data_3BLB
# 
_entry.id   3BLB 
# 
_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   3BLB         
RCSB  RCSB045661   
WWPDB D_1000045661 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 1HTY 'dGMII + Tris'                                                                                       unspecified 
PDB 1HWW 'dGMII + Swainsonine, 1.87 Angstrom'                                                                 unspecified 
PDB 1HXK 'dGMII + Deoxymannojirimicin'                                                                        unspecified 
PDB 1PS2 'dGMII + Kifunensine'                                                                                unspecified 
PDB 1QWN 'dGMII + 5fluoro-Gulosylfluoride'                                                                    unspecified 
PDB 1QX1 'dGMII + 2F-mannosylF'                                                                               unspecified 
PDB 1R33 'dGMII + 5-thio-D-mannopyranosylamine'                                                               unspecified 
PDB 1R34 'dGMII + 5-thio-D-mannopyranosylamidinium salt'                                                      unspecified 
PDB 1TQS 'dGMII + Salacinol'                                                                                  unspecified 
PDB 1TQT 'dGMII + Diastereomer of Salacinol'                                                                  unspecified 
PDB 1TQU 'dGMII + Ghavamiol'                                                                                  unspecified 
PDB 1TQV 'dGMII + Blintol'                                                                                    unspecified 
PDB 1TQW 'dGMII + Blintol Diastereomer'                                                                       unspecified 
PDB 2ALW 'dGMII + Noeuromycin'                                                                                unspecified 
PDB 2F18 'dGMII + (2R,3R,4S)-2-({[(1R)-2-hydroxy-1-phenylethyl]amino}methyl)pyrrolidine-3,4-diol'             unspecified 
PDB 2F1A 'dGMII + (2R,3R,4S)-2-({[(1S)-2-hydroxy-1-phenylethyl]amino}methyl)pyrrolidine-3,4-diol'             unspecified 
PDB 2F1B 'dGMII + (2R,3R,4S,5R)-2-({[(1R)-2-hydroxy-1-phenylethyl]amino}methyl)-5-methylpyrrolidine-3,4-diol' unspecified 
PDB 2F7O 'dGMII + Mannostatin A'                                                                              unspecified 
PDB 2F7P 'dGMII + Benzyl-mannostatin A'                                                                       unspecified 
PDB 2F7Q 'dGMII + Aminocyclopentitetrol'                                                                      unspecified 
PDB 2F7R 'dGMII + Benzyl-aminocyclopentitetrol'                                                               unspecified 
# 
_pdbx_database_status.entry_id                        3BLB 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.recvd_initial_deposition_date   2007-12-10 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Kuntz, D.A.' 1 
'Rose, D.R.'  2 
# 
_citation.id                        primary 
_citation.title                     'Golgi Mannosidase II in complex with swainsonine at 1.3 Angstrom.' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Kuntz, D.A.' 1 
primary 'Rose, D.R.'  2 
# 
_cell.length_a           68.767 
_cell.length_b           109.662 
_cell.length_c           138.900 
_cell.angle_alpha        90.000 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.entry_id           3BLB 
_cell.pdbx_unique_axis   ? 
_cell.Z_PDB              4 
_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.space_group_name_H-M             'P 21 21 21' 
_symmetry.entry_id                         3BLB 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.Int_Tables_number                19 
_symmetry.cell_setting                     ? 
_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 2'                        119701.617 1    3.2.1.114 ? 'Catalytic domain: Residues 76-1108' ? 
2 non-polymer man N-ACETYL-D-GLUCOSAMINE                       221.208    1    ?         ? ?                                    ? 
3 non-polymer syn 'ZINC ION'                                   65.409     1    ?         ? ?                                    ? 
4 non-polymer syn 1S-8AB-OCTAHYDRO-INDOLIZIDINE-1A,2A,8B-TRIOL 173.210    1    ?         ? ?                                    ? 
5 non-polymer syn '(4R)-2-METHYLPENTANE-2,4-DIOL'              118.174    1    ?         ? ?                                    ? 
6 water       nat water                                        18.015     1068 ?         ? ?                                    ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'Alpha-mannosidase II, 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, CG18802' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    Berkeley 
_entity_src_gen.gene_src_tissue                    Head 
_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                    UNP 
_struct_ref.db_code                    MAN2_DROME 
_struct_ref.pdbx_db_accession          Q24451 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;DDPIRPPLKVARSPRPGQCQDVVQDVPNVDVQMLELYDRMSFKDIDGGVWKQGWNIKYDPLKYNAHHKLKVFVVPHSHND
PGWIQTFEEYYQHDTKHILSNALRHLHDNPEMKFIWAEISYFARFYHDLGENKKLQMKSIVKNGQLEFVTGGWVMPDEAN
SHWRNVLLQLTEGQTWLKQFMNVTPTASWAIDPFGHSPTMPYILQKSGFKNMLIQRTHYSVKKELAQQRQLEFLWRQIWD
NKGDTALFTHMMPFYSYDIPHTCGPDPKVCCQFDFKRMGSFGLSCPWKVPPRTISDQNVAARSDLLVDQWKKKAELYRTN
VLLIPLGDDFRFKQNTEWDVQRVNYERLFEHINSQAHFNVQAQFGTLQEYFDAVHQAERAGQAEFPTLSGDFFTYADRSD
NYWSGYYTSRPYHKRMDRVLMHYVRAAEMLSAWHSWDGMARIEERLEQARRELSLFQHHDGITGTAKTHVVVDYEQRMQE
ALKACQMVMQQSVYRLLTKPSIYSPDFSFSYFTLDDSRWPGSGVEDSRTTIILGEDILPSKHVVMHNTLPHWREQLVDFY
VSSPFVSVTDLANNPVEAQVSPVWSWHHDTLTKTIHPQGSTTKYRIIFKARVPPMGLATYVLTISDSKPEHTSYASNLLL
RKNPTSLPLGQYPEDVKFGDPREISLRVGNGPTLAFSEQGLLKSIQLTQDSPHVPVHFKFLKYGVRSHGDRSGAYLFLPN
GPASPVELGQPVVLVTKGKLESSVSVGLPSVVHQTIMRGGAPEIRNLVDIGSLDNTEIVMRLETHIDSGDIFYTDLNGLQ
FIKRRRLDKLPLQANYYPIPSGMFIEDANTRLTLLTGQPLGGSSLASGELEIMQDRRLASDDERGLGQGVLDNKPVLHIY
RLVLEKVNNCVRPSELHPAGYLTSAAHKASQSLLDPLDKFIFAENEWIGAQGQFGGDHPSAREDLDVSVMRRLTKSSAKT
QRVGYVLHRTNLMQCGTPEEHTQKLDVCHLLPNVARCERTTLTFLQNLEHLDGMVAPEVCPMETAAYVSSHSS
;
_struct_ref.pdbx_align_begin           76 
_struct_ref.pdbx_db_isoform            ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              3BLB 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 13 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 1045 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q24451 
_struct_ref_seq.db_align_beg                  76 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1108 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       13 
_struct_ref_seq.pdbx_auth_seq_align_end       1045 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 3BLB ARG A 1   ? UNP Q24451 ?   ?   'EXPRESSION TAG' 1   1  
1 3BLB SER A 2   ? UNP Q24451 ?   ?   'EXPRESSION TAG' 2   2  
1 3BLB SER A 3   ? UNP Q24451 ?   ?   'EXPRESSION TAG' 3   3  
1 3BLB HIS A 4   ? UNP Q24451 ?   ?   'EXPRESSION TAG' 4   4  
1 3BLB HIS A 5   ? UNP Q24451 ?   ?   'EXPRESSION TAG' 5   5  
1 3BLB HIS A 6   ? UNP Q24451 ?   ?   'EXPRESSION TAG' 6   6  
1 3BLB HIS A 7   ? UNP Q24451 ?   ?   'EXPRESSION TAG' 7   7  
1 3BLB HIS A 8   ? UNP Q24451 ?   ?   'EXPRESSION TAG' 8   8  
1 3BLB HIS A 9   ? UNP Q24451 ?   ?   'EXPRESSION TAG' 9   9  
1 3BLB GLY A 10  ? UNP Q24451 ?   ?   'EXPRESSION TAG' 10  10 
1 3BLB GLU A 11  ? UNP Q24451 ?   ?   'EXPRESSION TAG' 11  11 
1 3BLB PHE A 12  ? UNP Q24451 ?   ?   'EXPRESSION TAG' 12  12 
1 3BLB LYS A 907 ? UNP Q24451 GLU 970 CONFLICT         907 13 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                      ?           'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                                     ?           'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                                   ?           'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                              ?           'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE                                     ?           'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE                                    ?           'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                              ?           'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                                      ?           'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                                    ?           'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                                        ?           'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                   ?           'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                                      ?           'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                                       ?           'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE                                   ?           'C5 H11 N O2 S'  149.211 
MRD non-polymer         . '(4R)-2-METHYLPENTANE-2,4-DIOL'              ?           'C6 H14 O2'      118.174 
NAG D-saccharide        . N-ACETYL-D-GLUCOSAMINE                       ?           'C8 H15 N O6'    221.208 
PHE 'L-peptide linking' y PHENYLALANINE                                ?           'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                                      ?           'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                                       ?           'C3 H7 N O3'     105.093 
SWA non-polymer         . 1S-8AB-OCTAHYDRO-INDOLIZIDINE-1A,2A,8B-TRIOL SWAINSONINE 'C8 H15 N O3'    173.210 
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.crystals_number   1 
_exptl.entry_id          3BLB 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.16 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_percent_sol   43.07 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              7.0 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_details    'Tris-HCl, PEG 6000, MPD, NaCl, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K' 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'ADSC QUANTUM 4' 
_diffrn_detector.pdbx_collection_date   2002-03-21 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97400 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'CHESS BEAMLINE F1' 
_diffrn_source.pdbx_synchrotron_site       CHESS 
_diffrn_source.pdbx_synchrotron_beamline   F1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        0.97400 
# 
_reflns.entry_id                     3BLB 
_reflns.B_iso_Wilson_estimate        11.900 
_reflns.observed_criterion_sigma_F   0 
_reflns.observed_criterion_sigma_I   0 
_reflns.d_resolution_high            1.30 
_reflns.d_resolution_low             30 
_reflns.number_all                   254722 
_reflns.number_obs                   254722 
_reflns.percent_possible_obs         99.3 
_reflns.pdbx_Rmerge_I_obs            0.112 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        14.04 
_reflns.pdbx_redundancy              5.94 
_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             1.30 
_reflns_shell.d_res_low              1.32 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.percent_possible_all   98.4 
_reflns_shell.Rmerge_I_obs           0.654 
_reflns_shell.meanI_over_sigI_obs    2.34 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.pdbx_redundancy        4 
_reflns_shell.number_unique_all      13861 
_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                                 3BLB 
_refine.ls_d_res_high                            1.300 
_refine.ls_d_res_low                             29.830 
_refine.pdbx_data_cutoff_high_absF               261670.734 
_refine.pdbx_data_cutoff_low_absF                0.000 
_refine.ls_percent_reflns_obs                    95.700 
_refine.ls_number_reflns_obs                     246212 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.ls_R_factor_R_work                       0.166 
_refine.ls_R_factor_R_free                       0.185 
_refine.ls_percent_reflns_R_free                 4.800 
_refine.ls_number_reflns_R_free                  11766 
_refine.ls_R_factor_R_free_error                 0.002 
_refine.B_iso_mean                               14.100 
_refine.solvent_model_param_bsol                 57.908 
_refine.solvent_model_param_ksol                 0.380 
_refine.pdbx_isotropic_thermal_model             RESTRAINED 
_refine.aniso_B[1][1]                            -1.990 
_refine.aniso_B[2][2]                            0.180 
_refine.aniso_B[3][3]                            1.820 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            0.000 
_refine.aniso_B[2][3]                            0.000 
_refine.solvent_model_details                    'FLAT MODEL' 
_refine.overall_FOM_work_R_set                   0.900 
_refine.pdbx_ls_sigma_F                          0 
_refine.pdbx_ls_sigma_I                          ? 
_refine.ls_number_reflns_all                     246212 
_refine.ls_R_factor_all                          0.168 
_refine.ls_R_factor_obs                          0.168 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      'PDB entry 1HWW' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_stereochemistry_target_values       'Engh & Huber' 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.details                                  ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_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                        3BLB 
_refine_analyze.Luzzati_coordinate_error_obs    0.120 
_refine_analyze.Luzzati_sigma_a_obs             0.110 
_refine_analyze.Luzzati_d_res_low_obs           30.000 
_refine_analyze.Luzzati_coordinate_error_free   0.140 
_refine_analyze.Luzzati_sigma_a_free            0.120 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        8181 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         35 
_refine_hist.number_atoms_solvent             1068 
_refine_hist.number_atoms_total               9284 
_refine_hist.d_res_high                       1.300 
_refine_hist.d_res_low                        29.830 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
c_bond_d           ? 0.019  ?     ? 'X-RAY DIFFRACTION' ? 
c_angle_deg        ? 1.950  ?     ? 'X-RAY DIFFRACTION' ? 
c_dihedral_angle_d ? 25.400 ?     ? 'X-RAY DIFFRACTION' ? 
c_improper_angle_d ? 1.430  ?     ? 'X-RAY DIFFRACTION' ? 
c_mcbond_it        ? 1.520  1.500 ? 'X-RAY DIFFRACTION' ? 
c_mcangle_it       ? 2.130  2.000 ? 'X-RAY DIFFRACTION' ? 
c_scbond_it        ? 3.040  2.000 ? 'X-RAY DIFFRACTION' ? 
c_scangle_it       ? 4.200  2.500 ? 'X-RAY DIFFRACTION' ? 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
1.300 1.310 50 . 3672 . 0.260 0.285 . 207 . . 3879 . 'X-RAY DIFFRACTION' 
1.310 1.320 50 . 4341 . 0.251 0.288 . 207 . . 4548 . 'X-RAY DIFFRACTION' 
1.320 1.330 50 . 4313 . 0.241 0.241 . 206 . . 4519 . 'X-RAY DIFFRACTION' 
1.330 1.340 50 . 4416 . 0.240 0.255 . 208 . . 4624 . 'X-RAY DIFFRACTION' 
1.340 1.350 50 . 4380 . 0.225 0.243 . 238 . . 4618 . 'X-RAY DIFFRACTION' 
1.350 1.360 50 . 4429 . 0.234 0.255 . 217 . . 4646 . 'X-RAY DIFFRACTION' 
1.360 1.370 50 . 4432 . 0.223 0.252 . 222 . . 4654 . 'X-RAY DIFFRACTION' 
1.370 1.380 50 . 4470 . 0.220 0.232 . 232 . . 4702 . 'X-RAY DIFFRACTION' 
1.380 1.390 50 . 4471 . 0.207 0.269 . 229 . . 4700 . 'X-RAY DIFFRACTION' 
1.390 1.400 50 . 4455 . 0.205 0.214 . 218 . . 4673 . 'X-RAY DIFFRACTION' 
1.400 1.410 50 . 4510 . 0.201 0.212 . 240 . . 4750 . 'X-RAY DIFFRACTION' 
1.410 1.420 50 . 4573 . 0.198 0.212 . 229 . . 4802 . 'X-RAY DIFFRACTION' 
1.420 1.440 50 . 4560 . 0.192 0.212 . 239 . . 4799 . 'X-RAY DIFFRACTION' 
1.440 1.450 50 . 4518 . 0.188 0.188 . 231 . . 4749 . 'X-RAY DIFFRACTION' 
1.450 1.460 50 . 4585 . 0.190 0.229 . 238 . . 4823 . 'X-RAY DIFFRACTION' 
1.460 1.480 50 . 4553 . 0.177 0.206 . 263 . . 4816 . 'X-RAY DIFFRACTION' 
1.480 1.490 50 . 4651 . 0.175 0.204 . 238 . . 4889 . 'X-RAY DIFFRACTION' 
1.490 1.510 50 . 4608 . 0.172 0.207 . 226 . . 4834 . 'X-RAY DIFFRACTION' 
1.510 1.520 50 . 4648 . 0.174 0.204 . 234 . . 4882 . 'X-RAY DIFFRACTION' 
1.520 1.540 50 . 4651 . 0.170 0.204 . 256 . . 4907 . 'X-RAY DIFFRACTION' 
1.540 1.560 50 . 4660 . 0.167 0.201 . 239 . . 4899 . 'X-RAY DIFFRACTION' 
1.560 1.580 50 . 4680 . 0.162 0.196 . 242 . . 4922 . 'X-RAY DIFFRACTION' 
1.580 1.600 50 . 4700 . 0.157 0.192 . 259 . . 4959 . 'X-RAY DIFFRACTION' 
1.600 1.620 50 . 4758 . 0.154 0.186 . 138 . . 4896 . 'X-RAY DIFFRACTION' 
1.620 1.640 50 . 4854 . 0.153 0.169 . 144 . . 4998 . 'X-RAY DIFFRACTION' 
1.640 1.660 50 . 4736 . 0.154 0.189 . 162 . . 4898 . 'X-RAY DIFFRACTION' 
1.660 1.680 50 . 4769 . 0.151 0.177 . 213 . . 4982 . 'X-RAY DIFFRACTION' 
1.680 1.710 50 . 4774 . 0.154 0.189 . 188 . . 4962 . 'X-RAY DIFFRACTION' 
1.710 1.740 50 . 4731 . 0.146 0.160 . 209 . . 4940 . 'X-RAY DIFFRACTION' 
1.740 1.760 50 . 4797 . 0.144 0.165 . 214 . . 5011 . 'X-RAY DIFFRACTION' 
1.760 1.790 50 . 4768 . 0.146 0.174 . 223 . . 4991 . 'X-RAY DIFFRACTION' 
1.790 1.830 50 . 4783 . 0.147 0.171 . 254 . . 5037 . 'X-RAY DIFFRACTION' 
1.830 1.860 50 . 4771 . 0.150 0.181 . 253 . . 5024 . 'X-RAY DIFFRACTION' 
1.860 1.900 50 . 4801 . 0.148 0.170 . 256 . . 5057 . 'X-RAY DIFFRACTION' 
1.900 1.940 50 . 4759 . 0.148 0.166 . 249 . . 5008 . 'X-RAY DIFFRACTION' 
1.940 1.990 50 . 4835 . 0.154 0.165 . 253 . . 5088 . 'X-RAY DIFFRACTION' 
1.990 2.040 50 . 4829 . 0.153 0.167 . 261 . . 5090 . 'X-RAY DIFFRACTION' 
2.040 2.090 50 . 4884 . 0.156 0.196 . 237 . . 5121 . 'X-RAY DIFFRACTION' 
2.090 2.150 50 . 4871 . 0.152 0.167 . 276 . . 5147 . 'X-RAY DIFFRACTION' 
2.150 2.220 50 . 4888 . 0.157 0.176 . 241 . . 5129 . 'X-RAY DIFFRACTION' 
2.220 2.300 50 . 4863 . 0.149 0.177 . 263 . . 5126 . 'X-RAY DIFFRACTION' 
2.300 2.390 50 . 4879 . 0.150 0.189 . 267 . . 5146 . 'X-RAY DIFFRACTION' 
2.390 2.500 50 . 4867 . 0.151 0.164 . 287 . . 5154 . 'X-RAY DIFFRACTION' 
2.500 2.640 50 . 4919 . 0.155 0.180 . 257 . . 5176 . 'X-RAY DIFFRACTION' 
2.640 2.800 50 . 4915 . 0.159 0.176 . 256 . . 5171 . 'X-RAY DIFFRACTION' 
2.800 3.020 50 . 4972 . 0.160 0.187 . 242 . . 5214 . 'X-RAY DIFFRACTION' 
3.020 3.320 50 . 4969 . 0.154 0.164 . 263 . . 5232 . 'X-RAY DIFFRACTION' 
3.320 3.800 50 . 4966 . 0.142 0.156 . 289 . . 5255 . 'X-RAY DIFFRACTION' 
3.800 4.780 50 . 5004 . 0.139 0.143 . 307 . . 5311 . '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 ion.param          ion.top          'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  3BLB 
_struct.title                     
'Crystal structure of Golgi Mannosidase II in complex with swainsonine at 1.3 Angstrom resolution' 
_struct.pdbx_descriptor           'Alpha-mannosidase 2 (E.C.3.2.1.114)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3BLB 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            
'Golgi mannosidase, Glycosidase, Golgi apparatus, Hydrolase, Membrane, Signal-anchor, Transmembrane' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
# 
_struct_biol.id        1 
_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 ? ? ? ? ? ? ? 2.056 ? 
disulf2 disulf ? ? A CYS 275  SG  ? ? ? 1_555 A CYS 282  SG  ? ? A CYS 275  A CYS 282  1_555 ? ? ? ? ? ? ? 2.049 ? 
disulf3 disulf ? ? A CYS 283  SG  ? ? ? 1_555 A CYS 297  SG  ? ? A CYS 283  A CYS 297  1_555 ? ? ? ? ? ? ? 2.087 ? 
disulf4 disulf ? ? A CYS 902  SG  ? ? ? 1_555 A CYS 987  SG  ? ? A CYS 902  A CYS 987  1_555 ? ? ? ? ? ? ? 2.061 ? 
disulf5 disulf ? ? A CYS 1000 SG  ? ? ? 1_555 A CYS 1009 SG  ? ? A CYS 1000 A CYS 1009 1_555 ? ? ? ? ? ? ? 2.040 ? 
metalc1 metalc ? ? A HIS 90   NE2 ? ? ? 1_555 C ZN  .    ZN  ? ? A HIS 90   A ZN  1047 1_555 ? ? ? ? ? ? ? 2.099 ? 
metalc2 metalc ? ? A ASP 92   OD1 ? ? ? 1_555 C ZN  .    ZN  ? ? A ASP 92   A ZN  1047 1_555 ? ? ? ? ? ? ? 2.240 ? 
covale1 covale ? ? A ASN 194  ND2 ? ? ? 1_555 B NAG .    C1  ? ? A ASN 194  A NAG 1046 1_555 ? ? ? ? ? ? ? 1.444 ? 
metalc3 metalc ? ? A ASP 204  OD2 ? ? ? 1_555 C ZN  .    ZN  ? ? A ASP 204  A ZN  1047 1_555 ? ? ? ? ? ? ? 2.167 ? 
metalc4 metalc ? ? A HIS 471  NE2 ? ? ? 1_555 C ZN  .    ZN  ? ? A HIS 471  A ZN  1047 1_555 ? ? ? ? ? ? ? 2.087 ? 
metalc5 metalc ? ? C ZN  .    ZN  ? ? ? 1_555 D SWA .    O11 ? ? A ZN  1047 A SWA 1048 1_555 ? ? ? ? ? ? ? 2.202 ? 
metalc6 metalc ? ? C ZN  .    ZN  ? ? ? 1_555 D SWA .    O13 ? ? A ZN  1047 A SWA 1048 1_555 ? ? ? ? ? ? ? 2.131 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
covale ? ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 PHE 405 A . ? PHE 405 A THR 406 A ? THR 406 A 1 -2.70 
2 TRP 531 A . ? TRP 531 A PRO 532 A ? PRO 532 A 1 -0.98 
# 
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  HIS A 705  ? TYR A 715  ? HIS A 705  TYR A 715  
I 5  SER A 736  ? PRO A 737  ? SER A 736  PRO A 737  
J 1  ILE A 676  ? ARG A 679  ? ILE A 676  ARG A 679  
J 2  THR A 685  ? PHE A 688  ? THR A 685  PHE A 688  
J 3  LEU A 694  ? GLN A 698  ? LEU A 694  GLN A 698  
J 4  HIS A 705  ? TYR A 715  ? HIS A 705  TYR A 715  
J 5  THR A 788  ? THR A 796  ? THR A 788  THR A 796  
J 6  GLU A 861  ? ARG A 869  ? GLU A 861  ARG A 869  
J 7  LEU A 852  ? SER A 855  ? LEU A 852  SER A 855  
J 8  TYR A 829  ? ILE A 831  ? TYR A 829  ILE A 831  
K 1  LEU A 957  ? ARG A 964  ? LEU A 957  ARG A 964  
K 2  GLN A 973  ? ARG A 981  ? GLN A 973  ARG A 981  
K 3  THR A 1036 ? HIS A 1043 ? THR A 1036 HIS A 1043 
K 4  VAL A 1006 ? THR A 1012 ? VAL A 1006 THR A 1012 
K 5  ASN A 1019 ? HIS A 1022 ? ASN A 1019 HIS A 1022 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1  2  N VAL A 43   ? N VAL A 43   O SER A 401  ? O SER A 401  
A 2  3  O LEU A 400  ? O LEU A 400  N LEU A 246  ? N LEU A 246  
A 3  4  N PHE A 245  ? N PHE A 245  O THR A 261  ? O THR A 261  
A 4  5  O HIS A 262  ? O HIS A 262  N MET A 224  ? N MET A 224  
A 5  6  O LEU A 225  ? O LEU A 225  N ALA A 202  ? N ALA A 202  
B 1  2  O LEU A 334  ? O LEU A 334  N LYS A 82   ? N LYS A 82   
B 2  3  N VAL A 85   ? N VAL A 85   O GLN A 375  ? O GLN A 375  
C 1  2  N PHE A 126  ? N PHE A 126  O GLU A 159  ? O GLU A 159  
D 1  2  N ARG A 410  ? N ARG A 410  O ASN A 413  ? O ASN A 413  
E 1  2  N THR A 525  ? N THR A 525  O ILE A 933  ? O ILE A 933  
E 2  3  O PHE A 932  ? O PHE A 932  N VAL A 556  ? N VAL A 556  
E 3  4  N VAL A 555  ? N VAL A 555  O TYR A 632  ? O TYR A 632  
E 4  5  O VAL A 633  ? O VAL A 633  N THR A 581  ? N THR A 581  
E 5  6  N VAL A 580  ? N VAL A 580  O VAL A 588  ? O VAL A 588  
F 1  2  N THR A 525  ? N THR A 525  O ILE A 933  ? O ILE A 933  
F 2  3  O PHE A 932  ? O PHE A 932  N VAL A 556  ? N VAL A 556  
F 3  4  N VAL A 555  ? N VAL A 555  O TYR A 632  ? O TYR A 632  
F 4  5  N LEU A 629  ? N LEU A 629  O PHE A 946  ? O PHE A 946  
G 1  2  N ILE A 543  ? N ILE A 543  O TYR A 572  ? O TYR A 572  
G 2  3  N PHE A 571  ? N PHE A 571  O ILE A 618  ? O ILE A 618  
G 3  4  O GLN A 610  ? O GLN A 610  N SER A 597  ? N SER A 597  
G 4  5  N VAL A 592  ? N VAL A 592  O SER A 645  ? O SER A 645  
H 1  2  O LYS A 669  ? O LYS A 669  N LEU A 651  ? N LEU A 651  
H 2  3  N LEU A 652  ? N LEU A 652  O VAL A 745  ? O VAL A 745  
H 3  4  N LEU A 746  ? N LEU A 746  O SER A 757  ? O SER A 757  
H 4  5  N SER A 754  ? N SER A 754  O MET A 769  ? O MET A 769  
H 5  6  N ILE A 768  ? N ILE A 768  O GLU A 775  ? O GLU A 775  
H 6  7  N VAL A 780  ? N VAL A 780  O VAL A 888  ? O VAL A 888  
H 7  8  O VAL A 895  ? O VAL A 895  N THR A 845  ? N THR A 845  
H 8  9  O LEU A 846  ? O LEU A 846  N MET A 835  ? N MET A 835  
H 9  10 O PHE A 836  ? O PHE A 836  N TYR A 805  ? N TYR A 805  
H 10 11 N PHE A 804  ? N PHE A 804  O ARG A 816  ? O ARG A 816  
H 11 12 N PHE A 813  ? N PHE A 813  O GLY A 912  ? O GLY A 912  
I 1  2  N ILE A 676  ? N ILE A 676  O PHE A 688  ? O PHE A 688  
I 2  3  N ALA A 687  ? N ALA A 687  O LYS A 695  ? O LYS A 695  
I 3  4  N ILE A 697  ? N ILE A 697  O VAL A 706  ? O VAL A 706  
I 4  5  N LYS A 714  ? N LYS A 714  O SER A 736  ? O SER A 736  
J 1  2  N ILE A 676  ? N ILE A 676  O PHE A 688  ? O PHE A 688  
J 2  3  N ALA A 687  ? N ALA A 687  O LYS A 695  ? O LYS A 695  
J 3  4  N ILE A 697  ? N ILE A 697  O VAL A 706  ? O VAL A 706  
J 4  5  N LYS A 711  ? N LYS A 711  O ARG A 793  ? O ARG A 793  
J 5  6  N ILE A 790  ? N ILE A 790  O GLN A 866  ? O GLN A 866  
J 6  7  O 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 ? ? ? ? 2  'BINDING SITE FOR RESIDUE NAG A 1046' 
AC2 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE ZN A 1047'  
AC3 Software ? ? ? ? 12 'BINDING SITE FOR RESIDUE SWA A 1048' 
AC4 Software ? ? ? ? 8  'BINDING SITE FOR RESIDUE MRD A 1049' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 2  LYS A 154 ? LYS A 154  . ? 1_555 ? 
2  AC1 2  ASN A 194 ? ASN A 194  . ? 1_555 ? 
3  AC2 5  HIS A 90  ? HIS A 90   . ? 1_555 ? 
4  AC2 5  ASP A 92  ? ASP A 92   . ? 1_555 ? 
5  AC2 5  ASP A 204 ? ASP A 204  . ? 1_555 ? 
6  AC2 5  HIS A 471 ? HIS A 471  . ? 1_555 ? 
7  AC2 5  SWA D .   ? SWA A 1048 . ? 1_555 ? 
8  AC3 12 HIS A 90  ? HIS A 90   . ? 1_555 ? 
9  AC3 12 ASP A 92  ? ASP A 92   . ? 1_555 ? 
10 AC3 12 TRP A 95  ? TRP A 95   . ? 1_555 ? 
11 AC3 12 ASP A 204 ? ASP A 204  . ? 1_555 ? 
12 AC3 12 PHE A 206 ? PHE A 206  . ? 1_555 ? 
13 AC3 12 ARG A 228 ? ARG A 228  . ? 1_555 ? 
14 AC3 12 TYR A 269 ? TYR A 269  . ? 1_555 ? 
15 AC3 12 ASP A 341 ? ASP A 341  . ? 1_555 ? 
16 AC3 12 HIS A 471 ? HIS A 471  . ? 1_555 ? 
17 AC3 12 ASP A 472 ? ASP A 472  . ? 1_555 ? 
18 AC3 12 TYR A 727 ? TYR A 727  . ? 1_555 ? 
19 AC3 12 ZN  C .   ? ZN  A 1047 . ? 1_555 ? 
20 AC4 8  LYS A 63  ? LYS A 63   . ? 1_555 ? 
21 AC4 8  GLN A 64  ? GLN A 64   . ? 1_555 ? 
22 AC4 8  TYR A 267 ? TYR A 267  . ? 1_555 ? 
23 AC4 8  HIS A 273 ? HIS A 273  . ? 1_555 ? 
24 AC4 8  HOH F .   ? HOH A 1339 . ? 1_555 ? 
25 AC4 8  HOH F .   ? HOH A 1813 . ? 1_555 ? 
26 AC4 8  HOH F .   ? HOH A 1927 . ? 1_555 ? 
27 AC4 8  HOH F .   ? HOH A 1929 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          3BLB 
_database_PDB_matrix.origx[1][1]       1.00000 
_database_PDB_matrix.origx[1][2]       0.00000 
_database_PDB_matrix.origx[1][3]       0.00000 
_database_PDB_matrix.origx[2][1]       0.00000 
_database_PDB_matrix.origx[2][2]       1.00000 
_database_PDB_matrix.origx[2][3]       0.00000 
_database_PDB_matrix.origx[3][1]       0.00000 
_database_PDB_matrix.origx[3][2]       0.00000 
_database_PDB_matrix.origx[3][3]       1.00000 
_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                    3BLB 
_atom_sites.fract_transf_matrix[1][1]   0.01454 
_atom_sites.fract_transf_matrix[1][2]   0.00000 
_atom_sites.fract_transf_matrix[1][3]   0.00000 
_atom_sites.fract_transf_matrix[2][1]   0.00000 
_atom_sites.fract_transf_matrix[2][2]   0.00912 
_atom_sites.fract_transf_matrix[2][3]   0.00000 
_atom_sites.fract_transf_matrix[3][1]   0.00000 
_atom_sites.fract_transf_matrix[3][2]   0.00000 
_atom_sites.fract_transf_matrix[3][3]   0.00720 
_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  
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   ? 44.035 36.106  -19.271 1.00 23.84 ? 31   CYS A N   1 
ATOM   2    C  CA  . CYS A 1 31   ? 43.339 37.313  -18.707 1.00 19.60 ? 31   CYS A CA  1 
ATOM   3    C  C   . CYS A 1 31   ? 41.847 37.087  -18.751 1.00 19.29 ? 31   CYS A C   1 
ATOM   4    O  O   . CYS A 1 31   ? 41.357 36.492  -19.726 1.00 20.53 ? 31   CYS A O   1 
ATOM   5    C  CB  . CYS A 1 31   ? 43.609 38.513  -19.569 1.00 18.32 ? 31   CYS A CB  1 
ATOM   6    S  SG  . CYS A 1 31   ? 45.319 39.131  -19.580 1.00 22.12 ? 31   CYS A SG  1 
ATOM   7    N  N   . GLN A 1 32   ? 41.131 37.539  -17.731 1.00 18.01 ? 32   GLN A N   1 
ATOM   8    C  CA  . GLN A 1 32   ? 39.662 37.495  -17.729 1.00 17.62 ? 32   GLN A CA  1 
ATOM   9    C  C   . GLN A 1 32   ? 39.137 38.451  -18.815 1.00 14.90 ? 32   GLN A C   1 
ATOM   10   O  O   . GLN A 1 32   ? 39.718 39.530  -19.067 1.00 15.61 ? 32   GLN A O   1 
ATOM   11   C  CB  . GLN A 1 32   ? 39.042 38.068  -16.439 1.00 20.07 ? 32   GLN A CB  1 
ATOM   12   C  CG  . GLN A 1 32   ? 39.209 37.273  -15.217 1.00 26.02 ? 32   GLN A CG  1 
ATOM   13   C  CD  . GLN A 1 32   ? 38.149 37.665  -14.198 1.00 29.14 ? 32   GLN A CD  1 
ATOM   14   O  OE1 . GLN A 1 32   ? 37.024 37.161  -14.232 1.00 29.63 ? 32   GLN A OE1 1 
ATOM   15   N  NE2 . GLN A 1 32   ? 38.495 38.589  -13.300 1.00 28.68 ? 32   GLN A NE2 1 
ATOM   16   N  N   . ASP A 1 33   ? 38.036 38.064  -19.455 1.00 18.70 ? 33   ASP A N   1 
ATOM   17   C  CA  . ASP A 1 33   ? 37.390 38.905  -20.476 1.00 13.20 ? 33   ASP A CA  1 
ATOM   18   C  C   . ASP A 1 33   ? 36.465 39.837  -19.673 1.00 16.86 ? 33   ASP A C   1 
ATOM   19   O  O   . ASP A 1 33   ? 35.558 39.401  -18.982 1.00 20.65 ? 33   ASP A O   1 
ATOM   20   C  CB  . ASP A 1 33   ? 36.609 37.992  -21.443 1.00 16.26 ? 33   ASP A CB  1 
ATOM   21   C  CG  . ASP A 1 33   ? 35.894 38.711  -22.559 1.00 20.36 ? 33   ASP A CG  1 
ATOM   22   O  OD1 . ASP A 1 33   ? 35.418 39.844  -22.420 1.00 17.42 ? 33   ASP A OD1 1 
ATOM   23   O  OD2 . ASP A 1 33   ? 35.727 38.045  -23.602 1.00 22.54 ? 33   ASP A OD2 1 
ATOM   24   N  N   . VAL A 1 34   ? 36.695 41.132  -19.796 1.00 10.33 ? 34   VAL A N   1 
ATOM   25   C  CA  . VAL A 1 34   ? 35.936 42.127  -19.034 1.00 10.21 ? 34   VAL A CA  1 
ATOM   26   C  C   . VAL A 1 34   ? 34.727 42.704  -19.775 1.00 8.86  ? 34   VAL A C   1 
ATOM   27   O  O   . VAL A 1 34   ? 34.005 43.603  -19.285 1.00 9.48  ? 34   VAL A O   1 
ATOM   28   C  CB  . VAL A 1 34   ? 36.873 43.295  -18.577 1.00 9.28  ? 34   VAL A CB  1 
ATOM   29   C  CG1 . VAL A 1 34   ? 38.106 42.750  -17.839 1.00 11.21 ? 34   VAL A CG1 1 
ATOM   30   C  CG2 . VAL A 1 34   ? 37.333 44.151  -19.774 1.00 10.89 ? 34   VAL A CG2 1 
ATOM   31   N  N   . VAL A 1 35   ? 34.477 42.175  -20.980 1.00 9.45  ? 35   VAL A N   1 
ATOM   32   C  CA  . VAL A 1 35   ? 33.385 42.654  -21.823 1.00 9.19  ? 35   VAL A CA  1 
ATOM   33   C  C   . VAL A 1 35   ? 32.195 41.727  -22.010 1.00 8.17  ? 35   VAL A C   1 
ATOM   34   O  O   . VAL A 1 35   ? 31.068 42.145  -21.955 1.00 9.57  ? 35   VAL A O   1 
ATOM   35   C  CB  . VAL A 1 35   ? 33.935 42.969  -23.231 1.00 10.51 ? 35   VAL A CB  1 
ATOM   36   C  CG1 . VAL A 1 35   ? 32.803 43.431  -24.185 1.00 10.95 ? 35   VAL A CG1 1 
ATOM   37   C  CG2 . VAL A 1 35   ? 35.008 44.091  -23.112 1.00 11.29 ? 35   VAL A CG2 1 
ATOM   38   N  N   . GLN A 1 36   ? 32.520 40.463  -22.262 1.00 10.82 ? 36   GLN A N   1 
ATOM   39   C  CA  . GLN A 1 36   ? 31.516 39.490  -22.742 1.00 13.02 ? 36   GLN A CA  1 
ATOM   40   C  C   . GLN A 1 36   ? 30.866 38.564  -21.780 1.00 17.77 ? 36   GLN A C   1 
ATOM   41   O  O   . GLN A 1 36   ? 29.983 37.833  -22.190 1.00 23.03 ? 36   GLN A O   1 
ATOM   42   C  CB  . GLN A 1 36   ? 32.209 38.653  -23.798 1.00 11.63 ? 36   GLN A CB  1 
ATOM   43   C  CG  . GLN A 1 36   ? 32.849 39.525  -24.893 1.00 14.31 ? 36   GLN A CG  1 
ATOM   44   C  CD  . GLN A 1 36   ? 33.364 38.679  -26.035 1.00 12.82 ? 36   GLN A CD  1 
ATOM   45   O  OE1 . GLN A 1 36   ? 32.675 38.552  -27.063 1.00 17.20 ? 36   GLN A OE1 1 
ATOM   46   N  NE2 . GLN A 1 36   ? 34.544 38.111  -25.876 1.00 14.28 ? 36   GLN A NE2 1 
ATOM   47   N  N   . ASP A 1 37   ? 31.314 38.531  -20.539 1.00 16.17 ? 37   ASP A N   1 
ATOM   48   C  CA  . ASP A 1 37   ? 30.787 37.641  -19.519 1.00 19.08 ? 37   ASP A CA  1 
ATOM   49   C  C   . ASP A 1 37   ? 30.152 38.490  -18.403 1.00 17.65 ? 37   ASP A C   1 
ATOM   50   O  O   . ASP A 1 37   ? 30.879 39.144  -17.666 1.00 22.57 ? 37   ASP A O   1 
ATOM   51   C  CB  . ASP A 1 37   ? 31.937 36.814  -18.891 1.00 21.83 ? 37   ASP A CB  1 
ATOM   52   C  CG  . ASP A 1 37   ? 32.594 35.827  -19.879 1.00 26.24 ? 37   ASP A CG  1 
ATOM   53   O  OD1 . ASP A 1 37   ? 31.846 35.241  -20.676 1.00 28.80 ? 37   ASP A OD1 1 
ATOM   54   O  OD2 . ASP A 1 37   ? 33.841 35.664  -19.835 1.00 26.88 ? 37   ASP A OD2 1 
ATOM   55   N  N   . VAL A 1 38   ? 28.843 38.479  -18.276 1.00 14.90 ? 38   VAL A N   1 
