0.50 24.29 ? 709  HIS A CD2 1 
ATOM   5667 C  CD2 B HIS A 1 709  ? 21.303 73.249  -29.148 0.50 25.08 ? 709  HIS A CD2 1 
ATOM   5668 C  CE1 A HIS A 1 709  ? 20.967 71.932  -33.294 0.50 25.44 ? 709  HIS A CE1 1 
ATOM   5669 C  CE1 B HIS A 1 709  ? 22.551 74.857  -29.966 0.50 24.28 ? 709  HIS A CE1 1 
ATOM   5670 N  NE2 A HIS A 1 709  ? 21.375 70.701  -33.549 0.50 20.28 ? 709  HIS A NE2 1 
ATOM   5671 N  NE2 B HIS A 1 709  ? 21.482 74.609  -29.232 0.50 26.07 ? 709  HIS A NE2 1 
ATOM   5672 N  N   . PHE A 1 710  ? 25.253 72.124  -28.302 1.00 16.25 ? 710  PHE A N   1 
ATOM   5673 C  CA  . PHE A 1 710  ? 25.638 72.566  -26.974 1.00 16.98 ? 710  PHE A CA  1 
ATOM   5674 C  C   . PHE A 1 710  ? 24.631 73.656  -26.538 1.00 17.52 ? 710  PHE A C   1 
ATOM   5675 O  O   . PHE A 1 710  ? 24.180 74.501  -27.360 1.00 17.73 ? 710  PHE A O   1 
ATOM   5676 C  CB  . PHE A 1 710  ? 27.046 73.177  -26.937 1.00 17.93 ? 710  PHE A CB  1 
ATOM   5677 C  CG  . PHE A 1 710  ? 28.147 72.208  -26.548 1.00 17.83 ? 710  PHE A CG  1 
ATOM   5678 C  CD1 . PHE A 1 710  ? 28.093 71.537  -25.344 1.00 20.69 ? 710  PHE A CD1 1 
ATOM   5679 C  CD2 . PHE A 1 710  ? 29.251 72.003  -27.374 1.00 20.76 ? 710  PHE A CD2 1 
ATOM   5680 C  CE1 . PHE A 1 710  ? 29.122 70.664  -24.948 1.00 21.24 ? 710  PHE A CE1 1 
ATOM   5681 C  CE2 . PHE A 1 710  ? 30.288 71.128  -26.959 1.00 19.80 ? 710  PHE A CE2 1 
ATOM   5682 C  CZ  . PHE A 1 710  ? 30.206 70.482  -25.770 1.00 20.62 ? 710  PHE A CZ  1 
ATOM   5683 N  N   . LYS A 1 711  ? 24.283 73.656  -25.274 1.00 16.42 ? 711  LYS A N   1 
ATOM   5684 C  CA  . LYS A 1 711  ? 23.371 74.619  -24.709 1.00 17.53 ? 711  LYS A CA  1 
ATOM   5685 C  C   . LYS A 1 711  ? 23.722 74.834  -23.252 1.00 17.71 ? 711  LYS A C   1 
ATOM   5686 O  O   . LYS A 1 711  ? 24.076 73.866  -22.555 1.00 19.33 ? 711  LYS A O   1 
ATOM   5687 C  CB  . LYS A 1 711  ? 21.913 74.111  -24.820 1.00 20.20 ? 711  LYS A CB  1 
ATOM   5688 C  CG  . LYS A 1 711  ? 20.880 75.041  -24.241 1.00 24.51 ? 711  LYS A CG  1 
ATOM   5689 C  CD  . LYS A 1 711  ? 19.455 74.457  -24.406 1.00 29.78 ? 711  LYS A CD  1 
ATOM   5690 C  CE  . LYS A 1 711  ? 19.073 74.396  -25.898 1.00 29.84 ? 711  LYS A CE  1 
ATOM   5691 N  NZ  . LYS A 1 711  ? 17.735 73.720  -26.070 1.00 31.38 ? 711  LYS A NZ  1 
ATOM   5692 N  N   . PHE A 1 712  ? 23.645 76.068  -22.784 1.00 15.78 ? 712  PHE A N   1 
ATOM   5693 C  CA  . PHE A 1 712  ? 23.867 76.405  -21.411 1.00 15.92 ? 712  PHE A CA  1 
ATOM   5694 C  C   . PHE A 1 712  ? 22.560 76.750  -20.731 1.00 16.85 ? 712  PHE A C   1 
ATOM   5695 O  O   . PHE A 1 712  ? 21.745 77.502  -21.275 1.00 17.06 ? 712  PHE A O   1 
ATOM   5696 C  CB  . PHE A 1 712  ? 24.884 77.554  -21.243 1.00 17.83 ? 712  PHE A CB  1 
ATOM   5697 C  CG  . PHE A 1 712  ? 26.306 77.149  -21.558 1.00 16.21 ? 712  PHE A CG  1 
ATOM   5698 C  CD1 . PHE A 1 712  ? 26.776 77.205  -22.852 1.00 17.44 ? 712  PHE A CD1 1 
ATOM   5699 C  CD2 . PHE A 1 712  ? 27.157 76.643  -20.557 1.00 16.63 ? 712  PHE A CD2 1 
ATOM   5700 C  CE1 . PHE A 1 712  ? 28.049 76.768  -23.184 1.00 15.45 ? 712  PHE A CE1 1 
ATOM   5701 C  CE2 . PHE A 1 712  ? 28.412 76.221  -20.878 1.00 15.66 ? 712  PHE A CE2 1 
ATOM   5702 C  CZ  . PHE A 1 712  ? 28.878 76.270  -22.179 1.00 16.87 ? 712  PHE A CZ  1 
ATOM   5703 N  N   . LEU A 1 713  ? 22.328 76.144  -19.579 1.00 15.04 ? 713  LEU A N   1 
ATOM   5704 C  CA  . LEU A 1 713  ? 21.097 76.367  -18.811 1.00 15.23 ? 713  LEU A CA  1 
ATOM   5705 C  C   . LEU A 1 713  ? 21.439 76.640  -17.363 1.00 15.21 ? 713  LEU A C   1 
ATOM   5706 O  O   . LEU A 1 713  ? 22.626 76.544  -16.932 1.00 16.52 ? 713  LEU A O   1 
ATOM   5707 C  CB  . LEU A 1 713  ? 20.145 75.163  -18.899 1.00 16.34 ? 713  LEU A CB  1 
ATOM   5708 C  CG  . LEU A 1 713  ? 19.842 74.709  -20.318 1.00 16.16 ? 713  LEU A CG  1 
ATOM   5709 C  CD1 . LEU A 1 713  ? 20.728 73.527  -20.693 1.00 17.56 ? 713  LEU A CD1 1 
ATOM   5710 C  CD2 . LEU A 1 713  ? 18.355 74.223  -20.406 1.00 18.18 ? 713  LEU A CD2 1 
ATOM   5711 N  N   . LYS A 1 714  ? 20.418 77.006  -16.592 1.00 15.57 ? 714  LYS A N   1 
ATOM   5712 C  CA  . LYS A 1 714  ? 20.611 77.287  -15.206 1.00 16.34 ? 714  LYS A CA  1 
ATOM   5713 C  C   . LYS A 1 714  ? 19.593 76.637  -14.316 1.00 18.33 ? 714  LYS A C   1 
ATOM   5714 O  O   . LYS A 1 714  ? 18.398 76.578  -14.632 1.00 18.63 ? 714  LYS A O   1 
ATOM   5715 C  CB  . LYS A 1 714  ? 20.563 78.783  -14.936 1.00 22.79 ? 714  LYS A CB  1 
ATOM   5716 C  CG  . LYS A 1 714  ? 19.423 79.488  -15.601 1.00 29.73 ? 714  LYS A CG  1 
ATOM   5717 C  CD  . LYS A 1 714  ? 19.490 81.001  -15.308 1.00 34.24 ? 714  LYS A CD  1 
ATOM   5718 C  CE  . LYS A 1 714  ? 20.879 81.592  -15.507 1.00 38.37 ? 714  LYS A CE  1 
ATOM   5719 N  NZ  . LYS A 1 714  ? 20.915 83.083  -15.261 1.00 43.04 ? 714  LYS A NZ  1 
ATOM   5720 N  N   . TYR A 1 715  ? 20.088 76.126  -13.192 1.00 15.04 ? 715  TYR A N   1 
ATOM   5721 C  CA  . TYR A 1 715  ? 19.218 75.592  -12.168 1.00 15.35 ? 715  TYR A CA  1 
ATOM   5722 C  C   . TYR A 1 715  ? 19.171 76.633  -11.060 1.00 18.16 ? 715  TYR A C   1 
ATOM   5723 O  O   . TYR A 1 715  ? 20.135 77.390  -10.813 1.00 18.41 ? 715  TYR A O   1 
ATOM   5724 C  CB  . TYR A 1 715  ? 19.790 74.308  -11.533 1.00 15.56 ? 715  TYR A CB  1 
ATOM   5725 C  CG  . TYR A 1 715  ? 19.706 73.096  -12.382 1.00 13.57 ? 715  TYR A CG  1 
ATOM   5726 C  CD1 . TYR A 1 715  ? 18.514 72.345  -12.441 1.00 14.32 ? 715  TYR A CD1 1 
ATOM   5727 C  CD2 . TYR A 1 715  ? 20.814 72.648  -13.149 1.00 13.29 ? 715  TYR A CD2 1 
ATOM   5728 C  CE1 . TYR A 1 715  ? 18.437 71.212  -13.212 1.00 15.82 ? 715  TYR A CE1 1 
ATOM   5729 C  CE2 . TYR A 1 715  ? 20.731 71.504  -13.934 1.00 14.07 ? 715  TYR A CE2 1 
ATOM   5730 C  CZ  . TYR A 1 715  ? 19.530 70.780  -13.959 1.00 16.02 ? 715  TYR A CZ  1 
ATOM   5731 O  OH  . TYR A 1 715  ? 19.397 69.632  -14.664 1.00 16.45 ? 715  TYR A OH  1 
ATOM   5732 N  N   . GLY A 1 716  ? 18.069 76.622  -10.332 1.00 17.14 ? 716  GLY A N   1 
ATOM   5733 C  CA  . GLY A 1 716  ? 17.891 77.545  -9.246  1.00 17.53 ? 716  GLY A CA  1 
ATOM   5734 C  C   . GLY A 1 716  ? 17.766 76.799  -7.925  1.00 18.66 ? 716  GLY A C   1 
ATOM   5735 O  O   . GLY A 1 716  ? 18.075 75.611  -7.819  1.00 18.83 ? 716  GLY A O   1 
ATOM   5736 N  N   . VAL A 1 717  ? 17.285 77.512  -6.922  1.00 17.30 ? 717  VAL A N   1 
ATOM   5737 C  CA  . VAL A 1 717  ? 17.139 76.989  -5.580  1.00 19.39 ? 717  VAL A CA  1 
ATOM   5738 C  C   . VAL A 1 717  ? 15.692 77.140  -5.148  1.00 20.75 ? 717  VAL A C   1 
ATOM   5739 O  O   . VAL A 1 717  ? 15.004 78.067  -5.587  1.00 22.36 ? 717  VAL A O   1 
ATOM   5740 C  CB  . VAL A 1 717  ? 18.102 77.758  -4.622  1.00 18.85 ? 717  VAL A CB  1 
ATOM   5741 C  CG1 . VAL A 1 717  ? 17.916 77.335  -3.196  1.00 22.20 ? 717  VAL A CG1 1 
ATOM   5742 C  CG2 . VAL A 1 717  ? 19.561 77.513  -5.052  1.00 19.87 ? 717  VAL A CG2 1 
ATOM   5743 N  N   . ARG A 1 718  ? 15.244 76.251  -4.273  1.00 20.63 ? 718  ARG A N   1 
ATOM   5744 C  CA  . ARG A 1 718  ? 13.873 76.288  -3.782  1.00 22.09 ? 718  ARG A CA  1 
ATOM   5745 C  C   . ARG A 1 718  ? 13.645 77.461  -2.861  1.00 24.39 ? 718  ARG A C   1 
ATOM   5746 O  O   . ARG A 1 718  ? 14.512 77.858  -2.096  1.00 27.48 ? 718  ARG A O   1 
ATOM   5747 C  CB  . ARG A 1 718  ? 13.525 74.963  -3.068  1.00 19.09 ? 718  ARG A CB  1 
ATOM   5748 C  CG  . ARG A 1 718  ? 13.565 73.784  -4.013  1.00 19.29 ? 718  ARG A CG  1 
ATOM   5749 C  CD  . ARG A 1 718  ? 13.542 72.448  -3.290  1.00 19.27 ? 718  ARG A CD  1 
ATOM   5750 N  NE  . ARG A 1 718  ? 13.834 71.422  -4.266  1.00 20.82 ? 718  ARG A NE  1 
ATOM   5751 C  CZ  . ARG A 1 718  ? 13.768 70.115  -4.024  1.00 21.85 ? 718  ARG A CZ  1 
ATOM   5752 N  NH1 . ARG A 1 718  ? 13.398 69.681  -2.827  1.00 21.98 ? 718  ARG A NH1 1 
ATOM   5753 N  NH2 . ARG A 1 718  ? 14.109 69.268  -4.988  1.00 22.68 ? 718  ARG A NH2 1 
ATOM   5754 N  N   . SER A 1 719  ? 12.454 78.030  -2.965  1.00 25.73 ? 719  SER A N   1 
ATOM   5755 C  CA  . SER A 1 719  ? 12.097 79.174  -2.137  1.00 28.57 ? 719  SER A CA  1 
ATOM   5756 C  C   . SER A 1 719  ? 11.422 78.696  -0.869  1.00 30.70 ? 719  SER A C   1 
ATOM   5757 O  O   . SER A 1 719  ? 11.247 79.459  0.058   1.00 32.60 ? 719  SER A O   1 
ATOM   5758 C  CB  . SER A 1 719  ? 11.164 80.116  -2.918  1.00 29.99 ? 719  SER A CB  1 
ATOM   5759 O  OG  . SER A 1 719  ? 10.039 79.408  -3.388  1.00 33.46 ? 719  SER A OG  1 
ATOM   5760 N  N   . HIS A 1 720  ? 11.010 77.436  -0.841  1.00 31.88 ? 720  HIS A N   1 
ATOM   5761 C  CA  . HIS A 1 720  ? 10.431 76.883  0.364   1.00 33.70 ? 720  HIS A CA  1 
ATOM   5762 C  C   . HIS A 1 720  ? 10.971 75.440  0.462   1.00 32.65 ? 720  HIS A C   1 
ATOM   5763 O  O   . HIS A 1 720  ? 11.245 74.783  -0.552  1.00 32.22 ? 720  HIS A O   1 
ATOM   5764 C  CB  . HIS A 1 720  ? 8.889  76.998  0.318   1.00 37.49 ? 720  HIS A CB  1 
ATOM   5765 C  CG  . HIS A 1 720  ? 8.200  75.882  -0.395  1.00 42.51 ? 720  HIS A CG  1 
ATOM   5766 N  ND1 . HIS A 1 720  ? 7.637  74.812  0.272   1.00 44.73 ? 720  HIS A ND1 1 
ATOM   5767 C  CD2 . HIS A 1 720  ? 7.959  75.677  -1.713  1.00 45.35 ? 720  HIS A CD2 1 
ATOM   5768 C  CE1 . HIS A 1 720  ? 7.077  73.995  -0.605  1.00 47.18 ? 720  HIS A CE1 1 
ATOM   5769 N  NE2 . HIS A 1 720  ? 7.258  74.496  -1.818  1.00 48.43 ? 720  HIS A NE2 1 
ATOM   5770 N  N   . GLY A 1 721  ? 11.165 74.962  1.679   1.00 30.81 ? 721  GLY A N   1 
ATOM   5771 C  CA  . GLY A 1 721  ? 11.719 73.631  1.841   1.00 30.31 ? 721  GLY A CA  1 
ATOM   5772 C  C   . GLY A 1 721  ? 13.244 73.683  2.027   1.00 30.04 ? 721  GLY A C   1 
ATOM   5773 O  O   . GLY A 1 721  ? 13.812 74.700  2.444   1.00 29.16 ? 721  GLY A O   1 
ATOM   5774 N  N   . ASP A 1 722  ? 13.922 72.592  1.679   1.00 26.87 ? 722  ASP A N   1 
ATOM   5775 C  CA  . ASP A 1 722  ? 15.372 72.518  1.885   1.00 24.52 ? 722  ASP A CA  1 
ATOM   5776 C  C   . ASP A 1 722  ? 16.131 73.215  0.770   1.00 20.76 ? 722  ASP A C   1 
ATOM   5777 O  O   . ASP A 1 722  ? 15.745 73.155  -0.383  1.00 21.16 ? 722  ASP A O   1 
ATOM   5778 C  CB  . ASP A 1 722  ? 15.815 71.051  1.992   1.00 21.80 ? 722  ASP A CB  1 
ATOM   5779 C  CG  . ASP A 1 722  ? 15.155 70.310  3.170   1.00 23.04 ? 722  ASP A CG  1 
ATOM   5780 O  OD1 . ASP A 1 722  ? 14.912 70.911  4.244   1.00 23.99 ? 722  ASP A OD1 1 
ATOM   5781 O  OD2 . ASP A 1 722  ? 14.876 69.105  3.025   1.00 23.16 ? 722  ASP A OD2 1 
ATOM   5782 N  N   . ARG A 1 723  ? 17.194 73.903  1.165   1.00 19.51 ? 723  ARG A N   1 
ATOM   5783 C  CA  . ARG A 1 723  ? 18.031 74.634  0.232   1.00 20.35 ? 723  ARG A CA  1 
ATOM   5784 C  C   . ARG A 1 723  ? 19.297 73.896  -0.186  1.00 19.05 ? 723  ARG A C   1 
ATOM   5785 O  O   . ARG A 1 723  ? 19.946 73.230  0.628   1.00 18.06 ? 723  ARG A O   1 
ATOM   5786 C  CB  . ARG A 1 723  ? 18.452 75.974  0.852   1.00 22.90 ? 723  ARG A CB  1 
ATOM   5787 C  CG  . ARG A 1 723  ? 17.423 77.108  0.732   1.00 32.46 ? 723  ARG A CG  1 
ATOM   5788 C  CD  . ARG A 1 723  ? 16.215 76.874  1.614   1.00 39.81 ? 723  ARG A CD  1 
ATOM   5789 N  NE  . ARG A 1 723  ? 15.206 77.942  1.539   1.00 44.91 ? 723  ARG A NE  1 
ATOM   5790 C  CZ  . ARG A 1 723  ? 15.445 79.225  1.804   1.00 48.52 ? 723  ARG A CZ  1 
ATOM   5791 N  NH1 . ARG A 1 723  ? 16.670 79.627  2.146   1.00 50.14 ? 723  ARG A NH1 1 
ATOM   5792 N  NH2 . ARG A 1 723  ? 14.445 80.101  1.788   1.00 48.57 ? 723  ARG A NH2 1 
ATOM   5793 N  N   . SER A 1 724  ? 19.630 74.033  -1.467  1.00 18.05 ? 724  SER A N   1 
ATOM   5794 C  CA  . SER A 1 724  ? 20.870 73.504  -2.002  1.00 16.91 ? 724  SER A CA  1 
ATOM   5795 C  C   . SER A 1 724  ? 22.009 74.207  -1.250  1.00 17.78 ? 724  SER A C   1 
ATOM   5796 O  O   . SER A 1 724  ? 21.890 75.378  -0.857  1.00 19.24 ? 724  SER A O   1 
ATOM   5797 C  CB  . SER A 1 724  ? 20.998 73.867  -3.475  1.00 18.04 ? 724  SER A CB  1 
ATOM   5798 O  OG  . SER A 1 724  ? 19.979 73.230  -4.216  1.00 17.10 ? 724  SER A OG  1 
ATOM   5799 N  N   . GLY A 1 725  ? 23.135 73.510  -1.098  1.00 15.24 ? 725  GLY A N   1 
ATOM   5800 C  CA  . GLY A 1 725  ? 24.304 74.088  -0.441  1.00 15.40 ? 725  GLY A CA  1 
ATOM   5801 C  C   . GLY A 1 725  ? 25.531 73.365  -1.004  1.00 13.09 ? 725  GLY A C   1 
ATOM   5802 O  O   . GLY A 1 725  ? 25.431 72.694  -2.045  1.00 15.44 ? 725  GLY A O   1 
ATOM   5803 N  N   . ALA A 1 726  ? 26.673 73.472  -0.328  1.00 13.83 ? 726  ALA A N   1 
ATOM   5804 C  CA  . ALA A 1 726  ? 27.915 72.822  -0.795  1.00 12.07 ? 726  ALA A CA  1 
ATOM   5805 C  C   . ALA A 1 726  ? 27.759 71.296  -0.994  1.00 12.55 ? 726  ALA A C   1 
ATOM   5806 O  O   . ALA A 1 726  ? 28.398 70.723  -1.882  1.00 13.43 ? 726  ALA A O   1 
ATOM   5807 C  CB  . ALA A 1 726  ? 29.062 73.071  0.220   1.00 14.25 ? 726  ALA A CB  1 
ATOM   5808 N  N   . TYR A 1 727  ? 26.931 70.652  -0.164  1.00 12.79 ? 727  TYR A N   1 
ATOM   5809 C  CA  . TYR A 1 727  ? 26.732 69.199  -0.266  1.00 12.27 ? 727  TYR A CA  1 
ATOM   5810 C  C   . TYR A 1 727  ? 25.530 68.802  -1.106  1.00 13.67 ? 727  TYR A C   1 
ATOM   5811 O  O   . TYR A 1 727  ? 25.659 67.978  -2.023  1.00 13.92 ? 727  TYR A O   1 
ATOM   5812 C  CB  . TYR A 1 727  ? 26.510 68.580  1.120   1.00 13.91 ? 727  TYR A CB  1 
ATOM   5813 C  CG  . TYR A 1 727  ? 27.614 68.787  2.128   1.00 14.68 ? 727  TYR A CG  1 
ATOM   5814 C  CD1 . TYR A 1 727  ? 27.628 69.905  2.951   1.00 14.45 ? 727  TYR A CD1 1 
ATOM   5815 C  CD2 . TYR A 1 727  ? 28.633 67.862  2.268   1.00 13.94 ? 727  TYR A CD2 1 
ATOM   5816 C  CE1 . TYR A 1 727  ? 28.631 70.101  3.902   1.00 14.59 ? 727  TYR A CE1 1 
ATOM   5817 C  CE2 . TYR A 1 727  ? 29.646 68.046  3.228   1.00 15.31 ? 727  TYR A CE2 1 
ATOM   5818 C  CZ  . TYR A 1 727  ? 29.632 69.159  4.027   1.00 16.19 ? 727  TYR A CZ  1 
ATOM   5819 O  OH  . TYR A 1 727  ? 30.665 69.305  4.944   1.00 16.91 ? 727  TYR A OH  1 
ATOM   5820 N  N   . LEU A 1 728  ? 24.380 69.422  -0.838  1.00 15.11 ? 728  LEU A N   1 
ATOM   5821 C  CA  . LEU A 1 728  ? 23.139 69.011  -1.516  1.00 13.64 ? 728  LEU A CA  1 
ATOM   5822 C  C   . LEU A 1 728  ? 22.767 69.757  -2.782  1.00 13.80 ? 728  LEU A C   1 
ATOM   5823 O  O   . LEU A 1 728  ? 23.006 70.967  -2.866  1.00 14.55 ? 728  LEU A O   1 
ATOM   5824 C  CB  . LEU A 1 728  ? 21.956 69.219  -0.538  1.00 14.80 ? 728  LEU A CB  1 
ATOM   5825 C  CG  . LEU A 1 728  ? 22.119 68.627  0.849   1.00 13.88 ? 728  LEU A CG  1 
ATOM   5826 C  CD1 . LEU A 1 728  ? 20.781 68.843  1.652   1.00 18.86 ? 728  LEU A CD1 1 
ATOM   5827 C  CD2 . LEU A 1 728  ? 22.451 67.160  0.767   1.00 16.18 ? 728  LEU A CD2 1 
ATOM   5828 N  N   . PHE A 1 729  ? 22.195 69.047  -3.751  1.00 14.74 ? 729  PHE A N   1 
ATOM   5829 C  CA  . PHE A 1 729  ? 21.662 69.632  -4.971  1.00 14.40 ? 729  PHE A CA  1 
ATOM   5830 C  C   . PHE A 1 729  ? 20.121 69.424  -4.849  1.00 14.85 ? 729  PHE A C   1 
ATOM   5831 O  O   . PHE A 1 729  ? 19.616 68.292  -4.908  1.00 15.38 ? 729  PHE A O   1 
ATOM   5832 C  CB  . PHE A 1 729  ? 22.238 68.902  -6.195  1.00 13.86 ? 729  PHE A CB  1 
ATOM   5833 C  CG  . PHE A 1 729  ? 21.699 69.389  -7.528  1.00 13.60 ? 729  PHE A CG  1 
ATOM   5834 C  CD1 . PHE A 1 729  ? 21.375 70.747  -7.746  1.00 14.67 ? 729  PHE A CD1 1 
ATOM   5835 C  CD2 . PHE A 1 729  ? 21.586 68.489  -8.571  1.00 12.85 ? 729  PHE A CD2 1 
ATOM   5836 C  CE1 . PHE A 1 729  ? 20.940 71.157  -9.051  1.00 14.11 ? 729  PHE A CE1 1 
ATOM   5837 C  CE2 . PHE A 1 729  ? 21.163 68.889  -9.842  1.00 13.93 ? 729  PHE A CE2 1 
ATOM   5838 C  CZ  . PHE A 1 729  ? 20.843 70.213  -10.077 1.00 16.03 ? 729  PHE A CZ  1 
ATOM   5839 N  N   . LEU A 1 730  ? 19.406 70.543  -4.672  1.00 15.45 ? 730  LEU A N   1 
ATOM   5840 C  CA  . LEU A 1 730  ? 17.949 70.537  -4.497  1.00 17.44 ? 730  LEU A CA  1 
ATOM   5841 C  C   . LEU A 1 730  ? 17.378 71.567  -5.462  1.00 15.18 ? 730  LEU A C   1 
ATOM   5842 O  O   . LEU A 1 730  ? 16.903 72.627  -5.040  1.00 16.97 ? 730  LEU A O   1 
ATOM   5843 C  CB  . LEU A 1 730  ? 17.595 70.895  -3.047  1.00 16.83 ? 730  LEU A CB  1 
ATOM   5844 C  CG  . LEU A 1 730  ? 18.001 69.845  -2.002  1.00 17.36 ? 730  LEU A CG  1 
ATOM   5845 C  CD1 . LEU A 1 730  ? 17.946 70.410  -0.600  1.00 16.33 ? 730  LEU A CD1 1 
ATOM   5846 C  CD2 . LEU A 1 730  ? 17.055 68.628  -2.149  1.00 20.60 ? 730  LEU A CD2 1 
ATOM   5847 N  N   . PRO A 1 731  ? 17.421 71.257  -6.762  1.00 15.92 ? 731  PRO A N   1 
ATOM   5848 C  CA  . PRO A 1 731  ? 16.916 72.213  -7.771  1.00 16.25 ? 731  PRO A CA  1 
ATOM   5849 C  C   . PRO A 1 731  ? 15.447 72.523  -7.642  1.00 18.07 ? 731  PRO A C   1 
ATOM   5850 O  O   . PRO A 1 731  ? 14.665 71.702  -7.164  1.00 18.21 ? 731  PRO A O   1 
ATOM   5851 C  CB  . PRO A 1 731  ? 17.233 71.533  -9.097  1.00 16.23 ? 731  PRO A CB  1 
ATOM   5852 C  CG  . PRO A 1 731  ? 17.150 70.016  -8.738  1.00 15.82 ? 731  PRO A CG  1 
ATOM   5853 C  CD  . PRO A 1 731  ? 17.799 69.964  -7.376  1.00 15.36 ? 731  PRO A CD  1 
ATOM   5854 N  N   . ASN A 1 732  ? 15.066 73.709  -8.108  1.00 19.59 ? 732  ASN A N   1 
ATOM   5855 C  CA  . ASN A 1 732  ? 13.656 74.102  -8.093  1.00 21.89 ? 732  ASN A CA  1 
ATOM   5856 C  C   . ASN A 1 732  ? 13.123 73.795  -9.488  1.00 20.55 ? 732  ASN A C   1 
ATOM   5857 O  O   . ASN A 1 732  ? 12.613 74.673  -10.198 1.00 24.10 ? 732  ASN A O   1 
ATOM   5858 C  CB  . ASN A 1 732  ? 13.519 75.589  -7.760  1.00 23.85 ? 732  ASN A CB  1 
ATOM   5859 C  CG  . ASN A 1 732  ? 14.200 76.484  -8.776  1.00 27.16 ? 732  ASN A CG  1 
ATOM   5860 O  OD1 . ASN A 1 732  ? 15.198 76.114  -9.390  1.00 28.45 ? 732  ASN A OD1 1 
ATOM   5861 N  ND2 . ASN A 1 732  ? 13.650 77.696  -8.962  1.00 30.50 ? 732  ASN A ND2 1 
ATOM   5862 N  N   . GLY A 1 733  ? 13.263 72.537  -9.893  1.00 18.74 ? 733  GLY A N   1 
ATOM   5863 C  CA  . GLY A 1 733  ? 12.782 72.083  -11.182 1.00 20.25 ? 733  GLY A CA  1 
ATOM   5864 C  C   . GLY A 1 733  ? 13.880 71.988  -12.232 1.00 18.97 ? 733  GLY A C   1 
ATOM   5865 O  O   . GLY A 1 733  ? 15.056 72.325  -11.967 1.00 19.84 ? 733  GLY A O   1 
ATOM   5866 N  N   . PRO A 1 734  ? 13.520 71.536  -13.435 1.00 18.10 ? 734  PRO A N   1 
ATOM   5867 C  CA  . PRO A 1 734  ? 14.460 71.407  -14.552 1.00 17.76 ? 734  PRO A CA  1 
ATOM   5868 C  C   . PRO A 1 734  ? 15.082 72.765  -14.837 1.00 18.99 ? 734  PRO A C   1 
ATOM   5869 O  O   . PRO A 1 734  ? 14.488 73.827  -14.596 1.00 18.72 ? 734  PRO A O   1 
ATOM   5870 C  CB  . PRO A 1 734  ? 13.581 70.991  -15.734 1.00 21.03 ? 734  PRO A CB  1 
ATOM   5871 C  CG  . PRO A 1 734  ? 12.463 70.279  -15.079 1.00 23.49 ? 734  PRO A CG  1 
ATOM   5872 C  CD  . PRO A 1 734  ? 12.188 71.006  -13.798 1.00 20.41 ? 734  PRO A CD  1 
ATOM   5873 N  N   . ALA A 1 735  ? 16.255 72.701  -15.445 1.00 18.04 ? 735  ALA A N   1 
ATOM   5874 C  CA  . ALA A 1 735  ? 17.008 73.902  -15.761 1.00 18.25 ? 735  ALA A CA  1 
ATOM   5875 C  C   . ALA A 1 735  ? 16.302 74.730  -16.847 1.00 19.01 ? 735  ALA A C   1 
ATOM   5876 O  O   . ALA A 1 735  ? 15.587 74.194  -17.669 1.00 20.73 ? 735  ALA A O   1 
ATOM   5877 C  CB  . ALA A 1 735  ? 18.440 73.483  -16.225 1.00 16.93 ? 735  ALA A CB  1 
ATOM   5878 N  N   . SER A 1 736  ? 16.552 76.036  -16.832 1.00 19.45 ? 736  SER A N   1 
ATOM   5879 C  CA  . SER A 1 736  ? 15.978 76.975  -17.822 1.00 19.85 ? 736  SER A CA  1 
ATOM   5880 C  C   . SER A 1 736  ? 17.141 77.492  -18.660 1.00 19.85 ? 736  SER A C   1 
ATOM   5881 O  O   . SER A 1 736  ? 18.213 77.733  -18.136 1.00 19.91 ? 736  SER A O   1 
ATOM   5882 C  CB  . SER A 1 736  ? 15.351 78.163  -17.118 1.00 23.61 ? 736  SER A CB  1 
ATOM   5883 O  OG  . SER A 1 736  ? 14.483 77.723  -16.095 1.00 31.15 ? 736  SER A OG  1 
ATOM   5884 N  N   . PRO A 1 737  ? 16.938 77.701  -19.960 1.00 21.38 ? 737  PRO A N   1 
ATOM   5885 C  CA  . PRO A 1 737  ? 18.041 78.195  -20.812 1.00 24.35 ? 737  PRO A CA  1 
ATOM   5886 C  C   . PRO A 1 737  ? 18.601 79.526  -20.368 1.00 23.27 ? 737  PRO A C   1 
ATOM   5887 O  O   . PRO A 1 737  ? 17.869 80.371  -19.873 1.00 25.30 ? 737  PRO A O   1 
ATOM   5888 C  CB  . PRO A 1 737  ? 17.410 78.297  -22.210 1.00 25.09 ? 737  PRO A CB  1 
ATOM   5889 C  CG  . PRO A 1 737  ? 16.238 77.371  -22.151 1.00 25.63 ? 737  PRO A CG  1 
ATOM   5890 C  CD  . PRO A 1 737  ? 15.696 77.529  -20.734 1.00 25.34 ? 737  PRO A CD  1 
ATOM   5891 N  N   . VAL A 1 738  ? 19.922 79.686  -20.500 1.00 23.97 ? 738  VAL A N   1 
ATOM   5892 C  CA  . VAL A 1 738  ? 20.555 80.963  -20.150 1.00 22.02 ? 738  VAL A CA  1 
ATOM   5893 C  C   . VAL A 1 738  ? 20.149 81.877  -21.321 1.00 23.84 ? 738  VAL A C   1 
ATOM   5894 O  O   . VAL A 1 738  ? 20.220 81.461  -22.476 1.00 23.93 ? 738  VAL A O   1 
ATOM   5895 C  CB  . VAL A 1 738  ? 22.108 80.833  -20.104 1.00 22.16 ? 738  VAL A CB  1 
ATOM   5896 C  CG1 . VAL A 1 738  ? 22.744 82.235  -20.032 1.00 23.13 ? 738  VAL A CG1 1 
ATOM   5897 C  CG2 . VAL A 1 738  ? 22.567 79.991  -18.871 1.00 22.74 ? 738  VAL A CG2 1 
ATOM   5898 N  N   . GLU A 1 739  ? 19.726 83.107  -21.049 1.00 24.61 ? 739  GLU A N   1 
ATOM   5899 C  CA  . GLU A 1 739  ? 19.361 83.994  -22.158 1.00 26.47 ? 739  GLU A CA  1 
ATOM   5900 C  C   . GLU A 1 739  ? 20.674 84.528  -22.701 1.00 24.10 ? 739  GLU A C   1 
ATOM   5901 O  O   . GLU A 1 739  ? 21.440 85.176  -21.987 1.00 24.63 ? 739  GLU A O   1 
ATOM   5902 C  CB  . GLU A 1 739  ? 18.482 85.135  -21.678 1.00 29.65 ? 739  GLU A CB  1 
ATOM   5903 C  CG  . GLU A 1 739  ? 17.067 84.703  -21.388 1.00 38.90 ? 739  GLU A CG  1 
ATOM   5904 C  CD  . GLU A 1 739  ? 16.205 85.872  -20.949 1.00 44.39 ? 739  GLU A CD  1 
ATOM   5905 O  OE1 . GLU A 1 739  ? 16.331 86.961  -21.558 1.00 45.60 ? 739  GLU A OE1 1 
ATOM   5906 O  OE2 . GLU A 1 739  ? 15.401 85.696  -19.999 1.00 48.93 ? 739  GLU A OE2 1 
ATOM   5907 N  N   . LEU A 1 740  ? 20.917 84.243  -23.970 1.00 24.33 ? 740  LEU A N   1 
ATOM   5908 C  CA  . LEU A 1 740  ? 22.191 84.597  -24.581 1.00 23.98 ? 740  LEU A CA  1 
ATOM   5909 C  C   . LEU A 1 740  ? 22.344 85.957  -25.200 1.00 26.00 ? 740  LEU A C   1 
ATOM   5910 O  O   . LEU A 1 740  ? 23.468 86.396  -25.356 1.00 26.01 ? 740  LEU A O   1 
ATOM   5911 C  CB  . LEU A 1 740  ? 22.554 83.560  -25.620 1.00 25.61 ? 740  LEU A CB  1 
ATOM   5912 C  CG  . LEU A 1 740  ? 22.523 82.105  -25.171 1.00 23.86 ? 740  LEU A CG  1 
ATOM   5913 C  CD1 . LEU A 1 740  ? 23.041 81.255  -26.303 1.00 21.22 ? 740  LEU A CD1 1 
ATOM   5914 C  CD2 . LEU A 1 740  ? 23.411 81.916  -23.910 1.00 23.25 ? 740  LEU A CD2 1 
ATOM   5915 N  N   . GLY A 1 741  ? 21.230 86.612  -25.542 1.00 26.39 ? 741  GLY A N   1 
ATOM   5916 C  CA  . GLY A 1 741  ? 21.328 87.921  -26.180 1.00 26.57 ? 741  GLY A CA  1 
ATOM   5917 C  C   . GLY A 1 741  ? 21.932 87.706  -27.567 1.00 24.95 ? 741  GLY A C   1 
ATOM   5918 O  O   . GLY A 1 741  ? 21.651 86.707  -28.219 1.00 26.42 ? 741  GLY A O   1 
ATOM   5919 N  N   . GLN A 1 742  ? 22.750 88.637  -28.037 1.00 26.43 ? 742  GLN A N   1 
ATOM   5920 C  CA  . GLN A 1 742  ? 23.398 88.443  -29.345 1.00 27.69 ? 742  GLN A CA  1 
ATOM   5921 C  C   . GLN A 1 742  ? 24.902 88.429  -29.012 1.00 25.41 ? 742  GLN A C   1 
ATOM   5922 O  O   . GLN A 1 742  ? 25.596 89.429  -29.109 1.00 26.34 ? 742  GLN A O   1 
ATOM   5923 C  CB  . GLN A 1 742  ? 23.048 89.599  -30.289 1.00 32.33 ? 742  GLN A CB  1 
ATOM   5924 C  CG  . GLN A 1 742  ? 23.477 89.370  -31.737 1.00 39.71 ? 742  GLN A CG  1 
ATOM   5925 C  CD  . GLN A 1 742  ? 22.762 90.307  -32.734 1.00 44.92 ? 742  GLN A CD  1 
ATOM   5926 O  OE1 . GLN A 1 742  ? 22.931 90.172  -33.950 1.00 46.15 ? 742  GLN A OE1 1 
ATOM   5927 N  NE2 . GLN A 1 742  ? 21.956 91.255  -32.215 1.00 47.02 ? 742  GLN A NE2 1 
ATOM   5928 N  N   . PRO A 1 743  ? 25.423 87.262  -28.623 1.00 22.95 ? 743  PRO A N   1 
ATOM   5929 C  CA  . PRO A 1 743  ? 26.844 87.215  -28.268 1.00 22.16 ? 743  PRO A CA  1 
ATOM   5930 C  C   . PRO A 1 743  ? 27.886 87.433  -29.364 1.00 20.64 ? 743  PRO A C   1 
ATOM   5931 O  O   . PRO A 1 743  ? 27.659 87.182  -30.562 1.00 23.22 ? 743  PRO A O   1 
ATOM   5932 C  CB  . PRO A 1 743  ? 26.979 85.842  -27.599 1.00 20.49 ? 743  PRO A CB  1 
ATOM   5933 C  CG  . PRO A 1 743  ? 26.014 85.006  -28.311 1.00 20.52 ? 743  PRO A CG  1 
ATOM   5934 C  CD  . PRO A 1 743  ? 24.826 85.913  -28.696 1.00 20.59 ? 743  PRO A CD  1 
ATOM   5935 N  N   . VAL A 1 744  ? 29.053 87.914  -28.943 1.00 18.01 ? 744  VAL A N   1 
ATOM   5936 C  CA  . VAL A 1 744  ? 30.140 88.118  -29.901 1.00 17.70 ? 744  VAL A CA  1 
ATOM   5937 C  C   . VAL A 1 744  ? 30.859 86.780  -30.136 1.00 18.43 ? 744  VAL A C   1 
ATOM   5938 O  O   . VAL A 1 744  ? 31.220 86.084  -29.173 1.00 19.07 ? 744  VAL A O   1 
ATOM   5939 C  CB  . VAL A 1 744  ? 31.118 89.152  -29.358 1.00 16.42 ? 744  VAL A CB  1 
ATOM   5940 C  CG1 . VAL A 1 744  ? 32.274 89.307  -30.302 1.00 17.19 ? 744  VAL A CG1 1 
ATOM   5941 C  CG2 . VAL A 1 744  ? 30.382 90.525  -29.148 1.00 19.60 ? 744  VAL A CG2 1 
ATOM   5942 N  N   . VAL A 1 745  ? 31.036 86.410  -31.391 1.00 17.49 ? 745  VAL A N   1 
ATOM   5943 C  CA  . VAL A 1 745  ? 31.668 85.165  -31.779 1.00 15.90 ? 745  VAL A CA  1 
ATOM   5944 C  C   . VAL A 1 745  ? 32.960 85.394  -32.535 1.00 17.34 ? 745  VAL A C   1 
ATOM   5945 O  O   . VAL A 1 745  ? 33.005 86.166  -33.485 1.00 17.23 ? 745  VAL A O   1 
ATOM   5946 C  CB  . VAL A 1 745  ? 30.704 84.310  -32.663 1.00 15.54 ? 745  VAL A CB  1 
ATOM   5947 C  CG1 . VAL A 1 745  ? 31.398 82.977  -33.078 1.00 17.20 ? 745  VAL A CG1 1 
ATOM   5948 C  CG2 . VAL A 1 745  ? 29.423 84.070  -31.914 1.00 15.88 ? 745  VAL A CG2 1 
ATOM   5949 N  N   . LEU A 1 746  ? 34.040 84.727  -32.140 1.00 15.05 ? 746  LEU A N   1 
ATOM   5950 C  CA  . LEU A 1 746  ? 35.341 84.853  -32.768 1.00 13.87 ? 746  LEU A CA  1 
ATOM   5951 C  C   . LEU A 1 746  ? 35.774 83.553  -33.412 1.00 14.92 ? 746  LEU A C   1 
ATOM   5952 O  O   . LEU A 1 746  ? 35.862 82.514  -32.725 1.00 15.20 ? 746  LEU A O   1 
ATOM   5953 C  CB  . LEU A 1 746  ? 36.377 85.274  -31.725 1.00 15.89 ? 746  LEU A CB  1 
ATOM   5954 C  CG  . LEU A 1 746  ? 37.833 85.252  -32.199 1.00 17.43 ? 746  LEU A CG  1 
ATOM   5955 C  CD1 . LEU A 1 746  ? 38.068 86.326  -33.220 1.00 19.26 ? 746  LEU A CD1 1 
ATOM   5956 C  CD2 . LEU A 1 746  ? 38.750 85.479  -30.988 1.00 19.79 ? 746  LEU A CD2 1 
ATOM   5957 N  N   . VAL A 1 747  ? 36.099 83.577  -34.701 1.00 15.35 ? 747  VAL A N   1 
ATOM   5958 C  CA  . VAL A 1 747  ? 36.480 82.384  -35.417 1.00 14.57 ? 747  VAL A CA  1 
ATOM   5959 C  C   . VAL A 1 747  ? 37.910 82.539  -35.848 1.00 17.20 ? 747  VAL A C   1 
ATOM   5960 O  O   . VAL A 1 747  ? 38.258 83.508  -36.521 1.00 17.91 ? 747  VAL A O   1 
ATOM   5961 C  CB  . VAL A 1 747  ? 35.562 82.170  -36.668 1.00 14.80 ? 747  VAL A CB  1 
ATOM   5962 C  CG1 . VAL A 1 747  ? 35.928 80.893  -37.344 1.00 16.56 ? 747  VAL A CG1 1 
ATOM   5963 C  CG2 . VAL A 1 747  ? 34.102 82.169  -36.265 1.00 16.34 ? 747  VAL A CG2 1 
ATOM   5964 N  N   . THR A 1 748  ? 38.780 81.613  -35.468 1.00 16.11 ? 748  THR A N   1 
ATOM   5965 C  CA  . THR A 1 748  ? 40.173 81.644  -35.884 1.00 16.39 ? 748  THR A CA  1 
ATOM   5966 C  C   . THR A 1 748  ? 40.366 80.400  -36.693 1.00 17.79 ? 748  THR A C   1 
ATOM   5967 O  O   . THR A 1 748  ? 40.056 79.304  -36.220 1.00 17.89 ? 748  THR A O   1 
ATOM   5968 C  CB  . THR A 1 748  ? 41.116 81.664  -34.647 1.00 18.49 ? 748  THR A CB  1 
ATOM   5969 O  OG1 . THR A 1 748  ? 40.871 82.857  -33.893 1.00 19.60 ? 748  THR A OG1 1 
ATOM   5970 C  CG2 . THR A 1 748  ? 42.609 81.606  -35.079 1.00 19.33 ? 748  THR A CG2 1 
ATOM   5971 N  N   . LYS A 1 749  ? 40.858 80.537  -37.925 1.00 16.64 ? 749  LYS A N   1 
ATOM   5972 C  CA  . LYS A 1 749  ? 41.019 79.398  -38.808 1.00 18.07 ? 749  LYS A CA  1 
ATOM   5973 C  C   . LYS A 1 749  ? 42.447 79.268  -39.248 1.00 17.90 ? 749  LYS A C   1 
ATOM   5974 O  O   . LYS A 1 749  ? 43.050 80.195  -39.841 1.00 17.75 ? 749  LYS A O   1 
ATOM   5975 C  CB  . LYS A 1 749  ? 40.110 79.576  -40.029 1.00 18.18 ? 749  LYS A CB  1 
ATOM   5976 C  CG  . LYS A 1 749  ? 40.251 78.451  -41.042 1.00 23.20 ? 749  LYS A CG  1 
ATOM   5977 C  CD  . LYS A 1 749  ? 39.333 78.756  -42.238 1.00 27.18 ? 749  LYS A CD  1 
ATOM   5978 C  CE  . LYS A 1 749  ? 39.590 77.783  -43.366 1.00 33.08 ? 749  LYS A CE  1 
ATOM   5979 N  NZ  . LYS A 1 749  ? 39.120 78.421  -44.642 1.00 38.17 ? 749  LYS A NZ  1 
ATOM   5980 N  N   . GLY A 1 750  ? 43.028 78.143  -38.885 1.00 16.39 ? 750  GLY A N   1 
ATOM   5981 C  CA  . GLY A 1 750  ? 44.405 77.880  -39.233 1.00 17.95 ? 750  GLY A CA  1 
ATOM   5982 C  C   . GLY A 1 750  ? 44.576 76.498  -39.792 1.00 18.44 ? 750  GLY A C   1 
ATOM   5983 O  O   . GLY A 1 750  ? 43.670 75.645  -39.692 1.00 19.55 ? 750  GLY A O   1 
ATOM   5984 N  N   . LYS A 1 751  ? 45.749 76.282  -40.365 1.00 18.98 ? 751  LYS A N   1 
ATOM   5985 C  CA  . LYS A 1 751  ? 46.061 75.001  -40.938 1.00 20.36 ? 751  LYS A CA  1 
ATOM   5986 C  C   . LYS A 1 751  ? 46.191 73.900  -39.884 1.00 18.62 ? 751  LYS A C   1 
ATOM   5987 O  O   . LYS A 1 751  ? 45.807 72.756  -40.127 1.00 19.57 ? 751  LYS A O   1 
ATOM   5988 C  CB  . LYS A 1 751  ? 47.368 75.103  -41.716 1.00 23.54 ? 751  LYS A CB  1 
ATOM   5989 C  CG  . LYS A 1 751  ? 47.751 73.781  -42.332 1.00 34.34 ? 751  LYS A CG  1 
ATOM   5990 C  CD  . LYS A 1 751  ? 49.079 73.873  -43.093 1.00 41.06 ? 751  LYS A CD  1 
ATOM   5991 C  CE  . LYS A 1 751  ? 49.337 72.576  -43.843 1.00 44.27 ? 751  LYS A CE  1 
ATOM   5992 N  NZ  . LYS A 1 751  ? 48.214 72.321  -44.813 1.00 48.36 ? 751  LYS A NZ  1 
ATOM   5993 N  N   . LEU A 1 752  ? 46.763 74.245  -38.735 1.00 18.65 ? 752  LEU A N   1 
ATOM   5994 C  CA  . LEU A 1 752  ? 46.989 73.272  -37.656 1.00 17.04 ? 752  LEU A CA  1 
ATOM   5995 C  C   . LEU A 1 752  ? 45.913 73.314  -36.576 1.00 17.57 ? 752  LEU A C   1 
ATOM   5996 O  O   . LEU A 1 752  ? 45.605 72.276  -35.983 1.00 17.16 ? 752  LEU A O   1 
ATOM   5997 C  CB  . LEU A 1 752  ? 48.334 73.533  -36.974 1.00 17.33 ? 752  LEU A CB  1 
ATOM   5998 C  CG  . LEU A 1 752  ? 49.560 73.471  -37.911 1.00 19.14 ? 752  LEU A CG  1 
ATOM   5999 C  CD1 . LEU A 1 752  ? 50.833 73.591  -37.075 1.00 21.53 ? 752  LEU A CD1 1 
ATOM   6000 C  CD2 . LEU A 1 752  ? 49.561 72.186  -38.714 1.00 22.99 ? 752  LEU A CD2 1 
ATOM   6001 N  N   . GLU A 1 753  ? 45.331 74.493  -36.337 1.00 16.53 ? 753  GLU A N   1 
ATOM   6002 C  CA  . GLU A 1 753  ? 44.368 74.625  -35.270 1.00 16.07 ? 753  GLU A CA  1 
ATOM   6003 C  C   . GLU A 1 753  ? 43.371 75.726  -35.592 1.00 16.10 ? 753  GLU A C   1 
ATOM   6004 O  O   . GLU A 1 753  ? 43.795 76.837  -35.998 1.00 17.94 ? 753  GLU A O   1 
ATOM   6005 C  CB  . GLU A 1 753  ? 45.105 74.997  -33.971 1.00 15.22 ? 753  GLU A CB  1 
ATOM   6006 C  CG  . GLU A 1 753  ? 44.167 75.264  -32.785 1.00 18.41 ? 753  GLU A CG  1 
ATOM   6007 C  CD  . GLU A 1 753  ? 44.916 75.810  -31.538 1.00 21.44 ? 753  GLU A CD  1 
ATOM   6008 O  OE1 . GLU A 1 753  ? 45.256 77.025  -31.501 1.00 28.58 ? 753  GLU A OE1 1 
ATOM   6009 O  OE2 . GLU A 1 753  ? 45.157 74.999  -30.631 1.00 28.46 ? 753  GLU A OE2 1 
ATOM   6010 N  N   . SER A 1 754  ? 42.095 75.441  -35.399 1.00 14.22 ? 754  SER A N   1 
ATOM   6011 C  CA  . SER A 1 754  ? 41.045 76.426  -35.591 1.00 15.50 ? 754  SER A CA  1 
ATOM   6012 C  C   . SER A 1 754  ? 40.150 76.424  -34.375 1.00 15.60 ? 754  SER A C   1 
ATOM   6013 O  O   . SER A 1 754  ? 40.140 75.455  -33.566 1.00 16.61 ? 754  SER A O   1 
ATOM   6014 C  CB  . SER A 1 754  ? 40.211 76.072  -36.824 1.00 16.38 ? 754  SER A CB  1 
ATOM   6015 O  OG  . SER A 1 754  ? 41.000 76.127  -38.002 1.00 16.98 ? 754  SER A OG  1 
ATOM   6016 N  N   . SER A 1 755  ? 39.405 77.501  -34.202 1.00 14.43 ? 755  SER A N   1 
ATOM   6017 C  CA  . SER A 1 755  ? 38.520 77.570  -33.060 1.00 15.45 ? 755  SER A CA  1 
ATOM   6018 C  C   . SER A 1 755  ? 37.345 78.505  -33.239 1.00 15.54 ? 755  SER A C   1 
ATOM   6019 O  O   . SER A 1 755  ? 37.372 79.383  -34.099 1.00 15.74 ? 755  SER A O   1 
ATOM   6020 C  CB  A SER A 1 755  ? 39.324 78.007  -31.832 0.50 16.41 ? 755  SER A CB  1 
ATOM   6021 C  CB  B SER A 1 755  ? 39.242 77.772  -31.742 0.50 18.61 ? 755  SER A CB  1 
ATOM   6022 O  OG  A SER A 1 755  ? 39.989 79.241  -32.052 0.50 17.17 ? 755  SER A OG  1 
ATOM   6023 O  OG  B SER A 1 755  ? 39.537 79.145  -31.605 0.50 20.24 ? 755  SER A OG  1 
ATOM   6024 N  N   . VAL A 1 756  ? 36.302 78.303  -32.447 1.00 13.91 ? 756  VAL A N   1 
ATOM   6025 C  CA  . VAL A 1 756  ? 35.160 79.183  -32.424 1.00 13.53 ? 756  VAL A CA  1 
ATOM   6026 C  C   . VAL A 1 756  ? 35.002 79.506  -30.933 1.00 14.24 ? 756  VAL A C   1 
ATOM   6027 O  O   . VAL A 1 756  ? 34.806 78.586  -30.087 1.00 15.80 ? 756  VAL A O   1 
ATOM   6028 C  CB  . VAL A 1 756  ? 33.867 78.533  -32.951 1.00 14.38 ? 756  VAL A CB  1 
ATOM   6029 C  CG1 . VAL A 1 756  ? 32.655 79.508  -32.693 1.00 16.27 ? 756  VAL A CG1 1 
ATOM   6030 C  CG2 . VAL A 1 756  ? 34.060 78.171  -34.441 1.00 17.12 ? 756  VAL A CG2 1 
ATOM   6031 N  N   . SER A 1 757  ? 35.063 80.783  -30.589 1.00 13.92 ? 757  SER A N   1 
ATOM   6032 C  CA  . SER A 1 757  ? 34.927 81.202  -29.198 1.00 14.19 ? 757  SER A CA  1 
ATOM   6033 C  C   . SER A 1 757  ? 33.772 82.162  -29.078 1.00 15.29 ? 757  SER A C   1 
ATOM   6034 O  O   . SER A 1 757  ? 33.592 82.993  -29.968 1.00 17.76 ? 757  SER A O   1 
ATOM   6035 C  CB  . SER A 1 757  ? 36.224 81.905  -28.709 1.00 15.68 ? 757  SER A CB  1 
ATOM   6036 O  OG  . SER A 1 757  ? 37.312 81.010  -28.893 1.00 19.96 ? 757  SER A OG  1 
ATOM   6037 N  N   . VAL A 1 758  ? 33.006 82.112  -27.999 1.00 14.03 ? 758  VAL A N   1 
ATOM   6038 C  CA  . VAL A 1 758  ? 31.877 83.018  -27.840 1.00 16.27 ? 758  VAL A CA  1 
ATOM   6039 C  C   . VAL A 1 758  ? 31.745 83.452  -26.403 1.00 15.81 ? 758  VAL A C   1 
ATOM   6040 O  O   . VAL A 1 758  ? 31.945 82.669  -25.474 1.00 15.96 ? 758  VAL A O   1 
ATOM   6041 C  CB  . VAL A 1 758  ? 30.557 82.386  -28.373 1.00 16.70 ? 758  VAL A CB  1 
ATOM   6042 C  CG1 . VAL A 1 758  ? 30.277 81.050  -27.677 1.00 17.89 ? 758  VAL A CG1 1 
ATOM   6043 C  CG2 . VAL A 1 758  ? 29.400 83.350  -28.148 1.00 17.51 ? 758  VAL A CG2 1 
ATOM   6044 N  N   . GLY A 1 759  ? 31.448 84.727  -26.213 1.00 16.03 ? 759  GLY A N   1 
ATOM   6045 C  CA  . GLY A 1 759  ? 31.328 85.314  -24.890 1.00 17.04 ? 759  GLY A CA  1 
ATOM   6046 C  C   . GLY A 1 759  ? 29.891 85.283  -24.420 1.00 18.43 ? 759  GLY A C   1 
ATOM   6047 O  O   . GLY A 1 759  ? 29.085 86.159  -24.739 1.00 18.28 ? 759  GLY A O   1 
ATOM   6048 N  N   . LEU A 1 760  ? 29.534 84.244  -23.678 1.00 17.39 ? 760  LEU A N   1 
ATOM   6049 C  CA  . LEU A 1 760  ? 28.174 84.109  -23.177 1.00 17.96 ? 760  LEU A CA  1 
ATOM   6050 C  C   . LEU A 1 760  ? 28.084 84.602  -21.765 1.00 17.02 ? 760  LEU A C   1 
ATOM   6051 O  O   . LEU A 1 760  ? 29.102 84.770  -21.095 1.00 20.23 ? 760  LEU A O   1 
ATOM   6052 C  CB  . LEU A 1 760  ? 27.788 82.622  -23.164 1.00 16.55 ? 760  LEU A CB  1 
ATOM   6053 C  CG  . LEU A 1 760  ? 28.003 81.928  -24.501 1.00 17.98 ? 760  LEU A CG  1 
ATOM   6054 C  CD1 . LEU A 1 760  ? 27.655 80.418  -24.396 1.00 21.38 ? 760  LEU A CD1 1 
ATOM   6055 C  CD2 . LEU A 1 760  ? 27.075 82.579  -25.554 1.00 19.98 ? 760  LEU A CD2 1 
ATOM   6056 N  N   . PRO A 1 761  ? 26.864 84.828  -21.255 1.00 20.44 ? 761  PRO A N   1 
ATOM   6057 C  CA  . PRO A 1 761  ? 26.815 85.292  -19.857 1.00 20.24 ? 761  PRO A CA  1 
ATOM   6058 C  C   . PRO A 1 761  ? 27.391 84.172  -18.954 1.00 20.54 ? 761  PRO A C   1 
ATOM   6059 O  O   . PRO A 1 761  ? 26.941 83.008  -19.010 1.00 19.93 ? 761  PRO A O   1 
ATOM   6060 C  CB  . PRO A 1 761  ? 25.311 85.526  -19.611 1.00 22.83 ? 761  PRO A CB  1 
ATOM   6061 C  CG  . PRO A 1 761  ? 24.822 85.883  -21.001 1.00 21.92 ? 761  PRO A CG  1 
ATOM   6062 C  CD  . PRO A 1 761  ? 25.552 84.925  -21.915 1.00 20.95 ? 761  PRO A CD  1 
ATOM   6063 N  N   . SER A 1 762  ? 28.376 84.564  -18.139 1.00 19.81 ? 762  SER A N   1 
ATOM   6064 C  CA  . SER A 1 762  ? 29.084 83.689  -17.210 1.00 18.10 ? 762  SER A CA  1 
ATOM   6065 C  C   . SER A 1 762  ? 30.028 82.684  -17.836 1.00 16.76 ? 762  SER A C   1 
ATOM   6066 O  O   . SER A 1 762  ? 30.714 81.991  -17.105 1.00 16.63 ? 762  SER A O   1 
ATOM   6067 C  CB  . SER A 1 762  ? 28.107 82.888  -16.354 1.00 18.71 ? 762  SER A CB  1 
ATOM   6068 O  OG  . SER A 1 762  ? 27.271 83.703  -15.539 1.00 21.74 ? 762  SER A OG  1 
ATOM   6069 N  N   . VAL A 1 763  ? 30.108 82.610  -19.156 1.00 15.62 ? 763  VAL A N   1 
ATOM   6070 C  CA  . VAL A 1 763  ? 30.973 81.610  -19.774 1.00 14.05 ? 763  VAL A CA  1 
ATOM   6071 C  C   . VAL A 1 763  ? 31.576 82.018  -21.089 1.00 17.88 ? 763  VAL A C   1 
ATOM   6072 O  O   . VAL A 1 763  ? 30.847 82.389  -21.974 1.00 17.16 ? 763  VAL A O   1 
ATOM   6073 C  CB  . VAL A 1 763  ? 30.199 80.282  -20.075 1.00 17.00 ? 763  VAL A CB  1 
ATOM   6074 C  CG1 . VAL A 1 763  ? 31.174 79.215  -20.613 1.00 17.94 ? 763  VAL A CG1 1 
ATOM   6075 C  CG2 . VAL A 1 763  ? 29.484 79.758  -18.835 1.00 20.38 ? 763  VAL A CG2 1 
ATOM   6076 N  N   . VAL A 1 764  ? 32.889 82.014  -21.199 1.00 13.55 ? 764  VAL A N   1 
ATOM   6077 C  CA  . VAL A 1 764  ? 33.499 82.195  -22.503 1.00 13.82 ? 764  VAL A CA  1 
ATOM   6078 C  C   . VAL A 1 764  ? 33.652 80.735  -22.950 1.00 13.75 ? 764  VAL A C   1 
ATOM   6079 O  O   . VAL A 1 764  ? 34.466 79.971  -22.374 1.00 13.77 ? 764  VAL A O   1 
ATOM   6080 C  CB  . VAL A 1 764  ? 34.867 82.903  -22.478 1.00 15.24 ? 764  VAL A CB  1 
ATOM   6081 C  CG1 . VAL A 1 764  ? 35.407 82.947  -23.945 1.00 15.68 ? 764  VAL A CG1 1 
ATOM   6082 C  CG2 . VAL A 1 764  ? 34.709 84.331  -21.908 1.00 17.26 ? 764  VAL A CG2 1 
ATOM   6083 N  N   . HIS A 1 765  ? 32.883 80.334  -23.971 1.00 13.78 ? 765  HIS A N   1 
ATOM   6084 C  CA  . HIS A 1 765  ? 32.829 78.954  -24.473 1.00 12.94 ? 765  HIS A CA  1 
ATOM   6085 C  C   . HIS A 1 765  ? 33.674 78.868  -25.740 1.00 16.27 ? 765  HIS A C   1 
ATOM   6086 O  O   . HIS A 1 765  ? 33.516 79.688  -26.643 1.00 15.44 ? 765  HIS A O   1 
ATOM   6087 C  CB  . HIS A 1 765  ? 31.353 78.621  -24.757 1.00 14.04 ? 765  HIS A CB  1 
ATOM   6088 C  CG  . HIS A 1 765  ? 31.123 77.262  -25.298 1.00 13.63 ? 765  HIS A CG  1 
ATOM   6089 N  ND1 . HIS A 1 765  ? 30.609 77.006  -26.556 1.00 17.09 ? 765  HIS A ND1 1 
ATOM   6090 C  CD2 . HIS A 1 765  ? 31.322 76.059  -24.717 1.00 10.63 ? 765  HIS A CD2 1 
ATOM   6091 C  CE1 . HIS A 1 765  ? 30.505 75.701  -26.735 1.00 13.10 ? 765  HIS A CE1 1 
ATOM   6092 N  NE2 . HIS A 1 765  ? 30.938 75.099  -25.629 1.00 16.75 ? 765  HIS A NE2 1 
ATOM   6093 N  N   . GLN A 1 766  ? 34.548 77.879  -25.818 1.00 13.63 ? 766  GLN A N   1 
ATOM   6094 C  CA  . GLN A 1 766  ? 35.459 77.715  -26.941 1.00 14.44 ? 766  GLN A CA  1 
ATOM   6095 C  C   . GLN A 1 766  ? 35.484 76.278  -27.443 1.00 14.09 ? 766  GLN A C   1 
ATOM   6096 O  O   . GLN A 1 766  ? 35.572 75.334  -26.640 1.00 14.68 ? 766  GLN A O   1 
ATOM   6097 C  CB  . GLN A 1 766  ? 36.887 78.110  -26.502 1.00 15.97 ? 766  GLN A CB  1 
ATOM   6098 C  CG  A GLN A 1 766  ? 36.981 79.421  -25.694 0.50 16.83 ? 766  GLN A CG  1 
ATOM   6099 C  CG  B GLN A 1 766  ? 37.868 78.066  -27.754 0.50 14.11 ? 766  GLN A CG  1 
ATOM   6100 C  CD  A GLN A 1 766  ? 38.030 79.372  -24.547 0.50 21.74 ? 766  GLN A CD  1 
ATOM   6101 C  CD  B GLN A 1 766  ? 39.252 78.610  -27.399 0.50 18.05 ? 766  GLN A CD  1 
ATOM   6102 O  OE1 A GLN A 1 766  ? 39.207 79.096  -24.791 0.50 19.94 ? 766  GLN A OE1 1 
ATOM   6103 O  OE1 B GLN A 1 766  ? 40.040 78.988  -28.287 0.50 18.13 ? 766  GLN A OE1 1 
ATOM   6104 N  NE2 A GLN A 1 766  ? 37.591 79.637  -23.295 0.50 18.94 ? 766  GLN A NE2 1 
ATOM   6105 N  NE2 B GLN A 1 766  ? 39.555 78.649  -26.100 0.50 17.26 ? 766  GLN A NE2 1 
ATOM   6106 N  N   . THR A 1 767  ? 35.408 76.099  -28.761 1.00 13.57 ? 767  THR A N   1 
ATOM   6107 C  CA  . THR A 1 767  ? 35.504 74.807  -29.375 1.00 13.36 ? 767  THR A CA  1 
ATOM   6108 C  C   . THR A 1 767  ? 36.768 74.886  -30.210 1.00 15.15 ? 767  THR A C   1 
ATOM   6109 O  O   . THR A 1 767  ? 36.870 75.744  -31.113 1.00 14.96 ? 767  THR A O   1 
ATOM   6110 C  CB  . THR A 1 767  ? 34.328 74.534  -30.290 1.00 13.33 ? 767  THR A CB  1 
ATOM   6111 O  OG1 . THR A 1 767  ? 33.133 74.638  -29.518 1.00 16.31 ? 767  THR A OG1 1 
ATOM   6112 C  CG2 . THR A 1 767  ? 34.444 73.119  -30.894 1.00 14.55 ? 767  THR A CG2 1 
ATOM   6113 N  N   . ILE A 1 768  ? 37.730 74.017  -29.943 1.00 15.03 ? 768  ILE A N   1 
ATOM   6114 C  CA  . ILE A 1 768  ? 39.015 73.976  -30.634 1.00 13.71 ? 768  ILE A CA  1 
ATOM   6115 C  C   . ILE A 1 768  ? 39.156 72.713  -31.450 1.00 15.01 ? 768  ILE A C   1 
ATOM   6116 O  O   . ILE A 1 768  ? 38.820 71.620  -30.987 1.00 16.38 ? 768  ILE A O   1 
ATOM   6117 C  CB  . ILE A 1 768  ? 40.184 74.075  -29.625 1.00 12.55 ? 768  ILE A CB  1 
ATOM   6118 C  CG1 . ILE A 1 768  ? 39.964 75.292  -28.777 1.00 15.31 ? 768  ILE A CG1 1 
ATOM   6119 C  CG2 . ILE A 1 768  ? 41.529 74.140  -30.352 1.00 16.56 ? 768  ILE A CG2 1 
ATOM   6120 C  CD1 . ILE A 1 768  ? 40.767 75.274  -27.476 1.00 18.75 ? 768  ILE A CD1 1 
ATOM   6121 N  N   . MET A 1 769  ? 39.698 72.872  -32.652 1.00 15.42 ? 769  MET A N   1 
ATOM   6122 C  CA  . MET A 1 769  ? 39.862 71.765  -33.574 1.00 17.04 ? 769  MET A CA  1 
ATOM   6123 C  C   . MET A 1 769  ? 41.289 71.638  -34.007 1.00 17.91 ? 769  MET A C   1 
ATOM   6124 O  O   . MET A 1 769  ? 41.906 72.610  -34.461 1.00 16.96 ? 769  MET A O   1 
ATOM   6125 C  CB  . MET A 1 769  ? 38.985 72.002  -34.796 1.00 18.56 ? 769  MET A CB  1 
ATOM   6126 C  CG  A MET A 1 769  ? 37.539 72.121  -34.438 0.50 17.62 ? 769  MET A CG  1 
ATOM   6127 C  CG  B MET A 1 769  ? 37.333 71.878  -34.485 0.50 19.95 ? 769  MET A CG  1 
ATOM   6128 S  SD  A MET A 1 769  ? 36.582 72.545  -35.889 0.50 18.84 ? 769  MET A SD  1 
ATOM   6129 S  SD  B MET A 1 769  ? 36.333 72.884  -35.643 0.50 20.79 ? 769  MET A SD  1 
ATOM   6130 C  CE  A MET A 1 769  ? 36.898 71.154  -36.933 0.50 16.19 ? 769  MET A CE  1 
ATOM   6131 C  CE  B MET A 1 769  ? 36.546 74.503  -34.865 0.50 21.99 ? 769  MET A CE  1 
ATOM   6132 N  N   . ARG A 1 770  ? 41.836 70.444  -33.831 1.00 16.93 ? 770  ARG A N   1 
ATOM   6133 C  CA  . ARG A 1 770  ? 43.198 70.206  -34.224 1.00 18.49 ? 770  ARG A CA  1 
ATOM   6134 C  C   . ARG A 1 770  ? 43.285 69.033  -35.197 1.00 20.79 ? 770  ARG A C   1 
ATOM   6135 O  O   . ARG A 1 770  ? 44.380 68.523  -35.443 1.00 21.91 ? 770  ARG A O   1 
ATOM   6136 C  CB  . ARG A 1 770  ? 44.072 70.002  -32.976 1.00 20.10 ? 770  ARG A CB  1 
ATOM   6137 C  CG  A ARG A 1 770  ? 43.858 71.077  -31.891 0.50 20.56 ? 770  ARG A CG  1 
ATOM   6138 C  CG  B ARG A 1 770  ? 44.423 71.045  -32.249 0.50 19.05 ? 770  ARG A CG  1 
ATOM   6139 C  CD  A ARG A 1 770  ? 44.956 71.087  -30.799 0.50 18.76 ? 770  ARG A CD  1 
ATOM   6140 C  CD  B ARG A 1 770  ? 45.312 70.568  -31.113 0.50 19.38 ? 770  ARG A CD  1 
ATOM   6141 N  NE  A ARG A 1 770  ? 44.768 72.128  -29.783 0.50 21.13 ? 770  ARG A NE  1 
ATOM   6142 N  NE  B ARG A 1 770  ? 44.626 69.526  -30.354 0.50 21.01 ? 770  ARG A NE  1 
ATOM   6143 C  CZ  A ARG A 1 770  ? 44.040 71.992  -28.676 0.50 19.09 ? 770  ARG A CZ  1 
ATOM   6144 C  CZ  B ARG A 1 770  ? 43.801 69.765  -29.340 0.50 21.02 ? 770  ARG A CZ  1 
ATOM   6145 N  NH1 A ARG A 1 770  ? 43.417 70.852  -28.420 0.50 21.53 ? 770  ARG A NH1 1 
ATOM   6146 N  NH1 B ARG A 1 770  ? 43.562 71.012  -28.946 0.50 22.42 ? 770  ARG A NH1 1 
ATOM   6147 N  NH2 A ARG A 1 770  ? 43.933 72.997  -27.820 0.50 19.45 ? 770  ARG A NH2 1 
ATOM   6148 N  NH2 B ARG A 1 770  ? 43.198 68.753  -28.735 0.50 19.87 ? 770  ARG A NH2 1 
ATOM   6149 N  N   . GLY A 1 771  ? 42.133 68.605  -35.727 1.00 19.17 ? 771  GLY A N   1 
ATOM   6150 C  CA  . GLY A 1 771  ? 42.130 67.530  -36.701 1.00 22.57 ? 771  GLY A CA  1 
ATOM   6151 C  C   . GLY A 1 771  ? 41.479 66.243  -36.280 1.00 25.27 ? 771  GLY A C   1 
ATOM   6152 O  O   . GLY A 1 771  ? 41.302 65.344  -37.129 1.00 26.93 ? 771  GLY A O   1 
ATOM   6153 N  N   . GLY A 1 772  ? 41.156 66.145  -34.987 1.00 24.01 ? 772  GLY A N   1 
ATOM   6154 C  CA  . GLY A 1 772  ? 40.490 64.966  -34.428 1.00 23.68 ? 772  GLY A CA  1 
ATOM   6155 C  C   . GLY A 1 772  ? 39.316 65.399  -33.556 1.00 21.34 ? 772  GLY A C   1 
ATOM   6156 O  O   . GLY A 1 772  ? 38.609 66.347  -33.888 1.00 21.76 ? 772  GLY A O   1 
ATOM   6157 N  N   . ALA A 1 773  ? 39.077 64.706  -32.440 1.00 18.97 ? 773  ALA A N   1 
ATOM   6158 C  CA  . ALA A 1 773  ? 37.975 65.076  -31.566 1.00 17.51 ? 773  ALA A CA  1 
ATOM   6159 C  C   . ALA A 1 773  ? 38.185 66.514  -31.087 1.00 15.41 ? 773  ALA A C   1 
ATOM   6160 O  O   . ALA A 1 773  ? 39.287 66.885  -30.663 1.00 17.12 ? 773  ALA A O   1 
ATOM   6161 C  CB  . ALA A 1 773  ? 37.914 64.137  -30.376 1.00 19.02 ? 773  ALA A CB  1 
ATOM   6162 N  N   . PRO A 1 774  ? 37.137 67.329  -31.130 1.00 16.16 ? 774  PRO A N   1 
ATOM   6163 C  CA  . PRO A 1 774  ? 37.358 68.697  -30.661 1.00 14.73 ? 774  PRO A CA  1 
ATOM   6164 C  C   . PRO A 1 774  ? 37.626 68.763  -29.170 1.00 14.80 ? 774  PRO A C   1 
ATOM   6165 O  O   . PRO A 1 774  ? 37.360 67.812  -28.419 1.00 14.30 ? 774  PRO A O   1 
ATOM   6166 C  CB  . PRO A 1 774  ? 36.059 69.430  -31.006 1.00 17.19 ? 774  PRO A CB  1 
ATOM   6167 C  CG  . PRO A 1 774  ? 35.039 68.354  -31.140 1.00 21.49 ? 774  PRO A CG  1 
ATOM   6168 C  CD  . PRO A 1 774  ? 35.796 67.152  -31.710 1.00 15.79 ? 774  PRO A CD  1 
ATOM   6169 N  N   . GLU A 1 775  ? 38.187 69.891  -28.801 1.00 14.17 ? 775  GLU A N   1 
ATOM   6170 C  CA  . GLU A 1 775  ? 38.457 70.237  -27.408 1.00 12.26 ? 775  GLU A CA  1 
ATOM   6171 C  C   . GLU A 1 775  ? 37.529 71.382  -27.049 1.00 13.59 ? 775  GLU A C   1 
ATOM   6172 O  O   . GLU A 1 775  ? 37.324 72.307  -27.859 1.00 15.48 ? 775  GLU A O   1 
ATOM   6173 C  CB  . GLU A 1 775  ? 39.884 70.674  -27.216 1.00 13.02 ? 775  GLU A CB  1 
ATOM   6174 C  CG  . GLU A 1 775  ? 40.192 71.107  -25.765 1.00 14.71 ? 775  GLU A CG  1 
ATOM   6175 C  CD  . GLU A 1 775  ? 41.659 71.326  -25.524 1.00 22.73 ? 775  GLU A CD  1 
ATOM   6176 O  OE1 . GLU A 1 775  ? 42.469 70.508  -25.999 1.00 26.13 ? 775  GLU A OE1 1 
ATOM   6177 O  OE2 . GLU A 1 775  ? 42.021 72.294  -24.833 1.00 25.28 ? 775  GLU A OE2 1 
ATOM   6178 N  N   . ILE A 1 776  ? 36.903 71.324  -25.896 1.00 12.54 ? 776  ILE A N   1 
ATOM   6179 C  CA  . ILE A 1 776  ? 36.021 72.376  -25.448 1.00 12.79 ? 776  ILE A CA  1 
ATOM   6180 C  C   . ILE A 1 776  ? 36.654 73.013  -24.228 1.00 13.99 ? 776  ILE A C   1 
ATOM   6181 O  O   . ILE A 1 776  ? 37.154 72.302  -23.336 1.00 14.29 ? 776  ILE A O   1 
ATOM   6182 C  CB  . ILE A 1 776  ? 34.636 71.838  -25.015 1.00 14.80 ? 776  ILE A CB  1 
ATOM   6183 C  CG1 . ILE A 1 776  ? 34.067 70.894  -26.091 1.00 17.86 ? 776  ILE A CG1 1 
ATOM   6184 C  CG2 . ILE A 1 776  ? 33.734 73.015  -24.620 1.00 15.50 ? 776  ILE A CG2 1 
ATOM   6185 C  CD1 . ILE A 1 776  ? 33.904 71.483  -27.477 1.00 20.77 ? 776  ILE A CD1 1 
ATOM   6186 N  N   . ARG A 1 777  ? 36.685 74.336  -24.183 1.00 13.90 ? 777  ARG A N   1 
ATOM   6187 C  CA  . ARG A 1 777  ? 37.187 75.039  -22.997 1.00 12.76 ? 777  ARG A CA  1 
ATOM   6188 C  C   . ARG A 1 777  ? 36.143 76.050  -22.581 1.00 14.33 ? 777  ARG A C   1 
ATOM   6189 O  O   . ARG A 1 777  ? 35.624 76.830  -23.423 1.00 14.43 ? 777  ARG A O   1 
ATOM   6190 C  CB  . ARG A 1 777  ? 38.496 75.800  -23.261 1.00 14.40 ? 777  ARG A CB  1 
ATOM   6191 C  CG  . ARG A 1 777  ? 39.629 74.908  -23.604 1.00 15.02 ? 777  ARG A CG  1 
ATOM   6192 C  CD  . ARG A 1 777  ? 40.915 75.717  -23.720 1.00 16.50 ? 777  ARG A CD  1 
ATOM   6193 N  NE  . ARG A 1 777  ? 42.009 74.880  -24.173 1.00 17.46 ? 777  ARG A NE  1 
ATOM   6194 C  CZ  . ARG A 1 777  ? 43.208 75.355  -24.479 1.00 23.21 ? 777  ARG A CZ  1 
ATOM   6195 N  NH1 . ARG A 1 777  ? 43.469 76.664  -24.345 1.00 27.82 ? 777  ARG A NH1 1 
ATOM   6196 N  NH2 . ARG A 1 777  ? 44.112 74.546  -25.026 1.00 27.59 ? 777  ARG A NH2 1 
ATOM   6197 N  N   . ASN A 1 778  ? 35.778 76.050  -21.311 1.00 11.58 ? 778  ASN A N   1 
ATOM   6198 C  CA  . ASN A 1 778  ? 34.843 76.998  -20.769 1.00 11.35 ? 778  ASN A CA  1 
ATOM   6199 C  C   . ASN A 1 778  ? 35.506 77.826  -19.692 1.00 13.62 ? 778  ASN A C   1 
ATOM   6200 O  O   . ASN A 1 778  ? 35.974 77.268  -18.670 1.00 13.40 ? 778  ASN A O   1 
ATOM   6201 C  CB  . ASN A 1 778  ? 33.624 76.329  -20.116 1.00 13.44 ? 778  ASN A CB  1 
ATOM   6202 C  CG  . ASN A 1 778  ? 32.710 75.663  -21.093 1.00 14.34 ? 778  ASN A CG  1 
ATOM   6203 O  OD1 . ASN A 1 778  ? 32.691 76.007  -22.278 1.00 15.30 ? 778  ASN A OD1 1 
ATOM   6204 N  ND2 . ASN A 1 778  ? 31.909 74.698  -20.598 1.00 13.31 ? 778  ASN A ND2 1 
ATOM   6205 N  N   . LEU A 1 779  ? 35.583 79.139  -19.903 1.00 13.62 ? 779  LEU A N   1 
ATOM   6206 C  CA  . LEU A 1 779  ? 36.086 80.011  -18.844 1.00 12.99 ? 779  LEU A CA  1 
ATOM   6207 C  C   . LEU A 1 779  ? 34.836 80.425  -18.088 1.00 13.39 ? 779  LEU A C   1 
ATOM   6208 O  O   . LEU A 1 779  ? 34.030 81.230  -18.579 1.00 14.08 ? 779  LEU A O   1 
ATOM   6209 C  CB  . LEU A 1 779  ? 36.824 81.214  -19.451 1.00 16.08 ? 779  LEU A CB  1 
ATOM   6210 C  CG  . LEU A 1 779  ? 37.369 82.193  -18.400 1.00 18.92 ? 779  LEU A CG  1 
ATOM   6211 C  CD1 . LEU A 1 779  ? 38.381 81.538  -17.515 1.00 22.38 ? 779  LEU A CD1 1 
ATOM   6212 C  CD2 . LEU A 1 779  ? 38.010 83.412  -19.131 1.00 23.55 ? 779  LEU A CD2 1 
ATOM   6213 N  N   . VAL A 1 780  ? 34.626 79.801  -16.930 1.00 12.46 ? 780  VAL A N   1 
ATOM   6214 C  CA  . VAL A 1 780  ? 33.388 79.983  -16.173 1.00 14.62 ? 780  VAL A CA  1 
ATOM   6215 C  C   . VAL A 1 780  ? 33.523 80.988  -15.021 1.00 14.67 ? 780  VAL A C   1 
ATOM   6216 O  O   . VAL A 1 780  ? 34.319 80.790  -14.082 1.00 14.42 ? 780  VAL A O   1 
ATOM   6217 C  CB  . VAL A 1 780  ? 32.905 78.602  -15.628 1.00 13.77 ? 780  VAL A CB  1 
ATOM   6218 C  CG1 . VAL A 1 780  ? 31.579 78.790  -14.886 1.00 14.02 ? 780  VAL A CG1 1 
ATOM   6219 C  CG2 . VAL A 1 780  ? 32.797 77.588  -16.749 1.00 12.84 ? 780  VAL A CG2 1 
ATOM   6220 N  N   . ASP A 1 781  ? 32.783 82.092  -15.125 1.00 14.34 ? 781  ASP A N   1 
ATOM   6221 C  CA  . ASP A 1 781  ? 32.776 83.111  -14.079 1.00 14.90 ? 781  ASP A CA  1 
ATOM   6222 C  C   . ASP A 1 781  ? 31.343 83.428  -13.705 1.00 15.92 ? 781  ASP A C   1 
ATOM   6223 O  O   . ASP A 1 781  ? 30.661 84.278  -14.356 1.00 15.62 ? 781  ASP A O   1 
ATOM   6224 C  CB  . ASP A 1 781  ? 33.471 84.373  -14.557 1.00 17.67 ? 781  ASP A CB  1 
ATOM   6225 C  CG  . ASP A 1 781  ? 33.542 85.423  -13.471 1.00 18.06 ? 781  ASP A CG  1 
ATOM   6226 O  OD1 . ASP A 1 781  ? 33.044 85.195  -12.350 1.00 18.43 ? 781  ASP A OD1 1 
ATOM   6227 O  OD2 . ASP A 1 781  ? 34.119 86.498  -13.739 1.00 24.27 ? 781  ASP A OD2 1 
ATOM   6228 N  N   . ILE A 1 782  ? 30.839 82.719  -12.699 1.00 14.85 ? 782  ILE A N   1 
ATOM   6229 C  CA  . ILE A 1 782  ? 29.438 82.860  -12.272 1.00 17.97 ? 782  ILE A CA  1 
ATOM   6230 C  C   . ILE A 1 782  ? 29.158 84.204  -11.630 1.00 20.80 ? 782  ILE A C   1 
ATOM   6231 O  O   . ILE A 1 782  ? 27.995 84.550  -11.329 1.00 22.79 ? 782  ILE A O   1 
ATOM   6232 C  CB  . ILE A 1 782  ? 29.068 81.654  -11.370 1.00 18.29 ? 782  ILE A CB  1 
ATOM   6233 C  CG1 . ILE A 1 782  ? 27.569 81.531  -11.182 1.00 21.97 ? 782  ILE A CG1 1 
ATOM   6234 C  CG2 . ILE A 1 782  ? 29.742 81.816  -10.021 1.00 18.91 ? 782  ILE A CG2 1 
ATOM   6235 C  CD1 . ILE A 1 782  ? 27.206 80.145  -10.692 1.00 23.19 ? 782  ILE A CD1 1 
ATOM   6236 N  N   . GLY A 1 783  ? 30.234 84.961  -11.414 1.00 19.61 ? 783  GLY A N   1 
ATOM   6237 C  CA  . GLY A 1 783  ? 30.098 86.327  -10.912 1.00 21.79 ? 783  GLY A CA  1 
ATOM   6238 C  C   . GLY A 1 783  ? 29.231 86.433  -9.678  1.00 22.19 ? 783  GLY A C   1 
ATOM   6239 O  O   . GLY A 1 783  ? 29.443 85.681  -8.732  1.00 26.23 ? 783  GLY A O   1 
ATOM   6240 N  N   . SER A 1 784  ? 28.237 87.325  -9.678  1.00 24.62 ? 784  SER A N   1 
ATOM   6241 C  CA  . SER A 1 784  ? 27.407 87.442  -8.487  1.00 26.31 ? 784  SER A CA  1 
ATOM   6242 C  C   . SER A 1 784  ? 26.012 86.842  -8.636  1.00 27.53 ? 784  SER A C   1 
ATOM   6243 O  O   . SER A 1 784  ? 25.061 87.243  -7.928  1.00 28.02 ? 784  SER A O   1 
ATOM   6244 C  CB  . SER A 1 784  ? 27.302 88.902  -8.045  1.00 29.05 ? 784  SER A CB  1 
ATOM   6245 O  OG  . SER A 1 784  ? 26.670 89.707  -9.035  1.00 34.64 ? 784  SER A OG  1 
ATOM   6246 N  N   . LEU A 1 785  ? 25.878 85.871  -9.538  1.00 26.77 ? 785  LEU A N   1 
ATOM   6247 C  CA  . LEU A 1 785  ? 24.579 85.226  -9.730  1.00 26.56 ? 785  LEU A CA  1 
ATOM   6248 C  C   . LEU A 1 785  ? 24.251 84.316  -8.560  1.00 27.89 ? 785  LEU A C   1 
ATOM   6249 O  O   . LEU A 1 785  ? 24.563 83.119  -8.575  1.00 28.56 ? 785  LEU A O   1 
ATOM   6250 C  CB  . LEU A 1 785  ? 24.573 84.405  -11.022 1.00 27.24 ? 785  LEU A CB  1 
ATOM   6251 C  CG  . LEU A 1 785  ? 24.877 85.179  -12.306 1.00 28.32 ? 785  LEU A CG  1 
ATOM   6252 C  CD1 . LEU A 1 785  ? 24.961 84.225  -13.474 1.00 30.30 ? 785  LEU A CD1 1 
ATOM   6253 C  CD2 . LEU A 1 785  ? 23.807 86.244  -12.508 1.00 28.84 ? 785  LEU A CD2 1 
ATOM   6254 N  N   . ASP A 1 786  ? 23.584 84.843  -7.550  1.00 27.64 ? 786  ASP A N   1 
ATOM   6255 C  CA  . ASP A 1 786  ? 23.264 84.017  -6.402  1.00 25.87 ? 786  ASP A CA  1 