ATOM   56   C  CA  . VAL A 1 38   ? 28.174 39.230  -17.204 1.00 13.68 ? 38   VAL A CA  1 
ATOM   57   C  C   . VAL A 1 38   ? 28.359 38.502  -15.859 1.00 15.13 ? 38   VAL A C   1 
ATOM   58   O  O   . VAL A 1 38   ? 27.894 37.358  -15.689 1.00 16.33 ? 38   VAL A O   1 
ATOM   59   C  CB  . VAL A 1 38   ? 26.668 39.373  -17.511 1.00 15.43 ? 38   VAL A CB  1 
ATOM   60   C  CG1 . VAL A 1 38   ? 25.924 40.117  -16.350 1.00 15.17 ? 38   VAL A CG1 1 
ATOM   61   C  CG2 . VAL A 1 38   ? 26.510 40.071  -18.921 1.00 15.00 ? 38   VAL A CG2 1 
ATOM   62   N  N   . PRO A 1 39   ? 28.994 39.134  -14.863 1.00 13.05 ? 39   PRO A N   1 
ATOM   63   C  CA  . PRO A 1 39   ? 29.182 38.440  -13.583 1.00 13.72 ? 39   PRO A CA  1 
ATOM   64   C  C   . PRO A 1 39   ? 27.898 38.086  -12.921 1.00 12.83 ? 39   PRO A C   1 
ATOM   65   O  O   . PRO A 1 39   ? 26.922 38.809  -12.963 1.00 12.97 ? 39   PRO A O   1 
ATOM   66   C  CB  . PRO A 1 39   ? 29.935 39.459  -12.722 1.00 13.41 ? 39   PRO A CB  1 
ATOM   67   C  CG  . PRO A 1 39   ? 30.711 40.297  -13.788 1.00 11.66 ? 39   PRO A CG  1 
ATOM   68   C  CD  . PRO A 1 39   ? 29.692 40.449  -14.898 1.00 12.94 ? 39   PRO A CD  1 
ATOM   69   N  N   . ASN A 1 40   ? 27.901 36.888  -12.293 1.00 12.85 ? 40   ASN A N   1 
ATOM   70   C  CA  . ASN A 1 40   ? 26.727 36.491  -11.535 1.00 15.29 ? 40   ASN A CA  1 
ATOM   71   C  C   . ASN A 1 40   ? 26.950 36.868  -10.049 1.00 13.75 ? 40   ASN A C   1 
ATOM   72   O  O   . ASN A 1 40   ? 27.837 36.310  -9.385  1.00 16.37 ? 40   ASN A O   1 
ATOM   73   C  CB  . ASN A 1 40   ? 26.501 34.984  -11.708 1.00 18.37 ? 40   ASN A CB  1 
ATOM   74   C  CG  . ASN A 1 40   ? 25.454 34.447  -10.784 1.00 26.42 ? 40   ASN A CG  1 
ATOM   75   O  OD1 . ASN A 1 40   ? 24.414 35.075  -10.544 1.00 29.68 ? 40   ASN A OD1 1 
ATOM   76   N  ND2 . ASN A 1 40   ? 25.707 33.248  -10.259 1.00 34.21 ? 40   ASN A ND2 1 
ATOM   77   N  N   . VAL A 1 41   ? 26.215 37.851  -9.557  1.00 11.38 ? 41   VAL A N   1 
ATOM   78   C  CA  . VAL A 1 41   ? 26.414 38.329  -8.189  1.00 10.39 ? 41   VAL A CA  1 
ATOM   79   C  C   . VAL A 1 41   ? 25.071 38.352  -7.482  1.00 11.59 ? 41   VAL A C   1 
ATOM   80   O  O   . VAL A 1 41   ? 24.047 38.499  -8.129  1.00 13.27 ? 41   VAL A O   1 
ATOM   81   C  CB  . VAL A 1 41   ? 27.055 39.754  -8.151  1.00 10.99 ? 41   VAL A CB  1 
ATOM   82   C  CG1 . VAL A 1 41   ? 28.491 39.701  -8.609  1.00 11.43 ? 41   VAL A CG1 1 
ATOM   83   C  CG2 . VAL A 1 41   ? 26.242 40.742  -8.988  1.00 11.85 ? 41   VAL A CG2 1 
ATOM   84   N  N   . ASP A 1 42   ? 25.062 38.215  -6.159  1.00 10.12 ? 42   ASP A N   1 
ATOM   85   C  CA  . ASP A 1 42   ? 23.808 38.255  -5.457  1.00 10.58 ? 42   ASP A CA  1 
ATOM   86   C  C   . ASP A 1 42   ? 23.125 39.591  -5.477  1.00 10.47 ? 42   ASP A C   1 
ATOM   87   O  O   . ASP A 1 42   ? 21.892 39.706  -5.483  1.00 12.16 ? 42   ASP A O   1 
ATOM   88   C  CB  . ASP A 1 42   ? 24.011 37.838  -3.981  1.00 12.00 ? 42   ASP A CB  1 
ATOM   89   C  CG  . ASP A 1 42   ? 24.552 36.438  -3.875  1.00 15.64 ? 42   ASP A CG  1 
ATOM   90   O  OD1 . ASP A 1 42   ? 23.884 35.480  -4.431  1.00 17.76 ? 42   ASP A OD1 1 
ATOM   91   O  OD2 . ASP A 1 42   ? 25.597 36.177  -3.284  1.00 13.67 ? 42   ASP A OD2 1 
ATOM   92   N  N   . VAL A 1 43   ? 23.925 40.674  -5.403  1.00 8.73  ? 43   VAL A N   1 
ATOM   93   C  CA  . VAL A 1 43   ? 23.394 42.026  -5.427  1.00 10.88 ? 43   VAL A CA  1 
ATOM   94   C  C   . VAL A 1 43   ? 24.176 42.827  -6.480  1.00 8.65  ? 43   VAL A C   1 
ATOM   95   O  O   . VAL A 1 43   ? 25.392 42.909  -6.423  1.00 9.57  ? 43   VAL A O   1 
ATOM   96   C  CB  . VAL A 1 43   ? 23.569 42.751  -4.090  1.00 9.13  ? 43   VAL A CB  1 
ATOM   97   C  CG1 . VAL A 1 43   ? 22.990 44.180  -4.171  1.00 10.43 ? 43   VAL A CG1 1 
ATOM   98   C  CG2 . VAL A 1 43   ? 22.844 41.970  -2.930  1.00 13.02 ? 43   VAL A CG2 1 
ATOM   99   N  N   . GLN A 1 44   ? 23.470 43.318  -7.489  1.00 8.25  ? 44   GLN A N   1 
ATOM   100  C  CA  . GLN A 1 44   ? 24.056 44.174  -8.542  1.00 8.81  ? 44   GLN A CA  1 
ATOM   101  C  C   . GLN A 1 44   ? 23.345 45.499  -8.377  1.00 7.80  ? 44   GLN A C   1 
ATOM   102  O  O   . GLN A 1 44   ? 22.130 45.569  -8.555  1.00 8.44  ? 44   GLN A O   1 
ATOM   103  C  CB  . GLN A 1 44   ? 23.876 43.540  -9.930  1.00 9.19  ? 44   GLN A CB  1 
ATOM   104  C  CG  . GLN A 1 44   ? 24.984 43.949  -10.894 1.00 7.94  ? 44   GLN A CG  1 
ATOM   105  C  CD  . GLN A 1 44   ? 25.047 45.492  -11.035 1.00 7.57  ? 44   GLN A CD  1 
ATOM   106  O  OE1 . GLN A 1 44   ? 24.034 46.093  -11.379 1.00 8.82  ? 44   GLN A OE1 1 
ATOM   107  N  NE2 . GLN A 1 44   ? 26.216 46.103  -10.712 1.00 7.36  ? 44   GLN A NE2 1 
ATOM   108  N  N   . MET A 1 45   ? 24.057 46.581  -8.012  1.00 7.26  ? 45   MET A N   1 
ATOM   109  C  CA  . MET A 1 45   ? 23.364 47.806  -7.634  1.00 7.49  ? 45   MET A CA  1 
ATOM   110  C  C   . MET A 1 45   ? 22.465 48.463  -8.667  1.00 6.90  ? 45   MET A C   1 
ATOM   111  O  O   . MET A 1 45   ? 21.472 49.074  -8.300  1.00 7.97  ? 45   MET A O   1 
ATOM   112  C  CB  . MET A 1 45   ? 24.355 48.829  -7.056  1.00 7.74  ? 45   MET A CB  1 
ATOM   113  C  CG  . MET A 1 45   ? 24.973 48.334  -5.719  1.00 8.30  ? 45   MET A CG  1 
ATOM   114  S  SD  . MET A 1 45   ? 23.773 48.059  -4.420  1.00 10.83 ? 45   MET A SD  1 
ATOM   115  C  CE  . MET A 1 45   ? 23.109 49.739  -4.283  1.00 12.64 ? 45   MET A CE  1 
ATOM   116  N  N   . LEU A 1 46   ? 22.832 48.353  -9.932  1.00 7.52  ? 46   LEU A N   1 
ATOM   117  C  CA  . LEU A 1 46   ? 21.952 48.936  -10.976 1.00 8.08  ? 46   LEU A CA  1 
ATOM   118  C  C   . LEU A 1 46   ? 20.617 48.159  -11.035 1.00 9.02  ? 46   LEU A C   1 
ATOM   119  O  O   . LEU A 1 46   ? 19.554 48.753  -11.154 1.00 9.55  ? 46   LEU A O   1 
ATOM   120  C  CB  . LEU A 1 46   ? 22.659 48.927  -12.325 1.00 9.59  ? 46   LEU A CB  1 
ATOM   121  C  CG  . LEU A 1 46   ? 21.863 49.658  -13.437 1.00 9.88  ? 46   LEU A CG  1 
ATOM   122  C  CD1 . LEU A 1 46   ? 21.908 51.201  -13.222 1.00 10.18 ? 46   LEU A CD1 1 
ATOM   123  C  CD2 . LEU A 1 46   ? 22.459 49.312  -14.773 1.00 12.32 ? 46   LEU A CD2 1 
ATOM   124  N  N   . GLU A 1 47   ? 20.707 46.833  -10.885 1.00 9.33  ? 47   GLU A N   1 
ATOM   125  C  CA  . GLU A 1 47   ? 19.503 45.984  -10.929 1.00 10.99 ? 47   GLU A CA  1 
ATOM   126  C  C   . GLU A 1 47   ? 18.695 46.269  -9.688  1.00 11.00 ? 47   GLU A C   1 
ATOM   127  O  O   . GLU A 1 47   ? 17.456 46.427  -9.718  1.00 11.92 ? 47   GLU A O   1 
ATOM   128  C  CB  . GLU A 1 47   ? 19.920 44.516  -11.017 1.00 11.93 ? 47   GLU A CB  1 
ATOM   129  C  CG  . GLU A 1 47   ? 18.703 43.565  -11.254 1.00 17.55 ? 47   GLU A CG  1 
ATOM   130  C  CD  . GLU A 1 47   ? 17.907 43.210  -10.000 1.00 27.38 ? 47   GLU A CD  1 
ATOM   131  O  OE1 . GLU A 1 47   ? 18.404 43.352  -8.853  1.00 23.15 ? 47   GLU A OE1 1 
ATOM   132  O  OE2 . GLU A 1 47   ? 16.739 42.753  -10.153 1.00 29.75 ? 47   GLU A OE2 1 
ATOM   133  N  N   . LEU A 1 48   ? 19.353 46.399  -8.531  1.00 9.73  ? 48   LEU A N   1 
ATOM   134  C  CA  . LEU A 1 48   ? 18.642 46.722  -7.302  1.00 9.06  ? 48   LEU A CA  1 
ATOM   135  C  C   . LEU A 1 48   ? 17.898 48.046  -7.416  1.00 9.04  ? 48   LEU A C   1 
ATOM   136  O  O   . LEU A 1 48   ? 16.718 48.168  -7.049  1.00 11.32 ? 48   LEU A O   1 
ATOM   137  C  CB  . LEU A 1 48   ? 19.632 46.744  -6.112  1.00 10.66 ? 48   LEU A CB  1 
ATOM   138  C  CG  . LEU A 1 48   ? 18.934 46.962  -4.771  1.00 12.68 ? 48   LEU A CG  1 
ATOM   139  C  CD1 . LEU A 1 48   ? 17.934 45.804  -4.508  1.00 18.75 ? 48   LEU A CD1 1 
ATOM   140  C  CD2 . LEU A 1 48   ? 19.958 47.099  -3.656  1.00 18.00 ? 48   LEU A CD2 1 
ATOM   141  N  N   . TYR A 1 49   ? 18.580 49.044  -7.960  1.00 9.59  ? 49   TYR A N   1 
ATOM   142  C  CA  . TYR A 1 49   ? 17.999 50.364  -8.168  1.00 9.05  ? 49   TYR A CA  1 
ATOM   143  C  C   . TYR A 1 49   ? 16.739 50.303  -9.032  1.00 9.46  ? 49   TYR A C   1 
ATOM   144  O  O   . TYR A 1 49   ? 15.790 51.004  -8.787  1.00 11.12 ? 49   TYR A O   1 
ATOM   145  C  CB  . TYR A 1 49   ? 19.048 51.342  -8.745  1.00 9.50  ? 49   TYR A CB  1 
ATOM   146  C  CG  . TYR A 1 49   ? 19.577 52.283  -7.694  1.00 7.98  ? 49   TYR A CG  1 
ATOM   147  C  CD1 . TYR A 1 49   ? 20.029 51.803  -6.472  1.00 8.75  ? 49   TYR A CD1 1 
ATOM   148  C  CD2 . TYR A 1 49   ? 19.600 53.647  -7.904  1.00 9.85  ? 49   TYR A CD2 1 
ATOM   149  C  CE1 . TYR A 1 49   ? 20.467 52.648  -5.499  1.00 8.37  ? 49   TYR A CE1 1 
ATOM   150  C  CE2 . TYR A 1 49   ? 20.050 54.508  -6.910  1.00 9.62  ? 49   TYR A CE2 1 
ATOM   151  C  CZ  . TYR A 1 49   ? 20.473 53.999  -5.713  1.00 7.99  ? 49   TYR A CZ  1 
ATOM   152  O  OH  . TYR A 1 49   ? 20.907 54.849  -4.738  1.00 9.76  ? 49   TYR A OH  1 
ATOM   153  N  N   . ASP A 1 50   ? 16.757 49.462  -10.044 1.00 10.61 ? 50   ASP A N   1 
ATOM   154  C  CA  . ASP A 1 50   ? 15.621 49.351  -10.984 1.00 13.49 ? 50   ASP A CA  1 
ATOM   155  C  C   . ASP A 1 50   ? 14.401 48.771  -10.274 1.00 14.39 ? 50   ASP A C   1 
ATOM   156  O  O   . ASP A 1 50   ? 13.269 49.189  -10.610 1.00 14.34 ? 50   ASP A O   1 
ATOM   157  C  CB  . ASP A 1 50   ? 16.050 48.504  -12.180 1.00 14.56 ? 50   ASP A CB  1 
ATOM   158  C  CG  . ASP A 1 50   ? 15.244 48.760  -13.447 1.00 20.90 ? 50   ASP A CG  1 
ATOM   159  O  OD1 . ASP A 1 50   ? 14.567 49.784  -13.540 1.00 24.56 ? 50   ASP A OD1 1 
ATOM   160  O  OD2 . ASP A 1 50   ? 15.365 47.896  -14.355 1.00 28.50 ? 50   ASP A OD2 1 
ATOM   161  N  N   . ARG A 1 51   ? 14.608 47.881  -9.304  1.00 13.40 ? 51   ARG A N   1 
ATOM   162  C  CA  . ARG A 1 51   ? 13.505 47.209  -8.560  1.00 15.84 ? 51   ARG A CA  1 
ATOM   163  C  C   . ARG A 1 51   ? 13.037 47.949  -7.311  1.00 16.18 ? 51   ARG A C   1 
ATOM   164  O  O   . ARG A 1 51   ? 11.856 47.870  -6.950  1.00 19.22 ? 51   ARG A O   1 
ATOM   165  C  CB  . ARG A 1 51   ? 13.936 45.798  -8.081  1.00 22.23 ? 51   ARG A CB  1 
ATOM   166  C  CG  . ARG A 1 51   ? 14.593 44.938  -9.085  1.00 30.27 ? 51   ARG A CG  1 
ATOM   167  C  CD  . ARG A 1 51   ? 14.926 43.551  -8.496  1.00 33.66 ? 51   ARG A CD  1 
ATOM   168  N  NE  . ARG A 1 51   ? 14.770 43.508  -7.048  1.00 38.12 ? 51   ARG A NE  1 
ATOM   169  C  CZ  . ARG A 1 51   ? 15.753 43.260  -6.189  1.00 36.78 ? 51   ARG A CZ  1 
ATOM   170  N  NH1 . ARG A 1 51   ? 16.986 43.022  -6.626  1.00 37.83 ? 51   ARG A NH1 1 
ATOM   171  N  NH2 . ARG A 1 51   ? 15.493 43.264  -4.884  1.00 39.74 ? 51   ARG A NH2 1 
ATOM   172  N  N   . MET A 1 52   ? 13.906 48.674  -6.621  1.00 14.12 ? 52   MET A N   1 
ATOM   173  C  CA  . MET A 1 52   ? 13.528 49.381  -5.389  1.00 16.90 ? 52   MET A CA  1 
ATOM   174  C  C   . MET A 1 52   ? 12.532 50.491  -5.549  1.00 13.40 ? 52   MET A C   1 
ATOM   175  O  O   . MET A 1 52   ? 12.560 51.207  -6.545  1.00 15.92 ? 52   MET A O   1 
ATOM   176  C  CB  . MET A 1 52   ? 14.773 50.055  -4.726  1.00 17.19 ? 52   MET A CB  1 
ATOM   177  C  CG  . MET A 1 52   ? 15.718 49.070  -4.114  1.00 16.72 ? 52   MET A CG  1 
ATOM   178  S  SD  . MET A 1 52   ? 17.313 49.981  -3.672  1.00 18.66 ? 52   MET A SD  1 
ATOM   179  C  CE  . MET A 1 52   ? 16.729 51.269  -2.550  1.00 17.55 ? 52   MET A CE  1 
ATOM   180  N  N   . SER A 1 53   ? 11.677 50.712  -4.539  1.00 15.22 ? 53   SER A N   1 
ATOM   181  C  CA  . SER A 1 53   ? 10.687 51.801  -4.633  1.00 18.34 ? 53   SER A CA  1 
ATOM   182  C  C   . SER A 1 53   ? 11.100 53.143  -4.007  1.00 15.08 ? 53   SER A C   1 
ATOM   183  O  O   . SER A 1 53   ? 10.494 54.189  -4.253  1.00 17.71 ? 53   SER A O   1 
ATOM   184  C  CB  . SER A 1 53   ? 9.368  51.327  -4.011  1.00 18.90 ? 53   SER A CB  1 
ATOM   185  O  OG  A SER A 1 53   ? 8.824  50.292  -4.805  0.50 27.66 ? 53   SER A OG  1 
ATOM   186  O  OG  B SER A 1 53   ? 9.422  51.332  -2.645  0.50 31.08 ? 53   SER A OG  1 
ATOM   187  N  N   . PHE A 1 54   ? 12.102 53.104  -3.153  1.00 12.93 ? 54   PHE A N   1 
ATOM   188  C  CA  . PHE A 1 54   ? 12.612 54.300  -2.511  1.00 12.03 ? 54   PHE A CA  1 
ATOM   189  C  C   . PHE A 1 54   ? 11.597 55.078  -1.710  1.00 13.43 ? 54   PHE A C   1 
ATOM   190  O  O   . PHE A 1 54   ? 11.692 56.304  -1.556  1.00 14.87 ? 54   PHE A O   1 
ATOM   191  C  CB  . PHE A 1 54   ? 13.279 55.238  -3.570  1.00 12.64 ? 54   PHE A CB  1 
ATOM   192  C  CG  . PHE A 1 54   ? 14.530 54.656  -4.222  1.00 10.32 ? 54   PHE A CG  1 
ATOM   193  C  CD1 . PHE A 1 54   ? 14.450 53.855  -5.340  1.00 10.92 ? 54   PHE A CD1 1 
ATOM   194  C  CD2 . PHE A 1 54   ? 15.792 54.973  -3.707  1.00 10.26 ? 54   PHE A CD2 1 
ATOM   195  C  CE1 . PHE A 1 54   ? 15.619 53.359  -5.963  1.00 10.87 ? 54   PHE A CE1 1 
ATOM   196  C  CE2 . PHE A 1 54   ? 16.935 54.501  -4.320  1.00 11.34 ? 54   PHE A CE2 1 
ATOM   197  C  CZ  . PHE A 1 54   ? 16.857 53.698  -5.447  1.00 10.62 ? 54   PHE A CZ  1 
ATOM   198  N  N   . LYS A 1 55   ? 10.571 54.408  -1.175  1.00 13.50 ? 55   LYS A N   1 
ATOM   199  C  CA  . LYS A 1 55   ? 9.590  55.201  -0.395  1.00 13.42 ? 55   LYS A CA  1 
ATOM   200  C  C   . LYS A 1 55   ? 10.151 55.628  0.925   1.00 14.13 ? 55   LYS A C   1 
ATOM   201  O  O   . LYS A 1 55   ? 10.755 54.826  1.627   1.00 17.24 ? 55   LYS A O   1 
ATOM   202  C  CB  . LYS A 1 55   ? 8.324  54.356  -0.110  1.00 13.98 ? 55   LYS A CB  1 
ATOM   203  C  CG  . LYS A 1 55   ? 7.680  53.857  -1.327  1.00 15.46 ? 55   LYS A CG  1 
ATOM   204  C  CD  . LYS A 1 55   ? 7.384  54.970  -2.345  1.00 14.34 ? 55   LYS A CD  1 
ATOM   205  C  CE  . LYS A 1 55   ? 6.572  54.414  -3.526  1.00 20.24 ? 55   LYS A CE  1 
ATOM   206  N  NZ  . LYS A 1 55   ? 6.262  55.493  -4.517  1.00 19.83 ? 55   LYS A NZ  1 
ATOM   207  N  N   . ASP A 1 56   ? 9.951  56.876  1.278   1.00 13.40 ? 56   ASP A N   1 
ATOM   208  C  CA  . ASP A 1 56   ? 10.440 57.442  2.504   1.00 13.55 ? 56   ASP A CA  1 
ATOM   209  C  C   . ASP A 1 56   ? 9.368  57.352  3.622   1.00 14.91 ? 56   ASP A C   1 
ATOM   210  O  O   . ASP A 1 56   ? 8.751  58.353  4.007   1.00 18.12 ? 56   ASP A O   1 
ATOM   211  C  CB  . ASP A 1 56   ? 10.862 58.882  2.219   1.00 14.09 ? 56   ASP A CB  1 
ATOM   212  C  CG  . ASP A 1 56   ? 11.536 59.534  3.406   1.00 14.32 ? 56   ASP A CG  1 
ATOM   213  O  OD1 . ASP A 1 56   ? 12.047 58.830  4.307   1.00 14.38 ? 56   ASP A OD1 1 
ATOM   214  O  OD2 . ASP A 1 56   ? 11.552 60.781  3.470   1.00 16.19 ? 56   ASP A OD2 1 
ATOM   215  N  N   . ILE A 1 57   ? 9.158  56.153  4.136   1.00 16.24 ? 57   ILE A N   1 
ATOM   216  C  CA  . ILE A 1 57   ? 8.143  55.989  5.159   1.00 17.22 ? 57   ILE A CA  1 
ATOM   217  C  C   . ILE A 1 57   ? 8.732  56.080  6.554   1.00 15.98 ? 57   ILE A C   1 
ATOM   218  O  O   . ILE A 1 57   ? 9.877  55.721  6.777   1.00 16.49 ? 57   ILE A O   1 
ATOM   219  C  CB  . ILE A 1 57   ? 7.294  54.708  4.976   1.00 26.26 ? 57   ILE A CB  1 
ATOM   220  C  CG1 . ILE A 1 57   ? 7.894  53.522  5.706   1.00 24.57 ? 57   ILE A CG1 1 
ATOM   221  C  CG2 . ILE A 1 57   ? 7.043  54.402  3.512   1.00 30.57 ? 57   ILE A CG2 1 
ATOM   222  C  CD1 . ILE A 1 57   ? 7.053  52.274  5.604   1.00 30.02 ? 57   ILE A CD1 1 
ATOM   223  N  N   . ASP A 1 58   ? 7.929  56.564  7.489   1.00 17.11 ? 58   ASP A N   1 
ATOM   224  C  CA  . ASP A 1 58   ? 8.323  56.679  8.879   1.00 15.79 ? 58   ASP A CA  1 
ATOM   225  C  C   . ASP A 1 58   ? 8.355  55.278  9.481   1.00 17.14 ? 58   ASP A C   1 
ATOM   226  O  O   . ASP A 1 58   ? 7.314  54.634  9.657   1.00 17.64 ? 58   ASP A O   1 
ATOM   227  C  CB  . ASP A 1 58   ? 7.312  57.533  9.617   1.00 19.71 ? 58   ASP A CB  1 
ATOM   228  C  CG  . ASP A 1 58   ? 7.714  57.837  11.051  1.00 23.37 ? 58   ASP A CG  1 
ATOM   229  O  OD1 . ASP A 1 58   ? 8.565  57.151  11.644  1.00 20.11 ? 58   ASP A OD1 1 
ATOM   230  O  OD2 . ASP A 1 58   ? 7.152  58.806  11.626  1.00 30.10 ? 58   ASP A OD2 1 
ATOM   231  N  N   . GLY A 1 59   ? 9.554  54.798  9.782   1.00 14.52 ? 59   GLY A N   1 
ATOM   232  C  CA  . GLY A 1 59   ? 9.705  53.465  10.338  1.00 14.59 ? 59   GLY A CA  1 
ATOM   233  C  C   . GLY A 1 59   ? 9.588  53.378  11.845  1.00 11.77 ? 59   GLY A C   1 
ATOM   234  O  O   . GLY A 1 59   ? 9.764  52.279  12.331  1.00 15.59 ? 59   GLY A O   1 
ATOM   235  N  N   . GLY A 1 60   ? 9.324  54.490  12.524  1.00 13.27 ? 60   GLY A N   1 
ATOM   236  C  CA  . GLY A 1 60   ? 9.258  54.441  13.973  1.00 15.38 ? 60   GLY A CA  1 
ATOM   237  C  C   . GLY A 1 60   ? 10.551 55.018  14.542  1.00 13.08 ? 60   GLY A C   1 
ATOM   238  O  O   . GLY A 1 60   ? 11.078 55.990  13.995  1.00 14.63 ? 60   GLY A O   1 
ATOM   239  N  N   . VAL A 1 61   ? 11.035 54.503  15.670  1.00 12.27 ? 61   VAL A N   1 
ATOM   240  C  CA  . VAL A 1 61   ? 12.254 55.059  16.284  1.00 11.47 ? 61   VAL A CA  1 
ATOM   241  C  C   . VAL A 1 61   ? 13.440 54.911  15.292  1.00 10.37 ? 61   VAL A C   1 
ATOM   242  O  O   . VAL A 1 61   ? 14.271 55.838  15.235  1.00 11.45 ? 61   VAL A O   1 
ATOM   243  C  CB  . VAL A 1 61   ? 12.588 54.453  17.645  1.00 11.36 ? 61   VAL A CB  1 
ATOM   244  C  CG1 . VAL A 1 61   ? 11.501 54.868  18.660  1.00 15.34 ? 61   VAL A CG1 1 
ATOM   245  C  CG2 . VAL A 1 61   ? 12.701 52.921  17.579  1.00 13.30 ? 61   VAL A CG2 1 
ATOM   246  N  N   . TRP A 1 62   ? 13.495 53.826  14.556  1.00 9.89  ? 62   TRP A N   1 
ATOM   247  C  CA  . TRP A 1 62   ? 14.404 53.763  13.438  1.00 9.22  ? 62   TRP A CA  1 
ATOM   248  C  C   . TRP A 1 62   ? 13.688 54.429  12.274  1.00 10.14 ? 62   TRP A C   1 
ATOM   249  O  O   . TRP A 1 62   ? 12.929 53.787  11.562  1.00 10.70 ? 62   TRP A O   1 
ATOM   250  C  CB  . TRP A 1 62   ? 14.841 52.316  13.146  1.00 9.27  ? 62   TRP A CB  1 
ATOM   251  C  CG  . TRP A 1 62   ? 15.831 52.204  11.995  1.00 8.55  ? 62   TRP A CG  1 
ATOM   252  C  CD1 . TRP A 1 62   ? 16.520 53.224  11.402  1.00 8.61  ? 62   TRP A CD1 1 
ATOM   253  C  CD2 . TRP A 1 62   ? 16.193 51.017  11.292  1.00 9.46  ? 62   TRP A CD2 1 
ATOM   254  N  NE1 . TRP A 1 62   ? 17.268 52.743  10.377  1.00 8.64  ? 62   TRP A NE1 1 
ATOM   255  C  CE2 . TRP A 1 62   ? 17.094 51.392  10.284  1.00 9.78  ? 62   TRP A CE2 1 
ATOM   256  C  CE3 . TRP A 1 62   ? 15.840 49.679  11.408  1.00 8.90  ? 62   TRP A CE3 1 
ATOM   257  C  CZ2 . TRP A 1 62   ? 17.645 50.479  9.406   1.00 9.33  ? 62   TRP A CZ2 1 
ATOM   258  C  CZ3 . TRP A 1 62   ? 16.368 48.780  10.539  1.00 9.68  ? 62   TRP A CZ3 1 
ATOM   259  C  CH2 . TRP A 1 62   ? 17.267 49.179  9.540   1.00 10.37 ? 62   TRP A CH2 1 
ATOM   260  N  N   . LYS A 1 63   ? 13.897 55.737  12.119  1.00 10.51 ? 63   LYS A N   1 
ATOM   261  C  CA  . LYS A 1 63   ? 13.037 56.497  11.191  1.00 10.23 ? 63   LYS A CA  1 
ATOM   262  C  C   . LYS A 1 63   ? 13.037 56.016  9.792   1.00 11.06 ? 63   LYS A C   1 
ATOM   263  O  O   . LYS A 1 63   ? 11.992 56.102  9.088   1.00 12.48 ? 63   LYS A O   1 
ATOM   264  C  CB  . LYS A 1 63   ? 13.411 57.977  11.254  1.00 11.69 ? 63   LYS A CB  1 
ATOM   265  C  CG  . LYS A 1 63   ? 13.008 58.706  12.545  1.00 16.75 ? 63   LYS A CG  1 
ATOM   266  C  CD  . LYS A 1 63   ? 11.643 59.294  12.329  1.00 22.67 ? 63   LYS A CD  1 
ATOM   267  C  CE  . LYS A 1 63   ? 10.954 59.571  13.619  1.00 31.06 ? 63   LYS A CE  1 
ATOM   268  N  NZ  . LYS A 1 63   ? 9.780  58.685  13.541  1.00 26.29 ? 63   LYS A NZ  1 
ATOM   269  N  N   . GLN A 1 64   ? 14.170 55.477  9.324   1.00 10.32 ? 64   GLN A N   1 
ATOM   270  C  CA  . GLN A 1 64   ? 14.262 55.014  7.949   1.00 10.16 ? 64   GLN A CA  1 
ATOM   271  C  C   . GLN A 1 64   ? 14.322 53.514  7.779   1.00 8.78  ? 64   GLN A C   1 
ATOM   272  O  O   . GLN A 1 64   ? 14.622 52.977  6.717   1.00 9.81  ? 64   GLN A O   1 
ATOM   273  C  CB  . GLN A 1 64   ? 15.494 55.670  7.281   1.00 9.30  ? 64   GLN A CB  1 
ATOM   274  C  CG  . GLN A 1 64   ? 15.342 57.148  7.293   1.00 10.52 ? 64   GLN A CG  1 
ATOM   275  C  CD  . GLN A 1 64   ? 16.694 57.848  7.144   1.00 9.66  ? 64   GLN A CD  1 
ATOM   276  O  OE1 . GLN A 1 64   ? 17.672 57.535  7.882   1.00 10.40 ? 64   GLN A OE1 1 
ATOM   277  N  NE2 . GLN A 1 64   ? 16.743 58.845  6.218   1.00 10.19 ? 64   GLN A NE2 1 
ATOM   278  N  N   . GLY A 1 65   ? 13.919 52.813  8.868   1.00 10.91 ? 65   GLY A N   1 
ATOM   279  C  CA  . GLY A 1 65   ? 13.885 51.355  8.875   1.00 10.44 ? 65   GLY A CA  1 
ATOM   280  C  C   . GLY A 1 65   ? 12.513 50.814  9.306   1.00 11.89 ? 65   GLY A C   1 
ATOM   281  O  O   . GLY A 1 65   ? 11.487 51.172  8.692   1.00 12.99 ? 65   GLY A O   1 
ATOM   282  N  N   . TRP A 1 66   ? 12.520 49.936  10.298  1.00 12.14 ? 66   TRP A N   1 
ATOM   283  C  CA  . TRP A 1 66   ? 11.277 49.302  10.814  1.00 12.45 ? 66   TRP A CA  1 
ATOM   284  C  C   . TRP A 1 66   ? 11.585 48.919  12.258  1.00 11.21 ? 66   TRP A C   1 
ATOM   285  O  O   . TRP A 1 66   ? 12.702 49.054  12.752  1.00 11.84 ? 66   TRP A O   1 
ATOM   286  C  CB  . TRP A 1 66   ? 10.881 48.071  9.972   1.00 12.11 ? 66   TRP A CB  1 
ATOM   287  C  CG  . TRP A 1 66   ? 11.816 46.946  10.117  1.00 12.55 ? 66   TRP A CG  1 
ATOM   288  C  CD1 . TRP A 1 66   ? 11.705 45.892  11.005  1.00 11.81 ? 66   TRP A CD1 1 
ATOM   289  C  CD2 . TRP A 1 66   ? 13.041 46.713  9.403   1.00 12.62 ? 66   TRP A CD2 1 
ATOM   290  N  NE1 . TRP A 1 66   ? 12.748 45.041  10.884  1.00 12.68 ? 66   TRP A NE1 1 
ATOM   291  C  CE2 . TRP A 1 66   ? 13.598 45.508  9.905   1.00 11.73 ? 66   TRP A CE2 1 
ATOM   292  C  CE3 . TRP A 1 66   ? 13.734 47.405  8.366   1.00 11.75 ? 66   TRP A CE3 1 
ATOM   293  C  CZ2 . TRP A 1 66   ? 14.791 44.970  9.430   1.00 13.45 ? 66   TRP A CZ2 1 
ATOM   294  C  CZ3 . TRP A 1 66   ? 14.928 46.859  7.888   1.00 13.48 ? 66   TRP A CZ3 1 
ATOM   295  C  CH2 . TRP A 1 66   ? 15.455 45.652  8.421   1.00 12.49 ? 66   TRP A CH2 1 
ATOM   296  N  N   . ASN A 1 67   ? 10.540 48.488  12.998  1.00 11.87 ? 67   ASN A N   1 
ATOM   297  C  CA  . ASN A 1 67   ? 10.698 48.069  14.403  1.00 11.16 ? 67   ASN A CA  1 
ATOM   298  C  C   . ASN A 1 67   ? 11.293 46.665  14.410  1.00 11.95 ? 67   ASN A C   1 
ATOM   299  O  O   . ASN A 1 67   ? 10.618 45.636  14.118  1.00 13.28 ? 67   ASN A O   1 
ATOM   300  C  CB  . ASN A 1 67   ? 9.309  48.008  15.083  1.00 13.30 ? 67   ASN A CB  1 
ATOM   301  C  CG  . ASN A 1 67   ? 8.757  49.362  15.397  1.00 18.37 ? 67   ASN A CG  1 
ATOM   302  O  OD1 . ASN A 1 67   ? 9.466  50.378  15.444  1.00 19.31 ? 67   ASN A OD1 1 
ATOM   303  N  ND2 . ASN A 1 67   ? 7.448  49.406  15.687  1.00 21.83 ? 67   ASN A ND2 1 
ATOM   304  N  N   . ILE A 1 68   ? 12.584 46.570  14.709  1.00 11.43 ? 68   ILE A N   1 
ATOM   305  C  CA  . ILE A 1 68   ? 13.241 45.285  14.649  1.00 11.72 ? 68   ILE A CA  1 
ATOM   306  C  C   . ILE A 1 68   ? 12.801 44.352  15.788  1.00 11.25 ? 68   ILE A C   1 
ATOM   307  O  O   . ILE A 1 68   ? 12.729 44.788  16.916  1.00 12.95 ? 68   ILE A O   1 
ATOM   308  C  CB  . ILE A 1 68   ? 14.811 45.466  14.761  1.00 12.15 ? 68   ILE A CB  1 
ATOM   309  C  CG1 . ILE A 1 68   ? 15.302 46.357  13.578  1.00 12.95 ? 68   ILE A CG1 1 
ATOM   310  C  CG2 . ILE A 1 68   ? 15.524 44.120  14.763  1.00 12.38 ? 68   ILE A CG2 1 
ATOM   311  C  CD1 . ILE A 1 68   ? 16.745 46.837  13.785  1.00 11.05 ? 68   ILE A CD1 1 
ATOM   312  N  N   . LYS A 1 69   ? 12.578 43.099  15.443  1.00 12.56 ? 69   LYS A N   1 
ATOM   313  C  CA  . LYS A 1 69   ? 12.199 42.091  16.453  1.00 14.13 ? 69   LYS A CA  1 
ATOM   314  C  C   . LYS A 1 69   ? 13.259 41.015  16.470  1.00 13.58 ? 69   LYS A C   1 
ATOM   315  O  O   . LYS A 1 69   ? 13.884 40.715  15.460  1.00 15.25 ? 69   LYS A O   1 
ATOM   316  C  CB  . LYS A 1 69   ? 10.809 41.488  16.049  1.00 16.21 ? 69   LYS A CB  1 
ATOM   317  C  CG  . LYS A 1 69   ? 9.659  42.539  16.184  1.00 21.62 ? 69   LYS A CG  1 
ATOM   318  C  CD  . LYS A 1 69   ? 9.327  42.820  17.647  1.00 30.87 ? 69   LYS A CD  1 
ATOM   319  C  CE  . LYS A 1 69   ? 8.263  41.835  18.296  1.00 37.46 ? 69   LYS A CE  1 
ATOM   320  N  NZ  . LYS A 1 69   ? 8.647  40.472  18.912  1.00 33.59 ? 69   LYS A NZ  1 
ATOM   321  N  N   . TYR A 1 70   ? 13.488 40.410  17.655  1.00 13.72 ? 70   TYR A N   1 
ATOM   322  C  CA  . TYR A 1 70   ? 14.445 39.314  17.735  1.00 14.02 ? 70   TYR A CA  1 
ATOM   323  C  C   . TYR A 1 70   ? 13.868 38.262  18.714  1.00 15.40 ? 70   TYR A C   1 
ATOM   324  O  O   . TYR A 1 70   ? 12.998 38.566  19.535  1.00 17.18 ? 70   TYR A O   1 
ATOM   325  C  CB  . TYR A 1 70   ? 15.854 39.813  18.218  1.00 13.50 ? 70   TYR A CB  1 
ATOM   326  C  CG  . TYR A 1 70   ? 15.870 40.454  19.585  1.00 11.25 ? 70   TYR A CG  1 
ATOM   327  C  CD1 . TYR A 1 70   ? 16.043 39.673  20.771  1.00 13.75 ? 70   TYR A CD1 1 
ATOM   328  C  CD2 . TYR A 1 70   ? 15.709 41.821  19.744  1.00 14.37 ? 70   TYR A CD2 1 
ATOM   329  C  CE1 . TYR A 1 70   ? 16.050 40.290  22.009  1.00 13.84 ? 70   TYR A CE1 1 
ATOM   330  C  CE2 . TYR A 1 70   ? 15.722 42.423  20.972  1.00 14.09 ? 70   TYR A CE2 1 
ATOM   331  C  CZ  . TYR A 1 70   ? 15.884 41.656  22.124  1.00 12.75 ? 70   TYR A CZ  1 
ATOM   332  O  OH  . TYR A 1 70   ? 15.869 42.285  23.336  1.00 15.77 ? 70   TYR A OH  1 
ATOM   333  N  N   . ASP A 1 71   ? 14.353 37.053  18.568  1.00 18.36 ? 71   ASP A N   1 
ATOM   334  C  CA  . ASP A 1 71   ? 13.949 35.948  19.428  1.00 19.01 ? 71   ASP A CA  1 
ATOM   335  C  C   . ASP A 1 71   ? 14.966 35.892  20.562  1.00 21.65 ? 71   ASP A C   1 
ATOM   336  O  O   . ASP A 1 71   ? 16.148 35.625  20.326  1.00 20.52 ? 71   ASP A O   1 
ATOM   337  C  CB  . ASP A 1 71   ? 14.002 34.689  18.602  1.00 21.45 ? 71   ASP A CB  1 
ATOM   338  C  CG  . ASP A 1 71   ? 13.655 33.444  19.415  1.00 25.28 ? 71   ASP A CG  1 
ATOM   339  O  OD1 . ASP A 1 71   ? 13.404 33.570  20.634  1.00 28.19 ? 71   ASP A OD1 1 
ATOM   340  O  OD2 . ASP A 1 71   ? 13.655 32.375  18.796  1.00 31.36 ? 71   ASP A OD2 1 
ATOM   341  N  N   . PRO A 1 72   ? 14.537 36.149  21.819  1.00 22.15 ? 72   PRO A N   1 
ATOM   342  C  CA  . PRO A 1 72   ? 15.501 36.107  22.924  1.00 24.33 ? 72   PRO A CA  1 
ATOM   343  C  C   . PRO A 1 72   ? 16.246 34.787  23.077  1.00 23.41 ? 72   PRO A C   1 
ATOM   344  O  O   . PRO A 1 72   ? 17.344 34.751  23.637  1.00 25.39 ? 72   PRO A O   1 
ATOM   345  C  CB  . PRO A 1 72   ? 14.656 36.479  24.154  1.00 27.00 ? 72   PRO A CB  1 
ATOM   346  C  CG  . PRO A 1 72   ? 13.277 36.084  23.759  1.00 29.60 ? 72   PRO A CG  1 
ATOM   347  C  CD  . PRO A 1 72   ? 13.196 36.492  22.309  1.00 25.61 ? 72   PRO A CD  1 
ATOM   348  N  N   . LEU A 1 73   ? 15.679 33.714  22.545  1.00 21.50 ? 73   LEU A N   1 
ATOM   349  C  CA  . LEU A 1 73   ? 16.321 32.407  22.626  1.00 24.93 ? 73   LEU A CA  1 
ATOM   350  C  C   . LEU A 1 73   ? 17.425 32.159  21.584  1.00 21.08 ? 73   LEU A C   1 
ATOM   351  O  O   . LEU A 1 73   ? 18.054 31.115  21.572  1.00 23.23 ? 73   LEU A O   1 
ATOM   352  C  CB  . LEU A 1 73   ? 15.245 31.315  22.505  1.00 22.05 ? 73   LEU A CB  1 
ATOM   353  C  CG  . LEU A 1 73   ? 14.168 31.389  23.595  1.00 28.56 ? 73   LEU A CG  1 
ATOM   354  C  CD1 . LEU A 1 73   ? 13.092 30.308  23.341  1.00 27.15 ? 73   LEU A CD1 1 
ATOM   355  C  CD2 . LEU A 1 73   ? 14.837 31.184  24.974  1.00 28.32 ? 73   LEU A CD2 1 
ATOM   356  N  N   . LYS A 1 74   ? 17.663 33.129  20.680  1.00 19.83 ? 74   LYS A N   1 
ATOM   357  C  CA  . LYS A 1 74   ? 18.690 32.919  19.679  1.00 18.39 ? 74   LYS A CA  1 
ATOM   358  C  C   . LYS A 1 74   ? 20.095 32.768  20.286  1.00 16.43 ? 74   LYS A C   1 
ATOM   359  O  O   . LYS A 1 74   ? 20.932 32.027  19.796  1.00 19.93 ? 74   LYS A O   1 
ATOM   360  C  CB  . LYS A 1 74   ? 18.684 34.087  18.678  1.00 18.85 ? 74   LYS A CB  1 
ATOM   361  C  CG  . LYS A 1 74   ? 19.773 33.999  17.618  1.00 20.41 ? 74   LYS A CG  1 
ATOM   362  C  CD  . LYS A 1 74   ? 19.558 35.119  16.564  1.00 20.90 ? 74   LYS A CD  1 
ATOM   363  C  CE  . LYS A 1 74   ? 20.576 34.942  15.437  1.00 23.29 ? 74   LYS A CE  1 
ATOM   364  N  NZ  . LYS A 1 74   ? 20.279 35.913  14.325  1.00 25.99 ? 74   LYS A NZ  1 
ATOM   365  N  N   . TYR A 1 75   ? 20.339 33.498  21.360  1.00 18.72 ? 75   TYR A N   1 
ATOM   366  C  CA  . TYR A 1 75   ? 21.628 33.460  22.035  1.00 17.55 ? 75   TYR A CA  1 
ATOM   367  C  C   . TYR A 1 75   ? 21.423 32.698  23.348  1.00 18.85 ? 75   TYR A C   1 
ATOM   368  O  O   . TYR A 1 75   ? 20.418 32.885  24.001  1.00 22.67 ? 75   TYR A O   1 
ATOM   369  C  CB  . TYR A 1 75   ? 22.192 34.899  22.198  1.00 18.30 ? 75   TYR A CB  1 
ATOM   370  C  CG  . TYR A 1 75   ? 22.528 35.505  20.843  1.00 16.97 ? 75   TYR A CG  1 
ATOM   371  C  CD1 . TYR A 1 75   ? 23.565 34.999  20.100  1.00 18.27 ? 75   TYR A CD1 1 
ATOM   372  C  CD2 . TYR A 1 75   ? 21.768 36.529  20.287  1.00 21.38 ? 75   TYR A CD2 1 
ATOM   373  C  CE1 . TYR A 1 75   ? 23.871 35.486  18.851  1.00 21.83 ? 75   TYR A CE1 1 
ATOM   374  C  CE2 . TYR A 1 75   ? 22.060 37.035  19.030  1.00 17.73 ? 75   TYR A CE2 1 
ATOM   375  C  CZ  . TYR A 1 75   ? 23.109 36.497  18.319  1.00 20.10 ? 75   TYR A CZ  1 
ATOM   376  O  OH  . TYR A 1 75   ? 23.436 36.970  17.057  1.00 21.74 ? 75   TYR A OH  1 
ATOM   377  N  N   . ASN A 1 76   ? 22.354 31.799  23.664  1.00 17.78 ? 76   ASN A N   1 
ATOM   378  C  CA  . ASN A 1 76   ? 22.235 30.930  24.850  1.00 20.61 ? 76   ASN A CA  1 
ATOM   379  C  C   . ASN A 1 76   ? 23.645 30.621  25.321  1.00 22.01 ? 76   ASN A C   1 
ATOM   380  O  O   . ASN A 1 76   ? 24.630 31.110  24.775  1.00 21.22 ? 76   ASN A O   1 
ATOM   381  C  CB  . ASN A 1 76   ? 21.493 29.626  24.489  1.00 24.77 ? 76   ASN A CB  1 
ATOM   382  C  CG  . ASN A 1 76   ? 22.122 28.904  23.335  1.00 22.27 ? 76   ASN A CG  1 
ATOM   383  O  OD1 . ASN A 1 76   ? 23.318 28.676  23.309  1.00 24.84 ? 76   ASN A OD1 1 
ATOM   384  N  ND2 . ASN A 1 76   ? 21.311 28.558  22.338  1.00 31.96 ? 76   ASN A ND2 1 
ATOM   385  N  N   . ALA A 1 77   ? 23.764 29.795  26.360  1.00 24.90 ? 77   ALA A N   1 
ATOM   386  C  CA  . ALA A 1 77   ? 25.094 29.509  26.892  1.00 26.21 ? 77   ALA A CA  1 
ATOM   387  C  C   . ALA A 1 77   ? 26.104 29.016  25.885  1.00 27.33 ? 77   ALA A C   1 
ATOM   388  O  O   . ALA A 1 77   ? 27.290 29.296  26.008  1.00 29.95 ? 77   ALA A O   1 
ATOM   389  C  CB  . ALA A 1 77   ? 24.986 28.490  28.036  1.00 31.75 ? 77   ALA A CB  1 
ATOM   390  N  N   . HIS A 1 78   ? 25.642 28.300  24.872  1.00 28.45 ? 78   HIS A N   1 
ATOM   391  C  CA  . HIS A 1 78   ? 26.591 27.778  23.902  1.00 30.55 ? 78   HIS A CA  1 
ATOM   392  C  C   . HIS A 1 78   ? 26.681 28.578  22.619  1.00 29.80 ? 78   HIS A C   1 
ATOM   393  O  O   . HIS A 1 78   ? 27.307 28.148  21.651  1.00 28.42 ? 78   HIS A O   1 
ATOM   394  C  CB  . HIS A 1 78   ? 26.262 26.308  23.617  1.00 33.69 ? 78   HIS A CB  1 
ATOM   395  C  CG  . HIS A 1 78   ? 26.334 25.456  24.847  1.00 39.84 ? 78   HIS A CG  1 
ATOM   396  N  ND1 . HIS A 1 78   ? 27.505 25.285  25.561  1.00 41.40 ? 78   HIS A ND1 1 
ATOM   397  C  CD2 . HIS A 1 78   ? 25.369 24.803  25.542  1.00 40.38 ? 78   HIS A CD2 1 
ATOM   398  C  CE1 . HIS A 1 78   ? 27.259 24.565  26.642  1.00 39.80 ? 78   HIS A CE1 1 
ATOM   399  N  NE2 . HIS A 1 78   ? 25.971 24.261  26.656  1.00 42.87 ? 78   HIS A NE2 1 
ATOM   400  N  N   . HIS A 1 79   ? 26.032 29.725  22.602  1.00 25.21 ? 79   HIS A N   1 
ATOM   401  C  CA  . HIS A 1 79   ? 26.091 30.570  21.425  1.00 20.01 ? 79   HIS A CA  1 
ATOM   402  C  C   . HIS A 1 79   ? 25.855 31.999  21.879  1.00 14.58 ? 79   HIS A C   1 
ATOM   403  O  O   . HIS A 1 79   ? 24.743 32.449  21.893  1.00 18.19 ? 79   HIS A O   1 
ATOM   404  C  CB  . HIS A 1 79   ? 25.038 30.108  20.410  1.00 21.09 ? 79   HIS A CB  1 
ATOM   405  C  CG  . HIS A 1 79   ? 24.967 30.936  19.156  1.00 22.14 ? 79   HIS A CG  1 
ATOM   406  N  ND1 . HIS A 1 79   ? 25.849 30.792  18.109  1.00 26.72 ? 79   HIS A ND1 1 
ATOM   407  C  CD2 . HIS A 1 79   ? 24.102 31.906  18.783  1.00 23.64 ? 79   HIS A CD2 1 
ATOM   408  C  CE1 . HIS A 1 79   ? 25.540 31.648  17.151  1.00 21.61 ? 79   HIS A CE1 1 
ATOM   409  N  NE2 . HIS A 1 79   ? 24.486 32.338  17.538  1.00 22.01 ? 79   HIS A NE2 1 
ATOM   410  N  N   . LYS A 1 80   ? 26.909 32.672  22.319  1.00 15.59 ? 80   LYS A N   1 
ATOM   411  C  CA  . LYS A 1 80   ? 26.724 34.014  22.870  1.00 14.51 ? 80   LYS A CA  1 
ATOM   412  C  C   . LYS A 1 80   ? 26.900 35.070  21.781  1.00 15.08 ? 80   LYS A C   1 
ATOM   413  O  O   . LYS A 1 80   ? 27.461 34.791  20.740  1.00 15.97 ? 80   LYS A O   1 
ATOM   414  C  CB  . LYS A 1 80   ? 27.756 34.292  23.938  1.00 13.62 ? 80   LYS A CB  1 
ATOM   415  C  CG  . LYS A 1 80   ? 27.670 33.250  25.074  1.00 16.42 ? 80   LYS A CG  1 
ATOM   416  C  CD  . LYS A 1 80   ? 28.872 33.324  25.940  1.00 25.10 ? 80   LYS A CD  1 
ATOM   417  C  CE  . LYS A 1 80   ? 28.758 34.483  26.850  1.00 22.73 ? 80   LYS A CE  1 
ATOM   418  N  NZ  . LYS A 1 80   ? 29.565 34.179  28.136  1.00 29.05 ? 80   LYS A NZ  1 
ATOM   419  N  N   . LEU A 1 81   ? 26.379 36.256  22.028  1.00 11.63 ? 81   LEU A N   1 
ATOM   420  C  CA  . LEU A 1 81   ? 26.645 37.401  21.165  1.00 11.04 ? 81   LEU A CA  1 
ATOM   421  C  C   . LEU A 1 81   ? 27.902 38.118  21.647  1.00 11.13 ? 81   LEU A C   1 
ATOM   422  O  O   . LEU A 1 81   ? 27.975 38.575  22.765  1.00 11.09 ? 81   LEU A O   1 
ATOM   423  C  CB  . LEU A 1 81   ? 25.442 38.332  21.193  1.00 12.23 ? 81   LEU A CB  1 
ATOM   424  C  CG  . LEU A 1 81   ? 25.596 39.626  20.388  1.00 11.02 ? 81   LEU A CG  1 
ATOM   425  C  CD1 . LEU A 1 81   ? 25.696 39.322  18.917  1.00 11.71 ? 81   LEU A CD1 1 
ATOM   426  C  CD2 . LEU A 1 81   ? 24.448 40.586  20.634  1.00 14.14 ? 81   LEU A CD2 1 
ATOM   427  N  N   . LYS A 1 82   ? 28.904 38.146  20.790  1.00 10.27 ? 82   LYS A N   1 
ATOM   428  C  CA  . LYS A 1 82   ? 30.156 38.800  21.117  1.00 9.94  ? 82   LYS A CA  1 
ATOM   429  C  C   . LYS A 1 82   ? 30.109 40.232  20.600  1.00 10.34 ? 82   LYS A C   1 
ATOM   430  O  O   . LYS A 1 82   ? 29.936 40.444  19.413  1.00 12.24 ? 82   LYS A O   1 
ATOM   431  C  CB  . LYS A 1 82   ? 31.313 38.056  20.449  1.00 11.61 ? 82   LYS A CB  1 
ATOM   432  C  CG  . LYS A 1 82   ? 32.677 38.632  20.763  1.00 22.52 ? 82   LYS A CG  1 
ATOM   433  C  CD  . LYS A 1 82   ? 33.145 38.226  22.147  1.00 29.17 ? 82   LYS A CD  1 
ATOM   434  C  CE  . LYS A 1 82   ? 34.656 38.395  22.309  1.00 35.57 ? 82   LYS A CE  1 
ATOM   435  N  NZ  . LYS A 1 82   ? 35.401 37.237  21.780  1.00 35.50 ? 82   LYS A NZ  1 
ATOM   436  N  N   . VAL A 1 83   ? 30.263 41.198  21.501  1.00 7.26  ? 83   VAL A N   1 
ATOM   437  C  CA  . VAL A 1 83   ? 30.107 42.610  21.147  1.00 8.22  ? 83   VAL A CA  1 
ATOM   438  C  C   . VAL A 1 83   ? 31.432 43.306  21.291  1.00 8.49  ? 83   VAL A C   1 
ATOM   439  O  O   . VAL A 1 83   ? 32.061 43.300  22.389  1.00 9.63  ? 83   VAL A O   1 
ATOM   440  C  CB  . VAL A 1 83   ? 29.068 43.276  22.081  1.00 7.23  ? 83   VAL A CB  1 
ATOM   441  C  CG1 . VAL A 1 83   ? 28.903 44.789  21.764  1.00 9.14  ? 83   VAL A CG1 1 
ATOM   442  C  CG2 . VAL A 1 83   ? 27.704 42.568  21.946  1.00 9.40  ? 83   VAL A CG2 1 
ATOM   443  N  N   . PHE A 1 84   ? 31.874 43.999  20.229  1.00 8.55  ? 84   PHE A N   1 
ATOM   444  C  CA  . PHE A 1 84   ? 33.109 44.804  20.280  1.00 9.19  ? 84   PHE A CA  1 
ATOM   445  C  C   . PHE A 1 84   ? 32.764 46.272  20.206  1.00 8.00  ? 84   PHE A C   1 
ATOM   446  O  O   . PHE A 1 84   ? 32.252 46.751  19.185  1.00 8.76  ? 84   PHE A O   1 
ATOM   447  C  CB  . PHE A 1 84   ? 34.010 44.448  19.118  1.00 9.30  ? 84   PHE A CB  1 
ATOM   448  C  CG  . PHE A 1 84   ? 34.636 43.116  19.261  1.00 10.34 ? 84   PHE A CG  1 
ATOM   449  C  CD1 . PHE A 1 84   ? 35.675 42.935  20.182  1.00 13.63 ? 84   PHE A CD1 1 
ATOM   450  C  CD2 . PHE A 1 84   ? 34.218 42.061  18.520  1.00 12.20 ? 84   PHE A CD2 1 
ATOM   451  C  CE1 . PHE A 1 84   ? 36.312 41.653  20.350  1.00 14.24 ? 84   PHE A CE1 1 
ATOM   452  C  CE2 . PHE A 1 84   ? 34.835 40.776  18.680  1.00 17.56 ? 84   PHE A CE2 1 
ATOM   453  C  CZ  . PHE A 1 84   ? 35.863 40.599  19.576  1.00 16.58 ? 84   PHE A CZ  1 
ATOM   454  N  N   . VAL A 1 85   ? 33.035 46.996  21.284  1.00 7.10  ? 85   VAL A N   1 
ATOM   455  C  CA  . VAL A 1 85   ? 32.817 48.446  21.347  1.00 6.76  ? 85   VAL A CA  1 
ATOM   456  C  C   . VAL A 1 85   ? 34.161 49.063  20.953  1.00 7.00  ? 85   VAL A C   1 
ATOM   457  O  O   . VAL A 1 85   ? 35.184 48.887  21.622  1.00 7.84  ? 85   VAL A O   1 
ATOM   458  C  CB  . VAL A 1 85   ? 32.374 48.860  22.757  1.00 7.91  ? 85   VAL A CB  1 
ATOM   459  C  CG1 . VAL A 1 85   ? 32.228 50.397  22.844  1.00 10.85 ? 85   VAL A CG1 1 
ATOM   460  C  CG2 . VAL A 1 85   ? 31.029 48.134  23.086  1.00 9.19  ? 85   VAL A CG2 1 
ATOM   461  N  N   . VAL A 1 86   ? 34.111 49.838  19.841  1.00 6.78  ? 86   VAL A N   1 
ATOM   462  C  CA  . VAL A 1 86   ? 35.354 50.338  19.231  1.00 6.31  ? 86   VAL A CA  1 
ATOM   463  C  C   . VAL A 1 86   ? 35.435 51.850  19.352  1.00 6.62  ? 86   VAL A C   1 
ATOM   464  O  O   . VAL A 1 86   ? 34.760 52.569  18.559  1.00 6.99  ? 86   VAL A O   1 
ATOM   465  C  CB  . VAL A 1 86   ? 35.374 49.895  17.748  1.00 7.07  ? 86   VAL A CB  1 
ATOM   466  C  CG1 . VAL A 1 86   ? 36.681 50.409  17.050  1.00 9.28  ? 86   VAL A CG1 1 
ATOM   467  C  CG2 . VAL A 1 86   ? 35.319 48.342  17.654  1.00 9.22  ? 86   VAL A CG2 1 
ATOM   468  N  N   . PRO A 1 87   ? 36.195 52.380  20.299  1.00 6.46  ? 87   PRO A N   1 
ATOM   469  C  CA  . PRO A 1 87   ? 36.315 53.832  20.462  1.00 7.81  ? 87   PRO A CA  1 
ATOM   470  C  C   . PRO A 1 87   ? 37.034 54.452  19.272  1.00 6.43  ? 87   PRO A C   1 
ATOM   471  O  O   . PRO A 1 87   ? 38.052 53.911  18.768  1.00 6.63  ? 87   PRO A O   1 
ATOM   472  C  CB  . PRO A 1 87   ? 37.144 54.007  21.769  1.00 7.22  ? 87   PRO A CB  1 
ATOM   473  C  CG  . PRO A 1 87   ? 36.863 52.660  22.484  1.00 8.41  ? 87   PRO A CG  1 
ATOM   474  C  CD  . PRO A 1 87   ? 36.962 51.666  21.361  1.00 7.74  ? 87   PRO A CD  1 
ATOM   475  N  N   . HIS A 1 88   ? 36.545 55.612  18.844  1.00 5.71  ? 88   HIS A N   1 
ATOM   476  C  CA  . HIS A 1 88   ? 37.130 56.315  17.687  1.00 6.69  ? 88   HIS A CA  1 
ATOM   477  C  C   . HIS A 1 88   ? 36.909 57.824  17.783  1.00 7.13  ? 88   HIS A C   1 
ATOM   478  O  O   . HIS A 1 88   ? 36.119 58.280  18.574  1.00 7.38  ? 88   HIS A O   1 
ATOM   479  C  CB  . HIS A 1 88   ? 36.579 55.753  16.363  1.00 7.70  ? 88   HIS A CB  1 
ATOM   480  C  CG  . HIS A 1 88   ? 35.142 56.079  16.121  1.00 6.39  ? 88   HIS A CG  1 
ATOM   481  N  ND1 . HIS A 1 88   ? 34.743 57.155  15.363  1.00 6.72  ? 88   HIS A ND1 1 
ATOM   482  C  CD2 . HIS A 1 88   ? 34.011 55.476  16.559  1.00 7.35  ? 88   HIS A CD2 1 
ATOM   483  C  CE1 . HIS A 1 88   ? 33.425 57.185  15.321  1.00 8.22  ? 88   HIS A CE1 1 
ATOM   484  N  NE2 . HIS A 1 88   ? 32.957 56.174  16.032  1.00 8.78  ? 88   HIS A NE2 1 
ATOM   485  N  N   . SER A 1 89   ? 37.625 58.583  16.959  1.00 7.00  ? 89   SER A N   1 
ATOM   486  C  CA  . SER A 1 89   ? 37.544 60.038  16.951  1.00 7.24  ? 89   SER A CA  1 
ATOM   487  C  C   . SER A 1 89   ? 37.705 60.479  15.479  1.00 6.79  ? 89   SER A C   1 
ATOM   488  O  O   . SER A 1 89   ? 38.795 60.305  14.915  1.00 6.95  ? 89   SER A O   1 
ATOM   489  C  CB  . SER A 1 89   ? 38.679 60.608  17.854  1.00 7.34  ? 89   SER A CB  1 
ATOM   490  O  OG  . SER A 1 89   ? 38.660 62.010  17.796  1.00 7.87  ? 89   SER A OG  1 
ATOM   491  N  N   . HIS A 1 90   ? 36.651 61.065  14.903  1.00 6.99  ? 90   HIS A N   1 
ATOM   492  C  CA  . HIS A 1 90   ? 36.750 61.455  13.486  1.00 6.16  ? 90   HIS A CA  1 
ATOM   493  C  C   . HIS A 1 90   ? 37.410 62.836  13.389  1.00 6.58  ? 90   HIS A C   1 
ATOM   494  O  O   . HIS A 1 90   ? 36.862 63.845  13.888  1.00 7.87  ? 90   HIS A O   1 
ATOM   495  C  CB  . HIS A 1 90   ? 35.352 61.427  12.909  1.00 6.80  ? 90   HIS A CB  1 
ATOM   496  C  CG  . HIS A 1 90   ? 35.307 61.791  11.457  1.00 5.81  ? 90   HIS A CG  1 
ATOM   497  N  ND1 . HIS A 1 90   ? 35.913 61.031  10.473  1.00 7.00  ? 90   HIS A ND1 1 
ATOM   498  C  CD2 . HIS A 1 90   ? 34.711 62.828  10.829  1.00 6.98  ? 90   HIS A CD2 1 
ATOM   499  C  CE1 . HIS A 1 90   ? 35.712 61.628  9.296   1.00 6.91  ? 90   HIS A CE1 1 
ATOM   500  N  NE2 . HIS A 1 90   ? 34.996 62.725  9.469   1.00 6.21  ? 90   HIS A NE2 1 
ATOM   501  N  N   . ASN A 1 91   ? 38.594 62.904  12.788  1.00 7.01  ? 91   ASN A N   1 
ATOM   502  C  CA  . ASN A 1 91   ? 39.395 64.142  12.751  1.00 7.32  ? 91   ASN A CA  1 
ATOM   503  C  C   . ASN A 1 91   ? 39.592 64.642  11.333  1.00 10.05 ? 91   ASN A C   1 
ATOM   504  O  O   . ASN A 1 91   ? 40.432 64.154  10.612  1.00 14.42 ? 91   ASN A O   1 
ATOM   505  C  CB  . ASN A 1 91   ? 40.779 63.889  13.363  1.00 7.97  ? 91   ASN A CB  1 
ATOM   506  C  CG  . ASN A 1 91   ? 40.745 63.871  14.875  1.00 9.00  ? 91   ASN A CG  1 
ATOM   507  O  OD1 . ASN A 1 91   ? 41.315 64.716  15.523  1.00 10.54 ? 91   ASN A OD1 1 
ATOM   508  N  ND2 . ASN A 1 91   ? 40.049 62.915  15.432  1.00 6.88  ? 91   ASN A ND2 1 
ATOM   509  N  N   . ASP A 1 92   ? 38.862 65.667  10.964  1.00 6.84  ? 92   ASP A N   1 
ATOM   510  C  CA  . ASP A 1 92   ? 38.979 66.183  9.578   1.00 6.68  ? 92   ASP A CA  1 
ATOM   511  C  C   . ASP A 1 92   ? 40.192 67.023  9.362   1.00 8.07  ? 92   ASP A C   1 
ATOM   512  O  O   . ASP A 1 92   ? 40.394 67.988  10.115  1.00 7.97  ? 92   ASP A O   1 
ATOM   513  C  CB  . ASP A 1 92   ? 37.777 67.114  9.338   1.00 7.05  ? 92   ASP A CB  1 
ATOM   514  C  CG  . ASP A 1 92   ? 36.508 66.356  9.418   1.00 8.25  ? 92   ASP A CG  1 
ATOM   515  O  OD1 . ASP A 1 92   ? 36.303 65.458  8.610   1.00 7.94  ? 92   ASP A OD1 1 
ATOM   516  O  OD2 . ASP A 1 92   ? 35.725 66.578  10.387  1.00 8.67  ? 92   ASP A OD2 1 
ATOM   517  N  N   . PRO A 1 93   ? 41.005 66.718  8.337   1.00 6.70  ? 93   PRO A N   1 
ATOM   518  C  CA  . PRO A 1 93   ? 42.207 67.539  8.022   1.00 7.81  ? 93   PRO A CA  1 
ATOM   519  C  C   . PRO A 1 93   ? 41.756 68.803  7.269   1.00 8.51  ? 93   PRO A C   1 
ATOM   520  O  O   . PRO A 1 93   ? 42.073 69.028  6.059   1.00 9.77  ? 93   PRO A O   1 
ATOM   521  C  CB  . PRO A 1 93   ? 43.035 66.627  7.148   1.00 8.37  ? 93   PRO A CB  1 
ATOM   522  C  CG  . PRO A 1 93   ? 42.545 65.196  7.490   1.00 13.17 ? 93   PRO A CG  1 
ATOM   523  C  CD  . PRO A 1 93   ? 41.024 65.403  7.645   1.00 6.83  ? 93   PRO A CD  1 
ATOM   524  N  N   . GLY A 1 94   ? 40.983 69.647  7.970   1.00 7.50  ? 94   GLY A N   1 
ATOM   525  C  CA  . GLY A 1 94   ? 40.379 70.862  7.437   1.00 7.92  ? 94   GLY A CA  1 
ATOM   526  C  C   . GLY A 1 94   ? 38.876 70.632  7.177   1.00 8.15  ? 94   GLY A C   1 
ATOM   527  O  O   . GLY A 1 94   ? 38.451 69.573  6.623   1.00 8.22  ? 94   GLY A O   1 
ATOM   528  N  N   . TRP A 1 95   ? 38.067 71.625  7.589   1.00 7.56  ? 95   TRP A N   1 
ATOM   529  C  CA  . TRP A 1 95   ? 36.648 71.635  7.309   1.00 7.46  ? 95   TRP A CA  1 
ATOM   530  C  C   . TRP A 1 95   ? 36.157 73.049  7.726   1.00 8.80  ? 95   TRP A C   1 
ATOM   531  O  O   . TRP A 1 95   ? 36.094 73.963  6.889   1.00 8.24  ? 95   TRP A O   1 
ATOM   532  C  CB  . TRP A 1 95   ? 35.854 70.513  8.003   1.00 6.85  ? 95   TRP A CB  1 
ATOM   533  C  CG  . TRP A 1 95   ? 34.363 70.687  7.660   1.00 7.18  ? 95   TRP A CG  1 
ATOM   534  C  CD1 . TRP A 1 95   ? 33.831 71.047  6.428   1.00 7.74  ? 95   TRP A CD1 1 
ATOM   535  C  CD2 . TRP A 1 95   ? 33.255 70.408  8.508   1.00 7.50  ? 95   TRP A CD2 1 
ATOM   536  N  NE1 . TRP A 1 95   ? 32.443 71.000  6.495   1.00 8.00  ? 95   TRP A NE1 1 
ATOM   537  C  CE2 . TRP A 1 95   ? 32.080 70.600  7.753   1.00 7.35  ? 95   TRP A CE2 1 
ATOM   538  C  CE3 . TRP A 1 95   ? 33.144 69.982  9.853   1.00 9.01  ? 95   TRP A CE3 1 
ATOM   539  C  CZ2 . TRP A 1 95   ? 30.800 70.384  8.282   1.00 7.63  ? 95   TRP A CZ2 1 
ATOM   540  C  CZ3 . TRP A 1 95   ? 31.870 69.781  10.381  1.00 9.24  ? 95   TRP A CZ3 1 
ATOM   541  C  CH2 . TRP A 1 95   ? 30.713 69.982  9.595   1.00 8.41  ? 95   TRP A CH2 1 
ATOM   542  N  N   . ILE A 1 96   ? 35.802 73.226  8.998   1.00 8.12  ? 96   ILE A N   1 
ATOM   543  C  CA  . ILE A 1 96   ? 35.432 74.532  9.572   1.00 9.22  ? 96   ILE A CA  1 
ATOM   544  C  C   . ILE A 1 96   ? 36.646 75.315  10.041  1.00 10.58 ? 96   ILE A C   1 
ATOM   545  O  O   . ILE A 1 96   ? 36.579 76.522  10.184  1.00 12.86 ? 96   ILE A O   1 
ATOM   546  C  CB  . ILE A 1 96   ? 34.543 74.398  10.859  1.00 15.36 ? 96   ILE A CB  1 
ATOM   547  C  CG1 . ILE A 1 96   ? 33.284 73.601  10.587  1.00 19.37 ? 96   ILE A CG1 1 
ATOM   548  C  CG2 . ILE A 1 96   ? 34.211 75.778  11.448  1.00 17.25 ? 96   ILE A CG2 1 
ATOM   549  C  CD1 . ILE A 1 96   ? 32.693 73.980  9.291   1.00 12.63 ? 96   ILE A CD1 1 
ATOM   550  N  N   . GLN A 1 97   ? 37.721 74.590  10.318  1.00 7.62  ? 97   GLN A N   1 
ATOM   551  C  CA  . GLN A 1 97   ? 39.041 75.162  10.653  1.00 7.89  ? 97   GLN A CA  1 
ATOM   552  C  C   . GLN A 1 97   ? 40.069 74.579  9.690   1.00 6.99  ? 97   GLN A C   1 
ATOM   553  O  O   . GLN A 1 97   ? 39.796 73.556  9.032   1.00 7.27  ? 97   GLN A O   1 
ATOM   554  C  CB  . GLN A 1 97   ? 39.472 74.814  12.076  1.00 9.24  ? 97   GLN A CB  1 
ATOM   555  C  CG  . GLN A 1 97   ? 38.472 75.363  13.113  1.00 12.79 ? 97   GLN A CG  1 
ATOM   556  C  CD  . GLN A 1 97   ? 38.944 75.121  14.530  1.00 17.09 ? 97   GLN A CD  1 
ATOM   557  O  OE1 . GLN A 1 97   ? 40.110 75.338  14.854  1.00 21.95 ? 97   GLN A OE1 1 
ATOM   558  N  NE2 . GLN A 1 97   ? 38.038 74.631  15.388  1.00 20.40 ? 97   GLN A NE2 1 
ATOM   559  N  N   . THR A 1 98   ? 41.253 75.193  9.553   1.00 7.64  ? 98   THR A N   1 
ATOM   560  C  CA  . THR A 1 98   ? 42.291 74.586  8.717   1.00 7.35  ? 98   THR A CA  1 
ATOM   561  C  C   . THR A 1 98   ? 42.892 73.373  9.441   1.00 7.28  ? 98   THR A C   1 
ATOM   562  O  O   . THR A 1 98   ? 42.679 73.160  10.646  1.00 7.86  ? 98   THR A O   1 
ATOM   563  C  CB  . THR A 1 98   ? 43.423 75.539  8.461   1.00 7.76  ? 98   THR A CB  1 
ATOM   564  O  OG1 . THR A 1 98   ? 44.022 75.893  9.724   1.00 9.09  ? 98   THR A OG1 1 
ATOM   565  C  CG2 . THR A 1 98   ? 42.912 76.855  7.813   1.00 8.91  ? 98   THR A CG2 1 
ATOM   566  N  N   . PHE A 1 99   ? 43.666 72.600  8.691   1.00 7.31  ? 99   PHE A N   1 
ATOM   567  C  CA  . PHE A 1 99   ? 44.474 71.532  9.260   1.00 7.38  ? 99   PHE A CA  1 
ATOM   568  C  C   . PHE A 1 99   ? 45.228 72.002  10.502  1.00 7.70  ? 99   PHE A C   1 
ATOM   569  O  O   . PHE A 1 99   ? 45.122 71.405  11.548  1.00 8.00  ? 99   PHE A O   1 
ATOM   570  C  CB  . PHE A 1 99   ? 45.454 70.976  8.210   1.00 8.25  ? 99   PHE A CB  1 
ATOM   571  C  CG  . PHE A 1 99   ? 46.324 69.854  8.732   1.00 8.00  ? 99   PHE A CG  1 
ATOM   572  C  CD1 . PHE A 1 99   ? 47.556 70.120  9.333   1.00 9.26  ? 99   PHE A CD1 1 
ATOM   573  C  CD2 . PHE A 1 99   ? 45.899 68.542  8.649   1.00 7.66  ? 99   PHE A CD2 1 
ATOM   574  C  CE1 . PHE A 1 99   ? 48.320 69.097  9.828   1.00 9.95  ? 99   PHE A CE1 1 
ATOM   575  C  CE2 . PHE A 1 99   ? 46.674 67.523  9.138   1.00 9.13  ? 99   PHE A CE2 1 
ATOM   576  C  CZ  . PHE A 1 99   ? 47.896 67.796  9.727   1.00 8.39  ? 99   PHE A CZ  1 
ATOM   577  N  N   . GLU A 1 100  ? 45.998 73.077  10.376  1.00 8.04  ? 100  GLU A N   1 
ATOM   578  C  CA  . GLU A 1 100  ? 46.826 73.477  11.503  1.00 8.54  ? 100  GLU A CA  1 
ATOM   579  C  C   . GLU A 1 100  ? 46.010 74.015  12.651  1.00 8.86  ? 100  GLU A C   1 
ATOM   580  O  O   . GLU A 1 100  ? 46.379 73.794  13.815  1.00 9.50  ? 100  GLU A O   1 
ATOM   581  C  CB  . GLU A 1 100  ? 47.878 74.508  11.039  1.00 9.38  ? 100  GLU A CB  1 
ATOM   582  C  CG  . GLU A 1 100  ? 48.897 74.862  12.125  1.00 11.81 ? 100  GLU A CG  1 
ATOM   583  C  CD  . GLU A 1 100  ? 49.773 73.689  12.549  1.00 13.55 ? 100  GLU A CD  1 
ATOM   584  O  OE1 . GLU A 1 100  ? 49.909 72.669  11.823  1.00 13.41 ? 100  GLU A OE1 1 
ATOM   585  O  OE2 . GLU A 1 100  ? 50.404 73.837  13.657  1.00 13.22 ? 100  GLU A OE2 1 
ATOM   586  N  N   . GLU A 1 101  ? 44.906 74.679  12.385  1.00 8.56  ? 101  GLU A N   1 
ATOM   587  C  CA  . GLU A 1 101  ? 44.059 75.181  13.457  1.00 8.41  ? 101  GLU A CA  1 
ATOM   588  C  C   . GLU A 1 101  ? 43.475 73.997  14.214  1.00 9.09  ? 101  GLU A C   1 
ATOM   589  O  O   . GLU A 1 101  ? 43.446 73.980  15.459  1.00 9.08  ? 101  GLU A O   1 
ATOM   590  C  CB  . GLU A 1 101  ? 42.940 76.043  12.871  1.00 9.29  ? 101  GLU A CB  1 
ATOM   591  C  CG  . GLU A 1 101  ? 43.405 77.436  12.471  1.00 11.99 ? 101  GLU A CG  1 
ATOM   592  C  CD  . GLU A 1 101  ? 42.404 78.166  11.524  1.00 12.97 ? 101  GLU A CD  1 
ATOM   593  O  OE1 . GLU A 1 101  ? 41.341 77.654  11.076  1.00 11.66 ? 101  GLU A OE1 1 
ATOM   594  O  OE2 . GLU A 1 101  ? 42.672 79.386  11.202  1.00 17.83 ? 101  GLU A OE2 1 
ATOM   595  N  N   . TYR A 1 102  ? 42.942 73.008  13.516  1.00 7.53  ? 102  TYR A N   1 
ATOM   596  C  CA  . TYR A 1 102  ? 42.376 71.864  14.224  1.00 7.67  ? 102  TYR A CA  1 
ATOM   597  C  C   . TYR A 1 102  ? 43.483 71.135  15.002  1.00 7.90  ? 102  TYR A C   1 
ATOM   598  O  O   . TYR A 1 102  ? 43.259 70.649  16.095  1.00 8.09  ? 102  TYR A O   1 
ATOM   599  C  CB  . TYR A 1 102  ? 41.757 70.874  13.243  1.00 8.16  ? 102  TYR A CB  1 
ATOM   600  C  CG  . TYR A 1 102  ? 40.317 71.086  12.801  1.00 7.41  ? 102  TYR A CG  1 
ATOM   601  C  CD1 . TYR A 1 102  ? 39.294 71.324  13.704  1.00 8.18  ? 102  TYR A CD1 1 
ATOM   602  C  CD2 . TYR A 1 102  ? 39.983 70.941  11.461  1.00 7.85  ? 102  TYR A CD2 1 
ATOM   603  C  CE1 . TYR A 1 102  ? 37.972 71.454  13.268  1.00 8.02  ? 102  TYR A CE1 1 
ATOM   604  C  CE2 . TYR A 1 102  ? 38.692 71.058  11.024  1.00 7.51  ? 102  TYR A CE2 1 
ATOM   605  C  CZ  . TYR A 1 102  ? 37.692 71.307  11.928  1.00 7.17  ? 102  TYR A CZ  1 
ATOM   606  O  OH  . TYR A 1 102  ? 36.402 71.422  11.459  1.00 9.51  ? 102  TYR A OH  1 
ATOM   607  N  N   . TYR A 1 103  ? 44.667 71.043  14.418  1.00 7.62  ? 103  TYR A N   1 
ATOM   608  C  CA  . TYR A 1 103  ? 45.729 70.329  15.096  1.00 8.44  ? 103  TYR A CA  1 
ATOM   609  C  C   . TYR A 1 103  ? 46.028 71.018  16.431  1.00 8.58  ? 103  TYR A C   1 
ATOM   610  O  O   . TYR A 1 103  ? 46.129 70.367  17.465  1.00 9.21  ? 103  TYR A O   1 
ATOM   611  C  CB  . TYR A 1 103  ? 46.993 70.245  14.226  1.00 7.90  ? 103  TYR A CB  1 
ATOM   612  C  CG  . TYR A 1 103  ? 48.133 69.616  14.994  1.00 8.51  ? 103  TYR A CG  1 
ATOM   613  C  CD1 . TYR A 1 103  ? 48.148 68.252  15.264  1.00 9.40  ? 103  TYR A CD1 1 
ATOM   614  C  CD2 . TYR A 1 103  ? 49.172 70.390  15.495  1.00 9.59  ? 103  TYR A CD2 1 
ATOM   615  C  CE1 . TYR A 1 103  ? 49.159 67.687  15.987  1.00 10.55 ? 103  TYR A CE1 1 
ATOM   616  C  CE2 . TYR A 1 103  ? 50.201 69.814  16.227  1.00 9.05  ? 103  TYR A CE2 1 
ATOM   617  C  CZ  . TYR A 1 103  ? 50.175 68.475  16.466  1.00 10.40 ? 103  TYR A CZ  1 
ATOM   618  O  OH  . TYR A 1 103  ? 51.181 67.890  17.195  1.00 12.43 ? 103  TYR A OH  1 
ATOM   619  N  N   . GLN A 1 104  ? 46.143 72.348  16.399  1.00 8.52  ? 104  GLN A N   1 
ATOM   620  C  CA  . GLN A 1 104  ? 46.513 73.066  17.633  1.00 9.05  ? 104  GLN A CA  1 
ATOM   621  C  C   . GLN A 1 104  ? 45.383 73.072  18.623  1.00 10.70 ? 104  GLN A C   1 
ATOM   622  O  O   . GLN A 1 104  ? 45.636 72.970  19.843  1.00 11.81 ? 104  GLN A O   1 
ATOM   623  C  CB  . GLN A 1 104  ? 46.873 74.536  17.280  1.00 12.18 ? 104  GLN A CB  1 
ATOM   624  C  CG  . GLN A 1 104  ? 48.163 74.674  16.549  1.00 12.14 ? 104  GLN A CG  1 
ATOM   625  C  CD  . GLN A 1 104  ? 49.355 74.151  17.330  1.00 13.01 ? 104  GLN A CD  1 
ATOM   626  O  OE1 . GLN A 1 104  ? 49.351 74.224  18.586  1.00 13.45 ? 104  GLN A OE1 1 
ATOM   627  N  NE2 . GLN A 1 104  ? 50.368 73.611  16.633  1.00 10.99 ? 104  GLN A NE2 1 
ATOM   628  N  N   . HIS A 1 105  ? 44.114 73.160  18.194  1.00 10.18 ? 105  HIS A N   1 
ATOM   629  C  CA  . HIS A 1 105  ? 42.990 73.323  19.122  1.00 11.21 ? 105  HIS A CA  1 
ATOM   630  C  C   . HIS A 1 105  ? 42.426 72.038  19.611  1.00 11.30 ? 105  HIS A C   1 
ATOM   631  O  O   . HIS A 1 105  ? 41.929 71.982  20.735  1.00 13.82 ? 105  HIS A O   1 
ATOM   632  C  CB  . HIS A 1 105  ? 41.857 74.103  18.429  1.00 12.79 ? 105  HIS A CB  1 
ATOM   633  C  CG  . HIS A 1 105  ? 42.276 75.464  17.938  1.00 16.48 ? 105  HIS A CG  1 
ATOM   634  N  ND1 . HIS A 1 105  ? 41.705 76.090  16.848  1.00 22.00 ? 105  HIS A ND1 1 
ATOM   635  C  CD2 . HIS A 1 105  ? 43.235 76.307  18.398  1.00 19.01 ? 105  HIS A CD2 1 
ATOM   636  C  CE1 . HIS A 1 105  ? 42.305 77.256  16.651  1.00 21.25 ? 105  HIS A CE1 1 
ATOM   637  N  NE2 . HIS A 1 105  ? 43.236 77.413  17.582  1.00 23.52 ? 105  HIS A NE2 1 
ATOM   638  N  N   . ASP A 1 106  ? 42.522 70.980  18.786  1.00 9.71  ? 106  ASP A N   1 
ATOM   639  C  CA  . ASP A 1 106  ? 41.894 69.723  19.094  1.00 10.79 ? 106  ASP A CA  1 
ATOM   640  C  C   . ASP A 1 106  ? 42.743 68.483  18.969  1.00 9.06  ? 106  ASP A C   1 
ATOM   641  O  O   . ASP A 1 106  ? 42.944 67.763  19.963  1.00 9.78  ? 106  ASP A O   1 
ATOM   642  C  CB  . ASP A 1 106  ? 40.672 69.541  18.155  1.00 12.07 ? 106  ASP A CB  1 
ATOM   643  C  CG  . ASP A 1 106  ? 39.627 70.629  18.355  1.00 20.52 ? 106  ASP A CG  1 
ATOM   644  O  OD1 . ASP A 1 106  ? 38.841 70.485  19.329  1.00 18.53 ? 106  ASP A OD1 1 
ATOM   645  O  OD2 . ASP A 1 106  ? 39.617 71.608  17.545  1.00 18.83 ? 106  ASP A OD2 1 
ATOM   646  N  N   . THR A 1 107  ? 43.276 68.216  17.772  1.00 8.61  ? 107  THR A N   1 
ATOM   647  C  CA  . THR A 1 107  ? 43.885 66.908  17.512  1.00 8.47  ? 107  THR A CA  1 
ATOM   648  C  C   . THR A 1 107  ? 45.126 66.635  18.337  1.00 8.11  ? 107  THR A C   1 
ATOM   649  O  O   . THR A 1 107  ? 45.335 65.496  18.778  1.00 7.70  ? 107  THR A O   1 
ATOM   650  C  CB  . THR A 1 107  ? 44.156 66.718  16.001  1.00 7.94  ? 107  THR A CB  1 
ATOM   651  O  OG1 . THR A 1 107  ? 42.930 66.988  15.323  1.00 8.84  ? 107  THR A OG1 1 
ATOM   652  C  CG2 . THR A 1 107  ? 44.653 65.332  15.694  1.00 8.31  ? 107  THR A CG2 1 
ATOM   653  N  N   . LYS A 1 108  ? 45.951 67.641  18.561  1.00 8.28  ? 108  LYS A N   1 
ATOM   654  C  CA  . LYS A 1 108  ? 47.122 67.321  19.380  1.00 7.87  ? 108  LYS A CA  1 
ATOM   655  C  C   . LYS A 1 108  ? 46.749 66.925  20.811  1.00 7.20  ? 108  LYS A C   1 
ATOM   656  O  O   . LYS A 1 108  ? 47.453 66.109  21.393  1.00 9.66  ? 108  LYS A O   1 
ATOM   657  C  CB  . LYS A 1 108  ? 48.107 68.506  19.352  1.00 11.15 ? 108  LYS A CB  1 
ATOM   658  C  CG  . LYS A 1 108  ? 47.832 69.661  20.284  1.00 10.42 ? 108  LYS A CG  1 
ATOM   659  C  CD  . LYS A 1 108  ? 48.943 70.720  20.090  1.00 13.54 ? 108  LYS A CD  1 
ATOM   660  C  CE  . LYS A 1 108  ? 48.804 71.859  21.042  1.00 13.43 ? 108  LYS A CE  1 
ATOM   661  N  NZ  . LYS A 1 108  ? 49.950 72.841  20.880  1.00 16.46 ? 108  LYS A NZ  1 
ATOM   662  N  N   . HIS A 1 109  ? 45.653 67.463  21.308  1.00 8.27  ? 109  HIS A N   1 
ATOM   663  C  CA  . HIS A 1 109  ? 45.164 67.094  22.645  1.00 8.75  ? 109  HIS A CA  1 
ATOM   664  C  C   . HIS A 1 109  ? 44.539 65.726  22.630  1.00 8.31  ? 109  HIS A C   1 
ATOM   665  O  O   . HIS A 1 109  ? 44.745 64.949  23.581  1.00 9.73  ? 109  HIS A O   1 
ATOM   666  C  CB  . HIS A 1 109  ? 44.200 68.150  23.139  1.00 10.40 ? 109  HIS A CB  1 
ATOM   667  C  CG  . HIS A 1 109  ? 44.791 69.507  23.147  1.00 13.29 ? 109  HIS A CG  1 
ATOM   668  N  ND1 . HIS A 1 109  ? 45.811 69.844  24.018  1.00 19.21 ? 109  HIS A ND1 1 
ATOM   669  C  CD2 . HIS A 1 109  ? 44.576 70.590  22.359  1.00 17.51 ? 109  HIS A CD2 1 
ATOM   670  C  CE1 . HIS A 1 109  ? 46.189 71.093  23.773  1.00 17.88 ? 109  HIS A CE1 1 
ATOM   671  N  NE2 . HIS A 1 109  ? 45.459 71.565  22.779  1.00 18.79 ? 109  HIS A NE2 1 
ATOM   672  N  N   . ILE A 1 110  ? 43.780 65.383  21.582  1.00 8.88  ? 110  ILE A N   1 
ATOM   673  C  CA  . ILE A 1 110  ? 43.215 64.048  21.477  1.00 7.67  ? 110  ILE A CA  1 
ATOM   674  C  C   . ILE A 1 110  ? 44.320 62.994  21.460  1.00 7.37  ? 110  ILE A C   1 
ATOM   675  O  O   . ILE A 1 110  ? 44.243 61.978  22.189  1.00 8.09  ? 110  ILE A O   1 
ATOM   676  C  CB  . ILE A 1 110  ? 42.382 63.964  20.176  1.00 8.04  ? 110  ILE A CB  1 
ATOM   677  C  CG1 . ILE A 1 110  ? 41.173 64.885  20.295  1.00 8.70  ? 110  ILE A CG1 1 
ATOM   678  C  CG2 . ILE A 1 110  ? 41.998 62.508  19.904  1.00 7.64  ? 110  ILE A CG2 1 
ATOM   679  C  CD1 . ILE A 1 110  ? 40.439 65.109  18.902  1.00 8.13  ? 110  ILE A CD1 1 
ATOM   680  N  N   . LEU A 1 111  ? 45.354 63.194  20.658  1.00 7.33  ? 111  LEU A N   1 
ATOM   681  C  CA  . LEU A 1 111  ? 46.408 62.192  20.559  1.00 7.41  ? 111  LEU A CA  1 
ATOM   682  C  C   . LEU A 1 111  ? 47.266 62.127  21.829  1.00 6.74  ? 111  LEU A C   1 
ATOM   683  O  O   . LEU A 1 111  ? 47.659 61.063  22.245  1.00 8.89  ? 111  LEU A O   1 
ATOM   684  C  CB  . LEU A 1 111  ? 47.262 62.440  19.306  1.00 7.61  ? 111  LEU A CB  1 
ATOM   685  C  CG  . LEU A 1 111  ? 46.531 62.071  18.001  1.00 8.52  ? 111  LEU A CG  1 
ATOM   686  C  CD1 . LEU A 1 111  ? 47.319 62.558  16.783  1.00 8.98  ? 111  LEU A CD1 1 
ATOM   687  C  CD2 . LEU A 1 111  ? 46.318 60.547  17.940  1.00 10.87 ? 111  LEU A CD2 1 
ATOM   688  N  N   . SER A 1 112  ? 47.542 63.271  22.432  1.00 8.29  ? 112  SER A N   1 
ATOM   689  C  CA  . SER A 1 112  ? 48.254 63.274  23.711  1.00 8.69  ? 112  SER A CA  1 
ATOM   690  C  C   . SER A 1 112  ? 47.489 62.543  24.812  1.00 8.81  ? 112  SER A C   1 
ATOM   691  O  O   . SER A 1 112  ? 48.067 61.757  25.546  1.00 9.84  ? 112  SER A O   1 
ATOM   692  C  CB  A SER A 1 112  ? 48.585 64.709  24.134  0.50 10.07 ? 112  SER A CB  1 
ATOM   693  C  CB  B SER A 1 112  ? 48.501 64.689  24.216  0.50 11.16 ? 112  SER A CB  1 
ATOM   694  O  OG  A SER A 1 112  ? 49.406 64.710  25.286  0.50 16.65 ? 112  SER A OG  1 
ATOM   695  O  OG  B SER A 1 112  ? 49.553 65.286  23.518  0.50 27.97 ? 112  SER A OG  1 
ATOM   696  N  N   . ASN A 1 113  ? 46.182 62.789  24.886  1.00 8.94  ? 113  ASN A N   1 
ATOM   697  C  CA  . ASN A 1 113  ? 45.386 62.127  25.910  1.00 9.76  ? 113  ASN A CA  1 
ATOM   698  C  C   . ASN A 1 113  ? 45.137 60.703  25.561  1.00 10.42 ? 113  ASN A C   1 
ATOM   699  O  O   . ASN A 1 113  ? 45.051 59.869  26.503  1.00 10.43 ? 113  ASN A O   1 
ATOM   700  C  CB  . ASN A 1 113  ? 44.123 62.941  26.213  1.00 10.36 ? 113  ASN A CB  1 
ATOM   701  C  CG  . ASN A 1 113  ? 44.527 64.237  26.948  1.00 14.46 ? 113  ASN A CG  1 
ATOM   702  O  OD1 . ASN A 1 113  ? 45.596 64.258  27.650  1.00 22.15 ? 113  ASN A OD1 1 
ATOM   703  N  ND2 . ASN A 1 113  ? 43.815 65.304  26.745  1.00 14.66 ? 113  ASN A ND2 1 
ATOM   704  N  N   . ALA A 1 114  ? 45.078 60.333  24.272  1.00 8.73  ? 114  ALA A N   1 
ATOM   705  C  CA  . ALA A 1 114  ? 44.947 58.910  23.934  1.00 8.84  ? 114  ALA A CA  1 
ATOM   706  C  C   . ALA A 1 114  ? 46.210 58.195  24.375  1.00 9.57  ? 114  ALA A C   1 
ATOM   707  O  O   . ALA A 1 114  ? 46.147 57.058  24.902  1.00 10.71 ? 114  ALA A O   1 
ATOM   708  C  CB  . ALA A 1 114  ? 44.754 58.717  22.414  1.00 9.10  ? 114  ALA A CB  1 
ATOM   709  N  N   . LEU A 1 115  ? 47.380 58.773  24.117  1.00 8.80  ? 115  LEU A N   1 
ATOM   710  C  CA  . LEU A 1 115  ? 48.614 58.122  24.532  1.00 10.46 ? 115  LEU A CA  1 
ATOM   711  C  C   . LEU A 1 115  ? 48.640 57.904  26.074  1.00 10.75 ? 115  LEU A C   1 
ATOM   712  O  O   . LEU A 1 115  ? 48.907 56.787  26.538  1.00 11.19 ? 115  LEU A O   1 
ATOM   713  C  CB  . LEU A 1 115  ? 49.806 58.961  24.085  1.00 10.67 ? 115  LEU A CB  1 
ATOM   714  C  CG  . LEU A 1 115  ? 51.190 58.450  24.534  1.00 11.05 ? 115  LEU A CG  1 
ATOM   715  C  CD1 . LEU A 1 115  ? 51.449 57.009  24.083  1.00 13.32 ? 115  LEU A CD1 1 
ATOM   716  C  CD2 . LEU A 1 115  ? 52.250 59.358  23.975  1.00 14.17 ? 115  LEU A CD2 1 
ATOM   717  N  N   . ARG A 1 116  ? 48.276 58.946  26.815  1.00 10.44 ? 116  ARG A N   1 
ATOM   718  C  CA  . ARG A 1 116  ? 48.278 58.813  28.270  1.00 10.86 ? 116  ARG A CA  1 
ATOM   719  C  C   . ARG A 1 116  ? 47.227 57.795  28.751  1.00 10.03 ? 116  ARG A C   1 
ATOM   720  O  O   . ARG A 1 116  ? 47.522 56.917  29.573  1.00 11.24 ? 116  ARG A O   1 
ATOM   721  C  CB  . ARG A 1 116  ? 47.993 60.181  28.875  1.00 12.70 ? 116  ARG A CB  1 
ATOM   722  C  CG  . ARG A 1 116  ? 47.739 60.129  30.409  1.00 17.34 ? 116  ARG A CG  1 
ATOM   723  C  CD  . ARG A 1 116  ? 46.777 61.315  30.789  1.00 25.88 ? 116  ARG A CD  1 
ATOM   724  N  NE  . ARG A 1 116  ? 46.339 61.271  32.198  1.00 29.84 ? 116  ARG A NE  1 
ATOM   725  C  CZ  . ARG A 1 116  ? 45.946 62.343  32.885  1.00 31.73 ? 116  ARG A CZ  1 
ATOM   726  N  NH1 . ARG A 1 116  ? 45.926 63.535  32.298  1.00 27.96 ? 116  ARG A NH1 1 
ATOM   727  N  NH2 . ARG A 1 116  ? 45.619 62.229  34.169  1.00 34.45 ? 116  ARG A NH2 1 
ATOM   728  N  N   . HIS A 1 117  ? 46.001 57.886  28.247  1.00 9.64  ? 117  HIS A N   1 
ATOM   729  C  CA  . HIS A 1 117  ? 44.924 57.021  28.724  1.00 11.71 ? 117  HIS A CA  1 
ATOM   730  C  C   . HIS A 1 117  ? 45.130 55.562  28.351  1.00 10.57 ? 117  HIS A C   1 
ATOM   731  O  O   . HIS A 1 117  ? 44.899 54.699  29.160  1.00 10.21 ? 117  HIS A O   1 
ATOM   732  C  CB  . HIS A 1 117  ? 43.525 57.516  28.270  1.00 12.08 ? 117  HIS A CB  1 
ATOM   733  C  CG  A HIS A 1 117  ? 43.164 58.595  29.243  0.50 20.15 ? 117  HIS A CG  1 
ATOM   734  C  CG  B HIS A 1 117  ? 42.515 57.173  29.231  0.50 21.12 ? 117  HIS A CG  1 
ATOM   735  N  ND1 A HIS A 1 117  ? 42.446 58.350  30.393  0.50 16.32 ? 117  HIS A ND1 1 
ATOM   736  N  ND1 B HIS A 1 117  ? 42.209 57.942  30.334  0.50 26.05 ? 117  HIS A ND1 1 
ATOM   737  C  CD2 A HIS A 1 117  ? 43.451 59.919  29.249  0.50 21.66 ? 117  HIS A CD2 1 
ATOM   738  C  CD2 B HIS A 1 117  ? 41.668 56.116  29.257  0.50 12.27 ? 117  HIS A CD2 1 
ATOM   739  C  CE1 A HIS A 1 117  ? 42.314 59.482  31.065  0.50 23.96 ? 117  HIS A CE1 1 
ATOM   740  C  CE1 B HIS A 1 117  ? 41.226 57.365  31.002  0.50 19.17 ? 117  HIS A CE1 1 
ATOM   741  N  NE2 A HIS A 1 117  ? 42.919 60.446  30.399  0.50 21.76 ? 117  HIS A NE2 1 
ATOM   742  N  NE2 B HIS A 1 117  ? 40.872 56.263  30.364  0.50 27.50 ? 117  HIS A NE2 1 
ATOM   743  N  N   . LEU A 1 118  ? 45.582 55.285  27.131  1.00 9.01  ? 118  LEU A N   1 
ATOM   744  C  CA  . LEU A 1 118  ? 45.810 53.903  26.721  1.00 8.59  ? 118  LEU A CA  1 
ATOM   745  C  C   . LEU A 1 118  ? 47.030 53.386  27.502  1.00 8.47  ? 118  LEU A C   1 
ATOM   746  O  O   . LEU A 1 118  ? 47.025 52.225  27.929  1.00 10.41 ? 118  LEU A O   1 
ATOM   747  C  CB  . LEU A 1 118  ? 46.037 53.803  25.162  1.00 9.06  ? 118  LEU A CB  1 
ATOM   748  C  CG  . LEU A 1 118  ? 44.754 54.266  24.409  1.00 14.63 ? 118  LEU A CG  1 
ATOM   749  C  CD1 . LEU A 1 118  ? 45.113 54.387  22.893  1.00 14.42 ? 118  LEU A CD1 1 
ATOM   750  C  CD2 . LEU A 1 118  ? 43.621 53.329  24.574  1.00 16.26 ? 118  LEU A CD2 1 
ATOM   751  N  N   . HIS A 1 119  ? 48.073 54.186  27.647  1.00 9.32  ? 119  HIS A N   1 
ATOM   752  C  CA  . HIS A 1 119  ? 49.249 53.728  28.438  1.00 10.13 ? 119  HIS A CA  1 
ATOM   753  C  C   . HIS A 1 119  ? 48.798 53.310  29.846  1.00 11.48 ? 119  HIS A C   1 
ATOM   754  O  O   . HIS A 1 119  ? 49.124 52.186  30.285  1.00 13.31 ? 119  HIS A O   1 
ATOM   755  C  CB  . HIS A 1 119  ? 50.245 54.888  28.557  1.00 12.14 ? 119  HIS A CB  1 
ATOM   756  C  CG  . HIS A 1 119  ? 51.420 54.594  29.421  1.00 17.51 ? 119  HIS A CG  1 
ATOM   757  N  ND1 . HIS A 1 119  ? 51.468 54.929  30.760  1.00 20.27 ? 119  HIS A ND1 1 
ATOM   758  C  CD2 . HIS A 1 119  ? 52.581 53.963  29.139  1.00 17.94 ? 119  HIS A CD2 1 
ATOM   759  C  CE1 . HIS A 1 119  ? 52.617 54.512  31.268  1.00 23.79 ? 119  HIS A CE1 1 
ATOM   760  N  NE2 . HIS A 1 119  ? 53.311 53.921  30.309  1.00 21.31 ? 119  HIS A NE2 1 
ATOM   761  N  N   . ASP A 1 120  ? 47.961 54.131  30.470  1.00 10.90 ? 120  ASP A N   1 
ATOM   762  C  CA  . ASP A 1 120  ? 47.555 53.847  31.864  1.00 12.85 ? 120  ASP A CA  1 
ATOM   763  C  C   . ASP A 1 120  ? 46.436 52.854  32.053  1.00 13.56 ? 120  ASP A C   1 
ATOM   764  O  O   . ASP A 1 120  ? 46.220 52.391  33.193  1.00 15.02 ? 120  ASP A O   1 
ATOM   765  C  CB  . ASP A 1 120  ? 47.123 55.174  32.495  1.00 14.10 ? 120  ASP A CB  1 