ATOM   6256 C  C   . ASP A 1 786  ? 22.215 82.938  -6.711  1.00 21.70 ? 786  ASP A C   1 
ATOM   6257 O  O   . ASP A 1 786  ? 21.371 83.075  -7.607  1.00 22.05 ? 786  ASP A O   1 
ATOM   6258 C  CB  . ASP A 1 786  ? 22.780 84.871  -5.225  1.00 30.42 ? 786  ASP A CB  1 
ATOM   6259 C  CG  . ASP A 1 786  ? 23.916 85.573  -4.481  1.00 33.71 ? 786  ASP A CG  1 
ATOM   6260 O  OD1 . ASP A 1 786  ? 25.076 85.641  -4.962  1.00 30.85 ? 786  ASP A OD1 1 
ATOM   6261 O  OD2 . ASP A 1 786  ? 23.635 86.090  -3.378  1.00 38.80 ? 786  ASP A OD2 1 
ATOM   6262 N  N   . ASN A 1 787  ? 22.345 81.840  -5.983  1.00 20.26 ? 787  ASN A N   1 
ATOM   6263 C  CA  . ASN A 1 787  ? 21.438 80.710  -6.093  1.00 18.43 ? 787  ASN A CA  1 
ATOM   6264 C  C   . ASN A 1 787  ? 21.251 80.249  -7.511  1.00 18.55 ? 787  ASN A C   1 
ATOM   6265 O  O   . ASN A 1 787  ? 20.138 80.054  -7.985  1.00 18.50 ? 787  ASN A O   1 
ATOM   6266 C  CB  . ASN A 1 787  ? 20.114 81.065  -5.402  1.00 20.53 ? 787  ASN A CB  1 
ATOM   6267 C  CG  . ASN A 1 787  ? 20.334 81.351  -3.970  1.00 23.45 ? 787  ASN A CG  1 
ATOM   6268 O  OD1 . ASN A 1 787  ? 21.057 80.606  -3.301  1.00 23.44 ? 787  ASN A OD1 1 
ATOM   6269 N  ND2 . ASN A 1 787  ? 19.744 82.446  -3.463  1.00 30.61 ? 787  ASN A ND2 1 
ATOM   6270 N  N   . THR A 1 788  ? 22.383 80.020  -8.172  1.00 16.52 ? 788  THR A N   1 
ATOM   6271 C  CA  . THR A 1 788  ? 22.386 79.615  -9.562  1.00 16.69 ? 788  THR A CA  1 
ATOM   6272 C  C   . THR A 1 788  ? 23.417 78.520  -9.786  1.00 14.94 ? 788  THR A C   1 
ATOM   6273 O  O   . THR A 1 788  ? 24.502 78.582  -9.212  1.00 15.30 ? 788  THR A O   1 
ATOM   6274 C  CB  . THR A 1 788  ? 22.797 80.805  -10.465 1.00 18.06 ? 788  THR A CB  1 
ATOM   6275 O  OG1 . THR A 1 788  ? 21.819 81.861  -10.306 1.00 20.66 ? 788  THR A OG1 1 
ATOM   6276 C  CG2 . THR A 1 788  ? 22.841 80.396  -11.936 1.00 21.02 ? 788  THR A CG2 1 
ATOM   6277 N  N   . GLU A 1 789  ? 23.042 77.506  -10.554 1.00 14.93 ? 789  GLU A N   1 
ATOM   6278 C  CA  . GLU A 1 789  ? 23.992 76.483  -10.955 1.00 13.92 ? 789  GLU A CA  1 
ATOM   6279 C  C   . GLU A 1 789  ? 23.964 76.501  -12.477 1.00 15.37 ? 789  GLU A C   1 
ATOM   6280 O  O   . GLU A 1 789  ? 22.889 76.390  -13.105 1.00 16.86 ? 789  GLU A O   1 
ATOM   6281 C  CB  . GLU A 1 789  ? 23.636 75.083  -10.380 1.00 14.95 ? 789  GLU A CB  1 
ATOM   6282 C  CG  . GLU A 1 789  ? 23.255 75.130  -8.915  1.00 15.30 ? 789  GLU A CG  1 
ATOM   6283 C  CD  . GLU A 1 789  ? 23.456 73.801  -8.175  1.00 14.19 ? 789  GLU A CD  1 
ATOM   6284 O  OE1 . GLU A 1 789  ? 24.277 72.963  -8.675  1.00 14.89 ? 789  GLU A OE1 1 
ATOM   6285 O  OE2 . GLU A 1 789  ? 22.792 73.638  -7.124  1.00 14.71 ? 789  GLU A OE2 1 
ATOM   6286 N  N   . ILE A 1 790  ? 25.121 76.673  -13.093 1.00 12.93 ? 790  ILE A N   1 
ATOM   6287 C  CA  . ILE A 1 790  ? 25.231 76.699  -14.551 1.00 15.64 ? 790  ILE A CA  1 
ATOM   6288 C  C   . ILE A 1 790  ? 25.591 75.328  -15.080 1.00 14.67 ? 790  ILE A C   1 
ATOM   6289 O  O   . ILE A 1 790  ? 26.598 74.732  -14.643 1.00 14.95 ? 790  ILE A O   1 
ATOM   6290 C  CB  . ILE A 1 790  ? 26.342 77.669  -15.008 1.00 16.46 ? 790  ILE A CB  1 
ATOM   6291 C  CG1 . ILE A 1 790  ? 25.982 79.111  -14.569 1.00 21.82 ? 790  ILE A CG1 1 
ATOM   6292 C  CG2 . ILE A 1 790  ? 26.474 77.605  -16.548 1.00 18.31 ? 790  ILE A CG2 1 
ATOM   6293 C  CD1 . ILE A 1 790  ? 27.196 80.072  -14.595 1.00 25.14 ? 790  ILE A CD1 1 
ATOM   6294 N  N   . VAL A 1 791  ? 24.789 74.822  -16.005 1.00 14.16 ? 791  VAL A N   1 
ATOM   6295 C  CA  . VAL A 1 791  ? 25.021 73.519  -16.580 1.00 13.71 ? 791  VAL A CA  1 
ATOM   6296 C  C   . VAL A 1 791  ? 25.274 73.611  -18.068 1.00 13.11 ? 791  VAL A C   1 
ATOM   6297 O  O   . VAL A 1 791  ? 24.651 74.475  -18.787 1.00 14.41 ? 791  VAL A O   1 
ATOM   6298 C  CB  . VAL A 1 791  ? 23.788 72.541  -16.300 1.00 13.86 ? 791  VAL A CB  1 
ATOM   6299 C  CG1 . VAL A 1 791  ? 22.525 73.001  -17.097 1.00 17.76 ? 791  VAL A CG1 1 
ATOM   6300 C  CG2 . VAL A 1 791  ? 24.146 71.073  -16.690 1.00 14.70 ? 791  VAL A CG2 1 
ATOM   6301 N  N   . MET A 1 792  ? 26.179 72.783  -18.565 1.00 13.01 ? 792  MET A N   1 
ATOM   6302 C  CA  . MET A 1 792  ? 26.421 72.676  -20.000 1.00 12.55 ? 792  MET A CA  1 
ATOM   6303 C  C   . MET A 1 792  ? 25.736 71.369  -20.467 1.00 13.58 ? 792  MET A C   1 
ATOM   6304 O  O   . MET A 1 792  ? 26.074 70.283  -19.971 1.00 14.21 ? 792  MET A O   1 
ATOM   6305 C  CB  . MET A 1 792  ? 27.916 72.621  -20.327 1.00 14.63 ? 792  MET A CB  1 
ATOM   6306 C  CG  . MET A 1 792  ? 28.197 72.412  -21.812 1.00 16.16 ? 792  MET A CG  1 
ATOM   6307 S  SD  . MET A 1 792  ? 29.955 72.538  -22.194 1.00 14.87 ? 792  MET A SD  1 
ATOM   6308 C  CE  . MET A 1 792  ? 30.580 71.037  -21.337 1.00 16.19 ? 792  MET A CE  1 
ATOM   6309 N  N   . ARG A 1 793  ? 24.815 71.451  -21.420 1.00 14.20 ? 793  ARG A N   1 
ATOM   6310 C  CA  . ARG A 1 793  ? 24.100 70.284  -21.913 1.00 15.44 ? 793  ARG A CA  1 
ATOM   6311 C  C   . ARG A 1 793  ? 24.404 70.061  -23.383 1.00 14.32 ? 793  ARG A C   1 
ATOM   6312 O  O   . ARG A 1 793  ? 24.618 71.023  -24.141 1.00 14.26 ? 793  ARG A O   1 
ATOM   6313 C  CB  . ARG A 1 793  ? 22.591 70.499  -21.719 1.00 15.06 ? 793  ARG A CB  1 
ATOM   6314 C  CG  . ARG A 1 793  ? 21.722 69.294  -22.187 1.00 14.30 ? 793  ARG A CG  1 
ATOM   6315 C  CD  . ARG A 1 793  ? 20.247 69.526  -21.881 1.00 13.90 ? 793  ARG A CD  1 
ATOM   6316 N  NE  . ARG A 1 793  ? 20.010 69.572  -20.450 1.00 16.94 ? 793  ARG A NE  1 
ATOM   6317 C  CZ  . ARG A 1 793  ? 18.956 70.154  -19.886 1.00 17.15 ? 793  ARG A CZ  1 
ATOM   6318 N  NH1 . ARG A 1 793  ? 18.030 70.743  -20.675 1.00 16.17 ? 793  ARG A NH1 1 
ATOM   6319 N  NH2 . ARG A 1 793  ? 18.822 70.202  -18.577 1.00 18.32 ? 793  ARG A NH2 1 
ATOM   6320 N  N   . LEU A 1 794  ? 24.427 68.803  -23.784 1.00 13.90 ? 794  LEU A N   1 
ATOM   6321 C  CA  . LEU A 1 794  ? 24.578 68.357  -25.159 1.00 13.60 ? 794  LEU A CA  1 
ATOM   6322 C  C   . LEU A 1 794  ? 23.253 67.672  -25.521 1.00 16.13 ? 794  LEU A C   1 
ATOM   6323 O  O   . LEU A 1 794  ? 22.748 66.799  -24.785 1.00 15.59 ? 794  LEU A O   1 
ATOM   6324 C  CB  . LEU A 1 794  ? 25.731 67.364  -25.281 1.00 16.08 ? 794  LEU A CB  1 
ATOM   6325 C  CG  . LEU A 1 794  ? 27.092 68.030  -25.392 1.00 14.98 ? 794  LEU A CG  1 
ATOM   6326 C  CD1 . LEU A 1 794  ? 28.215 67.042  -24.995 1.00 17.78 ? 794  LEU A CD1 1 
ATOM   6327 C  CD2 . LEU A 1 794  ? 27.277 68.481  -26.835 1.00 19.71 ? 794  LEU A CD2 1 
ATOM   6328 N  N   . GLU A 1 795  ? 22.665 68.101  -26.646 1.00 16.09 ? 795  GLU A N   1 
ATOM   6329 C  CA  . GLU A 1 795  ? 21.409 67.514  -27.133 1.00 17.34 ? 795  GLU A CA  1 
ATOM   6330 C  C   . GLU A 1 795  ? 21.700 66.798  -28.425 1.00 18.43 ? 795  GLU A C   1 
ATOM   6331 O  O   . GLU A 1 795  ? 22.260 67.361  -29.354 1.00 18.59 ? 795  GLU A O   1 
ATOM   6332 C  CB  . GLU A 1 795  ? 20.329 68.586  -27.349 1.00 17.51 ? 795  GLU A CB  1 
ATOM   6333 C  CG  . GLU A 1 795  ? 19.944 69.297  -26.084 1.00 21.01 ? 795  GLU A CG  1 
ATOM   6334 C  CD  . GLU A 1 795  ? 19.034 70.525  -26.289 1.00 25.45 ? 795  GLU A CD  1 
ATOM   6335 O  OE1 . GLU A 1 795  ? 19.038 71.099  -27.407 1.00 30.00 ? 795  GLU A OE1 1 
ATOM   6336 O  OE2 . GLU A 1 795  ? 18.335 70.937  -25.334 1.00 26.06 ? 795  GLU A OE2 1 
ATOM   6337 N  N   . THR A 1 796  ? 21.349 65.518  -28.491 1.00 16.47 ? 796  THR A N   1 
ATOM   6338 C  CA  . THR A 1 796  ? 21.568 64.739  -29.681 1.00 17.77 ? 796  THR A CA  1 
ATOM   6339 C  C   . THR A 1 796  ? 20.326 63.911  -29.996 1.00 16.25 ? 796  THR A C   1 
ATOM   6340 O  O   . THR A 1 796  ? 19.342 63.957  -29.236 1.00 20.45 ? 796  THR A O   1 
ATOM   6341 C  CB  . THR A 1 796  ? 22.744 63.728  -29.552 1.00 17.02 ? 796  THR A CB  1 
ATOM   6342 O  OG1 . THR A 1 796  ? 22.334 62.546  -28.829 1.00 16.63 ? 796  THR A OG1 1 
ATOM   6343 C  CG2 . THR A 1 796  ? 23.911 64.379  -28.765 1.00 17.40 ? 796  THR A CG2 1 
ATOM   6344 N  N   . HIS A 1 797  ? 20.423 63.158  -31.075 1.00 19.53 ? 797  HIS A N   1 
ATOM   6345 C  CA  . HIS A 1 797  ? 19.349 62.270  -31.500 1.00 20.74 ? 797  HIS A CA  1 
ATOM   6346 C  C   A HIS A 1 797  ? 19.514 60.873  -30.997 0.50 20.18 ? 797  HIS A C   1 
ATOM   6347 C  C   B HIS A 1 797  ? 19.737 60.795  -31.319 0.50 22.01 ? 797  HIS A C   1 
ATOM   6348 O  O   A HIS A 1 797  ? 18.575 60.079  -31.116 0.50 18.37 ? 797  HIS A O   1 
ATOM   6349 O  O   B HIS A 1 797  ? 19.212 59.875  -31.940 0.50 20.21 ? 797  HIS A O   1 
ATOM   6350 C  CB  A HIS A 1 797  ? 19.327 62.181  -33.017 0.50 21.46 ? 797  HIS A CB  1 
ATOM   6351 C  CB  B HIS A 1 797  ? 19.058 62.490  -33.027 0.50 25.37 ? 797  HIS A CB  1 
ATOM   6352 C  CG  A HIS A 1 797  ? 18.634 63.328  -33.648 0.50 20.60 ? 797  HIS A CG  1 
ATOM   6353 C  CG  B HIS A 1 797  ? 18.332 63.768  -33.283 0.50 27.15 ? 797  HIS A CG  1 
ATOM   6354 N  ND1 A HIS A 1 797  ? 18.774 63.657  -34.978 0.50 19.92 ? 797  HIS A ND1 1 
ATOM   6355 N  ND1 B HIS A 1 797  ? 18.172 64.284  -34.550 0.50 27.35 ? 797  HIS A ND1 1 
ATOM   6356 C  CD2 A HIS A 1 797  ? 17.809 64.252  -33.107 0.50 18.32 ? 797  HIS A CD2 1 
ATOM   6357 C  CD2 B HIS A 1 797  ? 17.752 64.652  -32.437 0.50 26.26 ? 797  HIS A CD2 1 
ATOM   6358 C  CE1 A HIS A 1 797  ? 18.063 64.742  -35.228 0.50 19.38 ? 797  HIS A CE1 1 
ATOM   6359 C  CE1 B HIS A 1 797  ? 17.527 65.431  -34.474 0.50 28.39 ? 797  HIS A CE1 1 
ATOM   6360 N  NE2 A HIS A 1 797  ? 17.471 65.122  -34.108 0.50 14.52 ? 797  HIS A NE2 1 
ATOM   6361 N  NE2 B HIS A 1 797  ? 17.258 65.680  -33.208 0.50 25.69 ? 797  HIS A NE2 1 
ATOM   6362 N  N   . ILE A 1 798  ? 20.700 60.585  -30.436 1.00 19.92 ? 798  ILE A N   1 
ATOM   6363 C  CA  . ILE A 1 798  ? 21.082 59.247  -30.024 1.00 18.16 ? 798  ILE A CA  1 
ATOM   6364 C  C   . ILE A 1 798  ? 19.974 58.670  -29.160 1.00 16.53 ? 798  ILE A C   1 
ATOM   6365 O  O   . ILE A 1 798  ? 19.442 59.318  -28.238 1.00 17.52 ? 798  ILE A O   1 
ATOM   6366 C  CB  . ILE A 1 798  ? 22.430 59.274  -29.274 1.00 16.50 ? 798  ILE A CB  1 
ATOM   6367 C  CG1 . ILE A 1 798  ? 23.547 59.708  -30.222 1.00 16.97 ? 798  ILE A CG1 1 
ATOM   6368 C  CG2 . ILE A 1 798  ? 22.709 57.877  -28.693 1.00 19.14 ? 798  ILE A CG2 1 
ATOM   6369 C  CD1 . ILE A 1 798  ? 24.913 60.062  -29.499 1.00 20.31 ? 798  ILE A CD1 1 
ATOM   6370 N  N   . ASP A 1 799  ? 19.564 57.440  -29.538 1.00 18.58 ? 799  ASP A N   1 
ATOM   6371 C  CA  . ASP A 1 799  ? 18.475 56.754  -28.880 1.00 16.62 ? 799  ASP A CA  1 
ATOM   6372 C  C   . ASP A 1 799  ? 18.988 55.993  -27.667 1.00 19.63 ? 799  ASP A C   1 
ATOM   6373 O  O   . ASP A 1 799  ? 18.967 54.792  -27.616 1.00 18.10 ? 799  ASP A O   1 
ATOM   6374 C  CB  . ASP A 1 799  ? 17.809 55.764  -29.878 1.00 20.53 ? 799  ASP A CB  1 
ATOM   6375 C  CG  . ASP A 1 799  ? 16.470 55.251  -29.386 1.00 22.93 ? 799  ASP A CG  1 
ATOM   6376 O  OD1 . ASP A 1 799  ? 15.879 55.799  -28.461 1.00 29.28 ? 799  ASP A OD1 1 
ATOM   6377 O  OD2 . ASP A 1 799  ? 16.012 54.248  -29.948 1.00 30.10 ? 799  ASP A OD2 1 
ATOM   6378 N  N   . SER A 1 800  ? 19.421 56.748  -26.668 1.00 17.74 ? 800  SER A N   1 
ATOM   6379 C  CA  . SER A 1 800  ? 19.981 56.154  -25.463 1.00 17.90 ? 800  SER A CA  1 
ATOM   6380 C  C   . SER A 1 800  ? 18.920 55.767  -24.446 1.00 16.80 ? 800  SER A C   1 
ATOM   6381 O  O   . SER A 1 800  ? 19.188 54.991  -23.538 1.00 16.15 ? 800  SER A O   1 
ATOM   6382 C  CB  . SER A 1 800  ? 20.988 57.157  -24.858 1.00 16.47 ? 800  SER A CB  1 
ATOM   6383 O  OG  . SER A 1 800  ? 20.346 58.367  -24.524 1.00 16.06 ? 800  SER A OG  1 
ATOM   6384 N  N   . GLY A 1 801  ? 17.712 56.297  -24.557 1.00 14.87 ? 801  GLY A N   1 
ATOM   6385 C  CA  . GLY A 1 801  ? 16.659 55.939  -23.620 1.00 16.70 ? 801  GLY A CA  1 
ATOM   6386 C  C   . GLY A 1 801  ? 16.907 56.495  -22.258 1.00 16.30 ? 801  GLY A C   1 
ATOM   6387 O  O   . GLY A 1 801  ? 16.922 57.698  -22.055 1.00 18.65 ? 801  GLY A O   1 
ATOM   6388 N  N   . ASP A 1 802  ? 17.056 55.589  -21.316 1.00 15.22 ? 802  ASP A N   1 
ATOM   6389 C  CA  . ASP A 1 802  ? 17.328 55.965  -19.941 1.00 14.88 ? 802  ASP A CA  1 
ATOM   6390 C  C   . ASP A 1 802  ? 18.702 55.496  -19.496 1.00 15.93 ? 802  ASP A C   1 
ATOM   6391 O  O   . ASP A 1 802  ? 18.971 55.531  -18.297 1.00 16.39 ? 802  ASP A O   1 
ATOM   6392 C  CB  . ASP A 1 802  ? 16.244 55.392  -18.989 1.00 17.39 ? 802  ASP A CB  1 
ATOM   6393 C  CG  . ASP A 1 802  ? 16.090 53.874  -19.101 1.00 17.41 ? 802  ASP A CG  1 
ATOM   6394 O  OD1 . ASP A 1 802  ? 16.873 53.225  -19.833 1.00 22.29 ? 802  ASP A OD1 1 
ATOM   6395 O  OD2 . ASP A 1 802  ? 15.171 53.330  -18.425 1.00 21.71 ? 802  ASP A OD2 1 
ATOM   6396 N  N   . ILE A 1 803  ? 19.552 55.111  -20.432 1.00 14.07 ? 803  ILE A N   1 
ATOM   6397 C  CA  . ILE A 1 803  ? 20.886 54.618  -20.081 1.00 14.99 ? 803  ILE A CA  1 
ATOM   6398 C  C   . ILE A 1 803  ? 21.990 55.609  -20.418 1.00 15.31 ? 803  ILE A C   1 
ATOM   6399 O  O   . ILE A 1 803  ? 21.946 56.265  -21.452 1.00 14.94 ? 803  ILE A O   1 
ATOM   6400 C  CB  . ILE A 1 803  ? 21.183 53.310  -20.860 1.00 14.60 ? 803  ILE A CB  1 
ATOM   6401 C  CG1 . ILE A 1 803  ? 20.154 52.218  -20.468 1.00 15.32 ? 803  ILE A CG1 1 
ATOM   6402 C  CG2 . ILE A 1 803  ? 22.638 52.824  -20.626 1.00 14.76 ? 803  ILE A CG2 1 
ATOM   6403 C  CD1 . ILE A 1 803  ? 20.139 51.883  -18.973 1.00 18.61 ? 803  ILE A CD1 1 
ATOM   6404 N  N   . PHE A 1 804  ? 22.981 55.722  -19.520 1.00 14.36 ? 804  PHE A N   1 
ATOM   6405 C  CA  . PHE A 1 804  ? 24.150 56.531  -19.774 1.00 13.39 ? 804  PHE A CA  1 
ATOM   6406 C  C   . PHE A 1 804  ? 25.277 55.919  -18.943 1.00 12.43 ? 804  PHE A C   1 
ATOM   6407 O  O   . PHE A 1 804  ? 25.031 55.054  -18.118 1.00 14.69 ? 804  PHE A O   1 
ATOM   6408 C  CB  . PHE A 1 804  ? 23.933 58.029  -19.455 1.00 13.08 ? 804  PHE A CB  1 
ATOM   6409 C  CG  . PHE A 1 804  ? 23.514 58.343  -18.058 1.00 12.58 ? 804  PHE A CG  1 
ATOM   6410 C  CD1 . PHE A 1 804  ? 22.222 58.114  -17.604 1.00 12.37 ? 804  PHE A CD1 1 
ATOM   6411 C  CD2 . PHE A 1 804  ? 24.449 58.976  -17.183 1.00 13.19 ? 804  PHE A CD2 1 
ATOM   6412 C  CE1 . PHE A 1 804  ? 21.837 58.492  -16.333 1.00 12.86 ? 804  PHE A CE1 1 
ATOM   6413 C  CE2 . PHE A 1 804  ? 24.090 59.363  -15.925 1.00 12.99 ? 804  PHE A CE2 1 
ATOM   6414 C  CZ  . PHE A 1 804  ? 22.791 59.132  -15.466 1.00 13.60 ? 804  PHE A CZ  1 
ATOM   6415 N  N   . TYR A 1 805  ? 26.492 56.360  -19.185 1.00 11.60 ? 805  TYR A N   1 
ATOM   6416 C  CA  . TYR A 1 805  ? 27.651 55.808  -18.491 1.00 11.14 ? 805  TYR A CA  1 
ATOM   6417 C  C   . TYR A 1 805  ? 28.469 56.915  -17.930 1.00 12.98 ? 805  TYR A C   1 
ATOM   6418 O  O   . TYR A 1 805  ? 28.617 57.954  -18.576 1.00 13.66 ? 805  TYR A O   1 
ATOM   6419 C  CB  . TYR A 1 805  ? 28.510 55.011  -19.483 1.00 12.27 ? 805  TYR A CB  1 
ATOM   6420 C  CG  . TYR A 1 805  ? 27.808 53.781  -20.041 1.00 12.80 ? 805  TYR A CG  1 
ATOM   6421 C  CD1 . TYR A 1 805  ? 26.846 53.898  -21.035 1.00 13.74 ? 805  TYR A CD1 1 
ATOM   6422 C  CD2 . TYR A 1 805  ? 28.104 52.521  -19.537 1.00 12.16 ? 805  TYR A CD2 1 
ATOM   6423 C  CE1 . TYR A 1 805  ? 26.192 52.757  -21.511 1.00 13.11 ? 805  TYR A CE1 1 
ATOM   6424 C  CE2 . TYR A 1 805  ? 27.462 51.366  -20.002 1.00 12.54 ? 805  TYR A CE2 1 
ATOM   6425 C  CZ  . TYR A 1 805  ? 26.509 51.525  -20.993 1.00 13.27 ? 805  TYR A CZ  1 
ATOM   6426 O  OH  . TYR A 1 805  ? 25.920 50.398  -21.548 1.00 15.98 ? 805  TYR A OH  1 
ATOM   6427 N  N   . THR A 1 806  ? 28.991 56.697  -16.722 1.00 12.75 ? 806  THR A N   1 
ATOM   6428 C  CA  . THR A 1 806  ? 29.855 57.693  -16.084 1.00 11.38 ? 806  THR A CA  1 
ATOM   6429 C  C   . THR A 1 806  ? 31.023 56.909  -15.500 1.00 12.67 ? 806  THR A C   1 
ATOM   6430 O  O   . THR A 1 806  ? 30.906 55.686  -15.258 1.00 13.18 ? 806  THR A O   1 
ATOM   6431 C  CB  . THR A 1 806  ? 29.143 58.476  -14.977 1.00 11.27 ? 806  THR A CB  1 
ATOM   6432 O  OG1 . THR A 1 806  ? 28.769 57.600  -13.919 1.00 13.53 ? 806  THR A OG1 1 
ATOM   6433 C  CG2 . THR A 1 806  ? 27.876 59.143  -15.487 1.00 11.16 ? 806  THR A CG2 1 
ATOM   6434 N  N   . ASP A 1 807  ? 32.152 57.569  -15.302 1.00 10.81 ? 807  ASP A N   1 
ATOM   6435 C  CA  . ASP A 1 807  ? 33.273 56.839  -14.730 1.00 12.96 ? 807  ASP A CA  1 
ATOM   6436 C  C   . ASP A 1 807  ? 33.369 56.944  -13.213 1.00 10.55 ? 807  ASP A C   1 
ATOM   6437 O  O   . ASP A 1 807  ? 32.714 57.766  -12.565 1.00 11.39 ? 807  ASP A O   1 
ATOM   6438 C  CB  . ASP A 1 807  ? 34.586 57.310  -15.360 1.00 13.05 ? 807  ASP A CB  1 
ATOM   6439 C  CG  . ASP A 1 807  ? 35.038 58.641  -14.854 1.00 12.48 ? 807  ASP A CG  1 
ATOM   6440 O  OD1 . ASP A 1 807  ? 34.276 59.632  -14.944 1.00 14.41 ? 807  ASP A OD1 1 
ATOM   6441 O  OD2 . ASP A 1 807  ? 36.201 58.700  -14.342 1.00 15.25 ? 807  ASP A OD2 1 
ATOM   6442 N  N   . LEU A 1 808  ? 34.136 56.023  -12.672 1.00 11.08 ? 808  LEU A N   1 
ATOM   6443 C  CA  . LEU A 1 808  ? 34.414 56.015  -11.230 1.00 10.88 ? 808  LEU A CA  1 
ATOM   6444 C  C   . LEU A 1 808  ? 35.902 56.225  -11.063 1.00 10.67 ? 808  LEU A C   1 
ATOM   6445 O  O   . LEU A 1 808  ? 36.714 55.401  -11.508 1.00 10.54 ? 808  LEU A O   1 
ATOM   6446 C  CB  . LEU A 1 808  ? 33.979 54.689  -10.579 1.00 12.61 ? 808  LEU A CB  1 
ATOM   6447 C  CG  . LEU A 1 808  ? 32.452 54.549  -10.534 1.00 12.54 ? 808  LEU A CG  1 
ATOM   6448 C  CD1 . LEU A 1 808  ? 32.074 53.080  -10.319 1.00 13.57 ? 808  LEU A CD1 1 
ATOM   6449 C  CD2 . LEU A 1 808  ? 31.881 55.345  -9.353  1.00 13.87 ? 808  LEU A CD2 1 
ATOM   6450 N  N   . ASN A 1 809  ? 36.248 57.389  -10.509 1.00 10.79 ? 809  ASN A N   1 
ATOM   6451 C  CA  . ASN A 1 809  ? 37.631 57.722  -10.183 1.00 11.65 ? 809  ASN A CA  1 
ATOM   6452 C  C   . ASN A 1 809  ? 38.600 57.600  -11.334 1.00 10.60 ? 809  ASN A C   1 
ATOM   6453 O  O   . ASN A 1 809  ? 39.769 57.329  -11.134 1.00 11.33 ? 809  ASN A O   1 
ATOM   6454 C  CB  . ASN A 1 809  ? 38.125 56.832  -9.020  1.00 9.96  ? 809  ASN A CB  1 
ATOM   6455 C  CG  . ASN A 1 809  ? 37.078 56.726  -7.923  1.00 10.68 ? 809  ASN A CG  1 
ATOM   6456 O  OD1 . ASN A 1 809  ? 36.238 55.820  -7.932  1.00 10.31 ? 809  ASN A OD1 1 
ATOM   6457 N  ND2 . ASN A 1 809  ? 37.103 57.661  -6.992  1.00 11.43 ? 809  ASN A ND2 1 
ATOM   6458 N  N   . GLY A 1 810  ? 38.105 57.785  -12.570 1.00 9.99  ? 810  GLY A N   1 
ATOM   6459 C  CA  . GLY A 1 810  ? 39.035 57.701  -13.712 1.00 12.35 ? 810  GLY A CA  1 
ATOM   6460 C  C   . GLY A 1 810  ? 39.558 56.299  -13.976 1.00 12.71 ? 810  GLY A C   1 
ATOM   6461 O  O   . GLY A 1 810  ? 40.496 56.134  -14.766 1.00 15.13 ? 810  GLY A O   1 
ATOM   6462 N  N   . LEU A 1 811  ? 38.931 55.305  -13.352 1.00 11.77 ? 811  LEU A N   1 
ATOM   6463 C  CA  . LEU A 1 811  ? 39.351 53.922  -13.420 1.00 12.19 ? 811  LEU A CA  1 
ATOM   6464 C  C   . LEU A 1 811  ? 38.466 53.019  -14.272 1.00 13.69 ? 811  LEU A C   1 
ATOM   6465 O  O   . LEU A 1 811  ? 38.972 52.133  -14.970 1.00 15.26 ? 811  LEU A O   1 
ATOM   6466 C  CB  . LEU A 1 811  ? 39.391 53.372  -11.978 1.00 13.26 ? 811  LEU A CB  1 
ATOM   6467 C  CG  . LEU A 1 811  ? 39.811 51.895  -11.896 1.00 14.30 ? 811  LEU A CG  1 
ATOM   6468 C  CD1 . LEU A 1 811  ? 41.221 51.704  -12.447 1.00 15.84 ? 811  LEU A CD1 1 
ATOM   6469 C  CD2 . LEU A 1 811  ? 39.726 51.447  -10.428 1.00 14.13 ? 811  LEU A CD2 1 
ATOM   6470 N  N   . GLN A 1 812  ? 37.163 53.254  -14.241 1.00 11.36 ? 812  GLN A N   1 
ATOM   6471 C  CA  . GLN A 1 812  ? 36.228 52.335  -14.922 1.00 10.73 ? 812  GLN A CA  1 
ATOM   6472 C  C   . GLN A 1 812  ? 34.948 53.078  -15.245 1.00 11.27 ? 812  GLN A C   1 
ATOM   6473 O  O   . GLN A 1 812  ? 34.645 54.089  -14.599 1.00 12.48 ? 812  GLN A O   1 
ATOM   6474 C  CB  . GLN A 1 812  ? 35.897 51.194  -13.971 1.00 13.21 ? 812  GLN A CB  1 
ATOM   6475 C  CG  . GLN A 1 812  ? 35.279 51.710  -12.637 1.00 16.53 ? 812  GLN A CG  1 
ATOM   6476 C  CD  . GLN A 1 812  ? 34.989 50.580  -11.645 1.00 18.60 ? 812  GLN A CD  1 
ATOM   6477 O  OE1 . GLN A 1 812  ? 34.068 49.806  -11.836 1.00 18.42 ? 812  GLN A OE1 1 
ATOM   6478 N  NE2 . GLN A 1 812  ? 35.777 50.504  -10.566 1.00 18.51 ? 812  GLN A NE2 1 
ATOM   6479 N  N   . PHE A 1 813  ? 34.203 52.610  -16.249 1.00 11.56 ? 813  PHE A N   1 
ATOM   6480 C  CA  . PHE A 1 813  ? 32.917 53.222  -16.579 1.00 11.72 ? 813  PHE A CA  1 
ATOM   6481 C  C   . PHE A 1 813  ? 31.806 52.303  -16.124 1.00 12.55 ? 813  PHE A C   1 
ATOM   6482 O  O   . PHE A 1 813  ? 31.832 51.064  -16.387 1.00 15.40 ? 813  PHE A O   1 
ATOM   6483 C  CB  . PHE A 1 813  ? 32.843 53.507  -18.082 1.00 12.27 ? 813  PHE A CB  1 
ATOM   6484 C  CG  . PHE A 1 813  ? 33.602 54.738  -18.466 1.00 11.08 ? 813  PHE A CG  1 
ATOM   6485 C  CD1 . PHE A 1 813  ? 34.973 54.719  -18.550 1.00 11.31 ? 813  PHE A CD1 1 
ATOM   6486 C  CD2 . PHE A 1 813  ? 32.908 55.945  -18.663 1.00 12.40 ? 813  PHE A CD2 1 
ATOM   6487 C  CE1 . PHE A 1 813  ? 35.692 55.923  -18.807 1.00 12.59 ? 813  PHE A CE1 1 
ATOM   6488 C  CE2 . PHE A 1 813  ? 33.610 57.133  -18.921 1.00 14.78 ? 813  PHE A CE2 1 
ATOM   6489 C  CZ  . PHE A 1 813  ? 35.007 57.095  -18.986 1.00 13.64 ? 813  PHE A CZ  1 
ATOM   6490 N  N   . ILE A 1 814  ? 30.843 52.887  -15.425 1.00 11.97 ? 814  ILE A N   1 
ATOM   6491 C  CA  . ILE A 1 814  ? 29.718 52.127  -14.911 1.00 12.87 ? 814  ILE A CA  1 
ATOM   6492 C  C   . ILE A 1 814  ? 28.404 52.560  -15.600 1.00 13.08 ? 814  ILE A C   1 
ATOM   6493 O  O   . ILE A 1 814  ? 28.180 53.745  -15.890 1.00 12.14 ? 814  ILE A O   1 
ATOM   6494 C  CB  . ILE A 1 814  ? 29.650 52.320  -13.365 1.00 12.09 ? 814  ILE A CB  1 
ATOM   6495 C  CG1 . ILE A 1 814  ? 28.607 51.371  -12.770 1.00 11.65 ? 814  ILE A CG1 1 
ATOM   6496 C  CG2 . ILE A 1 814  ? 29.420 53.776  -12.978 1.00 13.20 ? 814  ILE A CG2 1 
ATOM   6497 C  CD1 . ILE A 1 814  ? 28.784 51.216  -11.206 1.00 11.72 ? 814  ILE A CD1 1 
ATOM   6498 N  N   . LYS A 1 815  ? 27.560 51.554  -15.881 1.00 12.85 ? 815  LYS A N   1 
ATOM   6499 C  CA  . LYS A 1 815  ? 26.257 51.834  -16.476 1.00 12.80 ? 815  LYS A CA  1 
ATOM   6500 C  C   . LYS A 1 815  ? 25.334 52.463  -15.449 1.00 12.94 ? 815  LYS A C   1 
ATOM   6501 O  O   . LYS A 1 815  ? 25.191 51.988  -14.312 1.00 12.98 ? 815  LYS A O   1 
ATOM   6502 C  CB  . LYS A 1 815  ? 25.656 50.520  -16.981 1.00 13.65 ? 815  LYS A CB  1 
ATOM   6503 C  CG  . LYS A 1 815  ? 24.382 50.661  -17.791 1.00 15.39 ? 815  LYS A CG  1 
ATOM   6504 C  CD  . LYS A 1 815  ? 24.001 49.269  -18.325 1.00 18.76 ? 815  LYS A CD  1 
ATOM   6505 C  CE  . LYS A 1 815  ? 22.745 49.290  -19.158 1.00 25.65 ? 815  LYS A CE  1 
ATOM   6506 N  NZ  . LYS A 1 815  ? 22.518 47.919  -19.730 1.00 27.52 ? 815  LYS A NZ  1 
ATOM   6507 N  N   . ARG A 1 816  ? 24.715 53.552  -15.846 1.00 12.40 ? 816  ARG A N   1 
ATOM   6508 C  CA  . ARG A 1 816  ? 23.723 54.231  -15.040 1.00 11.70 ? 816  ARG A CA  1 
ATOM   6509 C  C   . ARG A 1 816  ? 22.364 54.127  -15.741 1.00 12.15 ? 816  ARG A C   1 
ATOM   6510 O  O   . ARG A 1 816  ? 22.302 54.077  -16.967 1.00 13.50 ? 816  ARG A O   1 
ATOM   6511 C  CB  . ARG A 1 816  ? 23.997 55.739  -14.923 1.00 12.77 ? 816  ARG A CB  1 
ATOM   6512 C  CG  . ARG A 1 816  ? 25.403 56.127  -14.433 1.00 14.28 ? 816  ARG A CG  1 
ATOM   6513 C  CD  . ARG A 1 816  ? 25.637 55.511  -13.069 1.00 13.68 ? 816  ARG A CD  1 
ATOM   6514 N  NE  . ARG A 1 816  ? 26.836 56.069  -12.449 1.00 12.43 ? 816  ARG A NE  1 
ATOM   6515 C  CZ  . ARG A 1 816  ? 27.233 55.673  -11.238 1.00 12.34 ? 816  ARG A CZ  1 
ATOM   6516 N  NH1 . ARG A 1 816  ? 26.536 54.743  -10.603 1.00 11.79 ? 816  ARG A NH1 1 
ATOM   6517 N  NH2 . ARG A 1 816  ? 28.249 56.269  -10.619 1.00 11.84 ? 816  ARG A NH2 1 
ATOM   6518 N  N   . ARG A 1 817  ? 21.303 54.088  -14.941 1.00 13.05 ? 817  ARG A N   1 
ATOM   6519 C  CA  . ARG A 1 817  ? 19.955 54.112  -15.520 1.00 13.54 ? 817  ARG A CA  1 
ATOM   6520 C  C   . ARG A 1 817  ? 19.218 55.250  -14.847 1.00 14.50 ? 817  ARG A C   1 
ATOM   6521 O  O   . ARG A 1 817  ? 19.098 55.321  -13.602 1.00 15.13 ? 817  ARG A O   1 
ATOM   6522 C  CB  . ARG A 1 817  ? 19.239 52.776  -15.252 1.00 15.09 ? 817  ARG A CB  1 
ATOM   6523 C  CG  . ARG A 1 817  ? 17.778 52.788  -15.717 1.00 16.21 ? 817  ARG A CG  1 
ATOM   6524 C  CD  . ARG A 1 817  ? 17.070 51.416  -15.512 1.00 17.07 ? 817  ARG A CD  1 
ATOM   6525 N  NE  . ARG A 1 817  ? 17.618 50.399  -16.402 1.00 17.75 ? 817  ARG A NE  1 
ATOM   6526 C  CZ  . ARG A 1 817  ? 18.387 49.387  -16.006 1.00 18.09 ? 817  ARG A CZ  1 
ATOM   6527 N  NH1 . ARG A 1 817  ? 18.710 49.258  -14.718 1.00 17.10 ? 817  ARG A NH1 1 
ATOM   6528 N  NH2 . ARG A 1 817  ? 18.828 48.494  -16.878 1.00 22.53 ? 817  ARG A NH2 1 
ATOM   6529 N  N   . ARG A 1 818  ? 18.750 56.195  -15.669 1.00 13.19 ? 818  ARG A N   1 
ATOM   6530 C  CA  . ARG A 1 818  ? 17.977 57.306  -15.145 1.00 14.92 ? 818  ARG A CA  1 
ATOM   6531 C  C   . ARG A 1 818  ? 16.701 56.681  -14.607 1.00 16.34 ? 818  ARG A C   1 
ATOM   6532 O  O   . ARG A 1 818  ? 16.074 55.848  -15.289 1.00 17.57 ? 818  ARG A O   1 
ATOM   6533 C  CB  . ARG A 1 818  ? 17.600 58.292  -16.264 1.00 16.13 ? 818  ARG A CB  1 
ATOM   6534 C  CG  A ARG A 1 818  ? 16.850 59.537  -15.763 0.50 15.17 ? 818  ARG A CG  1 
ATOM   6535 C  CG  B ARG A 1 818  ? 16.983 59.524  -15.969 0.50 19.71 ? 818  ARG A CG  1 
ATOM   6536 C  CD  A ARG A 1 818  ? 16.141 60.289  -16.910 0.50 12.90 ? 818  ARG A CD  1 
ATOM   6537 C  CD  B ARG A 1 818  ? 16.803 60.425  -17.198 0.50 20.38 ? 818  ARG A CD  1 
ATOM   6538 N  NE  A ARG A 1 818  ? 14.889 59.644  -17.266 0.50 14.45 ? 818  ARG A NE  1 
ATOM   6539 N  NE  B ARG A 1 818  ? 16.045 59.779  -18.246 0.50 21.95 ? 818  ARG A NE  1 
ATOM   6540 C  CZ  A ARG A 1 818  ? 14.627 59.078  -18.438 0.50 14.51 ? 818  ARG A CZ  1 
ATOM   6541 C  CZ  B ARG A 1 818  ? 16.533 59.376  -19.416 0.50 19.39 ? 818  ARG A CZ  1 
ATOM   6542 N  NH1 A ARG A 1 818  ? 15.527 59.069  -19.406 0.50 12.49 ? 818  ARG A NH1 1 
ATOM   6543 N  NH1 B ARG A 1 818  ? 17.833 59.543  -19.752 0.50 15.27 ? 818  ARG A NH1 1 
ATOM   6544 N  NH2 A ARG A 1 818  ? 13.457 58.503  -18.626 0.50 17.46 ? 818  ARG A NH2 1 
ATOM   6545 N  NH2 B ARG A 1 818  ? 15.692 58.790  -20.255 0.50 19.30 ? 818  ARG A NH2 1 
ATOM   6546 N  N   . LEU A 1 819  ? 16.314 57.087  -13.411 1.00 15.24 ? 819  LEU A N   1 
ATOM   6547 C  CA  . LEU A 1 819  ? 15.087 56.558  -12.764 1.00 15.82 ? 819  LEU A CA  1 
ATOM   6548 C  C   . LEU A 1 819  ? 14.114 57.717  -12.497 1.00 15.50 ? 819  LEU A C   1 
ATOM   6549 O  O   . LEU A 1 819  ? 14.355 58.587  -11.649 1.00 16.90 ? 819  LEU A O   1 
ATOM   6550 C  CB  . LEU A 1 819  ? 15.452 55.884  -11.432 1.00 16.52 ? 819  LEU A CB  1 
ATOM   6551 C  CG  . LEU A 1 819  ? 16.393 54.671  -11.577 1.00 17.87 ? 819  LEU A CG  1 
ATOM   6552 C  CD1 . LEU A 1 819  ? 16.825 54.191  -10.197 1.00 21.22 ? 819  LEU A CD1 1 
ATOM   6553 C  CD2 . LEU A 1 819  ? 15.699 53.554  -12.326 1.00 19.08 ? 819  LEU A CD2 1 
ATOM   6554 N  N   . ASP A 1 820  ? 13.003 57.714  -13.217 1.00 18.87 ? 820  ASP A N   1 
ATOM   6555 C  CA  . ASP A 1 820  ? 12.063 58.780  -12.996 1.00 19.57 ? 820  ASP A CA  1 
ATOM   6556 C  C   . ASP A 1 820  ? 11.357 58.649  -11.647 1.00 18.01 ? 820  ASP A C   1 
ATOM   6557 O  O   . ASP A 1 820  ? 10.727 59.601  -11.173 1.00 19.94 ? 820  ASP A O   1 
ATOM   6558 C  CB  . ASP A 1 820  ? 11.097 58.834  -14.179 1.00 21.16 ? 820  ASP A CB  1 
ATOM   6559 C  CG  . ASP A 1 820  ? 11.816 59.159  -15.479 1.00 23.93 ? 820  ASP A CG  1 
ATOM   6560 O  OD1 . ASP A 1 820  ? 12.896 59.818  -15.450 1.00 24.89 ? 820  ASP A OD1 1 
ATOM   6561 O  OD2 . ASP A 1 820  ? 11.306 58.776  -16.552 1.00 27.41 ? 820  ASP A OD2 1 
ATOM   6562 N  N   . LYS A 1 821  ? 11.466 57.481  -11.000 1.00 16.68 ? 821  LYS A N   1 
ATOM   6563 C  CA  . LYS A 1 821  ? 10.869 57.347  -9.673  1.00 17.87 ? 821  LYS A CA  1 
ATOM   6564 C  C   . LYS A 1 821  ? 11.715 58.087  -8.621  1.00 18.63 ? 821  LYS A C   1 
ATOM   6565 O  O   . LYS A 1 821  ? 11.262 58.281  -7.499  1.00 21.60 ? 821  LYS A O   1 
ATOM   6566 C  CB  . LYS A 1 821  ? 10.717 55.875  -9.280  1.00 18.30 ? 821  LYS A CB  1 
ATOM   6567 C  CG  . LYS A 1 821  ? 12.047 55.168  -9.018  1.00 16.93 ? 821  LYS A CG  1 
ATOM   6568 C  CD  . LYS A 1 821  ? 11.886 53.678  -8.994  1.00 18.84 ? 821  LYS A CD  1 
ATOM   6569 C  CE  . LYS A 1 821  ? 13.206 52.991  -8.768  1.00 19.51 ? 821  LYS A CE  1 
ATOM   6570 N  NZ  . LYS A 1 821  ? 13.133 51.526  -8.989  1.00 19.34 ? 821  LYS A NZ  1 
ATOM   6571 N  N   . LEU A 1 822  ? 12.886 58.587  -9.031  1.00 16.56 ? 822  LEU A N   1 
ATOM   6572 C  CA  . LEU A 1 822  ? 13.731 59.357  -8.084  1.00 18.22 ? 822  LEU A CA  1 
ATOM   6573 C  C   . LEU A 1 822  ? 13.753 60.803  -8.595  1.00 18.36 ? 822  LEU A C   1 
ATOM   6574 O  O   . LEU A 1 822  ? 13.581 61.030  -9.793  1.00 17.08 ? 822  LEU A O   1 
ATOM   6575 C  CB  . LEU A 1 822  ? 15.183 58.826  -8.067  1.00 18.27 ? 822  LEU A CB  1 
ATOM   6576 C  CG  . LEU A 1 822  ? 15.333 57.361  -7.614  1.00 18.93 ? 822  LEU A CG  1 
ATOM   6577 C  CD1 . LEU A 1 822  ? 16.810 56.983  -7.570  1.00 19.72 ? 822  LEU A CD1 1 
ATOM   6578 C  CD2 . LEU A 1 822  ? 14.651 57.136  -6.266  1.00 19.63 ? 822  LEU A CD2 1 
ATOM   6579 N  N   . PRO A 1 823  ? 13.984 61.770  -7.695  1.00 16.73 ? 823  PRO A N   1 
ATOM   6580 C  CA  . PRO A 1 823  ? 14.035 63.192  -8.104  1.00 17.23 ? 823  PRO A CA  1 
ATOM   6581 C  C   . PRO A 1 823  ? 15.261 63.473  -8.964  1.00 18.25 ? 823  PRO A C   1 
ATOM   6582 O  O   . PRO A 1 823  ? 16.235 62.698  -8.986  1.00 17.07 ? 823  PRO A O   1 
ATOM   6583 C  CB  . PRO A 1 823  ? 14.061 63.955  -6.796  1.00 17.77 ? 823  PRO A CB  1 
ATOM   6584 C  CG  . PRO A 1 823  ? 14.712 63.000  -5.814  1.00 19.10 ? 823  PRO A CG  1 
ATOM   6585 C  CD  . PRO A 1 823  ? 14.178 61.611  -6.244  1.00 17.50 ? 823  PRO A CD  1 
ATOM   6586 N  N   . LEU A 1 824  ? 15.210 64.584  -9.688  1.00 16.52 ? 824  LEU A N   1 
ATOM   6587 C  CA  . LEU A 1 824  ? 16.278 64.965  -10.579 1.00 15.90 ? 824  LEU A CA  1 
ATOM   6588 C  C   . LEU A 1 824  ? 17.688 64.840  -9.978  1.00 15.30 ? 824  LEU A C   1 
ATOM   6589 O  O   . LEU A 1 824  ? 18.575 64.261  -10.626 1.00 14.52 ? 824  LEU A O   1 
ATOM   6590 C  CB  . LEU A 1 824  ? 15.969 66.406  -11.053 1.00 16.79 ? 824  LEU A CB  1 
ATOM   6591 C  CG  . LEU A 1 824  ? 16.763 66.990  -12.221 1.00 15.90 ? 824  LEU A CG  1 
ATOM   6592 C  CD1 . LEU A 1 824  ? 15.945 68.258  -12.701 1.00 16.86 ? 824  LEU A CD1 1 
ATOM   6593 C  CD2 . LEU A 1 824  ? 18.225 67.396  -11.831 1.00 16.12 ? 824  LEU A CD2 1 
ATOM   6594 N  N   . GLN A 1 825  ? 17.869 65.385  -8.777  1.00 14.29 ? 825  GLN A N   1 
ATOM   6595 C  CA  . GLN A 1 825  ? 19.180 65.386  -8.140  1.00 14.56 ? 825  GLN A CA  1 
ATOM   6596 C  C   . GLN A 1 825  ? 19.715 63.990  -7.852  1.00 15.14 ? 825  GLN A C   1 
ATOM   6597 O  O   . GLN A 1 825  ? 20.953 63.828  -7.725  1.00 13.86 ? 825  GLN A O   1 
ATOM   6598 C  CB  . GLN A 1 825  ? 19.152 66.254  -6.885  1.00 14.36 ? 825  GLN A CB  1 
ATOM   6599 C  CG  . GLN A 1 825  ? 18.226 65.717  -5.786  1.00 13.61 ? 825  GLN A CG  1 
ATOM   6600 C  CD  . GLN A 1 825  ? 16.770 66.239  -5.886  1.00 14.26 ? 825  GLN A CD  1 
ATOM   6601 O  OE1 . GLN A 1 825  ? 16.318 66.679  -6.939  1.00 17.53 ? 825  GLN A OE1 1 
ATOM   6602 N  NE2 . GLN A 1 825  ? 16.049 66.166  -4.778  1.00 15.57 ? 825  GLN A NE2 1 
ATOM   6603 N  N   . ALA A 1 826  ? 18.814 62.996  -7.748  1.00 14.50 ? 826  ALA A N   1 
ATOM   6604 C  CA  . ALA A 1 826  ? 19.288 61.636  -7.506  1.00 13.66 ? 826  ALA A CA  1 
ATOM   6605 C  C   . ALA A 1 826  ? 19.873 61.048  -8.777  1.00 13.85 ? 826  ALA A C   1 
ATOM   6606 O  O   . ALA A 1 826  ? 20.624 60.073  -8.731  1.00 14.94 ? 826  ALA A O   1 
ATOM   6607 C  CB  . ALA A 1 826  ? 18.134 60.754  -7.017  1.00 15.50 ? 826  ALA A CB  1 
ATOM   6608 N  N   . ASN A 1 827  ? 19.513 61.599  -9.949  1.00 12.85 ? 827  ASN A N   1 
ATOM   6609 C  CA  . ASN A 1 827  ? 20.006 61.115  -11.229 1.00 12.79 ? 827  ASN A CA  1 
ATOM   6610 C  C   . ASN A 1 827  ? 21.308 61.782  -11.663 1.00 12.16 ? 827  ASN A C   1 
ATOM   6611 O  O   . ASN A 1 827  ? 21.853 61.471  -12.710 1.00 13.32 ? 827  ASN A O   1 
ATOM   6612 C  CB  . ASN A 1 827  ? 18.913 61.229  -12.302 1.00 14.32 ? 827  ASN A CB  1 
ATOM   6613 C  CG  . ASN A 1 827  ? 17.794 60.215  -12.050 1.00 16.29 ? 827  ASN A CG  1 
ATOM   6614 O  OD1 . ASN A 1 827  ? 18.009 59.012  -12.115 1.00 15.85 ? 827  ASN A OD1 1 
ATOM   6615 N  ND2 . ASN A 1 827  ? 16.620 60.709  -11.709 1.00 18.15 ? 827  ASN A ND2 1 
ATOM   6616 N  N   . TYR A 1 828  ? 21.827 62.630  -10.785 1.00 14.37 ? 828  TYR A N   1 
ATOM   6617 C  CA  . TYR A 1 828  ? 23.146 63.229  -11.018 1.00 12.51 ? 828  TYR A CA  1 
ATOM   6618 C  C   . TYR A 1 828  ? 24.182 62.294  -10.372 1.00 13.55 ? 828  TYR A C   1 
ATOM   6619 O  O   . TYR A 1 828  ? 23.968 61.766  -9.281  1.00 14.55 ? 828  TYR A O   1 
ATOM   6620 C  CB  . TYR A 1 828  ? 23.253 64.585  -10.320 1.00 13.55 ? 828  TYR A CB  1 
ATOM   6621 C  CG  . TYR A 1 828  ? 23.233 65.733  -11.280 1.00 13.35 ? 828  TYR A CG  1 
ATOM   6622 C  CD1 . TYR A 1 828  ? 22.163 65.932  -12.167 1.00 11.87 ? 828  TYR A CD1 1 
ATOM   6623 C  CD2 . TYR A 1 828  ? 24.326 66.574  -11.374 1.00 13.65 ? 828  TYR A CD2 1 
ATOM   6624 C  CE1 . TYR A 1 828  ? 22.201 66.927  -13.140 1.00 13.84 ? 828  TYR A CE1 1 
ATOM   6625 C  CE2 . TYR A 1 828  ? 24.378 67.559  -12.304 1.00 15.71 ? 828  TYR A CE2 1 
ATOM   6626 C  CZ  . TYR A 1 828  ? 23.319 67.734  -13.196 1.00 13.56 ? 828  TYR A CZ  1 
ATOM   6627 O  OH  . TYR A 1 828  ? 23.465 68.754  -14.109 1.00 15.40 ? 828  TYR A OH  1 
ATOM   6628 N  N   . TYR A 1 829  ? 25.283 62.103  -11.075 1.00 12.49 ? 829  TYR A N   1 
ATOM   6629 C  CA  . TYR A 1 829  ? 26.367 61.217  -10.667 1.00 12.76 ? 829  TYR A CA  1 
ATOM   6630 C  C   . TYR A 1 829  ? 27.703 61.939  -10.816 1.00 12.66 ? 829  TYR A C   1 
ATOM   6631 O  O   . TYR A 1 829  ? 27.800 62.955  -11.474 1.00 12.75 ? 829  TYR A O   1 
ATOM   6632 C  CB  . TYR A 1 829  ? 26.391 59.979  -11.584 1.00 11.44 ? 829  TYR A CB  1 
ATOM   6633 C  CG  . TYR A 1 829  ? 25.253 59.074  -11.264 1.00 12.55 ? 829  TYR A CG  1 
ATOM   6634 C  CD1 . TYR A 1 829  ? 25.329 58.176  -10.197 1.00 12.10 ? 829  TYR A CD1 1 
ATOM   6635 C  CD2 . TYR A 1 829  ? 24.074 59.133  -12.021 1.00 13.31 ? 829  TYR A CD2 1 
ATOM   6636 C  CE1 . TYR A 1 829  ? 24.225 57.347  -9.872  1.00 14.43 ? 829  TYR A CE1 1 
ATOM   6637 C  CE2 . TYR A 1 829  ? 22.992 58.302  -11.708 1.00 14.01 ? 829  TYR A CE2 1 
ATOM   6638 C  CZ  . TYR A 1 829  ? 23.066 57.416  -10.638 1.00 14.15 ? 829  TYR A CZ  1 
ATOM   6639 O  OH  . TYR A 1 829  ? 21.968 56.597  -10.332 1.00 14.67 ? 829  TYR A OH  1 
ATOM   6640 N  N   . PRO A 1 830  ? 28.749 61.429  -10.159 1.00 12.77 ? 830  PRO A N   1 
ATOM   6641 C  CA  . PRO A 1 830  ? 30.055 62.088  -10.323 1.00 11.56 ? 830  PRO A CA  1 
ATOM   6642 C  C   . PRO A 1 830  ? 30.541 61.843  -11.759 1.00 12.08 ? 830  PRO A C   1 
ATOM   6643 O  O   . PRO A 1 830  ? 30.313 60.747  -12.315 1.00 12.59 ? 830  PRO A O   1 
ATOM   6644 C  CB  . PRO A 1 830  ? 30.981 61.326  -9.316  1.00 16.27 ? 830  PRO A CB  1 
ATOM   6645 C  CG  . PRO A 1 830  ? 30.057 60.478  -8.425  1.00 15.61 ? 830  PRO A CG  1 
ATOM   6646 C  CD  . PRO A 1 830  ? 28.739 60.302  -9.204  1.00 13.56 ? 830  PRO A CD  1 
ATOM   6647 N  N   . ILE A 1 831  ? 31.150 62.854  -12.377 1.00 12.76 ? 831  ILE A N   1 
ATOM   6648 C  CA  . ILE A 1 831  ? 31.790 62.685  -13.680 1.00 12.03 ? 831  ILE A CA  1 
ATOM   6649 C  C   . ILE A 1 831  ? 33.251 63.004  -13.391 1.00 12.62 ? 831  ILE A C   1 
ATOM   6650 O  O   . ILE A 1 831  ? 33.767 64.075  -13.717 1.00 12.04 ? 831  ILE A O   1 
ATOM   6651 C  CB  . ILE A 1 831  ? 31.226 63.669  -14.752 1.00 11.44 ? 831  ILE A CB  1 
ATOM   6652 C  CG1 . ILE A 1 831  ? 29.709 63.707  -14.715 1.00 12.45 ? 831  ILE A CG1 1 
ATOM   6653 C  CG2 . ILE A 1 831  ? 31.742 63.244  -16.160 1.00 13.58 ? 831  ILE A CG2 1 
ATOM   6654 C  CD1 . ILE A 1 831  ? 28.954 62.416  -15.051 1.00 11.81 ? 831  ILE A CD1 1 
ATOM   6655 N  N   . PRO A 1 832  ? 33.968 62.050  -12.788 1.00 10.59 ? 832  PRO A N   1 
ATOM   6656 C  CA  . PRO A 1 832  ? 35.365 62.379  -12.475 1.00 11.35 ? 832  PRO A CA  1 
ATOM   6657 C  C   . PRO A 1 832  ? 36.271 62.503  -13.685 1.00 12.10 ? 832  PRO A C   1 
ATOM   6658 O  O   . PRO A 1 832  ? 37.242 63.235  -13.596 1.00 15.06 ? 832  PRO A O   1 
ATOM   6659 C  CB  . PRO A 1 832  ? 35.793 61.283  -11.489 1.00 11.52 ? 832  PRO A CB  1 
ATOM   6660 C  CG  . PRO A 1 832  ? 34.786 60.182  -11.704 1.00 12.71 ? 832  PRO A CG  1 
ATOM   6661 C  CD  . PRO A 1 832  ? 33.491 60.860  -12.076 1.00 12.42 ? 832  PRO A CD  1 
ATOM   6662 N  N   . SER A 1 833  ? 35.934 61.855  -14.803 1.00 11.38 ? 833  SER A N   1 
ATOM   6663 C  CA  . SER A 1 833  ? 36.790 62.020  -15.973 1.00 11.18 ? 833  SER A CA  1 
ATOM   6664 C  C   . SER A 1 833  ? 36.002 61.813  -17.282 1.00 12.19 ? 833  SER A C   1 
ATOM   6665 O  O   . SER A 1 833  ? 36.535 62.139  -18.335 1.00 11.29 ? 833  SER A O   1 
ATOM   6666 C  CB  . SER A 1 833  ? 37.985 61.062  -15.921 1.00 12.99 ? 833  SER A CB  1 
ATOM   6667 O  OG  . SER A 1 833  ? 37.648 59.728  -16.208 1.00 15.72 ? 833  SER A OG  1 
ATOM   6668 N  N   . GLY A 1 834  ? 34.784 61.264  -17.243 1.00 11.62 ? 834  GLY A N   1 
ATOM   6669 C  CA  . GLY A 1 834  ? 34.079 61.134  -18.545 1.00 12.00 ? 834  GLY A CA  1 
ATOM   6670 C  C   . GLY A 1 834  ? 32.715 60.529  -18.408 1.00 10.51 ? 834  GLY A C   1 
ATOM   6671 O  O   . GLY A 1 834  ? 32.330 59.946  -17.385 1.00 11.97 ? 834  GLY A O   1 
ATOM   6672 N  N   . MET A 1 835  ? 31.939 60.685  -19.477 1.00 12.01 ? 835  MET A N   1 
ATOM   6673 C  CA  . MET A 1 835  ? 30.578 60.135  -19.494 1.00 11.89 ? 835  MET A CA  1 
ATOM   6674 C  C   . MET A 1 835  ? 30.215 59.911  -20.965 1.00 12.65 ? 835  MET A C   1 
ATOM   6675 O  O   . MET A 1 835  ? 30.822 60.543  -21.872 1.00 13.28 ? 835  MET A O   1 
ATOM   6676 C  CB  . MET A 1 835  ? 29.596 61.137  -18.855 1.00 12.19 ? 835  MET A CB  1 
ATOM   6677 C  CG  . MET A 1 835  ? 29.517 62.476  -19.619 1.00 14.93 ? 835  MET A CG  1 
ATOM   6678 S  SD  . MET A 1 835  ? 28.605 63.761  -18.771 1.00 15.95 ? 835  MET A SD  1 
ATOM   6679 C  CE  . MET A 1 835  ? 27.134 62.965  -18.289 1.00 18.96 ? 835  MET A CE  1 
ATOM   6680 N  N   . PHE A 1 836  ? 29.286 58.997  -21.200 1.00 11.76 ? 836  PHE A N   1 
ATOM   6681 C  CA  . PHE A 1 836  ? 28.854 58.793  -22.593 1.00 11.88 ? 836  PHE A CA  1 
ATOM   6682 C  C   . PHE A 1 836  ? 27.466 58.243  -22.673 1.00 13.98 ? 836  PHE A C   1 
ATOM   6683 O  O   . PHE A 1 836  ? 26.919 57.712  -21.715 1.00 13.95 ? 836  PHE A O   1 
ATOM   6684 C  CB  . PHE A 1 836  ? 29.872 57.927  -23.403 1.00 13.09 ? 836  PHE A CB  1 
ATOM   6685 C  CG  . PHE A 1 836  ? 30.040 56.484  -22.945 1.00 13.32 ? 836  PHE A CG  1 
ATOM   6686 C  CD1 . PHE A 1 836  ? 29.173 55.474  -23.392 1.00 13.55 ? 836  PHE A CD1 1 
ATOM   6687 C  CD2 . PHE A 1 836  ? 31.131 56.123  -22.156 1.00 13.22 ? 836  PHE A CD2 1 
ATOM   6688 C  CE1 . PHE A 1 836  ? 29.405 54.128  -23.063 1.00 14.55 ? 836  PHE A CE1 1 
ATOM   6689 C  CE2 . PHE A 1 836  ? 31.359 54.775  -21.831 1.00 14.88 ? 836  PHE A CE2 1 
ATOM   6690 C  CZ  . PHE A 1 836  ? 30.501 53.780  -22.291 1.00 15.36 ? 836  PHE A CZ  1 
ATOM   6691 N  N   . ILE A 1 837  ? 26.858 58.446  -23.850 1.00 14.11 ? 837  ILE A N   1 
ATOM   6692 C  CA  . ILE A 1 837  ? 25.545 57.857  -24.164 1.00 14.56 ? 837  ILE A CA  1 
ATOM   6693 C  C   . ILE A 1 837  ? 25.724 57.169  -25.501 1.00 13.35 ? 837  ILE A C   1 
ATOM   6694 O  O   . ILE A 1 837  ? 26.578 57.559  -26.307 1.00 13.92 ? 837  ILE A O   1 
ATOM   6695 C  CB  . ILE A 1 837  ? 24.412 58.905  -24.289 1.00 14.87 ? 837  ILE A CB  1 
ATOM   6696 C  CG1 . ILE A 1 837  ? 24.878 60.109  -25.107 1.00 15.12 ? 837  ILE A CG1 1 
ATOM   6697 C  CG2 . ILE A 1 837  ? 23.818 59.227  -22.925 1.00 15.68 ? 837  ILE A CG2 1 
ATOM   6698 C  CD1 . ILE A 1 837  ? 23.641 60.967  -25.607 1.00 16.40 ? 837  ILE A CD1 1 
ATOM   6699 N  N   . GLU A 1 838  ? 24.935 56.123  -25.729 1.00 12.97 ? 838  GLU A N   1 
ATOM   6700 C  CA  . GLU A 1 838  ? 25.034 55.433  -27.015 1.00 15.36 ? 838  GLU A CA  1 
ATOM   6701 C  C   . GLU A 1 838  ? 23.754 54.702  -27.357 1.00 14.57 ? 838  GLU A C   1 
ATOM   6702 O  O   . GLU A 1 838  ? 22.876 54.504  -26.539 1.00 15.06 ? 838  GLU A O   1 
ATOM   6703 C  CB  . GLU A 1 838  ? 26.158 54.398  -27.015 1.00 15.74 ? 838  GLU A CB  1 
ATOM   6704 C  CG  . GLU A 1 838  ? 25.937 53.265  -25.982 1.00 16.36 ? 838  GLU A CG  1 
ATOM   6705 C  CD  . GLU A 1 838  ? 27.054 52.204  -25.965 1.00 19.17 ? 838  GLU A CD  1 
ATOM   6706 O  OE1 . GLU A 1 838  ? 28.061 52.337  -26.675 1.00 18.62 ? 838  GLU A OE1 1 
ATOM   6707 O  OE2 . GLU A 1 838  ? 26.901 51.186  -25.243 1.00 20.97 ? 838  GLU A OE2 1 
ATOM   6708 N  N   . ASP A 1 839  ? 23.637 54.393  -28.649 1.00 16.12 ? 839  ASP A N   1 
ATOM   6709 C  CA  . ASP A 1 839  ? 22.535 53.525  -29.101 1.00 16.48 ? 839  ASP A CA  1 
ATOM   6710 C  C   . ASP A 1 839  ? 23.230 52.443  -29.905 1.00 17.30 ? 839  ASP A C   1 
ATOM   6711 O  O   . ASP A 1 839  ? 24.429 52.232  -29.776 1.00 18.58 ? 839  ASP A O   1 
ATOM   6712 C  CB  . ASP A 1 839  ? 21.432 54.248  -29.907 1.00 15.66 ? 839  ASP A CB  1 
ATOM   6713 C  CG  . ASP A 1 839  ? 21.937 54.982  -31.171 1.00 15.22 ? 839  ASP A CG  1 
ATOM   6714 O  OD1 . ASP A 1 839  ? 22.956 54.583  -31.758 1.00 18.21 ? 839  ASP A OD1 1 
ATOM   6715 O  OD2 . ASP A 1 839  ? 21.234 55.976  -31.512 1.00 21.33 ? 839  ASP A OD2 1 
ATOM   6716 N  N   . ALA A 1 840  ? 22.490 51.714  -30.744 1.00 16.95 ? 840  ALA A N   1 
ATOM   6717 C  CA  . ALA A 1 840  ? 23.117 50.654  -31.490 1.00 19.20 ? 840  ALA A CA  1 
ATOM   6718 C  C   . ALA A 1 840  ? 24.220 51.100  -32.414 1.00 16.97 ? 840  ALA A C   1 
ATOM   6719 O  O   . ALA A 1 840  ? 25.175 50.377  -32.659 1.00 19.56 ? 840  ALA A O   1 
ATOM   6720 C  CB  . ALA A 1 840  ? 22.043 49.889  -32.318 1.00 20.41 ? 840  ALA A CB  1 
ATOM   6721 N  N   . ASN A 1 841  ? 24.098 52.326  -32.918 1.00 17.99 ? 841  ASN A N   1 
ATOM   6722 C  CA  . ASN A 1 841  ? 25.050 52.800  -33.899 1.00 17.53 ? 841  ASN A CA  1 
ATOM   6723 C  C   . ASN A 1 841  ? 25.991 53.936  -33.563 1.00 15.55 ? 841  ASN A C   1 
ATOM   6724 O  O   . ASN A 1 841  ? 27.052 54.031  -34.177 1.00 17.79 ? 841  ASN A O   1 
ATOM   6725 C  CB  . ASN A 1 841  ? 24.293 53.239  -35.174 1.00 19.79 ? 841  ASN A CB  1 
ATOM   6726 C  CG  . ASN A 1 841  ? 23.564 52.087  -35.864 1.00 21.77 ? 841  ASN A CG  1 
ATOM   6727 O  OD1 . ASN A 1 841  ? 24.095 50.988  -35.982 1.00 24.54 ? 841  ASN A OD1 1 
ATOM   6728 N  ND2 . ASN A 1 841  ? 22.365 52.363  -36.342 1.00 24.76 ? 841  ASN A ND2 1 
ATOM   6729 N  N   . THR A 1 842  ? 25.583 54.789  -32.633 1.00 16.02 ? 842  THR A N   1 
ATOM   6730 C  CA  . THR A 1 842  ? 26.335 55.996  -32.383 1.00 16.06 ? 842  THR A CA  1 
ATOM   6731 C  C   . THR A 1 842  ? 26.598 56.185  -30.904 1.00 15.06 ? 842  THR A C   1 
ATOM   6732 O  O   . THR A 1 842  ? 25.738 55.885  -30.079 1.00 16.88 ? 842  THR A O   1 
ATOM   6733 C  CB  . THR A 1 842  ? 25.511 57.213  -32.878 1.00 17.66 ? 842  THR A CB  1 
ATOM   6734 O  OG1 . THR A 1 842  ? 25.073 57.000  -34.239 1.00 18.13 ? 842  THR A OG1 1 
ATOM   6735 C  CG2 . THR A 1 842  ? 26.354 58.472  -32.873 1.00 17.57 ? 842  THR A CG2 1 
ATOM   6736 N  N   . ARG A 1 843  ? 27.768 56.732  -30.623 1.00 14.43 ? 843  ARG A N   1 
ATOM   6737 C  CA  . ARG A 1 843  ? 28.144 57.059  -29.253 1.00 15.16 ? 843  ARG A CA  1 
ATOM   6738 C  C   . ARG A 1 843  ? 28.707 58.483  -29.194 1.00 14.28 ? 843  ARG A C   1 
ATOM   6739 O  O   . ARG A 1 843  ? 29.420 58.942  -30.131 1.00 15.40 ? 843  ARG A O   1 
ATOM   6740 C  CB  . ARG A 1 843  ? 29.210 56.100  -28.742 1.00 15.93 ? 843  ARG A CB  1 
ATOM   6741 C  CG  . ARG A 1 843  ? 29.589 56.403  -27.231 1.00 13.60 ? 843  ARG A CG  1 
ATOM   6742 C  CD  . ARG A 1 843  ? 30.767 55.546  -26.814 1.00 13.89 ? 843  ARG A CD  1 
ATOM   6743 N  NE  . ARG A 1 843  ? 30.390 54.156  -26.527 1.00 14.65 ? 843  ARG A NE  1 
ATOM   6744 C  CZ  . ARG A 1 843  ? 31.206 53.317  -25.913 1.00 15.31 ? 843  ARG A CZ  1 
ATOM   6745 N  NH1 . ARG A 1 843  ? 32.425 53.718  -25.567 1.00 14.63 ? 843  ARG A NH1 1 
ATOM   6746 N  NH2 . ARG A 1 843  ? 30.761 52.111  -25.562 1.00 15.59 ? 843  ARG A NH2 1 
ATOM   6747 N  N   . LEU A 1 844  ? 28.325 59.172  -28.127 1.00 13.42 ? 844  LEU A N   1 
ATOM   6748 C  CA  . LEU A 1 844  ? 28.870 60.521  -27.849 1.00 13.04 ? 844  LEU A CA  1 
ATOM   6749 C  C   . LEU A 1 844  ? 29.532 60.418  -26.466 1.00 12.46 ? 844  LEU A C   1 
ATOM   6750 O  O   . LEU A 1 844  ? 28.837 60.109  -25.485 1.00 14.19 ? 844  LEU A O   1 
ATOM   6751 C  CB  . LEU A 1 844  ? 27.793 61.612  -27.823 1.00 13.85 ? 844  LEU A CB  1 
ATOM   6752 C  CG  . LEU A 1 844  ? 28.470 63.006  -27.702 1.00 15.01 ? 844  LEU A CG  1 
ATOM   6753 C  CD1 . LEU A 1 844  ? 29.360 63.321  -28.914 1.00 15.98 ? 844  LEU A CD1 1 
ATOM   6754 C  CD2 . LEU A 1 844  ? 27.404 64.084  -27.538 1.00 16.72 ? 844  LEU A CD2 1 
ATOM   6755 N  N   . THR A 1 845  ? 30.826 60.734  -26.441 1.00 13.31 ? 845  THR A N   1 
ATOM   6756 C  CA  . THR A 1 845  ? 31.600 60.659  -25.173 1.00 13.12 ? 845  THR A CA  1 
ATOM   6757 C  C   . THR A 1 845  ? 32.152 62.036  -24.881 1.00 13.38 ? 845  THR A C   1 
ATOM   6758 O  O   . THR A 1 845  ? 32.777 62.660  -25.758 1.00 13.17 ? 845  THR A O   1 
ATOM   6759 C  CB  . THR A 1 845  ? 32.798 59.708  -25.282 1.00 11.34 ? 845  THR A CB  1 
ATOM   6760 O  OG1 . THR A 1 845  ? 32.329 58.400  -25.672 1.00 13.38 ? 845  THR A OG1 1 
ATOM   6761 C  CG2 . THR A 1 845  ? 33.443 59.517  -23.924 1.00 13.76 ? 845  THR A CG2 1 
ATOM   6762 N  N   . LEU A 1 846  ? 31.939 62.493  -23.656 1.00 13.79 ? 846  LEU A N   1 
ATOM   6763 C  CA  . LEU A 1 846  ? 32.459 63.786  -23.206 1.00 12.15 ? 846  LEU A CA  1 
ATOM   6764 C  C   . LEU A 1 846  ? 33.514 63.450  -22.133 1.00 11.00 ? 846  LEU A C   1 
ATOM   6765 O  O   . LEU A 1 846  ? 33.168 62.864  -21.086 1.00 12.18 ? 846  LEU A O   1 
ATOM   6766 C  CB  . LEU A 1 846  ? 31.348 64.661  -22.598 1.00 15.11 ? 846  LEU A CB  1 
ATOM   6767 C  CG  . LEU A 1 846  ? 31.808 66.045  -22.079 1.00 14.54 ? 846  LEU A CG  1 
ATOM   6768 C  CD1 . LEU A 1 846  ? 32.308 66.907  -23.275 1.00 14.90 ? 846  LEU A CD1 1 
ATOM   6769 C  CD2 . LEU A 1 846  ? 30.683 66.757  -21.336 1.00 17.16 ? 846  LEU A CD2 1 
ATOM   6770 N  N   . LEU A 1 847  ? 34.780 63.752  -22.414 1.00 11.99 ? 847  LEU A N   1 
ATOM   6771 C  CA  . LEU A 1 847  ? 35.859 63.515  -21.426 1.00 9.76  ? 847  LEU A CA  1 
ATOM   6772 C  C   . LEU A 1 847  ? 36.107 64.837  -20.722 1.00 12.52 ? 847  LEU A C   1 
ATOM   6773 O  O   . LEU A 1 847  ? 35.988 65.909  -21.335 1.00 12.74 ? 847  LEU A O   1 
ATOM   6774 C  CB  . LEU A 1 847  ? 37.134 63.063  -22.098 1.00 11.58 ? 847  LEU A CB  1 
ATOM   6775 C  CG  . LEU A 1 847  ? 37.168 61.720  -22.838 1.00 10.33 ? 847  LEU A CG  1 
ATOM   6776 C  CD1 . LEU A 1 847  ? 36.555 60.614  -21.958 1.00 12.86 ? 847  LEU A CD1 1 
ATOM   6777 C  CD2 . LEU A 1 847  ? 36.424 61.823  -24.170 1.00 12.53 ? 847  LEU A CD2 1 
ATOM   6778 N  N   . THR A 1 848  ? 36.475 64.779  -19.445 1.00 11.15 ? 848  THR A N   1 
ATOM   6779 C  CA  . THR A 1 848  ? 36.730 65.997  -18.654 1.00 11.61 ? 848  THR A CA  1 
ATOM   6780 C  C   . THR A 1 848  ? 38.129 66.076  -18.040 1.00 13.78 ? 848  THR A C   1 
ATOM   6781 O  O   . THR A 1 848  ? 38.793 65.051  -17.772 1.00 13.29 ? 848  THR A O   1 
ATOM   6782 C  CB  . THR A 1 848  ? 35.739 66.095  -17.476 1.00 14.79 ? 848  THR A CB  1 
ATOM   6783 O  OG1 . THR A 1 848  ? 36.136 65.147  -16.447 1.00 17.01 ? 848  THR A OG1 1 
ATOM   6784 C  CG2 . THR A 1 848  ? 34.381 65.774  -17.889 1.00 14.94 ? 848  THR A CG2 1 
ATOM   6785 N  N   . GLY A 1 849  ? 38.588 67.318  -17.896 1.00 11.59 ? 849  GLY A N   1 
ATOM   6786 C  CA  . GLY A 1 849  ? 39.858 67.565  -17.238 1.00 11.60 ? 849  GLY A CA  1 
ATOM   6787 C  C   . GLY A 1 849  ? 39.691 67.923  -15.782 1.00 10.89 ? 849  GLY A C   1 
ATOM   6788 O  O   . GLY A 1 849  ? 40.642 68.378  -15.153 1.00 11.51 ? 849  GLY A O   1 
ATOM   6789 N  N   . GLN A 1 850  ? 38.500 67.721  -15.237 1.00 11.56 ? 850  GLN A N   1 
ATOM   6790 C  CA  . GLN A 1 850  ? 38.198 68.045  -13.851 1.00 10.36 ? 850  GLN A CA  1 
ATOM   6791 C  C   . GLN A 1 850  ? 36.922 67.308  -13.456 1.00 10.73 ? 850  GLN A C   1 
ATOM   6792 O  O   . GLN A 1 850  ? 36.021 67.106  -14.286 1.00 11.37 ? 850  GLN A O   1 
ATOM   6793 C  CB  . GLN A 1 850  ? 37.978 69.578  -13.689 1.00 11.55 ? 850  GLN A CB  1 
ATOM   6794 C  CG  . GLN A 1 850  ? 36.847 70.153  -14.628 1.00 11.61 ? 850  GLN A CG  1 
ATOM   6795 C  CD  . GLN A 1 850  ? 37.204 70.223  -16.072 1.00 13.03 ? 850  GLN A CD  1 
ATOM   6796 O  OE1 . GLN A 1 850  ? 38.296 70.624  -16.448 1.00 13.54 ? 850  GLN A OE1 1 
ATOM   6797 N  NE2 . GLN A 1 850  ? 36.232 69.880  -16.933 1.00 11.40 ? 850  GLN A NE2 1 
ATOM   6798 N  N   . PRO A 1 851  ? 36.809 66.895  -12.194 1.00 10.02 ? 851  PRO A N   1 
ATOM   6799 C  CA  . PRO A 1 851  ? 35.577 66.198  -11.780 1.00 10.71 ? 851  PRO A CA  1 
ATOM   6800 C  C   . PRO A 1 851  ? 34.452 67.181  -11.607 1.00 11.20 ? 851  PRO A C   1 
ATOM   6801 O  O   . PRO A 1 851  ? 34.645 68.219  -10.955 1.00 11.59 ? 851  PRO A O   1 
ATOM   6802 C  CB  . PRO A 1 851  ? 35.970 65.538  -10.443 1.00 11.41 ? 851  PRO A CB  1 
ATOM   6803 C  CG  . PRO A 1 851  ? 37.058 66.492  -9.898  1.00 10.94 ? 851  PRO A CG  1 
ATOM   6804 C  CD  . PRO A 1 851  ? 37.837 66.930  -11.129 1.00 10.39 ? 851  PRO A CD  1 
ATOM   6805 N  N   . LEU A 1 852  ? 33.285 66.855  -12.186 1.00 10.77 ? 852  LEU A N   1 
ATOM   6806 C  CA  . LEU A 1 852  ? 32.089 67.706  -12.070 1.00 13.10 ? 852  LEU A CA  1 
ATOM   6807 C  C   . LEU A 1 852  ? 30.877 66.795  -11.959 1.00 13.91 ? 852  LEU A C   1 
ATOM   6808 O  O   . LEU A 1 852  ? 31.009 65.595  -12.193 1.00 16.67 ? 852  LEU A O   1 
ATOM   6809 C  CB  . LEU A 1 852  ? 31.948 68.603  -13.309 1.00 13.19 ? 852  LEU A CB  1 
ATOM   6810 C  CG  . LEU A 1 852  ? 33.107 69.617  -13.453 1.00 12.44 ? 852  LEU A CG  1 
ATOM   6811 C  CD1 . LEU A 1 852  ? 33.064 70.195  -14.917 1.00 15.03 ? 852  LEU A CD1 1 
ATOM   6812 C  CD2 . LEU A 1 852  ? 33.035 70.748  -12.404 1.00 12.63 ? 852  LEU A CD2 1 
ATOM   6813 N  N   . GLY A 1 853  ? 29.726 67.330  -11.598 1.00 11.68 ? 853  GLY A N   1 
ATOM   6814 C  CA  . GLY A 1 853  ? 28.544 66.478  -11.551 1.00 12.01 ? 853  GLY A CA  1 
ATOM   6815 C  C   . GLY A 1 853  ? 27.790 66.464  -12.867 1.00 11.82 ? 853  GLY A C   1 
ATOM   6816 O  O   . GLY A 1 853  ? 27.832 67.454  -13.611 1.00 12.60 ? 853  GLY A O   1 
ATOM   6817 N  N   . GLY A 1 854  ? 27.080 65.394  -13.164 1.00 10.95 ? 854  GLY A N   1 
ATOM   6818 C  CA  . GLY A 1 854  ? 26.360 65.358  -14.434 1.00 12.80 ? 854  GLY A CA  1 
ATOM   6819 C  C   . GLY A 1 854  ? 25.337 64.259  -14.536 1.00 11.36 ? 854  GLY A C   1 
ATOM   6820 O  O   . GLY A 1 854  ? 25.166 63.418  -13.620 1.00 13.42 ? 854  GLY A O   1 
ATOM   6821 N  N   . SER A 1 855  ? 24.666 64.220  -15.692 1.00 12.87 ? 855  SER A N   1 
ATOM   6822 C  CA  . SER A 1 855  ? 23.606 63.231  -15.879 1.00 12.28 ? 855  SER A CA  1 
ATOM   6823 C  C   . SER A 1 855  ? 23.205 63.187  -17.317 1.00 13.97 ? 855  SER A C   1 
ATOM   6824 O  O   . SER A 1 855  ? 23.815 63.828  -18.156 1.00 14.79 ? 855  SER A O   1 
ATOM   6825 C  CB  . SER A 1 855  ? 22.380 63.675  -15.068 1.00 14.13 ? 855  SER A CB  1 
ATOM   6826 O  OG  . SER A 1 855  ? 21.364 62.670  -15.039 1.00 14.75 ? 855  SER A OG  1 
ATOM   6827 N  N   . SER A 1 856  ? 22.194 62.355  -17.582 1.00 14.00 ? 856  SER A N   1 
ATOM   6828 C  CA  . SER A 1 856  ? 21.536 62.292  -18.907 1.00 14.86 ? 856  SER A CA  1 
ATOM   6829 C  C   . SER A 1 856  ? 20.075 62.286  -18.461 1.00 14.78 ? 856  SER A C   1 
ATOM   6830 O  O   . SER A 1 856  ? 19.548 61.232  -18.073 1.00 16.37 ? 856  SER A O   1 
ATOM   6831 C  CB  . SER A 1 856  ? 21.869 61.002  -19.629 1.00 14.24 ? 856  SER A CB  1 
ATOM   6832 O  OG  . SER A 1 856  ? 21.091 60.962  -20.847 1.00 15.76 ? 856  SER A OG  1 
ATOM   6833 N  N   . LEU A 1 857  ? 19.400 63.446  -18.502 1.00 15.61 ? 857  LEU A N   1 
ATOM   6834 C  CA  . LEU A 1 857  ? 18.028 63.560  -17.982 1.00 14.30 ? 857  LEU A CA  1 
ATOM   6835 C  C   . LEU A 1 857  ? 16.932 63.237  -18.989 1.00 16.41 ? 857  LEU A C   1 
ATOM   6836 O  O   . LEU A 1 857  ? 15.767 63.185  -18.646 1.00 19.17 ? 857  LEU A O   1 
ATOM   6837 C  CB  . LEU A 1 857  ? 17.809 64.963  -17.359 1.00 15.35 ? 857  LEU A CB  1 
ATOM   6838 C  CG  . LEU A 1 857  ? 18.670 65.203  -16.126 1.00 16.75 ? 857  LEU A CG  1 
ATOM   6839 C  CD1 . LEU A 1 857  ? 18.473 66.647  -15.669 1.00 16.99 ? 857  LEU A CD1 1 
ATOM   6840 C  CD2 . LEU A 1 857  ? 18.270 64.242  -14.977 1.00 17.92 ? 857  LEU A CD2 1 
ATOM   6841 N  N   . ALA A 1 858  ? 17.356 63.012  -20.201 1.00 14.87 ? 858  ALA A N   1 
ATOM   6842 C  CA  . ALA A 1 858  ? 16.457 62.617  -21.298 1.00 15.46 ? 858  ALA A CA  1 
ATOM   6843 C  C   . ALA A 1 858  ? 17.276 61.918  -22.356 1.00 17.36 ? 858  ALA A C   1 
ATOM   6844 O  O   . ALA A 1 858  ? 18.479 62.142  -22.513 1.00 17.26 ? 858  ALA A O   1 