ATOM   766  C  CG  . ASP A 1 120  ? 48.273 56.121  32.758  1.00 16.49 ? 120  ASP A CG  1 
ATOM   767  O  OD1 . ASP A 1 120  ? 49.448 55.707  32.671  1.00 18.78 ? 120  ASP A OD1 1 
ATOM   768  O  OD2 . ASP A 1 120  ? 47.979 57.309  33.050  1.00 24.33 ? 120  ASP A OD2 1 
ATOM   769  N  N   . ASN A 1 121  ? 45.708 52.463  31.010  1.00 12.17 ? 121  ASN A N   1 
ATOM   770  C  CA  . ASN A 1 121  ? 44.535 51.581  31.097  1.00 10.72 ? 121  ASN A CA  1 
ATOM   771  C  C   . ASN A 1 121  ? 44.704 50.544  30.008  1.00 13.29 ? 121  ASN A C   1 
ATOM   772  O  O   . ASN A 1 121  ? 44.188 50.688  28.879  1.00 11.80 ? 121  ASN A O   1 
ATOM   773  C  CB  . ASN A 1 121  ? 43.206 52.362  30.868  1.00 11.95 ? 121  ASN A CB  1 
ATOM   774  C  CG  . ASN A 1 121  ? 43.034 53.447  31.923  1.00 12.06 ? 121  ASN A CG  1 
ATOM   775  O  OD1 . ASN A 1 121  ? 43.380 54.629  31.720  1.00 15.22 ? 121  ASN A OD1 1 
ATOM   776  N  ND2 . ASN A 1 121  ? 42.566 53.025  33.132  1.00 12.20 ? 121  ASN A ND2 1 
ATOM   777  N  N   . PRO A 1 122  ? 45.408 49.464  30.306  1.00 11.38 ? 122  PRO A N   1 
ATOM   778  C  CA  . PRO A 1 122  ? 45.701 48.414  29.329  1.00 11.64 ? 122  PRO A CA  1 
ATOM   779  C  C   . PRO A 1 122  ? 44.609 47.777  28.558  1.00 11.46 ? 122  PRO A C   1 
ATOM   780  O  O   . PRO A 1 122  ? 44.819 47.273  27.412  1.00 14.20 ? 122  PRO A O   1 
ATOM   781  C  CB  . PRO A 1 122  ? 46.511 47.383  30.135  1.00 12.83 ? 122  PRO A CB  1 
ATOM   782  C  CG  . PRO A 1 122  ? 47.096 48.209  31.253  1.00 16.33 ? 122  PRO A CG  1 
ATOM   783  C  CD  . PRO A 1 122  ? 45.984 49.154  31.649  1.00 13.66 ? 122  PRO A CD  1 
ATOM   784  N  N   . GLU A 1 123  ? 43.409 47.779  29.132  1.00 12.06 ? 123  GLU A N   1 
ATOM   785  C  CA  . GLU A 1 123  ? 42.256 47.213  28.478  1.00 12.55 ? 123  GLU A CA  1 
ATOM   786  C  C   . GLU A 1 123  ? 41.513 48.162  27.469  1.00 11.21 ? 123  GLU A C   1 
ATOM   787  O  O   . GLU A 1 123  ? 40.662 47.701  26.711  1.00 13.14 ? 123  GLU A O   1 
ATOM   788  C  CB  . GLU A 1 123  ? 41.262 46.787  29.573  1.00 16.39 ? 123  GLU A CB  1 
ATOM   789  C  CG  . GLU A 1 123  ? 40.400 47.928  30.106  1.00 18.42 ? 123  GLU A CG  1 
ATOM   790  C  CD  . GLU A 1 123  ? 41.060 48.952  31.063  1.00 14.75 ? 123  GLU A CD  1 
ATOM   791  O  OE1 . GLU A 1 123  ? 42.241 48.913  31.397  1.00 16.48 ? 123  GLU A OE1 1 
ATOM   792  O  OE2 . GLU A 1 123  ? 40.302 49.859  31.544  1.00 22.58 ? 123  GLU A OE2 1 
ATOM   793  N  N   . MET A 1 124  ? 41.835 49.447  27.539  1.00 10.75 ? 124  MET A N   1 
ATOM   794  C  CA  . MET A 1 124  ? 41.193 50.413  26.661  1.00 9.84  ? 124  MET A CA  1 
ATOM   795  C  C   . MET A 1 124  ? 41.799 50.273  25.251  1.00 10.33 ? 124  MET A C   1 
ATOM   796  O  O   . MET A 1 124  ? 42.946 49.949  25.083  1.00 9.32  ? 124  MET A O   1 
ATOM   797  C  CB  . MET A 1 124  ? 41.437 51.813  27.221  1.00 11.01 ? 124  MET A CB  1 
ATOM   798  C  CG  . MET A 1 124  ? 40.644 52.910  26.499  1.00 10.92 ? 124  MET A CG  1 
ATOM   799  S  SD  . MET A 1 124  ? 38.848 52.517  26.471  1.00 11.83 ? 124  MET A SD  1 
ATOM   800  C  CE  . MET A 1 124  ? 38.255 53.981  25.609  1.00 13.27 ? 124  MET A CE  1 
ATOM   801  N  N   . LYS A 1 125  ? 40.969 50.594  24.248  1.00 8.40  ? 125  LYS A N   1 
ATOM   802  C  CA  . LYS A 1 125  ? 41.339 50.486  22.838  1.00 8.51  ? 125  LYS A CA  1 
ATOM   803  C  C   . LYS A 1 125  ? 40.951 51.754  22.125  1.00 10.00 ? 125  LYS A C   1 
ATOM   804  O  O   . LYS A 1 125  ? 40.087 52.533  22.572  1.00 9.49  ? 125  LYS A O   1 
ATOM   805  C  CB  . LYS A 1 125  ? 40.597 49.338  22.182  1.00 10.50 ? 125  LYS A CB  1 
ATOM   806  C  CG  . LYS A 1 125  ? 40.736 47.941  22.825  1.00 15.49 ? 125  LYS A CG  1 
ATOM   807  C  CD  . LYS A 1 125  ? 42.110 47.450  22.567  1.00 17.55 ? 125  LYS A CD  1 
ATOM   808  C  CE  . LYS A 1 125  ? 42.457 46.046  23.167  1.00 27.06 ? 125  LYS A CE  1 
ATOM   809  N  NZ  . LYS A 1 125  ? 41.374 45.129  22.953  1.00 27.33 ? 125  LYS A NZ  1 
ATOM   810  N  N   . PHE A 1 126  ? 41.522 51.978  20.947  1.00 7.81  ? 126  PHE A N   1 
ATOM   811  C  CA  . PHE A 1 126  ? 41.235 53.201  20.148  1.00 7.18  ? 126  PHE A CA  1 
ATOM   812  C  C   . PHE A 1 126  ? 41.669 52.942  18.717  1.00 7.81  ? 126  PHE A C   1 
ATOM   813  O  O   . PHE A 1 126  ? 42.673 52.307  18.488  1.00 8.88  ? 126  PHE A O   1 
ATOM   814  C  CB  . PHE A 1 126  ? 42.054 54.372  20.713  1.00 9.48  ? 126  PHE A CB  1 
ATOM   815  C  CG  . PHE A 1 126  ? 41.653 55.753  20.250  1.00 7.20  ? 126  PHE A CG  1 
ATOM   816  C  CD1 . PHE A 1 126  ? 40.343 56.199  20.259  1.00 7.76  ? 126  PHE A CD1 1 
ATOM   817  C  CD2 . PHE A 1 126  ? 42.648 56.661  19.941  1.00 8.74  ? 126  PHE A CD2 1 
ATOM   818  C  CE1 . PHE A 1 126  ? 40.044 57.510  19.901  1.00 8.76  ? 126  PHE A CE1 1 
ATOM   819  C  CE2 . PHE A 1 126  ? 42.376 57.943  19.593  1.00 8.74  ? 126  PHE A CE2 1 
ATOM   820  C  CZ  . PHE A 1 126  ? 41.060 58.377  19.568  1.00 8.09  ? 126  PHE A CZ  1 
ATOM   821  N  N   . ILE A 1 127  ? 40.901 53.425  17.752  1.00 6.69  ? 127  ILE A N   1 
ATOM   822  C  CA  . ILE A 1 127  ? 41.361 53.294  16.341  1.00 6.48  ? 127  ILE A CA  1 
ATOM   823  C  C   . ILE A 1 127  ? 41.610 54.718  15.799  1.00 6.59  ? 127  ILE A C   1 
ATOM   824  O  O   . ILE A 1 127  ? 40.995 55.719  16.223  1.00 7.37  ? 127  ILE A O   1 
ATOM   825  C  CB  . ILE A 1 127  ? 40.359 52.574  15.421  1.00 6.50  ? 127  ILE A CB  1 
ATOM   826  C  CG1 . ILE A 1 127  ? 38.964 53.229  15.428  1.00 7.69  ? 127  ILE A CG1 1 
ATOM   827  C  CG2 . ILE A 1 127  ? 40.292 51.080  15.830  1.00 7.22  ? 127  ILE A CG2 1 
ATOM   828  C  CD1 . ILE A 1 127  ? 38.006 52.654  14.321  1.00 9.00  ? 127  ILE A CD1 1 
ATOM   829  N  N   . TRP A 1 128  ? 42.530 54.788  14.827  1.00 6.81  ? 128  TRP A N   1 
ATOM   830  C  CA  . TRP A 1 128  ? 42.959 56.080  14.231  1.00 6.63  ? 128  TRP A CA  1 
ATOM   831  C  C   . TRP A 1 128  ? 43.074 55.921  12.718  1.00 6.50  ? 128  TRP A C   1 
ATOM   832  O  O   . TRP A 1 128  ? 43.737 54.995  12.247  1.00 6.40  ? 128  TRP A O   1 
ATOM   833  C  CB  . TRP A 1 128  ? 44.297 56.529  14.815  1.00 7.13  ? 128  TRP A CB  1 
ATOM   834  C  CG  . TRP A 1 128  ? 44.564 57.977  14.463  1.00 7.00  ? 128  TRP A CG  1 
ATOM   835  C  CD1 . TRP A 1 128  ? 45.284 58.455  13.370  1.00 6.00  ? 128  TRP A CD1 1 
ATOM   836  C  CD2 . TRP A 1 128  ? 44.008 59.102  15.114  1.00 6.39  ? 128  TRP A CD2 1 
ATOM   837  N  NE1 . TRP A 1 128  ? 45.180 59.842  13.331  1.00 7.43  ? 128  TRP A NE1 1 
ATOM   838  C  CE2 . TRP A 1 128  ? 44.404 60.267  14.390  1.00 6.95  ? 128  TRP A CE2 1 
ATOM   839  C  CE3 . TRP A 1 128  ? 43.175 59.247  16.274  1.00 7.61  ? 128  TRP A CE3 1 
ATOM   840  C  CZ2 . TRP A 1 128  ? 44.023 61.548  14.780  1.00 7.39  ? 128  TRP A CZ2 1 
ATOM   841  C  CZ3 . TRP A 1 128  ? 42.806 60.504  16.639  1.00 7.64  ? 128  TRP A CZ3 1 
ATOM   842  C  CH2 . TRP A 1 128  ? 43.231 61.655  15.894  1.00 7.19  ? 128  TRP A CH2 1 
ATOM   843  N  N   . ALA A 1 129  ? 42.485 56.882  12.011  1.00 7.14  ? 129  ALA A N   1 
ATOM   844  C  CA  . ALA A 1 129  ? 42.497 56.810  10.541  1.00 7.63  ? 129  ALA A CA  1 
ATOM   845  C  C   . ALA A 1 129  ? 43.398 57.809  9.798   1.00 9.63  ? 129  ALA A C   1 
ATOM   846  O  O   . ALA A 1 129  ? 43.983 57.438  8.782   1.00 9.87  ? 129  ALA A O   1 
ATOM   847  C  CB  . ALA A 1 129  ? 41.087 57.077  10.035  1.00 9.12  ? 129  ALA A CB  1 
ATOM   848  N  N   . GLU A 1 130  ? 43.509 59.046  10.265  1.00 8.82  ? 130  GLU A N   1 
ATOM   849  C  CA  . GLU A 1 130  ? 44.118 60.110  9.447   1.00 8.46  ? 130  GLU A CA  1 
ATOM   850  C  C   . GLU A 1 130  ? 45.622 60.282  9.742   1.00 8.32  ? 130  GLU A C   1 
ATOM   851  O  O   . GLU A 1 130  ? 45.994 60.877  10.728  1.00 8.31  ? 130  GLU A O   1 
ATOM   852  C  CB  . GLU A 1 130  ? 43.369 61.431  9.672   1.00 9.60  ? 130  GLU A CB  1 
ATOM   853  C  CG  . GLU A 1 130  ? 41.842 61.363  9.372   1.00 8.96  ? 130  GLU A CG  1 
ATOM   854  C  CD  . GLU A 1 130  ? 41.000 60.915  10.561  1.00 11.16 ? 130  GLU A CD  1 
ATOM   855  O  OE1 . GLU A 1 130  ? 41.548 60.709  11.639  1.00 11.22 ? 130  GLU A OE1 1 
ATOM   856  O  OE2 . GLU A 1 130  ? 39.781 60.805  10.397  1.00 14.42 ? 130  GLU A OE2 1 
ATOM   857  N  N   . ILE A 1 131  ? 46.477 59.755  8.868   1.00 6.58  ? 131  ILE A N   1 
ATOM   858  C  CA  . ILE A 1 131  ? 47.893 59.763  9.171   1.00 6.76  ? 131  ILE A CA  1 
ATOM   859  C  C   . ILE A 1 131  ? 48.503 61.150  8.991   1.00 6.97  ? 131  ILE A C   1 
ATOM   860  O  O   . ILE A 1 131  ? 49.530 61.413  9.644   1.00 7.86  ? 131  ILE A O   1 
ATOM   861  C  CB  . ILE A 1 131  ? 48.614 58.642  8.356   1.00 7.57  ? 131  ILE A CB  1 
ATOM   862  C  CG1 . ILE A 1 131  ? 47.974 57.285  8.665   1.00 7.96  ? 131  ILE A CG1 1 
ATOM   863  C  CG2 . ILE A 1 131  ? 50.123 58.619  8.672   1.00 8.71  ? 131  ILE A CG2 1 
ATOM   864  C  CD1 . ILE A 1 131  ? 47.875 56.947  10.179  1.00 9.85  ? 131  ILE A CD1 1 
ATOM   865  N  N   . SER A 1 132  ? 47.926 62.052  8.205   1.00 5.96  ? 132  SER A N   1 
ATOM   866  C  CA  . SER A 1 132  ? 48.464 63.411  8.159   1.00 6.09  ? 132  SER A CA  1 
ATOM   867  C  C   . SER A 1 132  ? 48.554 63.999  9.589   1.00 7.31  ? 132  SER A C   1 
ATOM   868  O  O   . SER A 1 132  ? 49.613 64.553  9.936   1.00 7.26  ? 132  SER A O   1 
ATOM   869  C  CB  . SER A 1 132  ? 47.546 64.240  7.273   1.00 7.15  ? 132  SER A CB  1 
ATOM   870  O  OG  . SER A 1 132  ? 46.191 64.223  7.721   1.00 7.25  ? 132  SER A OG  1 
ATOM   871  N  N   . TYR A 1 133  ? 47.512 63.825  10.392  1.00 6.04  ? 133  TYR A N   1 
ATOM   872  C  CA  . TYR A 1 133  ? 47.567 64.320  11.769  1.00 6.75  ? 133  TYR A CA  1 
ATOM   873  C  C   . TYR A 1 133  ? 48.514 63.496  12.611  1.00 6.43  ? 133  TYR A C   1 
ATOM   874  O  O   . TYR A 1 133  ? 49.224 64.077  13.492  1.00 8.49  ? 133  TYR A O   1 
ATOM   875  C  CB  . TYR A 1 133  ? 46.205 64.226  12.439  1.00 7.05  ? 133  TYR A CB  1 
ATOM   876  C  CG  . TYR A 1 133  ? 45.287 65.388  12.063  1.00 5.66  ? 133  TYR A CG  1 
ATOM   877  C  CD1 . TYR A 1 133  ? 45.676 66.707  12.328  1.00 7.29  ? 133  TYR A CD1 1 
ATOM   878  C  CD2 . TYR A 1 133  ? 44.035 65.160  11.525  1.00 5.86  ? 133  TYR A CD2 1 
ATOM   879  C  CE1 . TYR A 1 133  ? 44.840 67.819  12.060  1.00 8.71  ? 133  TYR A CE1 1 
ATOM   880  C  CE2 . TYR A 1 133  ? 43.160 66.226  11.245  1.00 6.85  ? 133  TYR A CE2 1 
ATOM   881  C  CZ  . TYR A 1 133  ? 43.579 67.561  11.510  1.00 8.23  ? 133  TYR A CZ  1 
ATOM   882  O  OH  . TYR A 1 133  ? 42.774 68.655  11.200  1.00 8.37  ? 133  TYR A OH  1 
ATOM   883  N  N   . PHE A 1 134  ? 48.490 62.171  12.483  1.00 6.50  ? 134  PHE A N   1 
ATOM   884  C  CA  . PHE A 1 134  ? 49.311 61.342  13.366  1.00 6.95  ? 134  PHE A CA  1 
ATOM   885  C  C   . PHE A 1 134  ? 50.789 61.645  13.137  1.00 8.60  ? 134  PHE A C   1 
ATOM   886  O  O   . PHE A 1 134  ? 51.586 61.733  14.119  1.00 8.88  ? 134  PHE A O   1 
ATOM   887  C  CB  . PHE A 1 134  ? 49.046 59.882  13.144  1.00 7.05  ? 134  PHE A CB  1 
ATOM   888  C  CG  . PHE A 1 134  ? 49.585 59.027  14.257  1.00 8.68  ? 134  PHE A CG  1 
ATOM   889  C  CD1 . PHE A 1 134  ? 48.826 58.836  15.440  1.00 8.71  ? 134  PHE A CD1 1 
ATOM   890  C  CD2 . PHE A 1 134  ? 50.845 58.516  14.153  1.00 10.36 ? 134  PHE A CD2 1 
ATOM   891  C  CE1 . PHE A 1 134  ? 49.412 58.108  16.520  1.00 9.97  ? 134  PHE A CE1 1 
ATOM   892  C  CE2 . PHE A 1 134  ? 51.421 57.807  15.222  1.00 11.01 ? 134  PHE A CE2 1 
ATOM   893  C  CZ  . PHE A 1 134  ? 50.691 57.620  16.395  1.00 11.07 ? 134  PHE A CZ  1 
ATOM   894  N  N   . ALA A 1 135  ? 51.197 61.773  11.880  1.00 9.06  ? 135  ALA A N   1 
ATOM   895  C  CA  . ALA A 1 135  ? 52.581 62.143  11.542  1.00 9.19  ? 135  ALA A CA  1 
ATOM   896  C  C   . ALA A 1 135  ? 52.954 63.538  12.103  1.00 9.38  ? 135  ALA A C   1 
ATOM   897  O  O   . ALA A 1 135  ? 54.058 63.730  12.627  1.00 13.41 ? 135  ALA A O   1 
ATOM   898  C  CB  . ALA A 1 135  ? 52.792 62.087  10.034  1.00 10.52 ? 135  ALA A CB  1 
ATOM   899  N  N   . ARG A 1 136  ? 52.038 64.491  12.013  1.00 9.79  ? 136  ARG A N   1 
ATOM   900  C  CA  . ARG A 1 136  ? 52.267 65.876  12.522  1.00 11.41 ? 136  ARG A CA  1 
ATOM   901  C  C   . ARG A 1 136  ? 52.459 65.814  14.057  1.00 14.40 ? 136  ARG A C   1 
ATOM   902  O  O   . ARG A 1 136  ? 53.247 66.616  14.598  1.00 16.74 ? 136  ARG A O   1 
ATOM   903  C  CB  . ARG A 1 136  ? 51.070 66.760  12.218  1.00 12.64 ? 136  ARG A CB  1 
ATOM   904  C  CG  . ARG A 1 136  ? 51.067 68.169  12.914  1.00 14.10 ? 136  ARG A CG  1 
ATOM   905  C  CD  . ARG A 1 136  ? 51.784 69.231  12.037  1.00 14.54 ? 136  ARG A CD  1 
ATOM   906  N  NE  . ARG A 1 136  ? 51.782 70.551  12.690  1.00 14.30 ? 136  ARG A NE  1 
ATOM   907  C  CZ  . ARG A 1 136  ? 52.551 70.810  13.739  1.00 15.05 ? 136  ARG A CZ  1 
ATOM   908  N  NH1 . ARG A 1 136  ? 53.388 69.856  14.209  1.00 16.70 ? 136  ARG A NH1 1 
ATOM   909  N  NH2 . ARG A 1 136  ? 52.429 71.992  14.346  1.00 13.29 ? 136  ARG A NH2 1 
ATOM   910  N  N   . PHE A 1 137  ? 51.779 64.894  14.740  1.00 9.97  ? 137  PHE A N   1 
ATOM   911  C  CA  . PHE A 1 137  ? 51.875 64.728  16.195  1.00 9.88  ? 137  PHE A CA  1 
ATOM   912  C  C   . PHE A 1 137  ? 53.153 63.998  16.595  1.00 9.96  ? 137  PHE A C   1 
ATOM   913  O  O   . PHE A 1 137  ? 53.889 64.447  17.463  1.00 12.14 ? 137  PHE A O   1 
ATOM   914  C  CB  . PHE A 1 137  ? 50.671 63.934  16.704  1.00 8.76  ? 137  PHE A CB  1 
ATOM   915  C  CG  . PHE A 1 137  ? 50.669 63.714  18.192  1.00 10.49 ? 137  PHE A CG  1 
ATOM   916  C  CD1 . PHE A 1 137  ? 50.349 64.741  19.063  1.00 10.99 ? 137  PHE A CD1 1 
ATOM   917  C  CD2 . PHE A 1 137  ? 50.936 62.468  18.709  1.00 11.01 ? 137  PHE A CD2 1 
ATOM   918  C  CE1 . PHE A 1 137  ? 50.336 64.539  20.406  1.00 14.25 ? 137  PHE A CE1 1 
ATOM   919  C  CE2 . PHE A 1 137  ? 50.938 62.264  20.073  1.00 12.69 ? 137  PHE A CE2 1 
ATOM   920  C  CZ  . PHE A 1 137  ? 50.637 63.307  20.913  1.00 11.29 ? 137  PHE A CZ  1 
ATOM   921  N  N   . TYR A 1 138  ? 53.367 62.843  15.984  1.00 10.53 ? 138  TYR A N   1 
ATOM   922  C  CA  . TYR A 1 138  ? 54.473 61.963  16.323  1.00 12.85 ? 138  TYR A CA  1 
ATOM   923  C  C   . TYR A 1 138  ? 55.806 62.645  16.144  1.00 15.29 ? 138  TYR A C   1 
ATOM   924  O  O   . TYR A 1 138  ? 56.691 62.486  17.006  1.00 13.98 ? 138  TYR A O   1 
ATOM   925  C  CB  . TYR A 1 138  ? 54.443 60.682  15.466  1.00 12.94 ? 138  TYR A CB  1 
ATOM   926  C  CG  . TYR A 1 138  ? 55.458 59.659  15.853  1.00 13.72 ? 138  TYR A CG  1 
ATOM   927  C  CD1 . TYR A 1 138  ? 55.171 58.767  16.869  1.00 13.17 ? 138  TYR A CD1 1 
ATOM   928  C  CD2 . TYR A 1 138  ? 56.672 59.576  15.178  1.00 14.44 ? 138  TYR A CD2 1 
ATOM   929  C  CE1 . TYR A 1 138  ? 56.063 57.786  17.228  1.00 15.70 ? 138  TYR A CE1 1 
ATOM   930  C  CE2 . TYR A 1 138  ? 57.624 58.564  15.539  1.00 12.44 ? 138  TYR A CE2 1 
ATOM   931  C  CZ  . TYR A 1 138  ? 57.268 57.695  16.565  1.00 11.99 ? 138  TYR A CZ  1 
ATOM   932  O  OH  . TYR A 1 138  ? 58.157 56.693  16.940  1.00 16.94 ? 138  TYR A OH  1 
ATOM   933  N  N   . HIS A 1 139  ? 55.976 63.403  15.074  1.00 14.50 ? 139  HIS A N   1 
ATOM   934  C  CA  . HIS A 1 139  ? 57.249 64.054  14.866  1.00 18.70 ? 139  HIS A CA  1 
ATOM   935  C  C   . HIS A 1 139  ? 57.542 65.102  15.941  1.00 22.39 ? 139  HIS A C   1 
ATOM   936  O  O   . HIS A 1 139  ? 58.737 65.385  16.190  1.00 24.24 ? 139  HIS A O   1 
ATOM   937  C  CB  . HIS A 1 139  ? 57.347 64.593  13.429  1.00 18.31 ? 139  HIS A CB  1 
ATOM   938  C  CG  . HIS A 1 139  ? 57.605 63.509  12.405  1.00 22.94 ? 139  HIS A CG  1 
ATOM   939  N  ND1 . HIS A 1 139  ? 58.737 62.710  12.433  1.00 26.50 ? 139  HIS A ND1 1 
ATOM   940  C  CD2 . HIS A 1 139  ? 56.905 63.130  11.296  1.00 24.99 ? 139  HIS A CD2 1 
ATOM   941  C  CE1 . HIS A 1 139  ? 58.730 61.905  11.374  1.00 29.41 ? 139  HIS A CE1 1 
ATOM   942  N  NE2 . HIS A 1 139  ? 57.639 62.148  10.662  1.00 22.78 ? 139  HIS A NE2 1 
ATOM   943  N  N   . ASP A 1 140  ? 56.520 65.656  16.599  1.00 15.97 ? 140  ASP A N   1 
ATOM   944  C  CA  . ASP A 1 140  ? 56.720 66.650  17.672  1.00 16.85 ? 140  ASP A CA  1 
ATOM   945  C  C   . ASP A 1 140  ? 56.894 66.020  19.070  1.00 13.98 ? 140  ASP A C   1 
ATOM   946  O  O   . ASP A 1 140  ? 57.223 66.734  20.046  1.00 16.60 ? 140  ASP A O   1 
ATOM   947  C  CB  . ASP A 1 140  ? 55.576 67.626  17.738  1.00 18.69 ? 140  ASP A CB  1 
ATOM   948  C  CG  . ASP A 1 140  ? 55.689 68.709  16.665  1.00 23.99 ? 140  ASP A CG  1 
ATOM   949  O  OD1 . ASP A 1 140  ? 56.554 68.545  15.777  1.00 26.25 ? 140  ASP A OD1 1 
ATOM   950  O  OD2 . ASP A 1 140  ? 54.931 69.702  16.738  1.00 23.76 ? 140  ASP A OD2 1 
ATOM   951  N  N   . LEU A 1 141  ? 56.727 64.713  19.192  1.00 12.85 ? 141  LEU A N   1 
ATOM   952  C  CA  . LEU A 1 141  ? 56.894 64.028  20.465  1.00 12.56 ? 141  LEU A CA  1 
ATOM   953  C  C   . LEU A 1 141  ? 58.336 63.820  20.829  1.00 13.54 ? 141  LEU A C   1 
ATOM   954  O  O   . LEU A 1 141  ? 59.168 63.552  19.987  1.00 14.79 ? 141  LEU A O   1 
ATOM   955  C  CB  . LEU A 1 141  ? 56.313 62.597  20.409  1.00 14.49 ? 141  LEU A CB  1 
ATOM   956  C  CG  . LEU A 1 141  ? 54.816 62.420  20.485  1.00 16.89 ? 141  LEU A CG  1 
ATOM   957  C  CD1 . LEU A 1 141  ? 54.518 60.907  20.434  1.00 12.44 ? 141  LEU A CD1 1 
ATOM   958  C  CD2 . LEU A 1 141  ? 54.249 63.055  21.783  1.00 14.42 ? 141  LEU A CD2 1 
ATOM   959  N  N   . GLY A 1 142  ? 58.618 63.895  22.127  1.00 14.92 ? 142  GLY A N   1 
ATOM   960  C  CA  . GLY A 1 142  ? 59.948 63.559  22.586  1.00 14.77 ? 142  GLY A CA  1 
ATOM   961  C  C   . GLY A 1 142  ? 60.125 62.034  22.471  1.00 14.73 ? 142  GLY A C   1 
ATOM   962  O  O   . GLY A 1 142  ? 59.131 61.266  22.341  1.00 15.77 ? 142  GLY A O   1 
ATOM   963  N  N   . GLU A 1 143  ? 61.368 61.580  22.506  1.00 15.00 ? 143  GLU A N   1 
ATOM   964  C  CA  . GLU A 1 143  ? 61.700 60.174  22.346  1.00 15.67 ? 143  GLU A CA  1 
ATOM   965  C  C   . GLU A 1 143  ? 61.024 59.274  23.382  1.00 14.23 ? 143  GLU A C   1 
ATOM   966  O  O   . GLU A 1 143  ? 60.567 58.178  23.028  1.00 14.38 ? 143  GLU A O   1 
ATOM   967  C  CB  . GLU A 1 143  ? 63.230 59.979  22.358  1.00 19.79 ? 143  GLU A CB  1 
ATOM   968  C  CG  . GLU A 1 143  ? 63.697 58.622  21.856  1.00 21.83 ? 143  GLU A CG  1 
ATOM   969  C  CD  . GLU A 1 143  ? 63.451 58.376  20.342  1.00 27.87 ? 143  GLU A CD  1 
ATOM   970  O  OE1 . GLU A 1 143  ? 63.185 59.320  19.555  1.00 30.29 ? 143  GLU A OE1 1 
ATOM   971  O  OE2 . GLU A 1 143  ? 63.556 57.204  19.933  1.00 36.48 ? 143  GLU A OE2 1 
ATOM   972  N  N   . ASN A 1 144  ? 60.919 59.690  24.625  1.00 15.38 ? 144  ASN A N   1 
ATOM   973  C  CA  . ASN A 1 144  ? 60.274 58.826  25.620  1.00 15.44 ? 144  ASN A CA  1 
ATOM   974  C  C   . ASN A 1 144  ? 58.826 58.514  25.210  1.00 15.23 ? 144  ASN A C   1 
ATOM   975  O  O   . ASN A 1 144  ? 58.400 57.367  25.234  1.00 14.52 ? 144  ASN A O   1 
ATOM   976  C  CB  . ASN A 1 144  ? 60.334 59.517  27.008  1.00 17.19 ? 144  ASN A CB  1 
ATOM   977  C  CG  . ASN A 1 144  ? 59.552 58.772  28.090  1.00 28.53 ? 144  ASN A CG  1 
ATOM   978  O  OD1 . ASN A 1 144  ? 58.301 58.769  28.125  1.00 30.75 ? 144  ASN A OD1 1 
ATOM   979  N  ND2 . ASN A 1 144  ? 60.293 58.118  28.984  1.00 29.70 ? 144  ASN A ND2 1 
ATOM   980  N  N   . LYS A 1 145  ? 58.108 59.544  24.782  1.00 14.42 ? 145  LYS A N   1 
ATOM   981  C  CA  . LYS A 1 145  ? 56.723 59.390  24.354  1.00 12.64 ? 145  LYS A CA  1 
ATOM   982  C  C   . LYS A 1 145  ? 56.603 58.647  23.016  1.00 11.68 ? 145  LYS A C   1 
ATOM   983  O  O   . LYS A 1 145  ? 55.628 57.920  22.829  1.00 12.95 ? 145  LYS A O   1 
ATOM   984  C  CB  . LYS A 1 145  ? 56.043 60.767  24.293  1.00 15.25 ? 145  LYS A CB  1 
ATOM   985  C  CG  . LYS A 1 145  ? 55.762 61.395  25.723  1.00 17.87 ? 145  LYS A CG  1 
ATOM   986  C  CD  . LYS A 1 145  ? 54.900 60.532  26.639  1.00 26.02 ? 145  LYS A CD  1 
ATOM   987  C  CE  . LYS A 1 145  ? 54.643 61.293  27.976  1.00 29.53 ? 145  LYS A CE  1 
ATOM   988  N  NZ  . LYS A 1 145  ? 55.886 61.823  28.610  1.00 38.04 ? 145  LYS A NZ  1 
ATOM   989  N  N   . LYS A 1 146  ? 57.558 58.852  22.103  1.00 11.95 ? 146  LYS A N   1 
ATOM   990  C  CA  . LYS A 1 146  ? 57.541 58.086  20.838  1.00 11.73 ? 146  LYS A CA  1 
ATOM   991  C  C   . LYS A 1 146  ? 57.599 56.615  21.183  1.00 10.79 ? 146  LYS A C   1 
ATOM   992  O  O   . LYS A 1 146  ? 56.873 55.797  20.601  1.00 12.15 ? 146  LYS A O   1 
ATOM   993  C  CB  . LYS A 1 146  ? 58.743 58.413  19.928  1.00 13.15 ? 146  LYS A CB  1 
ATOM   994  C  CG  . LYS A 1 146  ? 58.655 59.744  19.187  1.00 12.21 ? 146  LYS A CG  1 
ATOM   995  C  CD  . LYS A 1 146  ? 59.835 59.891  18.205  1.00 11.87 ? 146  LYS A CD  1 
ATOM   996  C  CE  A LYS A 1 146  ? 59.680 61.088  17.287  0.50 14.43 ? 146  LYS A CE  1 
ATOM   997  C  CE  B LYS A 1 146  ? 59.742 60.918  17.161  0.50 13.64 ? 146  LYS A CE  1 
ATOM   998  N  NZ  A LYS A 1 146  ? 60.914 61.342  16.495  0.50 29.81 ? 146  LYS A NZ  1 
ATOM   999  N  NZ  B LYS A 1 146  ? 59.914 62.277  17.762  0.50 21.89 ? 146  LYS A NZ  1 
ATOM   1000 N  N   . LEU A 1 147  ? 58.466 56.234  22.129  1.00 13.13 ? 147  LEU A N   1 
ATOM   1001 C  CA  . LEU A 1 147  ? 58.599 54.845  22.534  1.00 12.32 ? 147  LEU A CA  1 
ATOM   1002 C  C   . LEU A 1 147  ? 57.309 54.346  23.218  1.00 11.88 ? 147  LEU A C   1 
ATOM   1003 O  O   . LEU A 1 147  ? 56.867 53.211  22.954  1.00 12.60 ? 147  LEU A O   1 
ATOM   1004 C  CB  . LEU A 1 147  ? 59.804 54.693  23.477  1.00 14.19 ? 147  LEU A CB  1 
ATOM   1005 C  CG  . LEU A 1 147  ? 61.145 54.856  22.760  1.00 16.85 ? 147  LEU A CG  1 
ATOM   1006 C  CD1 . LEU A 1 147  ? 62.279 54.839  23.786  1.00 21.24 ? 147  LEU A CD1 1 
ATOM   1007 C  CD2 . LEU A 1 147  ? 61.341 53.700  21.789  1.00 22.50 ? 147  LEU A CD2 1 
ATOM   1008 N  N   . GLN A 1 148  ? 56.684 55.165  24.049  1.00 12.11 ? 148  GLN A N   1 
ATOM   1009 C  CA  . GLN A 1 148  ? 55.407 54.768  24.622  1.00 11.68 ? 148  GLN A CA  1 
ATOM   1010 C  C   . GLN A 1 148  ? 54.329 54.541  23.541  1.00 10.51 ? 148  GLN A C   1 
ATOM   1011 O  O   . GLN A 1 148  ? 53.574 53.597  23.614  1.00 11.46 ? 148  GLN A O   1 
ATOM   1012 C  CB  . GLN A 1 148  ? 54.903 55.790  25.627  1.00 13.02 ? 148  GLN A CB  1 
ATOM   1013 C  CG  . GLN A 1 148  ? 55.690 55.895  26.913  1.00 14.59 ? 148  GLN A CG  1 
ATOM   1014 C  CD  . GLN A 1 148  ? 54.956 56.738  27.921  1.00 20.73 ? 148  GLN A CD  1 
ATOM   1015 O  OE1 . GLN A 1 148  ? 53.933 57.319  27.613  1.00 27.27 ? 148  GLN A OE1 1 
ATOM   1016 N  NE2 . GLN A 1 148  ? 55.477 56.800  29.132  1.00 20.87 ? 148  GLN A NE2 1 
ATOM   1017 N  N   . MET A 1 149  ? 54.305 55.409  22.537  1.00 10.65 ? 149  MET A N   1 
ATOM   1018 C  CA  . MET A 1 149  ? 53.330 55.312  21.454  1.00 9.65  ? 149  MET A CA  1 
ATOM   1019 C  C   . MET A 1 149  ? 53.568 54.025  20.651  1.00 9.54  ? 149  MET A C   1 
ATOM   1020 O  O   . MET A 1 149  ? 52.625 53.281  20.316  1.00 10.85 ? 149  MET A O   1 
ATOM   1021 C  CB  . MET A 1 149  ? 53.454 56.541  20.547  1.00 10.59 ? 149  MET A CB  1 
ATOM   1022 C  CG  . MET A 1 149  ? 52.437 56.550  19.396  1.00 10.88 ? 149  MET A CG  1 
ATOM   1023 S  SD  . MET A 1 149  ? 50.764 56.757  19.988  1.00 13.77 ? 149  MET A SD  1 
ATOM   1024 C  CE  . MET A 1 149  ? 50.626 58.505  20.133  1.00 20.83 ? 149  MET A CE  1 
ATOM   1025 N  N   . LYS A 1 150  ? 54.842 53.752  20.327  1.00 10.53 ? 150  LYS A N   1 
ATOM   1026 C  CA  . LYS A 1 150  ? 55.128 52.546  19.572  1.00 12.18 ? 150  LYS A CA  1 
ATOM   1027 C  C   . LYS A 1 150  ? 54.663 51.305  20.363  1.00 11.19 ? 150  LYS A C   1 
ATOM   1028 O  O   . LYS A 1 150  ? 54.178 50.323  19.782  1.00 13.43 ? 150  LYS A O   1 
ATOM   1029 C  CB  . LYS A 1 150  ? 56.637 52.464  19.241  1.00 12.36 ? 150  LYS A CB  1 
ATOM   1030 C  CG  . LYS A 1 150  ? 57.089 53.394  18.167  1.00 14.72 ? 150  LYS A CG  1 
ATOM   1031 C  CD  . LYS A 1 150  ? 58.627 53.373  17.930  1.00 19.63 ? 150  LYS A CD  1 
ATOM   1032 C  CE  . LYS A 1 150  ? 59.070 52.019  17.446  1.00 30.89 ? 150  LYS A CE  1 
ATOM   1033 N  NZ  . LYS A 1 150  ? 60.093 52.219  16.379  1.00 36.84 ? 150  LYS A NZ  1 
ATOM   1034 N  N   . SER A 1 151  ? 54.783 51.334  21.690  1.00 11.66 ? 151  SER A N   1 
ATOM   1035 C  CA  . SER A 1 151  ? 54.398 50.202  22.507  1.00 12.85 ? 151  SER A CA  1 
ATOM   1036 C  C   . SER A 1 151  ? 52.865 49.973  22.530  1.00 10.06 ? 151  SER A C   1 
ATOM   1037 O  O   . SER A 1 151  ? 52.414 48.828  22.503  1.00 11.93 ? 151  SER A O   1 
ATOM   1038 C  CB  . SER A 1 151  ? 54.968 50.368  23.932  1.00 14.58 ? 151  SER A CB  1 
ATOM   1039 O  OG  A SER A 1 151  ? 54.170 51.230  24.721  0.50 29.04 ? 151  SER A OG  1 
ATOM   1040 O  OG  B SER A 1 151  ? 54.665 49.204  24.664  0.50 20.95 ? 151  SER A OG  1 
ATOM   1041 N  N   . ILE A 1 152  ? 52.057 51.034  22.598  1.00 10.19 ? 152  ILE A N   1 
ATOM   1042 C  CA  . ILE A 1 152  ? 50.622 50.818  22.581  1.00 9.70  ? 152  ILE A CA  1 
ATOM   1043 C  C   . ILE A 1 152  ? 50.108 50.425  21.192  1.00 9.19  ? 152  ILE A C   1 
ATOM   1044 O  O   . ILE A 1 152  ? 49.042 49.837  21.103  1.00 10.95 ? 152  ILE A O   1 
ATOM   1045 C  CB  . ILE A 1 152  ? 49.776 52.002  23.158  1.00 11.27 ? 152  ILE A CB  1 
ATOM   1046 C  CG1 . ILE A 1 152  ? 50.011 53.300  22.402  1.00 11.06 ? 152  ILE A CG1 1 
ATOM   1047 C  CG2 . ILE A 1 152  ? 50.064 52.144  24.690  1.00 12.03 ? 152  ILE A CG2 1 
ATOM   1048 C  CD1 . ILE A 1 152  ? 48.947 54.405  22.740  1.00 11.76 ? 152  ILE A CD1 1 
ATOM   1049 N  N   . VAL A 1 153  ? 50.879 50.712  20.130  1.00 10.07 ? 153  VAL A N   1 
ATOM   1050 C  CA  . VAL A 1 153  ? 50.515 50.212  18.789  1.00 9.73  ? 153  VAL A CA  1 
ATOM   1051 C  C   . VAL A 1 153  ? 50.951 48.748  18.697  1.00 11.47 ? 153  VAL A C   1 
ATOM   1052 O  O   . VAL A 1 153  ? 50.167 47.862  18.270  1.00 11.91 ? 153  VAL A O   1 
ATOM   1053 C  CB  . VAL A 1 153  ? 51.195 51.084  17.735  1.00 9.47  ? 153  VAL A CB  1 
ATOM   1054 C  CG1 . VAL A 1 153  ? 51.086 50.408  16.343  1.00 12.12 ? 153  VAL A CG1 1 
ATOM   1055 C  CG2 . VAL A 1 153  ? 50.598 52.474  17.769  1.00 10.12 ? 153  VAL A CG2 1 
ATOM   1056 N  N   . LYS A 1 154  ? 52.159 48.452  19.151  1.00 12.37 ? 154  LYS A N   1 
ATOM   1057 C  CA  . LYS A 1 154  ? 52.668 47.092  19.062  1.00 14.29 ? 154  LYS A CA  1 
ATOM   1058 C  C   . LYS A 1 154  ? 51.797 46.086  19.815  1.00 14.87 ? 154  LYS A C   1 
ATOM   1059 O  O   . LYS A 1 154  ? 51.605 44.968  19.350  1.00 16.80 ? 154  LYS A O   1 
ATOM   1060 C  CB  . LYS A 1 154  ? 54.113 47.034  19.556  1.00 14.14 ? 154  LYS A CB  1 
ATOM   1061 C  CG  . LYS A 1 154  ? 54.789 45.696  19.337  1.00 22.12 ? 154  LYS A CG  1 
ATOM   1062 C  CD  . LYS A 1 154  ? 56.280 45.799  19.607  1.00 23.84 ? 154  LYS A CD  1 
ATOM   1063 C  CE  . LYS A 1 154  ? 57.000 44.558  19.122  1.00 29.58 ? 154  LYS A CE  1 
ATOM   1064 N  NZ  . LYS A 1 154  ? 57.549 44.741  17.751  1.00 32.07 ? 154  LYS A NZ  1 
ATOM   1065 N  N   . ASN A 1 155  ? 51.241 46.491  20.951  1.00 13.15 ? 155  ASN A N   1 
ATOM   1066 C  CA  . ASN A 1 155  ? 50.485 45.595  21.819  1.00 13.99 ? 155  ASN A CA  1 
ATOM   1067 C  C   . ASN A 1 155  ? 48.971 45.608  21.551  1.00 15.22 ? 155  ASN A C   1 
ATOM   1068 O  O   . ASN A 1 155  ? 48.207 44.974  22.258  1.00 16.93 ? 155  ASN A O   1 
ATOM   1069 C  CB  A ASN A 1 155  ? 50.528 45.976  23.370  0.50 21.47 ? 155  ASN A CB  1 
ATOM   1070 C  CB  B ASN A 1 155  ? 51.170 45.845  23.167  0.50 23.69 ? 155  ASN A CB  1 
ATOM   1071 C  CG  A ASN A 1 155  ? 49.866 47.325  23.713  0.50 23.45 ? 155  ASN A CG  1 
ATOM   1072 C  CG  B ASN A 1 155  ? 52.594 45.273  23.226  0.50 26.46 ? 155  ASN A CG  1 
ATOM   1073 O  OD1 A ASN A 1 155  ? 49.337 48.004  22.843  0.50 24.45 ? 155  ASN A OD1 1 
ATOM   1074 O  OD1 B ASN A 1 155  ? 52.933 44.354  22.480  0.50 28.54 ? 155  ASN A OD1 1 
ATOM   1075 N  ND2 A ASN A 1 155  ? 49.918 47.714  24.988  0.50 17.91 ? 155  ASN A ND2 1 
ATOM   1076 N  ND2 B ASN A 1 155  ? 53.430 45.819  24.116  0.50 27.66 ? 155  ASN A ND2 1 
ATOM   1077 N  N   . GLY A 1 156  ? 48.563 46.339  20.536  1.00 12.94 ? 156  GLY A N   1 
ATOM   1078 C  CA  . GLY A 1 156  ? 47.224 46.195  19.992  1.00 13.74 ? 156  GLY A CA  1 
ATOM   1079 C  C   . GLY A 1 156  ? 46.191 47.156  20.558  1.00 12.90 ? 156  GLY A C   1 
ATOM   1080 O  O   . GLY A 1 156  ? 45.030 47.096  20.182  1.00 14.90 ? 156  GLY A O   1 
ATOM   1081 N  N   . GLN A 1 157  ? 46.606 48.046  21.450  1.00 9.64  ? 157  GLN A N   1 
ATOM   1082 C  CA  . GLN A 1 157  ? 45.694 48.996  22.076  1.00 10.02 ? 157  GLN A CA  1 
ATOM   1083 C  C   . GLN A 1 157  ? 45.265 50.079  21.092  1.00 8.94  ? 157  GLN A C   1 
ATOM   1084 O  O   . GLN A 1 157  ? 44.073 50.302  20.880  1.00 9.33  ? 157  GLN A O   1 
ATOM   1085 C  CB  . GLN A 1 157  ? 46.344 49.631  23.307  1.00 9.02  ? 157  GLN A CB  1 
ATOM   1086 C  CG  . GLN A 1 157  ? 46.262 48.777  24.562  1.00 9.67  ? 157  GLN A CG  1 
ATOM   1087 C  CD  . GLN A 1 157  ? 46.629 49.547  25.815  1.00 8.53  ? 157  GLN A CD  1 
ATOM   1088 O  OE1 . GLN A 1 157  ? 47.781 49.537  26.250  1.00 12.27 ? 157  GLN A OE1 1 
ATOM   1089 N  NE2 . GLN A 1 157  ? 45.648 50.222  26.404  1.00 8.43  ? 157  GLN A NE2 1 
ATOM   1090 N  N   . LEU A 1 158  ? 46.219 50.753  20.453  1.00 8.93  ? 158  LEU A N   1 
ATOM   1091 C  CA  . LEU A 1 158  ? 45.947 51.739  19.389  1.00 8.43  ? 158  LEU A CA  1 
ATOM   1092 C  C   . LEU A 1 158  ? 46.165 51.073  18.054  1.00 9.63  ? 158  LEU A C   1 
ATOM   1093 O  O   . LEU A 1 158  ? 47.223 50.562  17.757  1.00 10.09 ? 158  LEU A O   1 
ATOM   1094 C  CB  A LEU A 1 158  ? 46.886 52.939  19.545  0.50 9.27  ? 158  LEU A CB  1 
ATOM   1095 C  CB  B LEU A 1 158  ? 46.883 52.913  19.595  0.50 9.45  ? 158  LEU A CB  1 
ATOM   1096 C  CG  A LEU A 1 158  ? 46.789 54.190  18.658  0.50 15.88 ? 158  LEU A CG  1 
ATOM   1097 C  CG  B LEU A 1 158  ? 46.938 53.939  18.474  0.50 16.65 ? 158  LEU A CG  1 
ATOM   1098 C  CD1 A LEU A 1 158  ? 48.065 55.004  18.853  0.50 15.72 ? 158  LEU A CD1 1 
ATOM   1099 C  CD1 B LEU A 1 158  ? 45.629 54.593  18.365  0.50 16.15 ? 158  LEU A CD1 1 
ATOM   1100 C  CD2 A LEU A 1 158  ? 46.672 53.905  17.217  0.50 21.77 ? 158  LEU A CD2 1 
ATOM   1101 C  CD2 B LEU A 1 158  ? 48.065 54.951  18.742  0.50 15.81 ? 158  LEU A CD2 1 
ATOM   1102 N  N   . GLU A 1 159  ? 45.114 51.062  17.260  1.00 7.94  ? 159  GLU A N   1 
ATOM   1103 C  CA  . GLU A 1 159  ? 45.141 50.392  15.966  1.00 8.48  ? 159  GLU A CA  1 
ATOM   1104 C  C   . GLU A 1 159  ? 44.841 51.368  14.833  1.00 7.41  ? 159  GLU A C   1 
ATOM   1105 O  O   . GLU A 1 159  ? 43.910 52.169  14.921  1.00 8.47  ? 159  GLU A O   1 
ATOM   1106 C  CB  . GLU A 1 159  ? 44.140 49.235  15.941  1.00 10.59 ? 159  GLU A CB  1 
ATOM   1107 C  CG  . GLU A 1 159  ? 44.061 48.512  14.606  1.00 10.82 ? 159  GLU A CG  1 
ATOM   1108 C  CD  . GLU A 1 159  ? 43.077 47.358  14.626  1.00 12.82 ? 159  GLU A CD  1 
ATOM   1109 O  OE1 . GLU A 1 159  ? 43.370 46.337  15.284  1.00 13.71 ? 159  GLU A OE1 1 
ATOM   1110 O  OE2 . GLU A 1 159  ? 42.012 47.471  13.984  1.00 11.18 ? 159  GLU A OE2 1 
ATOM   1111 N  N   . PHE A 1 160  ? 45.636 51.297  13.771  1.00 7.43  ? 160  PHE A N   1 
ATOM   1112 C  CA  . PHE A 1 160  ? 45.463 52.179  12.623  1.00 7.52  ? 160  PHE A CA  1 
ATOM   1113 C  C   . PHE A 1 160  ? 44.540 51.555  11.582  1.00 6.74  ? 160  PHE A C   1 
ATOM   1114 O  O   . PHE A 1 160  ? 44.741 50.415  11.164  1.00 7.82  ? 160  PHE A O   1 
ATOM   1115 C  CB  . PHE A 1 160  ? 46.817 52.512  11.994  1.00 7.14  ? 160  PHE A CB  1 
ATOM   1116 C  CG  . PHE A 1 160  ? 47.685 53.387  12.851  1.00 7.30  ? 160  PHE A CG  1 
ATOM   1117 C  CD1 . PHE A 1 160  ? 47.409 54.737  12.990  1.00 7.65  ? 160  PHE A CD1 1 
ATOM   1118 C  CD2 . PHE A 1 160  ? 48.778 52.860  13.520  1.00 8.33  ? 160  PHE A CD2 1 
ATOM   1119 C  CE1 . PHE A 1 160  ? 48.206 55.545  13.778  1.00 8.87  ? 160  PHE A CE1 1 
ATOM   1120 C  CE2 . PHE A 1 160  ? 49.579 53.663  14.310  1.00 9.69  ? 160  PHE A CE2 1 