ATOM   6845 C  CB  . ALA A 1 858  ? 15.749 63.845  -21.888 1.00 16.28 ? 858  ALA A CB  1 
ATOM   6846 N  N   . SER A 1 859  ? 16.628 61.029  -23.103 1.00 16.29 ? 859  SER A N   1 
ATOM   6847 C  CA  . SER A 1 859  ? 17.284 60.287  -24.153 1.00 14.72 ? 859  SER A CA  1 
ATOM   6848 C  C   . SER A 1 859  ? 18.030 61.243  -25.085 1.00 16.27 ? 859  SER A C   1 
ATOM   6849 O  O   . SER A 1 859  ? 17.496 62.291  -25.455 1.00 17.76 ? 859  SER A O   1 
ATOM   6850 C  CB  . SER A 1 859  ? 16.227 59.444  -24.965 1.00 15.99 ? 859  SER A CB  1 
ATOM   6851 O  OG  . SER A 1 859  ? 16.835 58.678  -25.963 1.00 18.15 ? 859  SER A OG  1 
ATOM   6852 N  N   . GLY A 1 860  ? 19.246 60.874  -25.447 1.00 16.22 ? 860  GLY A N   1 
ATOM   6853 C  CA  . GLY A 1 860  ? 20.039 61.689  -26.354 1.00 15.24 ? 860  GLY A CA  1 
ATOM   6854 C  C   . GLY A 1 860  ? 20.774 62.842  -25.670 1.00 14.65 ? 860  GLY A C   1 
ATOM   6855 O  O   . GLY A 1 860  ? 21.548 63.511  -26.374 1.00 14.80 ? 860  GLY A O   1 
ATOM   6856 N  N   . GLU A 1 861  ? 20.612 63.053  -24.366 1.00 15.00 ? 861  GLU A N   1 
ATOM   6857 C  CA  . GLU A 1 861  ? 21.296 64.158  -23.714 1.00 15.37 ? 861  GLU A CA  1 
ATOM   6858 C  C   . GLU A 1 861  ? 22.437 63.759  -22.805 1.00 16.59 ? 861  GLU A C   1 
ATOM   6859 O  O   . GLU A 1 861  ? 22.494 62.649  -22.250 1.00 15.91 ? 861  GLU A O   1 
ATOM   6860 C  CB  . GLU A 1 861  ? 20.369 64.956  -22.816 1.00 17.01 ? 861  GLU A CB  1 
ATOM   6861 C  CG  . GLU A 1 861  ? 19.208 65.588  -23.536 1.00 17.74 ? 861  GLU A CG  1 
ATOM   6862 C  CD  . GLU A 1 861  ? 18.297 66.415  -22.630 1.00 18.56 ? 861  GLU A CD  1 
ATOM   6863 O  OE1 . GLU A 1 861  ? 18.458 66.481  -21.396 1.00 18.47 ? 861  GLU A OE1 1 
ATOM   6864 O  OE2 . GLU A 1 861  ? 17.329 67.030  -23.191 1.00 22.06 ? 861  GLU A OE2 1 
ATOM   6865 N  N   . LEU A 1 862  ? 23.326 64.714  -22.650 1.00 14.05 ? 862  LEU A N   1 
ATOM   6866 C  CA  . LEU A 1 862  ? 24.413 64.603  -21.645 1.00 13.78 ? 862  LEU A CA  1 
ATOM   6867 C  C   . LEU A 1 862  ? 24.448 65.970  -21.022 1.00 13.65 ? 862  LEU A C   1 
ATOM   6868 O  O   . LEU A 1 862  ? 24.271 66.976  -21.720 1.00 14.97 ? 862  LEU A O   1 
ATOM   6869 C  CB  . LEU A 1 862  ? 25.806 64.334  -22.283 1.00 14.34 ? 862  LEU A CB  1 
ATOM   6870 C  CG  . LEU A 1 862  ? 26.123 62.952  -22.902 1.00 15.02 ? 862  LEU A CG  1 
ATOM   6871 C  CD1 . LEU A 1 862  ? 27.478 62.974  -23.636 1.00 16.05 ? 862  LEU A CD1 1 
ATOM   6872 C  CD2 . LEU A 1 862  ? 26.081 61.914  -21.802 1.00 15.50 ? 862  LEU A CD2 1 
ATOM   6873 N  N   . GLU A 1 863  ? 24.722 66.068  -19.733 1.00 12.69 ? 863  GLU A N   1 
ATOM   6874 C  CA  . GLU A 1 863  ? 24.884 67.388  -19.139 1.00 11.75 ? 863  GLU A CA  1 
ATOM   6875 C  C   . GLU A 1 863  ? 25.843 67.327  -17.989 1.00 13.26 ? 863  GLU A C   1 
ATOM   6876 O  O   . GLU A 1 863  ? 25.976 66.295  -17.330 1.00 12.83 ? 863  GLU A O   1 
ATOM   6877 C  CB  . GLU A 1 863  ? 23.566 68.024  -18.696 1.00 13.12 ? 863  GLU A CB  1 
ATOM   6878 C  CG  . GLU A 1 863  ? 22.949 67.450  -17.439 1.00 14.58 ? 863  GLU A CG  1 
ATOM   6879 C  CD  . GLU A 1 863  ? 21.666 68.203  -17.073 1.00 14.26 ? 863  GLU A CD  1 
ATOM   6880 O  OE1 . GLU A 1 863  ? 20.761 68.250  -17.948 1.00 16.60 ? 863  GLU A OE1 1 
ATOM   6881 O  OE2 . GLU A 1 863  ? 21.547 68.726  -15.958 1.00 15.27 ? 863  GLU A OE2 1 
ATOM   6882 N  N   . ILE A 1 864  ? 26.558 68.432  -17.804 1.00 13.02 ? 864  ILE A N   1 
ATOM   6883 C  CA  . ILE A 1 864  ? 27.596 68.475  -16.763 1.00 13.85 ? 864  ILE A CA  1 
ATOM   6884 C  C   . ILE A 1 864  ? 27.611 69.872  -16.178 1.00 14.02 ? 864  ILE A C   1 
ATOM   6885 O  O   . ILE A 1 864  ? 27.612 70.890  -16.904 1.00 14.14 ? 864  ILE A O   1 
ATOM   6886 C  CB  . ILE A 1 864  ? 28.961 68.049  -17.362 1.00 12.83 ? 864  ILE A CB  1 
ATOM   6887 C  CG1 . ILE A 1 864  ? 30.036 67.967  -16.256 1.00 15.30 ? 864  ILE A CG1 1 
ATOM   6888 C  CG2 . ILE A 1 864  ? 29.386 68.976  -18.481 1.00 17.78 ? 864  ILE A CG2 1 
ATOM   6889 C  CD1 . ILE A 1 864  ? 31.196 67.082  -16.777 1.00 16.68 ? 864  ILE A CD1 1 
ATOM   6890 N  N   . MET A 1 865  ? 27.567 69.920  -14.856 1.00 12.58 ? 865  MET A N   1 
ATOM   6891 C  CA  . MET A 1 865  ? 27.509 71.190  -14.146 1.00 13.10 ? 865  MET A CA  1 
ATOM   6892 C  C   . MET A 1 865  ? 28.886 71.901  -14.192 1.00 14.10 ? 865  MET A C   1 
ATOM   6893 O  O   . MET A 1 865  ? 29.933 71.278  -14.005 1.00 13.40 ? 865  MET A O   1 
ATOM   6894 C  CB  . MET A 1 865  ? 27.026 70.947  -12.696 1.00 12.46 ? 865  MET A CB  1 
ATOM   6895 C  CG  . MET A 1 865  ? 26.440 72.175  -11.991 1.00 11.74 ? 865  MET A CG  1 
ATOM   6896 S  SD  . MET A 1 865  ? 24.841 72.622  -12.763 1.00 15.44 ? 865  MET A SD  1 
ATOM   6897 C  CE  . MET A 1 865  ? 23.825 71.422  -11.848 1.00 13.61 ? 865  MET A CE  1 
ATOM   6898 N  N   . GLN A 1 866  ? 28.859 73.226  -14.413 1.00 13.07 ? 866  GLN A N   1 
ATOM   6899 C  CA  . GLN A 1 866  ? 30.078 74.042  -14.542 1.00 12.45 ? 866  GLN A CA  1 
ATOM   6900 C  C   . GLN A 1 866  ? 30.464 74.743  -13.238 1.00 12.25 ? 866  GLN A C   1 
ATOM   6901 O  O   . GLN A 1 866  ? 31.644 74.762  -12.871 1.00 13.78 ? 866  GLN A O   1 
ATOM   6902 C  CB  . GLN A 1 866  ? 29.861 75.076  -15.647 1.00 13.27 ? 866  GLN A CB  1 
ATOM   6903 C  CG  . GLN A 1 866  ? 29.559 74.469  -16.983 1.00 14.38 ? 866  GLN A CG  1 
ATOM   6904 C  CD  . GLN A 1 866  ? 30.603 73.480  -17.403 1.00 13.99 ? 866  GLN A CD  1 
ATOM   6905 O  OE1 . GLN A 1 866  ? 31.734 73.845  -17.772 1.00 14.47 ? 866  GLN A OE1 1 
ATOM   6906 N  NE2 . GLN A 1 866  ? 30.240 72.210  -17.367 1.00 13.68 ? 866  GLN A NE2 1 
ATOM   6907 N  N   . ASP A 1 867  ? 29.483 75.332  -12.533 1.00 12.74 ? 867  ASP A N   1 
ATOM   6908 C  CA  . ASP A 1 867  ? 29.724 75.965  -11.234 1.00 12.39 ? 867  ASP A CA  1 
ATOM   6909 C  C   . ASP A 1 867  ? 28.388 76.196  -10.581 1.00 14.17 ? 867  ASP A C   1 
ATOM   6910 O  O   . ASP A 1 867  ? 27.320 76.098  -11.237 1.00 13.11 ? 867  ASP A O   1 
ATOM   6911 C  CB  . ASP A 1 867  ? 30.495 77.301  -11.356 1.00 14.05 ? 867  ASP A CB  1 
ATOM   6912 C  CG  . ASP A 1 867  ? 31.244 77.680  -10.066 1.00 13.94 ? 867  ASP A CG  1 
ATOM   6913 O  OD1 . ASP A 1 867  ? 31.113 77.019  -9.023  1.00 14.43 ? 867  ASP A OD1 1 
ATOM   6914 O  OD2 . ASP A 1 867  ? 31.984 78.681  -10.110 1.00 14.99 ? 867  ASP A OD2 1 
ATOM   6915 N  N   . ARG A 1 868  ? 28.443 76.471  -9.297  1.00 12.95 ? 868  ARG A N   1 
ATOM   6916 C  CA  . ARG A 1 868  ? 27.236 76.693  -8.512  1.00 13.96 ? 868  ARG A CA  1 
ATOM   6917 C  C   . ARG A 1 868  ? 27.553 77.707  -7.420  1.00 14.07 ? 868  ARG A C   1 
ATOM   6918 O  O   . ARG A 1 868  ? 28.608 77.644  -6.764  1.00 14.78 ? 868  ARG A O   1 
ATOM   6919 C  CB  . ARG A 1 868  ? 26.736 75.345  -7.949  1.00 14.63 ? 868  ARG A CB  1 
ATOM   6920 C  CG  . ARG A 1 868  ? 27.770 74.584  -7.077  1.00 16.63 ? 868  ARG A CG  1 
ATOM   6921 C  CD  . ARG A 1 868  ? 27.477 73.074  -7.086  1.00 13.73 ? 868  ARG A CD  1 
ATOM   6922 N  NE  . ARG A 1 868  ? 26.107 72.791  -6.659  1.00 13.75 ? 868  ARG A NE  1 
ATOM   6923 C  CZ  . ARG A 1 868  ? 25.754 72.509  -5.421  1.00 13.79 ? 868  ARG A CZ  1 
ATOM   6924 N  NH1 . ARG A 1 868  ? 26.657 72.421  -4.425  1.00 12.86 ? 868  ARG A NH1 1 
ATOM   6925 N  NH2 . ARG A 1 868  ? 24.450 72.334  -5.171  1.00 14.87 ? 868  ARG A NH2 1 
ATOM   6926 N  N   . ARG A 1 869  ? 26.637 78.667  -7.239  1.00 14.83 ? 869  ARG A N   1 
ATOM   6927 C  CA  . ARG A 1 869  ? 26.812 79.741  -6.245  1.00 14.12 ? 869  ARG A CA  1 
ATOM   6928 C  C   . ARG A 1 869  ? 25.527 79.721  -5.455  1.00 16.60 ? 869  ARG A C   1 
ATOM   6929 O  O   . ARG A 1 869  ? 24.459 79.912  -6.009  1.00 16.63 ? 869  ARG A O   1 
ATOM   6930 C  CB  . ARG A 1 869  ? 27.023 81.085  -6.971  1.00 14.74 ? 869  ARG A CB  1 
ATOM   6931 C  CG  . ARG A 1 869  ? 27.245 82.211  -6.012  1.00 15.40 ? 869  ARG A CG  1 
ATOM   6932 C  CD  . ARG A 1 869  ? 27.526 83.511  -6.757  1.00 19.77 ? 869  ARG A CD  1 
ATOM   6933 N  NE  . ARG A 1 869  ? 27.712 84.659  -5.849  1.00 22.83 ? 869  ARG A NE  1 
ATOM   6934 C  CZ  . ARG A 1 869  ? 28.866 84.993  -5.293  1.00 21.33 ? 869  ARG A CZ  1 
ATOM   6935 N  NH1 . ARG A 1 869  ? 29.964 84.288  -5.535  1.00 20.03 ? 869  ARG A NH1 1 
ATOM   6936 N  NH2 . ARG A 1 869  ? 28.914 86.061  -4.485  1.00 24.85 ? 869  ARG A NH2 1 
ATOM   6937 N  N   . LEU A 1 870  ? 25.671 79.464  -4.169  1.00 16.35 ? 870  LEU A N   1 
ATOM   6938 C  CA  . LEU A 1 870  ? 24.531 79.229  -3.260  1.00 17.61 ? 870  LEU A CA  1 
ATOM   6939 C  C   . LEU A 1 870  ? 24.602 80.046  -2.001  1.00 18.06 ? 870  LEU A C   1 
ATOM   6940 O  O   . LEU A 1 870  ? 25.577 80.002  -1.266  1.00 17.90 ? 870  LEU A O   1 
ATOM   6941 C  CB  . LEU A 1 870  ? 24.502 77.736  -2.906  1.00 18.63 ? 870  LEU A CB  1 
ATOM   6942 C  CG  . LEU A 1 870  ? 24.556 76.864  -4.161  1.00 21.89 ? 870  LEU A CG  1 
ATOM   6943 C  CD1 . LEU A 1 870  ? 25.102 75.538  -3.819  1.00 22.51 ? 870  LEU A CD1 1 
ATOM   6944 C  CD2 . LEU A 1 870  ? 23.217 76.805  -4.844  1.00 18.40 ? 870  LEU A CD2 1 
ATOM   6945 N  N   . ALA A 1 871  ? 23.517 80.762  -1.732  1.00 18.64 ? 871  ALA A N   1 
ATOM   6946 C  CA  . ALA A 1 871  ? 23.501 81.638  -0.588  1.00 20.76 ? 871  ALA A CA  1 
ATOM   6947 C  C   . ALA A 1 871  ? 23.294 80.962  0.763   1.00 24.19 ? 871  ALA A C   1 
ATOM   6948 O  O   . ALA A 1 871  ? 23.766 81.437  1.798   1.00 25.31 ? 871  ALA A O   1 
ATOM   6949 C  CB  . ALA A 1 871  ? 22.406 82.714  -0.805  1.00 22.60 ? 871  ALA A CB  1 
ATOM   6950 N  N   . SER A 1 872  ? 22.645 79.815  0.748   1.00 22.79 ? 872  SER A N   1 
ATOM   6951 C  CA  . SER A 1 872  ? 22.329 79.175  2.012   1.00 24.49 ? 872  SER A CA  1 
ATOM   6952 C  C   . SER A 1 872  ? 23.166 77.980  2.377   1.00 21.81 ? 872  SER A C   1 
ATOM   6953 O  O   . SER A 1 872  ? 23.777 77.334  1.510   1.00 20.85 ? 872  SER A O   1 
ATOM   6954 C  CB  . SER A 1 872  ? 20.858 78.738  2.010   1.00 28.59 ? 872  SER A CB  1 
ATOM   6955 O  OG  . SER A 1 872  ? 19.999 79.805  1.634   1.00 32.86 ? 872  SER A OG  1 
ATOM   6956 N  N   . ASP A 1 873  ? 23.211 77.723  3.677   1.00 22.17 ? 873  ASP A N   1 
ATOM   6957 C  CA  . ASP A 1 873  ? 23.876 76.543  4.244   1.00 21.01 ? 873  ASP A CA  1 
ATOM   6958 C  C   . ASP A 1 873  ? 22.852 75.407  4.076   1.00 22.45 ? 873  ASP A C   1 
ATOM   6959 O  O   . ASP A 1 873  ? 21.639 75.654  4.092   1.00 22.43 ? 873  ASP A O   1 
ATOM   6960 C  CB  . ASP A 1 873  ? 24.181 76.750  5.723   1.00 21.04 ? 873  ASP A CB  1 
ATOM   6961 C  CG  . ASP A 1 873  ? 24.676 75.483  6.378   1.00 20.99 ? 873  ASP A CG  1 
ATOM   6962 O  OD1 . ASP A 1 873  ? 25.769 75.005  5.973   1.00 20.79 ? 873  ASP A OD1 1 
ATOM   6963 O  OD2 . ASP A 1 873  ? 23.967 74.951  7.255   1.00 23.24 ? 873  ASP A OD2 1 
ATOM   6964 N  N   . ASP A 1 874  ? 23.345 74.179  3.865   1.00 19.24 ? 874  ASP A N   1 
ATOM   6965 C  CA  . ASP A 1 874  ? 22.448 73.041  3.669   1.00 17.39 ? 874  ASP A CA  1 
ATOM   6966 C  C   . ASP A 1 874  ? 22.383 72.072  4.858   1.00 18.01 ? 874  ASP A C   1 
ATOM   6967 O  O   . ASP A 1 874  ? 22.200 70.861  4.711   1.00 20.70 ? 874  ASP A O   1 
ATOM   6968 C  CB  . ASP A 1 874  ? 22.782 72.310  2.367   1.00 18.77 ? 874  ASP A CB  1 
ATOM   6969 C  CG  . ASP A 1 874  ? 24.249 71.939  2.257   1.00 16.50 ? 874  ASP A CG  1 
ATOM   6970 O  OD1 . ASP A 1 874  ? 25.079 72.217  3.176   1.00 19.27 ? 874  ASP A OD1 1 
ATOM   6971 O  OD2 . ASP A 1 874  ? 24.561 71.356  1.201   1.00 16.72 ? 874  ASP A OD2 1 
ATOM   6972 N  N   . GLU A 1 875  ? 22.638 72.619  6.036   1.00 19.69 ? 875  GLU A N   1 
ATOM   6973 C  CA  . GLU A 1 875  ? 22.452 71.861  7.272   1.00 20.31 ? 875  GLU A CA  1 
ATOM   6974 C  C   . GLU A 1 875  ? 23.244 70.591  7.481   1.00 21.17 ? 875  GLU A C   1 
ATOM   6975 O  O   . GLU A 1 875  ? 22.797 69.676  8.179   1.00 19.83 ? 875  GLU A O   1 
ATOM   6976 C  CB  . GLU A 1 875  ? 20.950 71.564  7.451   1.00 24.39 ? 875  GLU A CB  1 
ATOM   6977 C  CG  . GLU A 1 875  ? 20.063 72.829  7.367   1.00 31.56 ? 875  GLU A CG  1 
ATOM   6978 C  CD  . GLU A 1 875  ? 18.688 72.657  8.016   1.00 37.13 ? 875  GLU A CD  1 
ATOM   6979 O  OE1 . GLU A 1 875  ? 18.627 72.320  9.216   1.00 42.54 ? 875  GLU A OE1 1 
ATOM   6980 O  OE2 . GLU A 1 875  ? 17.664 72.859  7.328   1.00 40.36 ? 875  GLU A OE2 1 
ATOM   6981 N  N   . ARG A 1 876  ? 24.431 70.534  6.895   1.00 18.18 ? 876  ARG A N   1 
ATOM   6982 C  CA  . ARG A 1 876  ? 25.303 69.363  7.098   1.00 17.83 ? 876  ARG A CA  1 
ATOM   6983 C  C   . ARG A 1 876  ? 26.557 69.746  7.897   1.00 17.85 ? 876  ARG A C   1 
ATOM   6984 O  O   . ARG A 1 876  ? 27.555 69.017  7.916   1.00 18.77 ? 876  ARG A O   1 
ATOM   6985 C  CB  . ARG A 1 876  ? 25.656 68.734  5.745   1.00 17.90 ? 876  ARG A CB  1 
ATOM   6986 C  CG  . ARG A 1 876  ? 24.410 68.190  5.004   1.00 15.94 ? 876  ARG A CG  1 
ATOM   6987 C  CD  . ARG A 1 876  ? 23.662 67.201  5.912   1.00 16.29 ? 876  ARG A CD  1 
ATOM   6988 N  NE  . ARG A 1 876  ? 22.553 66.506  5.248   1.00 15.99 ? 876  ARG A NE  1 
ATOM   6989 C  CZ  . ARG A 1 876  ? 21.358 67.042  4.972   1.00 19.53 ? 876  ARG A CZ  1 
ATOM   6990 N  NH1 . ARG A 1 876  ? 21.094 68.329  5.259   1.00 17.81 ? 876  ARG A NH1 1 
ATOM   6991 N  NH2 . ARG A 1 876  ? 20.392 66.268  4.488   1.00 16.71 ? 876  ARG A NH2 1 
ATOM   6992 N  N   . GLY A 1 877  ? 26.516 70.926  8.513   1.00 19.11 ? 877  GLY A N   1 
ATOM   6993 C  CA  . GLY A 1 877  ? 27.602 71.377  9.366   1.00 18.07 ? 877  GLY A CA  1 
ATOM   6994 C  C   . GLY A 1 877  ? 28.589 72.379  8.841   1.00 16.27 ? 877  GLY A C   1 
ATOM   6995 O  O   . GLY A 1 877  ? 29.396 72.891  9.634   1.00 18.88 ? 877  GLY A O   1 
ATOM   6996 N  N   . LEU A 1 878  ? 28.547 72.670  7.542   1.00 16.83 ? 878  LEU A N   1 
ATOM   6997 C  CA  . LEU A 1 878  ? 29.506 73.625  6.987   1.00 18.56 ? 878  LEU A CA  1 
ATOM   6998 C  C   . LEU A 1 878  ? 29.255 75.050  7.534   1.00 19.96 ? 878  LEU A C   1 
ATOM   6999 O  O   . LEU A 1 878  ? 30.209 75.805  7.796   1.00 19.64 ? 878  LEU A O   1 
ATOM   7000 C  CB  . LEU A 1 878  ? 29.448 73.606  5.440   1.00 18.35 ? 878  LEU A CB  1 
ATOM   7001 C  CG  . LEU A 1 878  ? 30.197 74.697  4.649   1.00 19.67 ? 878  LEU A CG  1 
ATOM   7002 C  CD1 . LEU A 1 878  ? 31.681 74.692  5.041   1.00 20.13 ? 878  LEU A CD1 1 
ATOM   7003 C  CD2 . LEU A 1 878  ? 30.033 74.467  3.150   1.00 18.56 ? 878  LEU A CD2 1 
ATOM   7004 N  N   . GLY A 1 879  ? 27.985 75.403  7.712   1.00 19.42 ? 879  GLY A N   1 
ATOM   7005 C  CA  . GLY A 1 879  ? 27.671 76.724  8.244   1.00 20.93 ? 879  GLY A CA  1 
ATOM   7006 C  C   . GLY A 1 879  ? 27.847 77.928  7.326   1.00 22.61 ? 879  GLY A C   1 
ATOM   7007 O  O   . GLY A 1 879  ? 28.012 79.053  7.804   1.00 23.94 ? 879  GLY A O   1 
ATOM   7008 N  N   . GLN A 1 880  ? 27.857 77.717  6.018   1.00 20.57 ? 880  GLN A N   1 
ATOM   7009 C  CA  . GLN A 1 880  ? 27.949 78.842  5.088   1.00 19.59 ? 880  GLN A CA  1 
ATOM   7010 C  C   . GLN A 1 880  ? 27.450 78.321  3.752   1.00 21.10 ? 880  GLN A C   1 
ATOM   7011 O  O   . GLN A 1 880  ? 27.336 77.100  3.576   1.00 21.93 ? 880  GLN A O   1 
ATOM   7012 C  CB  . GLN A 1 880  ? 29.411 79.358  4.960   1.00 19.78 ? 880  GLN A CB  1 
ATOM   7013 C  CG  . GLN A 1 880  ? 30.465 78.328  4.521   1.00 21.53 ? 880  GLN A CG  1 
ATOM   7014 C  CD  . GLN A 1 880  ? 31.701 78.979  3.900   1.00 17.41 ? 880  GLN A CD  1 
ATOM   7015 O  OE1 . GLN A 1 880  ? 31.741 79.223  2.699   1.00 23.13 ? 880  GLN A OE1 1 
ATOM   7016 N  NE2 . GLN A 1 880  ? 32.677 79.264  4.697   1.00 16.24 ? 880  GLN A NE2 1 
ATOM   7017 N  N   . GLY A 1 881  ? 27.119 79.237  2.851   1.00 20.79 ? 881  GLY A N   1 
ATOM   7018 C  CA  . GLY A 1 881  ? 26.735 78.843  1.497   1.00 22.24 ? 881  GLY A CA  1 
ATOM   7019 C  C   . GLY A 1 881  ? 28.043 78.752  0.707   1.00 20.26 ? 881  GLY A C   1 
ATOM   7020 O  O   . GLY A 1 881  ? 29.133 78.605  1.257   1.00 22.10 ? 881  GLY A O   1 
ATOM   7021 N  N   . VAL A 1 882  ? 27.917 78.803  -0.607  1.00 18.76 ? 882  VAL A N   1 
ATOM   7022 C  CA  . VAL A 1 882  ? 29.071 78.764  -1.494  1.00 16.94 ? 882  VAL A CA  1 
ATOM   7023 C  C   . VAL A 1 882  ? 29.006 80.069  -2.273  1.00 16.71 ? 882  VAL A C   1 
ATOM   7024 O  O   . VAL A 1 882  ? 28.272 80.204  -3.269  1.00 15.96 ? 882  VAL A O   1 
ATOM   7025 C  CB  . VAL A 1 882  ? 29.010 77.538  -2.448  1.00 17.60 ? 882  VAL A CB  1 
ATOM   7026 C  CG1 . VAL A 1 882  ? 30.163 77.584  -3.433  1.00 16.80 ? 882  VAL A CG1 1 
ATOM   7027 C  CG2 . VAL A 1 882  ? 29.052 76.230  -1.606  1.00 18.38 ? 882  VAL A CG2 1 
ATOM   7028 N  N   . LEU A 1 883  ? 29.770 81.047  -1.785  1.00 18.23 ? 883  LEU A N   1 
ATOM   7029 C  CA  . LEU A 1 883  ? 29.761 82.392  -2.405  1.00 19.15 ? 883  LEU A CA  1 
ATOM   7030 C  C   . LEU A 1 883  ? 31.173 82.879  -2.695  1.00 20.01 ? 883  LEU A C   1 
ATOM   7031 O  O   . LEU A 1 883  ? 31.391 84.080  -2.846  1.00 23.68 ? 883  LEU A O   1 
ATOM   7032 C  CB  . LEU A 1 883  ? 29.061 83.372  -1.440  1.00 19.62 ? 883  LEU A CB  1 
ATOM   7033 C  CG  . LEU A 1 883  ? 27.591 83.058  -1.122  1.00 18.78 ? 883  LEU A CG  1 
ATOM   7034 C  CD1 . LEU A 1 883  ? 27.021 84.001  -0.007  1.00 20.51 ? 883  LEU A CD1 1 
ATOM   7035 C  CD2 . LEU A 1 883  ? 26.758 83.240  -2.385  1.00 20.72 ? 883  LEU A CD2 1 
ATOM   7036 N  N   . ASP A 1 884  ? 32.127 81.962  -2.761  1.00 16.92 ? 884  ASP A N   1 
ATOM   7037 C  CA  . ASP A 1 884  ? 33.531 82.270  -2.987  1.00 16.55 ? 884  ASP A CA  1 
ATOM   7038 C  C   . ASP A 1 884  ? 34.026 81.818  -4.332  1.00 16.93 ? 884  ASP A C   1 
ATOM   7039 O  O   . ASP A 1 884  ? 35.213 81.533  -4.490  1.00 17.20 ? 884  ASP A O   1 
ATOM   7040 C  CB  . ASP A 1 884  ? 34.428 81.663  -1.891  1.00 17.75 ? 884  ASP A CB  1 
ATOM   7041 C  CG  . ASP A 1 884  ? 34.195 80.148  -1.661  1.00 19.04 ? 884  ASP A CG  1 
ATOM   7042 O  OD1 . ASP A 1 884  ? 33.394 79.517  -2.397  1.00 17.85 ? 884  ASP A OD1 1 
ATOM   7043 O  OD2 . ASP A 1 884  ? 34.851 79.640  -0.712  1.00 21.48 ? 884  ASP A OD2 1 
ATOM   7044 N  N   . ASN A 1 885  ? 33.114 81.761  -5.296  1.00 14.57 ? 885  ASN A N   1 
ATOM   7045 C  CA  . ASN A 1 885  ? 33.456 81.342  -6.634  1.00 15.95 ? 885  ASN A CA  1 
ATOM   7046 C  C   . ASN A 1 885  ? 34.518 82.218  -7.247  1.00 16.35 ? 885  ASN A C   1 
ATOM   7047 O  O   . ASN A 1 885  ? 34.635 83.410  -6.917  1.00 17.22 ? 885  ASN A O   1 
ATOM   7048 C  CB  . ASN A 1 885  ? 32.225 81.440  -7.540  1.00 15.29 ? 885  ASN A CB  1 
ATOM   7049 C  CG  . ASN A 1 885  ? 31.014 80.727  -6.964  1.00 16.82 ? 885  ASN A CG  1 
ATOM   7050 O  OD1 . ASN A 1 885  ? 30.667 79.612  -7.406  1.00 18.32 ? 885  ASN A OD1 1 
ATOM   7051 N  ND2 . ASN A 1 885  ? 30.354 81.339  -6.009  1.00 15.15 ? 885  ASN A ND2 1 
ATOM   7052 N  N   . LYS A 1 886  ? 35.277 81.629  -8.158  1.00 15.75 ? 886  LYS A N   1 
ATOM   7053 C  CA  . LYS A 1 886  ? 36.292 82.361  -8.886  1.00 18.00 ? 886  LYS A CA  1 
ATOM   7054 C  C   . LYS A 1 886  ? 36.373 81.783  -10.282 1.00 16.62 ? 886  LYS A C   1 
ATOM   7055 O  O   . LYS A 1 886  ? 35.986 80.646  -10.532 1.00 16.33 ? 886  LYS A O   1 
ATOM   7056 C  CB  . LYS A 1 886  ? 37.632 82.265  -8.127  1.00 21.68 ? 886  LYS A CB  1 
ATOM   7057 C  CG  . LYS A 1 886  ? 38.110 80.831  -7.896  1.00 21.22 ? 886  LYS A CG  1 
ATOM   7058 C  CD  . LYS A 1 886  ? 39.231 80.693  -6.816  1.00 26.18 ? 886  LYS A CD  1 
ATOM   7059 C  CE  . LYS A 1 886  ? 40.537 81.231  -7.340  1.00 27.11 ? 886  LYS A CE  1 
ATOM   7060 N  NZ  . LYS A 1 886  ? 41.622 81.312  -6.297  1.00 28.34 ? 886  LYS A NZ  1 
ATOM   7061 N  N   . PRO A 1 887  ? 36.864 82.555  -11.234 1.00 14.14 ? 887  PRO A N   1 
ATOM   7062 C  CA  . PRO A 1 887  ? 36.975 82.069  -12.609 1.00 14.25 ? 887  PRO A CA  1 
ATOM   7063 C  C   . PRO A 1 887  ? 37.755 80.784  -12.701 1.00 14.68 ? 887  PRO A C   1 
ATOM   7064 O  O   . PRO A 1 887  ? 38.806 80.622  -12.090 1.00 15.93 ? 887  PRO A O   1 
ATOM   7065 C  CB  . PRO A 1 887  ? 37.685 83.218  -13.341 1.00 16.02 ? 887  PRO A CB  1 
ATOM   7066 C  CG  . PRO A 1 887  ? 37.214 84.451  -12.552 1.00 15.73 ? 887  PRO A CG  1 
ATOM   7067 C  CD  . PRO A 1 887  ? 37.193 83.989  -11.122 1.00 14.77 ? 887  PRO A CD  1 
ATOM   7068 N  N   . VAL A 1 888  ? 37.240 79.852  -13.485 1.00 13.20 ? 888  VAL A N   1 
ATOM   7069 C  CA  . VAL A 1 888  ? 37.905 78.573  -13.693 1.00 12.93 ? 888  VAL A CA  1 
ATOM   7070 C  C   . VAL A 1 888  ? 37.839 78.191  -15.155 1.00 12.00 ? 888  VAL A C   1 
ATOM   7071 O  O   . VAL A 1 888  ? 36.810 78.474  -15.822 1.00 12.89 ? 888  VAL A O   1 
ATOM   7072 C  CB  . VAL A 1 888  ? 37.238 77.464  -12.769 1.00 14.79 ? 888  VAL A CB  1 
ATOM   7073 C  CG1 . VAL A 1 888  ? 35.708 77.370  -13.055 1.00 15.86 ? 888  VAL A CG1 1 
ATOM   7074 C  CG2 . VAL A 1 888  ? 37.905 76.122  -12.987 1.00 14.11 ? 888  VAL A CG2 1 
ATOM   7075 N  N   . LEU A 1 889  ? 38.920 77.618  -15.682 1.00 11.71 ? 889  LEU A N   1 
ATOM   7076 C  CA  . LEU A 1 889  ? 38.940 77.135  -17.045 1.00 12.50 ? 889  LEU A CA  1 
ATOM   7077 C  C   . LEU A 1 889  ? 38.729 75.611  -17.071 1.00 12.10 ? 889  LEU A C   1 
ATOM   7078 O  O   . LEU A 1 889  ? 39.622 74.818  -16.749 1.00 13.77 ? 889  LEU A O   1 
ATOM   7079 C  CB  . LEU A 1 889  ? 40.263 77.497  -17.732 1.00 12.94 ? 889  LEU A CB  1 
ATOM   7080 C  CG  . LEU A 1 889  ? 40.349 77.061  -19.209 1.00 15.38 ? 889  LEU A CG  1 
ATOM   7081 C  CD1 . LEU A 1 889  ? 39.374 77.963  -20.020 1.00 17.54 ? 889  LEU A CD1 1 
ATOM   7082 C  CD2 . LEU A 1 889  ? 41.776 77.167  -19.738 1.00 18.23 ? 889  LEU A CD2 1 
ATOM   7083 N  N   . HIS A 1 890  ? 37.512 75.214  -17.415 1.00 11.97 ? 890  HIS A N   1 
ATOM   7084 C  CA  . HIS A 1 890  ? 37.198 73.785  -17.546 1.00 12.21 ? 890  HIS A CA  1 
ATOM   7085 C  C   . HIS A 1 890  ? 37.583 73.300  -18.928 1.00 13.90 ? 890  HIS A C   1 
ATOM   7086 O  O   . HIS A 1 890  ? 37.377 74.025  -19.912 1.00 14.05 ? 890  HIS A O   1 
ATOM   7087 C  CB  . HIS A 1 890  ? 35.700 73.531  -17.331 1.00 11.98 ? 890  HIS A CB  1 
ATOM   7088 C  CG  . HIS A 1 890  ? 35.250 73.722  -15.925 1.00 11.69 ? 890  HIS A CG  1 
ATOM   7089 N  ND1 . HIS A 1 890  ? 36.050 73.337  -14.863 1.00 13.96 ? 890  HIS A ND1 1 
ATOM   7090 C  CD2 . HIS A 1 890  ? 34.084 74.158  -15.395 1.00 13.59 ? 890  HIS A CD2 1 
ATOM   7091 C  CE1 . HIS A 1 890  ? 35.379 73.514  -13.736 1.00 14.99 ? 890  HIS A CE1 1 
ATOM   7092 N  NE2 . HIS A 1 890  ? 34.183 74.013  -14.032 1.00 13.03 ? 890  HIS A NE2 1 
ATOM   7093 N  N   . ILE A 1 891  ? 38.110 72.089  -19.025 1.00 11.25 ? 891  ILE A N   1 
ATOM   7094 C  CA  . ILE A 1 891  ? 38.500 71.552  -20.302 1.00 11.54 ? 891  ILE A CA  1 
ATOM   7095 C  C   . ILE A 1 891  ? 37.841 70.217  -20.550 1.00 11.30 ? 891  ILE A C   1 
ATOM   7096 O  O   . ILE A 1 891  ? 37.569 69.433  -19.628 1.00 12.09 ? 891  ILE A O   1 
ATOM   7097 C  CB  . ILE A 1 891  ? 40.021 71.468  -20.447 1.00 11.78 ? 891  ILE A CB  1 
ATOM   7098 C  CG1 . ILE A 1 891  ? 40.638 70.506  -19.437 1.00 14.56 ? 891  ILE A CG1 1 
ATOM   7099 C  CG2 . ILE A 1 891  ? 40.630 72.887  -20.200 1.00 13.79 ? 891  ILE A CG2 1 
ATOM   7100 C  CD1 . ILE A 1 891  ? 42.154 70.315  -19.696 1.00 14.86 ? 891  ILE A CD1 1 
ATOM   7101 N  N   . TYR A 1 892  ? 37.582 69.941  -21.825 1.00 10.84 ? 892  TYR A N   1 
ATOM   7102 C  CA  . TYR A 1 892  ? 36.915 68.703  -22.241 1.00 12.03 ? 892  TYR A CA  1 
ATOM   7103 C  C   . TYR A 1 892  ? 37.331 68.254  -23.614 1.00 11.74 ? 892  TYR A C   1 
ATOM   7104 O  O   . TYR A 1 892  ? 37.919 69.035  -24.368 1.00 11.94 ? 892  TYR A O   1 
ATOM   7105 C  CB  . TYR A 1 892  ? 35.396 68.911  -22.383 1.00 12.55 ? 892  TYR A CB  1 
ATOM   7106 C  CG  . TYR A 1 892  ? 34.724 69.583  -21.202 1.00 10.12 ? 892  TYR A CG  1 
ATOM   7107 C  CD1 . TYR A 1 892  ? 34.698 70.972  -21.059 1.00 11.03 ? 892  TYR A CD1 1 
ATOM   7108 C  CD2 . TYR A 1 892  ? 34.122 68.808  -20.197 1.00 12.18 ? 892  TYR A CD2 1 
ATOM   7109 C  CE1 . TYR A 1 892  ? 34.110 71.577  -19.957 1.00 10.28 ? 892  TYR A CE1 1 
ATOM   7110 C  CE2 . TYR A 1 892  ? 33.526 69.395  -19.111 1.00 11.34 ? 892  TYR A CE2 1 
ATOM   7111 C  CZ  . TYR A 1 892  ? 33.528 70.783  -18.990 1.00 11.58 ? 892  TYR A CZ  1 
ATOM   7112 O  OH  . TYR A 1 892  ? 32.940 71.358  -17.901 1.00 12.74 ? 892  TYR A OH  1 
ATOM   7113 N  N   . ARG A 1 893  ? 37.023 66.988  -23.949 1.00 10.61 ? 893  ARG A N   1 
ATOM   7114 C  CA  . ARG A 1 893  ? 37.150 66.517  -25.351 1.00 11.32 ? 893  ARG A CA  1 
ATOM   7115 C  C   . ARG A 1 893  ? 35.792 65.914  -25.654 1.00 12.13 ? 893  ARG A C   1 
ATOM   7116 O  O   . ARG A 1 893  ? 35.170 65.285  -24.804 1.00 13.66 ? 893  ARG A O   1 
ATOM   7117 C  CB  . ARG A 1 893  ? 38.249 65.495  -25.567 1.00 11.85 ? 893  ARG A CB  1 
ATOM   7118 C  CG  . ARG A 1 893  ? 39.635 66.038  -25.279 1.00 13.48 ? 893  ARG A CG  1 
ATOM   7119 C  CD  . ARG A 1 893  ? 40.094 67.116  -26.323 1.00 12.59 ? 893  ARG A CD  1 
ATOM   7120 N  NE  . ARG A 1 893  ? 40.249 66.583  -27.675 1.00 13.00 ? 893  ARG A NE  1 
ATOM   7121 C  CZ  . ARG A 1 893  ? 41.321 65.935  -28.112 1.00 13.85 ? 893  ARG A CZ  1 
ATOM   7122 N  NH1 . ARG A 1 893  ? 42.345 65.729  -27.277 1.00 15.43 ? 893  ARG A NH1 1 
ATOM   7123 N  NH2 . ARG A 1 893  ? 41.412 65.507  -29.372 1.00 17.31 ? 893  ARG A NH2 1 
ATOM   7124 N  N   . LEU A 1 894  ? 35.327 66.107  -26.893 1.00 13.20 ? 894  LEU A N   1 
ATOM   7125 C  CA  . LEU A 1 894  ? 34.015 65.609  -27.335 1.00 14.55 ? 894  LEU A CA  1 
ATOM   7126 C  C   . LEU A 1 894  ? 34.251 64.635  -28.487 1.00 13.66 ? 894  LEU A C   1 
ATOM   7127 O  O   . LEU A 1 894  ? 34.786 65.003  -29.529 1.00 15.55 ? 894  LEU A O   1 
ATOM   7128 C  CB  . LEU A 1 894  ? 33.186 66.796  -27.785 1.00 15.21 ? 894  LEU A CB  1 
ATOM   7129 C  CG  . LEU A 1 894  ? 31.747 66.414  -28.132 1.00 16.53 ? 894  LEU A CG  1 
ATOM   7130 C  CD1 . LEU A 1 894  ? 30.993 65.918  -26.883 1.00 19.62 ? 894  LEU A CD1 1 
ATOM   7131 C  CD2 . LEU A 1 894  ? 31.029 67.635  -28.748 1.00 19.53 ? 894  LEU A CD2 1 
ATOM   7132 N  N   . VAL A 1 895  ? 33.894 63.374  -28.258 1.00 13.15 ? 895  VAL A N   1 
ATOM   7133 C  CA  . VAL A 1 895  ? 34.114 62.328  -29.236 1.00 15.07 ? 895  VAL A CA  1 
ATOM   7134 C  C   . VAL A 1 895  ? 32.823 61.683  -29.716 1.00 14.94 ? 895  VAL A C   1 
ATOM   7135 O  O   . VAL A 1 895  ? 32.139 60.963  -28.971 1.00 14.55 ? 895  VAL A O   1 
ATOM   7136 C  CB  . VAL A 1 895  ? 34.993 61.228  -28.624 1.00 14.38 ? 895  VAL A CB  1 
ATOM   7137 C  CG1 . VAL A 1 895  ? 35.407 60.251  -29.725 1.00 17.97 ? 895  VAL A CG1 1 
ATOM   7138 C  CG2 . VAL A 1 895  ? 36.215 61.854  -27.917 1.00 17.29 ? 895  VAL A CG2 1 
ATOM   7139 N  N   . LEU A 1 896  ? 32.451 61.971  -30.966 1.00 15.83 ? 896  LEU A N   1 
ATOM   7140 C  CA  . LEU A 1 896  ? 31.260 61.367  -31.587 1.00 15.53 ? 896  LEU A CA  1 
ATOM   7141 C  C   . LEU A 1 896  ? 31.842 60.234  -32.437 1.00 16.79 ? 896  LEU A C   1 
ATOM   7142 O  O   . LEU A 1 896  ? 32.792 60.443  -33.188 1.00 17.93 ? 896  LEU A O   1 
ATOM   7143 C  CB  . LEU A 1 896  ? 30.570 62.398  -32.493 1.00 14.97 ? 896  LEU A CB  1 
ATOM   7144 C  CG  . LEU A 1 896  ? 29.371 61.774  -33.248 1.00 17.87 ? 896  LEU A CG  1 
ATOM   7145 C  CD1 . LEU A 1 896  ? 28.207 61.594  -32.304 1.00 20.19 ? 896  LEU A CD1 1 
ATOM   7146 C  CD2 . LEU A 1 896  ? 28.928 62.729  -34.364 1.00 18.31 ? 896  LEU A CD2 1 
ATOM   7147 N  N   . GLU A 1 897  ? 31.308 59.018  -32.269 1.00 15.59 ? 897  GLU A N   1 
ATOM   7148 C  CA  . GLU A 1 897  ? 31.835 57.881  -33.001 1.00 17.55 ? 897  GLU A CA  1 
ATOM   7149 C  C   . GLU A 1 897  ? 30.725 56.910  -33.413 1.00 16.80 ? 897  GLU A C   1 
ATOM   7150 O  O   . GLU A 1 897  ? 29.682 56.823  -32.762 1.00 17.14 ? 897  GLU A O   1 
ATOM   7151 C  CB  . GLU A 1 897  ? 32.787 57.068  -32.098 1.00 20.10 ? 897  GLU A CB  1 
ATOM   7152 C  CG  . GLU A 1 897  ? 33.835 57.840  -31.360 1.00 24.11 ? 897  GLU A CG  1 
ATOM   7153 C  CD  . GLU A 1 897  ? 34.470 56.960  -30.235 1.00 19.91 ? 897  GLU A CD  1 
ATOM   7154 O  OE1 . GLU A 1 897  ? 33.827 56.731  -29.171 1.00 23.98 ? 897  GLU A OE1 1 
ATOM   7155 O  OE2 . GLU A 1 897  ? 35.600 56.540  -30.499 1.00 26.41 ? 897  GLU A OE2 1 
ATOM   7156 N  N   . LYS A 1 898  ? 31.004 56.140  -34.460 1.00 18.59 ? 898  LYS A N   1 
ATOM   7157 C  CA  . LYS A 1 898  ? 30.100 55.054  -34.870 1.00 20.26 ? 898  LYS A CA  1 
ATOM   7158 C  C   . LYS A 1 898  ? 30.560 53.831  -34.073 1.00 20.29 ? 898  LYS A C   1 
ATOM   7159 O  O   . LYS A 1 898  ? 31.753 53.511  -34.026 1.00 23.98 ? 898  LYS A O   1 
ATOM   7160 C  CB  . LYS A 1 898  ? 30.256 54.747  -36.364 1.00 20.92 ? 898  LYS A CB  1 
ATOM   7161 C  CG  . LYS A 1 898  ? 29.906 55.876  -37.282 1.00 26.97 ? 898  LYS A CG  1 
ATOM   7162 C  CD  . LYS A 1 898  ? 28.582 56.600  -36.930 1.00 32.63 ? 898  LYS A CD  1 
ATOM   7163 C  CE  . LYS A 1 898  ? 27.344 55.667  -36.720 1.00 33.73 ? 898  LYS A CE  1 
ATOM   7164 N  NZ  . LYS A 1 898  ? 27.102 54.634  -37.780 1.00 37.00 ? 898  LYS A NZ  1 
ATOM   7165 N  N   . VAL A 1 899  ? 29.626 53.142  -33.443 1.00 19.67 ? 899  VAL A N   1 
ATOM   7166 C  CA  . VAL A 1 899  ? 29.984 51.988  -32.633 1.00 20.43 ? 899  VAL A CA  1 
ATOM   7167 C  C   . VAL A 1 899  ? 29.261 50.697  -33.020 1.00 21.09 ? 899  VAL A C   1 
ATOM   7168 O  O   . VAL A 1 899  ? 29.350 49.708  -32.319 1.00 19.92 ? 899  VAL A O   1 
ATOM   7169 C  CB  . VAL A 1 899  ? 29.728 52.302  -31.143 1.00 21.01 ? 899  VAL A CB  1 
ATOM   7170 C  CG1 . VAL A 1 899  ? 30.761 53.376  -30.662 1.00 21.66 ? 899  VAL A CG1 1 
ATOM   7171 C  CG2 . VAL A 1 899  ? 28.315 52.826  -30.945 1.00 20.95 ? 899  VAL A CG2 1 
ATOM   7172 N  N   . ASN A 1 900  ? 28.558 50.703  -34.149 1.00 19.79 ? 900  ASN A N   1 
ATOM   7173 C  CA  . ASN A 1 900  ? 27.835 49.497  -34.544 1.00 21.10 ? 900  ASN A CA  1 
ATOM   7174 C  C   . ASN A 1 900  ? 28.781 48.328  -34.805 1.00 21.17 ? 900  ASN A C   1 
ATOM   7175 O  O   . ASN A 1 900  ? 28.349 47.172  -34.758 1.00 23.77 ? 900  ASN A O   1 
ATOM   7176 C  CB  . ASN A 1 900  ? 27.005 49.749  -35.815 1.00 24.21 ? 900  ASN A CB  1 
ATOM   7177 C  CG  . ASN A 1 900  ? 27.820 50.331  -36.936 1.00 26.49 ? 900  ASN A CG  1 
ATOM   7178 O  OD1 . ASN A 1 900  ? 28.406 51.408  -36.814 1.00 30.67 ? 900  ASN A OD1 1 
ATOM   7179 N  ND2 . ASN A 1 900  ? 27.873 49.610  -38.068 1.00 30.44 ? 900  ASN A ND2 1 
ATOM   7180 N  N   . ASN A 1 901  ? 30.042 48.595  -35.103 1.00 18.85 ? 901  ASN A N   1 
ATOM   7181 C  CA  . ASN A 1 901  ? 30.970 47.494  -35.336 1.00 19.93 ? 901  ASN A CA  1 
ATOM   7182 C  C   . ASN A 1 901  ? 31.776 47.098  -34.101 1.00 19.73 ? 901  ASN A C   1 
ATOM   7183 O  O   . ASN A 1 901  ? 32.538 46.150  -34.140 1.00 20.16 ? 901  ASN A O   1 
ATOM   7184 C  CB  . ASN A 1 901  ? 31.931 47.817  -36.469 1.00 22.51 ? 901  ASN A CB  1 
ATOM   7185 C  CG  . ASN A 1 901  ? 31.240 47.838  -37.788 1.00 26.78 ? 901  ASN A CG  1 
ATOM   7186 O  OD1 . ASN A 1 901  ? 30.600 46.866  -38.176 1.00 32.28 ? 901  ASN A OD1 1 
ATOM   7187 N  ND2 . ASN A 1 901  ? 31.351 48.957  -38.493 1.00 33.29 ? 901  ASN A ND2 1 
ATOM   7188 N  N   . CYS A 1 902  ? 31.557 47.776  -32.987 1.00 19.34 ? 902  CYS A N   1 
ATOM   7189 C  CA  . CYS A 1 902  ? 32.327 47.458  -31.784 1.00 19.89 ? 902  CYS A CA  1 
ATOM   7190 C  C   . CYS A 1 902  ? 31.782 46.275  -31.025 1.00 17.46 ? 902  CYS A C   1 
ATOM   7191 O  O   . CYS A 1 902  ? 30.579 46.099  -30.939 1.00 19.98 ? 902  CYS A O   1 
ATOM   7192 C  CB  . CYS A 1 902  ? 32.307 48.624  -30.815 1.00 19.92 ? 902  CYS A CB  1 
ATOM   7193 S  SG  . CYS A 1 902  ? 33.015 50.174  -31.426 1.00 23.29 ? 902  CYS A SG  1 
ATOM   7194 N  N   . VAL A 1 903  ? 32.670 45.468  -30.463 1.00 16.77 ? 903  VAL A N   1 
ATOM   7195 C  CA  . VAL A 1 903  ? 32.259 44.342  -29.634 1.00 18.47 ? 903  VAL A CA  1 
ATOM   7196 C  C   . VAL A 1 903  ? 31.969 44.920  -28.240 1.00 18.80 ? 903  VAL A C   1 
ATOM   7197 O  O   . VAL A 1 903  ? 32.886 45.231  -27.450 1.00 20.32 ? 903  VAL A O   1 
ATOM   7198 C  CB  . VAL A 1 903  ? 33.393 43.291  -29.590 1.00 16.89 ? 903  VAL A CB  1 
ATOM   7199 C  CG1 . VAL A 1 903  ? 32.982 42.146  -28.654 1.00 19.00 ? 903  VAL A CG1 1 
ATOM   7200 C  CG2 . VAL A 1 903  ? 33.619 42.696  -30.990 1.00 20.36 ? 903  VAL A CG2 1 
ATOM   7201 N  N   . ARG A 1 904  ? 30.702 45.053  -27.923 1.00 18.58 ? 904  ARG A N   1 
ATOM   7202 C  CA  . ARG A 1 904  ? 30.286 45.631  -26.653 1.00 17.89 ? 904  ARG A CA  1 
ATOM   7203 C  C   . ARG A 1 904  ? 29.724 44.603  -25.700 1.00 18.07 ? 904  ARG A C   1 
ATOM   7204 O  O   . ARG A 1 904  ? 29.333 43.496  -26.098 1.00 18.54 ? 904  ARG A O   1 
ATOM   7205 C  CB  . ARG A 1 904  ? 29.219 46.725  -26.896 1.00 19.26 ? 904  ARG A CB  1 
ATOM   7206 C  CG  . ARG A 1 904  ? 29.833 47.966  -27.577 1.00 19.91 ? 904  ARG A CG  1 
ATOM   7207 C  CD  . ARG A 1 904  ? 28.821 49.054  -27.834 1.00 23.60 ? 904  ARG A CD  1 
ATOM   7208 N  NE  . ARG A 1 904  ? 28.032 48.706  -29.005 1.00 21.83 ? 904  ARG A NE  1 
ATOM   7209 C  CZ  . ARG A 1 904  ? 27.018 49.439  -29.459 1.00 26.01 ? 904  ARG A CZ  1 
ATOM   7210 N  NH1 . ARG A 1 904  ? 26.661 50.559  -28.845 1.00 25.87 ? 904  ARG A NH1 1 
ATOM   7211 N  NH2 . ARG A 1 904  ? 26.354 49.032  -30.533 1.00 27.35 ? 904  ARG A NH2 1 
ATOM   7212 N  N   . PRO A 1 905  ? 29.709 44.938  -24.407 1.00 16.42 ? 905  PRO A N   1 
ATOM   7213 C  CA  . PRO A 1 905  ? 29.152 44.005  -23.433 1.00 17.14 ? 905  PRO A CA  1 
ATOM   7214 C  C   . PRO A 1 905  ? 27.679 43.787  -23.750 1.00 17.44 ? 905  PRO A C   1 
ATOM   7215 O  O   . PRO A 1 905  ? 27.037 44.609  -24.404 1.00 18.34 ? 905  PRO A O   1 
ATOM   7216 C  CB  . PRO A 1 905  ? 29.298 44.757  -22.108 1.00 14.59 ? 905  PRO A CB  1 
ATOM   7217 C  CG  . PRO A 1 905  ? 30.476 45.716  -22.342 1.00 15.15 ? 905  PRO A CG  1 
ATOM   7218 C  CD  . PRO A 1 905  ? 30.207 46.181  -23.769 1.00 17.29 ? 905  PRO A CD  1 
ATOM   7219 N  N   . SER A 1 906  ? 27.138 42.677  -23.274 1.00 17.10 ? 906  SER A N   1 
ATOM   7220 C  CA  . SER A 1 906  ? 25.719 42.392  -23.429 1.00 21.82 ? 906  SER A CA  1 
ATOM   7221 C  C   . SER A 1 906  ? 24.899 43.410  -22.638 1.00 21.07 ? 906  SER A C   1 
ATOM   7222 O  O   . SER A 1 906  ? 25.413 44.124  -21.743 1.00 20.29 ? 906  SER A O   1 
ATOM   7223 C  CB  . SER A 1 906  ? 25.392 41.018  -22.865 1.00 24.72 ? 906  SER A CB  1 
ATOM   7224 O  OG  . SER A 1 906  ? 25.016 41.154  -21.508 1.00 31.01 ? 906  SER A OG  1 
ATOM   7225 N  N   . LYS A 1 907  ? 23.616 43.466  -22.944 1.00 22.19 ? 907  LYS A N   1 
ATOM   7226 C  CA  . LYS A 1 907  ? 22.698 44.373  -22.279 1.00 24.18 ? 907  LYS A CA  1 
ATOM   7227 C  C   . LYS A 1 907  ? 22.653 44.194  -20.767 1.00 22.92 ? 907  LYS A C   1 
ATOM   7228 O  O   . LYS A 1 907  ? 22.325 45.136  -20.055 1.00 26.47 ? 907  LYS A O   1 
ATOM   7229 C  CB  . LYS A 1 907  ? 21.295 44.211  -22.876 1.00 28.57 ? 907  LYS A CB  1 
ATOM   7230 C  CG  . LYS A 1 907  ? 21.228 44.614  -24.341 1.00 35.86 ? 907  LYS A CG  1 
ATOM   7231 C  CD  . LYS A 1 907  ? 19.809 44.402  -24.859 1.00 40.34 ? 907  LYS A CD  1 
ATOM   7232 C  CE  . LYS A 1 907  ? 19.653 44.842  -26.302 1.00 42.42 ? 907  LYS A CE  1 
ATOM   7233 N  NZ  . LYS A 1 907  ? 18.240 44.588  -26.752 1.00 46.87 ? 907  LYS A NZ  1 
ATOM   7234 N  N   . LEU A 1 908  ? 22.989 43.012  -20.255 1.00 22.33 ? 908  LEU A N   1 
ATOM   7235 C  CA  . LEU A 1 908  ? 22.930 42.810  -18.802 1.00 23.54 ? 908  LEU A CA  1 
ATOM   7236 C  C   . LEU A 1 908  ? 24.248 43.141  -18.096 1.00 19.78 ? 908  LEU A C   1 
ATOM   7237 O  O   . LEU A 1 908  ? 24.322 43.106  -16.862 1.00 21.69 ? 908  LEU A O   1 
ATOM   7238 C  CB  . LEU A 1 908  ? 22.521 41.361  -18.468 1.00 25.67 ? 908  LEU A CB  1 
ATOM   7239 C  CG  . LEU A 1 908  ? 21.111 40.991  -18.955 1.00 28.11 ? 908  LEU A CG  1 
ATOM   7240 C  CD1 . LEU A 1 908  ? 20.891 39.490  -18.765 1.00 29.13 ? 908  LEU A CD1 1 
ATOM   7241 C  CD2 . LEU A 1 908  ? 20.057 41.792  -18.190 1.00 29.64 ? 908  LEU A CD2 1 
ATOM   7242 N  N   . HIS A 1 909  ? 25.283 43.490  -18.841 1.00 18.97 ? 909  HIS A N   1 
ATOM   7243 C  CA  . HIS A 1 909  ? 26.570 43.780  -18.212 1.00 16.89 ? 909  HIS A CA  1 
ATOM   7244 C  C   . HIS A 1 909  ? 26.499 45.152  -17.559 1.00 16.47 ? 909  HIS A C   1 
ATOM   7245 O  O   . HIS A 1 909  ? 25.993 46.105  -18.159 1.00 17.35 ? 909  HIS A O   1 
ATOM   7246 C  CB  . HIS A 1 909  ? 27.674 43.755  -19.259 1.00 16.52 ? 909  HIS A CB  1 
ATOM   7247 C  CG  . HIS A 1 909  ? 29.026 43.501  -18.692 1.00 17.45 ? 909  HIS A CG  1 
ATOM   7248 N  ND1 . HIS A 1 909  ? 29.700 44.447  -17.943 1.00 16.64 ? 909  HIS A ND1 1 
ATOM   7249 C  CD2 . HIS A 1 909  ? 29.835 42.415  -18.754 1.00 15.28 ? 909  HIS A CD2 1 
ATOM   7250 C  CE1 . HIS A 1 909  ? 30.869 43.951  -17.586 1.00 16.75 ? 909  HIS A CE1 1 
ATOM   7251 N  NE2 . HIS A 1 909  ? 30.982 42.720  -18.073 1.00 17.52 ? 909  HIS A NE2 1 
ATOM   7252 N  N   . PRO A 1 910  ? 27.003 45.282  -16.326 1.00 14.17 ? 910  PRO A N   1 
ATOM   7253 C  CA  . PRO A 1 910  ? 26.940 46.598  -15.670 1.00 14.32 ? 910  PRO A CA  1 
ATOM   7254 C  C   . PRO A 1 910  ? 28.043 47.598  -16.029 1.00 12.87 ? 910  PRO A C   1 
ATOM   7255 O  O   . PRO A 1 910  ? 28.016 48.716  -15.492 1.00 14.22 ? 910  PRO A O   1 
ATOM   7256 C  CB  . PRO A 1 910  ? 26.992 46.276  -14.173 1.00 16.85 ? 910  PRO A CB  1 
ATOM   7257 C  CG  . PRO A 1 910  ? 27.029 44.800  -14.074 1.00 17.37 ? 910  PRO A CG  1 
ATOM   7258 C  CD  . PRO A 1 910  ? 27.482 44.245  -15.392 1.00 15.30 ? 910  PRO A CD  1 
ATOM   7259 N  N   . ALA A 1 911  ? 28.999 47.206  -16.872 1.00 13.24 ? 911  ALA A N   1 
ATOM   7260 C  CA  . ALA A 1 911  ? 30.091 48.108  -17.237 1.00 15.20 ? 911  ALA A CA  1 
ATOM   7261 C  C   . ALA A 1 911  ? 30.004 48.576  -18.665 1.00 14.71 ? 911  ALA A C   1 
ATOM   7262 O  O   . ALA A 1 911  ? 29.266 47.998  -19.484 1.00 16.29 ? 911  ALA A O   1 
ATOM   7263 C  CB  . ALA A 1 911  ? 31.446 47.413  -17.053 1.00 13.80 ? 911  ALA A CB  1 
ATOM   7264 N  N   . GLY A 1 912  ? 30.766 49.631  -18.946 1.00 14.05 ? 912  GLY A N   1 
ATOM   7265 C  CA  . GLY A 1 912  ? 30.958 50.101  -20.304 1.00 14.63 ? 912  GLY A CA  1 
ATOM   7266 C  C   . GLY A 1 912  ? 32.454 50.352  -20.462 1.00 14.89 ? 912  GLY A C   1 
ATOM   7267 O  O   . GLY A 1 912  ? 33.193 50.435  -19.472 1.00 15.49 ? 912  GLY A O   1 
ATOM   7268 N  N   . TYR A 1 913  ? 32.921 50.517  -21.693 1.00 12.95 ? 913  TYR A N   1 
ATOM   7269 C  CA  . TYR A 1 913  ? 34.323 50.708  -21.998 1.00 14.04 ? 913  TYR A CA  1 
ATOM   7270 C  C   . TYR A 1 913  ? 34.482 51.726  -23.095 1.00 13.56 ? 913  TYR A C   1 
ATOM   7271 O  O   . TYR A 1 913  ? 33.692 51.762  -24.064 1.00 14.85 ? 913  TYR A O   1 
ATOM   7272 C  CB  . TYR A 1 913  ? 34.972 49.385  -22.467 1.00 15.21 ? 913  TYR A CB  1 
ATOM   7273 C  CG  . TYR A 1 913  ? 34.953 48.340  -21.392 1.00 13.25 ? 913  TYR A CG  1 
ATOM   7274 C  CD1 . TYR A 1 913  ? 35.848 48.403  -20.346 1.00 13.48 ? 913  TYR A CD1 1 
ATOM   7275 C  CD2 . TYR A 1 913  ? 33.991 47.349  -21.373 1.00 14.01 ? 913  TYR A CD2 1 
ATOM   7276 C  CE1 . TYR A 1 913  ? 35.795 47.519  -19.296 1.00 12.88 ? 913  TYR A CE1 1 
ATOM   7277 C  CE2 . TYR A 1 913  ? 33.900 46.444  -20.321 1.00 15.50 ? 913  TYR A CE2 1 
ATOM   7278 C  CZ  . TYR A 1 913  ? 34.814 46.549  -19.286 1.00 15.61 ? 913  TYR A CZ  1 
ATOM   7279 O  OH  . TYR A 1 913  ? 34.695 45.687  -18.206 1.00 16.45 ? 913  TYR A OH  1 
ATOM   7280 N  N   . LEU A 1 914  ? 35.557 52.483  -22.989 1.00 12.70 ? 914  LEU A N   1 
ATOM   7281 C  CA  . LEU A 1 914  ? 35.891 53.491  -23.976 1.00 13.27 ? 914  LEU A CA  1 
ATOM   7282 C  C   . LEU A 1 914  ? 36.479 52.862  -25.222 1.00 14.35 ? 914  LEU A C   1 
ATOM   7283 O  O   . LEU A 1 914  ? 36.977 51.731  -25.225 1.00 15.70 ? 914  LEU A O   1 
ATOM   7284 C  CB  . LEU A 1 914  ? 36.984 54.450  -23.428 1.00 14.08 ? 914  LEU A CB  1 
ATOM   7285 C  CG  . LEU A 1 914  ? 36.510 55.342  -22.269 1.00 13.45 ? 914  LEU A CG  1 
ATOM   7286 C  CD1 . LEU A 1 914  ? 37.610 56.361  -22.013 1.00 15.10 ? 914  LEU A CD1 1 
ATOM   7287 C  CD2 . LEU A 1 914  ? 35.212 56.099  -22.552 1.00 14.77 ? 914  LEU A CD2 1 
ATOM   7288 N  N   . THR A 1 915  ? 36.411 53.649  -26.293 1.00 15.51 ? 915  THR A N   1 
ATOM   7289 C  CA  . THR A 1 915  ? 37.083 53.314  -27.525 1.00 15.33 ? 915  THR A CA  1 
ATOM   7290 C  C   . THR A 1 915  ? 38.496 53.892  -27.397 1.00 16.37 ? 915  THR A C   1 
ATOM   7291 O  O   . THR A 1 915  ? 38.794 54.706  -26.488 1.00 15.84 ? 915  THR A O   1 
ATOM   7292 C  CB  . THR A 1 915  ? 36.456 54.005  -28.718 1.00 16.00 ? 915  THR A CB  1 
ATOM   7293 O  OG1 . THR A 1 915  ? 36.458 55.416  -28.441 1.00 18.78 ? 915  THR A OG1 1 
ATOM   7294 C  CG2 . THR A 1 915  ? 35.033 53.483  -29.000 1.00 18.47 ? 915  THR A CG2 1 
ATOM   7295 N  N   . SER A 1 916  ? 39.384 53.494  -28.298 1.00 14.97 ? 916  SER A N   1 
ATOM   7296 C  CA  . SER A 1 916  ? 40.734 53.992  -28.341 1.00 15.64 ? 916  SER A CA  1 
ATOM   7297 C  C   . SER A 1 916  ? 40.759 55.519  -28.438 1.00 15.02 ? 916  SER A C   1 
ATOM   7298 O  O   . SER A 1 916  ? 41.486 56.202  -27.685 1.00 14.39 ? 916  SER A O   1 
ATOM   7299 C  CB  . SER A 1 916  ? 41.473 53.432  -29.564 1.00 18.18 ? 916  SER A CB  1 
ATOM   7300 O  OG  . SER A 1 916  ? 42.633 54.195  -29.789 1.00 26.16 ? 916  SER A OG  1 
ATOM   7301 N  N   . ALA A 1 917  ? 39.965 56.092  -29.332 1.00 15.13 ? 917  ALA A N   1 
ATOM   7302 C  CA  . ALA A 1 917  ? 39.983 57.532  -29.467 1.00 13.23 ? 917  ALA A CA  1 
ATOM   7303 C  C   . ALA A 1 917  ? 39.541 58.267  -28.225 1.00 12.80 ? 917  ALA A C   1 
ATOM   7304 O  O   . ALA A 1 917  ? 40.110 59.322  -27.902 1.00 14.82 ? 917  ALA A O   1 
ATOM   7305 C  CB  . ALA A 1 917  ? 39.062 57.943  -30.624 1.00 15.78 ? 917  ALA A CB  1 
ATOM   7306 N  N   . ALA A 1 918  ? 38.521 57.737  -27.525 1.00 13.72 ? 918  ALA A N   1 
ATOM   7307 C  CA  . ALA A 1 918  ? 38.065 58.435  -26.317 1.00 12.60 ? 918  ALA A CA  1 
ATOM   7308 C  C   . ALA A 1 918  ? 39.077 58.294  -25.195 1.00 13.94 ? 918  ALA A C   1 
ATOM   7309 O  O   . ALA A 1 918  ? 39.302 59.259  -24.451 1.00 13.15 ? 918  ALA A O   1 
ATOM   7310 C  CB  . ALA A 1 918  ? 36.704 57.923  -25.906 1.00 15.14 ? 918  ALA A CB  1 
ATOM   7311 N  N   . HIS A 1 919  ? 39.691 57.131  -25.085 1.00 12.07 ? 919  HIS A N   1 
ATOM   7312 C  CA  . HIS A 1 919  ? 40.731 56.955  -24.077 1.00 11.69 ? 919  HIS A CA  1 
ATOM   7313 C  C   . HIS A 1 919  ? 41.903 57.896  -24.340 1.00 12.46 ? 919  HIS A C   1 
ATOM   7314 O  O   . HIS A 1 919  ? 42.408 58.546  -23.413 1.00 13.09 ? 919  HIS A O   1 
ATOM   7315 C  CB  . HIS A 1 919  ? 41.196 55.504  -24.081 1.00 13.73 ? 919  HIS A CB  1 
ATOM   7316 C  CG  . HIS A 1 919  ? 42.343 55.265  -23.153 1.00 16.27 ? 919  HIS A CG  1 
ATOM   7317 N  ND1 . HIS A 1 919  ? 43.601 54.940  -23.600 1.00 19.56 ? 919  HIS A ND1 1 
ATOM   7318 C  CD2 . HIS A 1 919  ? 42.421 55.339  -21.802 1.00 17.89 ? 919  HIS A CD2 1 
ATOM   7319 C  CE1 . HIS A 1 919  ? 44.415 54.810  -22.563 1.00 18.37 ? 919  HIS A CE1 1 
ATOM   7320 N  NE2 . HIS A 1 919  ? 43.731 55.051  -21.465 1.00 17.43 ? 919  HIS A NE2 1 
ATOM   7321 N  N   . LYS A 1 920  ? 42.363 57.984  -25.593 1.00 12.27 ? 920  LYS A N   1 
ATOM   7322 C  CA  . LYS A 1 920  ? 43.466 58.877  -25.904 1.00 13.50 ? 920  LYS A CA  1 
ATOM   7323 C  C   . LYS A 1 920  ? 43.047 60.316  -25.634 1.00 12.31 ? 920  LYS A C   1 
ATOM   7324 O  O   . LYS A 1 920  ? 43.870 61.109  -25.158 1.00 13.33 ? 920  LYS A O   1 
ATOM   7325 C  CB  . LYS A 1 920  ? 43.940 58.714  -27.347 1.00 17.42 ? 920  LYS A CB  1 
ATOM   7326 C  CG  . LYS A 1 920  ? 44.859 57.496  -27.487 1.00 20.59 ? 920  LYS A CG  1 
ATOM   7327 C  CD  . LYS A 1 920  ? 45.559 57.444  -28.859 1.00 24.38 ? 920  LYS A CD  1 
ATOM   7328 C  CE  . LYS A 1 920  ? 46.544 56.294  -28.936 1.00 26.82 ? 920  LYS A CE  1 
ATOM   7329 N  NZ  . LYS A 1 920  ? 47.703 56.394  -28.024 1.00 23.95 ? 920  LYS A NZ  1 
ATOM   7330 N  N   . ALA A 1 921  ? 41.798 60.666  -25.917 1.00 12.93 ? 921  ALA A N   1 
ATOM   7331 C  CA  . ALA A 1 921  ? 41.341 62.037  -25.655 1.00 12.74 ? 921  ALA A CA  1 
ATOM   7332 C  C   . ALA A 1 921  ? 41.405 62.325  -24.141 1.00 12.96 ? 921  ALA A C   1 
ATOM   7333 O  O   . ALA A 1 921  ? 41.739 63.438  -23.709 1.00 12.74 ? 921  ALA A O   1 
ATOM   7334 C  CB  . ALA A 1 921  ? 39.908 62.227  -26.224 1.00 12.11 ? 921  ALA A CB  1 
ATOM   7335 N  N   . SER A 1 922  ? 41.050 61.331  -23.339 1.00 12.80 ? 922  SER A N   1 
ATOM   7336 C  CA  . SER A 1 922  ? 41.113 61.520  -21.890 1.00 11.52 ? 922  SER A CA  1 
ATOM   7337 C  C   . SER A 1 922  ? 42.541 61.718  -21.464 1.00 13.89 ? 922  SER A C   1 
ATOM   7338 O  O   . SER A 1 922  ? 42.814 62.597  -20.641 1.00 12.80 ? 922  SER A O   1 
ATOM   7339 C  CB  . SER A 1 922  ? 40.505 60.307  -21.189 1.00 11.56 ? 922  SER A CB  1 
ATOM   7340 O  OG  . SER A 1 922  ? 40.643 60.477  -19.763 1.00 12.69 ? 922  SER A OG  1 
ATOM   7341 N  N   . GLN A 1 923  ? 43.470 60.929  -22.013 1.00 12.73 ? 923  GLN A N   1 
ATOM   7342 C  CA  . GLN A 1 923  ? 44.891 61.080  -21.680 1.00 12.08 ? 923  GLN A CA  1 
ATOM   7343 C  C   . GLN A 1 923  ? 45.393 62.478  -22.108 1.00 12.47 ? 923  GLN A C   1 
ATOM   7344 O  O   . GLN A 1 923  ? 46.248 63.042  -21.443 1.00 13.84 ? 923  GLN A O   1 
ATOM   7345 C  CB  . GLN A 1 923  ? 45.725 60.000  -22.379 1.00 13.66 ? 923  GLN A CB  1 
ATOM   7346 C  CG  . GLN A 1 923  ? 45.436 58.610  -21.849 1.00 12.49 ? 923  GLN A CG  1 
ATOM   7347 C  CD  . GLN A 1 923  ? 46.387 57.604  -22.444 1.00 13.62 ? 923  GLN A CD  1 
ATOM   7348 O  OE1 . GLN A 1 923  ? 46.561 57.554  -23.674 1.00 15.10 ? 923  GLN A OE1 1 
ATOM   7349 N  NE2 . GLN A 1 923  ? 47.050 56.805  -21.571 1.00 14.52 ? 923  GLN A NE2 1 
ATOM   7350 N  N   . SER A 1 924  ? 44.864 63.038  -23.204 1.00 12.31 ? 924  SER A N   1 
ATOM   7351 C  CA  . SER A 1 924  ? 45.322 64.340  -23.641 1.00 15.02 ? 924  SER A CA  1 
ATOM   7352 C  C   . SER A 1 924  ? 44.905 65.401  -22.639 1.00 14.17 ? 924  SER A C   1 
ATOM   7353 O  O   . SER A 1 924  ? 45.558 66.433  -22.518 1.00 16.53 ? 924  SER A O   1 
ATOM   7354 C  CB  . SER A 1 924  ? 44.723 64.679  -24.998 1.00 17.08 ? 924  SER A CB  1 
ATOM   7355 O  OG  A SER A 1 924  ? 43.384 65.156  -24.873 0.50 24.68 ? 924  SER A OG  1 
ATOM   7356 O  OG  B SER A 1 924  ? 45.273 63.861  -26.030 0.50 24.68 ? 924  SER A OG  1 
ATOM   7357 N  N   . LEU A 1 925  ? 43.804 65.163  -21.926 1.00 14.54 ? 925  LEU A N   1 
ATOM   7358 C  CA  . LEU A 1 925  ? 43.338 66.131  -20.929 1.00 13.94 ? 925  LEU A CA  1 
ATOM   7359 C  C   . LEU A 1 925  ? 44.085 65.978  -19.599 1.00 14.56 ? 925  LEU A C   1 
ATOM   7360 O  O   . LEU A 1 925  ? 44.480 66.978  -18.995 1.00 14.67 ? 925  LEU A O   1 
ATOM   7361 C  CB  . LEU A 1 925  ? 41.835 65.963  -20.633 1.00 12.93 ? 925  LEU A CB  1 
ATOM   7362 C  CG  . LEU A 1 925  ? 40.918 66.249  -21.823 1.00 12.29 ? 925  LEU A CG  1 
ATOM   7363 C  CD1 . LEU A 1 925  ? 39.464 65.977  -21.365 1.00 14.68 ? 925  LEU A CD1 1 
ATOM   7364 C  CD2 . LEU A 1 925  ? 41.100 67.722  -22.300 1.00 14.06 ? 925  LEU A CD2 1 
ATOM   7365 N  N   . LEU A 1 926  ? 44.265 64.731  -19.168 1.00 13.21 ? 926  LEU A N   1 
ATOM   7366 C  CA  . LEU A 1 926  ? 44.871 64.484  -17.862 1.00 13.30 ? 926  LEU A CA  1 
ATOM   7367 C  C   . LEU A 1 926  ? 46.368 64.467  -17.830 1.00 14.50 ? 926  LEU A C   1 
ATOM   7368 O  O   . LEU A 1 926  ? 46.955 64.867  -16.807 1.00 14.14 ? 926  LEU A O   1 
ATOM   7369 C  CB  . LEU A 1 926  ? 44.308 63.173  -17.285 1.00 13.34 ? 926  LEU A CB  1 
ATOM   7370 C  CG  . LEU A 1 926  ? 42.785 63.223  -17.051 1.00 16.39 ? 926  LEU A CG  1 
ATOM   7371 C  CD1 . LEU A 1 926  ? 42.351 61.858  -16.433 1.00 16.44 ? 926  LEU A CD1 1 
ATOM   7372 C  CD2 . LEU A 1 926  ? 42.387 64.390  -16.090 1.00 17.30 ? 926  LEU A CD2 1 
ATOM   7373 N  N   . ASP A 1 927  ? 47.004 63.978  -18.888 1.00 11.99 ? 927  ASP A N   1 
ATOM   7374 C  CA  . ASP A 1 927  ? 48.447 63.923  -18.928 1.00 12.56 ? 927  ASP A CA  1 
ATOM   7375 C  C   . ASP A 1 927  ? 49.034 64.452  -20.218 1.00 11.06 ? 927  ASP A C   1 
ATOM   7376 O  O   . ASP A 1 927  ? 49.600 63.721  -21.031 1.00 13.58 ? 927  ASP A O   1 
ATOM   7377 C  CB  . ASP A 1 927  ? 48.921 62.486  -18.630 1.00 12.41 ? 927  ASP A CB  1 
ATOM   7378 C  CG  . ASP A 1 927  ? 48.563 62.040  -17.207 1.00 12.02 ? 927  ASP A CG  1 
ATOM   7379 O  OD1 . ASP A 1 927  ? 49.261 62.451  -16.224 1.00 13.66 ? 927  ASP A OD1 1 
ATOM   7380 O  OD2 . ASP A 1 927  ? 47.560 61.329  -17.081 1.00 14.26 ? 927  ASP A OD2 1 
ATOM   7381 N  N   . PRO A 1 928  ? 48.859 65.749  -20.430 1.00 12.78 ? 928  PRO A N   1 
ATOM   7382 C  CA  . PRO A 1 928  ? 49.383 66.391  -21.640 1.00 11.60 ? 928  PRO A CA  1 
ATOM   7383 C  C   . PRO A 1 928  ? 50.897 66.419  -21.626 1.00 13.86 ? 928  PRO A C   1 
ATOM   7384 O  O   . PRO A 1 928  ? 51.536 66.120  -20.609 1.00 14.08 ? 928  PRO A O   1 
ATOM   7385 C  CB  . PRO A 1 928  ? 48.866 67.834  -21.533 1.00 13.75 ? 928  PRO A CB  1 
ATOM   7386 C  CG  . PRO A 1 928  ? 48.817 68.076  -20.051 1.00 15.74 ? 928  PRO A CG  1 
ATOM   7387 C  CD  . PRO A 1 928  ? 48.290 66.718  -19.478 1.00 13.86 ? 928  PRO A CD  1 
ATOM   7388 N  N   . LEU A 1 929  ? 51.494 66.748  -22.762 1.00 15.23 ? 929  LEU A N   1 
ATOM   7389 C  CA  . LEU A 1 929  ? 52.912 66.967  -22.779 1.00 13.49 ? 929  LEU A CA  1 
ATOM   7390 C  C   . LEU A 1 929  ? 53.223 68.153  -21.875 1.00 12.61 ? 929  LEU A C   1 
ATOM   7391 O  O   . LEU A 1 929  ? 52.464 69.109  -21.783 1.00 16.03 ? 929  LEU A O   1 
ATOM   7392 C  CB  . LEU A 1 929  ? 53.397 67.328  -24.196 1.00 13.86 ? 929  LEU A CB  1 
ATOM   7393 C  CG  . LEU A 1 929  ? 53.192 66.301  -25.300 1.00 13.08 ? 929  LEU A CG  1 
ATOM   7394 C  CD1 . LEU A 1 929  ? 53.721 66.950  -26.622 1.00 14.47 ? 929  LEU A CD1 1 
ATOM   7395 C  CD2 . LEU A 1 929  ? 54.037 65.020  -24.998 1.00 12.05 ? 929  LEU A CD2 1 
ATOM   7396 N  N   . ASP A 1 930  ? 54.337 68.081  -21.168 1.00 11.88 ? 930  ASP A N   1 
ATOM   7397 C  CA  . ASP A 1 930  ? 54.791 69.198  -20.361 1.00 11.43 ? 930  ASP A CA  1 
ATOM   7398 C  C   . ASP A 1 930  ? 55.730 70.063  -21.215 1.00 13.58 ? 930  ASP A C   1 
ATOM   7399 O  O   . ASP A 1 930  ? 56.481 69.544  -22.044 1.00 14.56 ? 930  ASP A O   1 
ATOM   7400 C  CB  . ASP A 1 930  ? 55.518 68.684  -19.121 1.00 11.98 ? 930  ASP A CB  1 
ATOM   7401 C  CG  . ASP A 1 930  ? 54.714 67.666  -18.380 1.00 14.30 ? 930  ASP A CG  1 
ATOM   7402 O  OD1 . ASP A 1 930  ? 53.649 68.091  -17.882 1.00 17.16 ? 930  ASP A OD1 1 
ATOM   7403 O  OD2 . ASP A 1 930  ? 55.138 66.492  -18.320 1.00 14.04 ? 930  ASP A OD2 1 
ATOM   7404 N  N   . LYS A 1 931  ? 55.690 71.359  -21.004 1.00 13.41 ? 931  LYS A N   1 
ATOM   7405 C  CA  . LYS A 1 931  ? 56.486 72.291  -21.801 1.00 13.25 ? 931  LYS A CA  1 
ATOM   7406 C  C   . LYS A 1 931  ? 57.435 73.074  -20.935 1.00 13.24 ? 931  LYS A C   1 
ATOM   7407 O  O   . LYS A 1 931  ? 57.031 73.704  -19.959 1.00 15.14 ? 931  LYS A O   1 
ATOM   7408 C  CB  . LYS A 1 931  ? 55.538 73.245  -22.556 1.00 13.91 ? 931  LYS A CB  1 
ATOM   7409 C  CG  . LYS A 1 931  ? 54.539 72.552  -23.522 1.00 16.89 ? 931  LYS A CG  1 
ATOM   7410 C  CD  . LYS A 1 931  ? 53.638 73.584  -24.210 1.00 20.19 ? 931  LYS A CD  1 
ATOM   7411 C  CE  . LYS A 1 931  ? 52.689 74.170  -23.207 1.00 21.70 ? 931  LYS A CE  1 
ATOM   7412 N  NZ  . LYS A 1 931  ? 51.965 75.308  -23.764 1.00 24.21 ? 931  LYS A NZ  1 
ATOM   7413 N  N   . PHE A 1 932  ? 58.695 73.126  -21.344 1.00 13.11 ? 932  PHE A N   1 
ATOM   7414 C  CA  . PHE A 1 932  ? 59.728 73.833  -20.599 1.00 12.34 ? 932  PHE A CA  1 
ATOM   7415 C  C   . PHE A 1 932  ? 60.410 74.869  -21.483 1.00 12.78 ? 932  PHE A C   1 
ATOM   7416 O  O   . PHE A 1 932  ? 60.746 74.568  -22.641 1.00 13.27 ? 932  PHE A O   1 
ATOM   7417 C  CB  . PHE A 1 932  ? 60.802 72.869  -20.111 1.00 13.06 ? 932  PHE A CB  1 
ATOM   7418 C  CG  . PHE A 1 932  ? 60.296 71.786  -19.207 1.00 15.07 ? 932  PHE A CG  1 
ATOM   7419 C  CD1 . PHE A 1 932  ? 59.718 70.637  -19.724 1.00 14.63 ? 932  PHE A CD1 1 
ATOM   7420 C  CD2 . PHE A 1 932  ? 60.447 71.927  -17.827 1.00 15.77 ? 932  PHE A CD2 1 
ATOM   7421 C  CE1 . PHE A 1 932  ? 59.276 69.604  -18.899 1.00 14.68 ? 932  PHE A CE1 1 
ATOM   7422 C  CE2 . PHE A 1 932  ? 60.020 70.905  -16.962 1.00 16.58 ? 932  PHE A CE2 1 
ATOM   7423 C  CZ  . PHE A 1 932  ? 59.433 69.753  -17.509 1.00 16.52 ? 932  PHE A CZ  1 
ATOM   7424 N  N   . ILE A 1 933  ? 60.593 76.077  -20.970 1.00 13.15 ? 933  ILE A N   1 
ATOM   7425 C  CA  . ILE A 1 933  ? 61.274 77.139  -21.744 1.00 13.98 ? 933  ILE A CA  1 
ATOM   7426 C  C   . ILE A 1 933  ? 62.634 77.373  -21.088 1.00 16.36 ? 933  ILE A C   1 
ATOM   7427 O  O   . ILE A 1 933  ? 62.694 77.679  -19.893 1.00 14.16 ? 933  ILE A O   1 
ATOM   7428 C  CB  . ILE A 1 933  ? 60.478 78.451  -21.688 1.00 15.11 ? 933  ILE A CB  1 
ATOM   7429 C  CG1 . ILE A 1 933  ? 59.056 78.214  -22.250 1.00 14.34 ? 933  ILE A CG1 1 
ATOM   7430 C  CG2 . ILE A 1 933  ? 61.223 79.552  -22.467 1.00 13.10 ? 933  ILE A CG2 1 
ATOM   7431 C  CD1 . ILE A 1 933  ? 58.168 79.427  -22.063 1.00 14.99 ? 933  ILE A CD1 1 
ATOM   7432 N  N   . PHE A 1 934  ? 63.737 77.235  -21.845 1.00 13.97 ? 934  PHE A N   1 
ATOM   7433 C  CA  . PHE A 1 934  ? 65.054 77.456  -21.240 1.00 15.21 ? 934  PHE A CA  1 
ATOM   7434 C  C   . PHE A 1 934  ? 65.113 78.928  -20.765 1.00 15.09 ? 934  PHE A C   1 
ATOM   7435 O  O   . PHE A 1 934  ? 64.776 79.866  -21.503 1.00 15.68 ? 934  PHE A O   1 
ATOM   7436 C  CB  . PHE A 1 934  ? 66.179 77.111  -22.247 1.00 15.57 ? 934  PHE A CB  1 
ATOM   7437 C  CG  . PHE A 1 934  ? 67.541 77.152  -21.641 1.00 17.94 ? 934  PHE A CG  1 
ATOM   7438 C  CD1 . PHE A 1 934  ? 67.967 76.140  -20.807 1.00 17.76 ? 934  PHE A CD1 1 
ATOM   7439 C  CD2 . PHE A 1 934  ? 68.370 78.259  -21.851 1.00 19.06 ? 934  PHE A CD2 1 
ATOM   7440 C  CE1 . PHE A 1 934  ? 69.212 76.215  -20.170 1.00 20.35 ? 934  PHE A CE1 1 
ATOM   7441 C  CE2 . PHE A 1 934  ? 69.617 78.356  -21.225 1.00 20.67 ? 934  PHE A CE2 1 
ATOM   7442 C  CZ  . PHE A 1 934  ? 70.041 77.331  -20.377 1.00 21.01 ? 934  PHE A CZ  1 
ATOM   7443 N  N   . ALA A 1 935  ? 65.576 79.145  -19.535 1.00 16.34 ? 935  ALA A N   1 
ATOM   7444 C  CA  . ALA A 1 935  ? 65.544 80.500  -18.998 1.00 18.97 ? 935  ALA A CA  1 
ATOM   7445 C  C   . ALA A 1 935  ? 66.666 81.430  -19.434 1.00 22.30 ? 935  ALA A C   1 
ATOM   7446 O  O   . ALA A 1 935  ? 66.411 82.615  -19.750 1.00 26.19 ? 935  ALA A O   1 
ATOM   7447 C  CB  . ALA A 1 935  ? 65.480 80.451  -17.468 1.00 23.06 ? 935  ALA A CB  1 
ATOM   7448 N  N   . GLU A 1 936  ? 67.881 80.903  -19.493 1.00 20.43 ? 936  GLU A N   1 
ATOM   7449 C  CA  . GLU A 1 936  ? 69.066 81.704  -19.852 1.00 22.04 ? 936  GLU A CA  1 
ATOM   7450 C  C   . GLU A 1 936  ? 69.166 81.920  -21.354 1.00 20.29 ? 936  GLU A C   1 
ATOM   7451 O  O   . GLU A 1 936  ? 68.380 81.376  -22.125 1.00 20.16 ? 936  GLU A O   1 
ATOM   7452 C  CB  . GLU A 1 936  ? 70.354 81.013  -19.359 1.00 24.20 ? 936  GLU A CB  1 
ATOM   7453 C  CG  . GLU A 1 936  ? 70.478 80.750  -17.830 1.00 30.94 ? 936  GLU A CG  1 
ATOM   7454 C  CD  . GLU A 1 936  ? 71.558 79.659  -17.497 1.00 33.59 ? 936  GLU A CD  1 
ATOM   7455 O  OE1 . GLU A 1 936  ? 71.332 78.445  -17.765 1.00 33.11 ? 936  GLU A OE1 1 
ATOM   7456 O  OE2 . GLU A 1 936  ? 72.652 80.008  -16.985 1.00 35.75 ? 936  GLU A OE2 1 
ATOM   7457 N  N   . ASN A 1 937  ? 70.148 82.694  -21.785 1.00 21.29 ? 937  ASN A N   1 
ATOM   7458 C  CA  . ASN A 1 937  ? 70.263 82.930  -23.200 1.00 18.90 ? 937  ASN A CA  1 
ATOM   7459 C  C   . ASN A 1 937  ? 70.849 81.791  -23.980 1.00 18.30 ? 937  ASN A C   1 
ATOM   7460 O  O   . ASN A 1 937  ? 70.471 81.589  -25.138 1.00 19.63 ? 937  ASN A O   1 
ATOM   7461 C  CB  . ASN A 1 937  ? 71.100 84.171  -23.457 1.00 18.39 ? 937  ASN A CB  1 
ATOM   7462 C  CG  . ASN A 1 937  ? 70.388 85.432  -23.050 1.00 24.63 ? 937  ASN A CG  1 
ATOM   7463 O  OD1 . ASN A 1 937  ? 69.143 85.480  -22.985 1.00 25.66 ? 937  ASN A OD1 1 
ATOM   7464 N  ND2 . ASN A 1 937  ? 71.168 86.484  -22.796 1.00 28.74 ? 937  ASN A ND2 1 
ATOM   7465 N  N   . GLU A 1 938  ? 71.778 81.054  -23.372 1.00 19.65 ? 938  GLU A N   1 
ATOM   7466 C  CA  . GLU A 1 938  ? 72.358 79.941  -24.104 1.00 22.28 ? 938  GLU A CA  1 
ATOM   7467 C  C   . GLU A 1 938  ? 72.452 78.696  -23.260 1.00 19.06 ? 938  GLU A C   1 
ATOM   7468 O  O   . GLU A 1 938  ? 72.864 78.753  -22.128 1.00 21.96 ? 938  GLU A O   1 
ATOM   7469 C  CB  . GLU A 1 938  ? 73.754 80.306  -24.613 1.00 27.37 ? 938  GLU A CB  1 
ATOM   7470 C  CG  . GLU A 1 938  ? 74.437 79.136  -25.272 1.00 32.85 ? 938  GLU A CG  1 
ATOM   7471 C  CD  . GLU A 1 938  ? 75.632 79.552  -26.122 1.00 37.36 ? 938  GLU A CD  1 
ATOM   7472 O  OE1 . GLU A 1 938  ? 76.439 80.390  -25.657 1.00 39.85 ? 938  GLU A OE1 1 
ATOM   7473 O  OE2 . GLU A 1 938  ? 75.752 79.018  -27.252 1.00 41.18 ? 938  GLU A OE2 1 
ATOM   7474 N  N   . TRP A 1 939  ? 72.088 77.573  -23.851 1.00 22.05 ? 939  TRP A N   1 
ATOM   7475 C  CA  . TRP A 1 939  ? 72.161 76.301  -23.135 1.00 21.37 ? 939  TRP A CA  1 
ATOM   7476 C  C   . TRP A 1 939  ? 73.368 75.528  -23.664 1.00 22.01 ? 939  TRP A C   1 
ATOM   7477 O  O   . TRP A 1 939  ? 73.276 74.882  -24.702 1.00 25.02 ? 939  TRP A O   1 
ATOM   7478 C  CB  . TRP A 1 939  ? 70.854 75.547  -23.389 1.00 21.77 ? 939  TRP A CB  1 
ATOM   7479 C  CG  . TRP A 1 939  ? 70.723 74.207  -22.734 1.00 18.07 ? 939  TRP A CG  1 
ATOM   7480 C  CD1 . TRP A 1 939  ? 71.604 73.579  -21.875 1.00 19.34 ? 939  TRP A CD1 1 
ATOM   7481 C  CD2 . TRP A 1 939  ? 69.639 73.306  -22.936 1.00 16.87 ? 939  TRP A CD2 1 
ATOM   7482 N  NE1 . TRP A 1 939  ? 71.110 72.324  -21.544 1.00 17.68 ? 939  TRP A NE1 1 
ATOM   7483 C  CE2 . TRP A 1 939  ? 69.911 72.138  -22.190 1.00 14.97 ? 939  TRP A CE2 1 
ATOM   7484 C  CE3 . TRP A 1 939  ? 68.457 73.371  -23.683 1.00 14.93 ? 939  TRP A CE3 1 
ATOM   7485 C  CZ2 . TRP A 1 939  ? 69.039 71.043  -22.177 1.00 16.43 ? 939  TRP A CZ2 1 
ATOM   7486 C  CZ3 . TRP A 1 939  ? 67.585 72.293  -23.670 1.00 16.65 ? 939  TRP A CZ3 1 
ATOM   7487 C  CH2 . TRP A 1 939  ? 67.880 71.140  -22.927 1.00 15.56 ? 939  TRP A CH2 1 
ATOM   7488 N  N   . ILE A 1 940  ? 74.488 75.589  -22.946 1.00 25.39 ? 940  ILE A N   1 
ATOM   7489 C  CA  . ILE A 1 940  ? 75.683 74.872  -23.398 1.00 26.97 ? 940  ILE A CA  1 
ATOM   7490 C  C   . ILE A 1 940  ? 75.549 73.353  -23.156 1.00 25.50 ? 940  ILE A C   1 
ATOM   7491 O  O   . ILE A 1 940  ? 75.112 72.926  -22.098 1.00 26.03 ? 940  ILE A O   1 
ATOM   7492 C  CB  . ILE A 1 940  ? 76.925 75.417  -22.678 1.00 27.95 ? 940  ILE A CB  1 
ATOM   7493 C  CG1 . ILE A 1 940  ? 77.131 76.883  -23.064 1.00 30.62 ? 940  ILE A CG1 1 
ATOM   7494 C  CG2 . ILE A 1 940  ? 78.156 74.584  -23.057 1.00 28.90 ? 940  ILE A CG2 1 
ATOM   7495 C  CD1 . ILE A 1 940  ? 77.355 77.781  -21.880 1.00 34.36 ? 940  ILE A CD1 1 
ATOM   7496 N  N   . GLY A 1 941  ? 75.915 72.547  -24.142 1.00 24.99 ? 941  GLY A N   1 
ATOM   7497 C  CA  . GLY A 1 941  ? 75.810 71.109  -23.956 1.00 24.48 ? 941  GLY A CA  1 
ATOM   7498 C  C   . GLY A 1 941  ? 74.418 70.519  -24.174 1.00 23.99 ? 941  GLY A C   1 
ATOM   7499 O  O   . GLY A 1 941  ? 74.206 69.316  -23.937 1.00 21.94 ? 941  GLY A O   1 
ATOM   7500 N  N   . ALA A 1 942  ? 73.471 71.333  -24.649 1.00 21.37 ? 942  ALA A N   1 
ATOM   7501 C  CA  . ALA A 1 942  ? 72.120 70.845  -24.898 1.00 20.94 ? 942  ALA A CA  1 
ATOM   7502 C  C   . ALA A 1 942  ? 72.045 69.641  -25.818 1.00 20.17 ? 942  ALA A C   1 
ATOM   7503 O  O   . ALA A 1 942  ? 72.762 69.562  -26.819 1.00 21.16 ? 942  ALA A O   1 
ATOM   7504 C  CB  . ALA A 1 942  ? 71.251 71.980  -25.458 1.00 21.74 ? 942  ALA A CB  1 
ATOM   7505 N  N   . GLN A 1 943  ? 71.151 68.708  -25.492 1.00 20.53 ? 943  GLN A N   1 
ATOM   7506 C  CA  . GLN A 1 943  ? 70.908 67.528  -26.276 1.00 21.08 ? 943  GLN A CA  1 
ATOM   7507 C  C   . GLN A 1 943  ? 69.488 67.565  -26.832 1.00 18.86 ? 943  GLN A C   1 
ATOM   7508 O  O   . GLN A 1 943  ? 68.587 68.235  -26.251 1.00 20.15 ? 943  GLN A O   1 
ATOM   7509 C  CB  . GLN A 1 943  ? 71.128 66.288  -25.419 1.00 23.12 ? 943  GLN A CB  1 
ATOM   7510 C  CG  . GLN A 1 943  ? 72.503 66.300  -24.756 1.00 29.58 ? 943  GLN A CG  1 
ATOM   7511 C  CD  . GLN A 1 943  ? 72.736 65.031  -23.966 1.00 34.13 ? 943  GLN A CD  1 
ATOM   7512 O  OE1 . GLN A 1 943  ? 71.822 64.565  -23.254 1.00 37.12 ? 943  GLN A OE1 1 
ATOM   7513 N  NE2 . GLN A 1 943  ? 73.945 64.457  -24.074 1.00 35.23 ? 943  GLN A NE2 1 
ATOM   7514 N  N   . GLY A 1 944  ? 69.255 66.838  -27.923 1.00 19.76 ? 944  GLY A N   1 
ATOM   7515 C  CA  . GLY A 1 944  ? 67.985 66.891  -28.604 1.00 19.82 ? 944  GLY A CA  1 
ATOM   7516 C  C   . GLY A 1 944  ? 66.879 65.972  -28.157 1.00 18.60 ? 944  GLY A C   1 
ATOM   7517 O  O   . GLY A 1 944  ? 65.711 66.209  -28.436 1.00 19.35 ? 944  GLY A O   1 
ATOM   7518 N  N   . GLN A 1 945  ? 67.231 64.910  -27.455 1.00 17.85 ? 945  GLN A N   1 
ATOM   7519 C  CA  . GLN A 1 945  ? 66.200 63.951  -27.094 1.00 19.18 ? 945  GLN A CA  1 
ATOM   7520 C  C   . GLN A 1 945  ? 66.644 63.045  -25.958 1.00 19.94 ? 945  GLN A C   1 
ATOM   7521 O  O   . GLN A 1 945  ? 67.832 62.833  -25.728 1.00 19.28 ? 945  GLN A O   1 
ATOM   7522 C  CB  . GLN A 1 945  ? 65.893 63.106  -28.334 1.00 20.33 ? 945  GLN A CB  1 
ATOM   7523 C  CG  . GLN A 1 945  ? 64.715 62.143  -28.246 1.00 23.69 ? 945  GLN A CG  1 
ATOM   7524 C  CD  . GLN A 1 945  ? 64.644 61.235  -29.478 1.00 23.60 ? 945  GLN A CD  1 
ATOM   7525 O  OE1 . GLN A 1 945  ? 63.829 61.442  -30.384 1.00 26.65 ? 945  GLN A OE1 1 
ATOM   7526 N  NE2 . GLN A 1 945  ? 65.509 60.241  -29.515 1.00 26.49 ? 945  GLN A NE2 1 
ATOM   7527 N  N   . PHE A 1 946  ? 65.659 62.568  -25.194 1.00 15.58 ? 946  PHE A N   1 
ATOM   7528 C  CA  . PHE A 1 946  ? 65.942 61.586  -24.141 1.00 15.21 ? 946  PHE A CA  1 
ATOM   7529 C  C   . PHE A 1 946  ? 64.833 60.572  -24.232 1.00 14.68 ? 946  PHE A C   1 
ATOM   7530 O  O   . PHE A 1 946  ? 63.689 60.934  -24.423 1.00 15.67 ? 946  PHE A O   1 
ATOM   7531 C  CB  . PHE A 1 946  ? 65.914 62.226  -22.750 1.00 15.76 ? 946  PHE A CB  1 
ATOM   7532 C  CG  . PHE A 1 946  ? 65.783 61.219  -21.631 1.00 16.55 ? 946  PHE A CG  1 
ATOM   7533 C  CD1 . PHE A 1 946  ? 66.836 60.381  -21.298 1.00 17.52 ? 946  PHE A CD1 1 
ATOM   7534 C  CD2 . PHE A 1 946  ? 64.572 61.102  -20.950 1.00 17.04 ? 946  PHE A CD2 1 
ATOM   7535 C  CE1 . PHE A 1 946  ? 66.681 59.421  -20.275 1.00 18.30 ? 946  PHE A CE1 1 
ATOM   7536 C  CE2 . PHE A 1 946  ? 64.397 60.150  -19.934 1.00 17.64 ? 946  PHE A CE2 1 
ATOM   7537 C  CZ  . PHE A 1 946  ? 65.431 59.315  -19.593 1.00 17.99 ? 946  PHE A CZ  1 
ATOM   7538 N  N   . GLY A 1 947  ? 65.169 59.289  -24.098 1.00 15.17 ? 947  GLY A N   1 
ATOM   7539 C  CA  . GLY A 1 947  ? 64.173 58.246  -24.149 1.00 16.67 ? 947  GLY A CA  1 
ATOM   7540 C  C   . GLY A 1 947  ? 63.841 57.656  -25.491 1.00 17.60 ? 947  GLY A C   1 
ATOM   7541 O  O   . GLY A 1 947  ? 62.889 56.908  -25.589 1.00 17.75 ? 947  GLY A O   1 
ATOM   7542 N  N   . GLY A 1 948  ? 64.624 57.979  -26.532 1.00 20.52 ? 948  GLY A N   1 
ATOM   7543 C  CA  . GLY A 1 948  ? 64.347 57.438  -27.852 1.00 19.57 ? 948  GLY A CA  1 
ATOM   7544 C  C   . GLY A 1 948  ? 64.372 55.911  -27.860 1.00 21.77 ? 948  GLY A C   1 
ATOM   7545 O  O   . GLY A 1 948  ? 63.728 55.272  -28.708 1.00 24.31 ? 948  GLY A O   1 
ATOM   7546 N  N   . ASP A 1 949  ? 65.111 55.325  -26.917 1.00 22.94 ? 949  ASP A N   1 
ATOM   7547 C  CA  . ASP A 1 949  ? 65.188 53.874  -26.808 1.00 25.68 ? 949  ASP A CA  1 
ATOM   7548 C  C   . ASP A 1 949  ? 64.176 53.259  -25.844 1.00 24.23 ? 949  ASP A C   1 
ATOM   7549 O  O   . ASP A 1 949  ? 64.191 52.035  -25.611 1.00 24.91 ? 949  ASP A O   1 
ATOM   7550 C  CB  . ASP A 1 949  ? 66.616 53.457  -26.406 1.00 29.25 ? 949  ASP A CB  1 
ATOM   7551 C  CG  . ASP A 1 949  ? 67.027 53.962  -25.005 1.00 35.12 ? 949  ASP A CG  1 
ATOM   7552 O  OD1 . ASP A 1 949  ? 66.575 55.044  -24.538 1.00 35.42 ? 949  ASP A OD1 1 
ATOM   7553 O  OD2 . ASP A 1 949  ? 67.843 53.266  -24.350 1.00 40.87 ? 949  ASP A OD2 1 
ATOM   7554 N  N   . HIS A 1 950  ? 63.295 54.080  -25.255 1.00 21.33 ? 950  HIS A N   1 
ATOM   7555 C  CA  . HIS A 1 950  ? 62.290 53.515  -24.339 1.00 17.29 ? 950  HIS A CA  1 
ATOM   7556 C  C   . HIS A 1 950  ? 61.212 52.775  -25.173 1.00 17.11 ? 950  HIS A C   1 
ATOM   7557 O  O   . HIS A 1 950  ? 60.814 53.230  -26.242 1.00 20.95 ? 950  HIS A O   1 
ATOM   7558 C  CB  . HIS A 1 950  ? 61.562 54.615  -23.574 1.00 17.49 ? 950  HIS A CB  1 
ATOM   7559 C  CG  . HIS A 1 950  ? 62.393 55.421  -22.633 1.00 17.40 ? 950  HIS A CG  1 
ATOM   7560 N  ND1 . HIS A 1 950  ? 63.640 55.064  -22.156 1.00 19.59 ? 950  HIS A ND1 1 
ATOM   7561 C  CD2 . HIS A 1 950  ? 62.075 56.580  -22.016 1.00 13.48 ? 950  HIS A CD2 1 
ATOM   7562 C  CE1 . HIS A 1 950  ? 64.045 55.969  -21.279 1.00 15.58 ? 950  HIS A CE1 1 
ATOM   7563 N  NE2 . HIS A 1 950  ? 63.109 56.899  -21.181 1.00 21.46 ? 950  HIS A NE2 1 
ATOM   7564 N  N   . PRO A 1 951  ? 60.717 51.631  -24.688 1.00 18.87 ? 951  PRO A N   1 
ATOM   7565 C  CA  . PRO A 1 951  ? 59.696 50.862  -25.400 1.00 19.75 ? 951  PRO A CA  1 
ATOM   7566 C  C   . PRO A 1 951  ? 58.403 51.659  -25.549 1.00 19.53 ? 951  PRO A C   1 
ATOM   7567 O  O   . PRO A 1 951  ? 57.971 52.334  -24.595 1.00 19.97 ? 951  PRO A O   1 
ATOM   7568 C  CB  . PRO A 1 951  ? 59.487 49.627  -24.495 1.00 21.21 ? 951  PRO A CB  1 
ATOM   7569 C  CG  . PRO A 1 951  ? 60.779 49.490  -23.828 1.00 24.11 ? 951  PRO A CG  1 
ATOM   7570 C  CD  . PRO A 1 951  ? 61.173 50.917  -23.485 1.00 21.78 ? 951  PRO A CD  1 
ATOM   7571 N  N   . SER A 1 952  ? 57.775 51.579  -26.711 1.00 19.33 ? 952  SER A N   1 
ATOM   7572 C  CA  . SER A 1 952  ? 56.531 52.291  -26.928 1.00 17.96 ? 952  SER A CA  1 
ATOM   7573 C  C   . SER A 1 952  ? 55.440 51.234  -26.757 1.00 18.90 ? 952  SER A C   1 
ATOM   7574 O  O   . SER A 1 952  ? 55.137 50.430  -27.685 1.00 20.37 ? 952  SER A O   1 
ATOM   7575 C  CB  . SER A 1 952  ? 56.499 52.921  -28.318 1.00 17.35 ? 952  SER A CB  1 
ATOM   7576 O  OG  . SER A 1 952  ? 55.404 53.824  -28.463 1.00 20.87 ? 952  SER A OG  1 
ATOM   7577 N  N   . ALA A 1 953  ? 54.858 51.217  -25.559 1.00 18.54 ? 953  ALA A N   1 
ATOM   7578 C  CA  . ALA A 1 953  ? 53.878 50.230  -25.167 1.00 17.53 ? 953  ALA A CA  1 
ATOM   7579 C  C   . ALA A 1 953  ? 52.515 50.346  -25.791 1.00 15.49 ? 953  ALA A C   1 
ATOM   7580 O  O   . ALA A 1 953  ? 52.115 51.396  -26.267 1.00 16.81 ? 953  ALA A O   1 
ATOM   7581 C  CB  . ALA A 1 953  ? 53.753 50.238  -23.620 1.00 18.87 ? 953  ALA A CB  1 
ATOM   7582 N  N   . ARG A 1 954  ? 51.795 49.236  -25.790 1.00 15.71 ? 954  ARG A N   1 
ATOM   7583 C  CA  . ARG A 1 954  ? 50.456 49.165  -26.315 1.00 17.65 ? 954  ARG A CA  1 
ATOM   7584 C  C   . ARG A 1 954  ? 49.616 50.306  -25.713 1.00 16.30 ? 954  ARG A C   1 
ATOM   7585 O  O   . ARG A 1 954  ? 49.750 50.640  -24.522 1.00 15.73 ? 954  ARG A O   1 
ATOM   7586 C  CB  . ARG A 1 954  ? 49.886 47.799  -25.968 1.00 21.14 ? 954  ARG A CB  1 
ATOM   7587 C  CG  . ARG A 1 954  ? 48.580 47.532  -26.660 1.00 33.61 ? 954  ARG A CG  1 
ATOM   7588 C  CD  . ARG A 1 954  ? 48.493 46.065  -27.092 1.00 37.54 ? 954  ARG A CD  1 
ATOM   7589 N  NE  . ARG A 1 954  ? 47.562 45.303  -26.263 1.00 42.89 ? 954  ARG A NE  1 
ATOM   7590 C  CZ  . ARG A 1 954  ? 46.318 45.694  -26.026 1.00 43.93 ? 954  ARG A CZ  1 
ATOM   7591 N  NH1 . ARG A 1 954  ? 45.882 46.838  -26.543 1.00 46.50 ? 954  ARG A NH1 1 
ATOM   7592 N  NH2 . ARG A 1 954  ? 45.493 44.935  -25.314 1.00 44.00 ? 954  ARG A NH2 1 
ATOM   7593 N  N   . GLU A 1 955  ? 48.712 50.855  -26.513 1.00 15.04 ? 955  GLU A N   1 
ATOM   7594 C  CA  . GLU A 1 955  ? 47.933 52.027  -26.125 1.00 16.11 ? 955  GLU A CA  1 
ATOM   7595 C  C   . GLU A 1 955  ? 47.089 51.905  -24.863 1.00 14.63 ? 955  GLU A C   1 
ATOM   7596 O  O   . GLU A 1 955  ? 46.777 52.944  -24.236 1.00 15.87 ? 955  GLU A O   1 
ATOM   7597 C  CB  . GLU A 1 955  ? 47.044 52.494  -27.303 1.00 19.07 ? 955  GLU A CB  1 
ATOM   7598 C  CG  . GLU A 1 955  ? 45.953 51.511  -27.642 1.00 20.02 ? 955  GLU A CG  1 
ATOM   7599 C  CD  . GLU A 1 955  ? 45.048 51.983  -28.743 1.00 25.65 ? 955  GLU A CD  1 
ATOM   7600 O  OE1 . GLU A 1 955  ? 44.864 53.209  -28.887 1.00 31.76 ? 955  GLU A OE1 1 
ATOM   7601 O  OE2 . GLU A 1 955  ? 44.514 51.105  -29.455 1.00 27.42 ? 955  GLU A OE2 1 
ATOM   7602 N  N   . ASP A 1 956  ? 46.700 50.684  -24.493 1.00 12.75 ? 956  ASP A N   1 
ATOM   7603 C  CA  . ASP A 1 956  ? 45.866 50.543  -23.300 1.00 13.84 ? 956  ASP A CA  1 
ATOM   7604 C  C   . ASP A 1 956  ? 46.694 50.434  -22.024 1.00 14.32 ? 956  ASP A C   1 
ATOM   7605 O  O   . ASP A 1 956  ? 46.114 50.356  -20.949 1.00 16.13 ? 956  ASP A O   1 
ATOM   7606 C  CB  . ASP A 1 956  ? 44.869 49.360  -23.418 1.00 14.34 ? 956  ASP A CB  1 
ATOM   7607 C  CG  . ASP A 1 956  ? 45.524 48.038  -23.758 1.00 18.25 ? 956  ASP A CG  1 
ATOM   7608 O  OD1 . ASP A 1 956  ? 46.741 48.011  -23.999 1.00 21.11 ? 956  ASP A OD1 1 
ATOM   7609 O  OD2 . ASP A 1 956  ? 44.785 47.026  -23.789 1.00 20.94 ? 956  ASP A OD2 1 
ATOM   7610 N  N   . LEU A 1 957  ? 48.010 50.436  -22.134 1.00 14.12 ? 957  LEU A N   1 
ATOM   7611 C  CA  . LEU A 1 957  ? 48.875 50.292  -20.947 1.00 13.12 ? 957  LEU A CA  1 
ATOM   7612 C  C   . LEU A 1 957  ? 49.449 51.636  -20.542 1.00 12.59 ? 957  LEU A C   1 
ATOM   7613 O  O   . LEU A 1 957  ? 49.877 52.415  -21.404 1.00 15.77 ? 957  LEU A O   1 
ATOM   7614 C  CB  . LEU A 1 957  ? 50.032 49.338  -21.290 1.00 13.17 ? 957  LEU A CB  1 
ATOM   7615 C  CG  . LEU A 1 957  ? 50.901 48.901  -20.106 1.00 16.87 ? 957  LEU A CG  1 
ATOM   7616 C  CD1 . LEU A 1 957  ? 50.047 48.189  -19.050 1.00 20.35 ? 957  LEU A CD1 1 
ATOM   7617 C  CD2 . LEU A 1 957  ? 52.012 47.950  -20.618 1.00 18.99 ? 957  LEU A CD2 1 
ATOM   7618 N  N   . ASP A 1 958  ? 49.465 51.918  -19.233 1.00 13.19 ? 958  ASP A N   1 
ATOM   7619 C  CA  . ASP A 1 958  ? 50.108 53.144  -18.755 1.00 12.87 ? 958  ASP A CA  1 
ATOM   7620 C  C   . ASP A 1 958  ? 51.046 52.844  -17.609 1.00 11.24 ? 958  ASP A C   1 
ATOM   7621 O  O   . ASP A 1 958  ? 50.819 51.868  -16.857 1.00 13.16 ? 958  ASP A O   1 
ATOM   7622 C  CB  . ASP A 1 958  ? 49.047 54.145  -18.272 1.00 12.55 ? 958  ASP A CB  1 
ATOM   7623 C  CG  . ASP A 1 958  ? 49.604 55.552  -18.082 1.00 12.87 ? 958  ASP A CG  1 
ATOM   7624 O  OD1 . ASP A 1 958  ? 50.720 55.846  -18.568 1.00 13.67 ? 958  ASP A OD1 1 
ATOM   7625 O  OD2 . ASP A 1 958  ? 48.887 56.349  -17.420 1.00 15.53 ? 958  ASP A OD2 1 
ATOM   7626 N  N   . VAL A 1 959  ? 52.109 53.639  -17.498 1.00 11.61 ? 959  VAL A N   1 
ATOM   7627 C  CA  . VAL A 1 959  ? 52.979 53.572  -16.318 1.00 11.68 ? 959  VAL A CA  1 
ATOM   7628 C  C   . VAL A 1 959  ? 52.415 54.705  -15.473 1.00 12.56 ? 959  VAL A C   1 
ATOM   7629 O  O   . VAL A 1 959  ? 52.823 55.849  -15.572 1.00 13.08 ? 959  VAL A O   1 
ATOM   7630 C  CB  . VAL A 1 959  ? 54.433 53.814  -16.687 1.00 12.39 ? 959  VAL A CB  1 
ATOM   7631 C  CG1 . VAL A 1 959  ? 55.295 53.952  -15.378 1.00 12.43 ? 959  VAL A CG1 1 
ATOM   7632 C  CG2 . VAL A 1 959  ? 54.936 52.611  -17.506 1.00 15.11 ? 959  VAL A CG2 1 
ATOM   7633 N  N   . SER A 1 960  ? 51.443 54.379  -14.621 1.00 11.50 ? 960  SER A N   1 
ATOM   7634 C  CA  . SER A 1 960  ? 50.745 55.377  -13.806 1.00 11.25 ? 960  SER A CA  1 
ATOM   7635 C  C   . SER A 1 960  ? 51.662 56.081  -12.828 1.00 13.44 ? 960  SER A C   1 
ATOM   7636 O  O   . SER A 1 960  ? 51.520 57.288  -12.573 1.00 14.36 ? 960  SER A O   1 
ATOM   7637 C  CB  . SER A 1 960  ? 49.636 54.680  -13.031 1.00 12.45 ? 960  SER A CB  1 
ATOM   7638 O  OG  . SER A 1 960  ? 48.803 53.881  -13.892 1.00 15.13 ? 960  SER A OG  1 
ATOM   7639 N  N   . VAL A 1 961  ? 52.592 55.289  -12.284 1.00 12.83 ? 961  VAL A N   1 
ATOM   7640 C  CA  . VAL A 1 961  ? 53.575 55.816  -11.336 1.00 12.86 ? 961  VAL A CA  1 
ATOM   7641 C  C   . VAL A 1 961  ? 54.976 55.252  -11.640 1.00 12.13 ? 961  VAL A C   1 
ATOM   7642 O  O   . VAL A 1 961  ? 55.136 54.051  -11.914 1.00 12.60 ? 961  VAL A O   1 
ATOM   7643 C  CB  . VAL A 1 961  ? 53.252 55.377  -9.886  1.00 12.29 ? 961  VAL A CB  1 
ATOM   7644 C  CG1 . VAL A 1 961  ? 54.395 55.812  -8.917  1.00 13.93 ? 961  VAL A CG1 1 
ATOM   7645 C  CG2 . VAL A 1 961  ? 51.913 56.004  -9.423  1.00 14.73 ? 961  VAL A CG2 1 
ATOM   7646 N  N   . MET A 1 962  ? 55.968 56.150  -11.634 1.00 12.52 ? 962  MET A N   1 
ATOM   7647 C  CA  . MET A 1 962  ? 57.370 55.731  -11.652 1.00 11.41 ? 962  MET A CA  1 
ATOM   7648 C  C   . MET A 1 962  ? 57.947 56.554  -10.500 1.00 11.75 ? 962  MET A C   1 
ATOM   7649 O  O   . MET A 1 962  ? 57.897 57.790  -10.493 1.00 13.43 ? 962  MET A O   1 
ATOM   7650 C  CB  . MET A 1 962  ? 58.106 56.076  -12.967 1.00 13.80 ? 962  MET A CB  1 
ATOM   7651 C  CG  . MET A 1 962  ? 59.593 55.717  -12.877 1.00 13.56 ? 962  MET A CG  1 
ATOM   7652 S  SD  . MET A 1 962  ? 60.348 56.024  -14.494 1.00 14.79 ? 962  MET A SD  1 
ATOM   7653 C  CE  . MET A 1 962  ? 62.094 55.519  -14.135 1.00 17.72 ? 962  MET A CE  1 
ATOM   7654 N  N   . ARG A 1 963  ? 58.511 55.851  -9.503  1.00 12.49 ? 963  ARG A N   1 
ATOM   7655 C  CA  . ARG A 1 963  ? 59.055 56.506  -8.321  1.00 11.52 ? 963  ARG A CA  1 
ATOM   7656 C  C   . ARG A 1 963  ? 60.292 55.841  -7.786  1.00 11.82 ? 963  ARG A C   1 
ATOM   7657 O  O   . ARG A 1 963  ? 60.237 54.666  -7.435  1.00 13.15 ? 963  ARG A O   1 
ATOM   7658 C  CB  . ARG A 1 963  ? 57.980 56.482  -7.200  1.00 13.19 ? 963  ARG A CB  1 
ATOM   7659 C  CG  . ARG A 1 963  ? 58.438 57.089  -5.844  1.00 13.59 ? 963  ARG A CG  1 
ATOM   7660 C  CD  . ARG A 1 963  ? 57.353 56.948  -4.716  1.00 14.95 ? 963  ARG A CD  1 
ATOM   7661 N  NE  . ARG A 1 963  ? 56.147 57.657  -5.155  1.00 12.86 ? 963  ARG A NE  1 
ATOM   7662 C  CZ  . ARG A 1 963  ? 54.918 57.148  -5.092  1.00 12.75 ? 963  ARG A CZ  1 
ATOM   7663 N  NH1 . ARG A 1 963  ? 54.638 55.943  -4.568  1.00 12.61 ? 963  ARG A NH1 1 
ATOM   7664 N  NH2 . ARG A 1 963  ? 53.945 57.824  -5.717  1.00 13.20 ? 963  ARG A NH2 1 
ATOM   7665 N  N   . ARG A 1 964  ? 61.398 56.578  -7.698  1.00 12.63 ? 964  ARG A N   1 
ATOM   7666 C  CA  . ARG A 1 964  ? 62.606 55.968  -7.081  1.00 13.42 ? 964  ARG A CA  1 
ATOM   7667 C  C   . ARG A 1 964  ? 62.283 55.920  -5.564  1.00 13.38 ? 964  ARG A C   1 
ATOM   7668 O  O   . ARG A 1 964  ? 61.852 56.902  -4.961  1.00 13.68 ? 964  ARG A O   1 
ATOM   7669 C  CB  . ARG A 1 964  ? 63.814 56.855  -7.356  1.00 13.20 ? 964  ARG A CB  1 
ATOM   7670 C  CG  . ARG A 1 964  ? 65.089 56.234  -6.762  1.00 14.09 ? 964  ARG A CG  1 
ATOM   7671 C  CD  . ARG A 1 964  ? 66.367 56.913  -7.246  1.00 14.26 ? 964  ARG A CD  1 
ATOM   7672 N  NE  . ARG A 1 964  ? 66.562 56.743  -8.678  1.00 15.03 ? 964  ARG A NE  1 
ATOM   7673 C  CZ  . ARG A 1 964  ? 67.435 55.922  -9.244  1.00 15.96 ? 964  ARG A CZ  1 
ATOM   7674 N  NH1 . ARG A 1 964  ? 68.228 55.142  -8.487  1.00 18.61 ? 964  ARG A NH1 1 
ATOM   7675 N  NH2 . ARG A 1 964  ? 67.562 55.887  -10.574 1.00 18.87 ? 964  ARG A NH2 1 
ATOM   7676 N  N   . LEU A 1 965  ? 62.531 54.747  -4.985  1.00 14.07 ? 965  LEU A N   1 
ATOM   7677 C  CA  . LEU A 1 965  ? 62.159 54.497  -3.589  1.00 12.78 ? 965  LEU A CA  1 
ATOM   7678 C  C   . LEU A 1 965  ? 63.324 54.627  -2.615  1.00 15.91 ? 965  LEU A C   1 
ATOM   7679 O  O   . LEU A 1 965  ? 63.111 54.575  -1.397  1.00 17.42 ? 965  LEU A O   1 
ATOM   7680 C  CB  . LEU A 1 965  ? 61.582 53.093  -3.478  1.00 14.89 ? 965  LEU A CB  1 
ATOM   7681 C  CG  . LEU A 1 965  ? 60.348 52.824  -4.376  1.00 14.50 ? 965  LEU A CG  1 
ATOM   7682 C  CD1 . LEU A 1 965  ? 59.978 51.344  -4.342  1.00 15.41 ? 965  LEU A CD1 1 
ATOM   7683 C  CD2 . LEU A 1 965  ? 59.179 53.671  -3.914  1.00 15.60 ? 965  LEU A CD2 1 
ATOM   7684 N  N   . THR A 1 966  ? 64.528 54.780  -3.153  1.00 15.29 ? 966  THR A N   1 
ATOM   7685 C  CA  . THR A 1 966  ? 65.732 54.883  -2.313  1.00 15.69 ? 966  THR A CA  1 
ATOM   7686 C  C   . THR A 1 966  ? 66.441 56.205  -2.507  1.00 15.46 ? 966  THR A C   1 
ATOM   7687 O  O   . THR A 1 966  ? 66.438 56.761  -3.608  1.00 15.40 ? 966  THR A O   1 
ATOM   7688 C  CB  . THR A 1 966  ? 66.753 53.797  -2.711  1.00 15.65 ? 966  THR A CB  1 
ATOM   7689 O  OG1 . THR A 1 966  ? 66.825 53.722  -4.142  1.00 17.61 ? 966  THR A OG1 1 
ATOM   7690 C  CG2 . THR A 1 966  ? 66.343 52.435  -2.175  1.00 17.75 ? 966  THR A CG2 1 
ATOM   7691 N  N   . LYS A 1 967  ? 67.096 56.682  -1.440  1.00 16.14 ? 967  LYS A N   1 
ATOM   7692 C  CA  . LYS A 1 967  ? 67.912 57.879  -1.484  1.00 17.66 ? 967  LYS A CA  1 
ATOM   7693 C  C   . LYS A 1 967  ? 69.312 57.454  -1.990  1.00 16.96 ? 967  LYS A C   1 
ATOM   7694 O  O   . LYS A 1 967  ? 69.596 56.266  -2.162  1.00 16.68 ? 967  LYS A O   1 
ATOM   7695 C  CB  . LYS A 1 967  ? 68.018 58.509  -0.113  1.00 19.65 ? 967  LYS A CB  1 
ATOM   7696 C  CG  . LYS A 1 967  ? 66.672 59.055  0.375   1.00 23.49 ? 967  LYS A CG  1 
ATOM   7697 C  CD  . LYS A 1 967  ? 66.860 59.826  1.649   1.00 27.33 ? 967  LYS A CD  1 
ATOM   7698 C  CE  . LYS A 1 967  ? 65.696 60.776  1.894   1.00 34.04 ? 967  LYS A CE  1 
ATOM   7699 N  NZ  . LYS A 1 967  ? 66.168 61.924  2.747   1.00 37.49 ? 967  LYS A NZ  1 
ATOM   7700 N  N   . SER A 1 968  ? 70.142 58.455  -2.264  1.00 18.07 ? 968  SER A N   1 
ATOM   7701 C  CA  . SER A 1 968  ? 71.440 58.208  -2.880  1.00 19.84 ? 968  SER A CA  1 
ATOM   7702 C  C   . SER A 1 968  ? 72.426 57.349  -2.091  1.00 21.68 ? 968  SER A C   1 
ATOM   7703 O  O   . SER A 1 968  ? 73.257 56.669  -2.696  1.00 24.33 ? 968  SER A O   1 
ATOM   7704 C  CB  . SER A 1 968  ? 72.102 59.548  -3.274  1.00 21.44 ? 968  SER A CB  1 
ATOM   7705 O  OG  . SER A 1 968  ? 72.403 60.329  -2.144  1.00 28.82 ? 968  SER A OG  1 
ATOM   7706 N  N   . SER A 1 969  ? 72.279 57.326  -0.777  1.00 21.57 ? 969  SER A N   1 
ATOM   7707 C  CA  . SER A 1 969  ? 73.222 56.553  0.053   1.00 24.27 ? 969  SER A CA  1 
ATOM   7708 C  C   . SER A 1 969  ? 72.963 55.046  0.027   1.00 23.53 ? 969  SER A C   1 
ATOM   7709 O  O   . SER A 1 969  ? 73.775 54.280  0.527   1.00 23.83 ? 969  SER A O   1 
ATOM   7710 C  CB  . SER A 1 969  ? 73.191 57.052  1.479   1.00 26.54 ? 969  SER A CB  1 
ATOM   7711 O  OG  . SER A 1 969  ? 71.969 56.699  2.095   1.00 34.72 ? 969  SER A OG  1 
ATOM   7712 N  N   . ALA A 1 970  ? 71.843 54.599  -0.541  1.00 20.04 ? 970  ALA A N   1 
ATOM   7713 C  CA  . ALA A 1 970  ? 71.580 53.173  -0.636  1.00 20.22 ? 970  ALA A CA  1 
ATOM   7714 C  C   . ALA A 1 970  ? 72.417 52.469  -1.676  1.00 22.02 ? 970  ALA A C   1 
ATOM   7715 O  O   . ALA A 1 970  ? 72.412 52.823  -2.863  1.00 22.20 ? 970  ALA A O   1 
ATOM   7716 C  CB  . ALA A 1 970  ? 70.073 52.879  -0.940  1.00 20.87 ? 970  ALA A CB  1 
ATOM   7717 N  N   . LYS A 1 971  ? 73.129 51.445  -1.227  1.00 23.65 ? 971  LYS A N   1 
ATOM   7718 C  CA  . LYS A 1 971  ? 73.957 50.634  -2.091  1.00 24.47 ? 971  LYS A CA  1 
ATOM   7719 C  C   . LYS A 1 971  ? 73.104 50.037  -3.210  1.00 23.19 ? 971  LYS A C   1 
ATOM   7720 O  O   . LYS A 1 971  ? 73.502 50.045  -4.368  1.00 24.26 ? 971  LYS A O   1 
ATOM   7721 C  CB  . LYS A 1 971  ? 74.596 49.518  -1.257  1.00 26.11 ? 971  LYS A CB  1 
ATOM   7722 C  CG  A LYS A 1 971  ? 75.738 48.801  -1.931  0.50 31.96 ? 971  LYS A CG  1 
ATOM   7723 C  CG  B LYS A 1 971  ? 75.764 48.825  -2.198  0.50 31.40 ? 971  LYS A CG  1 
ATOM   7724 C  CD  A LYS A 1 971  ? 76.336 47.751  -0.993  0.50 33.83 ? 971  LYS A CD  1 
ATOM   7725 C  CD  B LYS A 1 971  ? 76.697 47.999  -1.308  0.50 34.31 ? 971  LYS A CD  1 
ATOM   7726 C  CE  A LYS A 1 971  ? 76.535 48.295  0.420   0.50 36.04 ? 971  LYS A CE  1 
ATOM   7727 C  CE  B LYS A 1 971  ? 77.722 47.226  -2.132  0.50 35.43 ? 971  LYS A CE  1 
ATOM   7728 N  NZ  A LYS A 1 971  ? 77.302 49.568  0.436   0.50 36.30 ? 971  LYS A NZ  1 
ATOM   7729 N  NZ  B LYS A 1 971  ? 78.647 46.430  -1.272  0.50 38.36 ? 971  LYS A NZ  1 
ATOM   7730 N  N   . THR A 1 972  ? 71.934 49.509  -2.854  1.00 21.04 ? 972  THR A N   1 
ATOM   7731 C  CA  . THR A 1 972  ? 71.038 48.924  -3.844  1.00 22.11 ? 972  THR A CA  1 
ATOM   7732 C  C   . THR A 1 972  ? 69.878 49.897  -4.119  1.00 19.25 ? 972  THR A C   1 
ATOM   7733 O  O   . THR A 1 972  ? 69.025 50.091  -3.266  1.00 20.75 ? 972  THR A O   1 
ATOM   7734 C  CB  . THR A 1 972  ? 70.467 47.569  -3.399  1.00 24.57 ? 972  THR A CB  1 
ATOM   7735 O  OG1 . THR A 1 972  ? 71.560 46.662  -3.191  1.00 25.92 ? 972  THR A OG1 1 
ATOM   7736 C  CG2 . THR A 1 972  ? 69.579 46.946  -4.489  1.00 24.03 ? 972  THR A CG2 1 
ATOM   7737 N  N   . GLN A 1 973  ? 69.871 50.525  -5.290  1.00 18.07 ? 973  GLN A N   1 
ATOM   7738 C  CA  . GLN A 1 973  ? 68.771 51.452  -5.623  1.00 16.91 ? 973  GLN A CA  1 
ATOM   7739 C  C   . GLN A 1 973  ? 67.499 50.687  -5.995  1.00 16.87 ? 973  GLN A C   1 
ATOM   7740 O  O   . GLN A 1 973  ? 67.549 49.629  -6.579  1.00 19.03 ? 973  GLN A O   1 
ATOM   7741 C  CB  . GLN A 1 973  ? 69.214 52.340  -6.783  1.00 16.74 ? 973  GLN A CB  1 
ATOM   7742 C  CG  . GLN A 1 973  ? 70.313 53.318  -6.364  1.00 16.54 ? 973  GLN A CG  1 
ATOM   7743 C  CD  . GLN A 1 973  ? 69.869 54.304  -5.344  1.00 18.83 ? 973  GLN A CD  1 
ATOM   7744 O  OE1 . GLN A 1 973  ? 70.487 54.472  -4.263  1.00 20.54 ? 973  GLN A OE1 1 
ATOM   7745 N  NE2 . GLN A 1 973  ? 68.789 54.999  -5.662  1.00 14.69 ? 973  GLN A NE2 1 
ATOM   7746 N  N   . ARG A 1 974  ? 66.338 51.271  -5.693  1.00 16.39 ? 974  ARG A N   1 
ATOM   7747 C  CA  . ARG A 1 974  ? 65.083 50.608  -6.012  1.00 16.29 ? 974  ARG A CA  1 
ATOM   7748 C  C   . ARG A 1 974  ? 64.134 51.621  -6.658  1.00 13.79 ? 974  ARG A C   1 
ATOM   7749 O  O   . ARG A 1 974  ? 64.058 52.779  -6.211  1.00 16.01 ? 974  ARG A O   1 
ATOM   7750 C  CB  . ARG A 1 974  ? 64.426 50.064  -4.742  1.00 16.24 ? 974  ARG A CB  1 
ATOM   7751 C  CG  . ARG A 1 974  ? 65.311 49.035  -3.952  1.00 17.36 ? 974  ARG A CG  1 
ATOM   7752 C  CD  . ARG A 1 974  ? 64.741 48.810  -2.519  1.00 20.48 ? 974  ARG A CD  1 
ATOM   7753 N  NE  . ARG A 1 974  ? 63.478 48.076  -2.581  1.00 27.08 ? 974  ARG A NE  1 
ATOM   7754 C  CZ  . ARG A 1 974  ? 62.313 48.476  -2.077  1.00 24.60 ? 974  ARG A CZ  1 
ATOM   7755 N  NH1 . ARG A 1 974  ? 62.189 49.632  -1.429  1.00 26.85 ? 974  ARG A NH1 1 
ATOM   7756 N  NH2 . ARG A 1 974  ? 61.251 47.708  -2.255  1.00 23.13 ? 974  ARG A NH2 1 
ATOM   7757 N  N   . VAL A 1 975  ? 63.471 51.174  -7.715  1.00 16.00 ? 975  VAL A N   1 
ATOM   7758 C  CA  . VAL A 1 975  ? 62.528 52.048  -8.405  1.00 15.35 ? 975  VAL A CA  1 
ATOM   7759 C  C   . VAL A 1 975  ? 61.217 51.298  -8.511  1.00 16.33 ? 975  VAL A C   1 
ATOM   7760 O  O   . VAL A 1 975  ? 61.162 50.125  -8.967  1.00 14.70 ? 975  VAL A O   1 
ATOM   7761 C  CB  . VAL A 1 975  ? 63.039 52.409  -9.811  1.00 14.88 ? 975  VAL A CB  1 
ATOM   7762 C  CG1 . VAL A 1 975  ? 62.002 53.301  -10.542 1.00 15.63 ? 975  VAL A CG1 1 
ATOM   7763 C  CG2 . VAL A 1 975  ? 64.360 53.176  -9.665  1.00 17.43 ? 975  VAL A CG2 1 
ATOM   7764 N  N   . GLY A 1 976  ? 60.144 51.981  -8.107  1.00 15.69 ? 976  GLY A N   1 
ATOM   7765 C  CA  . GLY A 1 976  ? 58.822 51.387  -8.175  1.00 13.79 ? 976  GLY A CA  1 
ATOM   7766 C  C   . GLY A 1 976  ? 58.010 51.894  -9.346  1.00 13.04 ? 976  GLY A C   1 
ATOM   7767 O  O   . GLY A 1 976  ? 58.087 53.065  -9.738  1.00 14.47 ? 976  GLY A O   1 
ATOM   7768 N  N   . TYR A 1 977  ? 57.239 50.978  -9.885  1.00 12.96 ? 977  TYR A N   1 
ATOM   7769 C  CA  . TYR A 1 977  ? 56.344 51.275  -11.016 1.00 11.61 ? 977  TYR A CA  1 
ATOM   7770 C  C   . TYR A 1 977  ? 54.944 50.767  -10.737 1.00 13.46 ? 977  TYR A C   1 
ATOM   7771 O  O   . TYR A 1 977  ? 54.777 49.657  -10.233 1.00 14.22 ? 977  TYR A O   1 
ATOM   7772 C  CB  . TYR A 1 977  ? 56.808 50.563  -12.301 1.00 13.15 ? 977  TYR A CB  1 
ATOM   7773 C  CG  . TYR A 1 977  ? 58.188 50.927  -12.719 1.00 12.00 ? 977  TYR A CG  1 
ATOM   7774 C  CD1 . TYR A 1 977  ? 59.316 50.222  -12.229 1.00 14.02 ? 977  TYR A CD1 1 
ATOM   7775 C  CD2 . TYR A 1 977  ? 58.389 51.978  -13.576 1.00 13.43 ? 977  TYR A CD2 1 
ATOM   7776 C  CE1 . TYR A 1 977  ? 60.615 50.580  -12.621 1.00 14.99 ? 977  TYR A CE1 1 
ATOM   7777 C  CE2 . TYR A 1 977  ? 59.680 52.361  -13.969 1.00 15.69 ? 977  TYR A CE2 1 
ATOM   7778 C  CZ  . TYR A 1 977  ? 60.789 51.647  -13.487 1.00 15.12 ? 977  TYR A CZ  1 
ATOM   7779 O  OH  . TYR A 1 977  ? 62.056 52.027  -13.912 1.00 16.77 ? 977  TYR A OH  1 
ATOM   7780 N  N   . VAL A 1 978  ? 53.924 51.589  -11.045 1.00 12.64 ? 978  VAL A N   1 
ATOM   7781 C  CA  . VAL A 1 978  ? 52.574 51.106  -10.997 1.00 12.01 ? 978  VAL A CA  1 
ATOM   7782 C  C   . VAL A 1 978  ? 52.124 51.051  -12.477 1.00 13.62 ? 978  VAL A C   1 
ATOM   7783 O  O   . VAL A 1 978  ? 52.199 52.080  -13.159 1.00 13.16 ? 978  VAL A O   1 
ATOM   7784 C  CB  . VAL A 1 978  ? 51.599 52.027  -10.202 1.00 12.16 ? 978  VAL A CB  1 
ATOM   7785 C  CG1 . VAL A 1 978  ? 50.173 51.512  -10.361 1.00 14.48 ? 978  VAL A CG1 1 
ATOM   7786 C  CG2 . VAL A 1 978  ? 52.013 52.071  -8.702  1.00 13.62 ? 978  VAL A CG2 1 
ATOM   7787 N  N   . LEU A 1 979  ? 51.725 49.889  -12.960 1.00 12.40 ? 979  LEU A N   1 
ATOM   7788 C  CA  . LEU A 1 979  ? 51.280 49.697  -14.332 1.00 13.97 ? 979  LEU A CA  1 
ATOM   7789 C  C   . LEU A 1 979  ? 49.805 49.446  -14.340 1.00 14.46 ? 979  LEU A C   1 
ATOM   7790 O  O   . LEU A 1 979  ? 49.304 48.578  -13.612 1.00 16.26 ? 979  LEU A O   1 
ATOM   7791 C  CB  . LEU A 1 979  ? 51.903 48.448  -14.925 1.00 18.40 ? 979  LEU A CB  1 
ATOM   7792 C  CG  . LEU A 1 979  ? 53.322 48.403  -15.401 1.00 26.67 ? 979  LEU A CG  1 
ATOM   7793 C  CD1 . LEU A 1 979  ? 53.407 47.193  -16.362 1.00 29.40 ? 979  LEU A CD1 1 
ATOM   7794 C  CD2 . LEU A 1 979  ? 53.665 49.653  -16.167 1.00 27.47 ? 979  LEU A CD2 1 
ATOM   7795 N  N   . HIS A 1 980  ? 49.090 50.200  -15.156 1.00 13.96 ? 980  HIS A N   1 
ATOM   7796 C  CA  . HIS A 1 980  ? 47.665 50.037  -15.278 1.00 14.05 ? 980  HIS A CA  1 
ATOM   7797 C  C   . HIS A 1 980  ? 47.270 49.763  -16.721 1.00 14.48 ? 980  HIS A C   1 
ATOM   7798 O  O   . HIS A 1 980  ? 47.705 50.486  -17.595 1.00 16.00 ? 980  HIS A O   1 
ATOM   7799 C  CB  . HIS A 1 980  ? 46.873 51.292  -14.852 1.00 14.94 ? 980  HIS A CB  1 
ATOM   7800 C  CG  . HIS A 1 980  ? 45.401 51.072  -14.944 1.00 14.43 ? 980  HIS A CG  1 
ATOM   7801 N  ND1 . HIS A 1 980  ? 44.564 51.638  -15.891 1.00 16.94 ? 980  HIS A ND1 1 
ATOM   7802 C  CD2 . HIS A 1 980  ? 44.638 50.194  -14.257 1.00 11.34 ? 980  HIS A CD2 1 
ATOM   7803 C  CE1 . HIS A 1 980  ? 43.352 51.124  -15.769 1.00 12.29 ? 980  HIS A CE1 1 
ATOM   7804 N  NE2 . HIS A 1 980  ? 43.371 50.242  -14.788 1.00 17.88 ? 980  HIS A NE2 1 
ATOM   7805 N  N   . ARG A 1 981  ? 46.485 48.724  -16.956 1.00 13.62 ? 981  ARG A N   1 
ATOM   7806 C  CA  . ARG A 1 981  ? 46.007 48.475  -18.297 1.00 14.30 ? 981  ARG A CA  1 
ATOM   7807 C  C   . ARG A 1 981  ? 44.514 48.649  -18.251 1.00 13.77 ? 981  ARG A C   1 
ATOM   7808 O  O   . ARG A 1 981  ? 43.823 48.007  -17.465 1.00 14.85 ? 981  ARG A O   1 
ATOM   7809 C  CB  . ARG A 1 981  ? 46.359 47.077  -18.715 1.00 16.86 ? 981  ARG A CB  1 
ATOM   7810 C  CG  . ARG A 1 981  ? 46.043 46.827  -20.168 1.00 20.82 ? 981  ARG A CG  1 
ATOM   7811 C  CD  . ARG A 1 981  ? 46.749 45.545  -20.601 1.00 25.79 ? 981  ARG A CD  1 
ATOM   7812 N  NE  . ARG A 1 981  ? 46.263 45.137  -21.892 1.00 29.88 ? 981  ARG A NE  1 
ATOM   7813 C  CZ  . ARG A 1 981  ? 46.396 43.909  -22.371 1.00 32.12 ? 981  ARG A CZ  1 
ATOM   7814 N  NH1 . ARG A 1 981  ? 47.011 42.983  -21.652 1.00 31.44 ? 981  ARG A NH1 1 
ATOM   7815 N  NH2 . ARG A 1 981  ? 45.885 43.600  -23.554 1.00 32.84 ? 981  ARG A NH2 1 
ATOM   7816 N  N   . THR A 1 982  ? 44.000 49.524  -19.106 1.00 13.93 ? 982  THR A N   1 
ATOM   7817 C  CA  . THR A 1 982  ? 42.547 49.736  -19.181 1.00 13.78 ? 982  THR A CA  1 
ATOM   7818 C  C   . THR A 1 982  ? 41.988 48.704  -20.192 1.00 15.04 ? 982  THR A C   1 
ATOM   7819 O  O   . THR A 1 982  ? 42.715 47.773  -20.583 1.00 17.77 ? 982  THR A O   1 
ATOM   7820 C  CB  . THR A 1 982  ? 42.244 51.190  -19.626 1.00 13.53 ? 982  THR A CB  1 
ATOM   7821 O  OG1 . THR A 1 982  ? 40.853 51.477  -19.474 1.00 14.31 ? 982  THR A OG1 1 
ATOM   7822 C  CG2 . THR A 1 982  ? 42.666 51.467  -21.073 1.00 15.56 ? 982  THR A CG2 1 
ATOM   7823 N  N   . ASN A 1 983  ? 40.707 48.798  -20.507 1.00 14.44 ? 983  ASN A N   1 
ATOM   7824 C  CA  . ASN A 1 983  ? 40.144 47.895  -21.533 1.00 14.18 ? 983  ASN A CA  1 
ATOM   7825 C  C   . ASN A 1 983  ? 39.443 48.754  -22.560 1.00 15.62 ? 983  ASN A C   1 
ATOM   7826 O  O   . ASN A 1 983  ? 38.537 49.509  -22.223 1.00 16.01 ? 983  ASN A O   1 
ATOM   7827 C  CB  . ASN A 1 983  ? 39.156 46.880  -20.945 1.00 14.20 ? 983  ASN A CB  1 
ATOM   7828 C  CG  . ASN A 1 983  ? 38.674 45.925  -21.984 1.00 12.78 ? 983  ASN A CG  1 
ATOM   7829 O  OD1 . ASN A 1 983  ? 39.411 45.019  -22.368 1.00 16.67 ? 983  ASN A OD1 1 
ATOM   7830 N  ND2 . ASN A 1 983  ? 37.465 46.151  -22.477 1.00 15.12 ? 983  ASN A ND2 1 
ATOM   7831 N  N   . LEU A 1 984  ? 39.940 48.679  -23.791 1.00 14.84 ? 984  LEU A N   1 
ATOM   7832 C  CA  . LEU A 1 984  ? 39.353 49.457  -24.897 1.00 15.16 ? 984  LEU A CA  1 
ATOM   7833 C  C   . LEU A 1 984  ? 38.527 48.546  -25.772 1.00 16.73 ? 984  LEU A C   1 
ATOM   7834 O  O   . LEU A 1 984  ? 38.852 47.386  -25.929 1.00 17.45 ? 984  LEU A O   1 
ATOM   7835 C  CB  . LEU A 1 984  ? 40.457 50.084  -25.737 1.00 15.76 ? 984  LEU A CB  1 
ATOM   7836 C  CG  . LEU A 1 984  ? 41.417 50.940  -24.900 1.00 16.71 ? 984  LEU A CG  1 
ATOM   7837 C  CD1 . LEU A 1 984  ? 42.589 51.389  -25.812 1.00 17.65 ? 984  LEU A CD1 1 
ATOM   7838 C  CD2 . LEU A 1 984  ? 40.699 52.089  -24.282 1.00 18.37 ? 984  LEU A CD2 1 
ATOM   7839 N  N   . MET A 1 985  ? 37.445 49.072  -26.326 1.00 17.27 ? 985  MET A N   1 
ATOM   7840 C  CA  . MET A 1 985  ? 36.610 48.237  -27.184 1.00 20.98 ? 985  MET A CA  1 
ATOM   7841 C  C   . MET A 1 985  ? 37.276 47.867  -28.484 1.00 20.41 ? 985  MET A C   1 
ATOM   7842 O  O   . MET A 1 985  ? 38.051 48.645  -29.065 1.00 21.46 ? 985  MET A O   1 
ATOM   7843 C  CB  . MET A 1 985  ? 35.310 48.945  -27.513 1.00 21.40 ? 985  MET A CB  1 
ATOM   7844 C  CG  . MET A 1 985  ? 34.400 49.039  -26.337 1.00 25.04 ? 985  MET A CG  1 
ATOM   7845 S  SD  . MET A 1 985  ? 32.734 49.221  -26.875 1.00 27.23 ? 985  MET A SD  1 
ATOM   7846 C  CE  . MET A 1 985  ? 32.832 50.807  -27.603 1.00 27.68 ? 985  MET A CE  1 
ATOM   7847 N  N   . GLN A 1 986  ? 36.982 46.651  -28.939 1.00 20.42 ? 986  GLN A N   1 
ATOM   7848 C  CA  . GLN A 1 986  ? 37.492 46.156  -30.226 1.00 22.36 ? 986  GLN A CA  1 
ATOM   7849 C  C   . GLN A 1 986  ? 36.461 46.663  -31.227 1.00 21.49 ? 986  GLN A C   1 
ATOM   7850 O  O   . GLN A 1 986  ? 35.286 46.306  -31.129 1.00 21.58 ? 986  GLN A O   1 
ATOM   7851 C  CB  . GLN A 1 986  ? 37.504 44.615  -30.242 1.00 26.39 ? 986  GLN A CB  1 
ATOM   7852 C  CG  . GLN A 1 986  ? 38.540 44.006  -29.321 1.00 30.84 ? 986  GLN A CG  1 
ATOM   7853 C  CD  . GLN A 1 986  ? 39.950 44.235  -29.819 1.00 36.25 ? 986  GLN A CD  1 
ATOM   7854 O  OE1 . GLN A 1 986  ? 40.886 44.359  -29.024 1.00 40.10 ? 986  GLN A OE1 1 
ATOM   7855 N  NE2 . GLN A 1 986  ? 40.120 44.284  -31.145 1.00 36.02 ? 986  GLN A NE2 1 
ATOM   7856 N  N   . CYS A 1 987  ? 36.893 47.507  -32.162 1.00 22.71 ? 987  CYS A N   1 
ATOM   7857 C  CA  . CYS A 1 987  ? 35.967 48.042  -33.163 1.00 24.63 ? 987  CYS A CA  1 
ATOM   7858 C  C   . CYS A 1 987  ? 36.484 47.853  -34.573 1.00 26.67 ? 987  CYS A C   1 
ATOM   7859 O  O   . CYS A 1 987  ? 36.023 48.551  -35.489 1.00 28.10 ? 987  CYS A O   1 
ATOM   7860 C  CB  . CYS A 1 987  ? 35.689 49.526  -32.951 1.00 24.52 ? 987  CYS A CB  1 
ATOM   7861 S  SG  . CYS A 1 987  ? 35.061 49.911  -31.286 1.00 28.81 ? 987  CYS A SG  1 
ATOM   7862 N  N   . GLY A 1 988  ? 37.439 46.937  -34.736 1.00 26.24 ? 988  GLY A N   1 
ATOM   7863 C  CA  . GLY A 1 988  ? 37.972 46.647  -36.058 1.00 33.92 ? 988  GLY A CA  1 
ATOM   7864 C  C   . GLY A 1 988  ? 39.132 47.486  -36.511 1.00 39.14 ? 988  GLY A C   1 
ATOM   7865 O  O   . GLY A 1 988  ? 39.556 47.374  -37.670 1.00 39.97 ? 988  GLY A O   1 
ATOM   7866 N  N   . THR A 1 989  ? 39.641 48.333  -35.619 1.00 43.40 ? 989  THR A N   1 
ATOM   7867 C  CA  . THR A 1 989  ? 40.784 49.194  -35.931 1.00 48.63 ? 989  THR A CA  1 
ATOM   7868 C  C   . THR A 1 989  ? 42.030 48.400  -35.561 1.00 52.03 ? 989  THR A C   1 
ATOM   7869 O  O   . THR A 1 989  ? 42.401 48.344  -34.392 1.00 52.31 ? 989  THR A O   1 
ATOM   7870 C  CB  . THR A 1 989  ? 40.773 50.471  -35.081 1.00 48.96 ? 989  THR A CB  1 
ATOM   7871 O  OG1 . THR A 1 989  ? 39.556 51.187  -35.302 1.00 49.57 ? 989  THR A OG1 1 
ATOM   7872 C  CG2 . THR A 1 989  ? 41.945 51.355  -35.447 1.00 50.70 ? 989  THR A CG2 1 
ATOM   7873 N  N   . PRO A 1 990  ? 42.695 47.773  -36.553 1.00 55.67 ? 990  PRO A N   1 
ATOM   7874 C  CA  . PRO A 1 990  ? 43.895 46.997  -36.218 1.00 57.84 ? 990  PRO A CA  1 
ATOM   7875 C  C   . PRO A 1 990  ? 44.775 47.659  -35.146 1.00 59.79 ? 990  PRO A C   1 
ATOM   7876 O  O   . PRO A 1 990  ? 44.700 47.296  -33.968 1.00 60.37 ? 990  PRO A O   1 
ATOM   7877 C  CB  . PRO A 1 990  ? 44.606 46.858  -37.566 1.00 57.76 ? 990  PRO A CB  1 
ATOM   7878 C  CG  . PRO A 1 990  ? 43.457 46.788  -38.544 1.00 57.60 ? 990  PRO A CG  1 
ATOM   7879 C  CD  . PRO A 1 990  ? 42.541 47.897  -38.019 1.00 56.61 ? 990  PRO A CD  1 
ATOM   7880 N  N   . GLU A 1 991  ? 45.578 48.644  -35.541 1.00 61.55 ? 991  GLU A N   1 
ATOM   7881 C  CA  . GLU A 1 991  ? 46.480 49.308  -34.595 1.00 63.90 ? 991  GLU A CA  1 
ATOM   7882 C  C   . GLU A 1 991  ? 47.333 48.216  -33.957 1.00 64.04 ? 991  GLU A C   1 
ATOM   7883 O  O   . GLU A 1 991  ? 46.912 47.603  -32.980 1.00 64.83 ? 991  GLU A O   1 
ATOM   7884 C  CB  . GLU A 1 991  ? 45.696 50.026  -33.488 1.00 64.54 ? 991  GLU A CB  1 
ATOM   7885 C  CG  . GLU A 1 991  ? 44.796 51.163  -33.956 1.00 66.41 ? 991  GLU A CG  1 
ATOM   7886 C  CD  . GLU A 1 991  ? 44.122 51.890  -32.795 1.00 67.27 ? 991  GLU A CD  1 
ATOM   7887 O  OE1 . GLU A 1 991  ? 43.378 51.234  -32.024 1.00 66.22 ? 991  GLU A OE1 1 
ATOM   7888 O  OE2 . GLU A 1 991  ? 44.344 53.118  -32.658 1.00 67.76 ? 991  GLU A OE2 1 
ATOM   7889 N  N   . GLU A 1 992  ? 48.516 47.956  -34.497 1.00 64.06 ? 992  GLU A N   1 
ATOM   7890 C  CA  . GLU A 1 992  ? 49.343 46.912  -33.912 1.00 64.59 ? 992  GLU A CA  1 
ATOM   7891 C  C   . GLU A 1 992  ? 50.793 47.288  -33.727 1.00 63.31 ? 992  GLU A C   1 
ATOM   7892 O  O   . GLU A 1 992  ? 51.107 48.415  -33.327 1.00 62.92 ? 992  GLU A O   1 
ATOM   7893 C  CB  . GLU A 1 992  ? 49.245 45.630  -34.742 1.00 67.39 ? 992  GLU A CB  1 
ATOM   7894 C  CG  . GLU A 1 992  ? 47.884 44.941  -34.641 1.00 70.28 ? 992  GLU A CG  1 
ATOM   7895 C  CD  . GLU A 1 992  ? 47.568 44.438  -33.227 1.00 72.01 ? 992  GLU A CD  1 
ATOM   7896 O  OE1 . GLU A 1 992  ? 48.470 44.447  -32.355 1.00 72.01 ? 992  GLU A OE1 1 
ATOM   7897 O  OE2 . GLU A 1 992  ? 46.409 44.023  -32.992 1.00 73.15 ? 992  GLU A OE2 1 
ATOM   7898 N  N   . HIS A 1 993  ? 51.662 46.323  -34.024 1.00 61.90 ? 993  HIS A N   1 
ATOM   7899 C  CA  . HIS A 1 993  ? 53.115 46.458  -33.900 1.00 60.78 ? 993  HIS A CA  1 
ATOM   7900 C  C   . HIS A 1 993  ? 53.604 47.345  -32.756 1.00 57.35 ? 993  HIS A C   1 
ATOM   7901 O  O   . HIS A 1 993  ? 54.071 48.477  -32.980 1.00 57.72 ? 993  HIS A O   1 
ATOM   7902 C  CB  . HIS A 1 993  ? 53.763 46.923  -35.235 1.00 64.30 ? 993  HIS A CB  1 
ATOM   7903 C  CG  . HIS A 1 993  ? 53.254 48.236  -35.761 1.00 67.42 ? 993  HIS A CG  1 
ATOM   7904 N  ND1 . HIS A 1 993  ? 51.970 48.406  -36.242 1.00 69.16 ? 993  HIS A ND1 1 
ATOM   7905 C  CD2 . HIS A 1 993  ? 53.875 49.431  -35.925 1.00 68.46 ? 993  HIS A CD2 1 
ATOM   7906 C  CE1 . HIS A 1 993  ? 51.824 49.644  -36.681 1.00 69.09 ? 993  HIS A CE1 1 
ATOM   7907 N  NE2 . HIS A 1 993  ? 52.965 50.287  -36.501 1.00 69.57 ? 993  HIS A NE2 1 
ATOM   7908 N  N   . THR A 1 994  ? 53.477 46.844  -31.526 1.00 51.58 ? 994  THR A N   1 
ATOM   7909 C  CA  . THR A 1 994  ? 53.973 47.601  -30.382 1.00 44.76 ? 994  THR A CA  1 
ATOM   7910 C  C   . THR A 1 994  ? 54.943 46.750  -29.583 1.00 41.75 ? 994  THR A C   1 
ATOM   7911 O  O   . THR A 1 994  ? 54.903 45.508  -29.604 1.00 41.73 ? 994  THR A O   1 
ATOM   7912 C  CB  . THR A 1 994  ? 52.843 48.106  -29.448 1.00 43.83 ? 994  THR A CB  1 
ATOM   7913 O  OG1 . THR A 1 994  ? 52.040 47.005  -29.011 1.00 41.54 ? 994  THR A OG1 1 
ATOM   7914 C  CG2 . THR A 1 994  ? 51.982 49.128  -30.167 1.00 41.40 ? 994  THR A CG2 1 
ATOM   7915 N  N   . GLN A 1 995  ? 55.817 47.427  -28.857 1.00 36.52 ? 995  GLN A N   1 
ATOM   7916 C  CA  . GLN A 1 995  ? 56.811 46.726  -28.079 1.00 31.80 ? 995  GLN A CA  1 
ATOM   7917 C  C   . GLN A 1 995  ? 56.366 46.394  -26.674 1.00 27.82 ? 995  GLN A C   1 
ATOM   7918 O  O   . GLN A 1 995  ? 55.618 47.128  -26.045 1.00 26.08 ? 995  GLN A O   1 
ATOM   7919 C  CB  . GLN A 1 995  ? 58.051 47.565  -27.963 1.00 31.70 ? 995  GLN A CB  1 
ATOM   7920 C  CG  . GLN A 1 995  ? 58.557 48.085  -29.262 1.00 35.17 ? 995  GLN A CG  1 
ATOM   7921 C  CD  . GLN A 1 995  ? 59.477 49.245  -29.029 1.00 38.76 ? 995  GLN A CD  1 
ATOM   7922 O  OE1 . GLN A 1 995  ? 59.042 50.399  -29.014 1.00 32.83 ? 995  GLN A OE1 1 
ATOM   7923 N  NE2 . GLN A 1 995  ? 60.765 48.944  -28.798 1.00 39.00 ? 995  GLN A NE2 1 
ATOM   7924 N  N   . LYS A 1 996  ? 56.859 45.269  -26.191 1.00 25.96 ? 996  LYS A N   1 
ATOM   7925 C  CA  . LYS A 1 996  ? 56.575 44.852  -24.841 1.00 27.11 ? 996  LYS A CA  1 
ATOM   7926 C  C   . LYS A 1 996  ? 57.306 45.824  -23.917 1.00 25.40 ? 996  LYS A C   1 
ATOM   7927 O  O   . LYS A 1 996  ? 58.471 46.195  -24.147 1.00 24.27 ? 996  LYS A O   1 
ATOM   7928 C  CB  . LYS A 1 996  ? 57.107 43.424  -24.630 1.00 31.55 ? 996  LYS A CB  1 
ATOM   7929 C  CG  . LYS A 1 996  ? 56.971 42.900  -23.222 1.00 37.62 ? 996  LYS A CG  1 
ATOM   7930 C  CD  . LYS A 1 996  ? 57.442 41.427  -23.167 1.00 42.38 ? 996  LYS A CD  1 
ATOM   7931 C  CE  . LYS A 1 996  ? 57.177 40.811  -21.797 1.00 45.13 ? 996  LYS A CE  1 
ATOM   7932 N  NZ  . LYS A 1 996  ? 57.743 39.428  -21.715 1.00 49.27 ? 996  LYS A NZ  1 
ATOM   7933 N  N   . LEU A 1 997  ? 56.612 46.242  -22.871 1.00 21.95 ? 997  LEU A N   1 
ATOM   7934 C  CA  . LEU A 1 997  ? 57.244 47.133  -21.916 1.00 21.62 ? 997  LEU A CA  1 
ATOM   7935 C  C   . LEU A 1 997  ? 57.595 46.325  -20.680 1.00 21.29 ? 997  LEU A C   1 
ATOM   7936 O  O   . LEU A 1 997  ? 56.711 45.749  -20.064 1.00 22.08 ? 997  LEU A O   1 
ATOM   7937 C  CB  . LEU A 1 997  ? 56.275 48.273  -21.547 1.00 22.43 ? 997  LEU A CB  1 
ATOM   7938 C  CG  . LEU A 1 997  ? 56.805 49.108  -20.379 1.00 22.75 ? 997  LEU A CG  1 
ATOM   7939 C  CD1 . LEU A 1 997  ? 58.040 49.916  -20.764 1.00 25.04 ? 997  LEU A CD1 1 
ATOM   7940 C  CD2 . LEU A 1 997  ? 55.713 50.034  -19.944 1.00 22.96 ? 997  LEU A CD2 1 
ATOM   7941 N  N   . ASP A 1 998  ? 58.888 46.267  -20.354 1.00 18.37 ? 998  ASP A N   1 
ATOM   7942 C  CA  . ASP A 1 998  ? 59.345 45.576  -19.137 1.00 20.94 ? 998  ASP A CA  1 
ATOM   7943 C  C   . ASP A 1 998  ? 59.936 46.676  -18.285 1.00 20.02 ? 998  ASP A C   1 
ATOM   7944 O  O   . ASP A 1 998  ? 61.078 47.123  -18.484 1.00 20.06 ? 998  ASP A O   1 
ATOM   7945 C  CB  . ASP A 1 998  ? 60.415 44.530  -19.472 1.00 21.31 ? 998  ASP A CB  1 
ATOM   7946 C  CG  . ASP A 1 998  ? 61.109 44.006  -18.238 1.00 26.31 ? 998  ASP A CG  1 
ATOM   7947 O  OD1 . ASP A 1 998  ? 60.577 44.170  -17.106 1.00 22.80 ? 998  ASP A OD1 1 
ATOM   7948 O  OD2 . ASP A 1 998  ? 62.192 43.406  -18.415 1.00 26.09 ? 998  ASP A OD2 1 
ATOM   7949 N  N   . VAL A 1 999  ? 59.160 47.141  -17.313 1.00 18.94 ? 999  VAL A N   1 
ATOM   7950 C  CA  . VAL A 1 999  ? 59.662 48.237  -16.515 1.00 18.02 ? 999  VAL A CA  1 
ATOM   7951 C  C   . VAL A 1 999  ? 60.913 47.940  -15.722 1.00 17.79 ? 999  VAL A C   1 
ATOM   7952 O  O   . VAL A 1 999  ? 61.677 48.845  -15.405 1.00 18.00 ? 999  VAL A O   1 
ATOM   7953 C  CB  . VAL A 1 999  ? 58.565 48.801  -15.571 1.00 17.46 ? 999  VAL A CB  1 
ATOM   7954 C  CG1 . VAL A 1 999  ? 57.448 49.376  -16.420 1.00 18.35 ? 999  VAL A CG1 1 
ATOM   7955 C  CG2 . VAL A 1 999  ? 58.023 47.710  -14.634 1.00 19.56 ? 999  VAL A CG2 1 
ATOM   7956 N  N   . CYS A 1 1000 ? 61.149 46.663  -15.457 1.00 18.61 ? 1000 CYS A N   1 
ATOM   7957 C  CA  . CYS A 1 1000 ? 62.312 46.315  -14.643 1.00 20.26 ? 1000 CYS A CA  1 
ATOM   7958 C  C   . CYS A 1 1000 ? 63.646 46.521  -15.367 1.00 20.91 ? 1000 CYS A C   1 
ATOM   7959 O  O   . CYS A 1 1000 ? 64.684 46.638  -14.721 1.00 22.98 ? 1000 CYS A O   1 
ATOM   7960 C  CB  . CYS A 1 1000 ? 62.168 44.899  -14.077 1.00 23.90 ? 1000 CYS A CB  1 
ATOM   7961 S  SG  . CYS A 1 1000 ? 61.250 44.905  -12.468 1.00 30.23 ? 1000 CYS A SG  1 
ATOM   7962 N  N   . HIS A 1 1001 ? 63.600 46.632  -16.698 1.00 21.81 ? 1001 HIS A N   1 
ATOM   7963 C  CA  . HIS A 1 1001 ? 64.820 46.902  -17.456 1.00 22.33 ? 1001 HIS A CA  1 
ATOM   7964 C  C   . HIS A 1 1001 ? 64.899 48.349  -17.978 1.00 21.42 ? 1001 HIS A C   1 
ATOM   7965 O  O   . HIS A 1 1001 ? 65.745 48.682  -18.806 1.00 23.09 ? 1001 HIS A O   1 
ATOM   7966 C  CB  . HIS A 1 1001 ? 65.000 45.911  -18.605 1.00 22.82 ? 1001 HIS A CB  1 
ATOM   7967 C  CG  . HIS A 1 1001 ? 65.554 44.597  -18.168 1.00 23.88 ? 1001 HIS A CG  1 
ATOM   7968 N  ND1 . HIS A 1 1001 ? 64.762 43.584  -17.685 1.00 24.19 ? 1001 HIS A ND1 1 
ATOM   7969 C  CD2 . HIS A 1 1001 ? 66.827 44.134  -18.120 1.00 25.35 ? 1001 HIS A CD2 1 
ATOM   7970 C  CE1 . HIS A 1 1001 ? 65.515 42.544  -17.365 1.00 24.70 ? 1001 HIS A CE1 1 
ATOM   7971 N  NE2 . HIS A 1 1001 ? 66.771 42.851  -17.623 1.00 24.70 ? 1001 HIS A NE2 1 
ATOM   7972 N  N   . LEU A 1 1002 ? 64.027 49.232  -17.494 1.00 21.45 ? 1002 LEU A N   1 
ATOM   7973 C  CA  . LEU A 1 1002 ? 64.090 50.631  -17.929 1.00 19.24 ? 1002 LEU A CA  1 
ATOM   7974 C  C   . LEU A 1 1002 ? 65.360 51.303  -17.400 1.00 20.83 ? 1002 LEU A C   1 
ATOM   7975 O  O   . LEU A 1 1002 ? 65.888 52.212  -18.052 1.00 22.54 ? 1002 LEU A O   1 
ATOM   7976 C  CB  . LEU A 1 1002 ? 62.865 51.429  -17.435 1.00 19.10 ? 1002 LEU A CB  1 
ATOM   7977 C  CG  . LEU A 1 1002 ? 61.620 51.235  -18.275 1.00 17.66 ? 1002 LEU A CG  1 
ATOM   7978 C  CD1 . LEU A 1 1002 ? 60.427 51.923  -17.626 1.00 17.74 ? 1002 LEU A CD1 1 
ATOM   7979 C  CD2 . LEU A 1 1002 ? 61.872 51.823  -19.648 1.00 21.72 ? 1002 LEU A CD2 1 
ATOM   7980 N  N   . LEU A 1 1003 ? 65.852 50.895  -16.224 1.00 20.53 ? 1003 LEU A N   1 
ATOM   7981 C  CA  . LEU A 1 1003 ? 67.087 51.454  -15.696 1.00 21.58 ? 1003 LEU A CA  1 
ATOM   7982 C  C   . LEU A 1 1003 ? 68.141 50.343  -15.816 1.00 21.43 ? 1003 LEU A C   1 
ATOM   7983 O  O   . LEU A 1 1003 ? 67.829 49.157  -15.685 1.00 22.88 ? 1003 LEU A O   1 
ATOM   7984 C  CB  . LEU A 1 1003 ? 66.935 51.892  -14.243 1.00 21.33 ? 1003 LEU A CB  1 
ATOM   7985 C  CG  . LEU A 1 1003 ? 66.183 53.229  -14.135 1.00 27.23 ? 1003 LEU A CG  1 
ATOM   7986 C  CD1 . LEU A 1 1003 ? 65.526 53.330  -12.783 1.00 29.49 ? 1003 LEU A CD1 1 
ATOM   7987 C  CD2 . LEU A 1 1003 ? 67.155 54.394  -14.385 1.00 28.47 ? 1003 LEU A CD2 1 
ATOM   7988 N  N   . PRO A 1 1004 ? 69.390 50.726  -16.070 1.00 23.02 ? 1004 PRO A N   1 
ATOM   7989 C  CA  . PRO A 1 1004 ? 70.423 49.706  -16.211 1.00 21.70 ? 1004 PRO A CA  1 
ATOM   7990 C  C   . PRO A 1 1004 ? 70.844 48.996  -14.933 1.00 23.48 ? 1004 PRO A C   1 
ATOM   7991 O  O   . PRO A 1 1004 ? 70.488 49.388  -13.810 1.00 22.09 ? 1004 PRO A O   1 
ATOM   7992 C  CB  . PRO A 1 1004 ? 71.561 50.491  -16.838 1.00 23.27 ? 1004 PRO A CB  1 
ATOM   7993 C  CG  . PRO A 1 1004 ? 71.493 51.773  -16.117 1.00 25.11 ? 1004 PRO A CG  1 
ATOM   7994 C  CD  . PRO A 1 1004 ? 69.985 52.079  -16.109 1.00 23.58 ? 1004 PRO A CD  1 
ATOM   7995 N  N   . ASN A 1 1005 ? 71.616 47.932  -15.132 1.00 23.97 ? 1005 ASN A N   1 
ATOM   7996 C  CA  . ASN A 1 1005 ? 72.151 47.150  -14.029 1.00 22.86 ? 1005 ASN A CA  1 
ATOM   7997 C  C   . ASN A 1 1005 ? 71.087 46.591  -13.096 1.00 22.42 ? 1005 ASN A C   1 
ATOM   7998 O  O   . ASN A 1 1005 ? 71.269 46.623  -11.895 1.00 22.78 ? 1005 ASN A O   1 
ATOM   7999 C  CB  . ASN A 1 1005 ? 73.104 48.002  -13.214 1.00 26.18 ? 1005 ASN A CB  1 
ATOM   8000 C  CG  . ASN A 1 1005 ? 74.275 48.499  -14.019 1.00 30.08 ? 1005 ASN A CG  1 
ATOM   8001 O  OD1 . ASN A 1 1005 ? 74.962 49.402  -13.588 1.00 38.17 ? 1005 ASN A OD1 1 
ATOM   8002 N  ND2 . ASN A 1 1005 ? 74.522 47.905  -15.167 1.00 31.56 ? 1005 ASN A ND2 1 
ATOM   8003 N  N   . VAL A 1 1006 ? 69.991 46.085  -13.645 1.00 22.37 ? 1006 VAL A N   1 
ATOM   8004 C  CA  . VAL A 1 1006 ? 68.962 45.502  -12.798 1.00 23.22 ? 1006 VAL A CA  1 
ATOM   8005 C  C   . VAL A 1 1006 ? 69.538 44.223  -12.178 1.00 23.96 ? 1006 VAL A C   1 
ATOM   8006 O  O   . VAL A 1 1006 ? 70.212 43.434  -12.847 1.00 25.65 ? 1006 VAL A O   1 
ATOM   8007 C  CB  . VAL A 1 1006 ? 67.629 45.204  -13.587 1.00 21.84 ? 1006 VAL A CB  1 
ATOM   8008 C  CG1 . VAL A 1 1006 ? 67.812 44.188  -14.671 1.00 23.06 ? 1006 VAL A CG1 1 
ATOM   8009 C  CG2 . VAL A 1 1006 ? 66.566 44.711  -12.611 1.00 23.79 ? 1006 VAL A CG2 1 
ATOM   8010 N  N   . ALA A 1 1007 ? 69.287 44.053  -10.892 1.00 21.91 ? 1007 ALA A N   1 
ATOM   8011 C  CA  . ALA A 1 1007 ? 69.771 42.890  -10.147 1.00 23.47 ? 1007 ALA A CA  1 
ATOM   8012 C  C   . ALA A 1 1007 ? 68.595 42.082  -9.629  1.00 25.16 ? 1007 ALA A C   1 
ATOM   8013 O  O   . ALA A 1 1007 ? 68.738 40.899  -9.294  1.00 26.60 ? 1007 ALA A O   1 
ATOM   8014 C  CB  . ALA A 1 1007 ? 70.627 43.352  -8.983  1.00 22.61 ? 1007 ALA A CB  1 
ATOM   8015 N  N   . ARG A 1 1008 ? 67.415 42.699  -9.540  1.00 24.17 ? 1008 ARG A N   1 
ATOM   8016 C  CA  . ARG A 1 1008 ? 66.253 41.971  -9.035  1.00 22.31 ? 1008 ARG A CA  1 
ATOM   8017 C  C   . ARG A 1 1008 ? 64.976 42.688  -9.461  1.00 20.14 ? 1008 ARG A C   1 
ATOM   8018 O  O   . ARG A 1 1008 ? 64.992 43.909  -9.586  1.00 20.61 ? 1008 ARG A O   1 
ATOM   8019 C  CB  . ARG A 1 1008 ? 66.293 41.945  -7.517  1.00 23.10 ? 1008 ARG A CB  1 
ATOM   8020 C  CG  . ARG A 1 1008 ? 65.239 41.083  -6.862  1.00 28.26 ? 1008 ARG A CG  1 
ATOM   8021 C  CD  . ARG A 1 1008 ? 65.350 41.227  -5.337  1.00 33.48 ? 1008 ARG A CD  1 
ATOM   8022 N  NE  . ARG A 1 1008 ? 64.590 40.212  -4.607  1.00 39.07 ? 1008 ARG A NE  1 