ATOM   1121 C  CZ  . PHE A 1 160  ? 49.292 55.007  14.439  1.00 10.23 ? 160  PHE A CZ  1 
ATOM   1122 N  N   . VAL A 1 161  ? 43.528 52.310  11.167  1.00 6.40  ? 161  VAL A N   1 
ATOM   1123 C  CA  . VAL A 1 161  ? 42.525 51.804  10.237  1.00 6.86  ? 161  VAL A CA  1 
ATOM   1124 C  C   . VAL A 1 161  ? 42.732 52.625  8.953   1.00 6.99  ? 161  VAL A C   1 
ATOM   1125 O  O   . VAL A 1 161  ? 42.845 53.873  8.968   1.00 8.16  ? 161  VAL A O   1 
ATOM   1126 C  CB  . VAL A 1 161  ? 41.063 51.884  10.800  1.00 5.85  ? 161  VAL A CB  1 
ATOM   1127 C  CG1 . VAL A 1 161  ? 40.945 50.911  11.973  1.00 7.69  ? 161  VAL A CG1 1 
ATOM   1128 C  CG2 . VAL A 1 161  ? 40.748 53.270  11.282  1.00 8.56  ? 161  VAL A CG2 1 
ATOM   1129 N  N   . THR A 1 162  ? 42.728 51.894  7.835   1.00 6.73  ? 162  THR A N   1 
ATOM   1130 C  CA  . THR A 1 162  ? 43.126 52.376  6.500   1.00 7.77  ? 162  THR A CA  1 
ATOM   1131 C  C   . THR A 1 162  ? 44.592 52.832  6.415   1.00 6.16  ? 162  THR A C   1 
ATOM   1132 O  O   . THR A 1 162  ? 45.371 52.272  5.674   1.00 8.51  ? 162  THR A O   1 
ATOM   1133 C  CB  . THR A 1 162  ? 42.228 53.520  5.950   1.00 8.13  ? 162  THR A CB  1 
ATOM   1134 O  OG1 . THR A 1 162  ? 40.853 53.150  6.077   1.00 9.27  ? 162  THR A OG1 1 
ATOM   1135 C  CG2 . THR A 1 162  ? 42.534 53.774  4.434   1.00 10.00 ? 162  THR A CG2 1 
ATOM   1136 N  N   . GLY A 1 163  ? 44.933 53.865  7.172   1.00 7.26  ? 163  GLY A N   1 
ATOM   1137 C  CA  . GLY A 1 163  ? 46.328 54.302  7.204   1.00 7.43  ? 163  GLY A CA  1 
ATOM   1138 C  C   . GLY A 1 163  ? 46.662 55.246  6.055   1.00 6.09  ? 163  GLY A C   1 
ATOM   1139 O  O   . GLY A 1 163  ? 47.813 55.447  5.739   1.00 7.42  ? 163  GLY A O   1 
ATOM   1140 N  N   . GLY A 1 164  ? 45.621 55.812  5.415   1.00 6.60  ? 164  GLY A N   1 
ATOM   1141 C  CA  . GLY A 1 164  ? 45.915 56.854  4.412   1.00 6.83  ? 164  GLY A CA  1 
ATOM   1142 C  C   . GLY A 1 164  ? 46.243 58.193  5.024   1.00 6.22  ? 164  GLY A C   1 
ATOM   1143 O  O   . GLY A 1 164  ? 45.978 58.477  6.226   1.00 6.48  ? 164  GLY A O   1 
ATOM   1144 N  N   . TRP A 1 165  ? 46.816 59.109  4.232   1.00 5.40  ? 165  TRP A N   1 
ATOM   1145 C  CA  . TRP A 1 165  ? 47.082 60.482  4.718   1.00 5.71  ? 165  TRP A CA  1 
ATOM   1146 C  C   . TRP A 1 165  ? 45.779 61.089  5.184   1.00 5.00  ? 165  TRP A C   1 
ATOM   1147 O  O   . TRP A 1 165  ? 45.747 61.840  6.194   1.00 6.20  ? 165  TRP A O   1 
ATOM   1148 C  CB  . TRP A 1 165  ? 47.718 61.283  3.553   1.00 5.77  ? 165  TRP A CB  1 
ATOM   1149 C  CG  . TRP A 1 165  ? 48.538 62.430  4.031   1.00 5.71  ? 165  TRP A CG  1 
ATOM   1150 C  CD1 . TRP A 1 165  ? 48.351 63.756  3.709   1.00 8.29  ? 165  TRP A CD1 1 
ATOM   1151 C  CD2 . TRP A 1 165  ? 49.738 62.344  4.820   1.00 6.72  ? 165  TRP A CD2 1 
ATOM   1152 N  NE1 . TRP A 1 165  ? 49.377 64.500  4.285   1.00 8.79  ? 165  TRP A NE1 1 
ATOM   1153 C  CE2 . TRP A 1 165  ? 50.226 63.670  4.961   1.00 7.67  ? 165  TRP A CE2 1 
ATOM   1154 C  CE3 . TRP A 1 165  ? 50.443 61.275  5.404   1.00 9.28  ? 165  TRP A CE3 1 
ATOM   1155 C  CZ2 . TRP A 1 165  ? 51.426 63.972  5.727   1.00 9.83  ? 165  TRP A CZ2 1 
ATOM   1156 C  CZ3 . TRP A 1 165  ? 51.669 61.608  6.157   1.00 11.09 ? 165  TRP A CZ3 1 
ATOM   1157 C  CH2 . TRP A 1 165  ? 52.084 62.929  6.279   1.00 11.64 ? 165  TRP A CH2 1 
ATOM   1158 N  N   . VAL A 1 166  ? 44.691 60.796  4.476   1.00 5.53  ? 166  VAL A N   1 
ATOM   1159 C  CA  . VAL A 1 166  ? 43.351 61.294  4.798   1.00 5.82  ? 166  VAL A CA  1 
ATOM   1160 C  C   . VAL A 1 166  ? 42.308 60.160  4.658   1.00 5.60  ? 166  VAL A C   1 
ATOM   1161 O  O   . VAL A 1 166  ? 42.642 59.058  4.314   1.00 6.62  ? 166  VAL A O   1 
ATOM   1162 C  CB  . VAL A 1 166  ? 42.952 62.481  3.850   1.00 5.98  ? 166  VAL A CB  1 
ATOM   1163 C  CG1 . VAL A 1 166  ? 43.944 63.633  3.951   1.00 6.65  ? 166  VAL A CG1 1 
ATOM   1164 C  CG2 . VAL A 1 166  ? 42.882 62.006  2.408   1.00 7.68  ? 166  VAL A CG2 1 
ATOM   1165 N  N   . MET A 1 167  ? 41.062 60.459  4.934   1.00 6.13  ? 167  MET A N   1 
ATOM   1166 C  CA  . MET A 1 167  ? 39.961 59.607  4.529   1.00 5.46  ? 167  MET A CA  1 
ATOM   1167 C  C   . MET A 1 167  ? 39.313 60.298  3.321   1.00 7.13  ? 167  MET A C   1 
ATOM   1168 O  O   . MET A 1 167  ? 38.602 61.266  3.465   1.00 6.99  ? 167  MET A O   1 
ATOM   1169 C  CB  . MET A 1 167  ? 38.989 59.536  5.700   1.00 6.74  ? 167  MET A CB  1 
ATOM   1170 C  CG  . MET A 1 167  ? 37.686 58.771  5.427   1.00 6.07  ? 167  MET A CG  1 
ATOM   1171 S  SD  . MET A 1 167  ? 36.484 58.863  6.811   1.00 8.00  ? 167  MET A SD  1 
ATOM   1172 C  CE  . MET A 1 167  ? 37.420 58.082  8.142   1.00 8.66  ? 167  MET A CE  1 
ATOM   1173 N  N   . PRO A 1 168  ? 39.632 59.847  2.123   1.00 5.83  ? 168  PRO A N   1 
ATOM   1174 C  CA  . PRO A 1 168  ? 39.380 60.664  0.930   1.00 6.19  ? 168  PRO A CA  1 
ATOM   1175 C  C   . PRO A 1 168  ? 37.915 60.668  0.500   1.00 5.54  ? 168  PRO A C   1 
ATOM   1176 O  O   . PRO A 1 168  ? 37.171 59.730  0.769   1.00 6.23  ? 168  PRO A O   1 
ATOM   1177 C  CB  . PRO A 1 168  ? 40.234 59.983  -0.137  1.00 7.30  ? 168  PRO A CB  1 
ATOM   1178 C  CG  . PRO A 1 168  ? 40.286 58.585  0.303   1.00 6.17  ? 168  PRO A CG  1 
ATOM   1179 C  CD  . PRO A 1 168  ? 40.394 58.638  1.789   1.00 6.68  ? 168  PRO A CD  1 
ATOM   1180 N  N   . ASP A 1 169  ? 37.543 61.739  -0.176  1.00 5.63  ? 169  ASP A N   1 
ATOM   1181 C  CA  . ASP A 1 169  ? 36.340 61.736  -1.002  1.00 5.64  ? 169  ASP A CA  1 
ATOM   1182 C  C   . ASP A 1 169  ? 36.467 60.562  -1.975  1.00 5.62  ? 169  ASP A C   1 
ATOM   1183 O  O   . ASP A 1 169  ? 37.569 60.204  -2.427  1.00 6.77  ? 169  ASP A O   1 
ATOM   1184 C  CB  . ASP A 1 169  ? 36.338 63.027  -1.825  1.00 5.74  ? 169  ASP A CB  1 
ATOM   1185 C  CG  . ASP A 1 169  ? 35.155 63.092  -2.772  1.00 6.09  ? 169  ASP A CG  1 
ATOM   1186 O  OD1 . ASP A 1 169  ? 34.057 62.617  -2.463  1.00 7.48  ? 169  ASP A OD1 1 
ATOM   1187 O  OD2 . ASP A 1 169  ? 35.301 63.686  -3.869  1.00 8.20  ? 169  ASP A OD2 1 
ATOM   1188 N  N   . GLU A 1 170  ? 35.334 59.965  -2.320  1.00 5.92  ? 170  GLU A N   1 
ATOM   1189 C  CA  . GLU A 1 170  ? 35.322 58.846  -3.258  1.00 5.74  ? 170  GLU A CA  1 
ATOM   1190 C  C   . GLU A 1 170  ? 34.588 59.215  -4.570  1.00 5.89  ? 170  GLU A C   1 
ATOM   1191 O  O   . GLU A 1 170  ? 34.593 58.414  -5.525  1.00 5.96  ? 170  GLU A O   1 
ATOM   1192 C  CB  . GLU A 1 170  ? 34.643 57.600  -2.630  1.00 8.00  ? 170  GLU A CB  1 
ATOM   1193 C  CG  . GLU A 1 170  ? 35.414 57.202  -1.316  1.00 7.86  ? 170  GLU A CG  1 
ATOM   1194 C  CD  . GLU A 1 170  ? 34.926 55.924  -0.675  1.00 8.29  ? 170  GLU A CD  1 
ATOM   1195 O  OE1 . GLU A 1 170  ? 34.181 55.165  -1.304  1.00 8.56  ? 170  GLU A OE1 1 
ATOM   1196 O  OE2 . GLU A 1 170  ? 35.311 55.696  0.533   1.00 10.05 ? 170  GLU A OE2 1 
ATOM   1197 N  N   . ALA A 1 171  ? 34.020 60.400  -4.663  1.00 5.64  ? 171  ALA A N   1 
ATOM   1198 C  CA  . ALA A 1 171  ? 33.271 60.767  -5.887  1.00 5.32  ? 171  ALA A CA  1 
ATOM   1199 C  C   . ALA A 1 171  ? 34.129 61.538  -6.890  1.00 6.21  ? 171  ALA A C   1 
ATOM   1200 O  O   . ALA A 1 171  ? 34.154 61.252  -8.110  1.00 6.80  ? 171  ALA A O   1 
ATOM   1201 C  CB  . ALA A 1 171  ? 32.104 61.661  -5.509  1.00 6.38  ? 171  ALA A CB  1 
ATOM   1202 N  N   . ASN A 1 172  ? 34.849 62.557  -6.408  1.00 5.79  ? 172  ASN A N   1 
ATOM   1203 C  CA  . ASN A 1 172  ? 35.615 63.447  -7.333  1.00 5.59  ? 172  ASN A CA  1 
ATOM   1204 C  C   . ASN A 1 172  ? 37.061 63.060  -7.471  1.00 5.60  ? 172  ASN A C   1 
ATOM   1205 O  O   . ASN A 1 172  ? 37.740 63.501  -8.422  1.00 6.55  ? 172  ASN A O   1 
ATOM   1206 C  CB  . ASN A 1 172  ? 35.556 64.869  -6.742  1.00 6.19  ? 172  ASN A CB  1 
ATOM   1207 C  CG  . ASN A 1 172  ? 34.152 65.414  -6.635  1.00 7.95  ? 172  ASN A CG  1 
ATOM   1208 O  OD1 . ASN A 1 172  ? 33.471 65.645  -7.635  1.00 9.73  ? 172  ASN A OD1 1 
ATOM   1209 N  ND2 . ASN A 1 172  ? 33.721 65.711  -5.403  1.00 8.42  ? 172  ASN A ND2 1 
ATOM   1210 N  N   . SER A 1 173  ? 37.583 62.277  -6.545  1.00 5.28  ? 173  SER A N   1 
ATOM   1211 C  CA  . SER A 1 173  ? 38.984 61.936  -6.539  1.00 4.76  ? 173  SER A CA  1 
ATOM   1212 C  C   . SER A 1 173  ? 39.368 61.046  -7.689  1.00 4.53  ? 173  SER A C   1 
ATOM   1213 O  O   . SER A 1 173  ? 38.620 60.117  -8.070  1.00 5.90  ? 173  SER A O   1 
ATOM   1214 C  CB  . SER A 1 173  ? 39.324 61.255  -5.207  1.00 6.43  ? 173  SER A CB  1 
ATOM   1215 O  OG  . SER A 1 173  ? 38.403 60.132  -5.020  1.00 6.56  ? 173  SER A OG  1 
ATOM   1216 N  N   . HIS A 1 174  ? 40.555 61.279  -8.247  1.00 4.55  ? 174  HIS A N   1 
ATOM   1217 C  CA  . HIS A 1 174  ? 41.078 60.380  -9.267  1.00 4.55  ? 174  HIS A CA  1 
ATOM   1218 C  C   . HIS A 1 174  ? 41.743 59.175  -8.562  1.00 4.09  ? 174  HIS A C   1 
ATOM   1219 O  O   . HIS A 1 174  ? 42.395 59.352  -7.515  1.00 5.33  ? 174  HIS A O   1 
ATOM   1220 C  CB  . HIS A 1 174  ? 42.129 61.094  -10.092 1.00 5.93  ? 174  HIS A CB  1 
ATOM   1221 C  CG  . HIS A 1 174  ? 42.398 60.421  -11.393 1.00 5.96  ? 174  HIS A CG  1 
ATOM   1222 N  ND1 . HIS A 1 174  ? 43.139 59.255  -11.502 1.00 7.16  ? 174  HIS A ND1 1 
ATOM   1223 C  CD2 . HIS A 1 174  ? 41.930 60.718  -12.637 1.00 7.47  ? 174  HIS A CD2 1 
ATOM   1224 C  CE1 . HIS A 1 174  ? 43.092 58.853  -12.766 1.00 7.63  ? 174  HIS A CE1 1 
ATOM   1225 N  NE2 . HIS A 1 174  ? 42.363 59.716  -13.453 1.00 8.16  ? 174  HIS A NE2 1 
ATOM   1226 N  N   . TRP A 1 175  ? 41.592 57.971  -9.103  1.00 4.53  ? 175  TRP A N   1 
ATOM   1227 C  CA  . TRP A 1 175  ? 42.182 56.786  -8.473  1.00 4.44  ? 175  TRP A CA  1 
ATOM   1228 C  C   . TRP A 1 175  ? 43.672 56.981  -8.232  1.00 4.99  ? 175  TRP A C   1 
ATOM   1229 O  O   . TRP A 1 175  ? 44.196 56.446  -7.252  1.00 6.02  ? 175  TRP A O   1 
ATOM   1230 C  CB  . TRP A 1 175  ? 41.904 55.510  -9.289  1.00 4.84  ? 175  TRP A CB  1 
ATOM   1231 C  CG  . TRP A 1 175  ? 42.734 55.320  -10.534 1.00 5.78  ? 175  TRP A CG  1 
ATOM   1232 C  CD1 . TRP A 1 175  ? 42.389 55.701  -11.825 1.00 5.23  ? 175  TRP A CD1 1 
ATOM   1233 C  CD2 . TRP A 1 175  ? 43.998 54.685  -10.621 1.00 4.86  ? 175  TRP A CD2 1 
ATOM   1234 N  NE1 . TRP A 1 175  ? 43.408 55.309  -12.680 1.00 6.23  ? 175  TRP A NE1 1 
ATOM   1235 C  CE2 . TRP A 1 175  ? 44.395 54.683  -11.979 1.00 5.55  ? 175  TRP A CE2 1 
ATOM   1236 C  CE3 . TRP A 1 175  ? 44.849 54.091  -9.662  1.00 6.99  ? 175  TRP A CE3 1 
ATOM   1237 C  CZ2 . TRP A 1 175  ? 45.625 54.133  -12.422 1.00 6.53  ? 175  TRP A CZ2 1 
ATOM   1238 C  CZ3 . TRP A 1 175  ? 46.044 53.531  -10.089 1.00 7.06  ? 175  TRP A CZ3 1 
ATOM   1239 C  CH2 . TRP A 1 175  ? 46.431 53.565  -11.479 1.00 7.94  ? 175  TRP A CH2 1 
ATOM   1240 N  N   . ARG A 1 176  ? 44.357 57.684  -9.119  1.00 5.11  ? 176  ARG A N   1 
ATOM   1241 C  CA  . ARG A 1 176  ? 45.808 57.875  -8.962  1.00 5.40  ? 176  ARG A CA  1 
ATOM   1242 C  C   . ARG A 1 176  ? 46.094 58.635  -7.658  1.00 5.03  ? 176  ARG A C   1 
ATOM   1243 O  O   . ARG A 1 176  ? 47.054 58.312  -6.958  1.00 6.09  ? 176  ARG A O   1 
ATOM   1244 C  CB  . ARG A 1 176  ? 46.400 58.610  -10.185 1.00 6.67  ? 176  ARG A CB  1 
ATOM   1245 C  CG  . ARG A 1 176  ? 46.490 57.718  -11.439 1.00 7.63  ? 176  ARG A CG  1 
ATOM   1246 C  CD  . ARG A 1 176  ? 46.438 58.484  -12.766 1.00 11.03 ? 176  ARG A CD  1 
ATOM   1247 N  NE  . ARG A 1 176  ? 47.479 59.497  -12.835 1.00 10.56 ? 176  ARG A NE  1 
ATOM   1248 C  CZ  . ARG A 1 176  ? 47.641 60.338  -13.847 1.00 10.06 ? 176  ARG A CZ  1 
ATOM   1249 N  NH1 . ARG A 1 176  ? 46.817 60.322  -14.884 1.00 10.62 ? 176  ARG A NH1 1 
ATOM   1250 N  NH2 . ARG A 1 176  ? 48.597 61.229  -13.782 1.00 10.95 ? 176  ARG A NH2 1 
ATOM   1251 N  N   . ASN A 1 177  ? 45.228 59.595  -7.311  1.00 4.83  ? 177  ASN A N   1 
ATOM   1252 C  CA  . ASN A 1 177  ? 45.446 60.353  -6.083  1.00 4.48  ? 177  ASN A CA  1 
ATOM   1253 C  C   . ASN A 1 177  ? 44.927 59.616  -4.854  1.00 4.88  ? 177  ASN A C   1 
ATOM   1254 O  O   . ASN A 1 177  ? 45.470 59.814  -3.729  1.00 5.91  ? 177  ASN A O   1 
ATOM   1255 C  CB  . ASN A 1 177  ? 44.859 61.752  -6.187  1.00 5.40  ? 177  ASN A CB  1 
ATOM   1256 C  CG  . ASN A 1 177  ? 45.537 62.564  -7.211  1.00 6.66  ? 177  ASN A CG  1 
ATOM   1257 O  OD1 . ASN A 1 177  ? 46.694 62.364  -7.553  1.00 7.57  ? 177  ASN A OD1 1 
ATOM   1258 N  ND2 . ASN A 1 177  ? 44.777 63.521  -7.732  1.00 8.93  ? 177  ASN A ND2 1 
ATOM   1259 N  N   . VAL A 1 178  ? 43.940 58.770  -5.015  1.00 5.08  ? 178  VAL A N   1 
ATOM   1260 C  CA  . VAL A 1 178  ? 43.518 57.942  -3.879  1.00 5.85  ? 178  VAL A CA  1 
ATOM   1261 C  C   . VAL A 1 178  ? 44.695 56.996  -3.557  1.00 5.01  ? 178  VAL A C   1 
ATOM   1262 O  O   . VAL A 1 178  ? 45.046 56.830  -2.342  1.00 6.04  ? 178  VAL A O   1 
ATOM   1263 C  CB  . VAL A 1 178  ? 42.313 57.062  -4.257  1.00 5.83  ? 178  VAL A CB  1 
ATOM   1264 C  CG1 . VAL A 1 178  ? 41.989 56.040  -3.129  1.00 7.41  ? 178  VAL A CG1 1 
ATOM   1265 C  CG2 . VAL A 1 178  ? 41.082 57.974  -4.484  1.00 8.07  ? 178  VAL A CG2 1 
ATOM   1266 N  N   . LEU A 1 179  ? 45.363 56.446  -4.561  1.00 5.38  ? 179  LEU A N   1 
ATOM   1267 C  CA  . LEU A 1 179  ? 46.510 55.604  -4.304  1.00 5.36  ? 179  LEU A CA  1 
ATOM   1268 C  C   . LEU A 1 179  ? 47.681 56.424  -3.734  1.00 5.85  ? 179  LEU A C   1 
ATOM   1269 O  O   . LEU A 1 179  ? 48.354 55.961  -2.771  1.00 6.05  ? 179  LEU A O   1 
ATOM   1270 C  CB  . LEU A 1 179  ? 46.956 54.896  -5.624  1.00 5.34  ? 179  LEU A CB  1 
ATOM   1271 C  CG  . LEU A 1 179  ? 48.304 54.106  -5.448  1.00 6.63  ? 179  LEU A CG  1 
ATOM   1272 C  CD1 . LEU A 1 179  ? 48.180 52.947  -4.375  1.00 6.97  ? 179  LEU A CD1 1 
ATOM   1273 C  CD2 . LEU A 1 179  ? 48.709 53.482  -6.805  1.00 8.32  ? 179  LEU A CD2 1 
ATOM   1274 N  N   . LEU A 1 180  ? 47.893 57.657  -4.226  1.00 4.76  ? 180  LEU A N   1 
ATOM   1275 C  CA  . LEU A 1 180  ? 48.988 58.479  -3.737  1.00 5.75  ? 180  LEU A CA  1 
ATOM   1276 C  C   . LEU A 1 180  ? 48.800 58.718  -2.237  1.00 4.87  ? 180  LEU A C   1 
ATOM   1277 O  O   . LEU A 1 180  ? 49.783 58.531  -1.446  1.00 5.63  ? 180  LEU A O   1 
ATOM   1278 C  CB  . LEU A 1 180  ? 48.952 59.827  -4.508  1.00 6.47  ? 180  LEU A CB  1 
ATOM   1279 C  CG  . LEU A 1 180  ? 50.069 60.793  -4.107  1.00 7.33  ? 180  LEU A CG  1 
ATOM   1280 C  CD1 . LEU A 1 180  ? 51.366 60.268  -4.767  1.00 9.12  ? 180  LEU A CD1 1 
ATOM   1281 C  CD2 . LEU A 1 180  ? 49.813 62.210  -4.648  1.00 8.80  ? 180  LEU A CD2 1 
ATOM   1282 N  N   . GLN A 1 181  ? 47.593 59.103  -1.805  1.00 5.00  ? 181  GLN A N   1 
ATOM   1283 C  CA  . GLN A 1 181  ? 47.444 59.443  -0.385  1.00 5.69  ? 181  GLN A CA  1 
ATOM   1284 C  C   . GLN A 1 181  ? 47.495 58.190  0.494   1.00 5.66  ? 181  GLN A C   1 
ATOM   1285 O  O   . GLN A 1 181  ? 48.013 58.260  1.652   1.00 5.70  ? 181  GLN A O   1 
ATOM   1286 C  CB  . GLN A 1 181  ? 46.170 60.273  -0.175  1.00 5.73  ? 181  GLN A CB  1 
ATOM   1287 C  CG  . GLN A 1 181  ? 44.863 59.537  -0.397  1.00 5.25  ? 181  GLN A CG  1 
ATOM   1288 C  CD  . GLN A 1 181  ? 44.470 58.637  0.742   1.00 5.69  ? 181  GLN A CD  1 
ATOM   1289 O  OE1 . GLN A 1 181  ? 44.752 58.940  1.927   1.00 7.21  ? 181  GLN A OE1 1 
ATOM   1290 N  NE2 . GLN A 1 181  ? 43.800 57.518  0.412   1.00 7.04  ? 181  GLN A NE2 1 
ATOM   1291 N  N   . LEU A 1 182  ? 46.997 57.052  -0.013  1.00 5.93  ? 182  LEU A N   1 
ATOM   1292 C  CA  . LEU A 1 182  ? 47.101 55.821  0.736   1.00 5.50  ? 182  LEU A CA  1 
ATOM   1293 C  C   . LEU A 1 182  ? 48.554 55.469  0.928   1.00 5.40  ? 182  LEU A C   1 
ATOM   1294 O  O   . LEU A 1 182  ? 48.980 55.065  2.021   1.00 5.97  ? 182  LEU A O   1 
ATOM   1295 C  CB  . LEU A 1 182  ? 46.382 54.675  -0.008  1.00 6.77  ? 182  LEU A CB  1 
ATOM   1296 C  CG  . LEU A 1 182  ? 46.477 53.336  0.697   1.00 5.54  ? 182  LEU A CG  1 
ATOM   1297 C  CD1 . LEU A 1 182  ? 45.710 53.300  2.066   1.00 8.28  ? 182  LEU A CD1 1 
ATOM   1298 C  CD2 . LEU A 1 182  ? 45.891 52.227  -0.250  1.00 7.91  ? 182  LEU A CD2 1 
ATOM   1299 N  N   . THR A 1 183  ? 49.339 55.607  -0.117  1.00 5.86  ? 183  THR A N   1 
ATOM   1300 C  CA  . THR A 1 183  ? 50.750 55.244  -0.074  1.00 5.87  ? 183  THR A CA  1 
ATOM   1301 C  C   . THR A 1 183  ? 51.476 56.205  0.852   1.00 5.53  ? 183  THR A C   1 
ATOM   1302 O  O   . THR A 1 183  ? 52.419 55.779  1.598   1.00 6.30  ? 183  THR A O   1 
ATOM   1303 C  CB  . THR A 1 183  ? 51.377 55.316  -1.513  1.00 5.58  ? 183  THR A CB  1 
ATOM   1304 O  OG1 . THR A 1 183  ? 50.691 54.403  -2.371  1.00 6.38  ? 183  THR A OG1 1 
ATOM   1305 C  CG2 . THR A 1 183  ? 52.834 54.904  -1.477  1.00 7.06  ? 183  THR A CG2 1 
ATOM   1306 N  N   . GLU A 1 184  ? 51.135 57.495  0.853   1.00 5.68  ? 184  GLU A N   1 
ATOM   1307 C  CA  . GLU A 1 184  ? 51.840 58.441  1.738   1.00 6.28  ? 184  GLU A CA  1 
ATOM   1308 C  C   . GLU A 1 184  ? 51.616 58.063  3.189   1.00 5.81  ? 184  GLU A C   1 
ATOM   1309 O  O   . GLU A 1 184  ? 52.595 58.025  3.976   1.00 7.94  ? 184  GLU A O   1 
ATOM   1310 C  CB  . GLU A 1 184  ? 51.311 59.854  1.496   1.00 7.88  ? 184  GLU A CB  1 
ATOM   1311 C  CG  . GLU A 1 184  ? 52.218 60.964  2.013   1.00 10.82 ? 184  GLU A CG  1 
ATOM   1312 C  CD  . GLU A 1 184  ? 53.581 61.018  1.291   1.00 9.86  ? 184  GLU A CD  1 
ATOM   1313 O  OE1 . GLU A 1 184  ? 53.734 60.631  0.118   1.00 12.40 ? 184  GLU A OE1 1 
ATOM   1314 O  OE2 . GLU A 1 184  ? 54.500 61.496  1.964   1.00 13.42 ? 184  GLU A OE2 1 
ATOM   1315 N  N   . GLY A 1 185  ? 50.396 57.763  3.587   1.00 6.70  ? 185  GLY A N   1 
ATOM   1316 C  CA  . GLY A 1 185  ? 50.171 57.402  4.973   1.00 6.56  ? 185  GLY A CA  1 
ATOM   1317 C  C   . GLY A 1 185  ? 50.740 56.042  5.321   1.00 5.91  ? 185  GLY A C   1 
ATOM   1318 O  O   . GLY A 1 185  ? 51.338 55.859  6.406   1.00 6.89  ? 185  GLY A O   1 
ATOM   1319 N  N   . GLN A 1 186  ? 50.604 55.053  4.438   1.00 5.71  ? 186  GLN A N   1 
ATOM   1320 C  CA  . GLN A 1 186  ? 51.077 53.698  4.805   1.00 6.16  ? 186  GLN A CA  1 
ATOM   1321 C  C   . GLN A 1 186  ? 52.589 53.646  4.808   1.00 6.04  ? 186  GLN A C   1 
ATOM   1322 O  O   . GLN A 1 186  ? 53.181 52.879  5.586   1.00 7.22  ? 186  GLN A O   1 
ATOM   1323 C  CB  . GLN A 1 186  ? 50.509 52.632  3.870   1.00 6.22  ? 186  GLN A CB  1 
ATOM   1324 C  CG  . GLN A 1 186  ? 48.969 52.462  4.154   1.00 8.06  ? 186  GLN A CG  1 
ATOM   1325 C  CD  . GLN A 1 186  ? 48.522 51.072  3.932   1.00 7.43  ? 186  GLN A CD  1 
ATOM   1326 O  OE1 . GLN A 1 186  ? 49.151 50.386  3.102   1.00 11.62 ? 186  GLN A OE1 1 
ATOM   1327 N  NE2 . GLN A 1 186  ? 47.471 50.618  4.577   1.00 9.30  ? 186  GLN A NE2 1 
ATOM   1328 N  N   . THR A 1 187  ? 53.266 54.396  3.923   1.00 7.05  ? 187  THR A N   1 
ATOM   1329 C  CA  . THR A 1 187  ? 54.725 54.404  3.930   1.00 6.22  ? 187  THR A CA  1 
ATOM   1330 C  C   . THR A 1 187  ? 55.187 55.006  5.252   1.00 7.84  ? 187  THR A C   1 
ATOM   1331 O  O   . THR A 1 187  ? 56.177 54.498  5.850   1.00 8.33  ? 187  THR A O   1 
ATOM   1332 C  CB  . THR A 1 187  ? 55.260 55.180  2.741   1.00 6.60  ? 187  THR A CB  1 
ATOM   1333 O  OG1 . THR A 1 187  ? 54.789 54.529  1.538   1.00 7.25  ? 187  THR A OG1 1 
ATOM   1334 C  CG2 . THR A 1 187  ? 56.804 55.165  2.693   1.00 7.56  ? 187  THR A CG2 1 
ATOM   1335 N  N   . TRP A 1 188  ? 54.567 56.083  5.706   1.00 6.55  ? 188  TRP A N   1 
ATOM   1336 C  CA  . TRP A 1 188  ? 54.893 56.637  7.015   1.00 6.72  ? 188  TRP A CA  1 
ATOM   1337 C  C   . TRP A 1 188  ? 54.680 55.619  8.141   1.00 6.77  ? 188  TRP A C   1 
ATOM   1338 O  O   . TRP A 1 188  ? 55.547 55.422  8.986   1.00 7.29  ? 188  TRP A O   1 
ATOM   1339 C  CB  . TRP A 1 188  ? 54.095 57.925  7.276   1.00 7.56  ? 188  TRP A CB  1 
ATOM   1340 C  CG  . TRP A 1 188  ? 54.582 58.658  8.483   1.00 7.53  ? 188  TRP A CG  1 
ATOM   1341 C  CD1 . TRP A 1 188  ? 55.452 59.697  8.503   1.00 9.03  ? 188  TRP A CD1 1 
ATOM   1342 C  CD2 . TRP A 1 188  ? 54.252 58.377  9.850   1.00 7.83  ? 188  TRP A CD2 1 
ATOM   1343 N  NE1 . TRP A 1 188  ? 55.700 60.081  9.791   1.00 9.05  ? 188  TRP A NE1 1 
ATOM   1344 C  CE2 . TRP A 1 188  ? 54.971 59.295  10.641  1.00 8.69  ? 188  TRP A CE2 1 
ATOM   1345 C  CE3 . TRP A 1 188  ? 53.426 57.437  10.482  1.00 8.81  ? 188  TRP A CE3 1 
ATOM   1346 C  CZ2 . TRP A 1 188  ? 54.898 59.302  12.023  1.00 10.24 ? 188  TRP A CZ2 1 
ATOM   1347 C  CZ3 . TRP A 1 188  ? 53.358 57.444  11.869  1.00 9.09  ? 188  TRP A CZ3 1 
ATOM   1348 C  CH2 . TRP A 1 188  ? 54.093 58.374  12.618  1.00 9.94  ? 188  TRP A CH2 1 
ATOM   1349 N  N   . LEU A 1 189  ? 53.542 54.938  8.130   1.00 7.12  ? 189  LEU A N   1 
ATOM   1350 C  CA  . LEU A 1 189  ? 53.276 53.936  9.141   1.00 7.12  ? 189  LEU A CA  1 
ATOM   1351 C  C   . LEU A 1 189  ? 54.286 52.800  9.147   1.00 7.11  ? 189  LEU A C   1 
ATOM   1352 O  O   . LEU A 1 189  ? 54.670 52.351  10.218  1.00 9.16  ? 189  LEU A O   1 
ATOM   1353 C  CB  . LEU A 1 189  ? 51.866 53.354  9.004   1.00 7.69  ? 189  LEU A CB  1 
ATOM   1354 C  CG  . LEU A 1 189  ? 50.721 54.256  9.493   1.00 6.89  ? 189  LEU A CG  1 
ATOM   1355 C  CD1 . LEU A 1 189  ? 49.418 53.535  9.187   1.00 7.83  ? 189  LEU A CD1 1 
ATOM   1356 C  CD2 . LEU A 1 189  ? 50.823 54.517  10.996  1.00 7.86  ? 189  LEU A CD2 1 
ATOM   1357 N  N   . LYS A 1 190  ? 54.709 52.331  7.976   1.00 6.70  ? 190  LYS A N   1 
ATOM   1358 C  CA  . LYS A 1 190  ? 55.649 51.221  7.949   1.00 8.70  ? 190  LYS A CA  1 
ATOM   1359 C  C   . LYS A 1 190  ? 56.992 51.714  8.527   1.00 9.80  ? 190  LYS A C   1 
ATOM   1360 O  O   . LYS A 1 190  ? 57.608 51.008  9.359   1.00 10.11 ? 190  LYS A O   1 
ATOM   1361 C  CB  . LYS A 1 190  ? 55.893 50.715  6.510   1.00 9.94  ? 190  LYS A CB  1 
ATOM   1362 C  CG  . LYS A 1 190  ? 56.875 49.495  6.486   1.00 11.33 ? 190  LYS A CG  1 
ATOM   1363 C  CD  . LYS A 1 190  ? 57.039 48.954  5.118   1.00 17.50 ? 190  LYS A CD  1 
ATOM   1364 C  CE  . LYS A 1 190  ? 57.877 47.679  5.135   1.00 23.50 ? 190  LYS A CE  1 
ATOM   1365 N  NZ  . LYS A 1 190  ? 58.188 47.262  3.702   1.00 21.63 ? 190  LYS A NZ  1 
ATOM   1366 N  N   . GLN A 1 191  ? 57.460 52.883  8.123   1.00 9.39  ? 191  GLN A N   1 
ATOM   1367 C  CA  . GLN A 1 191  ? 58.741 53.412  8.604   1.00 11.11 ? 191  GLN A CA  1 
ATOM   1368 C  C   . GLN A 1 191  ? 58.755 53.656  10.108  1.00 11.41 ? 191  GLN A C   1 
ATOM   1369 O  O   . GLN A 1 191  ? 59.691 53.251  10.779  1.00 16.00 ? 191  GLN A O   1 
ATOM   1370 C  CB  . GLN A 1 191  ? 59.078 54.699  7.851   1.00 12.35 ? 191  GLN A CB  1 
ATOM   1371 C  CG  . GLN A 1 191  ? 60.458 55.311  8.217   1.00 20.38 ? 191  GLN A CG  1 
ATOM   1372 C  CD  . GLN A 1 191  ? 60.846 56.493  7.320   1.00 21.74 ? 191  GLN A CD  1 
ATOM   1373 O  OE1 . GLN A 1 191  ? 60.097 56.885  6.443   1.00 37.16 ? 191  GLN A OE1 1 
ATOM   1374 N  NE2 . GLN A 1 191  ? 62.019 57.067  7.563   1.00 25.71 ? 191  GLN A NE2 1 
ATOM   1375 N  N   . PHE A 1 192  ? 57.750 54.344  10.643  1.00 10.46 ? 192  PHE A N   1 
ATOM   1376 C  CA  . PHE A 1 192  ? 57.790 54.752  12.032  1.00 10.40 ? 192  PHE A CA  1 
ATOM   1377 C  C   . PHE A 1 192  ? 57.046 53.876  13.021  1.00 13.42 ? 192  PHE A C   1 
ATOM   1378 O  O   . PHE A 1 192  ? 57.449 53.799  14.202  1.00 16.18 ? 192  PHE A O   1 
ATOM   1379 C  CB  . PHE A 1 192  ? 57.302 56.203  12.137  1.00 9.07  ? 192  PHE A CB  1 
ATOM   1380 C  CG  . PHE A 1 192  ? 58.192 57.184  11.404  1.00 10.91 ? 192  PHE A CG  1 
ATOM   1381 C  CD1 . PHE A 1 192  ? 59.431 57.529  11.999  1.00 13.40 ? 192  PHE A CD1 1 
ATOM   1382 C  CD2 . PHE A 1 192  ? 57.890 57.679  10.132  1.00 11.89 ? 192  PHE A CD2 1 
ATOM   1383 C  CE1 . PHE A 1 192  ? 60.340 58.354  11.295  1.00 14.20 ? 192  PHE A CE1 1 
ATOM   1384 C  CE2 . PHE A 1 192  ? 58.774 58.490  9.438   1.00 12.86 ? 192  PHE A CE2 1 
ATOM   1385 C  CZ  . PHE A 1 192  ? 60.035 58.824  10.057  1.00 14.26 ? 192  PHE A CZ  1 
ATOM   1386 N  N   . MET A 1 193  ? 56.006 53.183  12.577  1.00 10.23 ? 193  MET A N   1 
ATOM   1387 C  CA  . MET A 1 193  ? 55.209 52.374  13.486  1.00 9.73  ? 193  MET A CA  1 
ATOM   1388 C  C   . MET A 1 193  ? 55.363 50.877  13.244  1.00 8.47  ? 193  MET A C   1 
ATOM   1389 O  O   . MET A 1 193  ? 54.893 50.080  14.037  1.00 11.83 ? 193  MET A O   1 
ATOM   1390 C  CB  A MET A 1 193  ? 53.701 52.657  13.406  0.50 10.73 ? 193  MET A CB  1 
ATOM   1391 C  CB  B MET A 1 193  ? 53.789 52.953  13.502  0.50 10.80 ? 193  MET A CB  1 
ATOM   1392 C  CG  A MET A 1 193  ? 53.198 53.927  14.083  0.50 12.08 ? 193  MET A CG  1 
ATOM   1393 C  CG  B MET A 1 193  ? 53.751 54.483  13.575  0.50 12.12 ? 193  MET A CG  1 
ATOM   1394 S  SD  A MET A 1 193  ? 53.533 54.116  15.857  0.50 22.77 ? 193  MET A SD  1 
ATOM   1395 S  SD  B MET A 1 193  ? 54.539 55.187  15.037  0.50 34.08 ? 193  MET A SD  1 
ATOM   1396 C  CE  A MET A 1 193  ? 54.736 55.374  15.519  0.50 26.76 ? 193  MET A CE  1 
ATOM   1397 C  CE  B MET A 1 193  ? 53.555 54.193  16.136  0.50 34.89 ? 193  MET A CE  1 
ATOM   1398 N  N   . ASN A 1 194  ? 56.003 50.509  12.140  1.00 9.18  ? 194  ASN A N   1 
ATOM   1399 C  CA  . ASN A 1 194  ? 56.157 49.114  11.742  1.00 10.09 ? 194  ASN A CA  1 
ATOM   1400 C  C   . ASN A 1 194  ? 54.831 48.333  11.613  1.00 12.13 ? 194  ASN A C   1 
ATOM   1401 O  O   . ASN A 1 194  ? 54.705 47.174  12.088  1.00 13.03 ? 194  ASN A O   1 
ATOM   1402 C  CB  . ASN A 1 194  ? 57.088 48.384  12.753  1.00 13.28 ? 194  ASN A CB  1 
ATOM   1403 C  CG  . ASN A 1 194  ? 57.557 47.042  12.222  1.00 15.37 ? 194  ASN A CG  1 
ATOM   1404 O  OD1 . ASN A 1 194  ? 57.681 46.848  11.012  1.00 18.38 ? 194  ASN A OD1 1 
ATOM   1405 N  ND2 . ASN A 1 194  ? 57.817 46.127  13.155  1.00 19.29 ? 194  ASN A ND2 1 
ATOM   1406 N  N   . VAL A 1 195  ? 53.806 48.983  11.062  1.00 9.77  ? 195  VAL A N   1 
ATOM   1407 C  CA  . VAL A 1 195  ? 52.514 48.338  10.826  1.00 9.53  ? 195  VAL A CA  1 
ATOM   1408 C  C   . VAL A 1 195  ? 51.962 48.751  9.488   1.00 9.03  ? 195  VAL A C   1 
ATOM   1409 O  O   . VAL A 1 195  ? 52.254 49.825  9.022   1.00 9.64  ? 195  VAL A O   1 
ATOM   1410 C  CB  . VAL A 1 195  ? 51.477 48.665  11.935  1.00 12.04 ? 195  VAL A CB  1 
ATOM   1411 C  CG1 . VAL A 1 195  ? 51.933 48.150  13.291  1.00 18.25 ? 195  VAL A CG1 1 
ATOM   1412 C  CG2 . VAL A 1 195  ? 51.151 50.137  11.987  1.00 13.48 ? 195  VAL A CG2 1 
ATOM   1413 N  N   . THR A 1 196  ? 51.155 47.877  8.898   1.00 9.38  ? 196  THR A N   1 
ATOM   1414 C  CA  . THR A 1 196  ? 50.449 48.153  7.622   1.00 9.12  ? 196  THR A CA  1 
ATOM   1415 C  C   . THR A 1 196  ? 48.994 47.692  7.837   1.00 9.27  ? 196  THR A C   1 
ATOM   1416 O  O   . THR A 1 196  ? 48.722 46.485  7.905   1.00 10.66 ? 196  THR A O   1 
ATOM   1417 C  CB  . THR A 1 196  ? 51.069 47.392  6.408   1.00 9.61  ? 196  THR A CB  1 
ATOM   1418 O  OG1 . THR A 1 196  ? 52.465 47.772  6.292   1.00 12.27 ? 196  THR A OG1 1 
ATOM   1419 C  CG2 . THR A 1 196  ? 50.334 47.753  5.129   1.00 12.06 ? 196  THR A CG2 1 
ATOM   1420 N  N   . PRO A 1 197  ? 48.046 48.609  7.942   1.00 8.41  ? 197  PRO A N   1 
ATOM   1421 C  CA  . PRO A 1 197  ? 46.664 48.228  8.151   1.00 8.32  ? 197  PRO A CA  1 
ATOM   1422 C  C   . PRO A 1 197  ? 46.132 47.373  7.046   1.00 7.33  ? 197  PRO A C   1 
ATOM   1423 O  O   . PRO A 1 197  ? 46.455 47.579  5.852   1.00 8.37  ? 197  PRO A O   1 
ATOM   1424 C  CB  . PRO A 1 197  ? 45.938 49.582  8.101   1.00 8.59  ? 197  PRO A CB  1 
ATOM   1425 C  CG  . PRO A 1 197  ? 46.935 50.528  8.682   1.00 8.62  ? 197  PRO A CG  1 
ATOM   1426 C  CD  . PRO A 1 197  ? 48.247 50.076  8.077   1.00 9.12  ? 197  PRO A CD  1 
ATOM   1427 N  N   . THR A 1 198  ? 45.272 46.411  7.402   1.00 7.43  ? 198  THR A N   1 
ATOM   1428 C  CA  . THR A 1 198  ? 44.610 45.580  6.404   1.00 7.36  ? 198  THR A CA  1 
ATOM   1429 C  C   . THR A 1 198  ? 43.090 45.745  6.470   1.00 6.84  ? 198  THR A C   1 
ATOM   1430 O  O   . THR A 1 198  ? 42.341 45.047  5.754   1.00 7.55  ? 198  THR A O   1 
ATOM   1431 C  CB  . THR A 1 198  ? 44.944 44.104  6.534   1.00 8.94  ? 198  THR A CB  1 
ATOM   1432 O  OG1 . THR A 1 198  ? 44.509 43.671  7.821   1.00 11.54 ? 198  THR A OG1 1 
ATOM   1433 C  CG2 . THR A 1 198  ? 46.446 43.899  6.383   1.00 11.11 ? 198  THR A CG2 1 
ATOM   1434 N  N   . ALA A 1 199  ? 42.613 46.609  7.358   1.00 6.58  ? 199  ALA A N   1 
ATOM   1435 C  CA  . ALA A 1 199  ? 41.191 46.950  7.475   1.00 6.62  ? 199  ALA A CA  1 
ATOM   1436 C  C   . ALA A 1 199  ? 41.021 48.447  7.238   1.00 7.34  ? 199  ALA A C   1 
ATOM   1437 O  O   . ALA A 1 199  ? 41.752 49.244  7.794   1.00 8.00  ? 199  ALA A O   1 
ATOM   1438 C  CB  . ALA A 1 199  ? 40.663 46.596  8.889   1.00 7.57  ? 199  ALA A CB  1 
ATOM   1439 N  N   . SER A 1 200  ? 40.047 48.802  6.410   1.00 6.43  ? 200  SER A N   1 
ATOM   1440 C  CA  . SER A 1 200  ? 39.760 50.200  6.089   1.00 6.56  ? 200  SER A CA  1 
ATOM   1441 C  C   . SER A 1 200  ? 38.502 50.676  6.783   1.00 7.31  ? 200  SER A C   1 
ATOM   1442 O  O   . SER A 1 200  ? 37.537 49.928  6.965   1.00 8.27  ? 200  SER A O   1 
ATOM   1443 C  CB  . SER A 1 200  ? 39.612 50.329  4.574   1.00 7.44  ? 200  SER A CB  1 
ATOM   1444 O  OG  . SER A 1 200  ? 39.426 51.698  4.181   1.00 10.65 ? 200  SER A OG  1 
ATOM   1445 N  N   . TRP A 1 201  ? 38.477 51.965  7.113   1.00 6.57  ? 201  TRP A N   1 
ATOM   1446 C  CA  . TRP A 1 201  ? 37.396 52.650  7.851   1.00 6.46  ? 201  TRP A CA  1 
ATOM   1447 C  C   . TRP A 1 201  ? 37.055 53.941  7.113   1.00 6.71  ? 201  TRP A C   1 
ATOM   1448 O  O   . TRP A 1 201  ? 37.848 54.864  7.086   1.00 8.73  ? 201  TRP A O   1 
ATOM   1449 C  CB  . TRP A 1 201  ? 37.921 52.971  9.249   1.00 7.23  ? 201  TRP A CB  1 
ATOM   1450 C  CG  . TRP A 1 201  ? 37.118 53.781  10.236  1.00 7.58  ? 201  TRP A CG  1 
ATOM   1451 C  CD1 . TRP A 1 201  ? 37.284 55.105  10.527  1.00 7.92  ? 201  TRP A CD1 1 
ATOM   1452 C  CD2 . TRP A 1 201  ? 36.164 53.286  11.172  1.00 7.27  ? 201  TRP A CD2 1 
ATOM   1453 N  NE1 . TRP A 1 201  ? 36.467 55.466  11.556  1.00 8.33  ? 201  TRP A NE1 1 
ATOM   1454 C  CE2 . TRP A 1 201  ? 35.757 54.375  11.968  1.00 7.07  ? 201  TRP A CE2 1 
ATOM   1455 C  CE3 . TRP A 1 201  ? 35.594 52.032  11.401  1.00 8.19  ? 201  TRP A CE3 1 
ATOM   1456 C  CZ2 . TRP A 1 201  ? 34.809 54.248  12.976  1.00 8.51  ? 201  TRP A CZ2 1 
ATOM   1457 C  CZ3 . TRP A 1 201  ? 34.657 51.908  12.403  1.00 9.46  ? 201  TRP A CZ3 1 
ATOM   1458 C  CH2 . TRP A 1 201  ? 34.275 53.007  13.179  1.00 9.53  ? 201  TRP A CH2 1 
ATOM   1459 N  N   . ALA A 1 202  ? 35.886 53.986  6.498   1.00 6.90  ? 202  ALA A N   1 
ATOM   1460 C  CA  . ALA A 1 202  ? 35.450 55.191  5.733   1.00 6.32  ? 202  ALA A CA  1 
ATOM   1461 C  C   . ALA A 1 202  ? 34.018 55.544  6.168   1.00 7.45  ? 202  ALA A C   1 
ATOM   1462 O  O   . ALA A 1 202  ? 33.036 55.118  5.581   1.00 8.70  ? 202  ALA A O   1 
ATOM   1463 C  CB  . ALA A 1 202  ? 35.521 54.860  4.237   1.00 9.12  ? 202  ALA A CB  1 
ATOM   1464 N  N   . ILE A 1 203  ? 33.939 56.328  7.245   1.00 6.81  ? 203  ILE A N   1 
ATOM   1465 C  CA  . ILE A 1 203  ? 32.644 56.639  7.869   1.00 6.85  ? 203  ILE A CA  1 
ATOM   1466 C  C   . ILE A 1 203  ? 32.001 57.920  7.416   1.00 6.83  ? 203  ILE A C   1 
ATOM   1467 O  O   . ILE A 1 203  ? 30.821 58.129  7.663   1.00 7.43  ? 203  ILE A O   1 
ATOM   1468 C  CB  . ILE A 1 203  ? 32.763 56.658  9.440   1.00 7.18  ? 203  ILE A CB  1 
ATOM   1469 C  CG1 . ILE A 1 203  ? 33.900 57.595  9.898   1.00 7.15  ? 203  ILE A CG1 1 
ATOM   1470 C  CG2 . ILE A 1 203  ? 33.052 55.209  9.934   1.00 8.36  ? 203  ILE A CG2 1 
ATOM   1471 C  CD1 . ILE A 1 203  ? 33.829 57.894  11.424  1.00 7.12  ? 203  ILE A CD1 1 
ATOM   1472 N  N   . ASP A 1 204  ? 32.761 58.785  6.716   1.00 6.63  ? 204  ASP A N   1 
ATOM   1473 C  CA  . ASP A 1 204  ? 32.198 60.091  6.328   1.00 6.84  ? 204  ASP A CA  1 
ATOM   1474 C  C   . ASP A 1 204  ? 32.132 60.493  4.845   1.00 7.31  ? 204  ASP A C   1 
ATOM   1475 O  O   . ASP A 1 204  ? 31.399 61.441  4.555   1.00 8.28  ? 204  ASP A O   1 
ATOM   1476 C  CB  . ASP A 1 204  ? 32.890 61.209  7.126   1.00 7.32  ? 204  ASP A CB  1 