ATOM   8023 C  CZ  . ARG A 1 1008 ? 64.878 38.909  -4.590  1.00 41.85 ? 1008 ARG A CZ  1 
ATOM   8024 N  NH1 . ARG A 1 1008 ? 65.930 38.437  -5.265  1.00 43.39 ? 1008 ARG A NH1 1 
ATOM   8025 N  NH2 . ARG A 1 1008 ? 64.103 38.069  -3.904  1.00 42.09 ? 1008 ARG A NH2 1 
ATOM   8026 N  N   . CYS A 1 1009 ? 63.902 41.934  -9.683  1.00 19.14 ? 1009 CYS A N   1 
ATOM   8027 C  CA  . CYS A 1 1009 ? 62.617 42.517  -10.068 1.00 21.04 ? 1009 CYS A CA  1 
ATOM   8028 C  C   . CYS A 1 1009 ? 61.549 41.768  -9.269  1.00 20.17 ? 1009 CYS A C   1 
ATOM   8029 O  O   . CYS A 1 1009 ? 61.446 40.538  -9.360  1.00 21.24 ? 1009 CYS A O   1 
ATOM   8030 C  CB  . CYS A 1 1009 ? 62.388 42.308  -11.547 1.00 23.46 ? 1009 CYS A CB  1 
ATOM   8031 S  SG  . CYS A 1 1009 ? 60.809 42.965  -12.197 1.00 30.60 ? 1009 CYS A SG  1 
ATOM   8032 N  N   . GLU A 1 1010 ? 60.739 42.515  -8.515  1.00 18.51 ? 1010 GLU A N   1 
ATOM   8033 C  CA  . GLU A 1 1010 ? 59.702 41.935  -7.711  1.00 18.74 ? 1010 GLU A CA  1 
ATOM   8034 C  C   . GLU A 1 1010 ? 58.333 42.557  -7.994  1.00 17.52 ? 1010 GLU A C   1 
ATOM   8035 O  O   . GLU A 1 1010 ? 58.213 43.746  -8.256  1.00 18.50 ? 1010 GLU A O   1 
ATOM   8036 C  CB  . GLU A 1 1010 ? 60.044 42.179  -6.236  1.00 21.76 ? 1010 GLU A CB  1 
ATOM   8037 C  CG  . GLU A 1 1010 ? 61.293 41.395  -5.794  1.00 28.43 ? 1010 GLU A CG  1 
ATOM   8038 C  CD  . GLU A 1 1010 ? 62.029 41.997  -4.600  1.00 32.38 ? 1010 GLU A CD  1 
ATOM   8039 O  OE1 . GLU A 1 1010 ? 62.463 43.174  -4.650  1.00 32.24 ? 1010 GLU A OE1 1 
ATOM   8040 O  OE2 . GLU A 1 1010 ? 62.187 41.261  -3.598  1.00 36.50 ? 1010 GLU A OE2 1 
ATOM   8041 N  N   . ARG A 1 1011 ? 57.304 41.743  -7.912  1.00 17.50 ? 1011 ARG A N   1 
ATOM   8042 C  CA  . ARG A 1 1011 ? 55.941 42.272  -7.999  1.00 15.04 ? 1011 ARG A CA  1 
ATOM   8043 C  C   . ARG A 1 1011 ? 55.615 42.618  -6.531  1.00 16.64 ? 1011 ARG A C   1 
ATOM   8044 O  O   . ARG A 1 1011 ? 55.941 41.845  -5.612  1.00 16.60 ? 1011 ARG A O   1 
ATOM   8045 C  CB  . ARG A 1 1011 ? 54.967 41.226  -8.506  1.00 17.00 ? 1011 ARG A CB  1 
ATOM   8046 C  CG  . ARG A 1 1011 ? 53.605 41.890  -8.770  1.00 20.05 ? 1011 ARG A CG  1 
ATOM   8047 C  CD  . ARG A 1 1011 ? 52.646 40.999  -9.509  1.00 24.59 ? 1011 ARG A CD  1 
ATOM   8048 N  NE  . ARG A 1 1011 ? 52.372 39.793  -8.744  1.00 32.05 ? 1011 ARG A NE  1 
ATOM   8049 C  CZ  . ARG A 1 1011 ? 51.470 39.718  -7.764  1.00 34.43 ? 1011 ARG A CZ  1 
ATOM   8050 N  NH1 . ARG A 1 1011 ? 50.748 40.791  -7.434  1.00 37.27 ? 1011 ARG A NH1 1 
ATOM   8051 N  NH2 . ARG A 1 1011 ? 51.286 38.567  -7.112  1.00 36.00 ? 1011 ARG A NH2 1 
ATOM   8052 N  N   . THR A 1 1012 ? 55.011 43.780  -6.300  1.00 16.01 ? 1012 THR A N   1 
ATOM   8053 C  CA  . THR A 1 1012 ? 54.674 44.216  -4.960  1.00 14.90 ? 1012 THR A CA  1 
ATOM   8054 C  C   . THR A 1 1012 ? 53.229 44.683  -4.858  1.00 13.52 ? 1012 THR A C   1 
ATOM   8055 O  O   . THR A 1 1012 ? 52.515 44.810  -5.866  1.00 14.52 ? 1012 THR A O   1 
ATOM   8056 C  CB  . THR A 1 1012 ? 55.557 45.438  -4.526  1.00 15.90 ? 1012 THR A CB  1 
ATOM   8057 O  OG1 . THR A 1 1012 ? 55.216 46.580  -5.342  1.00 14.97 ? 1012 THR A OG1 1 
ATOM   8058 C  CG2 . THR A 1 1012 ? 57.063 45.156  -4.736  1.00 17.11 ? 1012 THR A CG2 1 
ATOM   8059 N  N   . THR A 1 1013 ? 52.788 44.900  -3.620  1.00 13.29 ? 1013 THR A N   1 
ATOM   8060 C  CA  . THR A 1 1013 ? 51.492 45.525  -3.430  1.00 14.30 ? 1013 THR A CA  1 
ATOM   8061 C  C   . THR A 1 1013 ? 51.603 46.931  -4.061  1.00 13.53 ? 1013 THR A C   1 
ATOM   8062 O  O   . THR A 1 1013 ? 52.694 47.464  -4.285  1.00 12.74 ? 1013 THR A O   1 
ATOM   8063 C  CB  . THR A 1 1013 ? 51.186 45.666  -1.973  1.00 13.89 ? 1013 THR A CB  1 
ATOM   8064 O  OG1 . THR A 1 1013 ? 52.370 46.094  -1.276  1.00 14.51 ? 1013 THR A OG1 1 
ATOM   8065 C  CG2 . THR A 1 1013 ? 50.675 44.310  -1.426  1.00 16.27 ? 1013 THR A CG2 1 
ATOM   8066 N  N   . LEU A 1 1014 ? 50.448 47.552  -4.314  1.00 12.70 ? 1014 LEU A N   1 
ATOM   8067 C  CA  . LEU A 1 1014 ? 50.463 48.853  -5.016  1.00 12.30 ? 1014 LEU A CA  1 
ATOM   8068 C  C   . LEU A 1 1014 ? 51.140 50.005  -4.311  1.00 12.30 ? 1014 LEU A C   1 
ATOM   8069 O  O   . LEU A 1 1014 ? 51.506 51.005  -4.930  1.00 12.59 ? 1014 LEU A O   1 
ATOM   8070 C  CB  . LEU A 1 1014 ? 49.037 49.290  -5.415  1.00 11.94 ? 1014 LEU A CB  1 
ATOM   8071 C  CG  . LEU A 1 1014 ? 48.253 48.342  -6.318  1.00 11.60 ? 1014 LEU A CG  1 
ATOM   8072 C  CD1 . LEU A 1 1014 ? 46.957 49.063  -6.724  1.00 12.66 ? 1014 LEU A CD1 1 
ATOM   8073 C  CD2 . LEU A 1 1014 ? 49.034 47.997  -7.603  1.00 13.25 ? 1014 LEU A CD2 1 
ATOM   8074 N  N   . THR A 1 1015 ? 51.311 49.860  -2.993  1.00 11.01 ? 1015 THR A N   1 
ATOM   8075 C  CA  . THR A 1 1015 ? 51.971 50.831  -2.146  1.00 11.58 ? 1015 THR A CA  1 
ATOM   8076 C  C   . THR A 1 1015 ? 53.475 50.558  -2.071  1.00 12.01 ? 1015 THR A C   1 
ATOM   8077 O  O   . THR A 1 1015 ? 54.169 51.326  -1.418  1.00 12.48 ? 1015 THR A O   1 
ATOM   8078 C  CB  . THR A 1 1015 ? 51.440 50.707  -0.731  1.00 12.29 ? 1015 THR A CB  1 
ATOM   8079 O  OG1 . THR A 1 1015 ? 51.623 49.330  -0.334  1.00 13.09 ? 1015 THR A OG1 1 
ATOM   8080 C  CG2 . THR A 1 1015 ? 49.941 51.078  -0.640  1.00 13.21 ? 1015 THR A CG2 1 
ATOM   8081 N  N   . PHE A 1 1016 ? 53.941 49.497  -2.754  1.00 12.95 ? 1016 PHE A N   1 
ATOM   8082 C  CA  . PHE A 1 1016 ? 55.347 49.028  -2.790  1.00 13.04 ? 1016 PHE A CA  1 
ATOM   8083 C  C   . PHE A 1 1016 ? 55.836 48.494  -1.446  1.00 14.63 ? 1016 PHE A C   1 
ATOM   8084 O  O   . PHE A 1 1016 ? 57.007 48.144  -1.324  1.00 16.64 ? 1016 PHE A O   1 
ATOM   8085 C  CB  . PHE A 1 1016 ? 56.307 50.162  -3.229  1.00 14.29 ? 1016 PHE A CB  1 
ATOM   8086 C  CG  . PHE A 1 1016 ? 55.954 50.784  -4.546  1.00 13.63 ? 1016 PHE A CG  1 
ATOM   8087 C  CD1 . PHE A 1 1016 ? 55.853 50.023  -5.709  1.00 12.64 ? 1016 PHE A CD1 1 
ATOM   8088 C  CD2 . PHE A 1 1016 ? 55.767 52.181  -4.615  1.00 14.33 ? 1016 PHE A CD2 1 
ATOM   8089 C  CE1 . PHE A 1 1016 ? 55.566 50.652  -6.941  1.00 15.68 ? 1016 PHE A CE1 1 
ATOM   8090 C  CE2 . PHE A 1 1016 ? 55.491 52.788  -5.834  1.00 12.85 ? 1016 PHE A CE2 1 
ATOM   8091 C  CZ  . PHE A 1 1016 ? 55.393 52.011  -6.989  1.00 15.10 ? 1016 PHE A CZ  1 
ATOM   8092 N  N   . LEU A 1 1017 ? 54.926 48.321  -0.478  1.00 13.68 ? 1017 LEU A N   1 
ATOM   8093 C  CA  . LEU A 1 1017 ? 55.361 47.906  0.867   1.00 14.72 ? 1017 LEU A CA  1 
ATOM   8094 C  C   . LEU A 1 1017 ? 55.555 46.408  1.125   1.00 15.58 ? 1017 LEU A C   1 
ATOM   8095 O  O   . LEU A 1 1017 ? 56.211 46.041  2.110   1.00 20.11 ? 1017 LEU A O   1 
ATOM   8096 C  CB  . LEU A 1 1017 ? 54.405 48.508  1.900   1.00 14.59 ? 1017 LEU A CB  1 
ATOM   8097 C  CG  . LEU A 1 1017 ? 54.375 50.037  1.847   1.00 14.94 ? 1017 LEU A CG  1 
ATOM   8098 C  CD1 . LEU A 1 1017 ? 53.307 50.491  2.870   1.00 16.29 ? 1017 LEU A CD1 1 
ATOM   8099 C  CD2 . LEU A 1 1017 ? 55.713 50.643  2.192   1.00 15.76 ? 1017 LEU A CD2 1 
ATOM   8100 N  N   . GLN A 1 1018 ? 55.024 45.556  0.267   1.00 14.39 ? 1018 GLN A N   1 
ATOM   8101 C  CA  . GLN A 1 1018 ? 55.206 44.118  0.447   1.00 17.04 ? 1018 GLN A CA  1 
ATOM   8102 C  C   . GLN A 1 1018 ? 55.558 43.443  -0.870  1.00 16.75 ? 1018 GLN A C   1 
ATOM   8103 O  O   . GLN A 1 1018 ? 54.914 43.682  -1.887  1.00 18.04 ? 1018 GLN A O   1 
ATOM   8104 C  CB  . GLN A 1 1018 ? 53.945 43.458  1.032   1.00 18.85 ? 1018 GLN A CB  1 
ATOM   8105 C  CG  . GLN A 1 1018 ? 54.143 41.944  1.205   1.00 23.09 ? 1018 GLN A CG  1 
ATOM   8106 C  CD  . GLN A 1 1018 ? 52.877 41.169  1.592   1.00 28.34 ? 1018 GLN A CD  1 
ATOM   8107 O  OE1 . GLN A 1 1018 ? 52.949 39.950  1.856   1.00 32.84 ? 1018 GLN A OE1 1 
ATOM   8108 N  NE2 . GLN A 1 1018 ? 51.730 41.838  1.610   1.00 25.80 ? 1018 GLN A NE2 1 
ATOM   8109 N  N   . ASN A 1 1019 ? 56.579 42.583  -0.838  1.00 16.25 ? 1019 ASN A N   1 
ATOM   8110 C  CA  . ASN A 1 1019 ? 57.004 41.842  -2.017  1.00 19.14 ? 1019 ASN A CA  1 
ATOM   8111 C  C   . ASN A 1 1019 ? 56.118 40.637  -2.144  1.00 21.13 ? 1019 ASN A C   1 
ATOM   8112 O  O   . ASN A 1 1019 ? 55.984 39.845  -1.187  1.00 23.28 ? 1019 ASN A O   1 
ATOM   8113 C  CB  . ASN A 1 1019 ? 58.473 41.402  -1.909  1.00 20.08 ? 1019 ASN A CB  1 
ATOM   8114 C  CG  . ASN A 1 1019 ? 59.422 42.591  -1.773  1.00 25.39 ? 1019 ASN A CG  1 
ATOM   8115 O  OD1 . ASN A 1 1019 ? 59.216 43.624  -2.401  1.00 25.73 ? 1019 ASN A OD1 1 
ATOM   8116 N  ND2 . ASN A 1 1019 ? 60.477 42.449  -0.948  1.00 25.84 ? 1019 ASN A ND2 1 
ATOM   8117 N  N   . LEU A 1 1020 ? 55.492 40.487  -3.298  1.00 19.94 ? 1020 LEU A N   1 
ATOM   8118 C  CA  . LEU A 1 1020 ? 54.580 39.394  -3.549  1.00 21.06 ? 1020 LEU A CA  1 
ATOM   8119 C  C   . LEU A 1 1020 ? 55.148 38.298  -4.446  1.00 22.92 ? 1020 LEU A C   1 
ATOM   8120 O  O   . LEU A 1 1020 ? 54.701 37.140  -4.375  1.00 25.65 ? 1020 LEU A O   1 
ATOM   8121 C  CB  . LEU A 1 1020 ? 53.308 39.911  -4.209  1.00 20.82 ? 1020 LEU A CB  1 
ATOM   8122 C  CG  . LEU A 1 1020 ? 52.527 41.002  -3.479  1.00 21.31 ? 1020 LEU A CG  1 
ATOM   8123 C  CD1 . LEU A 1 1020 ? 51.376 41.427  -4.398  1.00 23.46 ? 1020 LEU A CD1 1 
ATOM   8124 C  CD2 . LEU A 1 1020 ? 52.003 40.503  -2.121  1.00 23.85 ? 1020 LEU A CD2 1 
ATOM   8125 N  N   . GLU A 1 1021 ? 56.100 38.647  -5.302  1.00 23.88 ? 1021 GLU A N   1 
ATOM   8126 C  CA  . GLU A 1 1021 ? 56.661 37.662  -6.236  1.00 26.67 ? 1021 GLU A CA  1 
ATOM   8127 C  C   . GLU A 1 1021 ? 58.038 38.060  -6.737  1.00 26.32 ? 1021 GLU A C   1 
ATOM   8128 O  O   . GLU A 1 1021 ? 58.271 39.203  -7.118  1.00 24.51 ? 1021 GLU A O   1 
ATOM   8129 C  CB  . GLU A 1 1021 ? 55.697 37.523  -7.415  1.00 28.85 ? 1021 GLU A CB  1 
ATOM   8130 C  CG  . GLU A 1 1021 ? 56.054 36.516  -8.471  1.00 37.66 ? 1021 GLU A CG  1 
ATOM   8131 C  CD  . GLU A 1 1021 ? 55.057 36.552  -9.616  1.00 39.87 ? 1021 GLU A CD  1 
ATOM   8132 O  OE1 . GLU A 1 1021 ? 54.065 37.330  -9.531  1.00 42.00 ? 1021 GLU A OE1 1 
ATOM   8133 O  OE2 . GLU A 1 1021 ? 55.279 35.811  -10.605 1.00 44.91 ? 1021 GLU A OE2 1 
ATOM   8134 N  N   . HIS A 1 1022 ? 58.968 37.104  -6.735  1.00 26.60 ? 1022 HIS A N   1 
ATOM   8135 C  CA  . HIS A 1 1022 ? 60.319 37.348  -7.204  1.00 27.63 ? 1022 HIS A CA  1 
ATOM   8136 C  C   . HIS A 1 1022 ? 60.241 36.958  -8.667  1.00 29.20 ? 1022 HIS A C   1 
ATOM   8137 O  O   . HIS A 1 1022 ? 59.898 35.828  -9.005  1.00 29.55 ? 1022 HIS A O   1 
ATOM   8138 C  CB  . HIS A 1 1022 ? 61.295 36.462  -6.428  1.00 30.12 ? 1022 HIS A CB  1 
ATOM   8139 C  CG  . HIS A 1 1022 ? 62.724 36.725  -6.755  1.00 35.02 ? 1022 HIS A CG  1 
ATOM   8140 N  ND1 . HIS A 1 1022 ? 63.696 35.750  -6.664  1.00 38.30 ? 1022 HIS A ND1 1 
ATOM   8141 C  CD2 . HIS A 1 1022 ? 63.347 37.843  -7.203  1.00 37.17 ? 1022 HIS A CD2 1 
ATOM   8142 C  CE1 . HIS A 1 1022 ? 64.856 36.254  -7.048  1.00 38.76 ? 1022 HIS A CE1 1 
ATOM   8143 N  NE2 . HIS A 1 1022 ? 64.673 37.522  -7.380  1.00 39.73 ? 1022 HIS A NE2 1 
ATOM   8144 N  N   . LEU A 1 1023 ? 60.552 37.886  -9.557  1.00 27.45 ? 1023 LEU A N   1 
ATOM   8145 C  CA  . LEU A 1 1023 ? 60.360 37.595  -10.959 1.00 28.72 ? 1023 LEU A CA  1 
ATOM   8146 C  C   . LEU A 1 1023 ? 61.534 37.032  -11.726 1.00 29.17 ? 1023 LEU A C   1 
ATOM   8147 O  O   . LEU A 1 1023 ? 62.636 37.580  -11.706 1.00 28.68 ? 1023 LEU A O   1 
ATOM   8148 C  CB  . LEU A 1 1023 ? 59.835 38.853  -11.654 1.00 27.86 ? 1023 LEU A CB  1 
ATOM   8149 C  CG  . LEU A 1 1023 ? 58.493 39.332  -11.086 1.00 28.09 ? 1023 LEU A CG  1 
ATOM   8150 C  CD1 . LEU A 1 1023 ? 58.361 40.816  -11.251 1.00 30.94 ? 1023 LEU A CD1 1 
ATOM   8151 C  CD2 . LEU A 1 1023 ? 57.352 38.572  -11.761 1.00 31.10 ? 1023 LEU A CD2 1 
ATOM   8152 N  N   . ASP A 1 1024 ? 61.264 35.936  -12.423 1.00 33.51 ? 1024 ASP A N   1 
ATOM   8153 C  CA  . ASP A 1 1024 ? 62.283 35.274  -13.229 1.00 36.00 ? 1024 ASP A CA  1 
ATOM   8154 C  C   . ASP A 1 1024 ? 62.829 36.136  -14.341 1.00 35.15 ? 1024 ASP A C   1 
ATOM   8155 O  O   . ASP A 1 1024 ? 62.083 36.827  -15.067 1.00 36.14 ? 1024 ASP A O   1 
ATOM   8156 C  CB  . ASP A 1 1024 ? 61.727 34.004  -13.847 1.00 40.99 ? 1024 ASP A CB  1 
ATOM   8157 C  CG  . ASP A 1 1024 ? 61.290 33.020  -12.812 1.00 45.99 ? 1024 ASP A CG  1 
ATOM   8158 O  OD1 . ASP A 1 1024 ? 62.009 32.915  -11.780 1.00 49.59 ? 1024 ASP A OD1 1 
ATOM   8159 O  OD2 . ASP A 1 1024 ? 60.242 32.355  -13.034 1.00 48.50 ? 1024 ASP A OD2 1 
ATOM   8160 N  N   . GLY A 1 1025 ? 64.141 36.077  -14.475 1.00 32.53 ? 1025 GLY A N   1 
ATOM   8161 C  CA  . GLY A 1 1025 ? 64.803 36.821  -15.516 1.00 31.65 ? 1025 GLY A CA  1 
ATOM   8162 C  C   . GLY A 1 1025 ? 64.714 38.303  -15.280 1.00 29.77 ? 1025 GLY A C   1 
ATOM   8163 O  O   . GLY A 1 1025 ? 65.087 39.081  -16.148 1.00 30.57 ? 1025 GLY A O   1 
ATOM   8164 N  N   . MET A 1 1026 ? 64.209 38.689  -14.111 1.00 28.27 ? 1026 MET A N   1 
ATOM   8165 C  CA  . MET A 1 1026 ? 64.092 40.103  -13.775 1.00 28.38 ? 1026 MET A CA  1 
ATOM   8166 C  C   . MET A 1 1026 ? 63.200 40.815  -14.778 1.00 26.05 ? 1026 MET A C   1 
ATOM   8167 O  O   . MET A 1 1026 ? 63.422 41.976  -15.106 1.00 25.46 ? 1026 MET A O   1 
ATOM   8168 C  CB  . MET A 1 1026 ? 65.475 40.761  -13.731 1.00 27.71 ? 1026 MET A CB  1 
ATOM   8169 C  CG  . MET A 1 1026 ? 66.445 40.061  -12.758 1.00 31.64 ? 1026 MET A CG  1 
ATOM   8170 S  SD  . MET A 1 1026 ? 68.051 40.863  -12.673 1.00 33.87 ? 1026 MET A SD  1 
ATOM   8171 C  CE  . MET A 1 1026 ? 68.714 40.490  -14.323 1.00 34.82 ? 1026 MET A CE  1 
ATOM   8172 N  N   . VAL A 1 1027 ? 62.189 40.116  -15.269 1.00 24.86 ? 1027 VAL A N   1 
ATOM   8173 C  CA  . VAL A 1 1027 ? 61.286 40.702  -16.239 1.00 25.64 ? 1027 VAL A CA  1 
ATOM   8174 C  C   . VAL A 1 1027 ? 59.919 40.930  -15.592 1.00 28.06 ? 1027 VAL A C   1 
ATOM   8175 O  O   . VAL A 1 1027 ? 59.342 40.029  -14.974 1.00 27.68 ? 1027 VAL A O   1 
ATOM   8176 C  CB  . VAL A 1 1027 ? 61.123 39.796  -17.470 1.00 25.85 ? 1027 VAL A CB  1 
ATOM   8177 C  CG1 . VAL A 1 1027 ? 60.043 40.351  -18.397 1.00 27.36 ? 1027 VAL A CG1 1 
ATOM   8178 C  CG2 . VAL A 1 1027 ? 62.443 39.721  -18.242 1.00 28.25 ? 1027 VAL A CG2 1 
ATOM   8179 N  N   . ALA A 1 1028 ? 59.405 42.145  -15.721 1.00 28.79 ? 1028 ALA A N   1 
ATOM   8180 C  CA  . ALA A 1 1028 ? 58.091 42.471  -15.159 1.00 29.72 ? 1028 ALA A CA  1 
ATOM   8181 C  C   . ALA A 1 1028 ? 57.095 42.242  -16.274 1.00 30.88 ? 1028 ALA A C   1 
ATOM   8182 O  O   . ALA A 1 1028 ? 57.124 42.955  -17.277 1.00 32.35 ? 1028 ALA A O   1 
ATOM   8183 C  CB  . ALA A 1 1028 ? 58.052 43.937  -14.733 1.00 29.68 ? 1028 ALA A CB  1 
ATOM   8184 N  N   . PRO A 1 1029 ? 56.212 41.246  -16.129 1.00 29.42 ? 1029 PRO A N   1 
ATOM   8185 C  CA  . PRO A 1 1029 ? 55.235 41.007  -17.196 1.00 31.23 ? 1029 PRO A CA  1 
ATOM   8186 C  C   . PRO A 1 1029 ? 54.153 42.083  -17.268 1.00 29.78 ? 1029 PRO A C   1 
ATOM   8187 O  O   . PRO A 1 1029 ? 53.863 42.734  -16.280 1.00 33.18 ? 1029 PRO A O   1 
ATOM   8188 C  CB  . PRO A 1 1029 ? 54.658 39.638  -16.856 1.00 30.95 ? 1029 PRO A CB  1 
ATOM   8189 C  CG  . PRO A 1 1029 ? 54.914 39.466  -15.397 1.00 31.20 ? 1029 PRO A CG  1 
ATOM   8190 C  CD  . PRO A 1 1029 ? 56.188 40.192  -15.102 1.00 29.43 ? 1029 PRO A CD  1 
ATOM   8191 N  N   . GLU A 1 1030 ? 53.576 42.288  -18.441 1.00 30.35 ? 1030 GLU A N   1 
ATOM   8192 C  CA  . GLU A 1 1030 ? 52.509 43.270  -18.555 1.00 30.58 ? 1030 GLU A CA  1 
ATOM   8193 C  C   . GLU A 1 1030 ? 51.239 42.697  -17.912 1.00 30.27 ? 1030 GLU A C   1 
ATOM   8194 O  O   . GLU A 1 1030 ? 51.047 41.469  -17.794 1.00 33.16 ? 1030 GLU A O   1 
ATOM   8195 C  CB  . GLU A 1 1030 ? 52.254 43.635  -20.029 1.00 30.83 ? 1030 GLU A CB  1 
ATOM   8196 C  CG  . GLU A 1 1030 ? 53.432 44.355  -20.717 1.00 29.20 ? 1030 GLU A CG  1 
ATOM   8197 C  CD  . GLU A 1 1030 ? 53.099 44.765  -22.141 1.00 31.77 ? 1030 GLU A CD  1 
ATOM   8198 O  OE1 . GLU A 1 1030 ? 52.063 44.283  -22.654 1.00 33.63 ? 1030 GLU A OE1 1 
ATOM   8199 O  OE2 . GLU A 1 1030 ? 53.870 45.551  -22.753 1.00 27.04 ? 1030 GLU A OE2 1 
ATOM   8200 N  N   . VAL A 1 1031 ? 50.369 43.595  -17.507 1.00 28.96 ? 1031 VAL A N   1 
ATOM   8201 C  CA  . VAL A 1 1031 ? 49.142 43.207  -16.836 1.00 24.05 ? 1031 VAL A CA  1 
ATOM   8202 C  C   . VAL A 1 1031 ? 47.956 42.985  -17.781 1.00 22.17 ? 1031 VAL A C   1 
ATOM   8203 O  O   . VAL A 1 1031 ? 48.014 43.335  -18.949 1.00 22.49 ? 1031 VAL A O   1 
ATOM   8204 C  CB  . VAL A 1 1031 ? 48.775 44.277  -15.781 1.00 27.11 ? 1031 VAL A CB  1 
ATOM   8205 C  CG1 . VAL A 1 1031 ? 49.976 44.499  -14.855 1.00 29.31 ? 1031 VAL A CG1 1 
ATOM   8206 C  CG2 . VAL A 1 1031 ? 48.367 45.546  -16.451 1.00 26.10 ? 1031 VAL A CG2 1 
ATOM   8207 N  N   . CYS A 1 1032 ? 46.914 42.351  -17.256 1.00 19.11 ? 1032 CYS A N   1 
ATOM   8208 C  CA  . CYS A 1 1032 ? 45.674 42.066  -17.972 1.00 18.66 ? 1032 CYS A CA  1 
ATOM   8209 C  C   . CYS A 1 1032 ? 44.756 43.288  -18.051 1.00 17.06 ? 1032 CYS A C   1 
ATOM   8210 O  O   . CYS A 1 1032 ? 44.913 44.209  -17.282 1.00 16.72 ? 1032 CYS A O   1 
ATOM   8211 C  CB  . CYS A 1 1032 ? 44.909 40.989  -17.244 1.00 17.03 ? 1032 CYS A CB  1 
ATOM   8212 S  SG  . CYS A 1 1032 ? 45.735 39.358  -17.399 1.00 27.38 ? 1032 CYS A SG  1 
ATOM   8213 N  N   . PRO A 1 1033 ? 43.818 43.323  -19.022 1.00 16.38 ? 1033 PRO A N   1 
ATOM   8214 C  CA  . PRO A 1 1033 ? 42.907 44.468  -19.103 1.00 16.31 ? 1033 PRO A CA  1 
ATOM   8215 C  C   . PRO A 1 1033 ? 42.179 44.629  -17.773 1.00 15.04 ? 1033 PRO A C   1 
ATOM   8216 O  O   . PRO A 1 1033 ? 41.680 43.677  -17.167 1.00 15.37 ? 1033 PRO A O   1 
ATOM   8217 C  CB  . PRO A 1 1033 ? 41.910 44.062  -20.216 1.00 16.63 ? 1033 PRO A CB  1 
ATOM   8218 C  CG  . PRO A 1 1033 ? 42.733 43.122  -21.055 1.00 16.82 ? 1033 PRO A CG  1 
ATOM   8219 C  CD  . PRO A 1 1033 ? 43.538 42.330  -20.089 1.00 18.37 ? 1033 PRO A CD  1 
ATOM   8220 N  N   . MET A 1 1034 ? 42.087 45.882  -17.361 1.00 13.82 ? 1034 MET A N   1 
ATOM   8221 C  CA  . MET A 1 1034 ? 41.477 46.332  -16.096 1.00 14.33 ? 1034 MET A CA  1 
ATOM   8222 C  C   . MET A 1 1034 ? 42.284 45.971  -14.852 1.00 18.16 ? 1034 MET A C   1 
ATOM   8223 O  O   . MET A 1 1034 ? 41.803 46.210  -13.731 1.00 21.78 ? 1034 MET A O   1 
ATOM   8224 C  CB  . MET A 1 1034 ? 40.025 45.850  -15.916 1.00 14.66 ? 1034 MET A CB  1 
ATOM   8225 C  CG  . MET A 1 1034 ? 39.093 46.360  -17.025 1.00 15.52 ? 1034 MET A CG  1 
ATOM   8226 S  SD  . MET A 1 1034 ? 39.147 48.210  -17.261 1.00 17.03 ? 1034 MET A SD  1 
ATOM   8227 C  CE  . MET A 1 1034 ? 38.356 48.775  -15.660 1.00 16.62 ? 1034 MET A CE  1 
ATOM   8228 N  N   . GLU A 1 1035 ? 43.494 45.475  -15.033 1.00 14.67 ? 1035 GLU A N   1 
ATOM   8229 C  CA  . GLU A 1 1035 ? 44.312 45.135  -13.875 1.00 14.72 ? 1035 GLU A CA  1 
ATOM   8230 C  C   . GLU A 1 1035 ? 45.362 46.215  -13.658 1.00 14.54 ? 1035 GLU A C   1 
ATOM   8231 O  O   . GLU A 1 1035 ? 45.708 46.962  -14.553 1.00 14.78 ? 1035 GLU A O   1 
ATOM   8232 C  CB  . GLU A 1 1035 ? 44.938 43.748  -14.050 1.00 20.54 ? 1035 GLU A CB  1 
ATOM   8233 C  CG  . GLU A 1 1035 ? 43.883 42.647  -13.841 1.00 29.76 ? 1035 GLU A CG  1 
ATOM   8234 C  CD  . GLU A 1 1035 ? 43.412 42.543  -12.379 1.00 35.79 ? 1035 GLU A CD  1 
ATOM   8235 O  OE1 . GLU A 1 1035 ? 42.606 43.395  -11.918 1.00 36.87 ? 1035 GLU A OE1 1 
ATOM   8236 O  OE2 . GLU A 1 1035 ? 43.872 41.598  -11.691 1.00 42.18 ? 1035 GLU A OE2 1 
ATOM   8237 N  N   . THR A 1 1036 ? 45.867 46.292  -12.426 1.00 14.73 ? 1036 THR A N   1 
ATOM   8238 C  CA  . THR A 1 1036 ? 46.881 47.251  -12.020 1.00 14.95 ? 1036 THR A CA  1 
ATOM   8239 C  C   . THR A 1 1036 ? 47.840 46.423  -11.186 1.00 15.73 ? 1036 THR A C   1 
ATOM   8240 O  O   . THR A 1 1036 ? 47.408 45.662  -10.318 1.00 17.11 ? 1036 THR A O   1 
ATOM   8241 C  CB  . THR A 1 1036 ? 46.273 48.359  -11.136 1.00 15.51 ? 1036 THR A CB  1 
ATOM   8242 O  OG1 . THR A 1 1036 ? 45.198 48.986  -11.832 1.00 15.03 ? 1036 THR A OG1 1 
ATOM   8243 C  CG2 . THR A 1 1036 ? 47.332 49.415  -10.768 1.00 15.45 ? 1036 THR A CG2 1 
ATOM   8244 N  N   . ALA A 1 1037 ? 49.129 46.527  -11.501 1.00 14.75 ? 1037 ALA A N   1 
ATOM   8245 C  CA  . ALA A 1 1037 ? 50.153 45.801  -10.754 1.00 14.62 ? 1037 ALA A CA  1 
ATOM   8246 C  C   . ALA A 1 1037 ? 51.279 46.748  -10.429 1.00 14.92 ? 1037 ALA A C   1 
ATOM   8247 O  O   . ALA A 1 1037 ? 51.436 47.797  -11.079 1.00 16.39 ? 1037 ALA A O   1 
ATOM   8248 C  CB  . ALA A 1 1037 ? 50.694 44.631  -11.602 1.00 18.43 ? 1037 ALA A CB  1 
ATOM   8249 N  N   . ALA A 1 1038 ? 52.066 46.415  -9.414  1.00 12.63 ? 1038 ALA A N   1 
ATOM   8250 C  CA  . ALA A 1 1038 ? 53.202 47.221  -9.054  1.00 14.96 ? 1038 ALA A CA  1 
ATOM   8251 C  C   . ALA A 1 1038 ? 54.463 46.358  -9.080  1.00 14.75 ? 1038 ALA A C   1 
ATOM   8252 O  O   . ALA A 1 1038 ? 54.426 45.190  -8.749  1.00 14.66 ? 1038 ALA A O   1 
ATOM   8253 C  CB  . ALA A 1 1038 ? 53.015 47.840  -7.670  1.00 14.18 ? 1038 ALA A CB  1 
ATOM   8254 N  N   . TYR A 1 1039 ? 55.549 46.962  -9.520  1.00 15.28 ? 1039 TYR A N   1 
ATOM   8255 C  CA  . TYR A 1 1039 ? 56.833 46.282  -9.592  1.00 15.45 ? 1039 TYR A CA  1 
ATOM   8256 C  C   . TYR A 1 1039 ? 57.911 47.157  -9.052  1.00 17.05 ? 1039 TYR A C   1 
ATOM   8257 O  O   . TYR A 1 1039 ? 57.836 48.368  -9.171  1.00 18.95 ? 1039 TYR A O   1 
ATOM   8258 C  CB  . TYR A 1 1039 ? 57.190 45.949  -11.036 1.00 15.98 ? 1039 TYR A CB  1 
ATOM   8259 C  CG  . TYR A 1 1039 ? 56.198 45.063  -11.718 1.00 17.06 ? 1039 TYR A CG  1 
ATOM   8260 C  CD1 . TYR A 1 1039 ? 56.171 43.686  -11.484 1.00 19.53 ? 1039 TYR A CD1 1 
ATOM   8261 C  CD2 . TYR A 1 1039 ? 55.268 45.599  -12.600 1.00 18.93 ? 1039 TYR A CD2 1 
ATOM   8262 C  CE1 . TYR A 1 1039 ? 55.242 42.872  -12.113 1.00 20.00 ? 1039 TYR A CE1 1 
ATOM   8263 C  CE2 . TYR A 1 1039 ? 54.337 44.804  -13.247 1.00 20.76 ? 1039 TYR A CE2 1 
ATOM   8264 C  CZ  . TYR A 1 1039 ? 54.325 43.452  -13.011 1.00 21.40 ? 1039 TYR A CZ  1 
ATOM   8265 O  OH  . TYR A 1 1039 ? 53.427 42.685  -13.724 1.00 27.07 ? 1039 TYR A OH  1 
ATOM   8266 N  N   . VAL A 1 1040 ? 58.914 46.543  -8.426  1.00 16.56 ? 1040 VAL A N   1 
ATOM   8267 C  CA  . VAL A 1 1040 ? 60.057 47.280  -7.932  1.00 17.33 ? 1040 VAL A CA  1 
ATOM   8268 C  C   . VAL A 1 1040 ? 61.287 46.627  -8.544  1.00 17.96 ? 1040 VAL A C   1 
ATOM   8269 O  O   . VAL A 1 1040 ? 61.498 45.409  -8.409  1.00 17.91 ? 1040 VAL A O   1 
ATOM   8270 C  CB  . VAL A 1 1040 ? 60.178 47.232  -6.420  1.00 16.28 ? 1040 VAL A CB  1 
ATOM   8271 C  CG1 . VAL A 1 1040 ? 61.502 47.900  -5.983  1.00 17.70 ? 1040 VAL A CG1 1 
ATOM   8272 C  CG2 . VAL A 1 1040 ? 58.998 48.013  -5.792  1.00 17.11 ? 1040 VAL A CG2 1 
ATOM   8273 N  N   . SER A 1 1041 ? 62.099 47.437  -9.223  1.00 16.46 ? 1041 SER A N   1 
ATOM   8274 C  CA  . SER A 1 1041 ? 63.340 46.938  -9.778  1.00 16.30 ? 1041 SER A CA  1 
ATOM   8275 C  C   . SER A 1 1041 ? 64.475 47.397  -8.854  1.00 16.00 ? 1041 SER A C   1 
ATOM   8276 O  O   . SER A 1 1041 ? 64.478 48.537  -8.332  1.00 16.32 ? 1041 SER A O   1 
ATOM   8277 C  CB  . SER A 1 1041 ? 63.564 47.445  -11.197 1.00 16.69 ? 1041 SER A CB  1 
ATOM   8278 O  OG  . SER A 1 1041 ? 63.636 48.834  -11.265 1.00 18.17 ? 1041 SER A OG  1 
ATOM   8279 N  N   . SER A 1 1042 ? 65.436 46.485  -8.634  1.00 17.99 ? 1042 SER A N   1 
ATOM   8280 C  CA  . SER A 1 1042 ? 66.602 46.765  -7.792  1.00 17.05 ? 1042 SER A CA  1 
ATOM   8281 C  C   . SER A 1 1042 ? 67.844 46.839  -8.697  1.00 17.13 ? 1042 SER A C   1 
ATOM   8282 O  O   . SER A 1 1042 ? 67.977 46.017  -9.611  1.00 20.83 ? 1042 SER A O   1 
ATOM   8283 C  CB  . SER A 1 1042 ? 66.778 45.653  -6.749  1.00 18.27 ? 1042 SER A CB  1 
ATOM   8284 O  OG  . SER A 1 1042 ? 65.708 45.679  -5.804  1.00 19.86 ? 1042 SER A OG  1 
ATOM   8285 N  N   . HIS A 1 1043 ? 68.705 47.812  -8.432  1.00 19.00 ? 1043 HIS A N   1 
ATOM   8286 C  CA  . HIS A 1 1043 ? 69.884 48.079  -9.272  1.00 17.76 ? 1043 HIS A CA  1 
ATOM   8287 C  C   . HIS A 1 1043 ? 71.149 48.189  -8.435  1.00 22.30 ? 1043 HIS A C   1 
ATOM   8288 O  O   . HIS A 1 1043 ? 71.184 48.861  -7.404  1.00 21.38 ? 1043 HIS A O   1 
ATOM   8289 C  CB  . HIS A 1 1043 ? 69.641 49.371  -10.066 1.00 19.48 ? 1043 HIS A CB  1 
ATOM   8290 C  CG  . HIS A 1 1043 ? 68.340 49.353  -10.809 1.00 20.30 ? 1043 HIS A CG  1 
ATOM   8291 N  ND1 . HIS A 1 1043 ? 68.227 48.868  -12.095 1.00 19.71 ? 1043 HIS A ND1 1 
ATOM   8292 C  CD2 . HIS A 1 1043 ? 67.074 49.614  -10.391 1.00 17.04 ? 1043 HIS A CD2 1 
ATOM   8293 C  CE1 . HIS A 1 1043 ? 66.948 48.834  -12.439 1.00 19.50 ? 1043 HIS A CE1 1 
ATOM   8294 N  NE2 . HIS A 1 1043 ? 66.230 49.278  -11.414 1.00 17.62 ? 1043 HIS A NE2 1 
ATOM   8295 N  N   . SER A 1 1044 ? 72.183 47.495  -8.916  1.00 26.43 ? 1044 SER A N   1 
ATOM   8296 C  CA  . SER A 1 1044 ? 73.461 47.460  -8.216  1.00 33.10 ? 1044 SER A CA  1 
ATOM   8297 C  C   . SER A 1 1044 ? 74.380 48.562  -8.716  1.00 34.92 ? 1044 SER A C   1 
ATOM   8298 O  O   . SER A 1 1044 ? 75.376 48.900  -8.086  1.00 37.81 ? 1044 SER A O   1 
ATOM   8299 C  CB  . SER A 1 1044 ? 74.117 46.096  -8.448  1.00 33.46 ? 1044 SER A CB  1 
ATOM   8300 O  OG  . SER A 1 1044 ? 74.118 45.760  -9.838  1.00 36.01 ? 1044 SER A OG  1 
ATOM   8301 N  N   . SER A 1 1045 ? 73.950 49.092  -9.850  1.00 38.70 ? 1045 SER A N   1 
ATOM   8302 C  CA  . SER A 1 1045 ? 74.537 50.117  -10.707 1.00 43.20 ? 1045 SER A CA  1 
ATOM   8303 C  C   . SER A 1 1045 ? 76.071 50.286  -10.851 1.00 44.01 ? 1045 SER A C   1 
ATOM   8304 O  O   . SER A 1 1045 ? 76.886 49.416  -10.427 1.00 46.45 ? 1045 SER A O   1 
ATOM   8305 C  CB  . SER A 1 1045 ? 73.832 51.460  -10.438 1.00 43.20 ? 1045 SER A CB  1 
ATOM   8306 O  OG  . SER A 1 1045 ? 74.165 52.448  -11.395 1.00 42.97 ? 1045 SER A OG  1 
ATOM   8307 O  OXT . SER A 1 1045 ? 76.470 51.320  -11.475 1.00 48.74 ? 1045 SER A OXT 1 
HETATM 8308 C  C1  . NAG B 2 .    ? 58.378 44.812  12.817  1.00 40.75 ? 1802 NAG A C1  1 
HETATM 8309 C  C2  . NAG B 2 .    ? 59.503 44.462  13.796  1.00 44.46 ? 1802 NAG A C2  1 
HETATM 8310 C  C3  . NAG B 2 .    ? 60.007 43.031  13.602  1.00 46.95 ? 1802 NAG A C3  1 
HETATM 8311 C  C4  . NAG B 2 .    ? 58.837 42.063  13.642  1.00 47.82 ? 1802 NAG A C4  1 
HETATM 8312 C  C5  . NAG B 2 .    ? 57.794 42.480  12.601  1.00 48.35 ? 1802 NAG A C5  1 
HETATM 8313 C  C6  . NAG B 2 .    ? 56.581 41.566  12.622  1.00 49.79 ? 1802 NAG A C6  1 
HETATM 8314 C  C7  . NAG B 2 .    ? 60.915 46.211  14.624  1.00 49.31 ? 1802 NAG A C7  1 
HETATM 8315 C  C8  . NAG B 2 .    ? 61.932 45.702  15.634  1.00 51.27 ? 1802 NAG A C8  1 
HETATM 8316 N  N2  . NAG B 2 .    ? 60.596 45.398  13.622  1.00 47.01 ? 1802 NAG A N2  1 
HETATM 8317 O  O3  . NAG B 2 .    ? 60.917 42.713  14.649  1.00 47.77 ? 1802 NAG A O3  1 
HETATM 8318 O  O4  . NAG B 2 .    ? 59.304 40.746  13.372  1.00 50.33 ? 1802 NAG A O4  1 
HETATM 8319 O  O5  . NAG B 2 .    ? 57.328 43.831  12.874  1.00 45.01 ? 1802 NAG A O5  1 
HETATM 8320 O  O6  . NAG B 2 .    ? 56.921 40.252  12.183  1.00 54.76 ? 1802 NAG A O6  1 
HETATM 8321 O  O7  . NAG B 2 .    ? 60.413 47.328  14.768  1.00 52.16 ? 1802 NAG A O7  1 
HETATM 8322 P  P   . PO4 C 3 .    ? 45.255 65.328  -29.614 1.00 32.06 ? 1803 PO4 A P   1 
HETATM 8323 O  O1  . PO4 C 3 .    ? 44.753 66.671  -30.271 1.00 37.51 ? 1803 PO4 A O1  1 
HETATM 8324 O  O2  . PO4 C 3 .    ? 46.657 64.906  -30.026 1.00 36.56 ? 1803 PO4 A O2  1 
HETATM 8325 O  O3  . PO4 C 3 .    ? 44.193 64.234  -29.989 1.00 38.52 ? 1803 PO4 A O3  1 
HETATM 8326 O  O4  . PO4 C 3 .    ? 45.217 65.562  -28.097 1.00 38.02 ? 1803 PO4 A O4  1 
HETATM 8327 ZN ZN  . ZN  D 4 .    ? 34.480 63.960  7.933   1.00 13.25 ? 1805 ZN  A ZN  1 
HETATM 8328 C  C8  . GB2 E 5 .    ? 29.014 65.265  12.129  1.00 30.03 ? 1804 GB2 A C8  1 
HETATM 8329 N  N7  . GB2 E 5 .    ? 29.894 65.067  10.978  1.00 27.70 ? 1804 GB2 A N7  1 
HETATM 8330 C  C6  . GB2 E 5 .    ? 29.808 65.758  9.700   1.00 22.48 ? 1804 GB2 A C6  1 
HETATM 8331 C  C5  . GB2 E 5 .    ? 30.957 65.230  8.842   1.00 17.95 ? 1804 GB2 A C5  1 
HETATM 8332 N  N1  . GB2 E 5 .    ? 30.755 65.365  7.415   1.00 16.62 ? 1804 GB2 A N1  1 
HETATM 8333 C  C2  . GB2 E 5 .    ? 31.326 66.569  6.813   1.00 18.00 ? 1804 GB2 A C2  1 
HETATM 8334 C  C3  . GB2 E 5 .    ? 32.651 66.527  7.575   1.00 16.61 ? 1804 GB2 A C3  1 
HETATM 8335 O  O3  . GB2 E 5 .    ? 33.681 65.767  6.967   1.00 16.03 ? 1804 GB2 A O3  1 
HETATM 8336 C  C4  . GB2 E 5 .    ? 32.254 66.020  8.976   1.00 17.26 ? 1804 GB2 A C4  1 
HETATM 8337 O  O4  . GB2 E 5 .    ? 33.208 65.124  9.529   1.00 14.94 ? 1804 GB2 A O4  1 
HETATM 8338 C  C15 . GB2 E 5 .    ? 27.382 67.327  11.668  1.00 31.87 ? 1804 GB2 A C15 1 
HETATM 8339 C  C14 . GB2 E 5 .    ? 27.073 68.715  11.823  1.00 34.62 ? 1804 GB2 A C14 1 
HETATM 8340 C  C13 . GB2 E 5 .    ? 27.924 69.560  12.572  1.00 31.55 ? 1804 GB2 A C13 1 
HETATM 8341 C  C12 . GB2 E 5 .    ? 29.064 68.969  13.140  1.00 32.41 ? 1804 GB2 A C12 1 
HETATM 8342 C  C11 . GB2 E 5 .    ? 29.417 67.596  13.017  1.00 32.20 ? 1804 GB2 A C11 1 
HETATM 8343 C  C10 . GB2 E 5 .    ? 28.556 66.736  12.259  1.00 32.23 ? 1804 GB2 A C10 1 
HETATM 8344 C  C9  . GB2 E 5 .    ? 27.851 64.285  12.003  1.00 33.01 ? 1804 GB2 A C9  1 
HETATM 8345 O  O9  . GB2 E 5 .    ? 28.327 63.103  11.363  1.00 33.67 ? 1804 GB2 A O9  1 
HETATM 8346 C  C1  . MPD F 6 .    ? 14.724 60.812  10.260  1.00 22.58 ? 1801 MPD A C1  1 
HETATM 8347 C  C2  . MPD F 6 .    ? 16.150 60.912  10.629  1.00 24.40 ? 1801 MPD A C2  1 
HETATM 8348 O  O2  . MPD F 6 .    ? 16.891 59.953  9.787   1.00 26.53 ? 1801 MPD A O2  1 
HETATM 8349 C  CM  . MPD F 6 .    ? 16.677 62.304  10.317  1.00 27.54 ? 1801 MPD A CM  1 
HETATM 8350 C  C3  . MPD F 6 .    ? 16.279 60.553  12.140  1.00 24.99 ? 1801 MPD A C3  1 
HETATM 8351 C  C4  . MPD F 6 .    ? 17.662 60.411  12.782  1.00 22.23 ? 1801 MPD A C4  1 
HETATM 8352 O  O4  . MPD F 6 .    ? 17.588 59.483  13.878  1.00 19.30 ? 1801 MPD A O4  1 
HETATM 8353 C  C5  . MPD F 6 .    ? 18.120 61.751  13.378  1.00 24.37 ? 1801 MPD A C5  1 
HETATM 8354 O  O   . HOH G 7 .    ? 27.976 46.752  -31.343 1.00 31.91 ? 1806 HOH A O   1 
HETATM 8355 O  O   . HOH G 7 .    ? 28.287 44.047  -29.444 1.00 39.55 ? 1807 HOH A O   1 
HETATM 8356 O  O   . HOH G 7 .    ? 26.306 44.063  -27.192 1.00 37.81 ? 1808 HOH A O   1 
HETATM 8357 O  O   . HOH G 7 .    ? 26.839 41.280  -27.395 1.00 38.61 ? 1809 HOH A O   1 
HETATM 8358 O  O   . HOH G 7 .    ? 29.301 40.809  -25.461 1.00 30.27 ? 1810 HOH A O   1 
HETATM 8359 O  O   . HOH G 7 .    ? 28.540 40.977  -21.542 1.00 18.58 ? 1811 HOH A O   1 
HETATM 8360 O  O   . HOH G 7 .    ? 27.702 38.397  -22.502 1.00 36.79 ? 1812 HOH A O   1 
HETATM 8361 O  O   . HOH G 7 .    ? 27.673 36.220  -19.559 1.00 29.16 ? 1813 HOH A O   1 
HETATM 8362 O  O   . HOH G 7 .    ? 29.273 33.978  -19.310 1.00 47.18 ? 1814 HOH A O   1 
HETATM 8363 O  O   . HOH G 7 .    ? 29.492 34.752  -16.226 1.00 34.33 ? 1815 HOH A O   1 
HETATM 8364 O  O   . HOH G 7 .    ? 30.266 34.933  -12.210 1.00 25.63 ? 1816 HOH A O   1 
HETATM 8365 O  O   . HOH G 7 .    ? 30.376 34.477  -9.532  1.00 37.78 ? 1817 HOH A O   1 
HETATM 8366 O  O   . HOH G 7 .    ? 30.125 33.131  -6.028  1.00 44.26 ? 1818 HOH A O   1 
HETATM 8367 O  O   . HOH G 7 .    ? 28.073 35.076  -6.572  1.00 27.98 ? 1819 HOH A O   1 
HETATM 8368 O  O   . HOH G 7 .    ? 25.248 34.197  -6.840  1.00 42.92 ? 1820 HOH A O   1 
HETATM 8369 O  O   . HOH G 7 .    ? 22.829 36.327  -9.364  1.00 38.05 ? 1821 HOH A O   1 
HETATM 8370 O  O   . HOH G 7 .    ? 24.409 38.853  -11.390 1.00 24.64 ? 1822 HOH A O   1 
HETATM 8371 O  O   . HOH G 7 .    ? 22.200 40.429  -11.079 1.00 26.15 ? 1823 HOH A O   1 
HETATM 8372 O  O   . HOH G 7 .    ? 21.874 40.086  -8.517  1.00 26.90 ? 1824 HOH A O   1 
HETATM 8373 O  O   . HOH G 7 .    ? 20.672 42.483  -7.203  1.00 22.01 ? 1825 HOH A O   1 
HETATM 8374 O  O   . HOH G 7 .    ? 19.690 41.264  -4.934  1.00 30.19 ? 1826 HOH A O   1 
HETATM 8375 O  O   . HOH G 7 .    ? 19.110 42.214  -2.469  1.00 31.77 ? 1827 HOH A O   1 
HETATM 8376 O  O   . HOH G 7 .    ? 16.607 42.807  -2.167  1.00 30.08 ? 1828 HOH A O   1 
HETATM 8377 O  O   . HOH G 7 .    ? 18.690 39.053  -2.508  1.00 42.50 ? 1829 HOH A O   1 
HETATM 8378 O  O   . HOH G 7 .    ? 17.771 37.598  -0.005  1.00 42.33 ? 1830 HOH A O   1 
HETATM 8379 O  O   . HOH G 7 .    ? 21.947 36.636  0.357   1.00 26.57 ? 1831 HOH A O   1 
HETATM 8380 O  O   . HOH G 7 .    ? 24.408 34.211  0.380   1.00 49.90 ? 1832 HOH A O   1 
HETATM 8381 O  O   . HOH G 7 .    ? 27.044 33.479  -3.086  1.00 44.06 ? 1833 HOH A O   1 
HETATM 8382 O  O   . HOH G 7 .    ? 30.037 33.977  -1.467  1.00 31.36 ? 1834 HOH A O   1 
HETATM 8383 O  O   . HOH G 7 .    ? 32.024 34.116  -3.143  1.00 25.25 ? 1835 HOH A O   1 
HETATM 8384 O  O   . HOH G 7 .    ? 33.171 36.406  -4.245  1.00 19.33 ? 1836 HOH A O   1 
HETATM 8385 O  O   . HOH G 7 .    ? 32.281 38.943  -4.791  1.00 14.82 ? 1837 HOH A O   1 
HETATM 8386 O  O   . HOH G 7 .    ? 35.940 35.815  -4.384  1.00 22.21 ? 1838 HOH A O   1 
HETATM 8387 O  O   . HOH G 7 .    ? 39.882 38.638  -3.398  1.00 27.01 ? 1839 HOH A O   1 
HETATM 8388 O  O   . HOH G 7 .    ? 39.920 39.483  -0.198  1.00 29.36 ? 1840 HOH A O   1 
HETATM 8389 O  O   . HOH G 7 .    ? 38.261 39.836  1.853   1.00 16.63 ? 1841 HOH A O   1 
HETATM 8390 O  O   . HOH G 7 .    ? 37.223 37.234  2.933   1.00 34.99 ? 1842 HOH A O   1 
HETATM 8391 O  O   . HOH G 7 .    ? 34.321 36.085  3.485   1.00 37.18 ? 1843 HOH A O   1 
HETATM 8392 O  O   . HOH G 7 .    ? 37.200 33.746  5.691   1.00 42.28 ? 1844 HOH A O   1 
HETATM 8393 O  O   . HOH G 7 .    ? 40.013 35.234  11.438  1.00 27.74 ? 1845 HOH A O   1 
HETATM 8394 O  O   . HOH G 7 .    ? 40.059 39.051  9.247   1.00 30.26 ? 1846 HOH A O   1 
HETATM 8395 O  O   . HOH G 7 .    ? 42.612 39.584  7.994   1.00 43.29 ? 1847 HOH A O   1 
HETATM 8396 O  O   . HOH G 7 .    ? 44.629 40.830  7.785   1.00 46.47 ? 1848 HOH A O   1 
HETATM 8397 O  O   . HOH G 7 .    ? 46.448 42.659  9.712   1.00 34.65 ? 1849 HOH A O   1 
HETATM 8398 O  O   . HOH G 7 .    ? 48.514 44.727  10.395  1.00 40.02 ? 1850 HOH A O   1 
HETATM 8399 O  O   . HOH G 7 .    ? 46.732 45.670  11.677  1.00 33.08 ? 1851 HOH A O   1 
HETATM 8400 O  O   . HOH G 7 .    ? 46.904 48.404  11.640  1.00 21.38 ? 1852 HOH A O   1 
HETATM 8401 O  O   . HOH G 7 .    ? 47.899 49.349  13.929  1.00 18.46 ? 1853 HOH A O   1 
HETATM 8402 O  O   . HOH G 7 .    ? 48.008 48.172  16.521  1.00 22.47 ? 1854 HOH A O   1 
HETATM 8403 O  O   . HOH G 7 .    ? 46.106 45.807  16.452  1.00 39.91 ? 1855 HOH A O   1 
HETATM 8404 O  O   . HOH G 7 .    ? 43.569 44.660  19.425  1.00 49.71 ? 1856 HOH A O   1 
HETATM 8405 O  O   . HOH G 7 .    ? 45.602 44.812  23.064  1.00 35.87 ? 1857 HOH A O   1 
HETATM 8406 O  O   . HOH G 7 .    ? 44.109 45.219  25.394  1.00 35.16 ? 1858 HOH A O   1 
HETATM 8407 O  O   . HOH G 7 .    ? 40.002 45.131  25.391  1.00 37.50 ? 1859 HOH A O   1 
HETATM 8408 O  O   . HOH G 7 .    ? 39.181 43.553  26.821  1.00 35.04 ? 1860 HOH A O   1 
HETATM 8409 O  O   . HOH G 7 .    ? 39.687 41.374  25.517  1.00 40.37 ? 1861 HOH A O   1 
HETATM 8410 O  O   . HOH G 7 .    ? 37.444 40.320  26.523  1.00 42.35 ? 1862 HOH A O   1 
HETATM 8411 O  O   . HOH G 7 .    ? 37.309 37.430  24.956  1.00 47.61 ? 1863 HOH A O   1 
HETATM 8412 O  O   . HOH G 7 .    ? 34.879 37.928  22.273  1.00 42.88 ? 1864 HOH A O   1 
HETATM 8413 O  O   . HOH G 7 .    ? 39.656 39.494  20.154  1.00 32.67 ? 1865 HOH A O   1 
HETATM 8414 O  O   . HOH G 7 .    ? 39.200 38.804  17.342  1.00 20.76 ? 1866 HOH A O   1 
HETATM 8415 O  O   . HOH G 7 .    ? 41.809 39.000  16.729  1.00 29.83 ? 1867 HOH A O   1 
HETATM 8416 O  O   . HOH G 7 .    ? 44.816 40.306  13.385  1.00 43.22 ? 1868 HOH A O   1 
HETATM 8417 O  O   . HOH G 7 .    ? 44.311 45.857  10.087  1.00 17.23 ? 1869 HOH A O   1 
HETATM 8418 O  O   . HOH G 7 .    ? 42.951 47.923  11.297  1.00 17.14 ? 1870 HOH A O   1 
HETATM 8419 O  O   . HOH G 7 .    ? 41.567 43.079  8.007   1.00 20.29 ? 1871 HOH A O   1 
HETATM 8420 O  O   . HOH G 7 .    ? 47.653 39.897  5.991   1.00 39.36 ? 1872 HOH A O   1 
HETATM 8421 O  O   . HOH G 7 .    ? 48.086 41.508  3.758   1.00 25.79 ? 1873 HOH A O   1 
HETATM 8422 O  O   . HOH G 7 .    ? 49.631 40.829  1.657   1.00 38.53 ? 1874 HOH A O   1 
HETATM 8423 O  O   . HOH G 7 .    ? 48.545 40.683  -0.876  1.00 29.52 ? 1875 HOH A O   1 
HETATM 8424 O  O   . HOH G 7 .    ? 47.434 42.699  -2.345  1.00 20.62 ? 1876 HOH A O   1 
HETATM 8425 O  O   . HOH G 7 .    ? 48.065 41.423  -5.360  1.00 32.12 ? 1877 HOH A O   1 
HETATM 8426 O  O   . HOH G 7 .    ? 48.707 43.969  -6.128  1.00 20.55 ? 1878 HOH A O   1 
HETATM 8427 O  O   . HOH G 7 .    ? 47.895 43.700  -8.567  1.00 23.95 ? 1879 HOH A O   1 
HETATM 8428 O  O   . HOH G 7 .    ? 45.578 41.796  -8.896  1.00 40.74 ? 1880 HOH A O   1 
HETATM 8429 O  O   . HOH G 7 .    ? 43.552 41.537  -7.543  1.00 29.98 ? 1881 HOH A O   1 
HETATM 8430 O  O   . HOH G 7 .    ? 42.080 40.384  -9.779  1.00 42.37 ? 1882 HOH A O   1 
HETATM 8431 O  O   . HOH G 7 .    ? 43.948 37.799  -9.746  1.00 46.09 ? 1883 HOH A O   1 
HETATM 8432 O  O   . HOH G 7 .    ? 43.222 38.334  -6.233  1.00 40.18 ? 1884 HOH A O   1 
HETATM 8433 O  O   . HOH G 7 .    ? 42.554 39.317  -1.310  1.00 32.81 ? 1885 HOH A O   1 
HETATM 8434 O  O   . HOH G 7 .    ? 44.506 41.619  -0.393  1.00 19.00 ? 1886 HOH A O   1 
HETATM 8435 O  O   . HOH G 7 .    ? 46.171 39.685  0.238   1.00 32.40 ? 1887 HOH A O   1 
HETATM 8436 O  O   . HOH G 7 .    ? 48.791 38.770  -2.897  1.00 45.43 ? 1888 HOH A O   1 
HETATM 8437 O  O   . HOH G 7 .    ? 50.948 44.072  -7.897  1.00 15.84 ? 1889 HOH A O   1 
HETATM 8438 O  O   . HOH G 7 .    ? 51.823 40.769  -12.960 1.00 34.90 ? 1890 HOH A O   1 
HETATM 8439 O  O   . HOH G 7 .    ? 47.134 41.216  -14.664 1.00 31.14 ? 1891 HOH A O   1 
HETATM 8440 O  O   . HOH G 7 .    ? 42.433 39.027  -15.518 1.00 30.99 ? 1892 HOH A O   1 
HETATM 8441 O  O   . HOH G 7 .    ? 41.529 40.918  -17.466 1.00 23.18 ? 1893 HOH A O   1 
HETATM 8442 O  O   . HOH G 7 .    ? 40.875 40.472  -21.331 1.00 31.46 ? 1894 HOH A O   1 
HETATM 8443 O  O   . HOH G 7 .    ? 38.655 41.949  -22.081 1.00 30.22 ? 1895 HOH A O   1 
HETATM 8444 O  O   . HOH G 7 .    ? 36.915 41.049  -24.591 1.00 34.34 ? 1896 HOH A O   1 
HETATM 8445 O  O   . HOH G 7 .    ? 38.329 39.860  -26.429 1.00 45.39 ? 1897 HOH A O   1 
HETATM 8446 O  O   . HOH G 7 .    ? 39.934 44.824  -26.359 1.00 42.58 ? 1898 HOH A O   1 
HETATM 8447 O  O   . HOH G 7 .    ? 41.408 44.423  -24.200 1.00 27.20 ? 1899 HOH A O   1 
HETATM 8448 O  O   . HOH G 7 .    ? 42.063 47.018  -24.402 1.00 19.09 ? 1900 HOH A O   1 
HETATM 8449 O  O   . HOH G 7 .    ? 42.657 47.197  -27.113 1.00 36.19 ? 1901 HOH A O   1 
HETATM 8450 O  O   . HOH G 7 .    ? 40.879 47.852  -29.223 1.00 37.16 ? 1902 HOH A O   1 
HETATM 8451 O  O   . HOH G 7 .    ? 39.448 48.371  -32.660 1.00 26.43 ? 1903 HOH A O   1 
HETATM 8452 O  O   . HOH G 7 .    ? 38.628 44.872  -33.550 1.00 25.71 ? 1904 HOH A O   1 
HETATM 8453 O  O   . HOH G 7 .    ? 35.454 44.908  -27.281 1.00 21.61 ? 1905 HOH A O   1 
HETATM 8454 O  O   . HOH G 7 .    ? 37.298 44.877  -25.321 1.00 25.22 ? 1906 HOH A O   1 
HETATM 8455 O  O   . HOH G 7 .    ? 43.374 42.489  -24.733 1.00 43.83 ? 1907 HOH A O   1 
HETATM 8456 O  O   . HOH G 7 .    ? 43.215 40.212  -22.897 1.00 37.82 ? 1908 HOH A O   1 
HETATM 8457 O  O   . HOH G 7 .    ? 48.584 45.679  -23.200 1.00 44.43 ? 1909 HOH A O   1 
HETATM 8458 O  O   . HOH G 7 .    ? 50.269 44.664  -24.673 1.00 39.62 ? 1910 HOH A O   1 
HETATM 8459 O  O   . HOH G 7 .    ? 52.191 45.089  -27.153 1.00 36.61 ? 1911 HOH A O   1 
HETATM 8460 O  O   . HOH G 7 .    ? 53.228 46.817  -24.986 1.00 24.52 ? 1912 HOH A O   1 
HETATM 8461 O  O   . HOH G 7 .    ? 50.058 46.872  -30.406 1.00 55.44 ? 1913 HOH A O   1 
HETATM 8462 O  O   . HOH G 7 .    ? 48.763 49.838  -29.217 1.00 33.05 ? 1914 HOH A O   1 
HETATM 8463 O  O   . HOH G 7 .    ? 47.700 49.569  -31.300 1.00 44.08 ? 1915 HOH A O   1 
HETATM 8464 O  O   . HOH G 7 .    ? 48.124 53.597  -31.226 1.00 47.68 ? 1916 HOH A O   1 
HETATM 8465 O  O   . HOH G 7 .    ? 49.782 54.832  -28.981 1.00 25.89 ? 1917 HOH A O   1 
HETATM 8466 O  O   . HOH G 7 .    ? 50.921 52.492  -28.469 1.00 24.24 ? 1918 HOH A O   1 
HETATM 8467 O  O   . HOH G 7 .    ? 53.242 53.051  -29.771 1.00 34.25 ? 1919 HOH A O   1 
HETATM 8468 O  O   . HOH G 7 .    ? 53.142 54.896  -31.860 1.00 36.48 ? 1920 HOH A O   1 
HETATM 8469 O  O   . HOH G 7 .    ? 52.044 56.102  -30.065 1.00 28.28 ? 1921 HOH A O   1 
HETATM 8470 O  O   . HOH G 7 .    ? 49.921 58.148  -30.840 1.00 46.13 ? 1922 HOH A O   1 
HETATM 8471 O  O   . HOH G 7 .    ? 49.041 59.004  -28.455 1.00 35.13 ? 1923 HOH A O   1 
HETATM 8472 O  O   . HOH G 7 .    ? 48.096 61.543  -28.403 1.00 32.70 ? 1924 HOH A O   1 
HETATM 8473 O  O   . HOH G 7 .    ? 47.016 61.878  -25.646 1.00 26.66 ? 1925 HOH A O   1 
HETATM 8474 O  O   . HOH G 7 .    ? 47.790 59.103  -25.584 1.00 18.45 ? 1926 HOH A O   1 
HETATM 8475 O  O   . HOH G 7 .    ? 46.844 55.418  -25.370 1.00 22.18 ? 1927 HOH A O   1 
HETATM 8476 O  O   . HOH G 7 .    ? 48.630 54.643  -22.637 1.00 23.54 ? 1928 HOH A O   1 
HETATM 8477 O  O   . HOH G 7 .    ? 46.819 53.625  -21.159 1.00 35.02 ? 1929 HOH A O   1 
HETATM 8478 O  O   . HOH G 7 .    ? 45.902 52.505  -19.027 1.00 21.90 ? 1930 HOH A O   1 
HETATM 8479 O  O   . HOH G 7 .    ? 44.952 54.834  -18.262 1.00 31.77 ? 1931 HOH A O   1 
HETATM 8480 O  O   . HOH G 7 .    ? 46.560 57.018  -18.680 1.00 17.33 ? 1932 HOH A O   1 
HETATM 8481 O  O   . HOH G 7 .    ? 45.650 59.613  -18.236 1.00 17.48 ? 1933 HOH A O   1 
HETATM 8482 O  O   . HOH G 7 .    ? 42.977 59.252  -18.876 1.00 24.49 ? 1934 HOH A O   1 
HETATM 8483 O  O   . HOH G 7 .    ? 41.590 58.414  -15.987 1.00 18.05 ? 1935 HOH A O   1 
HETATM 8484 O  O   . HOH G 7 .    ? 39.628 58.604  -17.932 1.00 23.93 ? 1936 HOH A O   1 
HETATM 8485 O  O   . HOH G 7 .    ? 40.189 56.022  -19.015 1.00 26.46 ? 1937 HOH A O   1 
HETATM 8486 O  O   . HOH G 7 .    ? 42.077 54.573  -17.319 1.00 29.14 ? 1938 HOH A O   1 
HETATM 8487 O  O   . HOH G 7 .    ? 40.975 52.029  -16.830 1.00 16.34 ? 1939 HOH A O   1 
HETATM 8488 O  O   . HOH G 7 .    ? 37.596 51.233  -18.470 1.00 23.88 ? 1940 HOH A O   1 
HETATM 8489 O  O   . HOH G 7 .    ? 37.569 51.819  -20.965 1.00 15.78 ? 1941 HOH A O   1 
HETATM 8490 O  O   . HOH G 7 .    ? 39.590 53.644  -20.637 1.00 20.15 ? 1942 HOH A O   1 
HETATM 8491 O  O   . HOH G 7 .    ? 35.049 50.282  -17.469 1.00 18.42 ? 1943 HOH A O   1 
HETATM 8492 O  O   . HOH G 7 .    ? 31.245 49.627  -23.893 1.00 17.23 ? 1944 HOH A O   1 
HETATM 8493 O  O   . HOH G 7 .    ? 28.629 49.452  -24.272 1.00 22.37 ? 1945 HOH A O   1 
HETATM 8494 O  O   . HOH G 7 .    ? 26.811 47.310  -23.900 1.00 36.35 ? 1946 HOH A O   1 
HETATM 8495 O  O   . HOH G 7 .    ? 27.499 48.157  -21.514 1.00 20.49 ? 1947 HOH A O   1 
HETATM 8496 O  O   . HOH G 7 .    ? 24.997 46.686  -20.568 1.00 26.35 ? 1948 HOH A O   1 
HETATM 8497 O  O   . HOH G 7 .    ? 23.945 48.128  -24.195 1.00 39.40 ? 1949 HOH A O   1 
HETATM 8498 O  O   . HOH G 7 .    ? 24.662 50.812  -23.930 1.00 19.35 ? 1950 HOH A O   1 
HETATM 8499 O  O   . HOH G 7 .    ? 22.795 52.793  -24.253 1.00 17.25 ? 1951 HOH A O   1 
HETATM 8500 O  O   . HOH G 7 .    ? 23.710 55.232  -23.281 1.00 14.57 ? 1952 HOH A O   1 
HETATM 8501 O  O   . HOH G 7 .    ? 19.958 52.416  -24.065 1.00 21.06 ? 1953 HOH A O   1 
HETATM 8502 O  O   . HOH G 7 .    ? 19.164 50.057  -23.287 1.00 34.10 ? 1954 HOH A O   1 
HETATM 8503 O  O   . HOH G 7 .    ? 16.467 52.606  -22.420 1.00 34.32 ? 1955 HOH A O   1 
HETATM 8504 O  O   . HOH G 7 .    ? 16.871 50.561  -19.135 1.00 26.09 ? 1956 HOH A O   1 
HETATM 8505 O  O   . HOH G 7 .    ? 18.036 48.356  -19.703 1.00 41.45 ? 1957 HOH A O   1 
HETATM 8506 O  O   . HOH G 7 .    ? 21.450 46.417  -17.381 1.00 31.79 ? 1958 HOH A O   1 
HETATM 8507 O  O   . HOH G 7 .    ? 23.594 45.706  -15.716 1.00 24.10 ? 1959 HOH A O   1 
HETATM 8508 O  O   . HOH G 7 .    ? 22.488 45.074  -13.335 1.00 21.18 ? 1960 HOH A O   1 
HETATM 8509 O  O   . HOH G 7 .    ? 22.000 42.358  -13.129 1.00 26.82 ? 1961 HOH A O   1 
HETATM 8510 O  O   . HOH G 7 .    ? 24.079 41.661  -14.447 1.00 27.00 ? 1962 HOH A O   1 
HETATM 8511 O  O   . HOH G 7 .    ? 26.618 41.331  -13.081 1.00 16.93 ? 1963 HOH A O   1 
HETATM 8512 O  O   . HOH G 7 .    ? 28.783 42.492  -11.828 1.00 16.32 ? 1964 HOH A O   1 
HETATM 8513 O  O   . HOH G 7 .    ? 31.702 46.768  -7.956  1.00 11.71 ? 1965 HOH A O   1 
HETATM 8514 O  O   . HOH G 7 .    ? 33.391 47.886  -10.033 1.00 12.27 ? 1966 HOH A O   1 
HETATM 8515 O  O   . HOH G 7 .    ? 36.669 44.667  -5.327  1.00 14.54 ? 1967 HOH A O   1 
HETATM 8516 O  O   . HOH G 7 .    ? 41.430 44.504  -6.770  1.00 18.73 ? 1968 HOH A O   1 
HETATM 8517 O  O   . HOH G 7 .    ? 39.428 37.965  -10.606 1.00 35.05 ? 1969 HOH A O   1 
HETATM 8518 O  O   . HOH G 7 .    ? 41.361 36.895  -12.477 1.00 45.11 ? 1970 HOH A O   1 
HETATM 8519 O  O   . HOH G 7 .    ? 36.789 34.889  -15.799 1.00 36.24 ? 1971 HOH A O   1 
HETATM 8520 O  O   . HOH G 7 .    ? 36.051 35.932  -18.123 1.00 41.02 ? 1972 HOH A O   1 
HETATM 8521 O  O   . HOH G 7 .    ? 35.763 38.762  -15.984 1.00 29.41 ? 1973 HOH A O   1 
HETATM 8522 O  O   . HOH G 7 .    ? 33.004 40.730  -17.818 1.00 29.19 ? 1974 HOH A O   1 
HETATM 8523 O  O   . HOH G 7 .    ? 25.567 35.888  -15.261 1.00 36.05 ? 1975 HOH A O   1 
HETATM 8524 O  O   . HOH G 7 .    ? 23.723 37.345  -17.496 1.00 40.06 ? 1976 HOH A O   1 
HETATM 8525 O  O   . HOH G 7 .    ? 22.914 39.030  -15.312 1.00 34.00 ? 1977 HOH A O   1 
HETATM 8526 O  O   . HOH G 7 .    ? 20.148 39.046  -12.112 1.00 45.30 ? 1978 HOH A O   1 
HETATM 8527 O  O   . HOH G 7 .    ? 19.561 41.766  -14.339 1.00 46.25 ? 1979 HOH A O   1 
HETATM 8528 O  O   . HOH G 7 .    ? 17.450 45.358  -13.863 1.00 36.69 ? 1980 HOH A O   1 
HETATM 8529 O  O   . HOH G 7 .    ? 19.872 46.476  -14.139 1.00 21.23 ? 1981 HOH A O   1 
HETATM 8530 O  O   . HOH G 7 .    ? 18.604 50.803  -12.330 1.00 16.34 ? 1982 HOH A O   1 
HETATM 8531 O  O   . HOH G 7 .    ? 19.603 53.228  -11.704 1.00 17.21 ? 1983 HOH A O   1 
HETATM 8532 O  O   . HOH G 7 .    ? 22.270 54.142  -11.893 1.00 15.00 ? 1984 HOH A O   1 
HETATM 8533 O  O   . HOH G 7 .    ? 24.689 52.639  -11.648 1.00 14.14 ? 1985 HOH A O   1 
HETATM 8534 O  O   . HOH G 7 .    ? 25.505 50.960  -9.335  1.00 17.39 ? 1986 HOH A O   1 
HETATM 8535 O  O   . HOH G 7 .    ? 22.861 51.554  -8.541  1.00 20.88 ? 1987 HOH A O   1 
HETATM 8536 O  O   . HOH G 7 .    ? 24.080 52.904  -6.191  1.00 26.22 ? 1988 HOH A O   1 
HETATM 8537 O  O   . HOH G 7 .    ? 23.289 53.715  -3.544  1.00 17.62 ? 1989 HOH A O   1 
HETATM 8538 O  O   . HOH G 7 .    ? 24.314 55.414  -1.686  1.00 15.98 ? 1990 HOH A O   1 
HETATM 8539 O  O   . HOH G 7 .    ? 20.593 57.188  -5.142  1.00 14.71 ? 1991 HOH A O   1 
HETATM 8540 O  O   . HOH G 7 .    ? 21.512 57.670  -7.660  1.00 14.80 ? 1992 HOH A O   1 
HETATM 8541 O  O   . HOH G 7 .    ? 19.749 57.078  -11.602 1.00 18.84 ? 1993 HOH A O   1 
HETATM 8542 O  O   . HOH G 7 .    ? 14.618 61.680  -14.383 1.00 25.32 ? 1994 HOH A O   1 
HETATM 8543 O  O   . HOH G 7 .    ? 14.223 62.612  -12.023 1.00 23.05 ? 1995 HOH A O   1 
HETATM 8544 O  O   . HOH G 7 .    ? 12.258 64.311  -12.342 1.00 30.84 ? 1996 HOH A O   1 
HETATM 8545 O  O   . HOH G 7 .    ? 10.657 62.283  -12.148 1.00 37.94 ? 1997 HOH A O   1 
HETATM 8546 O  O   . HOH G 7 .    ? 10.204 62.834  -14.588 1.00 36.98 ? 1998 HOH A O   1 
HETATM 8547 O  O   . HOH G 7 .    ? 11.744 63.357  -16.708 1.00 27.04 ? 1999 HOH A O   1 
HETATM 8548 O  O   . HOH G 7 .    ? 14.321 63.658  -16.231 1.00 19.98 ? 2000 HOH A O   1 
HETATM 8549 O  O   . HOH G 7 .    ? 13.315 62.045  -19.757 1.00 23.89 ? 2001 HOH A O   1 
HETATM 8550 O  O   . HOH G 7 .    ? 11.340 61.053  -18.297 1.00 24.20 ? 2002 HOH A O   1 
HETATM 8551 O  O   . HOH G 7 .    ? 9.730  60.054  -20.243 1.00 32.03 ? 2003 HOH A O   1 
HETATM 8552 O  O   . HOH G 7 .    ? 10.548 57.742  -20.859 1.00 41.32 ? 2004 HOH A O   1 
HETATM 8553 O  O   . HOH G 7 .    ? 13.845 60.472  -22.388 1.00 21.63 ? 2005 HOH A O   1 
HETATM 8554 O  O   . HOH G 7 .    ? 12.879 61.583  -24.925 1.00 41.41 ? 2006 HOH A O   1 
HETATM 8555 O  O   . HOH G 7 .    ? 14.990 63.308  -25.749 1.00 29.45 ? 2007 HOH A O   1 
HETATM 8556 O  O   . HOH G 7 .    ? 18.496 64.656  -26.906 1.00 24.29 ? 2008 HOH A O   1 
HETATM 8557 O  O   . HOH G 7 .    ? 16.966 66.907  -25.747 1.00 35.77 ? 2009 HOH A O   1 
HETATM 8558 O  O   . HOH G 7 .    ? 15.322 68.146  -27.299 1.00 38.27 ? 2010 HOH A O   1 
HETATM 8559 O  O   . HOH G 7 .    ? 17.178 69.765  -23.269 1.00 22.50 ? 2011 HOH A O   1 
HETATM 8560 O  O   . HOH G 7 .    ? 14.599 70.177  -22.925 1.00 29.87 ? 2012 HOH A O   1 
HETATM 8561 O  O   . HOH G 7 .    ? 14.988 73.354  -21.769 1.00 38.47 ? 2013 HOH A O   1 
HETATM 8562 O  O   . HOH G 7 .    ? 12.782 74.006  -23.021 1.00 41.61 ? 2014 HOH A O   1 
HETATM 8563 O  O   . HOH G 7 .    ? 16.235 74.761  -23.945 1.00 45.68 ? 2015 HOH A O   1 
HETATM 8564 O  O   . HOH G 7 .    ? 19.356 78.566  -25.464 1.00 34.25 ? 2016 HOH A O   1 
HETATM 8565 O  O   . HOH G 7 .    ? 20.739 78.085  -27.381 1.00 41.74 ? 2017 HOH A O   1 
HETATM 8566 O  O   . HOH G 7 .    ? 22.826 77.043  -27.257 1.00 31.31 ? 2018 HOH A O   1 
HETATM 8567 O  O   . HOH G 7 .    ? 23.199 78.090  -24.731 1.00 23.01 ? 2019 HOH A O   1 
HETATM 8568 O  O   . HOH G 7 .    ? 20.986 79.161  -23.417 1.00 27.64 ? 2020 HOH A O   1 
HETATM 8569 O  O   . HOH G 7 .    ? 19.074 82.882  -25.823 1.00 33.24 ? 2021 HOH A O   1 
HETATM 8570 O  O   . HOH G 7 .    ? 21.495 85.663  -30.898 1.00 35.77 ? 2022 HOH A O   1 
HETATM 8571 O  O   . HOH G 7 .    ? 23.245 86.709  -32.595 1.00 33.64 ? 2023 HOH A O   1 
HETATM 8572 O  O   . HOH G 7 .    ? 25.603 85.844  -31.900 1.00 22.43 ? 2024 HOH A O   1 
HETATM 8573 O  O   . HOH G 7 .    ? 27.051 89.396  -31.667 1.00 41.13 ? 2025 HOH A O   1 
HETATM 8574 O  O   . HOH G 7 .    ? 25.683 91.247  -32.842 1.00 40.87 ? 2026 HOH A O   1 
HETATM 8575 O  O   . HOH G 7 .    ? 28.120 93.240  -29.616 1.00 40.51 ? 2027 HOH A O   1 
HETATM 8576 O  O   . HOH G 7 .    ? 26.656 91.458  -27.456 1.00 40.26 ? 2028 HOH A O   1 
HETATM 8577 O  O   . HOH G 7 .    ? 28.116 90.576  -25.353 1.00 24.18 ? 2029 HOH A O   1 
HETATM 8578 O  O   . HOH G 7 .    ? 29.518 88.393  -26.237 1.00 18.21 ? 2030 HOH A O   1 
HETATM 8579 O  O   . HOH G 7 .    ? 26.980 87.582  -23.553 1.00 29.47 ? 2031 HOH A O   1 
HETATM 8580 O  O   . HOH G 7 .    ? 25.102 88.508  -25.198 1.00 38.57 ? 2032 HOH A O   1 
HETATM 8581 O  O   . HOH G 7 .    ? 23.623 90.565  -26.161 1.00 45.51 ? 2033 HOH A O   1 
HETATM 8582 O  O   . HOH G 7 .    ? 22.843 88.415  -18.657 1.00 44.40 ? 2034 HOH A O   1 
HETATM 8583 O  O   . HOH G 7 .    ? 21.383 85.904  -19.173 1.00 38.05 ? 2035 HOH A O   1 
HETATM 8584 O  O   . HOH G 7 .    ? 19.762 84.015  -18.351 1.00 34.44 ? 2036 HOH A O   1 
HETATM 8585 O  O   . HOH G 7 .    ? 22.864 84.806  -16.968 1.00 42.28 ? 2037 HOH A O   1 
HETATM 8586 O  O   . HOH G 7 .    ? 24.794 82.805  -16.839 1.00 25.94 ? 2038 HOH A O   1 
HETATM 8587 O  O   . HOH G 7 .    ? 27.723 85.964  -14.534 1.00 31.05 ? 2039 HOH A O   1 
HETATM 8588 O  O   . HOH G 7 .    ? 30.312 86.809  -15.100 1.00 28.37 ? 2040 HOH A O   1 
HETATM 8589 O  O   . HOH G 7 .    ? 29.707 86.982  -17.795 1.00 35.29 ? 2041 HOH A O   1 
HETATM 8590 O  O   . HOH G 7 .    ? 31.661 85.493  -19.888 1.00 27.44 ? 2042 HOH A O   1 
HETATM 8591 O  O   . HOH G 7 .    ? 33.327 84.035  -18.272 1.00 21.53 ? 2043 HOH A O   1 
HETATM 8592 O  O   . HOH G 7 .    ? 35.256 85.894  -17.916 1.00 30.87 ? 2044 HOH A O   1 
HETATM 8593 O  O   . HOH G 7 .    ? 34.755 87.868  -19.409 1.00 51.44 ? 2045 HOH A O   1 
HETATM 8594 O  O   . HOH G 7 .    ? 36.782 86.349  -15.711 1.00 41.16 ? 2046 HOH A O   1 
HETATM 8595 O  O   . HOH G 7 .    ? 40.783 85.008  -12.191 1.00 35.19 ? 2047 HOH A O   1 
HETATM 8596 O  O   . HOH G 7 .    ? 40.291 82.491  -10.674 1.00 22.68 ? 2048 HOH A O   1 
HETATM 8597 O  O   . HOH G 7 .    ? 42.964 82.064  -9.943  1.00 30.39 ? 2049 HOH A O   1 
HETATM 8598 O  O   . HOH G 7 .    ? 45.646 78.957  -7.865  1.00 31.02 ? 2050 HOH A O   1 
HETATM 8599 O  O   . HOH G 7 .    ? 47.564 80.938  -9.199  1.00 46.51 ? 2051 HOH A O   1 
HETATM 8600 O  O   . HOH G 7 .    ? 48.342 77.690  -9.750  1.00 31.15 ? 2052 HOH A O   1 
HETATM 8601 O  O   . HOH G 7 .    ? 50.170 79.391  -11.151 1.00 51.41 ? 2053 HOH A O   1 
HETATM 8602 O  O   . HOH G 7 .    ? 52.866 77.145  -11.078 1.00 42.74 ? 2054 HOH A O   1 
HETATM 8603 O  O   . HOH G 7 .    ? 52.727 75.955  -13.778 1.00 47.30 ? 2055 HOH A O   1 
HETATM 8604 O  O   . HOH G 7 .    ? 50.448 79.001  -15.790 1.00 35.84 ? 2056 HOH A O   1 
HETATM 8605 O  O   . HOH G 7 .    ? 52.498 78.740  -17.475 1.00 26.44 ? 2057 HOH A O   1 
HETATM 8606 O  O   . HOH G 7 .    ? 55.006 80.219  -19.302 1.00 28.09 ? 2058 HOH A O   1 
HETATM 8607 O  O   . HOH G 7 .    ? 57.195 80.015  -17.836 1.00 44.17 ? 2059 HOH A O   1 
HETATM 8608 O  O   . HOH G 7 .    ? 56.121 78.607  -14.565 1.00 37.52 ? 2060 HOH A O   1 
HETATM 8609 O  O   . HOH G 7 .    ? 61.215 77.171  -12.865 1.00 27.17 ? 2061 HOH A O   1 
HETATM 8610 O  O   . HOH G 7 .    ? 61.778 76.043  -10.491 1.00 23.26 ? 2062 HOH A O   1 
HETATM 8611 O  O   . HOH G 7 .    ? 59.491 76.227  -8.938  1.00 21.54 ? 2063 HOH A O   1 
HETATM 8612 O  O   . HOH G 7 .    ? 59.815 76.438  -4.176  1.00 40.43 ? 2064 HOH A O   1 
HETATM 8613 O  O   . HOH G 7 .    ? 57.190 75.117  -2.872  1.00 37.61 ? 2065 HOH A O   1 
HETATM 8614 O  O   . HOH G 7 .    ? 56.930 75.712  0.076   1.00 40.20 ? 2066 HOH A O   1 
HETATM 8615 O  O   . HOH G 7 .    ? 58.977 77.517  0.627   1.00 42.75 ? 2067 HOH A O   1 
HETATM 8616 O  O   . HOH G 7 .    ? 64.431 77.008  0.288   1.00 40.44 ? 2068 HOH A O   1 
HETATM 8617 O  O   . HOH G 7 .    ? 64.713 78.597  -1.484  1.00 35.54 ? 2069 HOH A O   1 
HETATM 8618 O  O   . HOH G 7 .    ? 65.331 78.407  -5.674  1.00 34.50 ? 2070 HOH A O   1 
HETATM 8619 O  O   . HOH G 7 .    ? 65.036 79.636  -8.796  1.00 41.93 ? 2071 HOH A O   1 
HETATM 8620 O  O   . HOH G 7 .    ? 67.034 81.223  -11.341 1.00 40.72 ? 2072 HOH A O   1 
HETATM 8621 O  O   . HOH G 7 .    ? 66.455 81.526  -14.252 1.00 36.89 ? 2073 HOH A O   1 
HETATM 8622 O  O   . HOH G 7 .    ? 63.679 81.893  -14.287 1.00 43.57 ? 2074 HOH A O   1 
HETATM 8623 O  O   . HOH G 7 .    ? 62.684 82.334  -17.023 1.00 41.53 ? 2075 HOH A O   1 
HETATM 8624 O  O   . HOH G 7 .    ? 61.995 80.382  -18.828 1.00 28.61 ? 2076 HOH A O   1 
HETATM 8625 O  O   . HOH G 7 .    ? 62.386 83.059  -21.558 1.00 43.81 ? 2077 HOH A O   1 
HETATM 8626 O  O   . HOH G 7 .    ? 62.040 85.258  -22.773 1.00 33.34 ? 2078 HOH A O   1 
HETATM 8627 O  O   . HOH G 7 .    ? 64.893 87.361  -24.167 1.00 34.92 ? 2079 HOH A O   1 
HETATM 8628 O  O   . HOH G 7 .    ? 67.608 87.658  -23.317 1.00 27.67 ? 2080 HOH A O   1 
HETATM 8629 O  O   . HOH G 7 .    ? 66.631 84.185  -22.294 1.00 37.24 ? 2081 HOH A O   1 
HETATM 8630 O  O   . HOH G 7 .    ? 67.733 81.321  -25.645 1.00 17.06 ? 2082 HOH A O   1 
HETATM 8631 O  O   . HOH G 7 .    ? 67.717 78.597  -25.262 1.00 17.84 ? 2083 HOH A O   1 
HETATM 8632 O  O   . HOH G 7 .    ? 70.387 77.731  -26.053 1.00 30.80 ? 2084 HOH A O   1 
HETATM 8633 O  O   . HOH G 7 .    ? 72.362 75.601  -26.932 1.00 43.54 ? 2085 HOH A O   1 
HETATM 8634 O  O   . HOH G 7 .    ? 71.719 73.486  -29.084 1.00 32.15 ? 2086 HOH A O   1 
HETATM 8635 O  O   . HOH G 7 .    ? 70.801 72.122  -34.121 1.00 41.31 ? 2087 HOH A O   1 
HETATM 8636 O  O   . HOH G 7 .    ? 67.842 74.710  -35.072 1.00 39.39 ? 2088 HOH A O   1 
HETATM 8637 O  O   . HOH G 7 .    ? 69.171 76.720  -34.157 1.00 28.71 ? 2089 HOH A O   1 
HETATM 8638 O  O   . HOH G 7 .    ? 71.476 76.346  -35.595 1.00 41.52 ? 2090 HOH A O   1 
HETATM 8639 O  O   . HOH G 7 .    ? 68.311 79.277  -34.771 1.00 29.19 ? 2091 HOH A O   1 
HETATM 8640 O  O   . HOH G 7 .    ? 69.802 81.603  -33.960 1.00 39.77 ? 2092 HOH A O   1 
HETATM 8641 O  O   . HOH G 7 .    ? 69.298 83.529  -35.909 1.00 35.01 ? 2093 HOH A O   1 
HETATM 8642 O  O   . HOH G 7 .    ? 67.391 85.285  -36.112 1.00 39.68 ? 2094 HOH A O   1 
HETATM 8643 O  O   . HOH G 7 .    ? 67.804 87.875  -35.146 1.00 39.58 ? 2095 HOH A O   1 
HETATM 8644 O  O   . HOH G 7 .    ? 65.354 87.259  -41.206 1.00 39.51 ? 2096 HOH A O   1 
HETATM 8645 O  O   . HOH G 7 .    ? 61.909 82.690  -38.315 1.00 30.90 ? 2097 HOH A O   1 
HETATM 8646 O  O   . HOH G 7 .    ? 63.853 78.148  -37.851 1.00 35.99 ? 2098 HOH A O   1 
HETATM 8647 O  O   . HOH G 7 .    ? 64.235 77.550  -35.242 1.00 18.75 ? 2099 HOH A O   1 
HETATM 8648 O  O   . HOH G 7 .    ? 67.684 76.961  -38.737 1.00 40.86 ? 2100 HOH A O   1 
HETATM 8649 O  O   . HOH G 7 .    ? 63.956 76.554  -40.510 1.00 36.74 ? 2101 HOH A O   1 
HETATM 8650 O  O   . HOH G 7 .    ? 61.311 76.343  -39.708 1.00 23.44 ? 2102 HOH A O   1 
HETATM 8651 O  O   . HOH G 7 .    ? 60.662 78.477  -41.502 1.00 30.05 ? 2103 HOH A O   1 
HETATM 8652 O  O   . HOH G 7 .    ? 62.141 81.114  -44.269 1.00 38.58 ? 2104 HOH A O   1 
HETATM 8653 O  O   . HOH G 7 .    ? 59.269 86.575  -45.685 1.00 45.40 ? 2105 HOH A O   1 
HETATM 8654 O  O   . HOH G 7 .    ? 56.605 89.574  -43.529 1.00 37.07 ? 2106 HOH A O   1 
HETATM 8655 O  O   . HOH G 7 .    ? 60.271 92.905  -37.997 1.00 38.75 ? 2107 HOH A O   1 
HETATM 8656 O  O   . HOH G 7 .    ? 61.289 90.459  -37.083 1.00 39.82 ? 2108 HOH A O   1 
HETATM 8657 O  O   . HOH G 7 .    ? 59.500 90.749  -35.358 1.00 27.79 ? 2109 HOH A O   1 
HETATM 8658 O  O   . HOH G 7 .    ? 56.329 92.450  -29.670 1.00 34.08 ? 2110 HOH A O   1 
HETATM 8659 O  O   . HOH G 7 .    ? 58.721 92.740  -27.011 1.00 46.55 ? 2111 HOH A O   1 
HETATM 8660 O  O   . HOH G 7 .    ? 57.856 92.976  -24.870 1.00 36.83 ? 2112 HOH A O   1 
HETATM 8661 O  O   . HOH G 7 .    ? 56.224 90.637  -25.824 1.00 30.20 ? 2113 HOH A O   1 
HETATM 8662 O  O   . HOH G 7 .    ? 54.851 89.893  -23.561 1.00 30.28 ? 2114 HOH A O   1 
HETATM 8663 O  O   . HOH G 7 .    ? 52.578 91.651  -23.527 1.00 35.89 ? 2115 HOH A O   1 
HETATM 8664 O  O   . HOH G 7 .    ? 50.732 90.389  -21.630 1.00 46.94 ? 2116 HOH A O   1 
HETATM 8665 O  O   . HOH G 7 .    ? 49.245 91.495  -24.517 1.00 38.19 ? 2117 HOH A O   1 
HETATM 8666 O  O   . HOH G 7 .    ? 46.844 89.155  -23.618 1.00 36.44 ? 2118 HOH A O   1 
HETATM 8667 O  O   . HOH G 7 .    ? 44.942 89.637  -25.518 1.00 26.17 ? 2119 HOH A O   1 
HETATM 8668 O  O   . HOH G 7 .    ? 44.906 92.295  -25.427 1.00 35.15 ? 2120 HOH A O   1 
HETATM 8669 O  O   . HOH G 7 .    ? 42.733 94.008  -30.288 1.00 42.12 ? 2121 HOH A O   1 
HETATM 8670 O  O   . HOH G 7 .    ? 40.033 99.382  -32.051 1.00 37.83 ? 2122 HOH A O   1 
HETATM 8671 O  O   . HOH G 7 .    ? 42.988 97.736  -37.098 1.00 37.48 ? 2123 HOH A O   1 
HETATM 8672 O  O   . HOH G 7 .    ? 40.705 95.835  -37.396 1.00 29.34 ? 2124 HOH A O   1 
HETATM 8673 O  O   . HOH G 7 .    ? 41.378 94.410  -39.433 1.00 34.41 ? 2125 HOH A O   1 
HETATM 8674 O  O   . HOH G 7 .    ? 43.454 93.408  -37.674 1.00 24.92 ? 2126 HOH A O   1 
HETATM 8675 O  O   . HOH G 7 .    ? 46.989 95.021  -37.124 1.00 45.12 ? 2127 HOH A O   1 
HETATM 8676 O  O   . HOH G 7 .    ? 48.638 97.391  -33.934 1.00 41.24 ? 2128 HOH A O   1 
HETATM 8677 O  O   . HOH G 7 .    ? 47.213 99.345  -32.746 1.00 41.53 ? 2129 HOH A O   1 
HETATM 8678 O  O   . HOH G 7 .    ? 48.239 88.815  -30.782 1.00 18.43 ? 2130 HOH A O   1 
HETATM 8679 O  O   . HOH G 7 .    ? 44.339 83.373  -28.048 1.00 33.82 ? 2131 HOH A O   1 
HETATM 8680 O  O   . HOH G 7 .    ? 42.152 82.122  -29.223 1.00 37.92 ? 2132 HOH A O   1 
HETATM 8681 O  O   . HOH G 7 .    ? 40.866 82.490  -31.359 1.00 33.13 ? 2133 HOH A O   1 
HETATM 8682 O  O   . HOH G 7 .    ? 38.110 81.344  -31.329 1.00 17.64 ? 2134 HOH A O   1 
HETATM 8683 O  O   . HOH G 7 .    ? 39.144 82.971  -27.476 1.00 28.60 ? 2135 HOH A O   1 
HETATM 8684 O  O   . HOH G 7 .    ? 43.456 80.607  -25.531 1.00 36.24 ? 2136 HOH A O   1 
HETATM 8685 O  O   . HOH G 7 .    ? 45.876 81.531  -25.706 1.00 50.68 ? 2137 HOH A O   1 
HETATM 8686 O  O   . HOH G 7 .    ? 46.772 80.269  -22.381 1.00 45.96 ? 2138 HOH A O   1 
HETATM 8687 O  O   . HOH G 7 .    ? 47.008 82.786  -20.990 1.00 44.70 ? 2139 HOH A O   1 
HETATM 8688 O  O   . HOH G 7 .    ? 48.681 84.098  -19.675 1.00 45.91 ? 2140 HOH A O   1 
HETATM 8689 O  O   . HOH G 7 .    ? 47.451 79.305  -18.281 1.00 30.24 ? 2141 HOH A O   1 
HETATM 8690 O  O   . HOH G 7 .    ? 43.872 79.288  -21.565 1.00 40.57 ? 2142 HOH A O   1 
HETATM 8691 O  O   . HOH G 7 .    ? 41.809 78.994  -23.429 1.00 31.63 ? 2143 HOH A O   1 
HETATM 8692 O  O   . HOH G 7 .    ? 39.561 81.366  -22.072 1.00 41.94 ? 2144 HOH A O   1 
HETATM 8693 O  O   . HOH G 7 .    ? 39.948 85.684  -21.872 1.00 28.23 ? 2145 HOH A O   1 
HETATM 8694 O  O   . HOH G 7 .    ? 42.635 78.583  -29.084 1.00 44.65 ? 2146 HOH A O   1 
HETATM 8695 O  O   . HOH G 7 .    ? 42.543 79.459  -31.782 1.00 35.18 ? 2147 HOH A O   1 
HETATM 8696 O  O   . HOH G 7 .    ? 44.592 78.863  -33.256 1.00 26.46 ? 2148 HOH A O   1 
HETATM 8697 O  O   . HOH G 7 .    ? 44.702 82.190  -30.604 1.00 28.23 ? 2149 HOH A O   1 
HETATM 8698 O  O   . HOH G 7 .    ? 46.328 76.743  -26.012 1.00 33.35 ? 2150 HOH A O   1 
HETATM 8699 O  O   . HOH G 7 .    ? 50.480 73.370  -25.485 1.00 25.96 ? 2151 HOH A O   1 
HETATM 8700 O  O   . HOH G 7 .    ? 51.056 70.589  -23.642 1.00 25.60 ? 2152 HOH A O   1 
HETATM 8701 O  O   . HOH G 7 .    ? 51.217 71.115  -20.314 1.00 27.51 ? 2153 HOH A O   1 
HETATM 8702 O  O   . HOH G 7 .    ? 53.574 72.264  -19.190 1.00 18.52 ? 2154 HOH A O   1 
HETATM 8703 O  O   . HOH G 7 .    ? 49.842 70.431  -17.691 1.00 34.53 ? 2155 HOH A O   1 
HETATM 8704 O  O   . HOH G 7 .    ? 46.896 72.065  -17.418 1.00 32.58 ? 2156 HOH A O   1 
HETATM 8705 O  O   . HOH G 7 .    ? 47.472 71.669  -19.909 1.00 38.09 ? 2157 HOH A O   1 
HETATM 8706 O  O   . HOH G 7 .    ? 45.605 69.807  -18.298 1.00 41.43 ? 2158 HOH A O   1 
HETATM 8707 O  O   . HOH G 7 .    ? 46.428 67.344  -15.559 1.00 20.72 ? 2159 HOH A O   1 
HETATM 8708 O  O   . HOH G 7 .    ? 39.221 64.477  -14.746 1.00 13.89 ? 2160 HOH A O   1 
HETATM 8709 O  O   . HOH G 7 .    ? 39.133 62.586  -19.048 1.00 12.09 ? 2161 HOH A O   1 
HETATM 8710 O  O   . HOH G 7 .    ? 44.517 58.444  -15.886 1.00 17.59 ? 2162 HOH A O   1 
HETATM 8711 O  O   . HOH G 7 .    ? 44.423 55.798  -15.284 1.00 21.69 ? 2163 HOH A O   1 
HETATM 8712 O  O   . HOH G 7 .    ? 47.226 55.521  -15.323 1.00 18.78 ? 2164 HOH A O   1 
HETATM 8713 O  O   . HOH G 7 .    ? 49.999 59.250  -11.475 1.00 14.66 ? 2165 HOH A O   1 
HETATM 8714 O  O   . HOH G 7 .    ? 50.809 59.627  -8.895  1.00 15.65 ? 2166 HOH A O   1 
HETATM 8715 O  O   . HOH G 7 .    ? 49.534 62.039  -8.584  1.00 14.10 ? 2167 HOH A O   1 
HETATM 8716 O  O   . HOH G 7 .    ? 53.592 59.617  -9.295  1.00 14.71 ? 2168 HOH A O   1 
HETATM 8717 O  O   . HOH G 7 .    ? 55.558 59.058  -11.415 1.00 14.12 ? 2169 HOH A O   1 
HETATM 8718 O  O   . HOH G 7 .    ? 60.996 59.411  -8.181  1.00 12.69 ? 2170 HOH A O   1 
HETATM 8719 O  O   . HOH G 7 .    ? 59.496 60.343  -6.151  1.00 17.53 ? 2171 HOH A O   1 
HETATM 8720 O  O   . HOH G 7 .    ? 60.629 60.585  -3.561  1.00 16.62 ? 2172 HOH A O   1 
HETATM 8721 O  O   . HOH G 7 .    ? 60.737 58.032  -2.739  1.00 16.59 ? 2173 HOH A O   1 
HETATM 8722 O  O   . HOH G 7 .    ? 63.122 58.423  -1.383  1.00 20.27 ? 2174 HOH A O   1 
HETATM 8723 O  O   . HOH G 7 .    ? 64.860 59.071  -3.521  1.00 18.21 ? 2175 HOH A O   1 
HETATM 8724 O  O   . HOH G 7 .    ? 63.059 60.872  -4.810  1.00 18.18 ? 2176 HOH A O   1 
HETATM 8725 O  O   . HOH G 7 .    ? 63.093 61.040  -7.528  1.00 14.21 ? 2177 HOH A O   1 
HETATM 8726 O  O   . HOH G 7 .    ? 65.623 60.033  -7.608  1.00 16.05 ? 2178 HOH A O   1 
HETATM 8727 O  O   . HOH G 7 .    ? 67.433 60.430  -5.522  1.00 16.51 ? 2179 HOH A O   1 
HETATM 8728 O  O   . HOH G 7 .    ? 68.752 57.987  -4.998  1.00 17.85 ? 2180 HOH A O   1 
HETATM 8729 O  O   . HOH G 7 .    ? 69.083 61.162  -2.325  1.00 19.69 ? 2181 HOH A O   1 
HETATM 8730 O  O   . HOH G 7 .    ? 70.297 61.747  0.094   1.00 43.26 ? 2182 HOH A O   1 
HETATM 8731 O  O   . HOH G 7 .    ? 71.337 59.351  0.788   1.00 39.48 ? 2183 HOH A O   1 
HETATM 8732 O  O   . HOH G 7 .    ? 73.555 62.843  -0.605  1.00 39.63 ? 2184 HOH A O   1 
HETATM 8733 O  O   . HOH G 7 .    ? 69.195 63.551  2.033   1.00 39.50 ? 2185 HOH A O   1 
HETATM 8734 O  O   . HOH G 7 .    ? 68.041 66.651  1.105   1.00 42.18 ? 2186 HOH A O   1 
HETATM 8735 O  O   . HOH G 7 .    ? 65.860 65.918  -0.328  1.00 29.09 ? 2187 HOH A O   1 
HETATM 8736 O  O   . HOH G 7 .    ? 67.940 65.299  -3.353  1.00 19.05 ? 2188 HOH A O   1 
HETATM 8737 O  O   . HOH G 7 .    ? 64.077 70.417  -5.251  1.00 19.85 ? 2189 HOH A O   1 
HETATM 8738 O  O   . HOH G 7 .    ? 66.395 71.221  -6.763  1.00 24.06 ? 2190 HOH A O   1 
HETATM 8739 O  O   . HOH G 7 .    ? 66.675 74.336  -4.414  1.00 32.64 ? 2191 HOH A O   1 
HETATM 8740 O  O   . HOH G 7 .    ? 73.512 73.891  -5.715  1.00 29.88 ? 2192 HOH A O   1 
HETATM 8741 O  O   . HOH G 7 .    ? 78.261 71.434  -10.084 1.00 35.47 ? 2193 HOH A O   1 
HETATM 8742 O  O   . HOH G 7 .    ? 78.652 68.815  -11.825 1.00 27.61 ? 2194 HOH A O   1 
HETATM 8743 O  O   . HOH G 7 .    ? 81.204 68.221  -11.343 1.00 25.50 ? 2195 HOH A O   1 
HETATM 8744 O  O   . HOH G 7 .    ? 81.640 66.782  -13.599 1.00 24.93 ? 2196 HOH A O   1 
HETATM 8745 O  O   . HOH G 7 .    ? 83.608 66.074  -15.334 1.00 24.27 ? 2197 HOH A O   1 
HETATM 8746 O  O   . HOH G 7 .    ? 84.285 68.012  -17.210 1.00 21.59 ? 2198 HOH A O   1 
HETATM 8747 O  O   . HOH G 7 .    ? 83.646 69.809  -20.146 1.00 31.66 ? 2199 HOH A O   1 
HETATM 8748 O  O   . HOH G 7 .    ? 83.567 67.174  -22.706 1.00 28.31 ? 2200 HOH A O   1 
HETATM 8749 O  O   . HOH G 7 .    ? 80.328 63.775  -21.113 1.00 28.76 ? 2201 HOH A O   1 
HETATM 8750 O  O   . HOH G 7 .    ? 78.994 62.602  -23.320 1.00 48.94 ? 2202 HOH A O   1 
HETATM 8751 O  O   . HOH G 7 .    ? 72.852 63.708  -20.865 1.00 32.55 ? 2203 HOH A O   1 
HETATM 8752 O  O   . HOH G 7 .    ? 71.766 62.365  -17.940 1.00 35.89 ? 2204 HOH A O   1 
HETATM 8753 O  O   . HOH G 7 .    ? 70.138 61.512  -20.338 1.00 30.60 ? 2205 HOH A O   1 
HETATM 8754 O  O   . HOH G 7 .    ? 69.811 62.638  -23.734 1.00 39.01 ? 2206 HOH A O   1 
HETATM 8755 O  O   . HOH G 7 .    ? 67.917 58.424  -24.022 1.00 25.46 ? 2207 HOH A O   1 
HETATM 8756 O  O   . HOH G 7 .    ? 68.021 56.354  -22.230 1.00 39.01 ? 2208 HOH A O   1 
HETATM 8757 O  O   . HOH G 7 .    ? 66.560 55.893  -20.165 1.00 22.01 ? 2209 HOH A O   1 
HETATM 8758 O  O   . HOH G 7 .    ? 67.604 54.399  -18.204 1.00 28.55 ? 2210 HOH A O   1 
HETATM 8759 O  O   . HOH G 7 .    ? 69.701 53.432  -19.646 1.00 38.36 ? 2211 HOH A O   1 
HETATM 8760 O  O   . HOH G 7 .    ? 65.812 52.466  -20.908 1.00 42.76 ? 2212 HOH A O   1 
HETATM 8761 O  O   . HOH G 7 .    ? 64.465 49.414  -21.570 1.00 38.76 ? 2213 HOH A O   1 
HETATM 8762 O  O   . HOH G 7 .    ? 62.336 47.831  -20.822 1.00 42.35 ? 2214 HOH A O   1 
HETATM 8763 O  O   . HOH G 7 .    ? 60.808 46.665  -22.278 1.00 35.37 ? 2215 HOH A O   1 
HETATM 8764 O  O   . HOH G 7 .    ? 63.105 42.665  -20.808 1.00 30.08 ? 2216 HOH A O   1 
HETATM 8765 O  O   . HOH G 7 .    ? 57.008 42.947  -19.749 1.00 30.85 ? 2217 HOH A O   1 
HETATM 8766 O  O   . HOH G 7 .    ? 56.437 45.907  -17.303 1.00 21.13 ? 2218 HOH A O   1 
HETATM 8767 O  O   . HOH G 7 .    ? 63.759 49.874  -13.909 1.00 18.17 ? 2219 HOH A O   1 
HETATM 8768 O  O   . HOH G 7 .    ? 68.497 46.717  -16.515 1.00 33.22 ? 2220 HOH A O   1 
HETATM 8769 O  O   . HOH G 7 .    ? 72.004 46.890  -17.779 1.00 37.14 ? 2221 HOH A O   1 
HETATM 8770 O  O   . HOH G 7 .    ? 71.032 42.851  -15.377 1.00 36.61 ? 2222 HOH A O   1 
HETATM 8771 O  O   . HOH G 7 .    ? 69.243 41.514  -17.186 1.00 34.82 ? 2223 HOH A O   1 
HETATM 8772 O  O   . HOH G 7 .    ? 67.077 38.271  -9.531  1.00 37.11 ? 2224 HOH A O   1 
HETATM 8773 O  O   . HOH G 7 .    ? 64.342 39.162  -10.060 1.00 27.30 ? 2225 HOH A O   1 
HETATM 8774 O  O   . HOH G 7 .    ? 63.462 44.414  -6.689  1.00 21.18 ? 2226 HOH A O   1 
HETATM 8775 O  O   . HOH G 7 .    ? 63.508 45.683  -3.160  1.00 48.57 ? 2227 HOH A O   1 
HETATM 8776 O  O   . HOH G 7 .    ? 66.023 45.297  -3.048  1.00 37.11 ? 2228 HOH A O   1 
HETATM 8777 O  O   . HOH G 7 .    ? 67.382 46.347  -1.263  1.00 29.03 ? 2229 HOH A O   1 
HETATM 8778 O  O   . HOH G 7 .    ? 68.108 49.088  -0.984  1.00 26.79 ? 2230 HOH A O   1 
HETATM 8779 O  O   . HOH G 7 .    ? 65.986 50.036  0.415   1.00 42.90 ? 2231 HOH A O   1 
HETATM 8780 O  O   . HOH G 7 .    ? 63.353 51.915  -0.223  1.00 38.54 ? 2232 HOH A O   1 
HETATM 8781 O  O   . HOH G 7 .    ? 60.497 54.545  -0.311  1.00 19.06 ? 2233 HOH A O   1 
HETATM 8782 O  O   . HOH G 7 .    ? 58.855 56.465  -1.345  1.00 17.15 ? 2234 HOH A O   1 
HETATM 8783 O  O   . HOH G 7 .    ? 58.902 57.890  0.962   1.00 29.37 ? 2235 HOH A O   1 
HETATM 8784 O  O   . HOH G 7 .    ? 56.542 58.288  1.408   1.00 29.13 ? 2236 HOH A O   1 
HETATM 8785 O  O   . HOH G 7 .    ? 56.860 60.782  1.623   1.00 18.92 ? 2237 HOH A O   1 
HETATM 8786 O  O   . HOH G 7 .    ? 55.174 58.793  3.969   1.00 20.26 ? 2238 HOH A O   1 
HETATM 8787 O  O   . HOH G 7 .    ? 57.440 58.299  5.538   1.00 30.66 ? 2239 HOH A O   1 
HETATM 8788 O  O   . HOH G 7 .    ? 58.600 60.292  5.915   1.00 35.41 ? 2240 HOH A O   1 
HETATM 8789 O  O   . HOH G 7 .    ? 57.688 62.195  7.892   1.00 28.26 ? 2241 HOH A O   1 
HETATM 8790 O  O   . HOH G 7 .    ? 56.593 66.817  5.150   1.00 38.24 ? 2242 HOH A O   1 
HETATM 8791 O  O   . HOH G 7 .    ? 54.950 68.368  3.639   1.00 40.97 ? 2243 HOH A O   1 
HETATM 8792 O  O   . HOH G 7 .    ? 52.023 68.686  4.069   1.00 39.27 ? 2244 HOH A O   1 
HETATM 8793 O  O   . HOH G 7 .    ? 49.853 67.303  4.345   1.00 26.21 ? 2245 HOH A O   1 
HETATM 8794 O  O   . HOH G 7 .    ? 49.274 67.876  6.698   1.00 32.20 ? 2246 HOH A O   1 
HETATM 8795 O  O   . HOH G 7 .    ? 51.288 66.187  8.586   1.00 28.68 ? 2247 HOH A O   1 
HETATM 8796 O  O   . HOH G 7 .    ? 53.175 67.704  9.064   1.00 36.27 ? 2248 HOH A O   1 
HETATM 8797 O  O   . HOH G 7 .    ? 52.595 70.424  8.967   1.00 37.09 ? 2249 HOH A O   1 
HETATM 8798 O  O   . HOH G 7 .    ? 50.353 72.058  9.208   1.00 22.83 ? 2250 HOH A O   1 
HETATM 8799 O  O   . HOH G 7 .    ? 51.248 74.342  8.502   1.00 41.79 ? 2251 HOH A O   1 
HETATM 8800 O  O   . HOH G 7 .    ? 48.245 76.347  8.248   1.00 38.53 ? 2252 HOH A O   1 
HETATM 8801 O  O   . HOH G 7 .    ? 46.113 77.368  9.477   1.00 25.79 ? 2253 HOH A O   1 
HETATM 8802 O  O   . HOH G 7 .    ? 47.287 78.132  11.652  1.00 33.66 ? 2254 HOH A O   1 
HETATM 8803 O  O   . HOH G 7 .    ? 47.086 77.290  14.179  1.00 40.96 ? 2255 HOH A O   1 
HETATM 8804 O  O   . HOH G 7 .    ? 50.905 76.113  14.367  1.00 25.95 ? 2256 HOH A O   1 
HETATM 8805 O  O   . HOH G 7 .    ? 51.693 77.458  11.819  1.00 46.43 ? 2257 HOH A O   1 
HETATM 8806 O  O   . HOH G 7 .    ? 49.201 76.356  5.349   1.00 34.75 ? 2258 HOH A O   1 
HETATM 8807 O  O   . HOH G 7 .    ? 50.599 77.123  2.145   1.00 40.37 ? 2259 HOH A O   1 
HETATM 8808 O  O   . HOH G 7 .    ? 52.381 75.284  1.870   1.00 46.60 ? 2260 HOH A O   1 
HETATM 8809 O  O   . HOH G 7 .    ? 52.627 72.848  3.996   1.00 37.07 ? 2261 HOH A O   1 
HETATM 8810 O  O   . HOH G 7 .    ? 52.347 70.663  5.972   1.00 33.50 ? 2262 HOH A O   1 
HETATM 8811 O  O   . HOH G 7 .    ? 56.211 71.153  3.714   1.00 43.13 ? 2263 HOH A O   1 
HETATM 8812 O  O   . HOH G 7 .    ? 59.148 68.093  2.549   1.00 28.33 ? 2264 HOH A O   1 
HETATM 8813 O  O   . HOH G 7 .    ? 60.441 61.987  -1.210  1.00 18.23 ? 2265 HOH A O   1 
HETATM 8814 O  O   . HOH G 7 .    ? 62.165 60.443  0.588   1.00 35.67 ? 2266 HOH A O   1 
HETATM 8815 O  O   . HOH G 7 .    ? 63.878 56.640  0.841   1.00 34.54 ? 2267 HOH A O   1 
HETATM 8816 O  O   . HOH G 7 .    ? 60.733 55.865  2.163   1.00 40.27 ? 2268 HOH A O   1 
HETATM 8817 O  O   . HOH G 7 .    ? 59.316 51.714  2.675   1.00 30.83 ? 2269 HOH A O   1 
HETATM 8818 O  O   . HOH G 7 .    ? 58.449 52.661  4.854   1.00 28.14 ? 2270 HOH A O   1 
HETATM 8819 O  O   . HOH G 7 .    ? 60.222 51.127  6.270   1.00 38.95 ? 2271 HOH A O   1 
HETATM 8820 O  O   . HOH G 7 .    ? 59.338 48.636  2.321   1.00 37.07 ? 2272 HOH A O   1 
HETATM 8821 O  O   . HOH G 7 .    ? 59.294 49.823  -0.615  1.00 22.30 ? 2273 HOH A O   1 
HETATM 8822 O  O   . HOH G 7 .    ? 58.702 52.438  -0.027  1.00 17.53 ? 2274 HOH A O   1 
HETATM 8823 O  O   . HOH G 7 .    ? 56.121 53.168  -0.565  1.00 13.01 ? 2275 HOH A O   1 
HETATM 8824 O  O   . HOH G 7 .    ? 56.274 55.550  -2.043  1.00 13.70 ? 2276 HOH A O   1 
HETATM 8825 O  O   . HOH G 7 .    ? 54.933 57.335  -0.433  1.00 17.78 ? 2277 HOH A O   1 
HETATM 8826 O  O   . HOH G 7 .    ? 52.724 58.693  -1.682  1.00 17.76 ? 2278 HOH A O   1 
HETATM 8827 O  O   . HOH G 7 .    ? 51.414 56.459  -5.537  1.00 13.90 ? 2279 HOH A O   1 
HETATM 8828 O  O   . HOH G 7 .    ? 49.714 57.378  -7.500  1.00 15.15 ? 2280 HOH A O   1 
HETATM 8829 O  O   . HOH G 7 .    ? 52.149 53.861  -4.803  1.00 12.90 ? 2281 HOH A O   1 
HETATM 8830 O  O   . HOH G 7 .    ? 49.799 48.240  1.450   1.00 14.16 ? 2282 HOH A O   1 
HETATM 8831 O  O   . HOH G 7 .    ? 51.868 46.292  1.364   1.00 17.40 ? 2283 HOH A O   1 
HETATM 8832 O  O   . HOH G 7 .    ? 51.546 44.237  3.129   1.00 29.13 ? 2284 HOH A O   1 
HETATM 8833 O  O   . HOH G 7 .    ? 49.352 44.010  4.540   1.00 20.11 ? 2285 HOH A O   1 
HETATM 8834 O  O   . HOH G 7 .    ? 49.978 43.823  7.093   1.00 23.60 ? 2286 HOH A O   1 
HETATM 8835 O  O   . HOH G 7 .    ? 49.096 41.665  8.414   1.00 31.30 ? 2287 HOH A O   1 
HETATM 8836 O  O   . HOH G 7 .    ? 51.414 44.988  9.919   1.00 34.86 ? 2288 HOH A O   1 
HETATM 8837 O  O   . HOH G 7 .    ? 52.051 50.389  6.371   1.00 15.32 ? 2289 HOH A O   1 
HETATM 8838 O  O   . HOH G 7 .    ? 47.457 45.811  3.729   1.00 14.79 ? 2290 HOH A O   1 
HETATM 8839 O  O   . HOH G 7 .    ? 38.815 52.796  2.191   1.00 28.28 ? 2291 HOH A O   1 
HETATM 8840 O  O   . HOH G 7 .    ? 39.607 55.501  3.040   1.00 18.23 ? 2292 HOH A O   1 
HETATM 8841 O  O   . HOH G 7 .    ? 37.492 56.784  1.755   1.00 13.14 ? 2293 HOH A O   1 
HETATM 8842 O  O   . HOH G 7 .    ? 35.885 52.860  1.389   1.00 14.35 ? 2294 HOH A O   1 
HETATM 8843 O  O   . HOH G 7 .    ? 34.180 52.211  -0.894  1.00 12.73 ? 2295 HOH A O   1 
HETATM 8844 O  O   . HOH G 7 .    ? 36.697 51.410  3.908   1.00 15.33 ? 2296 HOH A O   1 
HETATM 8845 O  O   . HOH G 7 .    ? 40.090 56.025  5.793   1.00 16.99 ? 2297 HOH A O   1 
HETATM 8846 O  O   . HOH G 7 .    ? 42.916 56.568  6.230   1.00 15.72 ? 2298 HOH A O   1 
HETATM 8847 O  O   . HOH G 7 .    ? 42.720 56.249  2.818   1.00 22.87 ? 2299 HOH A O   1 
HETATM 8848 O  O   . HOH G 7 .    ? 40.166 62.553  6.068   1.00 13.63 ? 2300 HOH A O   1 
HETATM 8849 O  O   . HOH G 7 .    ? 38.654 62.124  8.429   1.00 14.83 ? 2301 HOH A O   1 
HETATM 8850 O  O   . HOH G 7 .    ? 37.689 58.883  11.098  1.00 14.34 ? 2302 HOH A O   1 
HETATM 8851 O  O   . HOH G 7 .    ? 36.839 57.473  13.365  1.00 13.42 ? 2303 HOH A O   1 
HETATM 8852 O  O   . HOH G 7 .    ? 39.278 57.203  14.805  1.00 12.92 ? 2304 HOH A O   1 
HETATM 8853 O  O   . HOH G 7 .    ? 41.171 58.803  13.535  1.00 14.70 ? 2305 HOH A O   1 
HETATM 8854 O  O   . HOH G 7 .    ? 34.281 67.452  12.425  1.00 16.15 ? 2306 HOH A O   1 
HETATM 8855 O  O   . HOH G 7 .    ? 34.674 70.105  13.101  1.00 20.99 ? 2307 HOH A O   1 
HETATM 8856 O  O   . HOH G 7 .    ? 31.829 70.917  13.544  1.00 28.36 ? 2308 HOH A O   1 
HETATM 8857 O  O   . HOH G 7 .    ? 29.824 71.922  12.379  1.00 31.41 ? 2309 HOH A O   1 
HETATM 8858 O  O   . HOH G 7 .    ? 29.685 75.329  10.844  1.00 35.42 ? 2310 HOH A O   1 
HETATM 8859 O  O   . HOH G 7 .    ? 26.399 74.798  10.960  1.00 33.09 ? 2311 HOH A O   1 
HETATM 8860 O  O   . HOH G 7 .    ? 25.244 73.498  8.877   1.00 30.79 ? 2312 HOH A O   1 
HETATM 8861 O  O   . HOH G 7 .    ? 26.182 72.418  5.603   1.00 17.87 ? 2313 HOH A O   1 
HETATM 8862 O  O   . HOH G 7 .    ? 26.306 75.390  1.671   1.00 32.04 ? 2314 HOH A O   1 
HETATM 8863 O  O   . HOH G 7 .    ? 21.380 78.177  -1.384  1.00 23.61 ? 2315 HOH A O   1 
HETATM 8864 O  O   . HOH G 7 .    ? 16.470 79.953  -1.270  1.00 46.12 ? 2316 HOH A O   1 
HETATM 8865 O  O   . HOH G 7 .    ? 16.886 74.269  -2.912  1.00 21.60 ? 2317 HOH A O   1 
HETATM 8866 O  O   . HOH G 7 .    ? 20.127 74.045  -6.702  1.00 17.78 ? 2318 HOH A O   1 
HETATM 8867 O  O   . HOH G 7 .    ? 24.615 70.273  -8.681  1.00 16.78 ? 2319 HOH A O   1 
HETATM 8868 O  O   . HOH G 7 .    ? 26.756 68.637  -9.204  1.00 13.48 ? 2320 HOH A O   1 
HETATM 8869 O  O   . HOH G 7 .    ? 32.634 64.298  -9.957  1.00 21.13 ? 2321 HOH A O   1 
HETATM 8870 O  O   . HOH G 7 .    ? 34.210 58.325  -8.696  1.00 12.15 ? 2322 HOH A O   1 
HETATM 8871 O  O   . HOH G 7 .    ? 30.157 58.182  -11.716 1.00 12.69 ? 2323 HOH A O   1 
HETATM 8872 O  O   . HOH G 7 .    ? 26.756 60.612  -3.255  1.00 13.31 ? 2324 HOH A O   1 
HETATM 8873 O  O   . HOH G 7 .    ? 32.516 59.843  -1.747  1.00 12.97 ? 2325 HOH A O   1 
HETATM 8874 O  O   . HOH G 7 .    ? 33.061 62.480  0.123   1.00 11.93 ? 2326 HOH A O   1 
HETATM 8875 O  O   . HOH G 7 .    ? 30.836 57.021  4.544   1.00 25.84 ? 2327 HOH A O   1 
HETATM 8876 O  O   . HOH G 7 .    ? 27.211 59.063  8.546   1.00 20.30 ? 2328 HOH A O   1 
HETATM 8877 O  O   . HOH G 7 .    ? 26.945 61.102  10.367  1.00 34.29 ? 2329 HOH A O   1 
HETATM 8878 O  O   . HOH G 7 .    ? 24.580 61.173  9.286   1.00 24.31 ? 2330 HOH A O   1 
HETATM 8879 O  O   . HOH G 7 .    ? 24.157 63.144  7.490   1.00 17.92 ? 2331 HOH A O   1 
HETATM 8880 O  O   . HOH G 7 .    ? 26.003 64.909  8.331   1.00 29.22 ? 2332 HOH A O   1 
HETATM 8881 O  O   . HOH G 7 .    ? 27.976 66.320  7.280   1.00 26.22 ? 2333 HOH A O   1 
HETATM 8882 O  O   . HOH G 7 .    ? 20.832 64.987  7.795   1.00 21.38 ? 2334 HOH A O   1 
HETATM 8883 O  O   . HOH G 7 .    ? 20.755 67.812  8.559   1.00 24.63 ? 2335 HOH A O   1 
HETATM 8884 O  O   . HOH G 7 .    ? 17.892 70.607  6.698   1.00 39.49 ? 2336 HOH A O   1 
HETATM 8885 O  O   . HOH G 7 .    ? 15.813 69.936  6.351   1.00 37.13 ? 2337 HOH A O   1 
HETATM 8886 O  O   . HOH G 7 .    ? 18.581 69.690  4.270   1.00 21.18 ? 2338 HOH A O   1 
HETATM 8887 O  O   . HOH G 7 .    ? 19.208 72.179  3.087   1.00 23.35 ? 2339 HOH A O   1 
HETATM 8888 O  O   . HOH G 7 .    ? 17.677 74.146  4.002   1.00 28.75 ? 2340 HOH A O   1 
HETATM 8889 O  O   . HOH G 7 .    ? 15.646 73.328  5.489   1.00 35.03 ? 2341 HOH A O   1 
HETATM 8890 O  O   . HOH G 7 .    ? 19.196 76.298  4.929   1.00 32.77 ? 2342 HOH A O   1 
HETATM 8891 O  O   . HOH G 7 .    ? 21.575 79.442  5.436   1.00 35.37 ? 2343 HOH A O   1 
HETATM 8892 O  O   . HOH G 7 .    ? 22.165 76.304  8.861   1.00 34.89 ? 2344 HOH A O   1 
HETATM 8893 O  O   . HOH G 7 .    ? 27.461 82.092  3.482   1.00 34.48 ? 2345 HOH A O   1 
HETATM 8894 O  O   . HOH G 7 .    ? 29.752 82.792  2.454   1.00 24.85 ? 2346 HOH A O   1 
HETATM 8895 O  O   . HOH G 7 .    ? 31.061 82.982  4.797   1.00 38.41 ? 2347 HOH A O   1 
HETATM 8896 O  O   . HOH G 7 .    ? 30.255 82.036  7.383   1.00 41.88 ? 2348 HOH A O   1 
HETATM 8897 O  O   . HOH G 7 .    ? 32.218 80.171  7.373   1.00 37.52 ? 2349 HOH A O   1 
HETATM 8898 O  O   . HOH G 7 .    ? 36.179 80.729  6.374   1.00 23.72 ? 2350 HOH A O   1 
HETATM 8899 O  O   . HOH G 7 .    ? 34.877 77.455  12.240  1.00 35.62 ? 2351 HOH A O   1 
HETATM 8900 O  O   . HOH G 7 .    ? 35.814 73.256  15.402  1.00 35.07 ? 2352 HOH A O   1 
HETATM 8901 O  O   . HOH G 7 .    ? 35.605 70.395  16.191  1.00 46.99 ? 2353 HOH A O   1 
HETATM 8902 O  O   . HOH G 7 .    ? 36.004 70.034  19.291  1.00 41.35 ? 2354 HOH A O   1 
HETATM 8903 O  O   . HOH G 7 .    ? 36.028 67.905  20.589  1.00 44.65 ? 2355 HOH A O   1 
HETATM 8904 O  O   . HOH G 7 .    ? 35.798 68.204  23.378  1.00 33.19 ? 2356 HOH A O   1 
HETATM 8905 O  O   . HOH G 7 .    ? 32.573 69.219  24.474  1.00 27.20 ? 2357 HOH A O   1 
HETATM 8906 O  O   . HOH G 7 .    ? 30.925 70.714  21.511  1.00 40.91 ? 2358 HOH A O   1 
HETATM 8907 O  O   . HOH G 7 .    ? 28.684 72.312  22.433  1.00 30.58 ? 2359 HOH A O   1 
HETATM 8908 O  O   . HOH G 7 .    ? 29.536 74.841  22.228  1.00 29.33 ? 2360 HOH A O   1 
HETATM 8909 O  O   . HOH G 7 .    ? 25.003 70.986  22.655  1.00 40.63 ? 2361 HOH A O   1 
HETATM 8910 O  O   . HOH G 7 .    ? 24.738 68.080  21.797  1.00 26.23 ? 2362 HOH A O   1 
HETATM 8911 O  O   . HOH G 7 .    ? 22.364 67.927  20.436  1.00 27.93 ? 2363 HOH A O   1 
HETATM 8912 O  O   . HOH G 7 .    ? 20.437 68.154  22.263  1.00 30.24 ? 2364 HOH A O   1 
HETATM 8913 O  O   . HOH G 7 .    ? 20.725 65.225  27.466  1.00 29.96 ? 2365 HOH A O   1 
HETATM 8914 O  O   . HOH G 7 .    ? 22.519 65.836  29.353  1.00 34.28 ? 2366 HOH A O   1 
HETATM 8915 O  O   . HOH G 7 .    ? 22.061 65.492  32.387  1.00 32.90 ? 2367 HOH A O   1 
HETATM 8916 O  O   . HOH G 7 .    ? 22.178 62.657  33.649  1.00 32.58 ? 2368 HOH A O   1 
HETATM 8917 O  O   . HOH G 7 .    ? 24.275 60.809  36.226  1.00 37.26 ? 2369 HOH A O   1 
HETATM 8918 O  O   . HOH G 7 .    ? 23.977 57.323  38.597  1.00 38.88 ? 2370 HOH A O   1 
HETATM 8919 O  O   . HOH G 7 .    ? 21.556 55.325  40.203  1.00 31.59 ? 2371 HOH A O   1 
HETATM 8920 O  O   . HOH G 7 .    ? 17.772 52.649  35.889  1.00 41.34 ? 2372 HOH A O   1 
HETATM 8921 O  O   . HOH G 7 .    ? 17.421 52.425  33.322  1.00 46.31 ? 2373 HOH A O   1 
HETATM 8922 O  O   . HOH G 7 .    ? 18.838 48.604  37.733  1.00 25.46 ? 2374 HOH A O   1 
HETATM 8923 O  O   . HOH G 7 .    ? 21.333 47.187  39.177  1.00 26.31 ? 2375 HOH A O   1 
HETATM 8924 O  O   . HOH G 7 .    ? 24.185 45.497  40.979  1.00 38.70 ? 2376 HOH A O   1 
HETATM 8925 O  O   . HOH G 7 .    ? 28.210 44.387  38.292  1.00 33.49 ? 2377 HOH A O   1 
HETATM 8926 O  O   . HOH G 7 .    ? 29.152 46.892  37.196  1.00 27.34 ? 2378 HOH A O   1 
HETATM 8927 O  O   . HOH G 7 .    ? 31.692 47.248  38.058  1.00 38.57 ? 2379 HOH A O   1 
HETATM 8928 O  O   . HOH G 7 .    ? 34.164 47.863  36.563  1.00 38.58 ? 2380 HOH A O   1 
HETATM 8929 O  O   . HOH G 7 .    ? 34.993 51.011  35.977  1.00 38.34 ? 2381 HOH A O   1 
HETATM 8930 O  O   . HOH G 7 .    ? 39.462 49.782  36.342  1.00 34.71 ? 2382 HOH A O   1 
HETATM 8931 O  O   . HOH G 7 .    ? 40.138 52.510  36.358  1.00 34.74 ? 2383 HOH A O   1 
HETATM 8932 O  O   . HOH G 7 .    ? 42.701 53.222  35.565  1.00 25.18 ? 2384 HOH A O   1 
HETATM 8933 O  O   . HOH G 7 .    ? 44.823 55.153  36.076  1.00 40.90 ? 2385 HOH A O   1 
HETATM 8934 O  O   . HOH G 7 .    ? 43.527 56.544  33.657  1.00 33.30 ? 2386 HOH A O   1 
HETATM 8935 O  O   . HOH G 7 .    ? 41.853 58.217  34.653  1.00 36.64 ? 2387 HOH A O   1 
HETATM 8936 O  O   . HOH G 7 .    ? 40.632 57.012  30.966  1.00 28.13 ? 2388 HOH A O   1 
HETATM 8937 O  O   . HOH G 7 .    ? 45.621 58.077  32.734  1.00 42.55 ? 2389 HOH A O   1 
HETATM 8938 O  O   . HOH G 7 .    ? 50.803 55.587  34.745  1.00 49.21 ? 2390 HOH A O   1 
HETATM 8939 O  O   . HOH G 7 .    ? 49.571 50.598  32.631  1.00 31.18 ? 2391 HOH A O   1 
HETATM 8940 O  O   . HOH G 7 .    ? 49.062 49.723  28.342  1.00 20.86 ? 2392 HOH A O   1 
HETATM 8941 O  O   . HOH G 7 .    ? 49.737 47.021  28.923  1.00 30.17 ? 2393 HOH A O   1 
HETATM 8942 O  O   . HOH G 7 .    ? 49.481 45.431  30.964  1.00 35.45 ? 2394 HOH A O   1 
HETATM 8943 O  O   . HOH G 7 .    ? 47.414 43.493  30.619  1.00 45.26 ? 2395 HOH A O   1 
HETATM 8944 O  O   . HOH G 7 .    ? 42.122 48.632  31.280  1.00 23.13 ? 2396 HOH A O   1 
HETATM 8945 O  O   . HOH G 7 .    ? 41.124 50.267  33.202  1.00 23.68 ? 2397 HOH A O   1 
HETATM 8946 O  O   . HOH G 7 .    ? 39.379 49.121  30.117  1.00 23.18 ? 2398 HOH A O   1 
HETATM 8947 O  O   . HOH G 7 .    ? 37.525 47.109  29.804  1.00 22.50 ? 2399 HOH A O   1 
HETATM 8948 O  O   . HOH G 7 .    ? 35.973 45.112  30.938  1.00 22.56 ? 2400 HOH A O   1 
HETATM 8949 O  O   . HOH G 7 .    ? 35.137 43.611  28.735  1.00 18.08 ? 2401 HOH A O   1 
HETATM 8950 O  O   . HOH G 7 .    ? 37.066 45.473  27.503  1.00 17.80 ? 2402 HOH A O   1 
HETATM 8951 O  O   . HOH G 7 .    ? 38.907 42.851  22.800  1.00 31.05 ? 2403 HOH A O   1 
HETATM 8952 O  O   . HOH G 7 .    ? 34.761 45.756  33.381  1.00 22.50 ? 2404 HOH A O   1 
HETATM 8953 O  O   . HOH G 7 .    ? 30.825 43.770  40.697  1.00 45.95 ? 2405 HOH A O   1 
HETATM 8954 O  O   . HOH G 7 .    ? 28.120 49.277  38.530  1.00 31.86 ? 2406 HOH A O   1 
HETATM 8955 O  O   . HOH G 7 .    ? 30.575 51.402  39.634  1.00 48.02 ? 2407 HOH A O   1 
HETATM 8956 O  O   . HOH G 7 .    ? 28.877 55.018  40.053  1.00 32.17 ? 2408 HOH A O   1 
HETATM 8957 O  O   . HOH G 7 .    ? 30.442 57.358  40.064  1.00 36.02 ? 2409 HOH A O   1 
HETATM 8958 O  O   . HOH G 7 .    ? 31.534 57.401  37.353  1.00 29.87 ? 2410 HOH A O   1 
HETATM 8959 O  O   . HOH G 7 .    ? 30.147 59.159  35.312  1.00 32.04 ? 2411 HOH A O   1 
HETATM 8960 O  O   . HOH G 7 .    ? 35.265 62.194  33.992  1.00 31.84 ? 2412 HOH A O   1 
HETATM 8961 O  O   . HOH G 7 .    ? 37.645 62.192  35.635  1.00 34.98 ? 2413 HOH A O   1 
HETATM 8962 O  O   . HOH G 7 .    ? 39.842 66.898  31.270  1.00 27.83 ? 2414 HOH A O   1 
HETATM 8963 O  O   . HOH G 7 .    ? 42.009 67.231  29.262  1.00 31.25 ? 2415 HOH A O   1 
HETATM 8964 O  O   . HOH G 7 .    ? 44.599 67.768  28.142  1.00 39.94 ? 2416 HOH A O   1 
HETATM 8965 O  O   . HOH G 7 .    ? 46.379 68.319  26.472  1.00 36.04 ? 2417 HOH A O   1 
HETATM 8966 O  O   . HOH G 7 .    ? 47.677 65.928  26.937  1.00 29.32 ? 2418 HOH A O   1 
HETATM 8967 O  O   . HOH G 7 .    ? 50.783 61.715  26.403  1.00 26.97 ? 2419 HOH A O   1 
HETATM 8968 O  O   . HOH G 7 .    ? 51.865 59.996  28.169  1.00 34.95 ? 2420 HOH A O   1 
HETATM 8969 O  O   . HOH G 7 .    ? 51.787 63.628  24.503  1.00 32.58 ? 2421 HOH A O   1 
HETATM 8970 O  O   . HOH G 7 .    ? 52.705 67.241  22.458  1.00 46.98 ? 2422 HOH A O   1 
HETATM 8971 O  O   . HOH G 7 .    ? 50.841 69.478  24.353  1.00 46.32 ? 2423 HOH A O   1 
HETATM 8972 O  O   . HOH G 7 .    ? 51.899 71.401  22.326  1.00 41.86 ? 2424 HOH A O   1 
HETATM 8973 O  O   . HOH G 7 .    ? 52.488 72.328  18.290  1.00 31.01 ? 2425 HOH A O   1 
HETATM 8974 O  O   . HOH G 7 .    ? 53.026 69.464  18.217  1.00 28.22 ? 2426 HOH A O   1 
HETATM 8975 O  O   . HOH G 7 .    ? 55.999 70.798  19.701  1.00 47.08 ? 2427 HOH A O   1 
HETATM 8976 O  O   . HOH G 7 .    ? 57.854 67.985  13.517  1.00 46.32 ? 2428 HOH A O   1 
HETATM 8977 O  O   . HOH G 7 .    ? 55.541 67.293  13.467  1.00 36.16 ? 2429 HOH A O   1 
HETATM 8978 O  O   . HOH G 7 .    ? 60.703 63.351  15.372  1.00 43.39 ? 2430 HOH A O   1 
HETATM 8979 O  O   . HOH G 7 .    ? 62.115 64.003  13.702  1.00 41.66 ? 2431 HOH A O   1 
HETATM 8980 O  O   . HOH G 7 .    ? 61.502 59.189  14.616  1.00 35.39 ? 2432 HOH A O   1 
HETATM 8981 O  O   . HOH G 7 .    ? 61.094 56.930  15.453  1.00 41.15 ? 2433 HOH A O   1 
HETATM 8982 O  O   . HOH G 7 .    ? 58.744 50.829  14.788  1.00 41.96 ? 2434 HOH A O   1 
HETATM 8983 O  O   . HOH G 7 .    ? 57.543 49.088  16.702  1.00 37.68 ? 2435 HOH A O   1 
HETATM 8984 O  O   . HOH G 7 .    ? 55.227 50.026  16.918  1.00 31.33 ? 2436 HOH A O   1 
HETATM 8985 O  O   . HOH G 7 .    ? 54.194 47.470  15.636  1.00 31.11 ? 2437 HOH A O   1 
HETATM 8986 O  O   . HOH G 7 .    ? 56.723 46.360  15.956  1.00 39.00 ? 2438 HOH A O   1 
HETATM 8987 O  O   . HOH G 7 .    ? 57.320 48.737  21.525  1.00 30.84 ? 2439 HOH A O   1 
HETATM 8988 O  O   . HOH G 7 .    ? 58.654 50.941  22.160  1.00 27.56 ? 2440 HOH A O   1 
HETATM 8989 O  O   . HOH G 7 .    ? 60.174 50.587  20.344  1.00 37.80 ? 2441 HOH A O   1 
HETATM 8990 O  O   . HOH G 7 .    ? 59.472 50.618  24.787  1.00 40.13 ? 2442 HOH A O   1 
HETATM 8991 O  O   . HOH G 7 .    ? 57.911 52.559  26.321  1.00 45.55 ? 2443 HOH A O   1 
HETATM 8992 O  O   . HOH G 7 .    ? 55.820 51.624  27.362  1.00 35.57 ? 2444 HOH A O   1 
HETATM 8993 O  O   . HOH G 7 .    ? 53.111 52.437  26.334  1.00 35.03 ? 2445 HOH A O   1 
HETATM 8994 O  O   . HOH G 7 .    ? 51.812 50.228  27.447  1.00 33.32 ? 2446 HOH A O   1 
HETATM 8995 O  O   . HOH G 7 .    ? 52.368 48.936  25.635  1.00 38.05 ? 2447 HOH A O   1 
HETATM 8996 O  O   . HOH G 7 .    ? 53.885 46.631  23.461  1.00 36.83 ? 2448 HOH A O   1 
HETATM 8997 O  O   . HOH G 7 .    ? 53.125 44.279  23.056  1.00 45.00 ? 2449 HOH A O   1 
HETATM 8998 O  O   . HOH G 7 .    ? 59.252 55.326  27.072  1.00 43.31 ? 2450 HOH A O   1 
HETATM 8999 O  O   . HOH G 7 .    ? 59.422 61.998  25.785  1.00 37.03 ? 2451 HOH A O   1 
HETATM 9000 O  O   . HOH G 7 .    ? 62.325 62.022  25.530  1.00 35.41 ? 2452 HOH A O   1 
HETATM 9001 O  O   . HOH G 7 .    ? 56.931 64.654  24.163  1.00 32.45 ? 2453 HOH A O   1 
HETATM 9002 O  O   . HOH G 7 .    ? 45.781 74.083  22.552  1.00 37.82 ? 2454 HOH A O   1 
HETATM 9003 O  O   . HOH G 7 .    ? 38.312 73.466  18.016  1.00 42.42 ? 2455 HOH A O   1 
HETATM 9004 O  O   . HOH G 7 .    ? 32.938 66.772  21.286  1.00 28.96 ? 2456 HOH A O   1 
HETATM 9005 O  O   . HOH G 7 .    ? 31.831 65.246  18.866  1.00 19.79 ? 2457 HOH A O   1 
HETATM 9006 O  O   . HOH G 7 .    ? 29.723 66.831  18.109  1.00 39.29 ? 2458 HOH A O   1 
HETATM 9007 O  O   . HOH G 7 .    ? 29.357 65.632  15.919  1.00 43.68 ? 2459 HOH A O   1 
HETATM 9008 O  O   . HOH G 7 .    ? 28.145 63.983  14.606  1.00 45.76 ? 2460 HOH A O   1 
HETATM 9009 O  O   . HOH G 7 .    ? 25.648 62.854  13.664  1.00 30.55 ? 2461 HOH A O   1 
HETATM 9010 O  O   . HOH G 7 .    ? 26.245 63.468  17.126  1.00 21.77 ? 2462 HOH A O   1 
HETATM 9011 O  O   . HOH G 7 .    ? 25.558 65.805  17.239  1.00 31.82 ? 2463 HOH A O   1 
HETATM 9012 O  O   . HOH G 7 .    ? 26.359 66.579  19.812  1.00 32.41 ? 2464 HOH A O   1 
HETATM 9013 O  O   . HOH G 7 .    ? 28.603 65.017  19.680  1.00 20.20 ? 2465 HOH A O   1 
HETATM 9014 O  O   . HOH G 7 .    ? 27.921 60.834  19.492  1.00 16.11 ? 2466 HOH A O   1 
HETATM 9015 O  O   . HOH G 7 .    ? 23.101 64.182  18.387  1.00 36.31 ? 2467 HOH A O   1 
HETATM 9016 O  O   . HOH G 7 .    ? 22.598 62.294  16.256  1.00 25.24 ? 2468 HOH A O   1 
HETATM 9017 O  O   . HOH G 7 .    ? 21.540 63.390  14.438  1.00 40.66 ? 2469 HOH A O   1 
HETATM 9018 O  O   . HOH G 7 .    ? 15.463 60.066  15.604  1.00 19.79 ? 2470 HOH A O   1 
HETATM 9019 O  O   . HOH G 7 .    ? 13.969 58.009  16.441  1.00 19.62 ? 2471 HOH A O   1 
HETATM 9020 O  O   . HOH G 7 .    ? 13.965 57.393  19.133  1.00 23.36 ? 2472 HOH A O   1 
HETATM 9021 O  O   . HOH G 7 .    ? 11.650 58.181  20.187  1.00 34.80 ? 2473 HOH A O   1 
HETATM 9022 O  O   . HOH G 7 .    ? 12.363 55.011  22.696  1.00 29.49 ? 2474 HOH A O   1 
HETATM 9023 O  O   . HOH G 7 .    ? 12.879 54.769  25.380  1.00 34.76 ? 2475 HOH A O   1 
HETATM 9024 O  O   . HOH G 7 .    ? 13.267 52.186  25.961  1.00 36.28 ? 2476 HOH A O   1 
HETATM 9025 O  O   . HOH G 7 .    ? 14.111 50.248  24.318  1.00 28.84 ? 2477 HOH A O   1 
HETATM 9026 O  O   . HOH G 7 .    ? 13.441 51.271  21.844  1.00 22.95 ? 2478 HOH A O   1 
HETATM 9027 O  O   . HOH G 7 .    ? 10.793 51.153  21.487  1.00 32.30 ? 2479 HOH A O   1 
HETATM 9028 O  O   . HOH G 7 .    ? 10.309 50.504  19.047  1.00 28.90 ? 2480 HOH A O   1 
HETATM 9029 O  O   . HOH G 7 .    ? 9.365  52.186  17.032  1.00 25.28 ? 2481 HOH A O   1 
HETATM 9030 O  O   . HOH G 7 .    ? 7.714  54.447  17.439  1.00 37.58 ? 2482 HOH A O   1 
HETATM 9031 O  O   . HOH G 7 .    ? 9.858  53.465  22.171  1.00 37.15 ? 2483 HOH A O   1 
HETATM 9032 O  O   . HOH G 7 .    ? 12.115 48.716  25.490  1.00 46.84 ? 2484 HOH A O   1 
HETATM 9033 O  O   . HOH G 7 .    ? 14.267 47.321  26.912  1.00 44.66 ? 2485 HOH A O   1 
HETATM 9034 O  O   . HOH G 7 .    ? 13.842 45.001  27.236  1.00 42.09 ? 2486 HOH A O   1 
HETATM 9035 O  O   . HOH G 7 .    ? 12.795 44.098  22.829  1.00 45.27 ? 2487 HOH A O   1 
HETATM 9036 O  O   . HOH G 7 .    ? 11.142 46.581  21.741  1.00 45.90 ? 2488 HOH A O   1 
HETATM 9037 O  O   . HOH G 7 .    ? 11.521 46.702  17.968  1.00 27.10 ? 2489 HOH A O   1 
HETATM 9038 O  O   . HOH G 7 .    ? 12.597 49.306  17.914  1.00 24.96 ? 2490 HOH A O   1 
HETATM 9039 O  O   . HOH G 7 .    ? 14.366 49.490  19.964  1.00 22.36 ? 2491 HOH A O   1 
HETATM 9040 O  O   . HOH G 7 .    ? 14.025 48.896  15.487  1.00 20.49 ? 2492 HOH A O   1 
HETATM 9041 O  O   . HOH G 7 .    ? 11.766 51.305  14.456  1.00 20.72 ? 2493 HOH A O   1 
HETATM 9042 O  O   . HOH G 7 .    ? 8.047  47.764  11.971  1.00 28.81 ? 2494 HOH A O   1 
HETATM 9043 O  O   . HOH G 7 .    ? 8.720  44.256  13.329  1.00 34.19 ? 2495 HOH A O   1 
HETATM 9044 O  O   . HOH G 7 .    ? 10.344 41.324  12.302  1.00 38.58 ? 2496 HOH A O   1 
HETATM 9045 O  O   . HOH G 7 .    ? 12.926 42.295  12.783  1.00 24.35 ? 2497 HOH A O   1 
HETATM 9046 O  O   . HOH G 7 .    ? 17.269 41.425  9.325   1.00 33.55 ? 2498 HOH A O   1 
HETATM 9047 O  O   . HOH G 7 .    ? 20.489 37.619  12.287  1.00 35.60 ? 2499 HOH A O   1 
HETATM 9048 O  O   . HOH G 7 .    ? 23.012 36.872  13.564  1.00 34.30 ? 2500 HOH A O   1 
HETATM 9049 O  O   . HOH G 7 .    ? 21.767 37.699  15.742  1.00 41.85 ? 2501 HOH A O   1 
HETATM 9050 O  O   . HOH G 7 .    ? 19.665 39.060  17.714  1.00 20.67 ? 2502 HOH A O   1 
HETATM 9051 O  O   . HOH G 7 .    ? 15.999 36.068  16.279  1.00 33.04 ? 2503 HOH A O   1 
HETATM 9052 O  O   . HOH G 7 .    ? 16.149 33.406  15.849  1.00 42.79 ? 2504 HOH A O   1 
HETATM 9053 O  O   . HOH G 7 .    ? 15.891 30.688  18.113  1.00 47.58 ? 2505 HOH A O   1 
HETATM 9054 O  O   . HOH G 7 .    ? 24.185 34.405  15.835  1.00 37.43 ? 2506 HOH A O   1 
HETATM 9055 O  O   . HOH G 7 .    ? 25.236 33.163  13.452  1.00 37.73 ? 2507 HOH A O   1 
HETATM 9056 O  O   . HOH G 7 .    ? 24.295 32.929  9.746   1.00 34.63 ? 2508 HOH A O   1 
HETATM 9057 O  O   . HOH G 7 .    ? 24.750 32.815  6.594   1.00 30.38 ? 2509 HOH A O   1 
HETATM 9058 O  O   . HOH G 7 .    ? 30.547 29.524  6.122   1.00 46.58 ? 2510 HOH A O   1 
HETATM 9059 O  O   . HOH G 7 .    ? 31.056 33.300  2.932   1.00 26.91 ? 2511 HOH A O   1 
HETATM 9060 O  O   . HOH G 7 .    ? 25.878 39.533  5.350   1.00 14.12 ? 2512 HOH A O   1 
HETATM 9061 O  O   . HOH G 7 .    ? 26.253 39.900  8.042   1.00 15.99 ? 2513 HOH A O   1 
HETATM 9062 O  O   . HOH G 7 .    ? 23.983 41.774  7.021   1.00 14.78 ? 2514 HOH A O   1 
HETATM 9063 O  O   . HOH G 7 .    ? 28.141 39.499  11.379  1.00 16.58 ? 2515 HOH A O   1 
HETATM 9064 O  O   . HOH G 7 .    ? 27.224 41.209  13.422  1.00 20.17 ? 2516 HOH A O   1 
HETATM 9065 O  O   . HOH G 7 .    ? 28.207 43.698  13.285  1.00 13.73 ? 2517 HOH A O   1 
HETATM 9066 O  O   . HOH G 7 .    ? 27.193 46.186  13.715  1.00 18.90 ? 2518 HOH A O   1 
HETATM 9067 O  O   . HOH G 7 .    ? 27.875 48.359  12.161  1.00 18.52 ? 2519 HOH A O   1 
HETATM 9068 O  O   . HOH G 7 .    ? 27.556 50.722  13.351  1.00 22.69 ? 2520 HOH A O   1 
HETATM 9069 O  O   . HOH G 7 .    ? 25.637 51.980  12.990  1.00 26.43 ? 2521 HOH A O   1 
HETATM 9070 O  O   . HOH G 7 .    ? 25.423 53.498  11.143  1.00 17.69 ? 2522 HOH A O   1 
HETATM 9071 O  O   . HOH G 7 .    ? 19.288 55.011  11.614  1.00 17.15 ? 2523 HOH A O   1 
HETATM 9072 O  O   . HOH G 7 .    ? 17.014 55.984  10.382  1.00 16.59 ? 2524 HOH A O   1 
HETATM 9073 O  O   . HOH G 7 .    ? 16.712 56.812  13.068  1.00 20.02 ? 2525 HOH A O   1 
HETATM 9074 O  O   . HOH G 7 .    ? 18.339 54.736  14.214  1.00 17.47 ? 2526 HOH A O   1 
HETATM 9075 O  O   . HOH G 7 .    ? 20.043 54.543  16.236  1.00 14.74 ? 2527 HOH A O   1 
HETATM 9076 O  O   . HOH G 7 .    ? 19.221 53.336  8.235   1.00 15.70 ? 2528 HOH A O   1 
HETATM 9077 O  O   . HOH G 7 .    ? 17.539 52.586  6.411   1.00 15.79 ? 2529 HOH A O   1 
HETATM 9078 O  O   . HOH G 7 .    ? 20.015 55.829  7.250   1.00 16.93 ? 2530 HOH A O   1 
HETATM 9079 O  O   . HOH G 7 .    ? 21.643 56.860  5.089   1.00 15.70 ? 2531 HOH A O   1 
HETATM 9080 O  O   . HOH G 7 .    ? 23.757 57.903  6.389   1.00 15.30 ? 2532 HOH A O   1 
HETATM 9081 O  O   . HOH G 7 .    ? 14.402 59.800  5.269   1.00 18.96 ? 2533 HOH A O   1 
HETATM 9082 O  O   . HOH G 7 .    ? 13.646 60.471  7.732   1.00 35.05 ? 2534 HOH A O   1 
HETATM 9083 O  O   . HOH G 7 .    ? 11.611 58.512  8.001   1.00 28.36 ? 2535 HOH A O   1 
HETATM 9084 O  O   . HOH G 7 .    ? 9.817  59.479  6.569   1.00 40.17 ? 2536 HOH A O   1 
HETATM 9085 O  O   . HOH G 7 .    ? 11.385 61.894  5.489   1.00 35.70 ? 2537 HOH A O   1 
HETATM 9086 O  O   . HOH G 7 .    ? 10.303 61.938  2.022   1.00 37.28 ? 2538 HOH A O   1 
HETATM 9087 O  O   . HOH G 7 .    ? 11.675 61.467  0.145   1.00 44.40 ? 2539 HOH A O   1 
HETATM 9088 O  O   . HOH G 7 .    ? 12.895 61.752  -2.253  1.00 28.85 ? 2540 HOH A O   1 
HETATM 9089 O  O   . HOH G 7 .    ? 14.038 59.487  -3.287  1.00 19.20 ? 2541 HOH A O   1 
HETATM 9090 O  O   . HOH G 7 .    ? 13.886 57.715  -1.264  1.00 23.57 ? 2542 HOH A O   1 
HETATM 9091 O  O   . HOH G 7 .    ? 10.019 57.873  -2.983  1.00 33.42 ? 2543 HOH A O   1 
HETATM 9092 O  O   . HOH G 7 .    ? 11.731 59.237  -4.876  1.00 24.65 ? 2544 HOH A O   1 
HETATM 9093 O  O   . HOH G 7 .    ? 11.039 62.235  -4.353  1.00 45.73 ? 2545 HOH A O   1 
HETATM 9094 O  O   . HOH G 7 .    ? 13.152 66.537  -4.709  1.00 19.90 ? 2546 HOH A O   1 
HETATM 9095 O  O   . HOH G 7 .    ? 14.105 67.950  -7.626  1.00 23.86 ? 2547 HOH A O   1 
HETATM 9096 O  O   . HOH G 7 .    ? 13.710 69.879  -9.531  1.00 28.11 ? 2548 HOH A O   1 
HETATM 9097 O  O   . HOH G 7 .    ? 11.560 70.672  -7.543  1.00 39.36 ? 2549 HOH A O   1 
HETATM 9098 O  O   . HOH G 7 .    ? 12.659 66.085  -9.557  1.00 24.00 ? 2550 HOH A O   1 
HETATM 9099 O  O   . HOH G 7 .    ? 10.274 64.315  -10.124 1.00 38.75 ? 2551 HOH A O   1 
HETATM 9100 O  O   . HOH G 7 .    ? 8.727  65.862  -11.926 1.00 38.83 ? 2552 HOH A O   1 
HETATM 9101 O  O   . HOH G 7 .    ? 8.505  64.943  -14.623 1.00 30.18 ? 2553 HOH A O   1 
HETATM 9102 O  O   . HOH G 7 .    ? 16.450 67.592  -19.710 1.00 25.61 ? 2554 HOH A O   1 
HETATM 9103 O  O   . HOH G 7 .    ? 16.111 71.750  -18.827 1.00 24.97 ? 2555 HOH A O   1 
HETATM 9104 O  O   . HOH G 7 .    ? 17.050 70.027  -16.196 1.00 17.77 ? 2556 HOH A O   1 
HETATM 9105 O  O   . HOH G 7 .    ? 20.500 65.920  -19.520 1.00 17.01 ? 2557 HOH A O   1 
HETATM 9106 O  O   . HOH G 7 .    ? 20.257 58.503  -21.839 1.00 14.69 ? 2558 HOH A O   1 
HETATM 9107 O  O   . HOH G 7 .    ? 16.646 60.300  -27.968 1.00 27.36 ? 2559 HOH A O   1 
HETATM 9108 O  O   . HOH G 7 .    ? 14.520 54.935  -26.136 1.00 36.07 ? 2560 HOH A O   1 
HETATM 9109 O  O   . HOH G 7 .    ? 19.182 52.383  -26.735 1.00 33.34 ? 2561 HOH A O   1 
HETATM 9110 O  O   . HOH G 7 .    ? 19.133 51.889  -31.123 1.00 40.74 ? 2562 HOH A O   1 
HETATM 9111 O  O   . HOH G 7 .    ? 18.429 51.863  -37.185 1.00 40.08 ? 2563 HOH A O   1 
HETATM 9112 O  O   . HOH G 7 .    ? 20.729 50.789  -38.193 1.00 36.17 ? 2564 HOH A O   1 
HETATM 9113 O  O   . HOH G 7 .    ? 22.831 48.639  -36.106 1.00 35.89 ? 2565 HOH A O   1 
HETATM 9114 O  O   . HOH G 7 .    ? 21.301 55.105  -36.201 1.00 38.62 ? 2566 HOH A O   1 
HETATM 9115 O  O   . HOH G 7 .    ? 22.442 56.513  -34.077 1.00 21.92 ? 2567 HOH A O   1 
HETATM 9116 O  O   . HOH G 7 .    ? 20.763 58.661  -34.410 1.00 23.64 ? 2568 HOH A O   1 
HETATM 9117 O  O   . HOH G 7 .    ? 19.486 58.197  -36.644 1.00 28.44 ? 2569 HOH A O   1 
HETATM 9118 O  O   . HOH G 7 .    ? 18.699 60.388  -37.720 1.00 29.68 ? 2570 HOH A O   1 
HETATM 9119 O  O   . HOH G 7 .    ? 20.718 60.508  -40.181 1.00 36.89 ? 2571 HOH A O   1 
HETATM 9120 O  O   . HOH G 7 .    ? 25.577 58.545  -38.613 1.00 46.96 ? 2572 HOH A O   1 
HETATM 9121 O  O   . HOH G 7 .    ? 24.834 59.055  -36.180 1.00 45.06 ? 2573 HOH A O   1 
HETATM 9122 O  O   . HOH G 7 .    ? 21.745 61.090  -34.639 1.00 33.22 ? 2574 HOH A O   1 
HETATM 9123 O  O   . HOH G 7 .    ? 22.387 63.030  -32.914 1.00 26.05 ? 2575 HOH A O   1 
HETATM 9124 O  O   . HOH G 7 .    ? 18.578 70.363  -29.931 1.00 41.72 ? 2576 HOH A O   1 
HETATM 9125 O  O   . HOH G 7 .    ? 18.326 75.962  -29.336 1.00 44.91 ? 2577 HOH A O   1 
HETATM 9126 O  O   . HOH G 7 .    ? 22.901 78.244  -30.239 1.00 30.19 ? 2578 HOH A O   1 
HETATM 9127 O  O   . HOH G 7 .    ? 20.548 79.909  -33.311 1.00 45.24 ? 2579 HOH A O   1 
HETATM 9128 O  O   . HOH G 7 .    ? 22.107 79.644  -35.928 1.00 32.11 ? 2580 HOH A O   1 
HETATM 9129 O  O   . HOH G 7 .    ? 19.418 82.833  -34.334 1.00 48.67 ? 2581 HOH A O   1 
HETATM 9130 O  O   . HOH G 7 .    ? 23.254 82.207  -40.440 1.00 31.27 ? 2582 HOH A O   1 
HETATM 9131 O  O   . HOH G 7 .    ? 25.916 87.308  -42.897 1.00 46.32 ? 2583 HOH A O   1 
HETATM 9132 O  O   . HOH G 7 .    ? 28.322 87.370  -41.596 1.00 37.28 ? 2584 HOH A O   1 
HETATM 9133 O  O   . HOH G 7 .    ? 28.340 90.166  -42.771 1.00 34.53 ? 2585 HOH A O   1 
HETATM 9134 O  O   . HOH G 7 .    ? 32.560 88.661  -43.246 1.00 28.74 ? 2586 HOH A O   1 
HETATM 9135 O  O   . HOH G 7 .    ? 33.985 86.403  -43.521 1.00 44.81 ? 2587 HOH A O   1 
HETATM 9136 O  O   . HOH G 7 .    ? 32.757 89.748  -45.732 1.00 38.81 ? 2588 HOH A O   1 
HETATM 9137 O  O   . HOH G 7 .    ? 38.629 93.508  -42.326 1.00 29.62 ? 2589 HOH A O   1 
HETATM 9138 O  O   . HOH G 7 .    ? 42.047 87.283  -41.014 1.00 20.48 ? 2590 HOH A O   1 
HETATM 9139 O  O   . HOH G 7 .    ? 43.624 87.983  -38.629 1.00 21.00 ? 2591 HOH A O   1 
HETATM 9140 O  O   . HOH G 7 .    ? 38.931 85.999  -41.501 1.00 35.41 ? 2592 HOH A O   1 
HETATM 9141 O  O   . HOH G 7 .    ? 38.673 83.016  -39.697 1.00 28.29 ? 2593 HOH A O   1 
HETATM 9142 O  O   . HOH G 7 .    ? 37.012 81.990  -41.369 1.00 42.15 ? 2594 HOH A O   1 
HETATM 9143 O  O   . HOH G 7 .    ? 35.774 76.865  -43.068 1.00 38.50 ? 2595 HOH A O   1 
HETATM 9144 O  O   . HOH G 7 .    ? 37.695 75.169  -42.151 1.00 28.86 ? 2596 HOH A O   1 
HETATM 9145 O  O   . HOH G 7 .    ? 39.639 75.186  -40.202 1.00 22.96 ? 2597 HOH A O   1 
HETATM 9146 O  O   . HOH G 7 .    ? 42.181 74.419  -41.362 1.00 31.70 ? 2598 HOH A O   1 
HETATM 9147 O  O   . HOH G 7 .    ? 43.687 72.140  -41.883 1.00 27.51 ? 2599 HOH A O   1 
HETATM 9148 O  O   . HOH G 7 .    ? 44.566 71.461  -44.516 1.00 46.26 ? 2600 HOH A O   1 
HETATM 9149 O  O   . HOH G 7 .    ? 46.172 69.815  -39.842 1.00 41.89 ? 2601 HOH A O   1 
HETATM 9150 O  O   . HOH G 7 .    ? 46.570 69.901  -36.573 1.00 25.13 ? 2602 HOH A O   1 
HETATM 9151 O  O   . HOH G 7 .    ? 48.974 68.694  -36.845 1.00 34.72 ? 2603 HOH A O   1 
HETATM 9152 O  O   . HOH G 7 .    ? 51.636 69.807  -38.180 1.00 31.76 ? 2604 HOH A O   1 
HETATM 9153 O  O   . HOH G 7 .    ? 53.935 70.865  -36.816 1.00 19.70 ? 2605 HOH A O   1 
HETATM 9154 O  O   . HOH G 7 .    ? 55.513 68.693  -37.705 1.00 39.36 ? 2606 HOH A O   1 
HETATM 9155 O  O   . HOH G 7 .    ? 56.774 69.595  -39.667 1.00 36.83 ? 2607 HOH A O   1 
HETATM 9156 O  O   . HOH G 7 .    ? 60.087 68.340  -38.776 1.00 34.11 ? 2608 HOH A O   1 
HETATM 9157 O  O   . HOH G 7 .    ? 61.105 67.138  -36.659 1.00 38.16 ? 2609 HOH A O   1 
HETATM 9158 O  O   . HOH G 7 .    ? 59.359 66.999  -34.667 1.00 32.81 ? 2610 HOH A O   1 
HETATM 9159 O  O   . HOH G 7 .    ? 56.859 67.392  -35.444 1.00 26.18 ? 2611 HOH A O   1 
HETATM 9160 O  O   . HOH G 7 .    ? 56.097 64.791  -36.006 1.00 29.02 ? 2612 HOH A O   1 
HETATM 9161 O  O   . HOH G 7 .    ? 52.769 58.912  -32.422 1.00 42.81 ? 2613 HOH A O   1 
HETATM 9162 O  O   . HOH G 7 .    ? 50.400 60.986  -30.948 1.00 29.72 ? 2614 HOH A O   1 
HETATM 9163 O  O   . HOH G 7 .    ? 47.335 57.380  -32.108 1.00 42.44 ? 2615 HOH A O   1 
HETATM 9164 O  O   . HOH G 7 .    ? 42.789 56.480  -31.472 1.00 28.35 ? 2616 HOH A O   1 
HETATM 9165 O  O   . HOH G 7 .    ? 42.773 59.165  -31.308 1.00 29.73 ? 2617 HOH A O   1 
HETATM 9166 O  O   . HOH G 7 .    ? 41.656 60.900  -29.525 1.00 22.33 ? 2618 HOH A O   1 
HETATM 9167 O  O   . HOH G 7 .    ? 43.553 62.427  -28.333 1.00 25.72 ? 2619 HOH A O   1 
HETATM 9168 O  O   . HOH G 7 .    ? 43.366 63.323  -32.179 1.00 38.20 ? 2620 HOH A O   1 
HETATM 9169 O  O   . HOH G 7 .    ? 40.821 62.383  -31.702 1.00 26.02 ? 2621 HOH A O   1 
HETATM 9170 O  O   . HOH G 7 .    ? 37.542 61.053  -32.336 1.00 30.24 ? 2622 HOH A O   1 
HETATM 9171 O  O   . HOH G 7 .    ? 36.889 58.663  -33.380 1.00 33.10 ? 2623 HOH A O   1 
HETATM 9172 O  O   . HOH G 7 .    ? 34.723 59.223  -34.812 1.00 28.53 ? 2624 HOH A O   1 
HETATM 9173 O  O   . HOH G 7 .    ? 33.505 56.720  -35.861 1.00 21.18 ? 2625 HOH A O   1 
HETATM 9174 O  O   . HOH G 7 .    ? 35.341 55.031  -34.568 1.00 39.28 ? 2626 HOH A O   1 
HETATM 9175 O  O   . HOH G 7 .    ? 37.232 52.448  -32.252 1.00 33.29 ? 2627 HOH A O   1 
HETATM 9176 O  O   . HOH G 7 .    ? 38.477 54.818  -31.526 1.00 21.15 ? 2628 HOH A O   1 
HETATM 9177 O  O   . HOH G 7 .    ? 40.716 55.521  -33.190 1.00 31.33 ? 2629 HOH A O   1 
HETATM 9178 O  O   . HOH G 7 .    ? 38.420 51.103  -29.703 1.00 28.48 ? 2630 HOH A O   1 
HETATM 9179 O  O   . HOH G 7 .    ? 43.710 54.748  -26.742 1.00 38.46 ? 2631 HOH A O   1 
HETATM 9180 O  O   . HOH G 7 .    ? 51.315 53.056  -23.800 1.00 17.43 ? 2632 HOH A O   1 
HETATM 9181 O  O   . HOH G 7 .    ? 58.831 53.429  -22.086 1.00 24.35 ? 2633 HOH A O   1 
HETATM 9182 O  O   . HOH G 7 .    ? 61.318 54.015  -28.719 1.00 28.44 ? 2634 HOH A O   1 
HETATM 9183 O  O   . HOH G 7 .    ? 59.844 52.747  -30.497 1.00 37.06 ? 2635 HOH A O   1 
HETATM 9184 O  O   . HOH G 7 .    ? 56.417 49.794  -30.135 1.00 45.62 ? 2636 HOH A O   1 
HETATM 9185 O  O   . HOH G 7 .    ? 58.417 43.962  -27.983 1.00 42.06 ? 2637 HOH A O   1 
HETATM 9186 O  O   . HOH G 7 .    ? 58.278 37.060  -17.974 1.00 48.30 ? 2638 HOH A O   1 
HETATM 9187 O  O   . HOH G 7 .    ? 59.338 37.429  -15.144 1.00 32.53 ? 2639 HOH A O   1 
HETATM 9188 O  O   . HOH G 7 .    ? 57.204 35.867  -14.139 1.00 31.83 ? 2640 HOH A O   1 
HETATM 9189 O  O   . HOH G 7 .    ? 58.420 34.634  -12.025 1.00 40.72 ? 2641 HOH A O   1 
HETATM 9190 O  O   . HOH G 7 .    ? 58.119 34.636  -6.055  1.00 42.48 ? 2642 HOH A O   1 
HETATM 9191 O  O   . HOH G 7 .    ? 57.887 42.129  1.755   1.00 26.82 ? 2643 HOH A O   1 
HETATM 9192 O  O   . HOH G 7 .    ? 59.378 44.706  5.067   1.00 42.77 ? 2644 HOH A O   1 
HETATM 9193 O  O   . HOH G 7 .    ? 58.824 46.141  -1.315  1.00 27.40 ? 2645 HOH A O   1 
HETATM 9194 O  O   . HOH G 7 .    ? 61.069 45.090  -3.668  1.00 34.95 ? 2646 HOH A O   1 
HETATM 9195 O  O   . HOH G 7 .    ? 70.823 49.157  -0.023  1.00 27.84 ? 2647 HOH A O   1 
HETATM 9196 O  O   . HOH G 7 .    ? 72.247 50.198  1.702   1.00 48.29 ? 2648 HOH A O   1 
HETATM 9197 O  O   . HOH G 7 .    ? 74.244 51.965  1.637   1.00 39.43 ? 2649 HOH A O   1 
HETATM 9198 O  O   . HOH G 7 .    ? 79.571 51.179  -0.402  1.00 30.68 ? 2650 HOH A O   1 
HETATM 9199 O  O   . HOH G 7 .    ? 75.743 48.300  -5.474  1.00 44.70 ? 2651 HOH A O   1 
HETATM 9200 O  O   . HOH G 7 .    ? 73.653 46.288  -5.331  1.00 47.05 ? 2652 HOH A O   1 
HETATM 9201 O  O   . HOH G 7 .    ? 76.435 46.792  -11.466 1.00 32.23 ? 2653 HOH A O   1 