ATOM   1477 C  CG  . ASP A 1 204  ? 31.987 62.425  7.415   1.00 6.03  ? 204  ASP A CG  1 
ATOM   1478 O  OD1 . ASP A 1 204  ? 30.750 62.291  7.475   1.00 7.34  ? 204  ASP A OD1 1 
ATOM   1479 O  OD2 . ASP A 1 204  ? 32.489 63.558  7.627   1.00 6.77  ? 204  ASP A OD2 1 
ATOM   1480 N  N   . PRO A 1 205  ? 32.855 59.854  3.887   1.00 6.28  ? 205  PRO A N   1 
ATOM   1481 C  CA  . PRO A 1 205  ? 32.712 60.298  2.467   1.00 6.65  ? 205  PRO A CA  1 
ATOM   1482 C  C   . PRO A 1 205  ? 31.241 60.202  2.043   1.00 6.45  ? 205  PRO A C   1 
ATOM   1483 O  O   . PRO A 1 205  ? 30.473 59.331  2.517   1.00 7.50  ? 205  PRO A O   1 
ATOM   1484 C  CB  . PRO A 1 205  ? 33.583 59.324  1.686   1.00 8.68  ? 205  PRO A CB  1 
ATOM   1485 C  CG  . PRO A 1 205  ? 34.685 58.923  2.665   1.00 12.06 ? 205  PRO A CG  1 
ATOM   1486 C  CD  . PRO A 1 205  ? 33.853 58.769  3.989   1.00 9.04  ? 205  PRO A CD  1 
ATOM   1487 N  N   . PHE A 1 206  ? 30.847 61.079  1.099   1.00 6.02  ? 206  PHE A N   1 
ATOM   1488 C  CA  . PHE A 1 206  ? 29.392 61.251  0.847   1.00 6.96  ? 206  PHE A CA  1 
ATOM   1489 C  C   . PHE A 1 206  ? 28.974 60.337  -0.318  1.00 6.43  ? 206  PHE A C   1 
ATOM   1490 O  O   . PHE A 1 206  ? 28.747 60.736  -1.479  1.00 7.43  ? 206  PHE A O   1 
ATOM   1491 C  CB  . PHE A 1 206  ? 29.119 62.722  0.525   1.00 6.85  ? 206  PHE A CB  1 
ATOM   1492 C  CG  . PHE A 1 206  ? 29.918 63.723  1.351   1.00 6.15  ? 206  PHE A CG  1 
ATOM   1493 C  CD1 . PHE A 1 206  ? 30.195 63.487  2.691   1.00 6.44  ? 206  PHE A CD1 1 
ATOM   1494 C  CD2 . PHE A 1 206  ? 30.442 64.891  0.727   1.00 6.58  ? 206  PHE A CD2 1 
ATOM   1495 C  CE1 . PHE A 1 206  ? 31.005 64.403  3.404   1.00 7.55  ? 206  PHE A CE1 1 
ATOM   1496 C  CE2 . PHE A 1 206  ? 31.249 65.769  1.457   1.00 6.20  ? 206  PHE A CE2 1 
ATOM   1497 C  CZ  . PHE A 1 206  ? 31.517 65.505  2.806   1.00 6.81  ? 206  PHE A CZ  1 
ATOM   1498 N  N   . GLY A 1 207  ? 28.819 59.059  0.017   1.00 6.73  ? 207  GLY A N   1 
ATOM   1499 C  CA  . GLY A 1 207  ? 28.619 58.026  -0.976  1.00 7.48  ? 207  GLY A CA  1 
ATOM   1500 C  C   . GLY A 1 207  ? 29.974 57.312  -1.171  1.00 5.77  ? 207  GLY A C   1 
ATOM   1501 O  O   . GLY A 1 207  ? 31.065 57.819  -0.848  1.00 6.86  ? 207  GLY A O   1 
ATOM   1502 N  N   . HIS A 1 208  ? 29.923 56.099  -1.734  1.00 5.71  ? 208  HIS A N   1 
ATOM   1503 C  CA  . HIS A 1 208  ? 31.106 55.215  -1.846  1.00 5.73  ? 208  HIS A CA  1 
ATOM   1504 C  C   . HIS A 1 208  ? 31.310 54.586  -3.196  1.00 5.82  ? 208  HIS A C   1 
ATOM   1505 O  O   . HIS A 1 208  ? 30.324 54.257  -3.912  1.00 7.21  ? 208  HIS A O   1 
ATOM   1506 C  CB  . HIS A 1 208  ? 30.998 54.089  -0.764  1.00 6.61  ? 208  HIS A CB  1 
ATOM   1507 C  CG  . HIS A 1 208  ? 31.068 54.627  0.645   1.00 7.38  ? 208  HIS A CG  1 
ATOM   1508 N  ND1 . HIS A 1 208  ? 32.272 54.877  1.273   1.00 8.91  ? 208  HIS A ND1 1 
ATOM   1509 C  CD2 . HIS A 1 208  ? 30.093 54.959  1.526   1.00 8.83  ? 208  HIS A CD2 1 
ATOM   1510 C  CE1 . HIS A 1 208  ? 32.003 55.344  2.506   1.00 8.54  ? 208  HIS A CE1 1 
ATOM   1511 N  NE2 . HIS A 1 208  ? 30.714 55.392  2.683   1.00 10.79 ? 208  HIS A NE2 1 
ATOM   1512 N  N   . SER A 1 209  ? 32.577 54.463  -3.598  1.00 5.49  ? 209  SER A N   1 
ATOM   1513 C  CA  . SER A 1 209  ? 32.967 53.980  -4.901  1.00 5.40  ? 209  SER A CA  1 
ATOM   1514 C  C   . SER A 1 209  ? 33.677 52.635  -4.846  1.00 5.42  ? 209  SER A C   1 
ATOM   1515 O  O   . SER A 1 209  ? 34.497 52.388  -3.966  1.00 5.95  ? 209  SER A O   1 
ATOM   1516 C  CB  . SER A 1 209  ? 33.962 54.980  -5.505  1.00 6.37  ? 209  SER A CB  1 
ATOM   1517 O  OG  . SER A 1 209  ? 34.449 54.468  -6.741  1.00 6.58  ? 209  SER A OG  1 
ATOM   1518 N  N   . PRO A 1 210  ? 33.431 51.750  -5.824  1.00 5.32  ? 210  PRO A N   1 
ATOM   1519 C  CA  . PRO A 1 210  ? 34.128 50.454  -5.861  1.00 6.20  ? 210  PRO A CA  1 
ATOM   1520 C  C   . PRO A 1 210  ? 35.622 50.652  -6.193  1.00 5.60  ? 210  PRO A C   1 
ATOM   1521 O  O   . PRO A 1 210  ? 36.416 49.700  -6.135  1.00 6.26  ? 210  PRO A O   1 
ATOM   1522 C  CB  . PRO A 1 210  ? 33.391 49.672  -6.950  1.00 6.40  ? 210  PRO A CB  1 
ATOM   1523 C  CG  . PRO A 1 210  ? 32.827 50.787  -7.838  1.00 7.94  ? 210  PRO A CG  1 
ATOM   1524 C  CD  . PRO A 1 210  ? 32.422 51.890  -6.891  1.00 7.00  ? 210  PRO A CD  1 
ATOM   1525 N  N   . THR A 1 211  ? 36.042 51.880  -6.580  1.00 6.16  ? 211  THR A N   1 
ATOM   1526 C  CA  . THR A 1 211  ? 37.479 52.086  -6.768  1.00 5.97  ? 211  THR A CA  1 
ATOM   1527 C  C   . THR A 1 211  ? 38.226 51.843  -5.447  1.00 5.67  ? 211  THR A C   1 
ATOM   1528 O  O   . THR A 1 211  ? 39.385 51.461  -5.501  1.00 6.33  ? 211  THR A O   1 
ATOM   1529 C  CB  . THR A 1 211  ? 37.708 53.529  -7.237  1.00 6.64  ? 211  THR A CB  1 
ATOM   1530 O  OG1 . THR A 1 211  ? 37.146 53.608  -8.574  1.00 7.36  ? 211  THR A OG1 1 
ATOM   1531 C  CG2 . THR A 1 211  ? 39.208 53.922  -7.254  1.00 7.87  ? 211  THR A CG2 1 
ATOM   1532 N  N   . MET A 1 212  ? 37.580 52.080  -4.291  1.00 5.96  ? 212  MET A N   1 
ATOM   1533 C  CA  . MET A 1 212  ? 38.252 51.827  -3.019  1.00 5.79  ? 212  MET A CA  1 
ATOM   1534 C  C   . MET A 1 212  ? 38.605 50.338  -2.810  1.00 6.59  ? 212  MET A C   1 
ATOM   1535 O  O   . MET A 1 212  ? 39.764 50.040  -2.615  1.00 6.76  ? 212  MET A O   1 
ATOM   1536 C  CB  . MET A 1 212  ? 37.426 52.405  -1.862  1.00 8.19  ? 212  MET A CB  1 
ATOM   1537 C  CG  A MET A 1 212  ? 37.164 53.911  -1.955  0.50 9.82  ? 212  MET A CG  1 
ATOM   1538 C  CG  B MET A 1 212  ? 38.211 52.439  -0.607  0.50 26.74 ? 212  MET A CG  1 
ATOM   1539 S  SD  A MET A 1 212  ? 38.673 54.892  -2.224  0.50 13.36 ? 212  MET A SD  1 
ATOM   1540 S  SD  B MET A 1 212  ? 39.767 53.362  -0.764  0.50 43.52 ? 212  MET A SD  1 
ATOM   1541 C  CE  A MET A 1 212  ? 39.391 54.811  -0.638  0.50 13.51 ? 212  MET A CE  1 
ATOM   1542 C  CE  B MET A 1 212  ? 39.210 54.996  -0.591  0.50 15.28 ? 212  MET A CE  1 
ATOM   1543 N  N   . PRO A 1 213  ? 37.643 49.391  -2.869  1.00 6.04  ? 213  PRO A N   1 
ATOM   1544 C  CA  . PRO A 1 213  ? 38.068 47.999  -2.689  1.00 6.78  ? 213  PRO A CA  1 
ATOM   1545 C  C   . PRO A 1 213  ? 39.044 47.594  -3.804  1.00 7.76  ? 213  PRO A C   1 
ATOM   1546 O  O   . PRO A 1 213  ? 39.907 46.744  -3.560  1.00 7.67  ? 213  PRO A O   1 
ATOM   1547 C  CB  . PRO A 1 213  ? 36.747 47.219  -2.722  1.00 7.83  ? 213  PRO A CB  1 
ATOM   1548 C  CG  . PRO A 1 213  ? 35.717 48.173  -3.420  1.00 6.74  ? 213  PRO A CG  1 
ATOM   1549 C  CD  . PRO A 1 213  ? 36.173 49.527  -2.848  1.00 6.77  ? 213  PRO A CD  1 
ATOM   1550 N  N   . TYR A 1 214  ? 38.896 48.126  -5.014  1.00 6.72  ? 214  TYR A N   1 
ATOM   1551 C  CA  . TYR A 1 214  ? 39.870 47.840  -6.070  1.00 6.26  ? 214  TYR A CA  1 
ATOM   1552 C  C   . TYR A 1 214  ? 41.296 48.122  -5.627  1.00 7.15  ? 214  TYR A C   1 
ATOM   1553 O  O   . TYR A 1 214  ? 42.144 47.242  -5.711  1.00 7.56  ? 214  TYR A O   1 
ATOM   1554 C  CB  . TYR A 1 214  ? 39.574 48.638  -7.319  1.00 7.56  ? 214  TYR A CB  1 
ATOM   1555 C  CG  . TYR A 1 214  ? 40.510 48.389  -8.500  1.00 7.76  ? 214  TYR A CG  1 
ATOM   1556 C  CD1 . TYR A 1 214  ? 40.310 47.319  -9.358  1.00 13.09 ? 214  TYR A CD1 1 
ATOM   1557 C  CD2 . TYR A 1 214  ? 41.567 49.251  -8.777  1.00 7.83  ? 214  TYR A CD2 1 
ATOM   1558 C  CE1 . TYR A 1 214  ? 41.127 47.113  -10.458 1.00 14.71 ? 214  TYR A CE1 1 
ATOM   1559 C  CE2 . TYR A 1 214  ? 42.383 49.045  -9.878  1.00 8.24  ? 214  TYR A CE2 1 
ATOM   1560 C  CZ  . TYR A 1 214  ? 42.147 47.988  -10.713 1.00 11.94 ? 214  TYR A CZ  1 
ATOM   1561 O  OH  . TYR A 1 214  ? 42.947 47.799  -11.803 1.00 12.76 ? 214  TYR A OH  1 
ATOM   1562 N  N   . ILE A 1 215  ? 41.549 49.352  -5.190  1.00 6.07  ? 215  ILE A N   1 
ATOM   1563 C  CA  . ILE A 1 215  ? 42.892 49.721  -4.754  1.00 5.43  ? 215  ILE A CA  1 
ATOM   1564 C  C   . ILE A 1 215  ? 43.290 48.988  -3.461  1.00 6.21  ? 215  ILE A C   1 
ATOM   1565 O  O   . ILE A 1 215  ? 44.411 48.507  -3.338  1.00 6.54  ? 215  ILE A O   1 
ATOM   1566 C  CB  . ILE A 1 215  ? 42.946 51.248  -4.529  1.00 5.99  ? 215  ILE A CB  1 
ATOM   1567 C  CG1 . ILE A 1 215  ? 42.783 51.976  -5.851  1.00 7.07  ? 215  ILE A CG1 1 
ATOM   1568 C  CG2 . ILE A 1 215  ? 44.272 51.632  -3.840  1.00 8.07  ? 215  ILE A CG2 1 
ATOM   1569 C  CD1 . ILE A 1 215  ? 42.689 53.489  -5.720  1.00 10.52 ? 215  ILE A CD1 1 
ATOM   1570 N  N   . LEU A 1 216  ? 42.364 48.919  -2.509  1.00 5.72  ? 216  LEU A N   1 
ATOM   1571 C  CA  . LEU A 1 216  ? 42.700 48.303  -1.194  1.00 6.65  ? 216  LEU A CA  1 
ATOM   1572 C  C   . LEU A 1 216  ? 43.038 46.822  -1.357  1.00 6.80  ? 216  LEU A C   1 
ATOM   1573 O  O   . LEU A 1 216  ? 44.014 46.370  -0.749  1.00 6.64  ? 216  LEU A O   1 
ATOM   1574 C  CB  . LEU A 1 216  ? 41.514 48.478  -0.251  1.00 5.97  ? 216  LEU A CB  1 
ATOM   1575 C  CG  . LEU A 1 216  ? 41.137 49.925  0.119   1.00 6.74  ? 216  LEU A CG  1 
ATOM   1576 C  CD1 . LEU A 1 216  ? 39.835 49.891  0.890   1.00 7.90  ? 216  LEU A CD1 1 
ATOM   1577 C  CD2 . LEU A 1 216  ? 42.250 50.613  0.977   1.00 8.92  ? 216  LEU A CD2 1 
ATOM   1578 N  N   . GLN A 1 217  ? 42.281 46.096  -2.160  1.00 6.84  ? 217  GLN A N   1 
ATOM   1579 C  CA  . GLN A 1 217  ? 42.570 44.658  -2.311  1.00 7.26  ? 217  GLN A CA  1 
ATOM   1580 C  C   . GLN A 1 217  ? 43.911 44.437  -2.983  1.00 7.48  ? 217  GLN A C   1 
ATOM   1581 O  O   . GLN A 1 217  ? 44.555 43.419  -2.732  1.00 10.61 ? 217  GLN A O   1 
ATOM   1582 C  CB  . GLN A 1 217  ? 41.380 44.045  -3.059  1.00 8.40  ? 217  GLN A CB  1 
ATOM   1583 C  CG  . GLN A 1 217  ? 41.407 42.486  -3.133  1.00 9.74  ? 217  GLN A CG  1 
ATOM   1584 C  CD  . GLN A 1 217  ? 42.244 41.974  -4.239  1.00 13.06 ? 217  GLN A CD  1 
ATOM   1585 O  OE1 . GLN A 1 217  ? 42.317 42.588  -5.295  1.00 13.08 ? 217  GLN A OE1 1 
ATOM   1586 N  NE2 . GLN A 1 217  ? 42.867 40.788  -4.045  1.00 15.04 ? 217  GLN A NE2 1 
ATOM   1587 N  N   . LYS A 1 218  ? 44.371 45.372  -3.825  1.00 6.39  ? 218  LYS A N   1 
ATOM   1588 C  CA  . LYS A 1 218  ? 45.674 45.281  -4.478  1.00 6.86  ? 218  LYS A CA  1 
ATOM   1589 C  C   . LYS A 1 218  ? 46.806 45.878  -3.591  1.00 7.48  ? 218  LYS A C   1 
ATOM   1590 O  O   . LYS A 1 218  ? 47.963 45.956  -4.022  1.00 7.94  ? 218  LYS A O   1 
ATOM   1591 C  CB  . LYS A 1 218  ? 45.617 45.979  -5.816  1.00 7.87  ? 218  LYS A CB  1 
ATOM   1592 C  CG  . LYS A 1 218  ? 44.846 45.148  -6.876  1.00 9.18  ? 218  LYS A CG  1 
ATOM   1593 C  CD  . LYS A 1 218  ? 44.529 45.992  -8.140  1.00 9.55  ? 218  LYS A CD  1 
ATOM   1594 C  CE  . LYS A 1 218  ? 44.139 45.164  -9.347  1.00 13.90 ? 218  LYS A CE  1 
ATOM   1595 N  NZ  . LYS A 1 218  ? 43.070 44.135  -9.141  1.00 13.65 ? 218  LYS A NZ  1 
ATOM   1596 N  N   . SER A 1 219  ? 46.443 46.307  -2.393  1.00 6.49  ? 219  SER A N   1 
ATOM   1597 C  CA  . SER A 1 219  ? 47.354 46.911  -1.413  1.00 7.11  ? 219  SER A CA  1 
ATOM   1598 C  C   . SER A 1 219  ? 47.367 46.103  -0.107  1.00 7.32  ? 219  SER A C   1 
ATOM   1599 O  O   . SER A 1 219  ? 47.706 46.653  0.954   1.00 7.88  ? 219  SER A O   1 
ATOM   1600 C  CB  . SER A 1 219  ? 46.973 48.386  -1.150  1.00 7.05  ? 219  SER A CB  1 
ATOM   1601 O  OG  . SER A 1 219  ? 47.014 49.102  -2.431  1.00 7.79  ? 219  SER A OG  1 
ATOM   1602 N  N   . GLY A 1 220  ? 46.986 44.823  -0.195  1.00 7.87  ? 220  GLY A N   1 
ATOM   1603 C  CA  . GLY A 1 220  ? 47.035 43.932  0.972   1.00 7.96  ? 220  GLY A CA  1 
ATOM   1604 C  C   . GLY A 1 220  ? 45.847 43.923  1.879   1.00 7.88  ? 220  GLY A C   1 
ATOM   1605 O  O   . GLY A 1 220  ? 45.851 43.143  2.836   1.00 9.45  ? 220  GLY A O   1 
ATOM   1606 N  N   . PHE A 1 221  ? 44.800 44.689  1.617   1.00 7.60  ? 221  PHE A N   1 
ATOM   1607 C  CA  . PHE A 1 221  ? 43.682 44.712  2.549   1.00 6.78  ? 221  PHE A CA  1 
ATOM   1608 C  C   . PHE A 1 221  ? 42.866 43.470  2.487   1.00 7.44  ? 221  PHE A C   1 
ATOM   1609 O  O   . PHE A 1 221  ? 42.776 42.811  1.437   1.00 8.90  ? 221  PHE A O   1 
ATOM   1610 C  CB  . PHE A 1 221  ? 42.791 45.942  2.269   1.00 6.62  ? 221  PHE A CB  1 
ATOM   1611 C  CG  . PHE A 1 221  ? 43.348 47.212  2.808   1.00 5.81  ? 221  PHE A CG  1 
ATOM   1612 C  CD1 . PHE A 1 221  ? 44.463 47.835  2.232   1.00 6.23  ? 221  PHE A CD1 1 
ATOM   1613 C  CD2 . PHE A 1 221  ? 42.755 47.813  3.929   1.00 6.69  ? 221  PHE A CD2 1 
ATOM   1614 C  CE1 . PHE A 1 221  ? 44.986 49.026  2.776   1.00 5.64  ? 221  PHE A CE1 1 
ATOM   1615 C  CE2 . PHE A 1 221  ? 43.284 48.995  4.450   1.00 7.05  ? 221  PHE A CE2 1 
ATOM   1616 C  CZ  . PHE A 1 221  ? 44.412 49.623  3.875   1.00 6.27  ? 221  PHE A CZ  1 
ATOM   1617 N  N   . LYS A 1 222  ? 42.183 43.206  3.591   1.00 8.10  ? 222  LYS A N   1 
ATOM   1618 C  CA  . LYS A 1 222  ? 41.281 42.049  3.726   1.00 8.13  ? 222  LYS A CA  1 
ATOM   1619 C  C   . LYS A 1 222  ? 39.874 42.457  4.082   1.00 8.19  ? 222  LYS A C   1 
ATOM   1620 O  O   . LYS A 1 222  ? 38.962 41.676  3.871   1.00 8.43  ? 222  LYS A O   1 
ATOM   1621 C  CB  . LYS A 1 222  ? 41.800 41.099  4.808   1.00 11.06 ? 222  LYS A CB  1 
ATOM   1622 C  CG  . LYS A 1 222  ? 43.196 40.533  4.509   1.00 14.19 ? 222  LYS A CG  1 
ATOM   1623 C  CD  . LYS A 1 222  ? 43.263 39.876  3.120   1.00 23.16 ? 222  LYS A CD  1 
ATOM   1624 C  CE  . LYS A 1 222  ? 44.422 38.838  2.916   1.00 31.14 ? 222  LYS A CE  1 
ATOM   1625 N  NZ  . LYS A 1 222  ? 45.787 39.425  2.703   1.00 36.02 ? 222  LYS A NZ  1 
ATOM   1626 N  N   . ASN A 1 223  ? 39.647 43.676  4.560   1.00 6.45  ? 223  ASN A N   1 
ATOM   1627 C  CA  . ASN A 1 223  ? 38.315 44.091  5.012   1.00 6.81  ? 223  ASN A CA  1 
ATOM   1628 C  C   . ASN A 1 223  ? 38.156 45.595  4.868   1.00 6.32  ? 223  ASN A C   1 
ATOM   1629 O  O   . ASN A 1 223  ? 39.120 46.321  4.944   1.00 6.92  ? 223  ASN A O   1 
ATOM   1630 C  CB  . ASN A 1 223  ? 38.122 43.720  6.494   1.00 7.30  ? 223  ASN A CB  1 
ATOM   1631 C  CG  . ASN A 1 223  ? 38.094 42.223  6.742   1.00 8.90  ? 223  ASN A CG  1 
ATOM   1632 O  OD1 . ASN A 1 223  ? 37.118 41.559  6.461   1.00 11.35 ? 223  ASN A OD1 1 
ATOM   1633 N  ND2 . ASN A 1 223  ? 39.191 41.695  7.260   1.00 7.06  ? 223  ASN A ND2 1 
ATOM   1634 N  N   . MET A 1 224  ? 36.916 46.045  4.708   1.00 6.49  ? 224  MET A N   1 
ATOM   1635 C  CA  . MET A 1 224  ? 36.643 47.498  4.711   1.00 6.16  ? 224  MET A CA  1 
ATOM   1636 C  C   . MET A 1 224  ? 35.236 47.780  5.257   1.00 6.25  ? 224  MET A C   1 
ATOM   1637 O  O   . MET A 1 224  ? 34.352 46.891  5.242   1.00 7.34  ? 224  MET A O   1 
ATOM   1638 C  CB  . MET A 1 224  ? 36.787 48.084  3.312   1.00 8.78  ? 224  MET A CB  1 
ATOM   1639 C  CG  . MET A 1 224  ? 35.772 47.589  2.300   1.00 7.96  ? 224  MET A CG  1 
ATOM   1640 S  SD  . MET A 1 224  ? 35.922 48.307  0.650   1.00 9.36  ? 224  MET A SD  1 
ATOM   1641 C  CE  . MET A 1 224  ? 35.695 50.000  1.017   1.00 13.35 ? 224  MET A CE  1 
ATOM   1642 N  N   . LEU A 1 225  ? 35.091 49.010  5.755   1.00 6.42  ? 225  LEU A N   1 
ATOM   1643 C  CA  . LEU A 1 225  ? 33.823 49.446  6.309   1.00 6.23  ? 225  LEU A CA  1 
ATOM   1644 C  C   . LEU A 1 225  ? 33.421 50.767  5.676   1.00 6.89  ? 225  LEU A C   1 
ATOM   1645 O  O   . LEU A 1 225  ? 34.278 51.663  5.488   1.00 6.73  ? 225  LEU A O   1 
ATOM   1646 C  CB  . LEU A 1 225  ? 33.987 49.592  7.847   1.00 7.79  ? 225  LEU A CB  1 
ATOM   1647 C  CG  . LEU A 1 225  ? 32.785 50.223  8.580   1.00 7.16  ? 225  LEU A CG  1 
ATOM   1648 C  CD1 . LEU A 1 225  ? 32.700 49.616  10.000  1.00 8.55  ? 225  LEU A CD1 1 
ATOM   1649 C  CD2 . LEU A 1 225  ? 32.886 51.743  8.616   1.00 8.42  ? 225  LEU A CD2 1 
ATOM   1650 N  N   . ILE A 1 226  ? 32.132 50.879  5.389   1.00 5.88  ? 226  ILE A N   1 
ATOM   1651 C  CA  . ILE A 1 226  ? 31.535 52.109  4.815   1.00 6.60  ? 226  ILE A CA  1 
ATOM   1652 C  C   . ILE A 1 226  ? 30.307 52.510  5.583   1.00 6.84  ? 226  ILE A C   1 
ATOM   1653 O  O   . ILE A 1 226  ? 29.704 51.659  6.292   1.00 7.47  ? 226  ILE A O   1 
ATOM   1654 C  CB  . ILE A 1 226  ? 31.251 51.925  3.276   1.00 6.52  ? 226  ILE A CB  1 
ATOM   1655 C  CG1 . ILE A 1 226  ? 30.208 50.827  3.034   1.00 6.58  ? 226  ILE A CG1 1 
ATOM   1656 C  CG2 . ILE A 1 226  ? 32.554 51.619  2.568   1.00 7.59  ? 226  ILE A CG2 1 
ATOM   1657 C  CD1 . ILE A 1 226  ? 29.797 50.705  1.549   1.00 8.92  ? 226  ILE A CD1 1 
ATOM   1658 N  N   . GLN A 1 227  ? 29.875 53.749  5.429   1.00 7.88  ? 227  GLN A N   1 
ATOM   1659 C  CA  . GLN A 1 227  ? 28.729 54.249  6.186   1.00 8.05  ? 227  GLN A CA  1 
ATOM   1660 C  C   . GLN A 1 227  ? 27.719 55.072  5.374   1.00 7.78  ? 227  GLN A C   1 
ATOM   1661 O  O   . GLN A 1 227  ? 26.502 54.831  5.515   1.00 8.56  ? 227  GLN A O   1 
ATOM   1662 C  CB  . GLN A 1 227  ? 29.244 55.133  7.344   1.00 8.64  ? 227  GLN A CB  1 
ATOM   1663 C  CG  . GLN A 1 227  ? 28.223 56.211  7.902   1.00 10.90 ? 227  GLN A CG  1 
ATOM   1664 C  CD  . GLN A 1 227  ? 26.915 55.679  8.459   1.00 9.96  ? 227  GLN A CD  1 
ATOM   1665 O  OE1 . GLN A 1 227  ? 26.854 54.522  8.923   1.00 12.85 ? 227  GLN A OE1 1 
ATOM   1666 N  NE2 . GLN A 1 227  ? 25.877 56.506  8.444   1.00 11.23 ? 227  GLN A NE2 1 
ATOM   1667 N  N   . ARG A 1 228  ? 28.145 56.041  4.564   1.00 7.18  ? 228  ARG A N   1 
ATOM   1668 C  CA  . ARG A 1 228  ? 27.156 56.901  3.936   1.00 7.61  ? 228  ARG A CA  1 
ATOM   1669 C  C   . ARG A 1 228  ? 26.644 56.379  2.629   1.00 7.94  ? 228  ARG A C   1 
ATOM   1670 O  O   . ARG A 1 228  ? 27.211 56.621  1.547   1.00 8.49  ? 228  ARG A O   1 
ATOM   1671 C  CB  . ARG A 1 228  ? 27.710 58.344  3.732   1.00 7.52  ? 228  ARG A CB  1 
ATOM   1672 C  CG  . ARG A 1 228  ? 27.933 59.072  5.034   1.00 7.09  ? 228  ARG A CG  1 
ATOM   1673 C  CD  . ARG A 1 228  ? 28.220 60.578  4.746   1.00 8.26  ? 228  ARG A CD  1 
ATOM   1674 N  NE  . ARG A 1 228  ? 28.494 61.320  5.984   1.00 7.82  ? 228  ARG A NE  1 
ATOM   1675 C  CZ  . ARG A 1 228  ? 27.560 61.790  6.804   1.00 9.96  ? 228  ARG A CZ  1 
ATOM   1676 N  NH1 . ARG A 1 228  ? 26.249 61.640  6.557   1.00 12.04 ? 228  ARG A NH1 1 
ATOM   1677 N  NH2 . ARG A 1 228  ? 27.941 62.338  7.957   1.00 11.43 ? 228  ARG A NH2 1 
ATOM   1678 N  N   . THR A 1 229  ? 25.587 55.574  2.737   1.00 7.42  ? 229  THR A N   1 
ATOM   1679 C  CA  . THR A 1 229  ? 24.876 55.044  1.568   1.00 6.14  ? 229  THR A CA  1 
ATOM   1680 C  C   . THR A 1 229  ? 23.433 55.465  1.746   1.00 7.25  ? 229  THR A C   1 
ATOM   1681 O  O   . THR A 1 229  ? 22.941 55.738  2.863   1.00 7.83  ? 229  THR A O   1 
ATOM   1682 C  CB  . THR A 1 229  ? 24.984 53.508  1.463   1.00 8.31  ? 229  THR A CB  1 
ATOM   1683 O  OG1 . THR A 1 229  ? 24.360 52.938  2.623   1.00 8.84  ? 229  THR A OG1 1 
ATOM   1684 C  CG2 . THR A 1 229  ? 26.438 53.121  1.371   1.00 7.82  ? 229  THR A CG2 1 
ATOM   1685 N  N   . HIS A 1 230  ? 22.720 55.548  0.630   1.00 7.77  ? 230  HIS A N   1 
ATOM   1686 C  CA  . HIS A 1 230  ? 21.324 55.996  0.622   1.00 8.30  ? 230  HIS A CA  1 
ATOM   1687 C  C   . HIS A 1 230  ? 20.502 55.248  1.669   1.00 7.13  ? 230  HIS A C   1 
ATOM   1688 O  O   . HIS A 1 230  ? 20.570 54.014  1.745   1.00 8.55  ? 230  HIS A O   1 
ATOM   1689 C  CB  . HIS A 1 230  ? 20.774 55.754  -0.783  1.00 8.87  ? 230  HIS A CB  1 
ATOM   1690 C  CG  . HIS A 1 230  ? 19.487 56.442  -1.105  1.00 8.38  ? 230  HIS A CG  1 
ATOM   1691 N  ND1 . HIS A 1 230  ? 18.309 56.206  -0.407  1.00 9.03  ? 230  HIS A ND1 1 
ATOM   1692 C  CD2 . HIS A 1 230  ? 19.181 57.328  -2.083  1.00 10.44 ? 230  HIS A CD2 1 
ATOM   1693 C  CE1 . HIS A 1 230  ? 17.342 56.947  -0.937  1.00 9.25  ? 230  HIS A CE1 1 
ATOM   1694 N  NE2 . HIS A 1 230  ? 17.852 57.630  -1.962  1.00 8.97  ? 230  HIS A NE2 1 
ATOM   1695 N  N   . TYR A 1 231  ? 19.669 56.001  2.403   1.00 7.52  ? 231  TYR A N   1 
ATOM   1696 C  CA  . TYR A 1 231  ? 18.876 55.359  3.451   1.00 7.38  ? 231  TYR A CA  1 
ATOM   1697 C  C   . TYR A 1 231  ? 18.007 54.244  2.876   1.00 9.24  ? 231  TYR A C   1 
ATOM   1698 O  O   . TYR A 1 231  ? 17.718 53.294  3.603   1.00 9.88  ? 231  TYR A O   1 
ATOM   1699 C  CB  . TYR A 1 231  ? 18.038 56.396  4.209   1.00 9.25  ? 231  TYR A CB  1 
ATOM   1700 C  CG  . TYR A 1 231  ? 17.061 57.179  3.328   1.00 10.02 ? 231  TYR A CG  1 
ATOM   1701 C  CD1 . TYR A 1 231  ? 15.751 56.707  3.133   1.00 10.58 ? 231  TYR A CD1 1 
ATOM   1702 C  CD2 . TYR A 1 231  ? 17.422 58.404  2.739   1.00 8.36  ? 231  TYR A CD2 1 
ATOM   1703 C  CE1 . TYR A 1 231  ? 14.838 57.444  2.399   1.00 9.98  ? 231  TYR A CE1 1 
ATOM   1704 C  CE2 . TYR A 1 231  ? 16.503 59.155  1.976   1.00 8.81  ? 231  TYR A CE2 1 
ATOM   1705 C  CZ  . TYR A 1 231  ? 15.211 58.647  1.829   1.00 8.88  ? 231  TYR A CZ  1 
ATOM   1706 O  OH  . TYR A 1 231  ? 14.277 59.385  1.090   1.00 10.64 ? 231  TYR A OH  1 
ATOM   1707 N  N   . SER A 1 232  ? 17.536 54.341  1.645   1.00 8.83  ? 232  SER A N   1 
ATOM   1708 C  CA  . SER A 1 232  ? 16.691 53.252  1.111   1.00 9.83  ? 232  SER A CA  1 
ATOM   1709 C  C   . SER A 1 232  ? 17.500 52.018  0.863   1.00 10.10 ? 232  SER A C   1 
ATOM   1710 O  O   . SER A 1 232  ? 17.019 50.878  0.955   1.00 9.43  ? 232  SER A O   1 
ATOM   1711 C  CB  . SER A 1 232  ? 16.016 53.658  -0.188  1.00 11.00 ? 232  SER A CB  1 
ATOM   1712 O  OG  . SER A 1 232  ? 15.150 54.763  -0.001  1.00 12.86 ? 232  SER A OG  1 
ATOM   1713 N  N   . VAL A 1 233  ? 18.775 52.204  0.479   1.00 8.50  ? 233  VAL A N   1 
ATOM   1714 C  CA  . VAL A 1 233  ? 19.691 51.075  0.286   1.00 9.03  ? 233  VAL A CA  1 
ATOM   1715 C  C   . VAL A 1 233  ? 19.966 50.379  1.646   1.00 8.38  ? 233  VAL A C   1 
ATOM   1716 O  O   . VAL A 1 233  ? 19.936 49.128  1.701   1.00 9.83  ? 233  VAL A O   1 
ATOM   1717 C  CB  . VAL A 1 233  ? 21.038 51.527  -0.378  1.00 8.58  ? 233  VAL A CB  1 
ATOM   1718 C  CG1 . VAL A 1 233  ? 22.040 50.370  -0.389  1.00 9.28  ? 233  VAL A CG1 1 
ATOM   1719 C  CG2 . VAL A 1 233  ? 20.707 51.896  -1.847  1.00 10.34 ? 233  VAL A CG2 1 
ATOM   1720 N  N   . LYS A 1 234  ? 20.263 51.140  2.693   1.00 8.72  ? 234  LYS A N   1 
ATOM   1721 C  CA  . LYS A 1 234  ? 20.445 50.511  4.018   1.00 9.06  ? 234  LYS A CA  1 
ATOM   1722 C  C   . LYS A 1 234  ? 19.208 49.686  4.398   1.00 9.62  ? 234  LYS A C   1 
ATOM   1723 O  O   . LYS A 1 234  ? 19.394 48.543  4.852   1.00 9.50  ? 234  LYS A O   1 
ATOM   1724 C  CB  . LYS A 1 234  ? 20.664 51.607  5.042   1.00 8.14  ? 234  LYS A CB  1 
ATOM   1725 C  CG  . LYS A 1 234  ? 22.053 52.259  4.938   1.00 9.56  ? 234  LYS A CG  1 
ATOM   1726 C  CD  . LYS A 1 234  ? 22.094 53.539  5.722   1.00 9.40  ? 234  LYS A CD  1 
ATOM   1727 C  CE  . LYS A 1 234  ? 23.529 54.178  5.704   1.00 9.13  ? 234  LYS A CE  1 
ATOM   1728 N  NZ  . LYS A 1 234  ? 24.413 53.628  6.834   1.00 8.60  ? 234  LYS A NZ  1 
ATOM   1729 N  N   . LYS A 1 235  ? 18.009 50.196  4.177   1.00 8.81  ? 235  LYS A N   1 
ATOM   1730 C  CA  . LYS A 1 235  ? 16.799 49.460  4.546   1.00 9.02  ? 235  LYS A CA  1 
ATOM   1731 C  C   . LYS A 1 235  ? 16.678 48.167  3.742   1.00 9.89  ? 235  LYS A C   1 
ATOM   1732 O  O   . LYS A 1 235  ? 16.380 47.125  4.300   1.00 10.93 ? 235  LYS A O   1 
ATOM   1733 C  CB  . LYS A 1 235  ? 15.550 50.337  4.387   1.00 11.21 ? 235  LYS A CB  1 
ATOM   1734 C  CG  . LYS A 1 235  ? 14.245 49.647  4.812   1.00 11.74 ? 235  LYS A CG  1 
ATOM   1735 C  CD  . LYS A 1 235  ? 13.096 50.622  4.694   1.00 13.01 ? 235  LYS A CD  1 
ATOM   1736 C  CE  . LYS A 1 235  ? 11.776 50.037  5.187   1.00 16.32 ? 235  LYS A CE  1 
ATOM   1737 N  NZ  . LYS A 1 235  ? 10.613 50.950  4.971   1.00 20.58 ? 235  LYS A NZ  1 
ATOM   1738 N  N   . GLU A 1 236  ? 16.900 48.234  2.437   1.00 9.57  ? 236  GLU A N   1 
ATOM   1739 C  CA  . GLU A 1 236  ? 16.786 47.078  1.570   1.00 11.07 ? 236  GLU A CA  1 
ATOM   1740 C  C   . GLU A 1 236  ? 17.776 46.001  1.910   1.00 11.74 ? 236  GLU A C   1 
ATOM   1741 O  O   . GLU A 1 236  ? 17.440 44.817  2.021   1.00 12.53 ? 236  GLU A O   1 
ATOM   1742 C  CB  . GLU A 1 236  ? 17.004 47.554  0.112   1.00 12.83 ? 236  GLU A CB  1 
ATOM   1743 C  CG  . GLU A 1 236  ? 16.734 46.492  -0.947  1.00 21.91 ? 236  GLU A CG  1 
ATOM   1744 C  CD  . GLU A 1 236  ? 15.214 46.193  -1.068  1.00 30.06 ? 236  GLU A CD  1 
ATOM   1745 O  OE1 . GLU A 1 236  ? 14.386 47.029  -0.634  1.00 30.80 ? 236  GLU A OE1 1 
ATOM   1746 O  OE2 . GLU A 1 236  ? 14.872 45.136  -1.611  1.00 32.77 ? 236  GLU A OE2 1 
ATOM   1747 N  N   . LEU A 1 237  ? 19.053 46.363  2.044   1.00 9.96  ? 237  LEU A N   1 
ATOM   1748 C  CA  . LEU A 1 237  ? 20.081 45.396  2.360   1.00 9.15  ? 237  LEU A CA  1 
ATOM   1749 C  C   . LEU A 1 237  ? 19.879 44.889  3.798   1.00 9.94  ? 237  LEU A C   1 
ATOM   1750 O  O   . LEU A 1 237  ? 20.081 43.670  4.044   1.00 11.06 ? 237  LEU A O   1 
ATOM   1751 C  CB  . LEU A 1 237  ? 21.493 45.984  2.223   1.00 8.69  ? 237  LEU A CB  1 
ATOM   1752 C  CG  . LEU A 1 237  ? 21.818 46.428  0.758   1.00 10.26 ? 237  LEU A CG  1 
ATOM   1753 C  CD1 . LEU A 1 237  ? 23.264 46.986  0.782   1.00 12.86 ? 237  LEU A CD1 1 
ATOM   1754 C  CD2 . LEU A 1 237  ? 21.709 45.283  -0.283  1.00 12.30 ? 237  LEU A CD2 1 
ATOM   1755 N  N   . ALA A 1 238  ? 19.454 45.723  4.726   1.00 10.30 ? 238  ALA A N   1 
ATOM   1756 C  CA  . ALA A 1 238  ? 19.263 45.249  6.115   1.00 10.25 ? 238  ALA A CA  1 
ATOM   1757 C  C   . ALA A 1 238  ? 18.185 44.148  6.150   1.00 11.40 ? 238  ALA A C   1 
ATOM   1758 O  O   . ALA A 1 238  ? 18.356 43.119  6.846   1.00 12.14 ? 238  ALA A O   1 
ATOM   1759 C  CB  . ALA A 1 238  ? 18.873 46.409  7.028   1.00 11.78 ? 238  ALA A CB  1 
ATOM   1760 N  N   . GLN A 1 239  ? 17.127 44.315  5.377   1.00 10.72 ? 239  GLN A N   1 
ATOM   1761 C  CA  . GLN A 1 239  ? 16.037 43.301  5.402   1.00 12.05 ? 239  GLN A CA  1 
ATOM   1762 C  C   . GLN A 1 239  ? 16.508 41.944  4.926   1.00 14.82 ? 239  GLN A C   1 
ATOM   1763 O  O   . GLN A 1 239  ? 15.940 40.918  5.352   1.00 16.68 ? 239  GLN A O   1 
ATOM   1764 C  CB  . GLN A 1 239  ? 14.868 43.782  4.532   1.00 14.99 ? 239  GLN A CB  1 
ATOM   1765 C  CG  . GLN A 1 239  ? 14.077 44.914  5.190   1.00 19.13 ? 239  GLN A CG  1 
ATOM   1766 C  CD  . GLN A 1 239  ? 13.041 45.628  4.298   1.00 25.94 ? 239  GLN A CD  1 
ATOM   1767 O  OE1 . GLN A 1 239  ? 13.138 45.654  3.084   1.00 29.92 ? 239  GLN A OE1 1 
ATOM   1768 N  NE2 . GLN A 1 239  ? 12.055 46.254  4.942   1.00 31.64 ? 239  GLN A NE2 1 
ATOM   1769 N  N   . GLN A 1 240  ? 17.494 41.918  4.034   1.00 11.64 ? 240  GLN A N   1 
ATOM   1770 C  CA  . GLN A 1 240  ? 18.038 40.682  3.490   1.00 12.08 ? 240  GLN A CA  1 
ATOM   1771 C  C   . GLN A 1 240  ? 19.300 40.221  4.210   1.00 9.98  ? 240  GLN A C   1 
ATOM   1772 O  O   . GLN A 1 240  ? 19.889 39.260  3.828   1.00 11.24 ? 240  GLN A O   1 
ATOM   1773 C  CB  . GLN A 1 240  ? 18.356 40.855  2.013   1.00 15.00 ? 240  GLN A CB  1 
ATOM   1774 C  CG  . GLN A 1 240  ? 17.201 41.361  1.196   1.00 21.01 ? 240  GLN A CG  1 
ATOM   1775 C  CD  . GLN A 1 240  ? 16.040 40.412  1.238   1.00 26.56 ? 240  GLN A CD  1 
ATOM   1776 O  OE1 . GLN A 1 240  ? 16.199 39.198  1.223   1.00 32.34 ? 240  GLN A OE1 1 
ATOM   1777 N  NE2 . GLN A 1 240  ? 14.854 40.970  1.301   1.00 25.34 ? 240  GLN A NE2 1 
ATOM   1778 N  N   . ARG A 1 241  ? 19.707 40.946  5.240   1.00 10.08 ? 241  ARG A N   1 
ATOM   1779 C  CA  . ARG A 1 241  ? 20.997 40.717  5.916   1.00 10.70 ? 241  ARG A CA  1 
ATOM   1780 C  C   . ARG A 1 241  ? 22.131 40.693  4.907   1.00 10.32 ? 241  ARG A C   1 
ATOM   1781 O  O   . ARG A 1 241  ? 22.981 39.785  4.850   1.00 9.94  ? 241  ARG A O   1 
ATOM   1782 C  CB  . ARG A 1 241  ? 21.036 39.412  6.748   1.00 11.23 ? 241  ARG A CB  1 
ATOM   1783 C  CG  . ARG A 1 241  ? 19.970 39.485  7.868   1.00 13.26 ? 241  ARG A CG  1 
ATOM   1784 C  CD  . ARG A 1 241  ? 20.070 38.346  8.906   1.00 13.40 ? 241  ARG A CD  1 
ATOM   1785 N  NE  . ARG A 1 241  ? 20.108 37.044  8.265   1.00 20.16 ? 241  ARG A NE  1 
ATOM   1786 C  CZ  . ARG A 1 241  ? 20.556 35.942  8.872   1.00 18.98 ? 241  ARG A CZ  1 
ATOM   1787 N  NH1 . ARG A 1 241  ? 20.977 36.005  10.143  1.00 20.54 ? 241  ARG A NH1 1 
ATOM   1788 N  NH2 . ARG A 1 241  ? 20.647 34.788  8.201   1.00 24.65 ? 241  ARG A NH2 1 
ATOM   1789 N  N   . GLN A 1 242  ? 22.136 41.740  4.052   1.00 9.08  ? 242  GLN A N   1 
ATOM   1790 C  CA  . GLN A 1 242  ? 23.172 41.878  2.986   1.00 8.82  ? 242  GLN A CA  1 
ATOM   1791 C  C   . GLN A 1 242  ? 24.030 43.113  3.244   1.00 9.04  ? 242  GLN A C   1 
ATOM   1792 O  O   . GLN A 1 242  ? 24.573 43.660  2.281   1.00 10.23 ? 242  GLN A O   1 
ATOM   1793 C  CB  . GLN A 1 242  ? 22.481 41.961  1.606   1.00 8.96  ? 242  GLN A CB  1 
ATOM   1794 C  CG  . GLN A 1 242  ? 21.898 40.590  1.179   1.00 11.40 ? 242  GLN A CG  1 
ATOM   1795 C  CD  . GLN A 1 242  ? 21.028 40.699  -0.079  1.00 11.27 ? 242  GLN A CD  1 
ATOM   1796 O  OE1 . GLN A 1 242  ? 20.494 41.757  -0.363  1.00 12.88 ? 242  GLN A OE1 1 
ATOM   1797 N  NE2 . GLN A 1 242  ? 20.948 39.599  -0.846  1.00 13.84 ? 242  GLN A NE2 1 
ATOM   1798 N  N   . LEU A 1 243  ? 24.112 43.537  4.512   1.00 8.09  ? 243  LEU A N   1 
ATOM   1799 C  CA  . LEU A 1 243  ? 24.977 44.682  4.857   1.00 6.90  ? 243  LEU A CA  1 
ATOM   1800 C  C   . LEU A 1 243  ? 26.443 44.293  4.910   1.00 7.28  ? 243  LEU A C   1 
ATOM   1801 O  O   . LEU A 1 243  ? 27.307 45.198  4.907   1.00 9.53  ? 243  LEU A O   1 
ATOM   1802 C  CB  . LEU A 1 243  ? 24.522 45.258  6.185   1.00 8.17  ? 243  LEU A CB  1 
ATOM   1803 C  CG  . LEU A 1 243  ? 23.135 45.898  6.135   1.00 9.83  ? 243  LEU A CG  1 
ATOM   1804 C  CD1 . LEU A 1 243  ? 22.666 46.098  7.593   1.00 11.49 ? 243  LEU A CD1 1 
ATOM   1805 C  CD2 . LEU A 1 243  ? 23.133 47.296  5.448   1.00 10.93 ? 243  LEU A CD2 1 
ATOM   1806 N  N   . GLU A 1 244  ? 26.775 43.005  4.973   1.00 7.34  ? 244  GLU A N   1 
ATOM   1807 C  CA  . GLU A 1 244  ? 28.152 42.556  4.837   1.00 7.38  ? 244  GLU A CA  1 
ATOM   1808 C  C   . GLU A 1 244  ? 28.160 41.769  3.560   1.00 7.73  ? 244  GLU A C   1 
ATOM   1809 O  O   . GLU A 1 244  ? 27.341 40.833  3.338   1.00 8.85  ? 244  GLU A O   1 
ATOM   1810 C  CB  . GLU A 1 244  ? 28.630 41.689  6.025   1.00 7.52  ? 244  GLU A CB  1 
ATOM   1811 C  CG  . GLU A 1 244  ? 28.943 42.603  7.239   1.00 9.22  ? 244  GLU A CG  1 
ATOM   1812 C  CD  . GLU A 1 244  ? 29.251 41.929  8.552   1.00 9.59  ? 244  GLU A CD  1 
ATOM   1813 O  OE1 . GLU A 1 244  ? 28.662 40.849  8.842   1.00 9.88  ? 244  GLU A OE1 1 
ATOM   1814 O  OE2 . GLU A 1 244  ? 30.086 42.495  9.310   1.00 9.76  ? 244  GLU A OE2 1 
ATOM   1815 N  N   . PHE A 1 245  ? 29.127 42.053  2.695   1.00 7.67  ? 245  PHE A N   1 
ATOM   1816 C  CA  . PHE A 1 245  ? 29.168 41.436  1.370   1.00 6.85  ? 245  PHE A CA  1 
ATOM   1817 C  C   . PHE A 1 245  ? 30.571 41.409  0.810   1.00 6.98  ? 245  PHE A C   1 
ATOM   1818 O  O   . PHE A 1 245  ? 31.453 42.162  1.262   1.00 8.27  ? 245  PHE A O   1 
ATOM   1819 C  CB  . PHE A 1 245  ? 28.210 42.204  0.387   1.00 7.38  ? 245  PHE A CB  1 
ATOM   1820 C  CG  . PHE A 1 245  ? 28.361 43.713  0.442   1.00 6.04  ? 245  PHE A CG  1 
ATOM   1821 C  CD1 . PHE A 1 245  ? 29.341 44.348  -0.376  1.00 6.41  ? 245  PHE A CD1 1 
ATOM   1822 C  CD2 . PHE A 1 245  ? 27.575 44.467  1.287   1.00 7.77  ? 245  PHE A CD2 1 
ATOM   1823 C  CE1 . PHE A 1 245  ? 29.501 45.751  -0.334  1.00 6.93  ? 245  PHE A CE1 1 
ATOM   1824 C  CE2 . PHE A 1 245  ? 27.726 45.881  1.335   1.00 8.21  ? 245  PHE A CE2 1 
ATOM   1825 C  CZ  . PHE A 1 245  ? 28.691 46.485  0.509   1.00 6.94  ? 245  PHE A CZ  1 
ATOM   1826 N  N   . LEU A 1 246  ? 30.813 40.565  -0.180  1.00 6.91  ? 246  LEU A N   1 
ATOM   1827 C  CA  . LEU A 1 246  ? 32.092 40.486  -0.858  1.00 6.49  ? 246  LEU A CA  1 
ATOM   1828 C  C   . LEU A 1 246  ? 31.950 41.397  -2.078  1.00 6.56  ? 246  LEU A C   1 
ATOM   1829 O  O   . LEU A 1 246  ? 31.267 41.073  -3.066  1.00 7.68  ? 246  LEU A O   1 
ATOM   1830 C  CB  . LEU A 1 246  ? 32.369 39.028  -1.260  1.00 9.31  ? 246  LEU A CB  1 
ATOM   1831 C  CG  . LEU A 1 246  ? 32.666 38.135  -0.014  1.00 10.58 ? 246  LEU A CG  1 
ATOM   1832 C  CD1 . LEU A 1 246  ? 32.582 36.634  -0.485  1.00 16.38 ? 246  LEU A CD1 1 
ATOM   1833 C  CD2 . LEU A 1 246  ? 34.074 38.443  0.451   1.00 15.71 ? 246  LEU A CD2 1 
ATOM   1834 N  N   . TRP A 1 247  ? 32.577 42.581  -1.990  1.00 6.88  ? 247  TRP A N   1 
ATOM   1835 C  CA  . TRP A 1 247  ? 32.408 43.601  -3.013  1.00 6.14  ? 247  TRP A CA  1 
ATOM   1836 C  C   . TRP A 1 247  ? 33.428 43.400  -4.104  1.00 6.45  ? 247  TRP A C   1 
ATOM   1837 O  O   . TRP A 1 247  ? 34.621 43.568  -3.876  1.00 6.88  ? 247  TRP A O   1 
ATOM   1838 C  CB  . TRP A 1 247  ? 32.579 44.965  -2.339  1.00 6.34  ? 247  TRP A CB  1 
ATOM   1839 C  CG  . TRP A 1 247  ? 32.105 46.144  -3.184  1.00 6.25  ? 247  TRP A CG  1 
ATOM   1840 C  CD1 . TRP A 1 247  ? 31.582 46.144  -4.465  1.00 6.64  ? 247  TRP A CD1 1 
ATOM   1841 C  CD2 . TRP A 1 247  ? 32.127 47.518  -2.763  1.00 6.68  ? 247  TRP A CD2 1 
ATOM   1842 N  NE1 . TRP A 1 247  ? 31.246 47.441  -4.844  1.00 7.00  ? 247  TRP A NE1 1 
ATOM   1843 C  CE2 . TRP A 1 247  ? 31.570 48.291  -3.818  1.00 6.14  ? 247  TRP A CE2 1 
ATOM   1844 C  CE3 . TRP A 1 247  ? 32.564 48.167  -1.578  1.00 6.79  ? 247  TRP A CE3 1 
ATOM   1845 C  CZ2 . TRP A 1 247  ? 31.441 49.701  -3.728  1.00 7.24  ? 247  TRP A CZ2 1 
ATOM   1846 C  CZ3 . TRP A 1 247  ? 32.435 49.554  -1.516  1.00 6.38  ? 247  TRP A CZ3 1 
ATOM   1847 C  CH2 . TRP A 1 247  ? 31.890 50.307  -2.559  1.00 6.48  ? 247  TRP A CH2 1 
ATOM   1848 N  N   . ARG A 1 248  ? 32.943 43.015  -5.305  1.00 6.52  ? 248  ARG A N   1 
ATOM   1849 C  CA  . ARG A 1 248  ? 33.813 42.817  -6.451  1.00 6.87  ? 248  ARG A CA  1 
ATOM   1850 C  C   . ARG A 1 248  ? 33.539 43.887  -7.509  1.00 6.96  ? 248  ARG A C   1 
ATOM   1851 O  O   . ARG A 1 248  ? 32.493 44.542  -7.471  1.00 7.27  ? 248  ARG A O   1 
ATOM   1852 C  CB  . ARG A 1 248  ? 33.602 41.433  -7.134  1.00 7.88  ? 248  ARG A CB  1 
ATOM   1853 C  CG  . ARG A 1 248  ? 32.204 41.264  -7.771  1.00 7.69  ? 248  ARG A CG  1 
ATOM   1854 C  CD  . ARG A 1 248  ? 32.169 39.973  -8.629  1.00 10.20 ? 248  ARG A CD  1 
ATOM   1855 N  NE  . ARG A 1 248  ? 32.239 38.812  -7.713  1.00 10.98 ? 248  ARG A NE  1 
ATOM   1856 C  CZ  . ARG A 1 248  ? 32.150 37.562  -8.156  1.00 13.96 ? 248  ARG A CZ  1 
ATOM   1857 N  NH1 . ARG A 1 248  ? 32.033 37.336  -9.475  1.00 14.16 ? 248  ARG A NH1 1 
ATOM   1858 N  NH2 . ARG A 1 248  ? 32.081 36.546  -7.289  1.00 14.33 ? 248  ARG A NH2 1 
ATOM   1859 N  N   . GLN A 1 249  ? 34.469 44.055  -8.431  1.00 7.12  ? 249  GLN A N   1 
ATOM   1860 C  CA  . GLN A 1 249  ? 34.295 44.981  -9.536  1.00 5.93  ? 249  GLN A CA  1 
ATOM   1861 C  C   . GLN A 1 249  ? 33.204 44.548  -10.514 1.00 7.37  ? 249  GLN A C   1 
ATOM   1862 O  O   . GLN A 1 249  ? 32.934 43.372  -10.697 1.00 8.37  ? 249  GLN A O   1 
ATOM   1863 C  CB  . GLN A 1 249  ? 35.626 45.171  -10.268 1.00 8.04  ? 249  GLN A CB  1 
ATOM   1864 C  CG  . GLN A 1 249  ? 36.724 45.742  -9.349  1.00 7.45  ? 249  GLN A CG  1 
ATOM   1865 C  CD  . GLN A 1 249  ? 36.321 47.043  -8.684  1.00 7.40  ? 249  GLN A CD  1 
ATOM   1866 O  OE1 . GLN A 1 249  ? 36.054 48.010  -9.361  1.00 9.62  ? 249  GLN A OE1 1 
ATOM   1867 N  NE2 . GLN A 1 249  ? 36.300 47.064  -7.374  1.00 5.91  ? 249  GLN A NE2 1 
ATOM   1868 N  N   . ILE A 1 250  ? 32.605 45.535  -11.160 1.00 7.84  ? 250  ILE A N   1 
ATOM   1869 C  CA  . ILE A 1 250  ? 31.436 45.259  -11.998 1.00 8.41  ? 250  ILE A CA  1 
ATOM   1870 C  C   . ILE A 1 250  ? 31.733 44.324  -13.166 1.00 8.90  ? 250  ILE A C   1 
ATOM   1871 O  O   . ILE A 1 250  ? 30.822 43.685  -13.674 1.00 9.42  ? 250  ILE A O   1 
ATOM   1872 C  CB  . ILE A 1 250  ? 30.742 46.560  -12.493 1.00 9.21  ? 250  ILE A CB  1 
ATOM   1873 C  CG1 . ILE A 1 250  ? 31.694 47.449  -13.299 1.00 9.07  ? 250  ILE A CG1 1 
ATOM   1874 C  CG2 . ILE A 1 250  ? 30.085 47.299  -11.338 1.00 9.93  ? 250  ILE A CG2 1 
ATOM   1875 C  CD1 . ILE A 1 250  ? 31.053 48.775  -13.766 1.00 10.67 ? 250  ILE A CD1 1 
ATOM   1876 N  N   . TRP A 1 251  ? 32.990 44.258  -13.601 1.00 9.59  ? 251  TRP A N   1 
ATOM   1877 C  CA  . TRP A 1 251  ? 33.318 43.396  -14.758 1.00 9.68  ? 251  TRP A CA  1 
ATOM   1878 C  C   . TRP A 1 251  ? 33.956 42.084  -14.341 1.00 14.66 ? 251  TRP A C   1 
ATOM   1879 O  O   . TRP A 1 251  ? 34.288 41.247  -15.200 1.00 14.87 ? 251  TRP A O   1 
ATOM   1880 C  CB  . TRP A 1 251  ? 34.304 44.122  -15.665 1.00 12.08 ? 251  TRP A CB  1 
ATOM   1881 C  CG  . TRP A 1 251  ? 35.551 44.274  -14.965 1.00 15.64 ? 251  TRP A CG  1 
ATOM   1882 C  CD1 . TRP A 1 251  ? 36.523 43.293  -14.769 1.00 16.89 ? 251  TRP A CD1 1 
ATOM   1883 C  CD2 . TRP A 1 251  ? 35.982 45.400  -14.249 1.00 13.41 ? 251  TRP A CD2 1 
ATOM   1884 N  NE1 . TRP A 1 251  ? 37.489 43.768  -13.995 1.00 14.77 ? 251  TRP A NE1 1 
ATOM   1885 C  CE2 . TRP A 1 251  ? 37.213 45.062  -13.642 1.00 12.52 ? 251  TRP A CE2 1 
ATOM   1886 C  CE3 . TRP A 1 251  ? 35.446 46.659  -14.032 1.00 13.03 ? 251  TRP A CE3 1 
ATOM   1887 C  CZ2 . TRP A 1 251  ? 37.925 45.941  -12.828 1.00 14.15 ? 251  TRP A CZ2 1 
ATOM   1888 C  CZ3 . TRP A 1 251  ? 36.147 47.542  -13.217 1.00 15.46 ? 251  TRP A CZ3 1 
ATOM   1889 C  CH2 . TRP A 1 251  ? 37.376 47.176  -12.630 1.00 17.10 ? 251  TRP A CH2 1 
ATOM   1890 N  N   . ASP A 1 252  ? 34.117 41.867  -13.039 1.00 11.49 ? 252  ASP A N   1 
ATOM   1891 C  CA  . ASP A 1 252  ? 34.842 40.689  -12.533 1.00 12.66 ? 252  ASP A CA  1 
ATOM   1892 C  C   . ASP A 1 252  ? 34.034 39.429  -12.414 1.00 11.60 ? 252  ASP A C   1 
ATOM   1893 O  O   . ASP A 1 252  ? 33.295 39.217  -11.480 1.00 13.34 ? 252  ASP A O   1 
ATOM   1894 C  CB  . ASP A 1 252  ? 35.462 41.100  -11.200 1.00 10.38 ? 252  ASP A CB  1 
ATOM   1895 C  CG  . ASP A 1 252  ? 36.236 39.952  -10.530 1.00 13.57 ? 252  ASP A CG  1 
ATOM   1896 O  OD1 . ASP A 1 252  ? 36.519 38.923  -11.218 1.00 16.86 ? 252  ASP A OD1 1 
ATOM   1897 O  OD2 . ASP A 1 252  ? 36.550 40.070  -9.337  1.00 13.55 ? 252  ASP A OD2 1 
ATOM   1898 N  N   . ASN A 1 253  ? 34.178 38.589  -13.422 1.00 14.41 ? 253  ASN A N   1 
ATOM   1899 C  CA  . ASN A 1 253  ? 33.442 37.350  -13.506 1.00 14.17 ? 253  ASN A CA  1 
ATOM   1900 C  C   . ASN A 1 253  ? 33.871 36.323  -12.464 1.00 14.30 ? 253  ASN A C   1 
ATOM   1901 O  O   . ASN A 1 253  ? 33.062 35.622  -11.907 1.00 17.20 ? 253  ASN A O   1 
ATOM   1902 C  CB  . ASN A 1 253  ? 33.585 36.757  -14.916 1.00 16.19 ? 253  ASN A CB  1 
ATOM   1903 C  CG  . ASN A 1 253  ? 32.729 35.543  -15.117 1.00 25.96 ? 253  ASN A CG  1 
ATOM   1904 O  OD1 . ASN A 1 253  ? 31.523 35.581  -14.933 1.00 32.08 ? 253  ASN A OD1 1 
ATOM   1905 N  ND2 . ASN A 1 253  ? 33.359 34.450  -15.491 1.00 22.24 ? 253  ASN A ND2 1 
ATOM   1906 N  N   . LYS A 1 254  ? 35.157 36.243  -12.221 1.00 15.06 ? 254  LYS A N   1 
ATOM   1907 C  CA  . LYS A 1 254  ? 35.671 35.207  -11.300 1.00 20.09 ? 254  LYS A CA  1 
ATOM   1908 C  C   . LYS A 1 254  ? 35.559 35.581  -9.843  1.00 20.35 ? 254  LYS A C   1 
ATOM   1909 O  O   . LYS A 1 254  ? 35.329 34.704  -8.997  1.00 21.07 ? 254  LYS A O   1 
ATOM   1910 C  CB  . LYS A 1 254  ? 37.135 34.911  -11.631 1.00 23.90 ? 254  LYS A CB  1 
ATOM   1911 C  CG  . LYS A 1 254  ? 37.754 33.717  -10.886 1.00 31.15 ? 254  LYS A CG  1 
ATOM   1912 C  CD  . LYS A 1 254  ? 39.168 33.423  -11.442 1.00 35.30 ? 254  LYS A CD  1 
ATOM   1913 C  CE  . LYS A 1 254  ? 39.823 32.185  -10.788 1.00 37.21 ? 254  LYS A CE  1 
ATOM   1914 N  NZ  . LYS A 1 254  ? 39.551 32.090  -9.330  1.00 39.77 ? 254  LYS A NZ  1 
ATOM   1915 N  N   . GLY A 1 255  ? 35.741 36.870  -9.541  1.00 16.91 ? 255  GLY A N   1 
ATOM   1916 C  CA  . GLY A 1 255  ? 35.654 37.297  -8.159  1.00 15.68 ? 255  GLY A CA  1 
ATOM   1917 C  C   . GLY A 1 255  ? 37.020 37.559  -7.529  1.00 14.38 ? 255  GLY A C   1 
ATOM   1918 O  O   . GLY A 1 255  ? 37.030 37.833  -6.325  1.00 14.84 ? 255  GLY A O   1 
ATOM   1919 N  N   . ASP A 1 256  ? 38.121 37.581  -8.276  1.00 15.08 ? 256  ASP A N   1 
ATOM   1920 C  CA  . ASP A 1 256  ? 39.432 37.810  -7.651  1.00 18.93 ? 256  ASP A CA  1 
ATOM   1921 C  C   . ASP A 1 256  ? 39.651 39.219  -7.074  1.00 16.79 ? 256  ASP A C   1 
ATOM   1922 O  O   . ASP A 1 256  ? 40.533 39.434  -6.261  1.00 16.03 ? 256  ASP A O   1 
ATOM   1923 C  CB  . ASP A 1 256  ? 40.579 37.503  -8.620  1.00 26.21 ? 256  ASP A CB  1 
ATOM   1924 C  CG  . ASP A 1 256  ? 40.629 36.027  -9.040  1.00 37.03 ? 256  ASP A CG  1 
ATOM   1925 O  OD1 . ASP A 1 256  ? 40.175 35.162  -8.246  1.00 36.40 ? 256  ASP A OD1 1 
ATOM   1926 O  OD2 . ASP A 1 256  ? 41.139 35.753  -10.158 1.00 37.78 ? 256  ASP A OD2 1 
ATOM   1927 N  N   . THR A 1 257  ? 38.824 40.184  -7.473  1.00 12.21 ? 257  THR A N   1 
ATOM   1928 C  CA  . THR A 1 257  ? 38.932 41.533  -6.921  1.00 11.40 ? 257  THR A CA  1 
ATOM   1929 C  C   . THR A 1 257  ? 38.130 41.686  -5.622  1.00 11.41 ? 257  THR A C   1 
ATOM   1930 O  O   . THR A 1 257  ? 38.204 42.746  -5.005  1.00 11.36 ? 257  THR A O   1 
ATOM   1931 C  CB  . THR A 1 257  ? 38.356 42.604  -7.926  1.00 10.59 ? 257  THR A CB  1 
ATOM   1932 O  OG1 . THR A 1 257  ? 36.938 42.391  -8.133  1.00 10.35 ? 257  THR A OG1 1 
ATOM   1933 C  CG2 . THR A 1 257  ? 39.151 42.573  -9.237  1.00 13.22 ? 257  THR A CG2 1 
ATOM   1934 N  N   . ALA A 1 258  ? 37.367 40.661  -5.209  1.00 10.58 ? 258  ALA A N   1 
ATOM   1935 C  CA  . ALA A 1 258  ? 36.490 40.824  -4.057  1.00 9.78  ? 258  ALA A CA  1 
ATOM   1936 C  C   . ALA A 1 258  ? 37.125 41.195  -2.753  1.00 9.31  ? 258  ALA A C   1 
ATOM   1937 O  O   . ALA A 1 258  ? 38.220 40.696  -2.422  1.00 10.57 ? 258  ALA A O   1 
ATOM   1938 C  CB  . ALA A 1 258  ? 35.662 39.578  -3.821  1.00 11.64 ? 258  ALA A CB  1 
ATOM   1939 N  N   . LEU A 1 259  ? 36.475 42.121  -2.033  1.00 7.89  ? 259  LEU A N   1 
ATOM   1940 C  CA  . LEU A 1 259  ? 36.949 42.535  -0.694  1.00 7.43  ? 259  LEU A CA  1 
ATOM   1941 C  C   . LEU A 1 259  ? 35.753 42.530  0.227   1.00 7.22  ? 259  LEU A C   1 
ATOM   1942 O  O   . LEU A 1 259  ? 34.709 43.150  -0.053  1.00 7.52  ? 259  LEU A O   1 
ATOM   1943 C  CB  . LEU A 1 259  ? 37.546 43.942  -0.765  1.00 7.28  ? 259  LEU A CB  1 
ATOM   1944 C  CG  . LEU A 1 259  ? 38.295 44.366  0.519   1.00 7.31  ? 259  LEU A CG  1 
ATOM   1945 C  CD1 . LEU A 1 259  ? 39.558 43.469  0.822   1.00 11.65 ? 259  LEU A CD1 1 
ATOM   1946 C  CD2 . LEU A 1 259  ? 38.779 45.839  0.352   1.00 9.73  ? 259  LEU A CD2 1 
ATOM   1947 N  N   . PHE A 1 260  ? 35.911 41.889  1.402   1.00 6.97  ? 260  PHE A N   1 
ATOM   1948 C  CA  . PHE A 1 260  ? 34.832 41.868  2.379   1.00 6.58  ? 260  PHE A CA  1 
ATOM   1949 C  C   . PHE A 1 260  ? 34.531 43.262  2.873   1.00 6.23  ? 260  PHE A C   1 
ATOM   1950 O  O   . PHE A 1 260  ? 35.436 44.004  3.300   1.00 6.98  ? 260  PHE A O   1 
ATOM   1951 C  CB  . PHE A 1 260  ? 35.250 40.951  3.573   1.00 8.24  ? 260  PHE A CB  1 
ATOM   1952 C  CG  . PHE A 1 260  ? 34.152 40.799  4.593   1.00 7.53  ? 260  PHE A CG  1 
ATOM   1953 C  CD1 . PHE A 1 260  ? 33.163 39.847  4.375   1.00 10.88 ? 260  PHE A CD1 1 
ATOM   1954 C  CD2 . PHE A 1 260  ? 34.062 41.580  5.720   1.00 8.14  ? 260  PHE A CD2 1 
ATOM   1955 C  CE1 . PHE A 1 260  ? 32.090 39.689  5.290   1.00 11.34 ? 260  PHE A CE1 1 
ATOM   1956 C  CE2 . PHE A 1 260  ? 32.993 41.443  6.669   1.00 9.57  ? 260  PHE A CE2 1 
ATOM   1957 C  CZ  . PHE A 1 260  ? 32.016 40.487  6.433   1.00 9.87  ? 260  PHE A CZ  1 
ATOM   1958 N  N   . THR A 1 261  ? 33.253 43.611  2.839   1.00 6.02  ? 261  THR A N   1 
ATOM   1959 C  CA  . THR A 1 261  ? 32.838 44.949  3.170   1.00 5.99  ? 261  THR A CA  1 
ATOM   1960 C  C   . THR A 1 261  ? 31.696 44.916  4.199   1.00 6.86  ? 261  THR A C   1 
ATOM   1961 O  O   . THR A 1 261  ? 30.729 44.167  4.015   1.00 7.10  ? 261  THR A O   1 
ATOM   1962 C  CB  . THR A 1 261  ? 32.302 45.664  1.878   1.00 6.54  ? 261  THR A CB  1 
ATOM   1963 O  OG1 . THR A 1 261  ? 33.367 45.760  0.949   1.00 7.26  ? 261  THR A OG1 1 
ATOM   1964 C  CG2 . THR A 1 261  ? 31.840 47.085  2.169   1.00 7.94  ? 261  THR A CG2 1 
ATOM   1965 N  N   . HIS A 1 262  ? 31.776 45.789  5.202   1.00 6.32  ? 262  HIS A N   1 
ATOM   1966 C  CA  . HIS A 1 262  ? 30.732 45.970  6.182   1.00 6.57  ? 262  HIS A CA  1 
ATOM   1967 C  C   . HIS A 1 262  ? 30.110 47.362  5.990   1.00 7.03  ? 262  HIS A C   1 
ATOM   1968 O  O   . HIS A 1 262  ? 30.817 48.371  6.168   1.00 7.36  ? 262  HIS A O   1 
ATOM   1969 C  CB  . HIS A 1 262  ? 31.366 45.895  7.589   1.00 7.86  ? 262  HIS A CB  1 
ATOM   1970 C  CG  . HIS A 1 262  ? 30.404 46.239  8.695   1.00 6.39  ? 262  HIS A CG  1 
ATOM   1971 N  ND1 . HIS A 1 262  ? 29.819 45.272  9.493   1.00 8.93  ? 262  HIS A ND1 1 
ATOM   1972 C  CD2 . HIS A 1 262  ? 29.949 47.436  9.148   1.00 6.65  ? 262  HIS A CD2 1 
ATOM   1973 C  CE1 . HIS A 1 262  ? 29.071 45.872  10.419  1.00 9.03  ? 262  HIS A CE1 1 
ATOM   1974 N  NE2 . HIS A 1 262  ? 29.119 47.181  10.233  1.00 8.94  ? 262  HIS A NE2 1 
ATOM   1975 N  N   . MET A 1 263  ? 28.842 47.427  5.652   1.00 6.30  ? 263  MET A N   1 
ATOM   1976 C  CA  . MET A 1 263  ? 28.111 48.658  5.581   1.00 6.03  ? 263  MET A CA  1 
ATOM   1977 C  C   . MET A 1 263  ? 27.371 48.870  6.938   1.00 7.81  ? 263  MET A C   1 
ATOM   1978 O  O   . MET A 1 263  ? 26.614 47.945  7.378   1.00 8.47  ? 263  MET A O   1 
ATOM   1979 C  CB  . MET A 1 263  ? 27.094 48.610  4.428   1.00 7.87  ? 263  MET A CB  1 
ATOM   1980 C  CG  . MET A 1 263  ? 26.304 49.923  4.308   1.00 7.81  ? 263  MET A CG  1 
ATOM   1981 S  SD  . MET A 1 263  ? 24.941 49.783  3.098   1.00 8.63  ? 263  MET A SD  1 
ATOM   1982 C  CE  . MET A 1 263  ? 25.773 49.359  1.522   1.00 10.21 ? 263  MET A CE  1 
ATOM   1983 N  N   . MET A 1 264  ? 27.578 50.000  7.593   1.00 7.41  ? 264  MET A N   1 
ATOM   1984 C  CA  . MET A 1 264  ? 26.855 50.283  8.823   1.00 6.95  ? 264  MET A CA  1 
ATOM   1985 C  C   . MET A 1 264  ? 25.389 50.572  8.473   1.00 7.57  ? 264  MET A C   1 
ATOM   1986 O  O   . MET A 1 264  ? 25.090 51.004  7.370   1.00 8.24  ? 264  MET A O   1 
ATOM   1987 C  CB  . MET A 1 264  ? 27.497 51.467  9.551   1.00 8.77  ? 264  MET A CB  1 
ATOM   1988 C  CG  A MET A 1 264  ? 28.988 51.290  9.902   0.50 8.26  ? 264  MET A CG  1 
ATOM   1989 C  CG  B MET A 1 264  ? 28.853 50.901  10.007  0.50 8.16  ? 264  MET A CG  1 
ATOM   1990 S  SD  A MET A 1 264  ? 29.922 52.799  10.359  0.50 16.94 ? 264  MET A SD  1 
ATOM   1991 S  SD  B MET A 1 264  ? 29.580 51.769  11.411  0.50 32.26 ? 264  MET A SD  1 
ATOM   1992 C  CE  A MET A 1 264  ? 28.851 53.543  11.572  0.50 14.92 ? 264  MET A CE  1 
ATOM   1993 C  CE  B MET A 1 264  ? 29.978 53.132  10.407  0.50 22.78 ? 264  MET A CE  1 
ATOM   1994 N  N   . PRO A 1 265  ? 24.471 50.289  9.391   1.00 7.21  ? 265  PRO A N   1 
ATOM   1995 C  CA  . PRO A 1 265  ? 23.043 50.265  9.012   1.00 7.63  ? 265  PRO A CA  1 
ATOM   1996 C  C   . PRO A 1 265  ? 22.258 51.570  9.197   1.00 8.53  ? 265  PRO A C   1 
ATOM   1997 O  O   . PRO A 1 265  ? 21.185 51.680  8.625   1.00 9.11  ? 265  PRO A O   1 
ATOM   1998 C  CB  . PRO A 1 265  ? 22.455 49.184  9.924   1.00 9.82  ? 265  PRO A CB  1 
ATOM   1999 C  CG  . PRO A 1 265  ? 23.313 49.192  11.114  1.00 11.61 ? 265  PRO A CG  1 
ATOM   2000 C  CD  . PRO A 1 265  ? 24.693 49.695  10.720  1.00 8.40  ? 265  PRO A CD  1 
ATOM   2001 N  N   . PHE A 1 266  ? 22.781 52.509  9.965   1.00 8.26  ? 266  PHE A N   1 
ATOM   2002 C  CA  . PHE A 1 266  ? 22.008 53.630  10.406  1.00 8.48  ? 266  PHE A CA  1 
ATOM   2003 C  C   . PHE A 1 266  ? 22.385 54.974  9.827   1.00 8.11  ? 266  PHE A C   1 
ATOM   2004 O  O   . PHE A 1 266  ? 23.256 55.081  8.971   1.00 8.11  ? 266  PHE A O   1 
ATOM   2005 C  CB  . PHE A 1 266  ? 21.968 53.605  11.945  1.00 8.58  ? 266  PHE A CB  1 
ATOM   2006 C  CG  . PHE A 1 266  ? 21.413 52.291  12.555  1.00 8.17  ? 266  PHE A CG  1 
ATOM   2007 C  CD1 . PHE A 1 266  ? 20.245 51.715  12.090  1.00 10.00 ? 266  PHE A CD1 1 
ATOM   2008 C  CD2 . PHE A 1 266  ? 22.102 51.673  13.590  1.00 9.39  ? 266  PHE A CD2 1 
ATOM   2009 C  CE1 . PHE A 1 266  ? 19.757 50.488  12.680  1.00 9.58  ? 266  PHE A CE1 1 
ATOM   2010 C  CE2 . PHE A 1 266  ? 21.623 50.471  14.169  1.00 9.24  ? 266  PHE A CE2 1 
ATOM   2011 C  CZ  . PHE A 1 266  ? 20.465 49.900  13.704  1.00 9.21  ? 266  PHE A CZ  1 
ATOM   2012 N  N   . TYR A 1 267  ? 21.798 56.039  10.329  1.00 7.88  ? 267  TYR A N   1 
ATOM   2013 C  CA  . TYR A 1 267  ? 21.826 57.343  9.668   1.00 7.62  ? 267  TYR A CA  1 
ATOM   2014 C  C   . TYR A 1 267  ? 23.172 58.049  9.854   1.00 8.74  ? 267  TYR A C   1 
ATOM   2015 O  O   . TYR A 1 267  ? 23.553 58.845  9.027   1.00 8.46  ? 267  TYR A O   1 
ATOM   2016 C  CB  . TYR A 1 267  ? 20.655 58.186  10.198  1.00 9.22  ? 267  TYR A CB  1 
ATOM   2017 C  CG  . TYR A 1 267  ? 20.705 59.678  10.015  1.00 8.76  ? 267  TYR A CG  1 
ATOM   2018 C  CD1 . TYR A 1 267  ? 20.295 60.279  8.830   1.00 11.08 ? 267  TYR A CD1 1 
ATOM   2019 C  CD2 . TYR A 1 267  ? 21.096 60.492  11.056  1.00 10.79 ? 267  TYR A CD2 1 
ATOM   2020 C  CE1 . TYR A 1 267  ? 20.307 61.655  8.706   1.00 12.37 ? 267  TYR A CE1 1 
ATOM   2021 C  CE2 . TYR A 1 267  ? 21.128 61.848  10.922  1.00 11.36 ? 267  TYR A CE2 1 
ATOM   2022 C  CZ  . TYR A 1 267  ? 20.730 62.420  9.761   1.00 13.19 ? 267  TYR A CZ  1 
ATOM   2023 O  OH  . TYR A 1 267  ? 20.751 63.791  9.714   1.00 17.75 ? 267  TYR A OH  1 
ATOM   2024 N  N   . SER A 1 268  ? 23.888 57.727  10.924  1.00 8.07  ? 268  SER A N   1 
ATOM   2025 C  CA  . SER A 1 268  ? 25.165 58.423  11.201  1.00 9.04  ? 268  SER A CA  1 
ATOM   2026 C  C   . SER A 1 268  ? 26.128 57.475  11.888  1.00 8.17  ? 268  SER A C   1 
ATOM   2027 O  O   . SER A 1 268  ? 25.738 56.368  12.345  1.00 8.77  ? 268  SER A O   1 
ATOM   2028 C  CB  . SER A 1 268  ? 24.864 59.603  12.136  1.00 8.74  ? 268  SER A CB  1 
ATOM   2029 O  OG  . SER A 1 268  ? 26.046 60.263  12.582  1.00 11.26 ? 268  SER A OG  1 
ATOM   2030 N  N   . TYR A 1 269  ? 27.395 57.877  11.977  1.00 9.07  ? 269  TYR A N   1 
ATOM   2031 C  CA  . TYR A 1 269  ? 28.378 57.156  12.770  1.00 7.41  ? 269  TYR A CA  1 
ATOM   2032 C  C   . TYR A 1 269  ? 28.472 57.635  14.208  1.00 8.44  ? 269  TYR A C   1 
ATOM   2033 O  O   . TYR A 1 269  ? 29.290 57.157  14.952  1.00 8.69  ? 269  TYR A O   1 
ATOM   2034 C  CB  . TYR A 1 269  ? 29.751 57.295  12.105  1.00 7.44  ? 269  TYR A CB  1 
ATOM   2035 C  CG  . TYR A 1 269  ? 30.162 58.731  11.898  1.00 9.58  ? 269  TYR A CG  1 
ATOM   2036 C  CD1 . TYR A 1 269  ? 30.603 59.508  12.952  1.00 8.56  ? 269  TYR A CD1 1 
ATOM   2037 C  CD2 . TYR A 1 269  ? 30.099 59.303  10.647  1.00 9.25  ? 269  TYR A CD2 1 
ATOM   2038 C  CE1 . TYR A 1 269  ? 30.968 60.826  12.776  1.00 9.37  ? 269  TYR A CE1 1 
ATOM   2039 C  CE2 . TYR A 1 269  ? 30.471 60.633  10.446  1.00 10.30 ? 269  TYR A CE2 1 
ATOM   2040 C  CZ  . TYR A 1 269  ? 30.908 61.376  11.513  1.00 8.55  ? 269  TYR A CZ  1 
ATOM   2041 O  OH  . TYR A 1 269  ? 31.263 62.694  11.277  1.00 10.27 ? 269  TYR A OH  1 
ATOM   2042 N  N   . ASP A 1 270  ? 27.679 58.625  14.587  1.00 7.63  ? 270  ASP A N   1 
ATOM   2043 C  CA  . ASP A 1 270  ? 27.713 59.116  15.980  1.00 8.46  ? 270  ASP A CA  1 
ATOM   2044 C  C   . ASP A 1 270  ? 27.104 58.064  16.948  1.00 7.45  ? 270  ASP A C   1 
ATOM   2045 O  O   . ASP A 1 270  ? 26.517 57.069  16.509  1.00 7.89  ? 270  ASP A O   1 
ATOM   2046 C  CB  . ASP A 1 270  ? 27.071 60.523  16.084  1.00 9.06  ? 270  ASP A CB  1 
ATOM   2047 C  CG  . ASP A 1 270  ? 25.568 60.557  15.876  1.00 12.20 ? 270  ASP A CG  1 
ATOM   2048 O  OD1 . ASP A 1 270  ? 24.928 59.503  15.717  1.00 12.15 ? 270  ASP A OD1 1 
ATOM   2049 O  OD2 . ASP A 1 270  ? 25.012 61.721  15.914  1.00 13.57 ? 270  ASP A OD2 1 
ATOM   2050 N  N   . ILE A 1 271  ? 27.314 58.312  18.247  1.00 8.35  ? 271  ILE A N   1 
ATOM   2051 C  CA  . ILE A 1 271  ? 26.881 57.314  19.242  1.00 7.90  ? 271  ILE A CA  1 
ATOM   2052 C  C   . ILE A 1 271  ? 25.373 57.046  19.186  1.00 7.43  ? 271  ILE A C   1 
ATOM   2053 O  O   . ILE A 1 271  ? 24.959 55.891  19.179  1.00 7.88  ? 271  ILE A O   1 
ATOM   2054 C  CB  . ILE A 1 271  ? 27.470 57.646  20.631  1.00 8.71  ? 271  ILE A CB  1 
ATOM   2055 C  CG1 . ILE A 1 271  ? 29.014 57.489  20.535  1.00 8.09  ? 271  ILE A CG1 1 
ATOM   2056 C  CG2 . ILE A 1 271  ? 26.885 56.682  21.668  1.00 8.70  ? 271  ILE A CG2 1 
ATOM   2057 C  CD1 . ILE A 1 271  ? 29.735 58.153  21.697  1.00 8.71  ? 271  ILE A CD1 1 
ATOM   2058 N  N   . PRO A 1 272  ? 24.538 58.091  19.015  1.00 7.97  ? 272  PRO A N   1 
ATOM   2059 C  CA  . PRO A 1 272  ? 23.095 57.834  18.939  1.00 8.41  ? 272  PRO A CA  1 
ATOM   2060 C  C   . PRO A 1 272  ? 22.699 56.922  17.813  1.00 10.01 ? 272  PRO A C   1 
ATOM   2061 O  O   . PRO A 1 272  ? 21.612 56.301  17.888  1.00 10.37 ? 272  PRO A O   1 
ATOM   2062 C  CB  . PRO A 1 272  ? 22.473 59.239  18.766  1.00 8.90  ? 272  PRO A CB  1 
ATOM   2063 C  CG  . PRO A 1 272  ? 23.432 60.160  19.554  1.00 9.64  ? 272  PRO A CG  1 
ATOM   2064 C  CD  . PRO A 1 272  ? 24.818 59.531  19.203  1.00 8.66  ? 272  PRO A CD  1 
ATOM   2065 N  N   . HIS A 1 273  ? 23.521 56.815  16.771  1.00 9.08  ? 273  HIS A N   1 
ATOM   2066 C  CA  . HIS A 1 273  ? 23.175 55.999  15.610  1.00 8.37  ? 273  HIS A CA  1 
ATOM   2067 C  C   . HIS A 1 273  ? 24.085 54.801  15.410  1.00 8.39  ? 273  HIS A C   1 
ATOM   2068 O  O   . HIS A 1 273  ? 24.123 54.243  14.340  1.00 9.73  ? 273  HIS A O   1 
ATOM   2069 C  CB  . HIS A 1 273  ? 23.060 56.853  14.340  1.00 8.29  ? 273  HIS A CB  1 
ATOM   2070 C  CG  . HIS A 1 273  ? 22.004 57.905  14.432  1.00 8.76  ? 273  HIS A CG  1 
ATOM   2071 N  ND1 . HIS A 1 273  ? 22.260 59.167  14.914  1.00 11.10 ? 273  HIS A ND1 1 
ATOM   2072 C  CD2 . HIS A 1 273  ? 20.688 57.878  14.117  1.00 7.03  ? 273  HIS A CD2 1 
ATOM   2073 C  CE1 . HIS A 1 273  ? 21.146 59.877  14.881  1.00 6.33  ? 273  HIS A CE1 1 
ATOM   2074 N  NE2 . HIS A 1 273  ? 20.179 59.114  14.408  1.00 13.09 ? 273  HIS A NE2 1 
ATOM   2075 N  N   . THR A 1 274  ? 24.776 54.392  16.471  1.00 9.26  ? 274  THR A N   1 
ATOM   2076 C  CA  . THR A 1 274  ? 25.670 53.236  16.333  1.00 8.38  ? 274  THR A CA  1 
ATOM   2077 C  C   . THR A 1 274  ? 25.410 52.150  17.376  1.00 9.06  ? 274  THR A C   1 
ATOM   2078 O  O   . THR A 1 274  ? 25.910 51.051  17.208  1.00 11.49 ? 274  THR A O   1 
ATOM   2079 C  CB  . THR A 1 274  ? 27.167 53.629  16.330  1.00 9.44  ? 274  THR A CB  1 
ATOM   2080 O  OG1 . THR A 1 274  ? 27.396 54.578  17.368  1.00 9.12  ? 274  THR A OG1 1 
ATOM   2081 C  CG2 . THR A 1 274  ? 27.547 54.213  14.949  1.00 10.41 ? 274  THR A CG2 1 
ATOM   2082 N  N   . CYS A 1 275  ? 24.642 52.405  18.423  1.00 10.44 ? 275  CYS A N   1 
ATOM   2083 C  CA  . CYS A 1 275  ? 24.357 51.340  19.395  1.00 10.75 ? 275  CYS A CA  1 
ATOM   2084 C  C   . CYS A 1 275  ? 23.226 50.378  19.007  1.00 10.89 ? 275  CYS A C   1 
ATOM   2085 O  O   . CYS A 1 275  ? 23.169 49.263  19.499  1.00 10.85 ? 275  CYS A O   1 
ATOM   2086 C  CB  . CYS A 1 275  ? 24.104 51.928  20.786  1.00 10.82 ? 275  CYS A CB  1 
ATOM   2087 S  SG  . CYS A 1 275  ? 22.360 51.956  21.352  1.00 12.20 ? 275  CYS A SG  1 
ATOM   2088 N  N   . GLY A 1 276  ? 22.341 50.835  18.132  1.00 10.86 ? 276  GLY A N   1 
ATOM   2089 C  CA  . GLY A 1 276  ? 21.097 50.155  17.813  1.00 10.63 ? 276  GLY A CA  1 
ATOM   2090 C  C   . GLY A 1 276  ? 20.182 51.085  17.065  1.00 9.61  ? 276  GLY A C   1 
ATOM   2091 O  O   . GLY A 1 276  ? 20.531 52.246  16.804  1.00 10.33 ? 276  GLY A O   1 
ATOM   2092 N  N   . PRO A 1 277  ? 18.939 50.632  16.775  1.00 9.11  ? 277  PRO A N   1 
ATOM   2093 C  CA  . PRO A 1 277  ? 17.971 51.410  16.005  1.00 10.35 ? 277  PRO A CA  1 
ATOM   2094 C  C   . PRO A 1 277  ? 17.312 52.606  16.615  1.00 9.69  ? 277  PRO A C   1 
ATOM   2095 O  O   . PRO A 1 277  ? 16.736 53.406  15.873  1.00 10.14 ? 277  PRO A O   1 
ATOM   2096 C  CB  . PRO A 1 277  ? 16.897 50.354  15.596  1.00 10.89 ? 277  PRO A CB  1 
ATOM   2097 C  CG  . PRO A 1 277  ? 16.969 49.392  16.842  1.00 10.11 ? 277  PRO A CG  1 
ATOM   2098 C  CD  . PRO A 1 277  ? 18.439 49.286  17.126  1.00 9.48  ? 277  PRO A CD  1 
ATOM   2099 N  N   . ASP A 1 278  ? 17.349 52.745  17.923  1.00 9.63  ? 278  ASP A N   1 
ATOM   2100 C  CA  . ASP A 1 278  ? 16.639 53.859  18.553  1.00 9.26  ? 278  ASP A CA  1 
ATOM   2101 C  C   . ASP A 1 278  ? 17.598 54.900  19.099  1.00 10.34 ? 278  ASP A C   1 
ATOM   2102 O  O   . ASP A 1 278  ? 18.176 54.721  20.167  1.00 9.83  ? 278  ASP A O   1 
ATOM   2103 C  CB  . ASP A 1 278  ? 15.787 53.326  19.735  1.00 10.92 ? 278  ASP A CB  1 
ATOM   2104 C  CG  . ASP A 1 278  ? 14.874 54.411  20.282  1.00 10.41 ? 278  ASP A CG  1 
ATOM   2105 O  OD1 . ASP A 1 278  ? 15.017 55.609  19.963  1.00 12.74 ? 278  ASP A OD1 1 
ATOM   2106 O  OD2 . ASP A 1 278  ? 13.957 54.049  21.077  1.00 15.24 ? 278  ASP A OD2 1 
ATOM   2107 N  N   . PRO A 1 279  ? 17.740 56.043  18.404  1.00 10.09 ? 279  PRO A N   1 
ATOM   2108 C  CA  . PRO A 1 279  ? 18.677 57.060  18.910  1.00 10.26 ? 279  PRO A CA  1 
ATOM   2109 C  C   . PRO A 1 279  ? 18.374 57.652  20.249  1.00 9.64  ? 279  PRO A C   1 
ATOM   2110 O  O   . PRO A 1 279  ? 19.261 58.109  20.940  1.00 10.90 ? 279  PRO A O   1 
ATOM   2111 C  CB  . PRO A 1 279  ? 18.747 58.076  17.758  1.00 10.96 ? 279  PRO A CB  1 
ATOM   2112 C  CG  . PRO A 1 279  ? 17.360 57.968  17.148  1.00 10.75 ? 279  PRO A CG  1 
ATOM   2113 C  CD  . PRO A 1 279  ? 17.010 56.475  17.196  1.00 11.23 ? 279  PRO A CD  1 
ATOM   2114 N  N   . LYS A 1 280  ? 17.081 57.659  20.639  1.00 9.71  ? 280  LYS A N   1 
ATOM   2115 C  CA  . LYS A 1 280  ? 16.716 58.236  21.928  1.00 10.03 ? 280  LYS A CA  1 
ATOM   2116 C  C   . LYS A 1 280  ? 17.324 57.345  23.029  1.00 9.98  ? 280  LYS A C   1 
ATOM   2117 O  O   . LYS A 1 280  ? 17.670 57.858  24.103  1.00 12.22 ? 280  LYS A O   1 
ATOM   2118 C  CB  . LYS A 1 280  ? 15.190 58.318  22.072  1.00 13.31 ? 280  LYS A CB  1 
ATOM   2119 C  CG  . LYS A 1 280  ? 14.741 58.785  23.438  1.00 15.69 ? 280  LYS A CG  1 
ATOM   2120 C  CD  . LYS A 1 280  ? 13.199 58.768  23.454  1.00 24.50 ? 280  LYS A CD  1 
ATOM   2121 C  CE  . LYS A 1 280  ? 12.756 57.962  24.681  1.00 35.12 ? 280  LYS A CE  1 
ATOM   2122 N  NZ  . LYS A 1 280  ? 13.620 56.711  24.916  1.00 39.00 ? 280  LYS A NZ  1 
ATOM   2123 N  N   . VAL A 1 281  ? 17.453 56.046  22.763  1.00 10.80 ? 281  VAL A N   1 
ATOM   2124 C  CA  . VAL A 1 281  ? 18.089 55.176  23.732  1.00 10.75 ? 281  VAL A CA  1 
ATOM   2125 C  C   . VAL A 1 281  ? 19.632 55.284  23.636  1.00 9.71  ? 281  VAL A C   1 
ATOM   2126 O  O   . VAL A 1 281  ? 20.334 55.458  24.649  1.00 10.27 ? 281  VAL A O   1 
ATOM   2127 C  CB  . VAL A 1 281  ? 17.642 53.674  23.532  1.00 11.65 ? 281  VAL A CB  1 
ATOM   2128 C  CG1 . VAL A 1 281  ? 18.426 52.752  24.494  1.00 13.14 ? 281  VAL A CG1 1 
ATOM   2129 C  CG2 . VAL A 1 281  ? 16.113 53.539  23.789  1.00 12.57 ? 281  VAL A CG2 1 
ATOM   2130 N  N   . CYS A 1 282  ? 20.165 55.110  22.402  1.00 9.22  ? 282  CYS A N   1 
ATOM   2131 C  CA  . CYS A 1 282  ? 21.608 55.119  22.238  1.00 10.07 ? 282  CYS A CA  1 
ATOM   2132 C  C   . CYS A 1 282  ? 22.257 56.413  22.731  1.00 8.02  ? 282  CYS A C   1 
ATOM   2133 O  O   . CYS A 1 282  ? 23.366 56.394  23.245  1.00 9.29  ? 282  CYS A O   1 
ATOM   2134 C  CB  . CYS A 1 282  ? 21.977 54.913  20.761  1.00 10.10 ? 282  CYS A CB  1 
ATOM   2135 S  SG  . CYS A 1 282  ? 21.524 53.323  20.075  1.00 11.78 ? 282  CYS A SG  1 
ATOM   2136 N  N   . CYS A 1 283  ? 21.567 57.564  22.579  1.00 8.71  ? 283  CYS A N   1 
ATOM   2137 C  CA  . CYS A 1 283  ? 22.125 58.789  23.064  1.00 9.53  ? 283  CYS A CA  1 
ATOM   2138 C  C   . CYS A 1 283  ? 22.437 58.791  24.563  1.00 8.94  ? 283  CYS A C   1 
ATOM   2139 O  O   . CYS A 1 283  ? 23.348 59.451  25.026  1.00 9.09  ? 283  CYS A O   1 
ATOM   2140 C  CB  . CYS A 1 283  ? 21.183 59.950  22.682  1.00 10.49 ? 283  CYS A CB  1 
ATOM   2141 S  SG  . CYS A 1 283  ? 21.987 61.580  22.797  1.00 12.02 ? 283  CYS A SG  1 
ATOM   2142 N  N   . GLN A 1 284  ? 21.677 57.962  25.320  1.00 9.98  ? 284  GLN A N   1 
ATOM   2143 C  CA  . GLN A 1 284  ? 21.889 57.861  26.746  1.00 10.61 ? 284  GLN A CA  1 
ATOM   2144 C  C   . GLN A 1 284  ? 23.149 57.082  27.091  1.00 8.59  ? 284  GLN A C   1 
ATOM   2145 O  O   . GLN A 1 284  ? 23.516 57.008  28.257  1.00 11.21 ? 284  GLN A O   1 
ATOM   2146 C  CB  . GLN A 1 284  ? 20.687 57.186  27.404  1.00 11.12 ? 284  GLN A CB  1 
ATOM   2147 C  CG  . GLN A 1 284  ? 19.398 57.950  27.197  1.00 11.20 ? 284  GLN A CG  1 
ATOM   2148 C  CD  . GLN A 1 284  ? 18.205 57.151  27.719  1.00 15.03 ? 284  GLN A CD  1 
ATOM   2149 O  OE1 . GLN A 1 284  ? 18.182 56.773  28.886  1.00 16.22 ? 284  GLN A OE1 1 
ATOM   2150 N  NE2 . GLN A 1 284  ? 17.227 56.913  26.867  1.00 15.08 ? 284  GLN A NE2 1 
ATOM   2151 N  N   . PHE A 1 285  ? 23.846 56.548  26.076  1.00 8.68  ? 285  PHE A N   1 
ATOM   2152 C  CA  . PHE A 1 285  ? 25.082 55.826  26.286  1.00 8.83  ? 285  PHE A CA  1 
ATOM   2153 C  C   . PHE A 1 285  ? 26.271 56.566  25.668  1.00 8.19  ? 285  PHE A C   1 
ATOM   2154 O  O   . PHE A 1 285  ? 27.327 55.965  25.430  1.00 9.43  ? 285  PHE A O   1 
ATOM   2155 C  CB  . PHE A 1 285  ? 24.916 54.367  25.817  1.00 8.79  ? 285  PHE A CB  1 
ATOM   2156 C  CG  . PHE A 1 285  ? 23.896 53.628  26.672  1.00 9.74  ? 285  PHE A CG  1 
ATOM   2157 C  CD1 . PHE A 1 285  ? 24.286 53.031  27.872  1.00 10.68 ? 285  PHE A CD1 1 
ATOM   2158 C  CD2 . PHE A 1 285  ? 22.543 53.621  26.296  1.00 11.06 ? 285  PHE A CD2 1 
ATOM   2159 C  CE1 . PHE A 1 285  ? 23.318 52.424  28.696  1.00 11.44 ? 285  PHE A CE1 1 
ATOM   2160 C  CE2 . PHE A 1 285  ? 21.566 53.021  27.122  1.00 12.73 ? 285  PHE A CE2 1 
ATOM   2161 C  CZ  . PHE A 1 285  ? 21.980 52.418  28.334  1.00 12.19 ? 285  PHE A CZ  1 
ATOM   2162 N  N   . ASP A 1 286  ? 26.066 57.862  25.417  1.00 8.87  ? 286  ASP A N   1 
ATOM   2163 C  CA  . ASP A 1 286  ? 27.162 58.749  25.019  1.00 8.03  ? 286  ASP A CA  1 
ATOM   2164 C  C   . ASP A 1 286  ? 27.408 59.556  26.305  1.00 9.02  ? 286  ASP A C   1 
ATOM   2165 O  O   . ASP A 1 286  ? 26.724 60.563  26.532  1.00 9.50  ? 286  ASP A O   1 
ATOM   2166 C  CB  . ASP A 1 286  ? 26.763 59.638  23.865  1.00 9.24  ? 286  ASP A CB  1 
ATOM   2167 C  CG  . ASP A 1 286  ? 27.927 60.512  23.400  1.00 7.62  ? 286  ASP A CG  1 
ATOM   2168 O  OD1 . ASP A 1 286  ? 28.938 60.590  24.123  1.00 8.33  ? 286  ASP A OD1 1 
ATOM   2169 O  OD2 . ASP A 1 286  ? 27.738 61.141  22.346  1.00 8.76  ? 286  ASP A OD2 1 
ATOM   2170 N  N   . PHE A 1 287  ? 28.383 59.153  27.121  1.00 7.49  ? 287  PHE A N   1 
ATOM   2171 C  CA  . PHE A 1 287  ? 28.523 59.755  28.420  1.00 7.97  ? 287  PHE A CA  1 
ATOM   2172 C  C   . PHE A 1 287  ? 29.102 61.129  28.423  1.00 10.35 ? 287  PHE A C   1 
ATOM   2173 O  O   . PHE A 1 287  ? 29.199 61.750  29.473  1.00 10.97 ? 287  PHE A O   1 
ATOM   2174 C  CB  . PHE A 1 287  ? 29.232 58.774  29.373  1.00 9.80  ? 287  PHE A CB  1 
ATOM   2175 C  CG  . PHE A 1 287  ? 28.425 57.514  29.624  1.00 9.29  ? 287  PHE A CG  1 
ATOM   2176 C  CD1 . PHE A 1 287  ? 27.428 57.514  30.646  1.00 10.10 ? 287  PHE A CD1 1 
ATOM   2177 C  CD2 . PHE A 1 287  ? 28.586 56.388  28.841  1.00 9.84  ? 287  PHE A CD2 1 
ATOM   2178 C  CE1 . PHE A 1 287  ? 26.624 56.387  30.854  1.00 9.24  ? 287  PHE A CE1 1 
ATOM   2179 C  CE2 . PHE A 1 287  ? 27.779 55.275  29.017  1.00 10.89 ? 287  PHE A CE2 1 
ATOM   2180 C  CZ  . PHE A 1 287  ? 26.772 55.258  30.056  1.00 10.19 ? 287  PHE A CZ  1 
ATOM   2181 N  N   . LYS A 1 288  ? 29.466 61.648  27.238  1.00 9.59  ? 288  LYS A N   1 
ATOM   2182 C  CA  . LYS A 1 288  ? 29.906 63.031  27.141  1.00 9.32  ? 288  LYS A CA  1 
ATOM   2183 C  C   . LYS A 1 288  ? 28.695 63.983  27.077  1.00 10.49 ? 288  LYS A C   1 
ATOM   2184 O  O   . LYS A 1 288  ? 28.902 65.197  27.104  1.00 10.92 ? 288  LYS A O   1 
ATOM   2185 C  CB  . LYS A 1 288  ? 30.749 63.214  25.828  1.00 9.73  ? 288  LYS A CB  1 
ATOM   2186 C  CG  . LYS A 1 288  ? 31.627 64.521  25.918  1.00 9.58  ? 288  LYS A CG  1 