HETATM 9202 O  O   . HOH G 7 .    ? 79.375 50.652  -11.220 1.00 52.47 ? 2654 HOH A O   1 
HETATM 9203 O  O   . HOH G 7 .    ? 79.300 50.436  -8.875  1.00 35.20 ? 2655 HOH A O   1 
HETATM 9204 O  O   . HOH G 7 .    ? 78.353 53.298  -11.945 1.00 34.88 ? 2656 HOH A O   1 
HETATM 9205 O  O   . HOH G 7 .    ? 73.912 53.606  -13.658 1.00 46.25 ? 2657 HOH A O   1 
HETATM 9206 O  O   . HOH G 7 .    ? 75.204 52.409  -15.534 1.00 39.38 ? 2658 HOH A O   1 
HETATM 9207 O  O   . HOH G 7 .    ? 71.047 54.103  -13.839 1.00 32.68 ? 2659 HOH A O   1 
HETATM 9208 O  O   . HOH G 7 .    ? 70.327 56.152  -12.333 1.00 34.84 ? 2660 HOH A O   1 
HETATM 9209 O  O   . HOH G 7 .    ? 72.090 58.462  -11.120 1.00 30.03 ? 2661 HOH A O   1 
HETATM 9210 O  O   . HOH G 7 .    ? 74.164 59.868  -9.439  1.00 36.97 ? 2662 HOH A O   1 
HETATM 9211 O  O   . HOH G 7 .    ? 73.050 64.784  -7.711  1.00 25.94 ? 2663 HOH A O   1 
HETATM 9212 O  O   . HOH G 7 .    ? 72.842 66.334  -9.986  1.00 29.56 ? 2664 HOH A O   1 
HETATM 9213 O  O   . HOH G 7 .    ? 69.928 69.659  -12.566 1.00 18.78 ? 2665 HOH A O   1 
HETATM 9214 O  O   . HOH G 7 .    ? 73.885 65.700  -17.453 1.00 21.99 ? 2666 HOH A O   1 
HETATM 9215 O  O   . HOH G 7 .    ? 75.217 63.913  -16.264 1.00 33.95 ? 2667 HOH A O   1 
HETATM 9216 O  O   . HOH G 7 .    ? 79.650 67.785  -15.193 1.00 36.88 ? 2668 HOH A O   1 
HETATM 9217 O  O   . HOH G 7 .    ? 79.855 73.650  -17.516 1.00 35.63 ? 2669 HOH A O   1 
HETATM 9218 O  O   . HOH G 7 .    ? 77.505 75.052  -17.539 1.00 37.46 ? 2670 HOH A O   1 
HETATM 9219 O  O   . HOH G 7 .    ? 75.405 73.887  -19.400 1.00 28.51 ? 2671 HOH A O   1 
HETATM 9220 O  O   . HOH G 7 .    ? 75.266 73.597  -16.070 1.00 35.30 ? 2672 HOH A O   1 
HETATM 9221 O  O   . HOH G 7 .    ? 74.759 75.983  -14.481 1.00 32.35 ? 2673 HOH A O   1 
HETATM 9222 O  O   . HOH G 7 .    ? 73.732 78.301  -13.290 1.00 45.64 ? 2674 HOH A O   1 
HETATM 9223 O  O   . HOH G 7 .    ? 73.679 79.949  -10.703 1.00 47.22 ? 2675 HOH A O   1 
HETATM 9224 O  O   . HOH G 7 .    ? 69.904 83.516  -17.418 1.00 51.07 ? 2676 HOH A O   1 
HETATM 9225 O  O   . HOH G 7 .    ? 71.590 84.245  -20.060 1.00 33.73 ? 2677 HOH A O   1 
HETATM 9226 O  O   . HOH G 7 .    ? 73.227 82.005  -21.198 1.00 31.36 ? 2678 HOH A O   1 
HETATM 9227 O  O   . HOH G 7 .    ? 73.946 86.284  -23.278 1.00 47.48 ? 2679 HOH A O   1 
HETATM 9228 O  O   . HOH G 7 .    ? 71.314 81.953  -27.636 1.00 38.47 ? 2680 HOH A O   1 
HETATM 9229 O  O   . HOH G 7 .    ? 69.967 82.701  -29.776 1.00 26.04 ? 2681 HOH A O   1 
HETATM 9230 O  O   . HOH G 7 .    ? 68.435 79.130  -28.562 1.00 27.40 ? 2682 HOH A O   1 
HETATM 9231 O  O   . HOH G 7 .    ? 76.522 73.599  -26.772 1.00 41.91 ? 2683 HOH A O   1 
HETATM 9232 O  O   . HOH G 7 .    ? 74.706 77.052  -20.695 1.00 39.43 ? 2684 HOH A O   1 
HETATM 9233 O  O   . HOH G 7 .    ? 73.304 76.516  -18.492 1.00 35.11 ? 2685 HOH A O   1 
HETATM 9234 O  O   . HOH G 7 .    ? 68.482 78.498  -18.146 1.00 28.53 ? 2686 HOH A O   1 
HETATM 9235 O  O   . HOH G 7 .    ? 60.103 83.600  -16.701 1.00 42.88 ? 2687 HOH A O   1 
HETATM 9236 O  O   . HOH G 7 .    ? 56.826 87.396  -20.131 1.00 33.61 ? 2688 HOH A O   1 
HETATM 9237 O  O   . HOH G 7 .    ? 53.118 86.487  -21.431 1.00 32.53 ? 2689 HOH A O   1 
HETATM 9238 O  O   . HOH G 7 .    ? 54.882 80.728  -23.603 1.00 17.08 ? 2690 HOH A O   1 
HETATM 9239 O  O   . HOH G 7 .    ? 49.907 73.299  -21.762 1.00 33.76 ? 2691 HOH A O   1 
HETATM 9240 O  O   . HOH G 7 .    ? 44.959 71.544  -25.660 1.00 47.19 ? 2692 HOH A O   1 
HETATM 9241 O  O   . HOH G 7 .    ? 43.433 68.020  -25.211 1.00 19.36 ? 2693 HOH A O   1 
HETATM 9242 O  O   . HOH G 7 .    ? 45.900 67.777  -26.907 1.00 20.55 ? 2694 HOH A O   1 
HETATM 9243 O  O   . HOH G 7 .    ? 47.114 67.476  -24.591 1.00 28.53 ? 2695 HOH A O   1 
HETATM 9244 O  O   . HOH G 7 .    ? 47.889 64.691  -27.585 1.00 39.23 ? 2696 HOH A O   1 
HETATM 9245 O  O   . HOH G 7 .    ? 47.392 67.896  -30.776 1.00 22.51 ? 2697 HOH A O   1 
HETATM 9246 O  O   . HOH G 7 .    ? 47.306 69.739  -28.520 1.00 27.35 ? 2698 HOH A O   1 
HETATM 9247 O  O   . HOH G 7 .    ? 43.396 66.448  -32.275 1.00 32.82 ? 2699 HOH A O   1 
HETATM 9248 O  O   . HOH G 7 .    ? 41.288 67.978  -32.357 1.00 23.87 ? 2700 HOH A O   1 
HETATM 9249 O  O   . HOH G 7 .    ? 39.328 68.721  -35.300 1.00 22.46 ? 2701 HOH A O   1 
HETATM 9250 O  O   . HOH G 7 .    ? 38.551 68.753  -38.065 1.00 22.53 ? 2702 HOH A O   1 
HETATM 9251 O  O   . HOH G 7 .    ? 34.633 65.513  -42.206 1.00 38.46 ? 2703 HOH A O   1 
HETATM 9252 O  O   . HOH G 7 .    ? 34.434 69.808  -44.802 1.00 46.36 ? 2704 HOH A O   1 
HETATM 9253 O  O   . HOH G 7 .    ? 30.899 68.992  -45.489 1.00 42.74 ? 2705 HOH A O   1 
HETATM 9254 O  O   . HOH G 7 .    ? 27.939 67.600  -46.861 1.00 41.72 ? 2706 HOH A O   1 
HETATM 9255 O  O   . HOH G 7 .    ? 23.797 64.970  -43.647 1.00 45.34 ? 2707 HOH A O   1 
HETATM 9256 O  O   . HOH G 7 .    ? 28.942 61.901  -39.701 1.00 28.53 ? 2708 HOH A O   1 
HETATM 9257 O  O   . HOH G 7 .    ? 28.442 59.443  -38.978 1.00 37.51 ? 2709 HOH A O   1 
HETATM 9258 O  O   . HOH G 7 .    ? 31.089 57.975  -40.290 1.00 47.09 ? 2710 HOH A O   1 
HETATM 9259 O  O   . HOH G 7 .    ? 36.260 62.268  -38.391 1.00 33.95 ? 2711 HOH A O   1 
HETATM 9260 O  O   . HOH G 7 .    ? 35.924 62.998  -33.601 1.00 39.10 ? 2712 HOH A O   1 
HETATM 9261 O  O   . HOH G 7 .    ? 34.039 64.106  -32.181 1.00 18.54 ? 2713 HOH A O   1 
HETATM 9262 O  O   . HOH G 7 .    ? 32.040 58.241  -28.379 1.00 18.24 ? 2714 HOH A O   1 
HETATM 9263 O  O   . HOH G 7 .    ? 34.042 55.994  -26.180 1.00 15.54 ? 2715 HOH A O   1 
HETATM 9264 O  O   . HOH G 7 .    ? 31.831 50.930  -35.323 1.00 29.46 ? 2716 HOH A O   1 
HETATM 9265 O  O   . HOH G 7 .    ? 28.877 69.305  -39.562 1.00 28.69 ? 2717 HOH A O   1 
HETATM 9266 O  O   . HOH G 7 .    ? 24.707 71.180  -39.913 1.00 34.56 ? 2718 HOH A O   1 
HETATM 9267 O  O   . HOH G 7 .    ? 31.126 78.384  -42.961 1.00 35.68 ? 2719 HOH A O   1 
HETATM 9268 O  O   . HOH G 7 .    ? 30.202 81.250  -42.896 1.00 48.09 ? 2720 HOH A O   1 
HETATM 9269 O  O   . HOH G 7 .    ? 28.973 81.413  -35.616 1.00 23.23 ? 2721 HOH A O   1 
HETATM 9270 O  O   . HOH G 7 .    ? 28.029 84.107  -35.470 1.00 21.33 ? 2722 HOH A O   1 
HETATM 9271 O  O   . HOH G 7 .    ? 23.269 88.306  -38.329 1.00 40.05 ? 2723 HOH A O   1 
HETATM 9272 O  O   . HOH G 7 .    ? 28.922 93.287  -38.693 1.00 29.78 ? 2724 HOH A O   1 
HETATM 9273 O  O   . HOH G 7 .    ? 32.040 92.102  -36.833 1.00 30.67 ? 2725 HOH A O   1 
HETATM 9274 O  O   . HOH G 7 .    ? 34.998 94.556  -32.304 1.00 34.14 ? 2726 HOH A O   1 
HETATM 9275 O  O   . HOH G 7 .    ? 36.041 93.263  -30.039 1.00 37.72 ? 2727 HOH A O   1 
HETATM 9276 O  O   . HOH G 7 .    ? 31.799 96.611  -27.400 1.00 40.31 ? 2728 HOH A O   1 
HETATM 9277 O  O   . HOH G 7 .    ? 27.857 101.748 -19.250 1.00 34.75 ? 2729 HOH A O   1 
HETATM 9278 O  O   . HOH G 7 .    ? 27.188 88.158  -12.564 1.00 34.13 ? 2730 HOH A O   1 
HETATM 9279 O  O   . HOH G 7 .    ? 32.088 84.867  -8.438  1.00 25.33 ? 2731 HOH A O   1 
HETATM 9280 O  O   . HOH G 7 .    ? 33.562 83.257  -10.356 1.00 19.12 ? 2732 HOH A O   1 
HETATM 9281 O  O   . HOH G 7 .    ? 32.734 80.754  -11.667 1.00 15.04 ? 2733 HOH A O   1 
HETATM 9282 O  O   . HOH G 7 .    ? 34.530 78.833  -9.120  1.00 15.19 ? 2734 HOH A O   1 
HETATM 9283 O  O   . HOH G 7 .    ? 35.816 77.290  -7.278  1.00 17.78 ? 2735 HOH A O   1 
HETATM 9284 O  O   . HOH G 7 .    ? 36.286 78.992  -4.996  1.00 23.42 ? 2736 HOH A O   1 
HETATM 9285 O  O   . HOH G 7 .    ? 33.380 78.385  -5.073  1.00 17.50 ? 2737 HOH A O   1 
HETATM 9286 O  O   . HOH G 7 .    ? 31.399 76.452  -6.252  1.00 16.00 ? 2738 HOH A O   1 
HETATM 9287 O  O   . HOH G 7 .    ? 37.045 71.595  -4.541  1.00 13.27 ? 2739 HOH A O   1 
HETATM 9288 O  O   . HOH G 7 .    ? 37.902 73.106  -2.275  1.00 14.84 ? 2740 HOH A O   1 
HETATM 9289 O  O   . HOH G 7 .    ? 36.583 72.433  0.246   1.00 13.32 ? 2741 HOH A O   1 
HETATM 9290 O  O   . HOH G 7 .    ? 37.619 80.254  -0.647  1.00 26.52 ? 2742 HOH A O   1 
HETATM 9291 O  O   . HOH G 7 .    ? 38.740 80.040  -3.015  1.00 33.16 ? 2743 HOH A O   1 
HETATM 9292 O  O   . HOH G 7 .    ? 38.020 82.864  -0.861  1.00 31.11 ? 2744 HOH A O   1 
HETATM 9293 O  O   . HOH G 7 .    ? 37.329 83.291  -4.083  1.00 30.69 ? 2745 HOH A O   1 
HETATM 9294 O  O   . HOH G 7 .    ? 34.964 85.114  -0.915  1.00 47.72 ? 2746 HOH A O   1 
HETATM 9295 O  O   . HOH G 7 .    ? 32.783 84.000  0.296   1.00 34.50 ? 2747 HOH A O   1 
HETATM 9296 O  O   . HOH G 7 .    ? 31.320 81.469  0.530   1.00 22.32 ? 2748 HOH A O   1 
HETATM 9297 O  O   . HOH G 7 .    ? 24.794 83.561  2.644   1.00 35.14 ? 2749 HOH A O   1 
HETATM 9298 O  O   . HOH G 7 .    ? 21.162 86.608  -2.556  1.00 44.23 ? 2750 HOH A O   1 
HETATM 9299 O  O   . HOH G 7 .    ? 18.664 84.593  -4.889  1.00 46.57 ? 2751 HOH A O   1 
HETATM 9300 O  O   . HOH G 7 .    ? 18.198 84.415  -7.979  1.00 44.96 ? 2752 HOH A O   1 
HETATM 9301 O  O   . HOH G 7 .    ? 17.249 80.433  -7.381  1.00 29.31 ? 2753 HOH A O   1 
HETATM 9302 O  O   . HOH G 7 .    ? 18.815 80.347  -11.762 1.00 40.53 ? 2754 HOH A O   1 
HETATM 9303 O  O   . HOH G 7 .    ? 20.907 83.537  -12.497 1.00 36.50 ? 2755 HOH A O   1 
HETATM 9304 O  O   . HOH G 7 .    ? 17.422 81.118  -17.155 1.00 41.87 ? 2756 HOH A O   1 
HETATM 9305 O  O   . HOH G 7 .    ? 15.272 76.634  -13.599 1.00 35.98 ? 2757 HOH A O   1 
HETATM 9306 O  O   . HOH G 7 .    ? 15.854 74.923  -11.470 1.00 26.64 ? 2758 HOH A O   1 
HETATM 9307 O  O   . HOH G 7 .    ? 12.251 74.903  -13.264 1.00 33.29 ? 2759 HOH A O   1 
HETATM 9308 O  O   . HOH G 7 .    ? 12.958 74.408  -18.948 1.00 40.02 ? 2760 HOH A O   1 
HETATM 9309 O  O   . HOH G 7 .    ? 13.903 87.907  -19.876 1.00 40.81 ? 2761 HOH A O   1 
HETATM 9310 O  O   . HOH G 7 .    ? 7.871  80.895  -4.240  1.00 38.53 ? 2762 HOH A O   1 
HETATM 9311 O  O   . HOH G 7 .    ? 5.374  80.762  -3.417  1.00 38.17 ? 2763 HOH A O   1 
HETATM 9312 O  O   . HOH G 7 .    ? 10.552 76.737  -4.681  1.00 38.00 ? 2764 HOH A O   1 
HETATM 9313 O  O   . HOH G 7 .    ? 12.640 70.714  -0.259  1.00 27.81 ? 2765 HOH A O   1 
HETATM 9314 O  O   . HOH G 7 .    ? 13.294 68.415  1.117   1.00 25.83 ? 2766 HOH A O   1 
HETATM 9315 O  O   . HOH G 7 .    ? 10.635 67.879  -2.053  1.00 36.12 ? 2767 HOH A O   1 
HETATM 9316 O  O   . HOH G 7 .    ? 7.897  58.098  0.099   1.00 40.28 ? 2768 HOH A O   1 
HETATM 9317 O  O   . HOH G 7 .    ? 8.636  57.340  -6.747  1.00 30.34 ? 2769 HOH A O   1 
HETATM 9318 O  O   . HOH G 7 .    ? 8.704  54.595  -6.072  1.00 31.05 ? 2770 HOH A O   1 
HETATM 9319 O  O   . HOH G 7 .    ? 7.915  52.529  -7.369  1.00 47.99 ? 2771 HOH A O   1 
HETATM 9320 O  O   . HOH G 7 .    ? 7.535  53.837  -10.012 1.00 32.16 ? 2772 HOH A O   1 
HETATM 9321 O  O   . HOH G 7 .    ? 5.040  52.584  -6.101  1.00 36.05 ? 2773 HOH A O   1 
HETATM 9322 O  O   . HOH G 7 .    ? 4.283  56.230  -6.358  1.00 35.88 ? 2774 HOH A O   1 
HETATM 9323 O  O   . HOH G 7 .    ? 11.744 54.813  -12.224 1.00 21.59 ? 2775 HOH A O   1 
HETATM 9324 O  O   . HOH G 7 .    ? 12.281 55.532  -15.069 1.00 22.05 ? 2776 HOH A O   1 
HETATM 9325 O  O   . HOH G 7 .    ? 14.317 54.074  -16.089 1.00 23.96 ? 2777 HOH A O   1 
HETATM 9326 O  O   . HOH G 7 .    ? 13.211 51.828  -15.107 1.00 33.66 ? 2778 HOH A O   1 
HETATM 9327 O  O   . HOH G 7 .    ? 12.750 51.452  -12.067 1.00 34.53 ? 2779 HOH A O   1 
HETATM 9328 O  O   . HOH G 7 .    ? 9.465  47.588  -8.407  1.00 43.48 ? 2780 HOH A O   1 
HETATM 9329 O  O   . HOH G 7 .    ? 11.685 47.886  -2.262  1.00 35.21 ? 2781 HOH A O   1 
HETATM 9330 O  O   . HOH G 7 .    ? 13.363 50.553  -1.479  1.00 26.49 ? 2782 HOH A O   1 
HETATM 9331 O  O   . HOH G 7 .    ? 14.293 50.482  1.150   1.00 29.80 ? 2783 HOH A O   1 
HETATM 9332 O  O   . HOH G 7 .    ? 13.345 48.220  1.773   1.00 35.33 ? 2784 HOH A O   1 
HETATM 9333 O  O   . HOH G 7 .    ? 10.437 51.353  2.577   1.00 32.39 ? 2785 HOH A O   1 
HETATM 9334 O  O   . HOH G 7 .    ? 10.934 53.448  4.260   1.00 35.71 ? 2786 HOH A O   1 
HETATM 9335 O  O   . HOH G 7 .    ? 11.339 52.959  6.956   1.00 22.16 ? 2787 HOH A O   1 
HETATM 9336 O  O   . HOH G 7 .    ? 13.783 53.921  4.551   1.00 19.48 ? 2788 HOH A O   1 
HETATM 9337 O  O   . HOH G 7 .    ? 13.467 53.199  1.949   1.00 22.03 ? 2789 HOH A O   1 
HETATM 9338 O  O   . HOH G 7 .    ? 12.386 56.102  5.441   1.00 20.51 ? 2790 HOH A O   1 
HETATM 9339 O  O   . HOH G 7 .    ? 5.497  57.585  7.204   1.00 37.45 ? 2791 HOH A O   1 
HETATM 9340 O  O   . HOH G 7 .    ? 8.998  50.114  8.227   1.00 34.33 ? 2792 HOH A O   1 
HETATM 9341 O  O   . HOH G 7 .    ? 6.416  46.259  16.621  1.00 39.85 ? 2793 HOH A O   1 
HETATM 9342 O  O   . HOH G 7 .    ? 12.125 41.208  20.065  1.00 33.45 ? 2794 HOH A O   1 
HETATM 9343 O  O   . HOH G 7 .    ? 18.058 41.680  25.462  1.00 31.71 ? 2795 HOH A O   1 
HETATM 9344 O  O   . HOH G 7 .    ? 18.141 43.003  27.561  1.00 37.64 ? 2796 HOH A O   1 
HETATM 9345 O  O   . HOH G 7 .    ? 19.060 39.657  26.662  1.00 34.19 ? 2797 HOH A O   1 
HETATM 9346 O  O   . HOH G 7 .    ? 19.803 35.505  25.739  1.00 35.79 ? 2798 HOH A O   1 
HETATM 9347 O  O   . HOH G 7 .    ? 22.699 31.187  29.755  1.00 36.32 ? 2799 HOH A O   1 
HETATM 9348 O  O   . HOH G 7 .    ? 20.764 31.495  31.554  1.00 42.45 ? 2800 HOH A O   1 
HETATM 9349 O  O   . HOH G 7 .    ? 21.882 29.018  28.343  1.00 41.57 ? 2801 HOH A O   1 
HETATM 9350 O  O   . HOH G 7 .    ? 26.131 32.668  29.011  1.00 30.41 ? 2802 HOH A O   1 
HETATM 9351 O  O   . HOH G 7 .    ? 27.286 34.883  29.626  1.00 28.73 ? 2803 HOH A O   1 
HETATM 9352 O  O   . HOH G 7 .    ? 26.313 37.258  29.588  1.00 23.47 ? 2804 HOH A O   1 
HETATM 9353 O  O   . HOH G 7 .    ? 30.192 36.504  29.125  1.00 27.22 ? 2805 HOH A O   1 
HETATM 9354 O  O   . HOH G 7 .    ? 28.440 34.937  32.230  1.00 42.93 ? 2806 HOH A O   1 
HETATM 9355 O  O   . HOH G 7 .    ? 24.736 34.352  35.910  1.00 41.79 ? 2807 HOH A O   1 
HETATM 9356 O  O   . HOH G 7 .    ? 22.292 34.987  34.953  1.00 40.28 ? 2808 HOH A O   1 
HETATM 9357 O  O   . HOH G 7 .    ? 17.881 39.498  35.772  1.00 44.36 ? 2809 HOH A O   1 
HETATM 9358 O  O   . HOH G 7 .    ? 21.180 41.600  35.376  1.00 36.24 ? 2810 HOH A O   1 
HETATM 9359 O  O   . HOH G 7 .    ? 19.859 43.161  34.036  1.00 29.94 ? 2811 HOH A O   1 
HETATM 9360 O  O   . HOH G 7 .    ? 17.214 41.664  32.394  1.00 42.37 ? 2812 HOH A O   1 
HETATM 9361 O  O   . HOH G 7 .    ? 14.577 47.016  32.485  1.00 35.94 ? 2813 HOH A O   1 
HETATM 9362 O  O   . HOH G 7 .    ? 12.355 47.484  31.347  1.00 38.56 ? 2814 HOH A O   1 
HETATM 9363 O  O   . HOH G 7 .    ? 16.521 48.882  24.195  1.00 19.88 ? 2815 HOH A O   1 
HETATM 9364 O  O   . HOH G 7 .    ? 14.612 55.568  27.453  1.00 29.97 ? 2816 HOH A O   1 
HETATM 9365 O  O   . HOH G 7 .    ? 18.437 58.968  31.701  1.00 39.72 ? 2817 HOH A O   1 
HETATM 9366 O  O   . HOH G 7 .    ? 23.082 55.906  30.826  1.00 21.67 ? 2818 HOH A O   1 
HETATM 9367 O  O   . HOH G 7 .    ? 18.115 60.451  24.474  1.00 21.98 ? 2819 HOH A O   1 
HETATM 9368 O  O   . HOH G 7 .    ? 17.864 65.955  27.799  1.00 33.56 ? 2820 HOH A O   1 
HETATM 9369 O  O   . HOH G 7 .    ? 16.962 66.086  29.906  1.00 46.15 ? 2821 HOH A O   1 
HETATM 9370 O  O   . HOH G 7 .    ? 14.081 63.084  30.176  1.00 49.01 ? 2822 HOH A O   1 
HETATM 9371 O  O   . HOH G 7 .    ? 14.061 69.241  26.957  1.00 29.68 ? 2823 HOH A O   1 
HETATM 9372 O  O   . HOH G 7 .    ? 15.047 69.669  24.383  1.00 45.09 ? 2824 HOH A O   1 
HETATM 9373 O  O   . HOH G 7 .    ? 11.028 69.306  26.263  1.00 36.79 ? 2825 HOH A O   1 
HETATM 9374 O  O   . HOH G 7 .    ? 13.768 62.112  14.767  1.00 31.79 ? 2826 HOH A O   1 
HETATM 9375 O  O   . HOH G 7 .    ? 13.161 62.477  11.999  1.00 35.77 ? 2827 HOH A O   1 
HETATM 9376 O  O   . HOH G 7 .    ? 27.661 53.203  20.159  1.00 18.59 ? 2828 HOH A O   1 
HETATM 9377 O  O   . HOH G 7 .    ? 27.001 52.099  22.649  1.00 28.76 ? 2829 HOH A O   1 
HETATM 9378 O  O   . HOH G 7 .    ? 27.392 50.036  23.325  1.00 31.52 ? 2830 HOH A O   1 
HETATM 9379 O  O   . HOH G 7 .    ? 30.155 55.590  17.280  1.00 14.12 ? 2831 HOH A O   1 
HETATM 9380 O  O   . HOH G 7 .    ? 33.688 60.134  23.294  1.00 16.46 ? 2832 HOH A O   1 
HETATM 9381 O  O   . HOH G 7 .    ? 28.863 64.258  30.150  1.00 24.86 ? 2833 HOH A O   1 
HETATM 9382 O  O   . HOH G 7 .    ? 27.783 67.391  28.198  1.00 22.28 ? 2834 HOH A O   1 
HETATM 9383 O  O   . HOH G 7 .    ? 27.173 71.949  34.019  1.00 39.38 ? 2835 HOH A O   1 
HETATM 9384 O  O   . HOH G 7 .    ? 29.627 72.181  34.207  1.00 27.72 ? 2836 HOH A O   1 
HETATM 9385 O  O   . HOH G 7 .    ? 29.622 73.400  36.617  1.00 43.37 ? 2837 HOH A O   1 
HETATM 9386 O  O   . HOH G 7 .    ? 26.244 69.267  35.382  1.00 43.45 ? 2838 HOH A O   1 
HETATM 9387 O  O   . HOH G 7 .    ? 27.713 52.004  42.519  1.00 37.89 ? 2839 HOH A O   1 
HETATM 9388 O  O   . HOH G 7 .    ? 27.889 47.315  46.059  1.00 47.80 ? 2840 HOH A O   1 
HETATM 9389 O  O   . HOH G 7 .    ? 21.095 51.653  47.596  1.00 33.39 ? 2841 HOH A O   1 
HETATM 9390 O  O   . HOH G 7 .    ? 21.182 53.984  46.865  1.00 43.66 ? 2842 HOH A O   1 
HETATM 9391 O  O   . HOH G 7 .    ? 29.328 31.430  21.974  1.00 41.04 ? 2843 HOH A O   1 
HETATM 9392 O  O   . HOH G 7 .    ? 31.709 33.477  17.208  1.00 34.13 ? 2844 HOH A O   1 
HETATM 9393 O  O   . HOH G 7 .    ? 34.247 34.234  16.333  1.00 26.69 ? 2845 HOH A O   1 
HETATM 9394 O  O   . HOH G 7 .    ? 36.808 29.022  13.206  1.00 33.45 ? 2846 HOH A O   1 
HETATM 9395 O  O   . HOH G 7 .    ? 24.990 39.883  14.326  1.00 22.67 ? 2847 HOH A O   1 
HETATM 9396 O  O   . HOH G 7 .    ? 18.170 36.634  5.847   1.00 39.25 ? 2848 HOH A O   1 
HETATM 9397 O  O   . HOH G 7 .    ? 21.233 35.382  -5.069  1.00 37.76 ? 2849 HOH A O   1 
HETATM 9398 O  O   . HOH G 7 .    ? 15.865 44.722  -11.466 1.00 46.46 ? 2850 HOH A O   1 
HETATM 9399 O  O   . HOH G 7 .    ? 26.225 48.646  -10.853 1.00 14.66 ? 2851 HOH A O   1 
HETATM 9400 O  O   . HOH G 7 .    ? 26.058 49.358  -13.600 1.00 15.12 ? 2852 HOH A O   1 
HETATM 9401 O  O   . HOH G 7 .    ? 23.823 38.741  -20.858 1.00 40.15 ? 2853 HOH A O   1 
HETATM 9402 O  O   . HOH G 7 .    ? 44.608 33.136  -19.148 1.00 49.24 ? 2854 HOH A O   1 
HETATM 9403 O  O   . HOH G 7 .    ? 60.342 60.684  -18.044 1.00 15.39 ? 2855 HOH A O   1 
HETATM 9404 O  O   . HOH G 7 .    ? 53.623 64.554  -19.782 1.00 12.81 ? 2856 HOH A O   1 
HETATM 9405 O  O   . HOH G 7 .    ? 61.712 63.474  -30.562 1.00 33.12 ? 2857 HOH A O   1 
HETATM 9406 O  O   . HOH G 7 .    ? 63.545 67.580  -31.482 1.00 35.82 ? 2858 HOH A O   1 
HETATM 9407 O  O   . HOH G 7 .    ? 69.659 63.580  -28.521 1.00 30.30 ? 2859 HOH A O   1 
HETATM 9408 O  O   . HOH G 7 .    ? 66.804 59.693  -27.056 1.00 24.10 ? 2860 HOH A O   1 
HETATM 9409 O  O   . HOH G 7 .    ? 66.479 58.017  -30.902 1.00 44.28 ? 2861 HOH A O   1 
HETATM 9410 O  O   . HOH G 7 .    ? 69.975 58.763  -17.189 1.00 39.38 ? 2862 HOH A O   1 
HETATM 9411 O  O   . HOH G 7 .    ? 68.821 56.920  -16.604 1.00 39.38 ? 2863 HOH A O   1 
HETATM 9412 O  O   . HOH G 7 .    ? 70.581 51.842  -12.507 1.00 23.56 ? 2864 HOH A O   1 
HETATM 9413 O  O   . HOH G 7 .    ? 69.972 53.411  -10.154 1.00 36.55 ? 2865 HOH A O   1 
HETATM 9414 O  O   . HOH G 7 .    ? 66.499 62.311  -13.026 1.00 21.64 ? 2866 HOH A O   1 
HETATM 9415 O  O   . HOH G 7 .    ? 67.018 55.042  0.914   1.00 24.40 ? 2867 HOH A O   1 
HETATM 9416 O  O   . HOH G 7 .    ? 65.719 77.336  2.876   1.00 37.90 ? 2868 HOH A O   1 
HETATM 9417 O  O   . HOH G 7 .    ? 51.627 79.863  0.822   1.00 41.60 ? 2869 HOH A O   1 
HETATM 9418 O  O   . HOH G 7 .    ? 51.236 79.123  -1.812  1.00 28.92 ? 2870 HOH A O   1 
HETATM 9419 O  O   . HOH G 7 .    ? 48.019 80.095  -4.392  1.00 45.10 ? 2871 HOH A O   1 
HETATM 9420 O  O   . HOH G 7 .    ? 45.209 80.273  -1.528  1.00 35.65 ? 2872 HOH A O   1 
HETATM 9421 O  O   . HOH G 7 .    ? 46.468 82.396  -0.865  1.00 44.24 ? 2873 HOH A O   1 
HETATM 9422 O  O   . HOH G 7 .    ? 46.125 79.352  4.911   1.00 31.96 ? 2874 HOH A O   1 
HETATM 9423 O  O   . HOH G 7 .    ? 43.413 80.360  5.214   1.00 27.90 ? 2875 HOH A O   1 
HETATM 9424 O  O   . HOH G 7 .    ? 46.699 74.211  7.739   1.00 15.07 ? 2876 HOH A O   1 
HETATM 9425 O  O   . HOH G 7 .    ? 43.480 72.892  5.776   1.00 15.46 ? 2877 HOH A O   1 
HETATM 9426 O  O   . HOH G 7 .    ? 46.079 70.721  0.049   1.00 18.82 ? 2878 HOH A O   1 
HETATM 9427 O  O   . HOH G 7 .    ? 42.012 63.208  -7.121  1.00 10.55 ? 2879 HOH A O   1 
HETATM 9428 O  O   . HOH G 7 .    ? 42.107 74.946  -15.973 1.00 18.97 ? 2880 HOH A O   1 
HETATM 9429 O  O   . HOH G 7 .    ? 41.266 77.264  -14.089 1.00 17.98 ? 2881 HOH A O   1 
HETATM 9430 O  O   . HOH G 7 .    ? 35.466 85.868  -8.076  1.00 39.10 ? 2882 HOH A O   1 
HETATM 9431 O  O   . HOH G 7 .    ? 34.201 86.830  -10.319 1.00 34.29 ? 2883 HOH A O   1 
HETATM 9432 O  O   . HOH G 7 .    ? 32.801 85.069  -5.611  1.00 22.18 ? 2884 HOH A O   1 
HETATM 9433 O  O   . HOH G 7 .    ? 26.677 87.620  -3.809  1.00 39.82 ? 2885 HOH A O   1 
HETATM 9434 O  O   . HOH G 7 .    ? 51.789 81.717  -5.345  1.00 48.08 ? 2886 HOH A O   1 
HETATM 9435 O  O   . HOH G 7 .    ? 60.269 91.492  -28.577 1.00 37.50 ? 2887 HOH A O   1 
HETATM 9436 O  O   . HOH G 7 .    ? 72.268 95.183  -31.270 1.00 32.53 ? 2888 HOH A O   1 
HETATM 9437 O  O   . HOH G 7 .    ? 70.814 95.036  -35.074 1.00 38.31 ? 2889 HOH A O   1 
HETATM 9438 O  O   . HOH G 7 .    ? 58.292 76.851  -38.488 1.00 19.27 ? 2890 HOH A O   1 
HETATM 9439 O  O   . HOH G 7 .    ? 51.286 75.748  -40.854 1.00 35.27 ? 2891 HOH A O   1 
HETATM 9440 O  O   . HOH G 7 .    ? 47.476 78.554  -40.327 1.00 23.49 ? 2892 HOH A O   1 
HETATM 9441 O  O   . HOH G 7 .    ? 46.471 79.882  -42.552 1.00 26.54 ? 2893 HOH A O   1 
HETATM 9442 O  O   . HOH G 7 .    ? 43.808 79.553  -42.520 1.00 31.76 ? 2894 HOH A O   1 
HETATM 9443 O  O   . HOH G 7 .    ? 45.368 83.372  -42.965 1.00 39.05 ? 2895 HOH A O   1 
HETATM 9444 O  O   . HOH G 7 .    ? 49.744 81.877  -43.834 1.00 22.12 ? 2896 HOH A O   1 
HETATM 9445 O  O   . HOH G 7 .    ? 54.241 82.397  -44.305 1.00 49.48 ? 2897 HOH A O   1 
HETATM 9446 O  O   . HOH G 7 .    ? 48.596 95.603  -44.276 1.00 48.44 ? 2898 HOH A O   1 
HETATM 9447 O  O   . HOH G 7 .    ? 46.084 96.525  -43.872 1.00 31.61 ? 2899 HOH A O   1 
HETATM 9448 O  O   . HOH G 7 .    ? 32.364 77.299  -29.597 1.00 18.53 ? 2900 HOH A O   1 
HETATM 9449 O  O   . HOH G 7 .    ? 30.244 74.507  -29.182 1.00 16.79 ? 2901 HOH A O   1 
HETATM 9450 O  O   . HOH G 7 .    ? 44.971 66.049  -34.569 1.00 42.48 ? 2902 HOH A O   1 
HETATM 9451 O  O   . HOH G 7 .    ? 61.514 68.728  -41.693 1.00 35.49 ? 2903 HOH A O   1 
HETATM 9452 O  O   . HOH G 7 .    ? 31.274 68.078  14.401  1.00 35.27 ? 2904 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  ASP 341  341  341  ASP ASP A . n 
A 1 342  PHE 342  342  342  PHE PHE A . n 
A 1 343  ARG 343  343  343  ARG ARG A . n 
A 1 344  PHE 344  344  344  PHE PHE A . n 
A 1 345  LYS 345  345  345  LYS LYS A . n 
A 1 346  GLN 346  346  346  GLN GLN A . n 
A 1 347  ASN 347  347  347  ASN ASN A . n 
A 1 348  THR 348  348  348  THR THR A . n 
A 1 349  GLU 349  349  349  GLU GLU A . n 
A 1 350  TRP 350  350  350  TRP TRP A . n 
A 1 351  ASP 351  351  351  ASP ASP A . n 
A 1 352  VAL 352  352  352  VAL VAL A . n 
A 1 353  GLN 353  353  353  GLN GLN A . n 
A 1 354  ARG 354  354  354  ARG ARG A . n 
A 1 355  VAL 355  355  355  VAL VAL A . n 
A 1 356  ASN 356  356  356  ASN ASN A . n 
A 1 357  TYR 357  357  357  TYR TYR A . n 
A 1 358  GLU 358  358  358  GLU GLU A . n 
A 1 359  ARG 359  359  359  ARG ARG A . n 
A 1 360  LEU 360  360  360  LEU LEU A . n 
A 1 361  PHE 361  361  361  PHE PHE A . n 
A 1 362  GLU 362  362  362  GLU GLU A . n 
A 1 363  HIS 363  363  363  HIS HIS A . n 
A 1 364  ILE 364  364  364  ILE ILE A . n 
A 1 365  ASN 365  365  365  ASN ASN A . n 
A 1 366  SER 366  366  366  SER SER A . n 
A 1 367  GLN 367  367  367  GLN GLN A . n 
A 1 368  ALA 368  368  368  ALA ALA A . n 
A 1 369  HIS 369  369  369  HIS HIS A . n 
A 1 370  PHE 370  370  370  PHE PHE A . n 
A 1 371  ASN 371  371  371  ASN ASN A . n 
A 1 372  VAL 372  372  372  VAL VAL A . n 
A 1 373  GLN 373  373  373  GLN GLN A . n 
A 1 374  ALA 374  374  374  ALA ALA A . n 
A 1 375  GLN 375  375  375  GLN GLN A . n 
A 1 376  PHE 376  376  376  PHE PHE A . n 
A 1 377  GLY 377  377  377  GLY GLY A . n 
A 1 378  THR 378  378  378  THR THR A . n 
A 1 379  LEU 379  379  379  LEU LEU A . n 
A 1 380  GLN 380  380  380  GLN GLN A . n 
A 1 381  GLU 381  381  381  GLU GLU A . n 
A 1 382  TYR 382  382  382  TYR TYR A . n 
A 1 383  PHE 383  383  383  PHE PHE A . n 
A 1 384  ASP 384  384  384  ASP ASP A . n 
A 1 385  ALA 385  385  385  ALA ALA A . n 
A 1 386  VAL 386  386  386  VAL VAL A . n 
A 1 387  HIS 387  387  387  HIS HIS A . n 
A 1 388  GLN 388  388  388  GLN GLN A . n 
A 1 389  ALA 389  389  389  ALA ALA A . n 
A 1 390  GLU 390  390  390  GLU GLU A . n 
A 1 391  ARG 391  391  391  ARG ARG A . n 
A 1 392  ALA 392  392  392  ALA ALA A . n 
A 1 393  GLY 393  393  393  GLY GLY A . n 
A 1 394  GLN 394  394  394  GLN GLN A . n 
A 1 395  ALA 395  395  395  ALA ALA A . n 
A 1 396  GLU 396  396  396  GLU GLU A . n 
A 1 397  PHE 397  397  397  PHE PHE A . n 
A 1 398  PRO 398  398  398  PRO PRO A . n 
A 1 399  THR 399  399  399  THR THR A . n 
A 1 400  LEU 400  400  400  LEU LEU A . n 
A 1 401  SER 401  401  401  SER SER A . n 
A 1 402  GLY 402  402  402  GLY GLY A . n 
A 1 403  ASP 403  403  403  ASP ASP A . n 
A 1 404  PHE 404  404  404  PHE PHE A . n 
A 1 405  PHE 405  405  405  PHE PHE A . n 
A 1 406  THR 406  406  406  THR THR A . n 
A 1 407  TYR 407  407  407  TYR TYR A . n 
A 1 408  ALA 408  408  408  ALA ALA A . n 
A 1 409  ASP 409  409  409  ASP ASP A . n 
A 1 410  ARG 410  410  410  ARG ARG A . n 
A 1 411  SER 411  411  411  SER SER A . n 
A 1 412  ASP 412  412  412  ASP ASP A . n 
A 1 413  ASN 413  413  413  ASN ASN A . n 
A 1 414  TYR 414  414  414  TYR TYR A . n 
A 1 415  TRP 415  415  415  TRP TRP A . n 
A 1 416  SER 416  416  416  SER SER A . n 
A 1 417  GLY 417  417  417  GLY GLY A . n 
A 1 418  TYR 418  418  418  TYR TYR A . n 
A 1 419  TYR 419  419  419  TYR TYR A . n 
A 1 420  THR 420  420  420  THR THR A . n 
A 1 421  SER 421  421  421  SER SER A . n 
A 1 422  ARG 422  422  422  ARG ARG A . n 
A 1 423  PRO 423  423  423  PRO PRO A . n 
A 1 424  TYR 424  424  424  TYR TYR A . n 
A 1 425  HIS 425  425  425  HIS HIS A . n 
A 1 426  LYS 426  426  426  LYS LYS A . n 
A 1 427  ARG 427  427  427  ARG ARG A . n 
A 1 428  MET 428  428  428  MET MET A . n 
A 1 429  ASP 429  429  429  ASP ASP A . n 
A 1 430  ARG 430  430  430  ARG ARG A . n 
A 1 431  VAL 431  431  431  VAL VAL A . n 
A 1 432  LEU 432  432  432  LEU LEU A . n 
A 1 433  MET 433  433  433  MET MET A . n 
A 1 434  HIS 434  434  434  HIS HIS A . n 
A 1 435  TYR 435  435  435  TYR TYR A . n 
A 1 436  VAL 436  436  436  VAL VAL A . n 
A 1 437  ARG 437  437  437  ARG ARG A . n 
A 1 438  ALA 438  438  438  ALA ALA A . n 
A 1 439  ALA 439  439  439  ALA ALA A . n 
A 1 440  GLU 440  440  440  GLU GLU A . n 
A 1 441  MET 441  441  441  MET MET A . n 
A 1 442  LEU 442  442  442  LEU LEU A . n 
A 1 443  SER 443  443  443  SER SER A . n 
A 1 444  ALA 444  444  444  ALA ALA A . n 
A 1 445  TRP 445  445  445  TRP TRP A . n 
A 1 446  HIS 446  446  446  HIS HIS A . n 
A 1 447  SER 447  447  447  SER SER A . n 
A 1 448  TRP 448  448  448  TRP TRP A . n 
A 1 449  ASP 449  449  449  ASP ASP A . n 
A 1 450  GLY 450  450  450  GLY GLY A . n 
A 1 451  MET 451  451  451  MET MET A . n 
A 1 452  ALA 452  452  452  ALA ALA A . n 
A 1 453  ARG 453  453  453  ARG ARG A . n 
A 1 454  ILE 454  454  454  ILE ILE A . n 
A 1 455  GLU 455  455  455  GLU GLU A . n 
A 1 456  GLU 456  456  456  GLU GLU A . n 
A 1 457  ARG 457  457  457  ARG ARG A . n 
A 1 458  LEU 458  458  458  LEU LEU A . n 
A 1 459  GLU 459  459  459  GLU GLU A . n 
A 1 460  GLN 460  460  460  GLN GLN A . n 
A 1 461  ALA 461  461  461  ALA ALA A . n 
A 1 462  ARG 462  462  462  ARG ARG A . n 
A 1 463  ARG 463  463  463  ARG ARG A . n 
A 1 464  GLU 464  464  464  GLU GLU A . n 
A 1 465  LEU 465  465  465  LEU LEU A . n 
A 1 466  SER 466  466  466  SER SER A . n 
A 1 467  LEU 467  467  467  LEU LEU A . n 
A 1 468  PHE 468  468  468  PHE PHE A . n 
A 1 469  GLN 469  469  469  GLN GLN A . n 
A 1 470  HIS 470  470  470  HIS HIS A . n 
A 1 471  HIS 471  471  471  HIS HIS A . n 
A 1 472  ASP 472  472  472  ASP ASP A . n 
A 1 473  GLY 473  473  473  GLY GLY A . n 
A 1 474  ILE 474  474  474  ILE ILE A . n 
A 1 475  THR 475  475  475  THR THR A . n 
A 1 476  GLY 476  476  476  GLY GLY A . n 
A 1 477  THR 477  477  477  THR THR A . n 
A 1 478  ALA 478  478  478  ALA ALA A . n 
A 1 479  LYS 479  479  479  LYS LYS A . n 
A 1 480  THR 480  480  480  THR THR A . n 
A 1 481  HIS 481  481  481  HIS HIS A . n 
A 1 482  VAL 482  482  482  VAL VAL A . n 
A 1 483  VAL 483  483  483  VAL VAL A . n 
A 1 484  VAL 484  484  484  VAL VAL A . n 
A 1 485  ASP 485  485  485  ASP ASP A . n 
A 1 486  TYR 486  486  486  TYR TYR A . n 
A 1 487  GLU 487  487  487  GLU GLU A . n 
A 1 488  GLN 488  488  488  GLN GLN A . n 
A 1 489  ARG 489  489  489  ARG ARG A . n 
A 1 490  MET 490  490  490  MET MET A . n 
A 1 491  GLN 491  491  491  GLN GLN A . n 
A 1 492  GLU 492  492  492  GLU GLU A . n 
A 1 493  ALA 493  493  493  ALA ALA A . n 
A 1 494  LEU 494  494  494  LEU LEU A . n 
A 1 495  LYS 495  495  495  LYS LYS A . n 
A 1 496  ALA 496  496  496  ALA ALA A . n 
A 1 497  CYS 497  497  497  CYS CYS A . n 
A 1 498  GLN 498  498  498  GLN GLN A . n 
A 1 499  MET 499  499  499  MET MET A . n 
A 1 500  VAL 500  500  500  VAL VAL A . n 
A 1 501  MET 501  501  501  MET MET A . n 
A 1 502  GLN 502  502  502  GLN GLN A . n 
A 1 503  GLN 503  503  503  GLN GLN A . n 
A 1 504  SER 504  504  504  SER SER A . n 
A 1 505  VAL 505  505  505  VAL VAL A . n 
A 1 506  TYR 506  506  506  TYR TYR A . n 
A 1 507  ARG 507  507  507  ARG ARG A . n 
A 1 508  LEU 508  508  508  LEU LEU A . n 
A 1 509  LEU 509  509  509  LEU LEU A . n 
A 1 510  THR 510  510  510  THR THR A . n 
A 1 511  LYS 511  511  511  LYS LYS A . n 
A 1 512  PRO 512  512  512  PRO PRO A . n 
A 1 513  SER 513  513  513  SER SER A . n 
A 1 514  ILE 514  514  514  ILE ILE A . n 
A 1 515  TYR 515  515  515  TYR TYR A . n 
A 1 516  SER 516  516  516  SER SER A . n 
A 1 517  PRO 517  517  517  PRO PRO A . n 
A 1 518  ASP 518  518  518  ASP ASP A . n 
A 1 519  PHE 519  519  519  PHE PHE A . n 
A 1 520  SER 520  520  520  SER SER A . n 
A 1 521  PHE 521  521  521  PHE PHE A . n 
A 1 522  SER 522  522  522  SER SER A . n 
A 1 523  TYR 523  523  523  TYR TYR A . n 
A 1 524  PHE 524  524  524  PHE PHE A . n 
A 1 525  THR 525  525  525  THR THR A . n 
A 1 526  LEU 526  526  526  LEU LEU A . n 
A 1 527  ASP 527  527  527  ASP ASP A . n 
A 1 528  ASP 528  528  528  ASP ASP A . n 
A 1 529  SER 529  529  529  SER SER A . n 
A 1 530  ARG 530  530  530  ARG ARG A . n 
A 1 531  TRP 531  531  531  TRP TRP A . n 
A 1 532  PRO 532  532  532  PRO PRO A . n 
A 1 533  GLY 533  533  533  GLY GLY A . n 
A 1 534  SER 534  534  534  SER SER A . n 
A 1 535  GLY 535  535  535  GLY GLY A . n 
A 1 536  VAL 536  536  536  VAL VAL A . n 
A 1 537  GLU 537  537  537  GLU GLU A . n 
A 1 538  ASP 538  538  538  ASP ASP A . n 
A 1 539  SER 539  539  539  SER SER A . n 
A 1 540  ARG 540  540  540  ARG ARG A . n 
A 1 541  THR 541  541  541  THR THR A . n 
A 1 542  THR 542  542  542  THR THR A . n 
A 1 543  ILE 543  543  543  ILE ILE A . n 
A 1 544  ILE 544  544  544  ILE ILE A . n 
A 1 545  LEU 545  545  545  LEU LEU A . n 
A 1 546  GLY 546  546  546  GLY GLY A . n 
A 1 547  GLU 547  547  547  GLU GLU A . n 
A 1 548  ASP 548  548  548  ASP ASP A . n 
A 1 549  ILE 549  549  549  ILE ILE A . n 
A 1 550  LEU 550  550  550  LEU LEU A . n 
A 1 551  PRO 551  551  551  PRO PRO A . n 
A 1 552  SER 552  552  552  SER SER A . n 
A 1 553  LYS 553  553  553  LYS LYS A . n 
A 1 554  HIS 554  554  554  HIS HIS A . n 
A 1 555  VAL 555  555  555  VAL VAL A . n 
A 1 556  VAL 556  556  556  VAL VAL A . n 
A 1 557  MET 557  557  557  MET MET A . n 
A 1 558  HIS 558  558  558  HIS HIS A . n 
A 1 559  ASN 559  559  559  ASN ASN A . n 
A 1 560  THR 560  560  560  THR THR A . n 
A 1 561  LEU 561  561  561  LEU LEU A . n 
A 1 562  PRO 562  562  562  PRO PRO A . n 
A 1 563  HIS 563  563  563  HIS HIS A . n 
A 1 564  TRP 564  564  564  TRP TRP A . n 
A 1 565  ARG 565  565  565  ARG ARG A . n 
A 1 566  GLU 566  566  566  GLU GLU A . n 
A 1 567  GLN 567  567  567  GLN GLN A . n 
A 1 568  LEU 568  568  568  LEU LEU A . n 
A 1 569  VAL 569  569  569  VAL VAL A . n 
A 1 570  ASP 570  570  570  ASP ASP A . n 
A 1 571  PHE 571  571  571  PHE PHE A . n 
A 1 572  TYR 572  572  572  TYR TYR A . n 
A 1 573  VAL 573  573  573  VAL VAL A . n 
A 1 574  SER 574  574  574  SER SER A . n 
A 1 575  SER 575  575  575  SER SER A . n 
A 1 576  PRO 576  576  576  PRO PRO A . n 
A 1 577  PHE 577  577  577  PHE PHE A . n 
A 1 578  VAL 578  578  578  VAL VAL A . n 
A 1 579  SER 579  579  579  SER SER A . n 
A 1 580  VAL 580  580  580  VAL VAL A . n 
A 1 581  THR 581  581  581  THR THR A . n 
A 1 582  ASP 582  582  582  ASP ASP A . n 
A 1 583  LEU 583  583  583  LEU LEU A . n 
A 1 584  ALA 584  584  584  ALA ALA A . n 
A 1 585  ASN 585  585  585  ASN ASN A . n 
A 1 586  ASN 586  586  586  ASN ASN A . n 
A 1 587  PRO 587  587  587  PRO PRO A . n 
A 1 588  VAL 588  588  588  VAL VAL A . n 
A 1 589  GLU 589  589  589  GLU GLU A . n 
A 1 590  ALA 590  590  590  ALA ALA A . n 
A 1 591  GLN 591  591  591  GLN GLN A . n 
A 1 592  VAL 592  592  592  VAL VAL A . n 
A 1 593  SER 593  593  593  SER SER A . n 
A 1 594  PRO 594  594  594  PRO PRO A . n 
A 1 595  VAL 595  595  595  VAL VAL A . n 
A 1 596  TRP 596  596  596  TRP TRP A . n 
A 1 597  SER 597  597  597  SER SER A . n 
A 1 598  TRP 598  598  598  TRP TRP A . n 
A 1 599  HIS 599  599  599  HIS HIS A . n 
A 1 600  HIS 600  600  600  HIS HIS A . n 
A 1 601  ASP 601  601  601  ASP ASP A . n 
A 1 602  THR 602  602  602  THR THR A . n 
A 1 603  LEU 603  603  603  LEU LEU A . n 
A 1 604  THR 604  604  604  THR THR A . n 
A 1 605  LYS 605  605  605  LYS LYS A . n 
A 1 606  THR 606  606  606  THR THR A . n 
A 1 607  ILE 607  607  607  ILE ILE A . n 
A 1 608  HIS 608  608  608  HIS HIS A . n 
A 1 609  PRO 609  609  609  PRO PRO A . n 
A 1 610  GLN 610  610  610  GLN GLN A . n 
A 1 611  GLY 611  611  611  GLY GLY A . n 
A 1 612  SER 612  612  612  SER SER A . n 
A 1 613  THR 613  613  613  THR THR A . n 
A 1 614  THR 614  614  614  THR THR A . n 
A 1 615  LYS 615  615  615  LYS LYS A . n 
A 1 616  TYR 616  616  616  TYR TYR A . n 
A 1 617  ARG 617  617  617  ARG ARG A . n 
A 1 618  ILE 618  618  618  ILE ILE A . n 
A 1 619  ILE 619  619  619  ILE ILE A . n 
A 1 620  PHE 620  620  620  PHE PHE A . n 
A 1 621  LYS 621  621  621  LYS LYS A . n 
A 1 622  ALA 622  622  622  ALA ALA A . n 
A 1 623  ARG 623  623  623  ARG ARG A . n 
A 1 624  VAL 624  624  624  VAL VAL A . n 
A 1 625  PRO 625  625  625  PRO PRO A . n 
A 1 626  PRO 626  626  626  PRO PRO A . n 
A 1 627  MET 627  627  627  MET MET A . n 
A 1 628  GLY 628  628  628  GLY GLY A . n 
A 1 629  LEU 629  629  629  LEU LEU A . n 
A 1 630  ALA 630  630  630  ALA ALA A . n 
A 1 631  THR 631  631  631  THR THR A . n 
A 1 632  TYR 632  632  632  TYR TYR A . n 
A 1 633  VAL 633  633  633  VAL VAL A . n 
A 1 634  LEU 634  634  634  LEU LEU A . n 
A 1 635  THR 635  635  635  THR THR A . n 
A 1 636  ILE 636  636  636  ILE ILE A . n 
A 1 637  SER 637  637  637  SER SER A . n 
A 1 638  ASP 638  638  638  ASP ASP A . n 
A 1 639  SER 639  639  639  SER SER A . n 
A 1 640  LYS 640  640  640  LYS LYS A . n 
A 1 641  PRO 641  641  641  PRO PRO A . n 
A 1 642  GLU 642  642  642  GLU GLU A . n 
A 1 643  HIS 643  643  643  HIS HIS A . n 
A 1 644  THR 644  644  644  THR THR A . n 
A 1 645  SER 645  645  645  SER SER A . n 
A 1 646  TYR 646  646  646  TYR TYR A . n 
A 1 647  ALA 647  647  647  ALA ALA A . n 
A 1 648  SER 648  648  648  SER SER A . n 
A 1 649  ASN 649  649  649  ASN ASN A . n 
A 1 650  LEU 650  650  650  LEU LEU A . n 
A 1 651  LEU 651  651  651  LEU LEU A . n 
A 1 652  LEU 652  652  652  LEU LEU A . n 
A 1 653  ARG 653  653  653  ARG ARG A . n 
A 1 654  LYS 654  654  654  LYS LYS A . n 
A 1 655  ASN 655  655  655  ASN ASN A . n 
A 1 656  PRO 656  656  656  PRO PRO A . n 
A 1 657  THR 657  657  657  THR THR A . n 
A 1 658  SER 658  658  658  SER SER A . n 
A 1 659  LEU 659  659  659  LEU LEU A . n 
A 1 660  PRO 660  660  660  PRO PRO A . n 
A 1 661  LEU 661  661  661  LEU LEU A . n 
A 1 662  GLY 662  662  662  GLY GLY A . n 
A 1 663  GLN 663  663  663  GLN GLN A . n 
A 1 664  TYR 664  664  664  TYR TYR A . n 
A 1 665  PRO 665  665  665  PRO PRO A . n 
A 1 666  GLU 666  666  666  GLU GLU A . n 
A 1 667  ASP 667  667  667  ASP ASP A . n 
A 1 668  VAL 668  668  668  VAL VAL A . n 
A 1 669  LYS 669  669  669  LYS LYS A . n 
A 1 670  PHE 670  670  670  PHE PHE A . n 
A 1 671  GLY 671  671  671  GLY GLY A . n 
A 1 672  ASP 672  672  672  ASP ASP A . n 
A 1 673  PRO 673  673  673  PRO PRO A . n 
A 1 674  ARG 674  674  674  ARG ARG A . n 
A 1 675  GLU 675  675  675  GLU GLU A . n 
A 1 676  ILE 676  676  676  ILE ILE A . n 
A 1 677  SER 677  677  677  SER SER A . n 
A 1 678  LEU 678  678  678  LEU LEU A . n 
A 1 679  ARG 679  679  679  ARG ARG A . n 
A 1 680  VAL 680  680  680  VAL VAL A . n 
A 1 681  GLY 681  681  681  GLY GLY A . n 
A 1 682  ASN 682  682  682  ASN ASN A . n 
A 1 683  GLY 683  683  683  GLY GLY A . n 
A 1 684  PRO 684  684  684  PRO PRO A . n 
A 1 685  THR 685  685  685  THR THR A . n 
A 1 686  LEU 686  686  686  LEU LEU A . n 
A 1 687  ALA 687  687  687  ALA ALA A . n 
A 1 688  PHE 688  688  688  PHE PHE A . n 
A 1 689  SER 689  689  689  SER SER A . n 
A 1 690  GLU 690  690  690  GLU GLU A . n 
A 1 691  GLN 691  691  691  GLN GLN A . n 
A 1 692  GLY 692  692  692  GLY GLY A . n 
A 1 693  LEU 693  693  693  LEU LEU A . n 
A 1 694  LEU 694  694  694  LEU LEU A . n 
A 1 695  LYS 695  695  695  LYS LYS A . n 
A 1 696  SER 696  696  696  SER SER A . n 
A 1 697  ILE 697  697  697  ILE ILE A . n 
A 1 698  GLN 698  698  698  GLN GLN A . n 
A 1 699  LEU 699  699  699  LEU LEU A . n 
A 1 700  THR 700  700  700  THR THR A . n 
A 1 701  GLN 701  701  701  GLN GLN A . n 
A 1 702  ASP 702  702  702  ASP ASP A . n 
A 1 703  SER 703  703  703  SER SER A . n 
A 1 704  PRO 704  704  704  PRO PRO A . n 
A 1 705  HIS 705  705  705  HIS HIS A . n 
A 1 706  VAL 706  706  706  VAL VAL A . n 
A 1 707  PRO 707  707  707  PRO PRO A . n 
A 1 708  VAL 708  708  708  VAL VAL A . n 
A 1 709  HIS 709  709  709  HIS HIS A . n 
A 1 710  PHE 710  710  710  PHE PHE A . n 
A 1 711  LYS 711  711  711  LYS LYS A . n 
A 1 712  PHE 712  712  712  PHE PHE A . n 
A 1 713  LEU 713  713  713  LEU LEU A . n 
A 1 714  LYS 714  714  714  LYS LYS A . n 
A 1 715  TYR 715  715  715  TYR TYR A . n 
A 1 716  GLY 716  716  716  GLY GLY A . n 
A 1 717  VAL 717  717  717  VAL VAL A . n 
A 1 718  ARG 718  718  718  ARG ARG A . n 
A 1 719  SER 719  719  719  SER SER A . n 
A 1 720  HIS 720  720  720  HIS HIS A . n 
A 1 721  GLY 721  721  721  GLY GLY A . n 
A 1 722  ASP 722  722  722  ASP ASP A . n 
A 1 723  ARG 723  723  723  ARG ARG A . n 
A 1 724  SER 724  724  724  SER SER A . n 
A 1 725  GLY 725  725  725  GLY GLY A . n 
A 1 726  ALA 726  726  726  ALA ALA A . n 
A 1 727  TYR 727  727  727  TYR TYR A . n 
A 1 728  LEU 728  728  728  LEU LEU A . n 
A 1 729  PHE 729  729  729  PHE PHE A . n 
A 1 730  LEU 730  730  730  LEU LEU A . n 
A 1 731  PRO 731  731  731  PRO PRO A . n 
A 1 732  ASN 732  732  732  ASN ASN A . n 
A 1 733  GLY 733  733  733  GLY GLY A . n 
A 1 734  PRO 734  734  734  PRO PRO A . n 
A 1 735  ALA 735  735  735  ALA ALA A . n 
A 1 736  SER 736  736  736  SER SER A . n 
A 1 737  PRO 737  737  737  PRO PRO A . n 
A 1 738  VAL 738  738  738  VAL VAL A . n 
A 1 739  GLU 739  739  739  GLU GLU A . n 
A 1 740  LEU 740  740  740  LEU LEU A . n 
A 1 741  GLY 741  741  741  GLY GLY A . n 
A 1 742  GLN 742  742  742  GLN GLN A . n 
A 1 743  PRO 743  743  743  PRO PRO A . n 
A 1 744  VAL 744  744  744  VAL VAL A . n 
A 1 745  VAL 745  745  745  VAL VAL A . n 
A 1 746  LEU 746  746  746  LEU LEU A . n 
A 1 747  VAL 747  747  747  VAL VAL A . n 
A 1 748  THR 748  748  748  THR THR A . n 
A 1 749  LYS 749  749  749  LYS LYS A . n 
A 1 750  GLY 750  750  750  GLY GLY A . n 
A 1 751  LYS 751  751  751  LYS LYS A . n 
A 1 752  LEU 752  752  752  LEU LEU A . n 
A 1 753  GLU 753  753  753  GLU GLU A . n 
A 1 754  SER 754  754  754  SER SER A . n 
A 1 755  SER 755  755  755  SER SER A . n 
A 1 756  VAL 756  756  756  VAL VAL A . n 
A 1 757  SER 757  757  757  SER SER A . n 
A 1 758  VAL 758  758  758  VAL VAL A . n 
A 1 759  GLY 759  759  759  GLY GLY A . n 
A 1 760  LEU 760  760  760  LEU LEU A . n 
A 1 761  PRO 761  761  761  PRO PRO A . n 
A 1 762  SER 762  762  762  SER SER A . n 
A 1 763  VAL 763  763  763  VAL VAL A . n 
A 1 764  VAL 764  764  764  VAL VAL A . n 
A 1 765  HIS 765  765  765  HIS HIS A . n 
A 1 766  GLN 766  766  766  GLN GLN A . n 
A 1 767  THR 767  767  767  THR THR A . n 
A 1 768  ILE 768  768  768  ILE ILE A . n 
A 1 769  MET 769  769  769  MET MET A . n 
A 1 770  ARG 770  770  770  ARG ARG A . n 
A 1 771  GLY 771  771  771  GLY GLY A . n 
A 1 772  GLY 772  772  772  GLY GLY A . n 
A 1 773  ALA 773  773  773  ALA ALA A . n 
A 1 774  PRO 774  774  774  PRO PRO A . n 
A 1 775  GLU 775  775  775  GLU GLU A . n 
A 1 776  ILE 776  776  776  ILE ILE A . n 
A 1 777  ARG 777  777  777  ARG ARG A . n 
A 1 778  ASN 778  778  778  ASN ASN A . n 
A 1 779  LEU 779  779  779  LEU LEU A . n 
A 1 780  VAL 780  780  780  VAL VAL A . n 
A 1 781  ASP 781  781  781  ASP ASP A . n 
A 1 782  ILE 782  782  782  ILE ILE A . n 
A 1 783  GLY 783  783  783  GLY GLY A . n 
A 1 784  SER 784  784  784  SER SER A . n 
A 1 785  LEU 785  785  785  LEU LEU A . n 
A 1 786  ASP 786  786  786  ASP ASP A . n 
A 1 787  ASN 787  787  787  ASN ASN A . n 
A 1 788  THR 788  788  788  THR THR A . n 
A 1 789  GLU 789  789  789  GLU GLU A . n 
A 1 790  ILE 790  790  790  ILE ILE A . n 
A 1 791  VAL 791  791  791  VAL VAL A . n 
A 1 792  MET 792  792  792  MET MET A . n 
A 1 793  ARG 793  793  793  ARG ARG A . n 
A 1 794  LEU 794  794  794  LEU LEU A . n 
A 1 795  GLU 795  795  795  GLU GLU A . n 
A 1 796  THR 796  796  796  THR THR A . n 
A 1 797  HIS 797  797  797  HIS HIS A . n 
A 1 798  ILE 798  798  798  ILE ILE A . n 
A 1 799  ASP 799  799  799  ASP ASP A . n 
A 1 800  SER 800  800  800  SER SER A . n 
A 1 801  GLY 801  801  801  GLY GLY A . n 
A 1 802  ASP 802  802  802  ASP ASP A . n 
A 1 803  ILE 803  803  803  ILE ILE A . n 
A 1 804  PHE 804  804  804  PHE PHE A . n 
A 1 805  TYR 805  805  805  TYR TYR A . n 
A 1 806  THR 806  806  806  THR THR A . n 
A 1 807  ASP 807  807  807  ASP ASP A . n 
A 1 808  LEU 808  808  808  LEU LEU A . n 
A 1 809  ASN 809  809  809  ASN ASN A . n 
A 1 810  GLY 810  810  810  GLY GLY A . n 
A 1 811  LEU 811  811  811  LEU LEU A . n 
A 1 812  GLN 812  812  812  GLN GLN A . n 
A 1 813  PHE 813  813  813  PHE PHE A . n 
A 1 814  ILE 814  814  814  ILE ILE A . n 
A 1 815  LYS 815  815  815  LYS LYS A . n 
A 1 816  ARG 816  816  816  ARG ARG A . n 
A 1 817  ARG 817  817  817  ARG ARG A . n 
A 1 818  ARG 818  818  818  ARG ARG A . n 
A 1 819  LEU 819  819  819  LEU LEU A . n 
A 1 820  ASP 820  820  820  ASP ASP A . n 
A 1 821  LYS 821  821  821  LYS LYS A . n 
A 1 822  LEU 822  822  822  LEU LEU A . n 
A 1 823  PRO 823  823  823  PRO PRO A . n 
A 1 824  LEU 824  824  824  LEU LEU A . n 
A 1 825  GLN 825  825  825  GLN GLN A . n 
A 1 826  ALA 826  826  826  ALA ALA A . n 
A 1 827  ASN 827  827  827  ASN ASN A . n 
A 1 828  TYR 828  828  828  TYR TYR A . n 
A 1 829  TYR 829  829  829  TYR TYR A . n 
A 1 830  PRO 830  830  830  PRO PRO A . n 
A 1 831  ILE 831  831  831  ILE ILE A . n 
A 1 832  PRO 832  832  832  PRO PRO A . n 
A 1 833  SER 833  833  833  SER SER A . n 
A 1 834  GLY 834  834  834  GLY GLY A . n 
A 1 835  MET 835  835  835  MET MET A . n 
A 1 836  PHE 836  836  836  PHE PHE A . n 
A 1 837  ILE 837  837  837  ILE ILE A . n 
A 1 838  GLU 838  838  838  GLU GLU A . n 
A 1 839  ASP 839  839  839  ASP ASP A . n 
A 1 840  ALA 840  840  840  ALA ALA A . n 
A 1 841  ASN 841  841  841  ASN ASN A . n 
A 1 842  THR 842  842  842  THR THR A . n 
A 1 843  ARG 843  843  843  ARG ARG A . n 
A 1 844  LEU 844  844  844  LEU LEU A . n 
A 1 845  THR 845  845  845  THR THR A . n 
A 1 846  LEU 846  846  846  LEU LEU A . n 
A 1 847  LEU 847  847  847  LEU LEU A . n 
A 1 848  THR 848  848  848  THR THR A . n 
A 1 849  GLY 849  849  849  GLY GLY A . n 
A 1 850  GLN 850  850  850  GLN GLN A . n 
A 1 851  PRO 851  851  851  PRO PRO A . n 
A 1 852  LEU 852  852  852  LEU LEU A . n 
A 1 853  GLY 853  853  853  GLY GLY A . n 
A 1 854  GLY 854  854  854  GLY GLY A . n 
A 1 855  SER 855  855  855  SER SER A . n 
A 1 856  SER 856  856  856  SER SER A . n 
A 1 857  LEU 857  857  857  LEU LEU A . n 
A 1 858  ALA 858  858  858  ALA ALA A . n 
A 1 859  SER 859  859  859  SER SER A . n 
A 1 860  GLY 860  860  860  GLY GLY A . n 
A 1 861  GLU 861  861  861  GLU GLU A . n 
A 1 862  LEU 862  862  862  LEU LEU A . n 
A 1 863  GLU 863  863  863  GLU GLU A . n 
A 1 864  ILE 864  864  864  ILE ILE A . n 
A 1 865  MET 865  865  865  MET MET A . n 
A 1 866  GLN 866  866  866  GLN GLN A . n 
A 1 867  ASP 867  867  867  ASP ASP A . n 
A 1 868  ARG 868  868  868  ARG ARG A . n 
A 1 869  ARG 869  869  869  ARG ARG A . n 
A 1 870  LEU 870  870  870  LEU LEU A . n 
A 1 871  ALA 871  871  871  ALA ALA A . n 
A 1 872  SER 872  872  872  SER SER A . n 
A 1 873  ASP 873  873  873  ASP ASP A . n 
A 1 874  ASP 874  874  874  ASP ASP A . n 
A 1 875  GLU 875  875  875  GLU GLU A . n 
A 1 876  ARG 876  876  876  ARG ARG A . n 
A 1 877  GLY 877  877  877  GLY GLY A . n 
A 1 878  LEU 878  878  878  LEU LEU A . n 
A 1 879  GLY 879  879  879  GLY GLY A . n 
A 1 880  GLN 880  880  880  GLN GLN A . n 
A 1 881  GLY 881  881  881  GLY GLY A . n 
A 1 882  VAL 882  882  882  VAL VAL A . n 
A 1 883  LEU 883  883  883  LEU LEU A . n 
A 1 884  ASP 884  884  884  ASP ASP A . n 
A 1 885  ASN 885  885  885  ASN ASN A . n 
A 1 886  LYS 886  886  886  LYS LYS A . n 
A 1 887  PRO 887  887  887  PRO PRO A . n 
A 1 888  VAL 888  888  888  VAL VAL A . n 
A 1 889  LEU 889  889  889  LEU LEU A . n 
A 1 890  HIS 890  890  890  HIS HIS A . n 
A 1 891  ILE 891  891  891  ILE ILE A . n 
A 1 892  TYR 892  892  892  TYR TYR A . n 
A 1 893  ARG 893  893  893  ARG ARG A . n 
A 1 894  LEU 894  894  894  LEU LEU A . n 
A 1 895  VAL 895  895  895  VAL VAL A . n 
A 1 896  LEU 896  896  896  LEU LEU A . n 
A 1 897  GLU 897  897  897  GLU GLU A . n 
A 1 898  LYS 898  898  898  LYS LYS A . n 
A 1 899  VAL 899  899  899  VAL VAL A . n 
A 1 900  ASN 900  900  900  ASN ASN A . n 
A 1 901  ASN 901  901  901  ASN ASN A . n 
A 1 902  CYS 902  902  902  CYS CYS A . n 
A 1 903  VAL 903  903  903  VAL VAL A . n 
A 1 904  ARG 904  904  904  ARG ARG A . n 
A 1 905  PRO 905  905  905  PRO PRO A . n 
A 1 906  SER 906  906  906  SER SER A . n 
A 1 907  LYS 907  907  907  LYS LYS A . n 
A 1 908  LEU 908  908  908  LEU LEU A . n 
A 1 909  HIS 909  909  909  HIS HIS A . n 
A 1 910  PRO 910  910  910  PRO PRO A . n 
A 1 911  ALA 911  911  911  ALA ALA A . n 
A 1 912  GLY 912  912  912  GLY GLY A . n 
A 1 913  TYR 913  913  913  TYR TYR A . n 
A 1 914  LEU 914  914  914  LEU LEU A . n 
A 1 915  THR 915  915  915  THR THR A . n 
A 1 916  SER 916  916  916  SER SER A . n 
A 1 917  ALA 917  917  917  ALA ALA A . n 
A 1 918  ALA 918  918  918  ALA ALA A . n 
A 1 919  HIS 919  919  919  HIS HIS A . n 
A 1 920  LYS 920  920  920  LYS LYS A . n 
A 1 921  ALA 921  921  921  ALA ALA A . n 
A 1 922  SER 922  922  922  SER SER A . n 
A 1 923  GLN 923  923  923  GLN GLN A . n 
A 1 924  SER 924  924  924  SER SER A . n 
A 1 925  LEU 925  925  925  LEU LEU A . n 
A 1 926  LEU 926  926  926  LEU LEU A . n 
A 1 927  ASP 927  927  927  ASP ASP A . n 
A 1 928  PRO 928  928  928  PRO PRO A . n 
A 1 929  LEU 929  929  929  LEU LEU A . n 
A 1 930  ASP 930  930  930  ASP ASP A . n 
A 1 931  LYS 931  931  931  LYS LYS A . n 
A 1 932  PHE 932  932  932  PHE PHE A . n 
A 1 933  ILE 933  933  933  ILE ILE A . n 
A 1 934  PHE 934  934  934  PHE PHE A . n 
A 1 935  ALA 935  935  935  ALA ALA A . n 
A 1 936  GLU 936  936  936  GLU GLU A . n 
A 1 937  ASN 937  937  937  ASN ASN A . n 
A 1 938  GLU 938  938  938  GLU GLU A . n 
A 1 939  TRP 939  939  939  TRP TRP A . n 
A 1 940  ILE 940  940  940  ILE ILE A . n 
A 1 941  GLY 941  941  941  GLY GLY A . n 
A 1 942  ALA 942  942  942  ALA ALA A . n 
A 1 943  GLN 943  943  943  GLN GLN A . n 
A 1 944  GLY 944  944  944  GLY GLY A . n 
A 1 945  GLN 945  945  945  GLN GLN A . n 
A 1 946  PHE 946  946  946  PHE PHE A . n 
A 1 947  GLY 947  947  947  GLY GLY A . n 
A 1 948  GLY 948  948  948  GLY GLY A . n 
A 1 949  ASP 949  949  949  ASP ASP A . n 
A 1 950  HIS 950  950  950  HIS HIS A . n 
A 1 951  PRO 951  951  951  PRO PRO A . n 
A 1 952  SER 952  952  952  SER SER A . n 
A 1 953  ALA 953  953  953  ALA ALA A . n 
A 1 954  ARG 954  954  954  ARG ARG A . n 
A 1 955  GLU 955  955  955  GLU GLU A . n 
A 1 956  ASP 956  956  956  ASP ASP A . n 
A 1 957  LEU 957  957  957  LEU LEU A . n 
A 1 958  ASP 958  958  958  ASP ASP A . n 
A 1 959  VAL 959  959  959  VAL VAL A . n 
A 1 960  SER 960  960  960  SER SER A . n 
A 1 961  VAL 961  961  961  VAL VAL A . n 
A 1 962  MET 962  962  962  MET MET A . n 
A 1 963  ARG 963  963  963  ARG ARG A . n 
A 1 964  ARG 964  964  964  ARG ARG A . n 
A 1 965  LEU 965  965  965  LEU LEU A . n 
A 1 966  THR 966  966  966  THR THR A . n 
A 1 967  LYS 967  967  967  LYS LYS A . n 
A 1 968  SER 968  968  968  SER SER A . n 
A 1 969  SER 969  969  969  SER SER A . n 
A 1 970  ALA 970  970  970  ALA ALA A . n 
A 1 971  LYS 971  971  971  LYS LYS A . n 
A 1 972  THR 972  972  972  THR THR A . n 
A 1 973  GLN 973  973  973  GLN GLN A . n 
A 1 974  ARG 974  974  974  ARG ARG A . n 
A 1 975  VAL 975  975  975  VAL VAL A . n 
A 1 976  GLY 976  976  976  GLY GLY A . n 
A 1 977  TYR 977  977  977  TYR TYR A . n 
A 1 978  VAL 978  978  978  VAL VAL A . n 
A 1 979  LEU 979  979  979  LEU LEU A . n 
A 1 980  HIS 980  980  980  HIS HIS A . n 
A 1 981  ARG 981  981  981  ARG ARG A . n 
A 1 982  THR 982  982  982  THR THR A . n 
A 1 983  ASN 983  983  983  ASN ASN A . n 
A 1 984  LEU 984  984  984  LEU LEU A . n 
A 1 985  MET 985  985  985  MET MET A . n 
A 1 986  GLN 986  986  986  GLN GLN A . n 
A 1 987  CYS 987  987  987  CYS CYS A . n 
A 1 988  GLY 988  988  988  GLY GLY A . n 
A 1 989  THR 989  989  989  THR THR A . n 
A 1 990  PRO 990  990  990  PRO PRO A . n 
A 1 991  GLU 991  991  991  GLU GLU A . n 
A 1 992  GLU 992  992  992  GLU GLU A . n 
A 1 993  HIS 993  993  993  HIS HIS A . n 
A 1 994  THR 994  994  994  THR THR A . n 
A 1 995  GLN 995  995  995  GLN GLN A . n 
A 1 996  LYS 996  996  996  LYS LYS A . n 
A 1 997  LEU 997  997  997  LEU LEU A . n 
A 1 998  ASP 998  998  998  ASP ASP A . n 
A 1 999  VAL 999  999  999  VAL VAL A . n 
A 1 1000 CYS 1000 1000 1000 CYS CYS A . n 
A 1 1001 HIS 1001 1001 1001 HIS HIS A . n 
A 1 1002 LEU 1002 1002 1002 LEU LEU A . n 
A 1 1003 LEU 1003 1003 1003 LEU LEU A . n 
A 1 1004 PRO 1004 1004 1004 PRO PRO A . n 
A 1 1005 ASN 1005 1005 1005 ASN ASN A . n 
A 1 1006 VAL 1006 1006 1006 VAL VAL A . n 
A 1 1007 ALA 1007 1007 1007 ALA ALA A . n 
A 1 1008 ARG 1008 1008 1008 ARG ARG A . n 
A 1 1009 CYS 1009 1009 1009 CYS CYS A . n 
A 1 1010 GLU 1010 1010 1010 GLU GLU A . n 
A 1 1011 ARG 1011 1011 1011 ARG ARG A . n 
A 1 1012 THR 1012 1012 1012 THR THR A . n 
A 1 1013 THR 1013 1013 1013 THR THR A . n 
A 1 1014 LEU 1014 1014 1014 LEU LEU A . n 
A 1 1015 THR 1015 1015 1015 THR THR A . n 
A 1 1016 PHE 1016 1016 1016 PHE PHE A . n 
A 1 1017 LEU 1017 1017 1017 LEU LEU A . n 
A 1 1018 GLN 1018 1018 1018 GLN GLN A . n 
A 1 1019 ASN 1019 1019 1019 ASN ASN A . n 
A 1 1020 LEU 1020 1020 1020 LEU LEU A . n 
A 1 1021 GLU 1021 1021 1021 GLU GLU A . n 
A 1 1022 HIS 1022 1022 1022 HIS HIS A . n 
A 1 1023 LEU 1023 1023 1023 LEU LEU A . n 
A 1 1024 ASP 1024 1024 1024 ASP ASP A . n 
A 1 1025 GLY 1025 1025 1025 GLY GLY A . n 
A 1 1026 MET 1026 1026 1026 MET MET A . n 
A 1 1027 VAL 1027 1027 1027 VAL VAL A . n 
A 1 1028 ALA 1028 1028 1028 ALA ALA A . n 
A 1 1029 PRO 1029 1029 1029 PRO PRO A . n 
A 1 1030 GLU 1030 1030 1030 GLU GLU A . n 
A 1 1031 VAL 1031 1031 1031 VAL VAL A . n 
A 1 1032 CYS 1032 1032 1032 CYS CYS A . n 
A 1 1033 PRO 1033 1033 1033 PRO PRO A . n 
A 1 1034 MET 1034 1034 1034 MET MET A . n 
A 1 1035 GLU 1035 1035 1035 GLU GLU A . n 
A 1 1036 THR 1036 1036 1036 THR THR A . n 
A 1 1037 ALA 1037 1037 1037 ALA ALA A . n 
A 1 1038 ALA 1038 1038 1038 ALA ALA A . n 
A 1 1039 TYR 1039 1039 1039 TYR TYR A . n 
A 1 1040 VAL 1040 1040 1040 VAL VAL A . n 
A 1 1041 SER 1041 1041 1041 SER SER A . n 
A 1 1042 SER 1042 1042 1042 SER SER A . n 
A 1 1043 HIS 1043 1043 1043 HIS HIS A . n 
A 1 1044 SER 1044 1044 1044 SER SER A . n 
A 1 1045 SER 1045 1045 1045 SER SER A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 NAG 1    1802 1    NAG NAG A . 
C 3 PO4 1    1803 1    PO4 PO4 A . 
D 4 ZN  1    1805 1    ZN  ZN  A . 
E 5 GB2 1    1804 1    GB2 GB2 A . 
F 6 MPD 1    1801 1    MPD MPD A . 
G 7 HOH 1    1806 1    HOH WAT A . 
G 7 HOH 2    1807 2    HOH WAT A . 
G 7 HOH 3    1808 3    HOH WAT A . 
G 7 HOH 4    1809 4    HOH WAT A . 
G 7 HOH 5    1810 5    HOH WAT A . 
G 7 HOH 6    1811 6    HOH WAT A . 
G 7 HOH 7    1812 7    HOH WAT A . 
G 7 HOH 8    1813 8    HOH WAT A . 
G 7 HOH 9    1814 9    HOH WAT A . 
G 7 HOH 10   1815 10   HOH WAT A . 
G 7 HOH 11   1816 11   HOH WAT A . 
G 7 HOH 12   1817 12   HOH WAT A . 
G 7 HOH 13   1818 13   HOH WAT A . 
G 7 HOH 14   1819 14   HOH WAT A . 
G 7 HOH 15   1820 15   HOH WAT A . 
G 7 HOH 16   1821 16   HOH WAT A . 
G 7 HOH 17   1822 17   HOH WAT A . 
G 7 HOH 18   1823 18   HOH WAT A . 
G 7 HOH 19   1824 19   HOH WAT A . 
G 7 HOH 20   1825 20   HOH WAT A . 
G 7 HOH 21   1826 21   HOH WAT A . 
G 7 HOH 22   1827 22   HOH WAT A . 
G 7 HOH 23   1828 23   HOH WAT A . 
G 7 HOH 24   1829 24   HOH WAT A . 
G 7 HOH 25   1830 25   HOH WAT A . 
G 7 HOH 26   1831 26   HOH WAT A . 
G 7 HOH 27   1832 27   HOH WAT A . 
G 7 HOH 28   1833 28   HOH WAT A . 
G 7 HOH 29   1834 29   HOH WAT A . 
G 7 HOH 30   1835 30   HOH WAT A . 
G 7 HOH 31   1836 31   HOH WAT A . 
G 7 HOH 32   1837 32   HOH WAT A . 
G 7 HOH 33   1838 33   HOH WAT A . 
G 7 HOH 34   1839 34   HOH WAT A . 
G 7 HOH 35   1840 35   HOH WAT A . 
G 7 HOH 36   1841 36   HOH WAT A . 
G 7 HOH 37   1842 37   HOH WAT A . 
G 7 HOH 38   1843 38   HOH WAT A . 
G 7 HOH 39   1844 39   HOH WAT A . 
G 7 HOH 40   1845 40   HOH WAT A . 
G 7 HOH 41   1846 41   HOH WAT A . 
G 7 HOH 42   1847 42   HOH WAT A . 
G 7 HOH 43   1848 43   HOH WAT A . 
G 7 HOH 44   1849 44   HOH WAT A . 
G 7 HOH 45   1850 45   HOH WAT A . 
G 7 HOH 46   1851 46   HOH WAT A . 
G 7 HOH 47   1852 47   HOH WAT A . 
G 7 HOH 48   1853 48   HOH WAT A . 
G 7 HOH 49   1854 49   HOH WAT A . 
G 7 HOH 50   1855 50   HOH WAT A . 
G 7 HOH 51   1856 51   HOH WAT A . 
G 7 HOH 52   1857 52   HOH WAT A . 
G 7 HOH 53   1858 53   HOH WAT A . 
G 7 HOH 54   1859 54   HOH WAT A . 
G 7 HOH 55   1860 55   HOH WAT A . 
G 7 HOH 56   1861 56   HOH WAT A . 
G 7 HOH 57   1862 57   HOH WAT A . 
G 7 HOH 58   1863 58   HOH WAT A . 
G 7 HOH 59   1864 59   HOH WAT A . 
G 7 HOH 60   1865 60   HOH WAT A . 
G 7 HOH 61   1866 61   HOH WAT A . 
G 7 HOH 62   1867 62   HOH WAT A . 
G 7 HOH 63   1868 63   HOH WAT A . 
G 7 HOH 64   1869 64   HOH WAT A . 
G 7 HOH 65   1870 65   HOH WAT A . 
G 7 HOH 66   1871 66   HOH WAT A . 
G 7 HOH 67   1872 67   HOH WAT A . 
G 7 HOH 68   1873 68   HOH WAT A . 
G 7 HOH 69   1874 69   HOH WAT A . 
G 7 HOH 70   1875 70   HOH WAT A . 
G 7 HOH 71   1876 71   HOH WAT A . 
G 7 HOH 72   1877 72   HOH WAT A . 
G 7 HOH 73   1878 73   HOH WAT A . 
G 7 HOH 74   1879 74   HOH WAT A . 
G 7 HOH 75   1880 75   HOH WAT A . 
G 7 HOH 76   1881 76   HOH WAT A . 
G 7 HOH 77   1882 77   HOH WAT A . 
G 7 HOH 78   1883 78   HOH WAT A . 
G 7 HOH 79   1884 79   HOH WAT A . 
G 7 HOH 80   1885 80   HOH WAT A . 
G 7 HOH 81   1886 81   HOH WAT A . 
G 7 HOH 82   1887 82   HOH WAT A . 
G 7 HOH 83   1888 83   HOH WAT A . 
G 7 HOH 84   1889 84   HOH WAT A . 
G 7 HOH 85   1890 85   HOH WAT A . 
G 7 HOH 86   1891 86   HOH WAT A . 
G 7 HOH 87   1892 87   HOH WAT A . 
G 7 HOH 88   1893 88   HOH WAT A . 
G 7 HOH 89   1894 89   HOH WAT A . 
G 7 HOH 90   1895 90   HOH WAT A . 
G 7 HOH 91   1896 91   HOH WAT A . 
G 7 HOH 92   1897 92   HOH WAT A . 
G 7 HOH 93   1898 93   HOH WAT A . 
G 7 HOH 94   1899 94   HOH WAT A . 
G 7 HOH 95   1900 95   HOH WAT A . 
G 7 HOH 96   1901 96   HOH WAT A . 
G 7 HOH 97   1902 97   HOH WAT A . 
G 7 HOH 98   1903 98   HOH WAT A . 
G 7 HOH 99   1904 99   HOH WAT A . 
G 7 HOH 100  1905 100  HOH WAT A . 
G 7 HOH 101  1906 101  HOH WAT A . 
G 7 HOH 102  1907 102  HOH WAT A . 
G 7 HOH 103  1908 103  HOH WAT A . 
G 7 HOH 104  1909 104  HOH WAT A . 
G 7 HOH 105  1910 105  HOH WAT A . 
G 7 HOH 106  1911 106  HOH WAT A . 
G 7 HOH 107  1912 107  HOH WAT A . 
G 7 HOH 108  1913 108  HOH WAT A . 
G 7 HOH 109  1914 109  HOH WAT A . 
G 7 HOH 110  1915 110  HOH WAT A . 
G 7 HOH 111  1916 111  HOH WAT A . 
G 7 HOH 112  1917 112  HOH WAT A . 
G 7 HOH 113  1918 113  HOH WAT A . 
G 7 HOH 114  1919 114  HOH WAT A . 
G 7 HOH 115  1920 115  HOH WAT A . 
G 7 HOH 116  1921 116  HOH WAT A . 
G 7 HOH 117  1922 117  HOH WAT A . 
G 7 HOH 118  1923 118  HOH WAT A . 
G 7 HOH 119  1924 119  HOH WAT A . 
G 7 HOH 120  1925 120  HOH WAT A . 
G 7 HOH 121  1926 121  HOH WAT A . 
G 7 HOH 122  1927 122  HOH WAT A . 
G 7 HOH 123  1928 123  HOH WAT A . 
G 7 HOH 124  1929 124  HOH WAT A . 
G 7 HOH 125  1930 125  HOH WAT A . 
G 7 HOH 126  1931 126  HOH WAT A . 
G 7 HOH 127  1932 127  HOH WAT A . 
G 7 HOH 128  1933 128  HOH WAT A . 
G 7 HOH 129  1934 129  HOH WAT A . 
G 7 HOH 130  1935 130  HOH WAT A . 
G 7 HOH 131  1936 131  HOH WAT A . 
G 7 HOH 132  1937 132  HOH WAT A . 
G 7 HOH 133  1938 133  HOH WAT A . 
G 7 HOH 134  1939 134  HOH WAT A . 
G 7 HOH 135  1940 135  HOH WAT A . 
G 7 HOH 136  1941 136  HOH WAT A . 
G 7 HOH 137  1942 137  HOH WAT A . 
G 7 HOH 138  1943 138  HOH WAT A . 
G 7 HOH 139  1944 139  HOH WAT A . 
G 7 HOH 140  1945 140  HOH WAT A . 
G 7 HOH 141  1946 141  HOH WAT A . 
G 7 HOH 142  1947 142  HOH WAT A . 
G 7 HOH 143  1948 143  HOH WAT A . 
G 7 HOH 144  1949 144  HOH WAT A . 
G 7 HOH 145  1950 145  HOH WAT A . 
G 7 HOH 146  1951 146  HOH WAT A . 
G 7 HOH 147  1952 147  HOH WAT A . 
G 7 HOH 148  1953 148  HOH WAT A . 
G 7 HOH 149  1954 149  HOH WAT A . 
G 7 HOH 150  1955 150  HOH WAT A . 
G 7 HOH 151  1956 151  HOH WAT A . 
G 7 HOH 152  1957 152  HOH WAT A . 
G 7 HOH 153  1958 153  HOH WAT A . 
G 7 HOH 154  1959 154  HOH WAT A . 
G 7 HOH 155  1960 155  HOH WAT A . 
G 7 HOH 156  1961 156  HOH WAT A . 
G 7 HOH 157  1962 157  HOH WAT A . 
G 7 HOH 158  1963 158  HOH WAT A . 
G 7 HOH 159  1964 159  HOH WAT A . 
G 7 HOH 160  1965 160  HOH WAT A . 
G 7 HOH 161  1966 161  HOH WAT A . 
G 7 HOH 162  1967 162  HOH WAT A . 
G 7 HOH 163  1968 163  HOH WAT A . 
G 7 HOH 164  1969 164  HOH WAT A . 
G 7 HOH 165  1970 165  HOH WAT A . 
G 7 HOH 166  1971 166  HOH WAT A . 
G 7 HOH 167  1972 167  HOH WAT A . 
G 7 HOH 168  1973 168  HOH WAT A . 
G 7 HOH 169  1974 169  HOH WAT A . 
G 7 HOH 170  1975 170  HOH WAT A . 
G 7 HOH 171  1976 171  HOH WAT A . 
G 7 HOH 172  1977 172  HOH WAT A . 
G 7 HOH 173  1978 173  HOH WAT A . 
G 7 HOH 174  1979 174  HOH WAT A . 
G 7 HOH 175  1980 175  HOH WAT A . 
G 7 HOH 176  1981 176  HOH WAT A . 
G 7 HOH 177  1982 177  HOH WAT A . 
G 7 HOH 178  1983 178  HOH WAT A . 
G 7 HOH 179  1984 179  HOH WAT A . 
G 7 HOH 180  1985 180  HOH WAT A . 
G 7 HOH 181  1986 181  HOH WAT A . 
G 7 HOH 182  1987 182  HOH WAT A . 
G 7 HOH 183  1988 183  HOH WAT A . 
G 7 HOH 184  1989 184  HOH WAT A . 
G 7 HOH 185  1990 185  HOH WAT A . 
G 7 HOH 186  1991 186  HOH WAT A . 
G 7 HOH 187  1992 187  HOH WAT A . 
G 7 HOH 188  1993 188  HOH WAT A . 
G 7 HOH 189  1994 189  HOH WAT A . 
G 7 HOH 190  1995 190  HOH WAT A . 
G 7 HOH 191  1996 191  HOH WAT A . 
G 7 HOH 192  1997 192  HOH WAT A . 
G 7 HOH 193  1998 193  HOH WAT A . 
G 7 HOH 194  1999 194  HOH WAT A . 
G 7 HOH 195  2000 195  HOH WAT A . 
G 7 HOH 196  2001 196  HOH WAT A . 
G 7 HOH 197  2002 197  HOH WAT A . 
G 7 HOH 198  2003 198  HOH WAT A . 
G 7 HOH 199  2004 199  HOH WAT A . 
G 7 HOH 200  2005 200  HOH WAT A . 
G 7 HOH 201  2006 201  HOH WAT A . 
G 7 HOH 202  2007 202  HOH WAT A . 
G 7 HOH 203  2008 203  HOH WAT A . 
G 7 HOH 204  2009 204  HOH WAT A . 
G 7 HOH 205  2010 205  HOH WAT A . 
G 7 HOH 206  2011 206  HOH WAT A . 
G 7 HOH 207  2012 207  HOH WAT A . 
G 7 HOH 208  2013 208  HOH WAT A . 
G 7 HOH 209  2014 209  HOH WAT A . 
G 7 HOH 210  2015 210  HOH WAT A . 
G 7 HOH 211  2016 211  HOH WAT A . 
G 7 HOH 212  2017 212  HOH WAT A . 
G 7 HOH 213  2018 213  HOH WAT A . 
G 7 HOH 214  2019 214  HOH WAT A . 
G 7 HOH 215  2020 215  HOH WAT A . 
G 7 HOH 216  2021 216  HOH WAT A . 
G 7 HOH 217  2022 217  HOH WAT A . 
G 7 HOH 218  2023 218  HOH WAT A . 
G 7 HOH 219  2024 219  HOH WAT A . 
G 7 HOH 220  2025 220  HOH WAT A . 
G 7 HOH 221  2026 221  HOH WAT A . 
G 7 HOH 222  2027 222  HOH WAT A . 
G 7 HOH 223  2028 223  HOH WAT A . 
G 7 HOH 224  2029 224  HOH WAT A . 
G 7 HOH 225  2030 225  HOH WAT A . 
G 7 HOH 226  2031 226  HOH WAT A . 
G 7 HOH 227  2032 227  HOH WAT A . 
G 7 HOH 228  2033 228  HOH WAT A . 
G 7 HOH 229  2034 229  HOH WAT A . 
G 7 HOH 230  2035 230  HOH WAT A . 
G 7 HOH 231  2036 231  HOH WAT A . 
G 7 HOH 232  2037 232  HOH WAT A . 
G 7 HOH 233  2038 233  HOH WAT A . 
G 7 HOH 234  2039 234  HOH WAT A . 
G 7 HOH 235  2040 235  HOH WAT A . 
G 7 HOH 236  2041 236  HOH WAT A . 
G 7 HOH 237  2042 237  HOH WAT A . 
G 7 HOH 238  2043 238  HOH WAT A . 
G 7 HOH 239  2044 239  HOH WAT A . 
G 7 HOH 240  2045 240  HOH WAT A . 
G 7 HOH 241  2046 241  HOH WAT A . 
G 7 HOH 242  2047 242  HOH WAT A . 
G 7 HOH 243  2048 243  HOH WAT A . 
G 7 HOH 244  2049 244  HOH WAT A . 
G 7 HOH 245  2050 245  HOH WAT A . 
G 7 HOH 246  2051 246  HOH WAT A . 
G 7 HOH 247  2052 247  HOH WAT A . 
G 7 HOH 248  2053 248  HOH WAT A . 
G 7 HOH 249  2054 249  HOH WAT A . 
G 7 HOH 250  2055 250  HOH WAT A . 
G 7 HOH 251  2056 251  HOH WAT A . 
G 7 HOH 252  2057 252  HOH WAT A . 
G 7 HOH 253  2058 253  HOH WAT A . 
G 7 HOH 254  2059 254  HOH WAT A . 
G 7 HOH 255  2060 255  HOH WAT A . 
G 7 HOH 256  2061 256  HOH WAT A . 
G 7 HOH 257  2062 257  HOH WAT A . 
G 7 HOH 258  2063 258  HOH WAT A . 
G 7 HOH 259  2064 259  HOH WAT A . 
G 7 HOH 260  2065 260  HOH WAT A . 
G 7 HOH 261  2066 261  HOH WAT A . 
G 7 HOH 262  2067 262  HOH WAT A . 
G 7 HOH 263  2068 263  HOH WAT A . 
G 7 HOH 264  2069 264  HOH WAT A . 
G 7 HOH 265  2070 265  HOH WAT A . 
G 7 HOH 266  2071 266  HOH WAT A . 
G 7 HOH 267  2072 267  HOH WAT A . 
G 7 HOH 268  2073 268  HOH WAT A . 
G 7 HOH 269  2074 269  HOH WAT A . 
G 7 HOH 270  2075 270  HOH WAT A . 
G 7 HOH 271  2076 271  HOH WAT A . 
G 7 HOH 272  2077 272  HOH WAT A . 
G 7 HOH 273  2078 273  HOH WAT A . 
G 7 HOH 274  2079 274  HOH WAT A . 
G 7 HOH 275  2080 275  HOH WAT A . 
G 7 HOH 276  2081 276  HOH WAT A . 
G 7 HOH 277  2082 277  HOH WAT A . 
G 7 HOH 278  2083 278  HOH WAT A . 
G 7 HOH 279  2084 279  HOH WAT A . 
G 7 HOH 280  2085 280  HOH WAT A . 
G 7 HOH 281  2086 281  HOH WAT A . 
G 7 HOH 282  2087 282  HOH WAT A . 
G 7 HOH 283  2088 283  HOH WAT A . 
G 7 HOH 284  2089 284  HOH WAT A . 
G 7 HOH 285  2090 285  HOH WAT A . 
G 7 HOH 286  2091 286  HOH WAT A . 
G 7 HOH 287  2092 287  HOH WAT A . 
G 7 HOH 288  2093 288  HOH WAT A . 
G 7 HOH 289  2094 289  HOH WAT A . 
G 7 HOH 290  2095 290  HOH WAT A . 
G 7 HOH 291  2096 291  HOH WAT A . 
G 7 HOH 292  2097 292  HOH WAT A . 
G 7 HOH 293  2098 293  HOH WAT A . 
G 7 HOH 294  2099 294  HOH WAT A . 
G 7 HOH 295  2100 295  HOH WAT A . 
G 7 HOH 296  2101 296  HOH WAT A . 
G 7 HOH 297  2102 297  HOH WAT A . 
G 7 HOH 298  2103 298  HOH WAT A . 
G 7 HOH 299  2104 299  HOH WAT A . 
G 7 HOH 300  2105 300  HOH WAT A . 
G 7 HOH 301  2106 301  HOH WAT A . 
G 7 HOH 302  2107 302  HOH WAT A . 
G 7 HOH 303  2108 303  HOH WAT A . 
G 7 HOH 304  2109 304  HOH WAT A . 
G 7 HOH 305  2110 305  HOH WAT A . 
G 7 HOH 306  2111 306  HOH WAT A . 
G 7 HOH 307  2112 307  HOH WAT A . 
G 7 HOH 308  2113 308  HOH WAT A . 
G 7 HOH 309  2114 309  HOH WAT A . 
G 7 HOH 310  2115 310  HOH WAT A . 
G 7 HOH 311  2116 311  HOH WAT A . 
G 7 HOH 312  2117 312  HOH WAT A . 
G 7 HOH 313  2118 313  HOH WAT A . 
G 7 HOH 314  2119 314  HOH WAT A . 
G 7 HOH 315  2120 315  HOH WAT A . 
G 7 HOH 316  2121 316  HOH WAT A . 
G 7 HOH 317  2122 317  HOH WAT A . 
G 7 HOH 318  2123 318  HOH WAT A . 
G 7 HOH 319  2124 319  HOH WAT A . 
G 7 HOH 320  2125 320  HOH WAT A . 
G 7 HOH 321  2126 321  HOH WAT A . 
G 7 HOH 322  2127 322  HOH WAT A . 
G 7 HOH 323  2128 323  HOH WAT A . 
G 7 HOH 324  2129 324  HOH WAT A . 
G 7 HOH 325  2130 325  HOH WAT A . 
G 7 HOH 326  2131 326  HOH WAT A . 
G 7 HOH 327  2132 327  HOH WAT A . 
G 7 HOH 328  2133 328  HOH WAT A . 
G 7 HOH 329  2134 329  HOH WAT A . 
G 7 HOH 330  2135 330  HOH WAT A . 
G 7 HOH 331  2136 331  HOH WAT A . 
G 7 HOH 332  2137 332  HOH WAT A . 
G 7 HOH 333  2138 333  HOH WAT A . 
G 7 HOH 334  2139 334  HOH WAT A . 
G 7 HOH 335  2140 335  HOH WAT A . 
G 7 HOH 336  2141 336  HOH WAT A . 
G 7 HOH 337  2142 337  HOH WAT A . 
G 7 HOH 338  2143 338  HOH WAT A . 
G 7 HOH 339  2144 339  HOH WAT A . 
G 7 HOH 340  2145 340  HOH WAT A . 
G 7 HOH 341  2146 341  HOH WAT A . 
G 7 HOH 342  2147 342  HOH WAT A . 
G 7 HOH 343  2148 343  HOH WAT A . 
G 7 HOH 344  2149 344  HOH WAT A . 
G 7 HOH 345  2150 345  HOH WAT A . 
G 7 HOH 346  2151 346  HOH WAT A . 
G 7 HOH 347  2152 347  HOH WAT A . 
G 7 HOH 348  2153 348  HOH WAT A . 
G 7 HOH 349  2154 349  HOH WAT A . 
G 7 HOH 350  2155 350  HOH WAT A . 
G 7 HOH 351  2156 351  HOH WAT A . 
G 7 HOH 352  2157 352  HOH WAT A . 
G 7 HOH 353  2158 353  HOH WAT A . 
G 7 HOH 354  2159 354  HOH WAT A . 
G 7 HOH 355  2160 355  HOH WAT A . 
G 7 HOH 356  2161 356  HOH WAT A . 
G 7 HOH 357  2162 357  HOH WAT A . 
G 7 HOH 358  2163 358  HOH WAT A . 
G 7 HOH 359  2164 359  HOH WAT A . 
G 7 HOH 360  2165 360  HOH WAT A . 
G 7 HOH 361  2166 361  HOH WAT A . 
G 7 HOH 362  2167 362  HOH WAT A . 
G 7 HOH 363  2168 363  HOH WAT A . 
G 7 HOH 364  2169 364  HOH WAT A . 
G 7 HOH 365  2170 365  HOH WAT A . 
G 7 HOH 366  2171 366  HOH WAT A . 
G 7 HOH 367  2172 367  HOH WAT A . 
G 7 HOH 368  2173 368  HOH WAT A . 
G 7 HOH 369  2174 369  HOH WAT A . 
G 7 HOH 370  2175 370  HOH WAT A . 
G 7 HOH 371  2176 371  HOH WAT A . 
G 7 HOH 372  2177 372  HOH WAT A . 
G 7 HOH 373  2178 373  HOH WAT A . 
G 7 HOH 374  2179 374  HOH WAT A . 
G 7 HOH 375  2180 375  HOH WAT A . 
G 7 HOH 376  2181 376  HOH WAT A . 
G 7 HOH 377  2182 377  HOH WAT A . 
G 7 HOH 378  2183 378  HOH WAT A . 
G 7 HOH 379  2184 379  HOH WAT A . 
G 7 HOH 380  2185 380  HOH WAT A . 
G 7 HOH 381  2186 381  HOH WAT A . 
G 7 HOH 382  2187 382  HOH WAT A . 
G 7 HOH 383  2188 383  HOH WAT A . 
G 7 HOH 384  2189 384  HOH WAT A . 
G 7 HOH 385  2190 385  HOH WAT A . 
G 7 HOH 386  2191 386  HOH WAT A . 
G 7 HOH 387  2192 387  HOH WAT A . 
G 7 HOH 388  2193 388  HOH WAT A . 
G 7 HOH 389  2194 389  HOH WAT A . 
G 7 HOH 390  2195 390  HOH WAT A . 
G 7 HOH 391  2196 391  HOH WAT A . 
G 7 HOH 392  2197 392  HOH WAT A . 
G 7 HOH 393  2198 393  HOH WAT A . 
G 7 HOH 394  2199 394  HOH WAT A . 
G 7 HOH 395  2200 395  HOH WAT A . 
G 7 HOH 396  2201 396  HOH WAT A . 
G 7 HOH 397  2202 397  HOH WAT A . 
G 7 HOH 398  2203 398  HOH WAT A . 
G 7 HOH 399  2204 399  HOH WAT A . 
G 7 HOH 400  2205 400  HOH WAT A . 
G 7 HOH 401  2206 401  HOH WAT A . 
G 7 HOH 402  2207 402  HOH WAT A . 
G 7 HOH 403  2208 403  HOH WAT A . 
G 7 HOH 404  2209 404  HOH WAT A . 
G 7 HOH 405  2210 405  HOH WAT A . 
G 7 HOH 406  2211 406  HOH WAT A . 
G 7 HOH 407  2212 407  HOH WAT A . 
G 7 HOH 408  2213 408  HOH WAT A . 
G 7 HOH 409  2214 409  HOH WAT A . 
G 7 HOH 410  2215 410  HOH WAT A . 
G 7 HOH 411  2216 411  HOH WAT A . 
G 7 HOH 412  2217 412  HOH WAT A . 
G 7 HOH 413  2218 413  HOH WAT A . 
G 7 HOH 414  2219 414  HOH WAT A . 
G 7 HOH 415  2220 415  HOH WAT A . 
G 7 HOH 416  2221 416  HOH WAT A . 
G 7 HOH 417  2222 417  HOH WAT A . 
G 7 HOH 418  2223 418  HOH WAT A . 
G 7 HOH 419  2224 419  HOH WAT A . 
G 7 HOH 420  2225 420  HOH WAT A . 
G 7 HOH 421  2226 421  HOH WAT A . 
G 7 HOH 422  2227 422  HOH WAT A . 
G 7 HOH 423  2228 423  HOH WAT A . 
G 7 HOH 424  2229 424  HOH WAT A . 
G 7 HOH 425  2230 425  HOH WAT A . 
G 7 HOH 426  2231 426  HOH WAT A . 
G 7 HOH 427  2232 427  HOH WAT A . 
G 7 HOH 428  2233 428  HOH WAT A . 
G 7 HOH 429  2234 429  HOH WAT A . 
G 7 HOH 430  2235 430  HOH WAT A . 
G 7 HOH 431  2236 431  HOH WAT A . 
G 7 HOH 432  2237 432  HOH WAT A . 
G 7 HOH 433  2238 433  HOH WAT A . 
G 7 HOH 434  2239 434  HOH WAT A . 
G 7 HOH 435  2240 435  HOH WAT A . 
G 7 HOH 436  2241 436  HOH WAT A . 
G 7 HOH 437  2242 437  HOH WAT A . 
G 7 HOH 438  2243 438  HOH WAT A . 
G 7 HOH 439  2244 439  HOH WAT A . 
G 7 HOH 440  2245 440  HOH WAT A . 
G 7 HOH 441  2246 441  HOH WAT A . 
G 7 HOH 442  2247 442  HOH WAT A . 
G 7 HOH 443  2248 443  HOH WAT A . 
G 7 HOH 444  2249 444  HOH WAT A . 
G 7 HOH 445  2250 445  HOH WAT A . 
G 7 HOH 446  2251 446  HOH WAT A . 
G 7 HOH 447  2252 447  HOH WAT A . 
G 7 HOH 448  2253 448  HOH WAT A . 
G 7 HOH 449  2254 449  HOH WAT A . 
G 7 HOH 450  2255 450  HOH WAT A . 
G 7 HOH 451  2256 451  HOH WAT A . 
G 7 HOH 452  2257 452  HOH WAT A . 
G 7 HOH 453  2258 453  HOH WAT A . 
G 7 HOH 454  2259 454  HOH WAT A . 
G 7 HOH 455  2260 455  HOH WAT A . 
G 7 HOH 456  2261 456  HOH WAT A . 
G 7 HOH 457  2262 457  HOH WAT A . 
G 7 HOH 458  2263 458  HOH WAT A . 
G 7 HOH 459  2264 459  HOH WAT A . 
G 7 HOH 460  2265 460  HOH WAT A . 
G 7 HOH 461  2266 461  HOH WAT A . 
G 7 HOH 462  2267 462  HOH WAT A . 
G 7 HOH 463  2268 463  HOH WAT A . 
G 7 HOH 464  2269 464  HOH WAT A . 
G 7 HOH 465  2270 465  HOH WAT A . 
G 7 HOH 466  2271 466  HOH WAT A . 
G 7 HOH 467  2272 467  HOH WAT A . 
G 7 HOH 468  2273 468  HOH WAT A . 
G 7 HOH 469  2274 469  HOH WAT A . 
G 7 HOH 470  2275 470  HOH WAT A . 
G 7 HOH 471  2276 471  HOH WAT A . 
G 7 HOH 472  2277 472  HOH WAT A . 
G 7 HOH 473  2278 473  HOH WAT A . 
G 7 HOH 474  2279 474  HOH WAT A . 
G 7 HOH 475  2280 475  HOH WAT A . 
G 7 HOH 476  2281 476  HOH WAT A . 
G 7 HOH 477  2282 477  HOH WAT A . 
G 7 HOH 478  2283 478  HOH WAT A . 
G 7 HOH 479  2284 479  HOH WAT A . 
G 7 HOH 480  2285 480  HOH WAT A . 
G 7 HOH 481  2286 481  HOH WAT A . 
G 7 HOH 482  2287 482  HOH WAT A . 
G 7 HOH 483  2288 483  HOH WAT A . 
G 7 HOH 484  2289 484  HOH WAT A . 
G 7 HOH 485  2290 485  HOH WAT A . 
G 7 HOH 486  2291 486  HOH WAT A . 
G 7 HOH 487  2292 487  HOH WAT A . 
G 7 HOH 488  2293 488  HOH WAT A . 
G 7 HOH 489  2294 489  HOH WAT A . 
G 7 HOH 490  2295 490  HOH WAT A . 
G 7 HOH 491  2296 491  HOH WAT A . 
G 7 HOH 492  2297 492  HOH WAT A . 
G 7 HOH 493  2298 493  HOH WAT A . 
G 7 HOH 494  2299 494  HOH WAT A . 
G 7 HOH 495  2300 495  HOH WAT A . 
G 7 HOH 496  2301 496  HOH WAT A . 
G 7 HOH 497  2302 497  HOH WAT A . 
G 7 HOH 498  2303 498  HOH WAT A . 
G 7 HOH 499  2304 499  HOH WAT A . 
G 7 HOH 500  2305 500  HOH WAT A . 
G 7 HOH 501  2306 501  HOH WAT A . 
G 7 HOH 502  2307 502  HOH WAT A . 
G 7 HOH 503  2308 503  HOH WAT A . 
G 7 HOH 504  2309 504  HOH WAT A . 
G 7 HOH 505  2310 505  HOH WAT A . 
G 7 HOH 506  2311 506  HOH WAT A . 
G 7 HOH 507  2312 507  HOH WAT A . 
G 7 HOH 508  2313 508  HOH WAT A . 
G 7 HOH 509  2314 509  HOH WAT A . 
G 7 HOH 510  2315 510  HOH WAT A . 
G 7 HOH 511  2316 511  HOH WAT A . 
G 7 HOH 512  2317 512  HOH WAT A . 
G 7 HOH 513  2318 513  HOH WAT A . 
G 7 HOH 514  2319 514  HOH WAT A . 
G 7 HOH 515  2320 515  HOH WAT A . 
G 7 HOH 516  2321 516  HOH WAT A . 
G 7 HOH 517  2322 517  HOH WAT A . 
G 7 HOH 518  2323 518  HOH WAT A . 
G 7 HOH 519  2324 519  HOH WAT A . 
G 7 HOH 520  2325 520  HOH WAT A . 
G 7 HOH 521  2326 521  HOH WAT A . 
G 7 HOH 522  2327 522  HOH WAT A . 
G 7 HOH 523  2328 523  HOH WAT A . 
G 7 HOH 524  2329 524  HOH WAT A . 
G 7 HOH 525  2330 525  HOH WAT A . 
G 7 HOH 526  2331 526  HOH WAT A . 
G 7 HOH 527  2332 527  HOH WAT A . 
G 7 HOH 528  2333 528  HOH WAT A . 
G 7 HOH 529  2334 529  HOH WAT A . 
G 7 HOH 530  2335 530  HOH WAT A . 
G 7 HOH 531  2336 531  HOH WAT A . 
G 7 HOH 532  2337 532  HOH WAT A . 
G 7 HOH 533  2338 533  HOH WAT A . 
G 7 HOH 534  2339 534  HOH WAT A . 
G 7 HOH 535  2340 535  HOH WAT A . 
G 7 HOH 536  2341 536  HOH WAT A . 
G 7 HOH 537  2342 537  HOH WAT A . 
G 7 HOH 538  2343 538  HOH WAT A . 
G 7 HOH 539  2344 539  HOH WAT A . 
G 7 HOH 540  2345 540  HOH WAT A . 
G 7 HOH 541  2346 541  HOH WAT A . 
G 7 HOH 542  2347 542  HOH WAT A . 
G 7 HOH 543  2348 543  HOH WAT A . 
G 7 HOH 544  2349 544  HOH WAT A . 
G 7 HOH 545  2350 545  HOH WAT A . 
G 7 HOH 546  2351 546  HOH WAT A . 
G 7 HOH 547  2352 547  HOH WAT A . 
G 7 HOH 548  2353 548  HOH WAT A . 
G 7 HOH 549  2354 549  HOH WAT A . 
G 7 HOH 550  2355 550  HOH WAT A . 
G 7 HOH 551  2356 551  HOH WAT A . 
G 7 HOH 552  2357 552  HOH WAT A . 
G 7 HOH 553  2358 553  HOH WAT A . 
G 7 HOH 554  2359 554  HOH WAT A . 
G 7 HOH 555  2360 555  HOH WAT A . 
G 7 HOH 556  2361 556  HOH WAT A . 
G 7 HOH 557  2362 557  HOH WAT A . 
G 7 HOH 558  2363 558  HOH WAT A . 
G 7 HOH 559  2364 559  HOH WAT A . 
G 7 HOH 560  2365 560  HOH WAT A . 
G 7 HOH 561  2366 561  HOH WAT A . 
G 7 HOH 562  2367 562  HOH WAT A . 
G 7 HOH 563  2368 563  HOH WAT A . 
G 7 HOH 564  2369 564  HOH WAT A . 
G 7 HOH 565  2370 565  HOH WAT A . 
G 7 HOH 566  2371 566  HOH WAT A . 
G 7 HOH 567  2372 567  HOH WAT A . 
G 7 HOH 568  2373 568  HOH WAT A . 
G 7 HOH 569  2374 569  HOH WAT A . 
G 7 HOH 570  2375 570  HOH WAT A . 
G 7 HOH 571  2376 571  HOH WAT A . 
G 7 HOH 572  2377 572  HOH WAT A . 
G 7 HOH 573  2378 573  HOH WAT A . 
G 7 HOH 574  2379 574  HOH WAT A . 
G 7 HOH 575  2380 575  HOH WAT A . 
G 7 HOH 576  2381 576  HOH WAT A . 
G 7 HOH 577  2382 577  HOH WAT A . 
G 7 HOH 578  2383 578  HOH WAT A . 
G 7 HOH 579  2384 579  HOH WAT A . 
G 7 HOH 580  2385 580  HOH WAT A . 
G 7 HOH 581  2386 581  HOH WAT A . 
G 7 HOH 582  2387 582  HOH WAT A . 
G 7 HOH 583  2388 583  HOH WAT A . 
G 7 HOH 584  2389 584  HOH WAT A . 
G 7 HOH 585  2390 585  HOH WAT A . 
G 7 HOH 586  2391 586  HOH WAT A . 
G 7 HOH 587  2392 587  HOH WAT A . 
G 7 HOH 588  2393 588  HOH WAT A . 
G 7 HOH 589  2394 589  HOH WAT A . 
G 7 HOH 590  2395 590  HOH WAT A . 
G 7 HOH 591  2396 591  HOH WAT A . 
G 7 HOH 592  2397 592  HOH WAT A . 
G 7 HOH 593  2398 593  HOH WAT A . 
G 7 HOH 594  2399 594  HOH WAT A . 
G 7 HOH 595  2400 595  HOH WAT A . 
G 7 HOH 596  2401 596  HOH WAT A . 
G 7 HOH 597  2402 597  HOH WAT A . 
G 7 HOH 598  2403 598  HOH WAT A . 
G 7 HOH 599  2404 599  HOH WAT A . 
G 7 HOH 600  2405 600  HOH WAT A . 
G 7 HOH 601  2406 601  HOH WAT A . 
G 7 HOH 602  2407 602  HOH WAT A . 
G 7 HOH 603  2408 603  HOH WAT A . 
G 7 HOH 604  2409 604  HOH WAT A . 
G 7 HOH 605  2410 605  HOH WAT A . 
G 7 HOH 606  2411 606  HOH WAT A . 
G 7 HOH 607  2412 607  HOH WAT A . 
G 7 HOH 608  2413 608  HOH WAT A . 
G 7 HOH 609  2414 609  HOH WAT A . 
G 7 HOH 610  2415 610  HOH WAT A . 
G 7 HOH 611  2416 611  HOH WAT A . 
G 7 HOH 612  2417 612  HOH WAT A . 
G 7 HOH 613  2418 613  HOH WAT A . 
G 7 HOH 614  2419 614  HOH WAT A . 
G 7 HOH 615  2420 615  HOH WAT A . 
G 7 HOH 616  2421 616  HOH WAT A . 
G 7 HOH 617  2422 617  HOH WAT A . 
G 7 HOH 618  2423 618  HOH WAT A . 
G 7 HOH 619  2424 619  HOH WAT A . 
G 7 HOH 620  2425 620  HOH WAT A . 
G 7 HOH 621  2426 621  HOH WAT A . 
G 7 HOH 622  2427 622  HOH WAT A . 
G 7 HOH 623  2428 623  HOH WAT A . 
G 7 HOH 624  2429 624  HOH WAT A . 
G 7 HOH 625  2430 625  HOH WAT A . 
G 7 HOH 626  2431 626  HOH WAT A . 
G 7 HOH 627  2432 627  HOH WAT A . 
G 7 HOH 628  2433 628  HOH WAT A . 
G 7 HOH 629  2434 629  HOH WAT A . 
G 7 HOH 630  2435 630  HOH WAT A . 
G 7 HOH 631  2436 631  HOH WAT A . 
G 7 HOH 632  2437 632  HOH WAT A . 
G 7 HOH 633  2438 633  HOH WAT A . 
G 7 HOH 634  2439 634  HOH WAT A . 
G 7 HOH 635  2440 635  HOH WAT A . 
G 7 HOH 636  2441 636  HOH WAT A . 
G 7 HOH 637  2442 637  HOH WAT A . 
G 7 HOH 638  2443 638  HOH WAT A . 
G 7 HOH 639  2444 639  HOH WAT A . 
G 7 HOH 640  2445 640  HOH WAT A . 
G 7 HOH 641  2446 641  HOH WAT A . 
G 7 HOH 642  2447 642  HOH WAT A . 
G 7 HOH 643  2448 643  HOH WAT A . 
G 7 HOH 644  2449 644  HOH WAT A . 
G 7 HOH 645  2450 645  HOH WAT A . 
G 7 HOH 646  2451 646  HOH WAT A . 
G 7 HOH 647  2452 647  HOH WAT A . 
G 7 HOH 648  2453 648  HOH WAT A . 
G 7 HOH 649  2454 649  HOH WAT A . 
G 7 HOH 650  2455 650  HOH WAT A . 
G 7 HOH 651  2456 651  HOH WAT A . 
G 7 HOH 652  2457 652  HOH WAT A . 
G 7 HOH 653  2458 653  HOH WAT A . 
G 7 HOH 654  2459 654  HOH WAT A . 
G 7 HOH 655  2460 655  HOH WAT A . 
G 7 HOH 656  2461 656  HOH WAT A . 
G 7 HOH 657  2462 657  HOH WAT A . 
G 7 HOH 658  2463 658  HOH WAT A . 
G 7 HOH 659  2464 659  HOH WAT A . 
G 7 HOH 660  2465 660  HOH WAT A . 
G 7 HOH 661  2466 661  HOH WAT A . 
G 7 HOH 662  2467 662  HOH WAT A . 
G 7 HOH 663  2468 663  HOH WAT A . 
G 7 HOH 664  2469 664  HOH WAT A . 
G 7 HOH 665  2470 665  HOH WAT A . 
G 7 HOH 666  2471 666  HOH WAT A . 
G 7 HOH 667  2472 667  HOH WAT A . 
G 7 HOH 668  2473 668  HOH WAT A . 
G 7 HOH 669  2474 669  HOH WAT A . 
G 7 HOH 670  2475 670  HOH WAT A . 
G 7 HOH 671  2476 671  HOH WAT A . 
G 7 HOH 672  2477 672  HOH WAT A . 
G 7 HOH 673  2478 673  HOH WAT A . 
G 7 HOH 674  2479 674  HOH WAT A . 
G 7 HOH 675  2480 675  HOH WAT A . 
G 7 HOH 676  2481 676  HOH WAT A . 
G 7 HOH 677  2482 677  HOH WAT A . 
G 7 HOH 678  2483 678  HOH WAT A . 
G 7 HOH 679  2484 679  HOH WAT A . 
G 7 HOH 680  2485 680  HOH WAT A . 
G 7 HOH 681  2486 681  HOH WAT A . 
G 7 HOH 682  2487 682  HOH WAT A . 
G 7 HOH 683  2488 683  HOH WAT A . 
G 7 HOH 684  2489 684  HOH WAT A . 
G 7 HOH 685  2490 685  HOH WAT A . 
G 7 HOH 686  2491 686  HOH WAT A . 
G 7 HOH 687  2492 687  HOH WAT A . 
G 7 HOH 688  2493 688  HOH WAT A . 
G 7 HOH 689  2494 689  HOH WAT A . 
G 7 HOH 690  2495 690  HOH WAT A . 
G 7 HOH 691  2496 691  HOH WAT A . 
G 7 HOH 692  2497 692  HOH WAT A . 
G 7 HOH 693  2498 693  HOH WAT A . 
G 7 HOH 694  2499 694  HOH WAT A . 
G 7 HOH 695  2500 695  HOH WAT A . 
G 7 HOH 696  2501 696  HOH WAT A . 
G 7 HOH 697  2502 697  HOH WAT A . 
G 7 HOH 698  2503 698  HOH WAT A . 
G 7 HOH 699  2504 699  HOH WAT A . 
G 7 HOH 700  2505 700  HOH WAT A . 
G 7 HOH 701  2506 701  HOH WAT A . 
G 7 HOH 702  2507 702  HOH WAT A . 
G 7 HOH 703  2508 703  HOH WAT A . 
G 7 HOH 704  2509 704  HOH WAT A . 
G 7 HOH 705  2510 705  HOH WAT A . 
G 7 HOH 706  2511 706  HOH WAT A . 
G 7 HOH 707  2512 707  HOH WAT A . 
G 7 HOH 708  2513 708  HOH WAT A . 
G 7 HOH 709  2514 709  HOH WAT A . 
G 7 HOH 710  2515 710  HOH WAT A . 
G 7 HOH 711  2516 711  HOH WAT A . 
G 7 HOH 712  2517 712  HOH WAT A . 
G 7 HOH 713  2518 713  HOH WAT A . 
G 7 HOH 714  2519 714  HOH WAT A . 
G 7 HOH 715  2520 715  HOH WAT A . 
G 7 HOH 716  2521 716  HOH WAT A . 
G 7 HOH 717  2522 717  HOH WAT A . 
G 7 HOH 718  2523 718  HOH WAT A . 
G 7 HOH 719  2524 719  HOH WAT A . 
G 7 HOH 720  2525 720  HOH WAT A . 
G 7 HOH 721  2526 721  HOH WAT A . 
G 7 HOH 722  2527 722  HOH WAT A . 
G 7 HOH 723  2528 723  HOH WAT A . 
G 7 HOH 724  2529 724  HOH WAT A . 
G 7 HOH 725  2530 725  HOH WAT A . 
G 7 HOH 726  2531 726  HOH WAT A . 
G 7 HOH 727  2532 727  HOH WAT A . 
G 7 HOH 728  2533 728  HOH WAT A . 
G 7 HOH 729  2534 729  HOH WAT A . 
G 7 HOH 730  2535 730  HOH WAT A . 
G 7 HOH 731  2536 731  HOH WAT A . 
G 7 HOH 732  2537 732  HOH WAT A . 
G 7 HOH 733  2538 733  HOH WAT A . 
G 7 HOH 734  2539 734  HOH WAT A . 
G 7 HOH 735  2540 735  HOH WAT A . 
G 7 HOH 736  2541 736  HOH WAT A . 
G 7 HOH 737  2542 737  HOH WAT A . 
G 7 HOH 738  2543 738  HOH WAT A . 
G 7 HOH 739  2544 739  HOH WAT A . 
G 7 HOH 740  2545 740  HOH WAT A . 
G 7 HOH 741  2546 741  HOH WAT A . 
G 7 HOH 742  2547 742  HOH WAT A . 
G 7 HOH 743  2548 743  HOH WAT A . 
G 7 HOH 744  2549 744  HOH WAT A . 
G 7 HOH 745  2550 745  HOH WAT A . 
G 7 HOH 746  2551 746  HOH WAT A . 
G 7 HOH 747  2552 747  HOH WAT A . 
G 7 HOH 748  2553 748  HOH WAT A . 
G 7 HOH 749  2554 749  HOH WAT A . 
G 7 HOH 750  2555 750  HOH WAT A . 
G 7 HOH 751  2556 751  HOH WAT A . 
G 7 HOH 752  2557 752  HOH WAT A . 
G 7 HOH 753  2558 753  HOH WAT A . 
G 7 HOH 754  2559 754  HOH WAT A . 
G 7 HOH 755  2560 755  HOH WAT A . 
G 7 HOH 756  2561 756  HOH WAT A . 
G 7 HOH 757  2562 757  HOH WAT A . 
G 7 HOH 758  2563 758  HOH WAT A . 
G 7 HOH 759  2564 759  HOH WAT A . 
G 7 HOH 760  2565 760  HOH WAT A . 
G 7 HOH 761  2566 761  HOH WAT A . 
G 7 HOH 762  2567 762  HOH WAT A . 
G 7 HOH 763  2568 763  HOH WAT A . 
G 7 HOH 764  2569 764  HOH WAT A . 
G 7 HOH 765  2570 765  HOH WAT A . 
G 7 HOH 766  2571 766  HOH WAT A . 
G 7 HOH 767  2572 767  HOH WAT A . 
G 7 HOH 768  2573 768  HOH WAT A . 
G 7 HOH 769  2574 769  HOH WAT A . 
G 7 HOH 770  2575 770  HOH WAT A . 
G 7 HOH 771  2576 771  HOH WAT A . 
G 7 HOH 772  2577 772  HOH WAT A . 
G 7 HOH 773  2578 773  HOH WAT A . 
G 7 HOH 774  2579 774  HOH WAT A . 
G 7 HOH 775  2580 775  HOH WAT A . 
G 7 HOH 776  2581 776  HOH WAT A . 
G 7 HOH 777  2582 777  HOH WAT A . 
G 7 HOH 778  2583 778  HOH WAT A . 
G 7 HOH 779  2584 779  HOH WAT A . 
G 7 HOH 780  2585 780  HOH WAT A . 
G 7 HOH 781  2586 781  HOH WAT A . 
G 7 HOH 782  2587 782  HOH WAT A . 
G 7 HOH 783  2588 783  HOH WAT A . 
G 7 HOH 784  2589 784  HOH WAT A . 
G 7 HOH 785  2590 785  HOH WAT A . 
G 7 HOH 786  2591 786  HOH WAT A . 
G 7 HOH 787  2592 787  HOH WAT A . 
G 7 HOH 788  2593 788  HOH WAT A . 
G 7 HOH 789  2594 789  HOH WAT A . 
G 7 HOH 790  2595 790  HOH WAT A . 
G 7 HOH 791  2596 791  HOH WAT A . 
G 7 HOH 792  2597 792  HOH WAT A . 
G 7 HOH 793  2598 793  HOH WAT A . 
G 7 HOH 794  2599 794  HOH WAT A . 
G 7 HOH 795  2600 795  HOH WAT A . 
G 7 HOH 796  2601 796  HOH WAT A . 
G 7 HOH 797  2602 797  HOH WAT A . 
G 7 HOH 798  2603 798  HOH WAT A . 
G 7 HOH 799  2604 799  HOH WAT A . 
G 7 HOH 800  2605 800  HOH WAT A . 
G 7 HOH 801  2606 801  HOH WAT A . 
G 7 HOH 802  2607 802  HOH WAT A . 
G 7 HOH 803  2608 803  HOH WAT A . 
G 7 HOH 804  2609 804  HOH WAT A . 
G 7 HOH 805  2610 805  HOH WAT A . 
G 7 HOH 806  2611 806  HOH WAT A . 
G 7 HOH 807  2612 807  HOH WAT A . 
G 7 HOH 808  2613 808  HOH WAT A . 
G 7 HOH 809  2614 809  HOH WAT A . 
G 7 HOH 810  2615 810  HOH WAT A . 
G 7 HOH 811  2616 811  HOH WAT A . 
G 7 HOH 812  2617 812  HOH WAT A . 
G 7 HOH 813  2618 813  HOH WAT A . 
G 7 HOH 814  2619 814  HOH WAT A . 
G 7 HOH 815  2620 815  HOH WAT A . 
G 7 HOH 816  2621 816  HOH WAT A . 
G 7 HOH 817  2622 817  HOH WAT A . 
G 7 HOH 818  2623 818  HOH WAT A . 
G 7 HOH 819  2624 819  HOH WAT A . 
G 7 HOH 820  2625 820  HOH WAT A . 
G 7 HOH 821  2626 821  HOH WAT A . 
G 7 HOH 822  2627 822  HOH WAT A . 
G 7 HOH 823  2628 823  HOH WAT A . 
G 7 HOH 824  2629 824  HOH WAT A . 
G 7 HOH 825  2630 825  HOH WAT A . 
G 7 HOH 826  2631 826  HOH WAT A . 
G 7 HOH 827  2632 827  HOH WAT A . 
G 7 HOH 828  2633 828  HOH WAT A . 
G 7 HOH 829  2634 829  HOH WAT A . 
G 7 HOH 830  2635 830  HOH WAT A . 
G 7 HOH 831  2636 831  HOH WAT A . 
G 7 HOH 832  2637 832  HOH WAT A . 
G 7 HOH 833  2638 833  HOH WAT A . 
G 7 HOH 834  2639 834  HOH WAT A . 
G 7 HOH 835  2640 835  HOH WAT A . 
G 7 HOH 836  2641 836  HOH WAT A . 
G 7 HOH 837  2642 837  HOH WAT A . 
G 7 HOH 838  2643 838  HOH WAT A . 
G 7 HOH 839  2644 839  HOH WAT A . 
G 7 HOH 840  2645 840  HOH WAT A . 
G 7 HOH 841  2646 841  HOH WAT A . 
G 7 HOH 842  2647 842  HOH WAT A . 
G 7 HOH 843  2648 843  HOH WAT A . 
G 7 HOH 844  2649 844  HOH WAT A . 
G 7 HOH 845  2650 845  HOH WAT A . 
G 7 HOH 846  2651 846  HOH WAT A . 
G 7 HOH 847  2652 847  HOH WAT A . 
G 7 HOH 848  2653 848  HOH WAT A . 
G 7 HOH 849  2654 849  HOH WAT A . 
G 7 HOH 850  2655 850  HOH WAT A . 
G 7 HOH 851  2656 851  HOH WAT A . 
G 7 HOH 852  2657 852  HOH WAT A . 
G 7 HOH 853  2658 853  HOH WAT A . 
G 7 HOH 854  2659 854  HOH WAT A . 
G 7 HOH 855  2660 855  HOH WAT A . 
G 7 HOH 856  2661 856  HOH WAT A . 
G 7 HOH 857  2662 857  HOH WAT A . 
G 7 HOH 858  2663 858  HOH WAT A . 
G 7 HOH 859  2664 859  HOH WAT A . 
G 7 HOH 860  2665 860  HOH WAT A . 
G 7 HOH 861  2666 861  HOH WAT A . 
G 7 HOH 862  2667 862  HOH WAT A . 
G 7 HOH 863  2668 863  HOH WAT A . 
G 7 HOH 864  2669 864  HOH WAT A . 
G 7 HOH 865  2670 865  HOH WAT A . 
G 7 HOH 866  2671 866  HOH WAT A . 
G 7 HOH 867  2672 867  HOH WAT A . 
G 7 HOH 868  2673 868  HOH WAT A . 
G 7 HOH 869  2674 869  HOH WAT A . 
G 7 HOH 870  2675 870  HOH WAT A . 
G 7 HOH 871  2676 871  HOH WAT A . 
G 7 HOH 872  2677 872  HOH WAT A . 
G 7 HOH 873  2678 873  HOH WAT A . 
G 7 HOH 874  2679 874  HOH WAT A . 
G 7 HOH 875  2680 875  HOH WAT A . 
G 7 HOH 876  2681 876  HOH WAT A . 
G 7 HOH 877  2682 877  HOH WAT A . 
G 7 HOH 878  2683 878  HOH WAT A . 
G 7 HOH 879  2684 879  HOH WAT A . 
G 7 HOH 880  2685 880  HOH WAT A . 
G 7 HOH 881  2686 881  HOH WAT A . 
G 7 HOH 882  2687 882  HOH WAT A . 
G 7 HOH 883  2688 883  HOH WAT A . 
G 7 HOH 884  2689 884  HOH WAT A . 
G 7 HOH 885  2690 885  HOH WAT A . 
G 7 HOH 886  2691 886  HOH WAT A . 
G 7 HOH 887  2692 887  HOH WAT A . 
G 7 HOH 888  2693 888  HOH WAT A . 
G 7 HOH 889  2694 889  HOH WAT A . 
G 7 HOH 890  2695 890  HOH WAT A . 
G 7 HOH 891  2696 891  HOH WAT A . 
G 7 HOH 892  2697 892  HOH WAT A . 
G 7 HOH 893  2698 893  HOH WAT A . 
G 7 HOH 894  2699 894  HOH WAT A . 
G 7 HOH 895  2700 895  HOH WAT A . 
G 7 HOH 896  2701 896  HOH WAT A . 
G 7 HOH 897  2702 897  HOH WAT A . 
G 7 HOH 898  2703 898  HOH WAT A . 
G 7 HOH 899  2704 899  HOH WAT A . 
G 7 HOH 900  2705 900  HOH WAT A . 
G 7 HOH 901  2706 901  HOH WAT A . 
G 7 HOH 902  2707 902  HOH WAT A . 
G 7 HOH 903  2708 903  HOH WAT A . 
G 7 HOH 904  2709 904  HOH WAT A . 
G 7 HOH 905  2710 905  HOH WAT A . 
G 7 HOH 906  2711 906  HOH WAT A . 
G 7 HOH 907  2712 907  HOH WAT A . 
G 7 HOH 908  2713 908  HOH WAT A . 
G 7 HOH 909  2714 909  HOH WAT A . 
G 7 HOH 910  2715 910  HOH WAT A . 
G 7 HOH 911  2716 911  HOH WAT A . 
G 7 HOH 912  2717 912  HOH WAT A . 
G 7 HOH 913  2718 913  HOH WAT A . 
G 7 HOH 914  2719 914  HOH WAT A . 
G 7 HOH 915  2720 915  HOH WAT A . 
G 7 HOH 916  2721 916  HOH WAT A . 
G 7 HOH 917  2722 917  HOH WAT A . 
G 7 HOH 918  2723 918  HOH WAT A . 
G 7 HOH 919  2724 919  HOH WAT A . 
G 7 HOH 920  2725 920  HOH WAT A . 
G 7 HOH 921  2726 921  HOH WAT A . 
G 7 HOH 922  2727 922  HOH WAT A . 
G 7 HOH 923  2728 923  HOH WAT A . 
G 7 HOH 924  2729 924  HOH WAT A . 
G 7 HOH 925  2730 925  HOH WAT A . 
G 7 HOH 926  2731 926  HOH WAT A . 
G 7 HOH 927  2732 927  HOH WAT A . 
G 7 HOH 928  2733 928  HOH WAT A . 
G 7 HOH 929  2734 929  HOH WAT A . 
G 7 HOH 930  2735 930  HOH WAT A . 
G 7 HOH 931  2736 931  HOH WAT A . 
G 7 HOH 932  2737 932  HOH WAT A . 
G 7 HOH 933  2738 933  HOH WAT A . 
G 7 HOH 934  2739 934  HOH WAT A . 
G 7 HOH 935  2740 935  HOH WAT A . 
G 7 HOH 936  2741 936  HOH WAT A . 
G 7 HOH 937  2742 937  HOH WAT A . 
G 7 HOH 938  2743 938  HOH WAT A . 
G 7 HOH 939  2744 939  HOH WAT A . 
G 7 HOH 940  2745 940  HOH WAT A . 
G 7 HOH 941  2746 941  HOH WAT A . 
G 7 HOH 942  2747 942  HOH WAT A . 
G 7 HOH 943  2748 943  HOH WAT A . 
G 7 HOH 944  2749 944  HOH WAT A . 
G 7 HOH 945  2750 945  HOH WAT A . 
G 7 HOH 946  2751 946  HOH WAT A . 
G 7 HOH 947  2752 947  HOH WAT A . 
G 7 HOH 948  2753 948  HOH WAT A . 
G 7 HOH 949  2754 949  HOH WAT A . 
G 7 HOH 950  2755 950  HOH WAT A . 
G 7 HOH 951  2756 951  HOH WAT A . 
G 7 HOH 952  2757 952  HOH WAT A . 
G 7 HOH 953  2758 953  HOH WAT A . 
G 7 HOH 954  2759 954  HOH WAT A . 
G 7 HOH 955  2760 955  HOH WAT A . 
G 7 HOH 956  2761 956  HOH WAT A . 
G 7 HOH 957  2762 957  HOH WAT A . 
G 7 HOH 958  2763 958  HOH WAT A . 
G 7 HOH 959  2764 959  HOH WAT A . 
G 7 HOH 960  2765 960  HOH WAT A . 
G 7 HOH 961  2766 961  HOH WAT A . 
G 7 HOH 962  2767 962  HOH WAT A . 
G 7 HOH 963  2768 963  HOH WAT A . 
G 7 HOH 964  2769 964  HOH WAT A . 
G 7 HOH 965  2770 965  HOH WAT A . 
G 7 HOH 966  2771 966  HOH WAT A . 
G 7 HOH 967  2772 967  HOH WAT A . 
G 7 HOH 968  2773 968  HOH WAT A . 
G 7 HOH 969  2774 969  HOH WAT A . 
G 7 HOH 970  2775 970  HOH WAT A . 
G 7 HOH 971  2776 971  HOH WAT A . 
G 7 HOH 972  2777 972  HOH WAT A . 
G 7 HOH 973  2778 973  HOH WAT A . 
G 7 HOH 974  2779 974  HOH WAT A . 
G 7 HOH 975  2780 975  HOH WAT A . 
G 7 HOH 976  2781 976  HOH WAT A . 
G 7 HOH 977  2782 977  HOH WAT A . 
G 7 HOH 978  2783 978  HOH WAT A . 
G 7 HOH 979  2784 979  HOH WAT A . 
G 7 HOH 980  2785 980  HOH WAT A . 
G 7 HOH 981  2786 981  HOH WAT A . 
G 7 HOH 982  2787 982  HOH WAT A . 
G 7 HOH 983  2788 983  HOH WAT A . 
G 7 HOH 984  2789 984  HOH WAT A . 
G 7 HOH 985  2790 985  HOH WAT A . 
G 7 HOH 986  2791 986  HOH WAT A . 
G 7 HOH 987  2792 987  HOH WAT A . 
G 7 HOH 988  2793 988  HOH WAT A . 
G 7 HOH 989  2794 989  HOH WAT A . 
G 7 HOH 990  2795 990  HOH WAT A . 
G 7 HOH 991  2796 991  HOH WAT A . 
G 7 HOH 992  2797 992  HOH WAT A . 
G 7 HOH 993  2798 993  HOH WAT A . 
G 7 HOH 994  2799 994  HOH WAT A . 
G 7 HOH 995  2800 995  HOH WAT A . 
G 7 HOH 996  2801 996  HOH WAT A . 
G 7 HOH 997  2802 997  HOH WAT A . 
G 7 HOH 998  2803 998  HOH WAT A . 
G 7 HOH 999  2804 999  HOH WAT A . 
G 7 HOH 1000 2805 1000 HOH WAT A . 
G 7 HOH 1001 2806 1001 HOH WAT A . 
G 7 HOH 1002 2807 1002 HOH WAT A . 
G 7 HOH 1003 2808 1003 HOH WAT A . 
G 7 HOH 1004 2809 1004 HOH WAT A . 
G 7 HOH 1005 2810 1005 HOH WAT A . 
G 7 HOH 1006 2811 1006 HOH WAT A . 
G 7 HOH 1007 2812 1007 HOH WAT A . 
G 7 HOH 1008 2813 1008 HOH WAT A . 
G 7 HOH 1009 2814 1009 HOH WAT A . 
G 7 HOH 1010 2815 1010 HOH WAT A . 
G 7 HOH 1011 2816 1011 HOH WAT A . 
G 7 HOH 1012 2817 1012 HOH WAT A . 
G 7 HOH 1013 2818 1013 HOH WAT A . 
G 7 HOH 1014 2819 1014 HOH WAT A . 
G 7 HOH 1015 2820 1015 HOH WAT A . 
G 7 HOH 1016 2821 1016 HOH WAT A . 
G 7 HOH 1017 2822 1017 HOH WAT A . 
G 7 HOH 1018 2823 1018 HOH WAT A . 
G 7 HOH 1019 2824 1019 HOH WAT A . 
G 7 HOH 1020 2825 1020 HOH WAT A . 
G 7 HOH 1021 2826 1021 HOH WAT A . 
G 7 HOH 1022 2827 1022 HOH WAT A . 
G 7 HOH 1023 2828 1023 HOH WAT A . 
G 7 HOH 1024 2829 1024 HOH WAT A . 
G 7 HOH 1025 2830 1025 HOH WAT A . 
G 7 HOH 1026 2831 1026 HOH WAT A . 
G 7 HOH 1027 2832 1027 HOH WAT A . 
G 7 HOH 1028 2833 1028 HOH WAT A . 
G 7 HOH 1029 2834 1029 HOH WAT A . 
G 7 HOH 1030 2835 1030 HOH WAT A . 
G 7 HOH 1031 2836 1031 HOH WAT A . 
G 7 HOH 1032 2837 1032 HOH WAT A . 
G 7 HOH 1033 2838 1033 HOH WAT A . 
G 7 HOH 1034 2839 1034 HOH WAT A . 
G 7 HOH 1035 2840 1035 HOH WAT A . 
G 7 HOH 1036 2841 1036 HOH WAT A . 
G 7 HOH 1037 2842 1037 HOH WAT A . 
G 7 HOH 1038 2843 1038 HOH WAT A . 
G 7 HOH 1039 2844 1039 HOH WAT A . 
G 7 HOH 1040 2845 1040 HOH WAT A . 
G 7 HOH 1041 2846 1041 HOH WAT A . 
G 7 HOH 1042 2847 1042 HOH WAT A . 
G 7 HOH 1043 2848 1043 HOH WAT A . 
G 7 HOH 1044 2849 1044 HOH WAT A . 
G 7 HOH 1045 2850 1045 HOH WAT A . 
G 7 HOH 1046 2851 1046 HOH WAT A . 
G 7 HOH 1047 2852 1047 HOH WAT A . 
G 7 HOH 1048 2853 1048 HOH WAT A . 
G 7 HOH 1049 2854 1049 HOH WAT A . 
G 7 HOH 1050 2855 1050 HOH WAT A . 
G 7 HOH 1051 2856 1051 HOH WAT A . 
G 7 HOH 1052 2857 1052 HOH WAT A . 
G 7 HOH 1053 2858 1053 HOH WAT A . 
G 7 HOH 1054 2859 1054 HOH WAT A . 
G 7 HOH 1055 2860 1055 HOH WAT A . 
G 7 HOH 1056 2861 1056 HOH WAT A . 
G 7 HOH 1057 2862 1057 HOH WAT A . 
G 7 HOH 1058 2863 1058 HOH WAT A . 
G 7 HOH 1059 2864 1059 HOH WAT A . 
G 7 HOH 1060 2865 1060 HOH WAT A . 
G 7 HOH 1061 2866 1061 HOH WAT A . 
G 7 HOH 1062 2867 1062 HOH WAT A . 
G 7 HOH 1063 2868 1063 HOH WAT A . 
G 7 HOH 1064 2869 1064 HOH WAT A . 
G 7 HOH 1065 2870 1065 HOH WAT A . 
G 7 HOH 1066 2871 1066 HOH WAT A . 
G 7 HOH 1067 2872 1067 HOH WAT A . 
G 7 HOH 1068 2873 1068 HOH WAT A . 
G 7 HOH 1069 2874 1069 HOH WAT A . 
G 7 HOH 1070 2875 1070 HOH WAT A . 
G 7 HOH 1071 2876 1071 HOH WAT A . 
G 7 HOH 1072 2877 1072 HOH WAT A . 
G 7 HOH 1073 2878 1073 HOH WAT A . 
G 7 HOH 1074 2879 1074 HOH WAT A . 
G 7 HOH 1075 2880 1075 HOH WAT A . 
G 7 HOH 1076 2881 1076 HOH WAT A . 
G 7 HOH 1077 2882 1077 HOH WAT A . 
G 7 HOH 1078 2883 1078 HOH WAT A . 
G 7 HOH 1079 2884 1079 HOH WAT A . 
G 7 HOH 1080 2885 1080 HOH WAT A . 
G 7 HOH 1081 2886 1081 HOH WAT A . 
G 7 HOH 1082 2887 1082 HOH WAT A . 
G 7 HOH 1083 2888 1083 HOH WAT A . 
G 7 HOH 1084 2889 1084 HOH WAT A . 
G 7 HOH 1085 2890 1085 HOH WAT A . 
G 7 HOH 1086 2891 1086 HOH WAT A . 
G 7 HOH 1087 2892 1087 HOH WAT A . 
G 7 HOH 1088 2893 1088 HOH WAT A . 
G 7 HOH 1089 2894 1089 HOH WAT A . 
G 7 HOH 1090 2895 1090 HOH WAT A . 
G 7 HOH 1091 2896 1091 HOH WAT A . 
G 7 HOH 1092 2897 1092 HOH WAT A . 
G 7 HOH 1093 2898 1093 HOH WAT A . 
G 7 HOH 1094 2899 1094 HOH WAT A . 
G 7 HOH 1095 2900 1095 HOH WAT A . 
G 7 HOH 1096 2901 1096 HOH WAT A . 
G 7 HOH 1097 2902 1097 HOH WAT A . 
G 7 HOH 1098 2903 1098 HOH WAT A . 
G 7 HOH 1099 2904 1099 HOH WAT 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,G 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 90  ? A HIS 90   ? 1_555 ZN ? D ZN . ? A ZN 1805 ? 1_555 OD1 ? A ASP 92  ? A ASP 92   ? 1_555 93.2  ? 
2  NE2 ? A HIS 90  ? A HIS 90   ? 1_555 ZN ? D ZN . ? A ZN 1805 ? 1_555 OD2 ? A ASP 204 ? A ASP 204  ? 1_555 96.8  ? 
3  OD1 ? A ASP 92  ? A ASP 92   ? 1_555 ZN ? D ZN . ? A ZN 1805 ? 1_555 OD2 ? A ASP 204 ? A ASP 204  ? 1_555 168.1 ? 
4  NE2 ? A HIS 90  ? A HIS 90   ? 1_555 ZN ? D ZN . ? A ZN 1805 ? 1_555 NE2 ? A HIS 471 ? A HIS 471  ? 1_555 104.7 ? 
5  OD1 ? A ASP 92  ? A ASP 92   ? 1_555 ZN ? D ZN . ? A ZN 1805 ? 1_555 NE2 ? A HIS 471 ? A HIS 471  ? 1_555 91.7  ? 
6  OD2 ? A ASP 204 ? A ASP 204  ? 1_555 ZN ? D ZN . ? A ZN 1805 ? 1_555 NE2 ? A HIS 471 ? A HIS 471  ? 1_555 92.1  ? 
7  NE2 ? A HIS 90  ? A HIS 90   ? 1_555 ZN ? D ZN . ? A ZN 1805 ? 1_555 O3  ? E GB2 .   ? A GB2 1804 ? 1_555 162.5 ? 
8  OD1 ? A ASP 92  ? A ASP 92   ? 1_555 ZN ? D ZN . ? A ZN 1805 ? 1_555 O3  ? E GB2 .   ? A GB2 1804 ? 1_555 86.5  ? 
9  OD2 ? A ASP 204 ? A ASP 204  ? 1_555 ZN ? D ZN . ? A ZN 1805 ? 1_555 O3  ? E GB2 .   ? A GB2 1804 ? 1_555 82.1  ? 
10 NE2 ? A HIS 471 ? A HIS 471  ? 1_555 ZN ? D ZN . ? A ZN 1805 ? 1_555 O3  ? E GB2 .   ? A GB2 1804 ? 1_555 92.8  ? 
11 NE2 ? A HIS 90  ? A HIS 90   ? 1_555 ZN ? D ZN . ? A ZN 1805 ? 1_555 O4  ? E GB2 .   ? A GB2 1804 ? 1_555 90.3  ? 
12 OD1 ? A ASP 92  ? A ASP 92   ? 1_555 ZN ? D ZN . ? A ZN 1805 ? 1_555 O4  ? E GB2 .   ? A GB2 1804 ? 1_555 89.8  ? 
13 OD2 ? A ASP 204 ? A ASP 204  ? 1_555 ZN ? D ZN . ? A ZN 1805 ? 1_555 O4  ? E GB2 .   ? A GB2 1804 ? 1_555 83.7  ? 
14 NE2 ? A HIS 471 ? A HIS 471  ? 1_555 ZN ? D ZN . ? A ZN 1805 ? 1_555 O4  ? E GB2 .   ? A GB2 1804 ? 1_555 164.8 ? 
15 O3  ? E GB2 .   ? A GB2 1804 ? 1_555 ZN ? D ZN . ? A ZN 1805 ? 1_555 O4  ? E GB2 .   ? A GB2 1804 ? 1_555 72.2  ? 
# 
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 2006-12-05 
2 'Structure model' 1 1 2007-10-16 
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       1.1 ? 1 
HKL-2000  'data reduction' .   ? 2 
SCALEPACK 'data scaling'   .   ? 3 
CNS       phasing          .   ? 4 
# 
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 CG A GLN 97  ? ? CD A GLN 97  ? B 1.677 1.506 0.171  0.023 N 
2 1 CA A SER 411 ? ? CB A SER 411 ? B 1.707 1.525 0.182  0.015 N 
3 1 CB A ARG 770 ? ? CG A ARG 770 ? B 1.319 1.521 -0.202 0.027 N 
# 
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 CB A ASP 204 ? ? CG A ASP 204 ? ? OD1 A ASP 204 ? ? 123.77 118.30 5.47  0.90 N 
2 1 NE A ARG 818 ? B CZ A ARG 818 ? B NH2 A ARG 818 ? B 117.27 120.30 -3.03 0.50 N 
3 1 NE A ARG 963 ? ? CZ A ARG 963 ? ? NH1 A ARG 963 ? ? 123.61 120.30 3.31  0.50 N 
4 1 NE A ARG 963 ? ? CZ A ARG 963 ? ? NH2 A ARG 963 ? ? 117.09 120.30 -3.21 0.50 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 ASP A 56  ? ? -103.63 78.55   
2  1 TRP A 95  ? ? -172.00 -86.15  
3  1 ASP A 106 ? ? -131.62 -58.11  
4  1 THR A 162 ? ? 68.54   -64.05  
5  1 GLN A 227 ? ? -137.57 -45.99  
6  1 ASP A 340 ? ? -170.66 -170.61 
7  1 LYS A 345 ? ? -92.62  -71.52  
8  1 SER A 411 ? ? 40.53   -122.07 
9  1 TRP A 415 ? ? -90.32  58.07   
10 1 HIS A 471 ? ? -69.76  4.53    
11 1 ILE A 549 ? ? -148.69 -47.26  
12 1 LEU A 550 ? ? -165.95 116.03  
13 1 PRO A 562 ? ? -80.62  38.61   
14 1 SER A 703 ? ? -42.70  158.17  
15 1 ASN A 732 ? ? -97.04  56.63   
16 1 SER A 762 ? ? 71.36   -3.25   
17 1 ILE A 831 ? ? -118.10 77.59   
18 1 SER A 833 ? ? -153.13 -13.45  
19 1 ASP A 839 ? ? -128.08 -162.11 
20 1 PRO A 990 ? ? -39.17  -79.51  
21 1 GLU A 991 ? ? 55.41   94.17   
22 1 GLU A 992 ? ? -134.40 -139.38 
23 1 HIS A 993 ? ? 33.34   72.50   
# 
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 75  ? B 12.77 
2 1 HIS A 709 ? B 10.62 
# 
_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     1801 
_pdbx_validate_chiral.PDB_ins_code    ? 
_pdbx_validate_chiral.details         'WRONG HAND' 
_pdbx_validate_chiral.omega           . 
# 
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 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 N-ACETYL-D-GLUCOSAMINE                                                           NAG 
3 'PHOSPHATE ION'                                                                  PO4 
4 'ZINC ION'                                                                       ZN  
5 '(2R,3R,4S)-2-({[(1S)-2-HYDROXY-1-PHENYLETHYL]AMINO}METHYL)PYRROLIDINE-3,4-DIOL' GB2 
6 '(4S)-2-METHYL-2,4-PENTANEDIOL'                                                  MPD 
7 water                                                                            HOH 
# 