ATOM   2187 C  CD  . LYS A 1 288  ? 32.490 64.649  24.667  1.00 8.93  ? 288  LYS A CD  1 
ATOM   2188 C  CE  . LYS A 1 288  ? 33.311 65.916  24.828  1.00 9.52  ? 288  LYS A CE  1 
ATOM   2189 N  NZ  . LYS A 1 288  ? 34.326 66.065  23.656  1.00 12.01 ? 288  LYS A NZ  1 
ATOM   2190 N  N   . ARG A 1 289  ? 27.443 63.485  27.068  1.00 10.19 ? 289  ARG A N   1 
ATOM   2191 C  CA  . ARG A 1 289  ? 26.294 64.367  26.909  1.00 10.70 ? 289  ARG A CA  1 
ATOM   2192 C  C   . ARG A 1 289  ? 25.483 64.656  28.216  1.00 13.16 ? 289  ARG A C   1 
ATOM   2193 O  O   . ARG A 1 289  ? 24.267 64.920  28.129  1.00 14.46 ? 289  ARG A O   1 
ATOM   2194 C  CB  . ARG A 1 289  ? 25.326 63.788  25.879  1.00 10.17 ? 289  ARG A CB  1 
ATOM   2195 C  CG  . ARG A 1 289  ? 25.960 63.588  24.507  1.00 10.86 ? 289  ARG A CG  1 
ATOM   2196 C  CD  . ARG A 1 289  ? 24.963 63.151  23.520  1.00 11.92 ? 289  ARG A CD  1 
ATOM   2197 N  NE  . ARG A 1 289  ? 25.515 62.868  22.190  1.00 10.85 ? 289  ARG A NE  1 
ATOM   2198 C  CZ  . ARG A 1 289  ? 25.075 63.390  21.057  1.00 9.95  ? 289  ARG A CZ  1 
ATOM   2199 N  NH1 . ARG A 1 289  ? 24.074 64.287  21.032  1.00 12.75 ? 289  ARG A NH1 1 
ATOM   2200 N  NH2 . ARG A 1 289  ? 25.573 62.910  19.903  1.00 10.99 ? 289  ARG A NH2 1 
ATOM   2201 N  N   . MET A 1 290  ? 26.137 64.666  29.387  1.00 17.11 ? 290  MET A N   1 
ATOM   2202 C  CA  . MET A 1 290  ? 25.404 64.897  30.661  1.00 18.53 ? 290  MET A CA  1 
ATOM   2203 C  C   . MET A 1 290  ? 25.329 66.377  31.069  1.00 20.95 ? 290  MET A C   1 
ATOM   2204 O  O   . MET A 1 290  ? 24.562 66.720  32.017  1.00 22.25 ? 290  MET A O   1 
ATOM   2205 C  CB  . MET A 1 290  ? 25.962 64.003  31.795  1.00 19.33 ? 290  MET A CB  1 
ATOM   2206 C  CG  . MET A 1 290  ? 25.758 62.551  31.479  1.00 20.76 ? 290  MET A CG  1 
ATOM   2207 S  SD  . MET A 1 290  ? 26.182 61.426  32.816  1.00 21.64 ? 290  MET A SD  1 
ATOM   2208 C  CE  . MET A 1 290  ? 27.963 61.510  32.717  1.00 21.57 ? 290  MET A CE  1 
ATOM   2209 N  N   . GLY A 1 291  ? 26.081 67.248  30.351  1.00 18.51 ? 291  GLY A N   1 
ATOM   2210 C  CA  . GLY A 1 291  ? 26.021 68.692  30.601  1.00 17.87 ? 291  GLY A CA  1 
ATOM   2211 C  C   . GLY A 1 291  ? 27.324 69.521  30.693  1.00 20.67 ? 291  GLY A C   1 
ATOM   2212 O  O   . GLY A 1 291  ? 27.490 70.582  30.030  1.00 20.15 ? 291  GLY A O   1 
ATOM   2213 N  N   . SER A 1 292  ? 28.270 69.046  31.503  1.00 17.54 ? 292  SER A N   1 
ATOM   2214 C  CA  . SER A 1 292  ? 29.515 69.775  31.707  1.00 13.00 ? 292  SER A CA  1 
ATOM   2215 C  C   . SER A 1 292  ? 30.406 69.960  30.470  1.00 12.39 ? 292  SER A C   1 
ATOM   2216 O  O   . SER A 1 292  ? 31.318 70.796  30.505  1.00 12.32 ? 292  SER A O   1 
ATOM   2217 C  CB  . SER A 1 292  ? 30.308 69.109  32.822  1.00 15.62 ? 292  SER A CB  1 
ATOM   2218 O  OG  . SER A 1 292  ? 30.804 67.867  32.333  1.00 17.98 ? 292  SER A OG  1 
ATOM   2219 N  N   . PHE A 1 293  ? 30.183 69.151  29.424  1.00 10.96 ? 293  PHE A N   1 
ATOM   2220 C  CA  . PHE A 1 293  ? 30.900 69.255  28.163  1.00 10.31 ? 293  PHE A CA  1 
ATOM   2221 C  C   . PHE A 1 293  ? 30.139 70.068  27.129  1.00 11.60 ? 293  PHE A C   1 
ATOM   2222 O  O   . PHE A 1 293  ? 30.586 70.144  25.983  1.00 13.58 ? 293  PHE A O   1 
ATOM   2223 C  CB  . PHE A 1 293  ? 31.175 67.814  27.578  1.00 12.87 ? 293  PHE A CB  1 
ATOM   2224 C  CG  . PHE A 1 293  ? 32.092 66.991  28.418  1.00 11.65 ? 293  PHE A CG  1 
ATOM   2225 C  CD1 . PHE A 1 293  ? 33.442 67.123  28.290  1.00 11.61 ? 293  PHE A CD1 1 
ATOM   2226 C  CD2 . PHE A 1 293  ? 31.577 66.061  29.291  1.00 11.96 ? 293  PHE A CD2 1 
ATOM   2227 C  CE1 . PHE A 1 293  ? 34.332 66.291  29.048  1.00 14.16 ? 293  PHE A CE1 1 
ATOM   2228 C  CE2 . PHE A 1 293  ? 32.429 65.230  30.062  1.00 12.52 ? 293  PHE A CE2 1 
ATOM   2229 C  CZ  . PHE A 1 293  ? 33.800 65.371  29.914  1.00 13.92 ? 293  PHE A CZ  1 
ATOM   2230 N  N   . GLY A 1 294  ? 29.008 70.654  27.528  1.00 12.71 ? 294  GLY A N   1 
ATOM   2231 C  CA  . GLY A 1 294  ? 28.258 71.451  26.544  1.00 13.53 ? 294  GLY A CA  1 
ATOM   2232 C  C   . GLY A 1 294  ? 27.532 70.671  25.452  1.00 14.33 ? 294  GLY A C   1 
ATOM   2233 O  O   . GLY A 1 294  ? 27.231 71.188  24.365  1.00 17.20 ? 294  GLY A O   1 
ATOM   2234 N  N   . LEU A 1 295  ? 27.276 69.388  25.693  1.00 12.56 ? 295  LEU A N   1 
ATOM   2235 C  CA  . LEU A 1 295  ? 26.561 68.560  24.745  1.00 11.38 ? 295  LEU A CA  1 
ATOM   2236 C  C   . LEU A 1 295  ? 25.320 68.001  25.452  1.00 13.19 ? 295  LEU A C   1 
ATOM   2237 O  O   . LEU A 1 295  ? 25.321 67.864  26.668  1.00 14.43 ? 295  LEU A O   1 
ATOM   2238 C  CB  . LEU A 1 295  ? 27.432 67.390  24.270  1.00 12.54 ? 295  LEU A CB  1 
ATOM   2239 C  CG  . LEU A 1 295  ? 28.773 67.842  23.671  1.00 13.80 ? 295  LEU A CG  1 
ATOM   2240 C  CD1 . LEU A 1 295  ? 29.615 66.599  23.374  1.00 14.54 ? 295  LEU A CD1 1 
ATOM   2241 C  CD2 . LEU A 1 295  ? 28.523 68.622  22.350  1.00 15.60 ? 295  LEU A CD2 1 
ATOM   2242 N  N   . SER A 1 296  ? 24.304 67.663  24.668  1.00 11.40 ? 296  SER A N   1 
ATOM   2243 C  CA  . SER A 1 296  ? 23.057 67.127  25.216  1.00 13.78 ? 296  SER A CA  1 
ATOM   2244 C  C   . SER A 1 296  ? 22.460 66.201  24.180  1.00 13.70 ? 296  SER A C   1 
ATOM   2245 O  O   . SER A 1 296  ? 22.981 66.047  23.074  1.00 12.90 ? 296  SER A O   1 
ATOM   2246 C  CB  . SER A 1 296  ? 22.080 68.302  25.579  1.00 14.91 ? 296  SER A CB  1 
ATOM   2247 O  OG  . SER A 1 296  ? 21.828 69.089  24.435  1.00 17.19 ? 296  SER A OG  1 
ATOM   2248 N  N   . CYS A 1 297  ? 21.348 65.529  24.556  1.00 13.35 ? 297  CYS A N   1 
ATOM   2249 C  CA  . CYS A 1 297  ? 20.628 64.612  23.656  1.00 13.81 ? 297  CYS A CA  1 
ATOM   2250 C  C   . CYS A 1 297  ? 19.412 65.320  23.071  1.00 13.63 ? 297  CYS A C   1 
ATOM   2251 O  O   . CYS A 1 297  ? 18.522 65.733  23.858  1.00 15.63 ? 297  CYS A O   1 
ATOM   2252 C  CB  . CYS A 1 297  ? 20.153 63.366  24.429  1.00 14.08 ? 297  CYS A CB  1 
ATOM   2253 S  SG  . CYS A 1 297  ? 21.574 62.228  24.737  1.00 15.65 ? 297  CYS A SG  1 
ATOM   2254 N  N   . PRO A 1 298  ? 19.315 65.419  21.748  1.00 15.85 ? 298  PRO A N   1 
ATOM   2255 C  CA  . PRO A 1 298  ? 18.135 66.115  21.213  1.00 17.10 ? 298  PRO A CA  1 
ATOM   2256 C  C   . PRO A 1 298  ? 16.842 65.346  21.410  1.00 14.91 ? 298  PRO A C   1 
ATOM   2257 O  O   . PRO A 1 298  ? 15.751 65.924  21.240  1.00 16.74 ? 298  PRO A O   1 
ATOM   2258 C  CB  . PRO A 1 298  ? 18.460 66.365  19.752  1.00 20.69 ? 298  PRO A CB  1 
ATOM   2259 C  CG  . PRO A 1 298  ? 19.665 65.510  19.417  1.00 18.83 ? 298  PRO A CG  1 
ATOM   2260 C  CD  . PRO A 1 298  ? 20.366 65.170  20.732  1.00 13.32 ? 298  PRO A CD  1 
ATOM   2261 N  N   . TRP A 1 299  ? 16.904 64.061  21.743  1.00 12.32 ? 299  TRP A N   1 
ATOM   2262 C  CA  . TRP A 1 299  ? 15.692 63.263  21.989  1.00 13.91 ? 299  TRP A CA  1 
ATOM   2263 C  C   . TRP A 1 299  ? 15.217 63.478  23.425  1.00 14.51 ? 299  TRP A C   1 
ATOM   2264 O  O   . TRP A 1 299  ? 14.245 62.883  23.865  1.00 16.89 ? 299  TRP A O   1 
ATOM   2265 C  CB  . TRP A 1 299  ? 15.962 61.761  21.694  1.00 13.00 ? 299  TRP A CB  1 
ATOM   2266 C  CG  . TRP A 1 299  ? 16.339 61.581  20.255  1.00 12.18 ? 299  TRP A CG  1 
ATOM   2267 C  CD1 . TRP A 1 299  ? 15.498 61.395  19.211  1.00 12.75 ? 299  TRP A CD1 1 
ATOM   2268 C  CD2 . TRP A 1 299  ? 17.654 61.649  19.704  1.00 10.15 ? 299  TRP A CD2 1 
ATOM   2269 N  NE1 . TRP A 1 299  ? 16.206 61.309  18.042  1.00 15.17 ? 299  TRP A NE1 1 
ATOM   2270 C  CE2 . TRP A 1 299  ? 17.532 61.470  18.323  1.00 12.78 ? 299  TRP A CE2 1 
ATOM   2271 C  CE3 . TRP A 1 299  ? 18.924 61.811  20.253  1.00 12.71 ? 299  TRP A CE3 1 
ATOM   2272 C  CZ2 . TRP A 1 299  ? 18.622 61.470  17.477  1.00 13.72 ? 299  TRP A CZ2 1 
ATOM   2273 C  CZ3 . TRP A 1 299  ? 20.005 61.809  19.411  1.00 12.76 ? 299  TRP A CZ3 1 
ATOM   2274 C  CH2 . TRP A 1 299  ? 19.845 61.648  18.038  1.00 12.15 ? 299  TRP A CH2 1 
ATOM   2275 N  N   . LYS A 1 300  ? 15.914 64.356  24.134  1.00 13.14 ? 300  LYS A N   1 
ATOM   2276 C  CA  . LYS A 1 300  ? 15.496 64.837  25.469  1.00 15.29 ? 300  LYS A CA  1 
ATOM   2277 C  C   . LYS A 1 300  ? 15.598 63.896  26.651  1.00 19.05 ? 300  LYS A C   1 
ATOM   2278 O  O   . LYS A 1 300  ? 14.974 64.142  27.701  1.00 20.06 ? 300  LYS A O   1 
ATOM   2279 C  CB  . LYS A 1 300  ? 14.057 65.391  25.366  1.00 19.22 ? 300  LYS A CB  1 
ATOM   2280 C  CG  . LYS A 1 300  ? 13.891 66.517  24.400  1.00 23.96 ? 300  LYS A CG  1 
ATOM   2281 C  CD  . LYS A 1 300  ? 12.401 66.831  24.303  1.00 26.23 ? 300  LYS A CD  1 
ATOM   2282 C  CE  . LYS A 1 300  ? 12.144 67.988  23.378  1.00 33.03 ? 300  LYS A CE  1 
ATOM   2283 N  NZ  . LYS A 1 300  ? 12.786 67.759  22.060  1.00 38.40 ? 300  LYS A NZ  1 
ATOM   2284 N  N   . VAL A 1 301  ? 16.319 62.789  26.508  1.00 15.02 ? 301  VAL A N   1 
ATOM   2285 C  CA  . VAL A 1 301  ? 16.558 61.907  27.621  1.00 15.59 ? 301  VAL A CA  1 
ATOM   2286 C  C   . VAL A 1 301  ? 18.100 61.899  27.730  1.00 14.44 ? 301  VAL A C   1 
ATOM   2287 O  O   . VAL A 1 301  ? 18.782 61.458  26.808  1.00 16.12 ? 301  VAL A O   1 
ATOM   2288 C  CB  . VAL A 1 301  ? 16.025 60.499  27.388  1.00 17.04 ? 301  VAL A CB  1 
ATOM   2289 C  CG1 . VAL A 1 301  ? 16.266 59.715  28.681  1.00 19.29 ? 301  VAL A CG1 1 
ATOM   2290 C  CG2 . VAL A 1 301  ? 14.458 60.531  27.049  1.00 20.03 ? 301  VAL A CG2 1 
ATOM   2291 N  N   . PRO A 1 302  ? 18.657 62.349  28.841  1.00 14.57 ? 302  PRO A N   1 
ATOM   2292 C  CA  . PRO A 1 302  ? 20.110 62.382  28.954  1.00 15.15 ? 302  PRO A CA  1 
ATOM   2293 C  C   . PRO A 1 302  ? 20.737 61.111  29.446  1.00 14.33 ? 302  PRO A C   1 
ATOM   2294 O  O   . PRO A 1 302  ? 20.072 60.194  29.928  1.00 14.55 ? 302  PRO A O   1 
ATOM   2295 C  CB  . PRO A 1 302  ? 20.339 63.473  30.004  1.00 15.35 ? 302  PRO A CB  1 
ATOM   2296 C  CG  . PRO A 1 302  ? 19.140 63.207  30.988  1.00 17.82 ? 302  PRO A CG  1 
ATOM   2297 C  CD  . PRO A 1 302  ? 17.996 62.926  30.043  1.00 16.43 ? 302  PRO A CD  1 
ATOM   2298 N  N   . PRO A 1 303  ? 22.045 60.969  29.231  1.00 11.82 ? 303  PRO A N   1 
ATOM   2299 C  CA  . PRO A 1 303  ? 22.709 59.798  29.780  1.00 11.87 ? 303  PRO A CA  1 
ATOM   2300 C  C   . PRO A 1 303  ? 22.735 60.012  31.314  1.00 14.87 ? 303  PRO A C   1 
ATOM   2301 O  O   . PRO A 1 303  ? 22.659 61.150  31.828  1.00 14.07 ? 303  PRO A O   1 
ATOM   2302 C  CB  . PRO A 1 303  ? 24.168 59.933  29.331  1.00 12.50 ? 303  PRO A CB  1 
ATOM   2303 C  CG  . PRO A 1 303  ? 24.241 61.209  28.525  1.00 15.96 ? 303  PRO A CG  1 
ATOM   2304 C  CD  . PRO A 1 303  ? 22.953 61.899  28.534  1.00 14.20 ? 303  PRO A CD  1 
ATOM   2305 N  N   . ARG A 1 304  ? 22.810 58.906  32.044  1.00 14.72 ? 304  ARG A N   1 
ATOM   2306 C  CA  . ARG A 1 304  ? 22.959 58.971  33.483  1.00 16.15 ? 304  ARG A CA  1 
ATOM   2307 C  C   . ARG A 1 304  ? 24.140 58.100  33.850  1.00 11.40 ? 304  ARG A C   1 
ATOM   2308 O  O   . ARG A 1 304  ? 24.345 57.019  33.253  1.00 12.65 ? 304  ARG A O   1 
ATOM   2309 C  CB  . ARG A 1 304  ? 21.710 58.459  34.200  1.00 19.21 ? 304  ARG A CB  1 
ATOM   2310 C  CG  . ARG A 1 304  ? 20.625 59.508  34.284  1.00 24.58 ? 304  ARG A CG  1 
ATOM   2311 C  CD  . ARG A 1 304  ? 19.412 58.946  34.979  1.00 28.06 ? 304  ARG A CD  1 
ATOM   2312 N  NE  . ARG A 1 304  ? 18.639 58.086  34.087  1.00 30.08 ? 304  ARG A NE  1 
ATOM   2313 C  CZ  . ARG A 1 304  ? 18.436 56.790  34.297  1.00 34.99 ? 304  ARG A CZ  1 
ATOM   2314 N  NH1 . ARG A 1 304  ? 18.958 56.199  35.372  1.00 37.80 ? 304  ARG A NH1 1 
ATOM   2315 N  NH2 . ARG A 1 304  ? 17.696 56.093  33.448  1.00 37.25 ? 304  ARG A NH2 1 
ATOM   2316 N  N   . THR A 1 305  ? 24.923 58.568  34.808  1.00 12.67 ? 305  THR A N   1 
ATOM   2317 C  CA  . THR A 1 305  ? 26.085 57.826  35.302  1.00 13.04 ? 305  THR A CA  1 
ATOM   2318 C  C   . THR A 1 305  ? 25.673 56.438  35.734  1.00 13.03 ? 305  THR A C   1 
ATOM   2319 O  O   . THR A 1 305  ? 24.633 56.300  36.396  1.00 13.52 ? 305  THR A O   1 
ATOM   2320 C  CB  . THR A 1 305  ? 26.743 58.562  36.487  1.00 15.80 ? 305  THR A CB  1 
ATOM   2321 O  OG1 . THR A 1 305  ? 27.268 59.805  35.975  1.00 16.18 ? 305  THR A OG1 1 
ATOM   2322 C  CG2 . THR A 1 305  ? 27.819 57.768  37.157  1.00 16.50 ? 305  THR A CG2 1 
ATOM   2323 N  N   . ILE A 1 306  ? 26.422 55.405  35.363  1.00 10.70 ? 306  ILE A N   1 
ATOM   2324 C  CA  . ILE A 1 306  ? 26.080 54.025  35.728  1.00 10.00 ? 306  ILE A CA  1 
ATOM   2325 C  C   . ILE A 1 306  ? 26.470 53.804  37.175  1.00 10.86 ? 306  ILE A C   1 
ATOM   2326 O  O   . ILE A 1 306  ? 27.539 54.178  37.619  1.00 12.96 ? 306  ILE A O   1 
ATOM   2327 C  CB  . ILE A 1 306  ? 26.798 53.029  34.758  1.00 9.13  ? 306  ILE A CB  1 
ATOM   2328 C  CG1 . ILE A 1 306  ? 26.448 53.343  33.286  1.00 10.55 ? 306  ILE A CG1 1 
ATOM   2329 C  CG2 . ILE A 1 306  ? 26.386 51.548  35.116  1.00 11.00 ? 306  ILE A CG2 1 
ATOM   2330 C  CD1 . ILE A 1 306  ? 24.947 53.301  32.940  1.00 11.43 ? 306  ILE A CD1 1 
ATOM   2331 N  N   . SER A 1 307  ? 25.527 53.200  37.920  1.00 12.11 ? 307  SER A N   1 
ATOM   2332 C  CA  . SER A 1 307  ? 25.733 52.892  39.354  1.00 12.54 ? 307  SER A CA  1 
ATOM   2333 C  C   . SER A 1 307  ? 25.254 51.464  39.608  1.00 11.43 ? 307  SER A C   1 
ATOM   2334 O  O   . SER A 1 307  ? 24.556 50.867  38.784  1.00 11.07 ? 307  SER A O   1 
ATOM   2335 C  CB  . SER A 1 307  ? 24.863 53.821  40.217  1.00 12.67 ? 307  SER A CB  1 
ATOM   2336 O  OG  . SER A 1 307  ? 23.493 53.492  40.032  1.00 13.53 ? 307  SER A OG  1 
ATOM   2337 N  N   . ASP A 1 308  ? 25.562 50.929  40.802  1.00 13.42 ? 308  ASP A N   1 
ATOM   2338 C  CA  . ASP A 1 308  ? 25.028 49.599  41.060  1.00 13.95 ? 308  ASP A CA  1 
ATOM   2339 C  C   . ASP A 1 308  ? 23.486 49.579  41.125  1.00 12.49 ? 308  ASP A C   1 
ATOM   2340 O  O   . ASP A 1 308  ? 22.905 48.507  40.886  1.00 13.28 ? 308  ASP A O   1 
ATOM   2341 C  CB  . ASP A 1 308  ? 25.554 49.035  42.377  1.00 19.28 ? 308  ASP A CB  1 
ATOM   2342 C  CG  . ASP A 1 308  ? 27.063 48.866  42.394  1.00 24.36 ? 308  ASP A CG  1 
ATOM   2343 O  OD1 . ASP A 1 308  ? 27.710 48.751  41.320  1.00 25.87 ? 308  ASP A OD1 1 
ATOM   2344 O  OD2 . ASP A 1 308  ? 27.608 48.825  43.522  1.00 30.14 ? 308  ASP A OD2 1 
ATOM   2345 N  N   . GLN A 1 309  ? 22.844 50.723  41.364  1.00 12.83 ? 309  GLN A N   1 
ATOM   2346 C  CA  . GLN A 1 309  ? 21.376 50.770  41.463  1.00 13.22 ? 309  GLN A CA  1 
ATOM   2347 C  C   . GLN A 1 309  ? 20.681 50.874  40.122  1.00 14.20 ? 309  GLN A C   1 
ATOM   2348 O  O   . GLN A 1 309  ? 19.519 50.508  40.007  1.00 15.10 ? 309  GLN A O   1 
ATOM   2349 C  CB  . GLN A 1 309  ? 20.934 51.934  42.363  1.00 11.47 ? 309  GLN A CB  1 
ATOM   2350 C  CG  . GLN A 1 309  ? 21.365 51.811  43.819  1.00 14.86 ? 309  GLN A CG  1 
ATOM   2351 C  CD  . GLN A 1 309  ? 22.869 51.958  44.005  1.00 16.57 ? 309  GLN A CD  1 
ATOM   2352 O  OE1 . GLN A 1 309  ? 23.478 52.902  43.477  1.00 17.82 ? 309  GLN A OE1 1 
ATOM   2353 N  NE2 . GLN A 1 309  ? 23.476 51.036  44.755  1.00 18.70 ? 309  GLN A NE2 1 
ATOM   2354 N  N   . ASN A 1 310  ? 21.371 51.369  39.089  1.00 12.70 ? 310  ASN A N   1 
ATOM   2355 C  CA  . ASN A 1 310  ? 20.732 51.477  37.785  1.00 10.67 ? 310  ASN A CA  1 
ATOM   2356 C  C   . ASN A 1 310  ? 21.384 50.605  36.719  1.00 10.08 ? 310  ASN A C   1 
ATOM   2357 O  O   . ASN A 1 310  ? 20.858 50.530  35.631  1.00 11.12 ? 310  ASN A O   1 
ATOM   2358 C  CB  . ASN A 1 310  ? 20.655 52.956  37.307  1.00 12.19 ? 310  ASN A CB  1 
ATOM   2359 C  CG  . ASN A 1 310  ? 22.029 53.527  36.925  1.00 12.76 ? 310  ASN A CG  1 
ATOM   2360 O  OD1 . ASN A 1 310  ? 22.975 52.782  36.674  1.00 12.03 ? 310  ASN A OD1 1 
ATOM   2361 N  ND2 . ASN A 1 310  ? 22.114 54.852  36.855  1.00 14.44 ? 310  ASN A ND2 1 
ATOM   2362 N  N   . VAL A 1 311  ? 22.439 49.880  37.045  1.00 10.19 ? 311  VAL A N   1 
ATOM   2363 C  CA  . VAL A 1 311  ? 23.145 49.145  36.001  1.00 10.76 ? 311  VAL A CA  1 
ATOM   2364 C  C   . VAL A 1 311  ? 22.285 48.070  35.354  1.00 10.63 ? 311  VAL A C   1 
ATOM   2365 O  O   . VAL A 1 311  ? 22.378 47.877  34.166  1.00 10.98 ? 311  VAL A O   1 
ATOM   2366 C  CB  . VAL A 1 311  ? 24.507 48.602  36.441  1.00 10.27 ? 311  VAL A CB  1 
ATOM   2367 C  CG1 . VAL A 1 311  ? 24.346 47.533  37.504  1.00 12.94 ? 311  VAL A CG1 1 
ATOM   2368 C  CG2 . VAL A 1 311  ? 25.328 48.097  35.215  1.00 11.88 ? 311  VAL A CG2 1 
ATOM   2369 N  N   . ALA A 1 312  ? 21.432 47.390  36.112  1.00 10.06 ? 312  ALA A N   1 
ATOM   2370 C  CA  . ALA A 1 312  ? 20.580 46.358  35.515  1.00 10.64 ? 312  ALA A CA  1 
ATOM   2371 C  C   . ALA A 1 312  ? 19.609 46.928  34.487  1.00 11.38 ? 312  ALA A C   1 
ATOM   2372 O  O   . ALA A 1 312  ? 19.470 46.383  33.422  1.00 11.27 ? 312  ALA A O   1 
ATOM   2373 C  CB  . ALA A 1 312  ? 19.837 45.518  36.598  1.00 11.91 ? 312  ALA A CB  1 
ATOM   2374 N  N   . ALA A 1 313  ? 18.931 48.027  34.817  1.00 10.99 ? 313  ALA A N   1 
ATOM   2375 C  CA  . ALA A 1 313  ? 17.954 48.639  33.910  1.00 10.60 ? 313  ALA A CA  1 
ATOM   2376 C  C   . ALA A 1 313  ? 18.679 49.249  32.713  1.00 12.57 ? 313  ALA A C   1 
ATOM   2377 O  O   . ALA A 1 313  ? 18.192 49.142  31.605  1.00 12.51 ? 313  ALA A O   1 
ATOM   2378 C  CB  . ALA A 1 313  ? 17.168 49.698  34.655  1.00 12.76 ? 313  ALA A CB  1 
ATOM   2379 N  N   . ARG A 1 314  ? 19.819 49.871  32.958  1.00 11.34 ? 314  ARG A N   1 
ATOM   2380 C  CA  . ARG A 1 314  ? 20.581 50.461  31.841  1.00 10.35 ? 314  ARG A CA  1 
ATOM   2381 C  C   . ARG A 1 314  ? 21.099 49.345  30.921  1.00 12.45 ? 314  ARG A C   1 
ATOM   2382 O  O   . ARG A 1 314  ? 21.025 49.515  29.666  1.00 11.59 ? 314  ARG A O   1 
ATOM   2383 C  CB  . ARG A 1 314  ? 21.759 51.248  32.417  1.00 10.59 ? 314  ARG A CB  1 
ATOM   2384 C  CG  . ARG A 1 314  ? 21.414 52.451  33.286  1.00 13.09 ? 314  ARG A CG  1 
ATOM   2385 C  CD  . ARG A 1 314  ? 21.132 53.715  32.476  1.00 15.94 ? 314  ARG A CD  1 
ATOM   2386 N  NE  . ARG A 1 314  ? 19.796 53.736  31.924  1.00 17.57 ? 314  ARG A NE  1 
ATOM   2387 C  CZ  . ARG A 1 314  ? 19.324 54.662  31.093  1.00 17.21 ? 314  ARG A CZ  1 
ATOM   2388 N  NH1 . ARG A 1 314  ? 20.134 55.664  30.675  1.00 16.16 ? 314  ARG A NH1 1 
ATOM   2389 N  NH2 . ARG A 1 314  ? 18.028 54.687  30.764  1.00 18.11 ? 314  ARG A NH2 1 
ATOM   2390 N  N   . SER A 1 315  ? 21.560 48.212  31.473  1.00 11.81 ? 315  SER A N   1 
ATOM   2391 C  CA  . SER A 1 315  ? 22.017 47.086  30.653  1.00 12.78 ? 315  SER A CA  1 
ATOM   2392 C  C   . SER A 1 315  ? 20.858 46.492  29.910  1.00 13.42 ? 315  SER A C   1 
ATOM   2393 O  O   . SER A 1 315  ? 20.978 46.073  28.746  1.00 13.31 ? 315  SER A O   1 
ATOM   2394 C  CB  . SER A 1 315  ? 22.685 46.005  31.530  1.00 10.57 ? 315  SER A CB  1 
ATOM   2395 O  OG  . SER A 1 315  ? 23.845 46.491  32.157  1.00 12.39 ? 315  SER A OG  1 
ATOM   2396 N  N   . ASP A 1 316  ? 19.685 46.400  30.548  1.00 12.99 ? 316  ASP A N   1 
ATOM   2397 C  CA  . ASP A 1 316  ? 18.512 45.848  29.853  1.00 14.20 ? 316  ASP A CA  1 
ATOM   2398 C  C   . ASP A 1 316  ? 18.277 46.665  28.563  1.00 11.87 ? 316  ASP A C   1 
ATOM   2399 O  O   . ASP A 1 316  ? 18.017 46.112  27.476  1.00 12.14 ? 316  ASP A O   1 
ATOM   2400 C  CB  . ASP A 1 316  ? 17.212 45.989  30.701  1.00 14.76 ? 316  ASP A CB  1 
ATOM   2401 C  CG  . ASP A 1 316  ? 17.141 45.090  31.919  1.00 15.92 ? 316  ASP A CG  1 
ATOM   2402 O  OD1 . ASP A 1 316  ? 17.846 44.067  31.974  1.00 18.16 ? 316  ASP A OD1 1 
ATOM   2403 O  OD2 . ASP A 1 316  ? 16.299 45.451  32.811  1.00 16.48 ? 316  ASP A OD2 1 
ATOM   2404 N  N   . LEU A 1 317  ? 18.335 47.988  28.697  1.00 10.80 ? 317  LEU A N   1 
ATOM   2405 C  CA  . LEU A 1 317  ? 18.106 48.867  27.534  1.00 11.21 ? 317  LEU A CA  1 
ATOM   2406 C  C   . LEU A 1 317  ? 19.178 48.738  26.472  1.00 10.53 ? 317  LEU A C   1 
ATOM   2407 O  O   . LEU A 1 317  ? 18.859 48.596  25.299  1.00 11.61 ? 317  LEU A O   1 
ATOM   2408 C  CB  . LEU A 1 317  ? 18.054 50.333  27.955  1.00 14.52 ? 317  LEU A CB  1 
ATOM   2409 C  CG  . LEU A 1 317  ? 16.752 50.814  28.530  1.00 17.13 ? 317  LEU A CG  1 
ATOM   2410 C  CD1 . LEU A 1 317  ? 17.029 52.180  29.167  1.00 21.42 ? 317  LEU A CD1 1 
ATOM   2411 C  CD2 . LEU A 1 317  ? 15.695 50.984  27.427  1.00 17.41 ? 317  LEU A CD2 1 
ATOM   2412 N  N   . LEU A 1 318  ? 20.427 48.674  26.898  1.00 10.20 ? 318  LEU A N   1 
ATOM   2413 C  CA  . LEU A 1 318  ? 21.516 48.650  25.935  1.00 9.96  ? 318  LEU A CA  1 
ATOM   2414 C  C   . LEU A 1 318  ? 21.590 47.321  25.238  1.00 11.68 ? 318  LEU A C   1 
ATOM   2415 O  O   . LEU A 1 318  ? 21.717 47.278  23.984  1.00 11.24 ? 318  LEU A O   1 
ATOM   2416 C  CB  . LEU A 1 318  ? 22.820 48.957  26.676  1.00 10.64 ? 318  LEU A CB  1 
ATOM   2417 C  CG  . LEU A 1 318  ? 24.078 49.036  25.782  1.00 11.98 ? 318  LEU A CG  1 
ATOM   2418 C  CD1 . LEU A 1 318  ? 23.856 50.163  24.759  1.00 12.44 ? 318  LEU A CD1 1 
ATOM   2419 C  CD2 . LEU A 1 318  ? 25.295 49.320  26.661  1.00 12.55 ? 318  LEU A CD2 1 
ATOM   2420 N  N   . VAL A 1 319  ? 21.456 46.198  25.965  1.00 9.98  ? 319  VAL A N   1 
ATOM   2421 C  CA  . VAL A 1 319  ? 21.544 44.879  25.332  1.00 10.63 ? 319  VAL A CA  1 
ATOM   2422 C  C   . VAL A 1 319  ? 20.398 44.732  24.331  1.00 9.86  ? 319  VAL A C   1 
ATOM   2423 O  O   . VAL A 1 319  ? 20.604 44.128  23.267  1.00 9.94  ? 319  VAL A O   1 
ATOM   2424 C  CB  . VAL A 1 319  ? 21.574 43.727  26.389  1.00 10.14 ? 319  VAL A CB  1 
ATOM   2425 C  CG1 . VAL A 1 319  ? 21.452 42.362  25.706  1.00 11.35 ? 319  VAL A CG1 1 
ATOM   2426 C  CG2 . VAL A 1 319  ? 22.881 43.832  27.166  1.00 12.25 ? 319  VAL A CG2 1 
ATOM   2427 N  N   . ASP A 1 320  ? 19.203 45.246  24.645  1.00 10.65 ? 320  ASP A N   1 
ATOM   2428 C  CA  . ASP A 1 320  ? 18.085 45.174  23.704  1.00 9.64  ? 320  ASP A CA  1 
ATOM   2429 C  C   . ASP A 1 320  ? 18.445 45.921  22.390  1.00 9.65  ? 320  ASP A C   1 
ATOM   2430 O  O   . ASP A 1 320  ? 18.122 45.412  21.318  1.00 10.47 ? 320  ASP A O   1 
ATOM   2431 C  CB  . ASP A 1 320  ? 16.820 45.741  24.396  1.00 12.24 ? 320  ASP A CB  1 
ATOM   2432 C  CG  . ASP A 1 320  ? 15.649 45.877  23.469  1.00 12.68 ? 320  ASP A CG  1 
ATOM   2433 O  OD1 . ASP A 1 320  ? 15.084 44.806  23.107  1.00 15.84 ? 320  ASP A OD1 1 
ATOM   2434 O  OD2 . ASP A 1 320  ? 15.265 47.012  23.076  1.00 12.67 ? 320  ASP A OD2 1 
ATOM   2435 N  N   . GLN A 1 321  ? 19.069 47.102  22.502  1.00 9.61  ? 321  GLN A N   1 
ATOM   2436 C  CA  . GLN A 1 321  ? 19.524 47.804  21.262  1.00 9.22  ? 321  GLN A CA  1 
ATOM   2437 C  C   . GLN A 1 321  ? 20.536 46.929  20.498  1.00 7.45  ? 321  GLN A C   1 
ATOM   2438 O  O   . GLN A 1 321  ? 20.444 46.772  19.278  1.00 8.76  ? 321  GLN A O   1 
ATOM   2439 C  CB  . GLN A 1 321  ? 20.189 49.135  21.639  1.00 9.37  ? 321  GLN A CB  1 
ATOM   2440 C  CG  . GLN A 1 321  ? 19.175 50.202  22.081  1.00 9.12  ? 321  GLN A CG  1 
ATOM   2441 C  CD  . GLN A 1 321  ? 18.102 50.423  20.971  1.00 12.10 ? 321  GLN A CD  1 
ATOM   2442 O  OE1 . GLN A 1 321  ? 18.429 50.816  19.855  1.00 12.45 ? 321  GLN A OE1 1 
ATOM   2443 N  NE2 . GLN A 1 321  ? 16.819 50.150  21.274  1.00 12.64 ? 321  GLN A NE2 1 
ATOM   2444 N  N   . TRP A 1 322  ? 21.522 46.371  21.204  1.00 8.40  ? 322  TRP A N   1 
ATOM   2445 C  CA  . TRP A 1 322  ? 22.516 45.531  20.550  1.00 8.95  ? 322  TRP A CA  1 
ATOM   2446 C  C   . TRP A 1 322  ? 21.907 44.326  19.864  1.00 9.05  ? 322  TRP A C   1 
ATOM   2447 O  O   . TRP A 1 322  ? 22.301 43.976  18.734  1.00 9.48  ? 322  TRP A O   1 
ATOM   2448 C  CB  . TRP A 1 322  ? 23.551 45.013  21.564  1.00 8.22  ? 322  TRP A CB  1 
ATOM   2449 C  CG  . TRP A 1 322  ? 24.467 46.071  22.124  1.00 9.25  ? 322  TRP A CG  1 
ATOM   2450 C  CD1 . TRP A 1 322  ? 24.667 47.360  21.679  1.00 10.14 ? 322  TRP A CD1 1 
ATOM   2451 C  CD2 . TRP A 1 322  ? 25.385 45.892  23.237  1.00 8.63  ? 322  TRP A CD2 1 
ATOM   2452 N  NE1 . TRP A 1 322  ? 25.656 47.990  22.452  1.00 10.86 ? 322  TRP A NE1 1 
ATOM   2453 C  CE2 . TRP A 1 322  ? 26.103 47.094  23.401  1.00 9.71  ? 322  TRP A CE2 1 
ATOM   2454 C  CE3 . TRP A 1 322  ? 25.656 44.821  24.108  1.00 9.67  ? 322  TRP A CE3 1 
ATOM   2455 C  CZ2 . TRP A 1 322  ? 27.084 47.269  24.416  1.00 10.62 ? 322  TRP A CZ2 1 
ATOM   2456 C  CZ3 . TRP A 1 322  ? 26.615 44.998  25.115  1.00 10.54 ? 322  TRP A CZ3 1 
ATOM   2457 C  CH2 . TRP A 1 322  ? 27.300 46.188  25.260  1.00 11.10 ? 322  TRP A CH2 1 
ATOM   2458 N  N   . LYS A 1 323  ? 20.943 43.674  20.514  1.00 9.26  ? 323  LYS A N   1 
ATOM   2459 C  CA  . LYS A 1 323  ? 20.339 42.473  19.906  1.00 9.45  ? 323  LYS A CA  1 
ATOM   2460 C  C   . LYS A 1 323  ? 19.481 42.847  18.712  1.00 9.77  ? 323  LYS A C   1 
ATOM   2461 O  O   . LYS A 1 323  ? 19.398 42.067  17.766  1.00 10.86 ? 323  LYS A O   1 
ATOM   2462 C  CB  . LYS A 1 323  ? 19.520 41.640  20.941  1.00 10.81 ? 323  LYS A CB  1 
ATOM   2463 C  CG  . LYS A 1 323  ? 20.521 40.981  21.947  1.00 13.00 ? 323  LYS A CG  1 
ATOM   2464 C  CD  . LYS A 1 323  ? 19.859 39.926  22.866  1.00 13.91 ? 323  LYS A CD  1 
ATOM   2465 C  CE  . LYS A 1 323  ? 20.920 39.171  23.637  1.00 14.22 ? 323  LYS A CE  1 
ATOM   2466 N  NZ  . LYS A 1 323  ? 20.207 38.127  24.413  1.00 18.48 ? 323  LYS A NZ  1 
ATOM   2467 N  N   . LYS A 1 324  ? 18.913 44.018  18.714  1.00 9.86  ? 324  LYS A N   1 
ATOM   2468 C  CA  . LYS A 1 324  ? 18.193 44.471  17.514  1.00 8.22  ? 324  LYS A CA  1 
ATOM   2469 C  C   . LYS A 1 324  ? 19.193 44.738  16.388  1.00 9.25  ? 324  LYS A C   1 
ATOM   2470 O  O   . LYS A 1 324  ? 18.969 44.308  15.254  1.00 10.14 ? 324  LYS A O   1 
ATOM   2471 C  CB  . LYS A 1 324  ? 17.392 45.738  17.828  1.00 9.55  ? 324  LYS A CB  1 
ATOM   2472 C  CG  . LYS A 1 324  ? 16.119 45.391  18.646  1.00 9.88  ? 324  LYS A CG  1 
ATOM   2473 C  CD  . LYS A 1 324  ? 15.516 46.654  19.250  1.00 11.40 ? 324  LYS A CD  1 
ATOM   2474 C  CE  . LYS A 1 324  ? 14.218 46.256  19.971  1.00 12.18 ? 324  LYS A CE  1 
ATOM   2475 N  NZ  . LYS A 1 324  ? 13.644 47.344  20.819  1.00 13.15 ? 324  LYS A NZ  1 
ATOM   2476 N  N   . LYS A 1 325  ? 20.267 45.464  16.679  1.00 9.26  ? 325  LYS A N   1 
ATOM   2477 C  CA  . LYS A 1 325  ? 21.293 45.701  15.632  1.00 8.42  ? 325  LYS A CA  1 
ATOM   2478 C  C   . LYS A 1 325  ? 21.793 44.354  15.096  1.00 8.03  ? 325  LYS A C   1 
ATOM   2479 O  O   . LYS A 1 325  ? 22.020 44.161  13.860  1.00 9.17  ? 325  LYS A O   1 
ATOM   2480 C  CB  . LYS A 1 325  ? 22.454 46.505  16.229  1.00 8.23  ? 325  LYS A CB  1 
ATOM   2481 C  CG  . LYS A 1 325  ? 23.382 47.097  15.061  1.00 8.18  ? 325  LYS A CG  1 
ATOM   2482 C  CD  . LYS A 1 325  ? 24.503 47.925  15.677  1.00 8.95  ? 325  LYS A CD  1 
ATOM   2483 C  CE  . LYS A 1 325  ? 25.281 48.622  14.512  1.00 9.97  ? 325  LYS A CE  1 
ATOM   2484 N  NZ  . LYS A 1 325  ? 26.483 49.285  15.128  1.00 11.02 ? 325  LYS A NZ  1 
ATOM   2485 N  N   . ALA A 1 326  ? 22.060 43.373  15.974  1.00 8.93  ? 326  ALA A N   1 
ATOM   2486 C  CA  . ALA A 1 326  ? 22.579 42.081  15.549  1.00 9.51  ? 326  ALA A CA  1 
ATOM   2487 C  C   . ALA A 1 326  ? 21.667 41.302  14.619  1.00 9.31  ? 326  ALA A C   1 
ATOM   2488 O  O   . ALA A 1 326  ? 22.125 40.456  13.851  1.00 10.79 ? 326  ALA A O   1 
ATOM   2489 C  CB  . ALA A 1 326  ? 22.894 41.223  16.808  1.00 11.69 ? 326  ALA A CB  1 
ATOM   2490 N  N   . GLU A 1 327  ? 20.375 41.600  14.691  1.00 10.91 ? 327  GLU A N   1 
ATOM   2491 C  CA  . GLU A 1 327  ? 19.430 40.932  13.782  1.00 11.97 ? 327  GLU A CA  1 
ATOM   2492 C  C   . GLU A 1 327  ? 19.673 41.263  12.324  1.00 11.87 ? 327  GLU A C   1 
ATOM   2493 O  O   . GLU A 1 327  ? 19.212 40.542  11.449  1.00 14.63 ? 327  GLU A O   1 
ATOM   2494 C  CB  . GLU A 1 327  ? 18.008 41.375  14.118  1.00 15.63 ? 327  GLU A CB  1 
ATOM   2495 C  CG  . GLU A 1 327  ? 17.295 40.557  15.127  1.00 22.50 ? 327  GLU A CG  1 
ATOM   2496 C  CD  . GLU A 1 327  ? 17.299 39.041  14.840  1.00 17.38 ? 327  GLU A CD  1 
ATOM   2497 O  OE1 . GLU A 1 327  ? 16.728 38.479  13.900  1.00 21.67 ? 327  GLU A OE1 1 
ATOM   2498 O  OE2 . GLU A 1 327  ? 17.948 38.396  15.601  1.00 18.98 ? 327  GLU A OE2 1 
ATOM   2499 N  N   . LEU A 1 328  ? 20.366 42.379  12.058  1.00 10.82 ? 328  LEU A N   1 
ATOM   2500 C  CA  . LEU A 1 328  ? 20.608 42.833  10.687  1.00 9.18  ? 328  LEU A CA  1 
ATOM   2501 C  C   . LEU A 1 328  ? 21.832 42.190  10.065  1.00 10.91 ? 328  LEU A C   1 
ATOM   2502 O  O   . LEU A 1 328  ? 22.097 42.453  8.878   1.00 11.76 ? 328  LEU A O   1 
ATOM   2503 C  CB  . LEU A 1 328  ? 20.787 44.363  10.697  1.00 10.53 ? 328  LEU A CB  1 
ATOM   2504 C  CG  . LEU A 1 328  ? 19.660 45.136  11.398  1.00 9.63  ? 328  LEU A CG  1 
ATOM   2505 C  CD1 . LEU A 1 328  ? 19.894 46.642  11.201  1.00 10.45 ? 328  LEU A CD1 1 
ATOM   2506 C  CD2 . LEU A 1 328  ? 18.269 44.800  10.881  1.00 11.57 ? 328  LEU A CD2 1 
ATOM   2507 N  N   . TYR A 1 329  ? 22.568 41.358  10.803  1.00 9.94  ? 329  TYR A N   1 
ATOM   2508 C  CA  . TYR A 1 329  ? 23.808 40.751  10.328  1.00 9.87  ? 329  TYR A CA  1 
ATOM   2509 C  C   . TYR A 1 329  ? 23.788 39.249  10.533  1.00 10.67 ? 329  TYR A C   1 
ATOM   2510 O  O   . TYR A 1 329  ? 22.931 38.745  11.295  1.00 11.93 ? 329  TYR A O   1 
ATOM   2511 C  CB  . TYR A 1 329  ? 25.025 41.365  11.058  1.00 9.74  ? 329  TYR A CB  1 
ATOM   2512 C  CG  . TYR A 1 329  ? 25.214 42.853  10.716  1.00 9.29  ? 329  TYR A CG  1 
ATOM   2513 C  CD1 . TYR A 1 329  ? 25.977 43.213  9.604   1.00 9.74  ? 329  TYR A CD1 1 
ATOM   2514 C  CD2 . TYR A 1 329  ? 24.632 43.862  11.471  1.00 10.54 ? 329  TYR A CD2 1 
ATOM   2515 C  CE1 . TYR A 1 329  ? 26.144 44.580  9.235   1.00 9.62  ? 329  TYR A CE1 1 
ATOM   2516 C  CE2 . TYR A 1 329  ? 24.809 45.233  11.128  1.00 11.09 ? 329  TYR A CE2 1 
ATOM   2517 C  CZ  . TYR A 1 329  ? 25.541 45.553  10.022  1.00 9.84  ? 329  TYR A CZ  1 
ATOM   2518 O  OH  . TYR A 1 329  ? 25.608 46.890  9.683   1.00 10.97 ? 329  TYR A OH  1 
ATOM   2519 N  N   . ARG A 1 330  ? 24.695 38.545  9.883   1.00 10.07 ? 330  ARG A N   1 
ATOM   2520 C  CA  . ARG A 1 330  ? 24.676 37.096  9.883   1.00 10.04 ? 330  ARG A CA  1 
ATOM   2521 C  C   . ARG A 1 330  ? 25.501 36.351  10.915  1.00 12.05 ? 330  ARG A C   1 
ATOM   2522 O  O   . ARG A 1 330  ? 25.294 35.122  11.026  1.00 13.58 ? 330  ARG A O   1 
ATOM   2523 C  CB  . ARG A 1 330  ? 25.077 36.622  8.460   1.00 11.08 ? 330  ARG A CB  1 
ATOM   2524 C  CG  . ARG A 1 330  ? 24.110 37.070  7.354   1.00 10.02 ? 330  ARG A CG  1 
ATOM   2525 C  CD  . ARG A 1 330  ? 24.505 36.534  6.004   1.00 11.43 ? 330  ARG A CD  1 
ATOM   2526 N  NE  . ARG A 1 330  ? 23.540 37.079  5.042   1.00 13.14 ? 330  ARG A NE  1 
ATOM   2527 C  CZ  . ARG A 1 330  ? 23.230 36.547  3.857   1.00 14.65 ? 330  ARG A CZ  1 
ATOM   2528 N  NH1 . ARG A 1 330  ? 23.811 35.437  3.440   1.00 14.76 ? 330  ARG A NH1 1 
ATOM   2529 N  NH2 . ARG A 1 330  ? 22.343 37.173  3.082   1.00 15.00 ? 330  ARG A NH2 1 
ATOM   2530 N  N   . THR A 1 331  ? 26.443 36.993  11.608  1.00 11.39 ? 331  THR A N   1 
ATOM   2531 C  CA  . THR A 1 331  ? 27.230 36.232  12.593  1.00 10.57 ? 331  THR A CA  1 
ATOM   2532 C  C   . THR A 1 331  ? 26.805 36.626  14.001  1.00 10.60 ? 331  THR A C   1 
ATOM   2533 O  O   . THR A 1 331  ? 25.950 37.493  14.198  1.00 13.73 ? 331  THR A O   1 
ATOM   2534 C  CB  . THR A 1 331  ? 28.776 36.472  12.442  1.00 10.42 ? 331  THR A CB  1 
ATOM   2535 O  OG1 . THR A 1 331  ? 29.109 37.773  12.941  1.00 10.70 ? 331  THR A OG1 1 
ATOM   2536 C  CG2 . THR A 1 331  ? 29.213 36.322  10.912  1.00 11.73 ? 331  THR A CG2 1 
ATOM   2537 N  N   . ASN A 1 332  ? 27.434 35.973  14.975  1.00 10.90 ? 332  ASN A N   1 
ATOM   2538 C  CA  . ASN A 1 332  ? 27.197 36.306  16.381  1.00 10.14 ? 332  ASN A CA  1 
ATOM   2539 C  C   . ASN A 1 332  ? 28.287 37.264  16.887  1.00 11.40 ? 332  ASN A C   1 
ATOM   2540 O  O   . ASN A 1 332  ? 28.599 37.280  18.103  1.00 11.69 ? 332  ASN A O   1 
ATOM   2541 C  CB  . ASN A 1 332  ? 27.185 35.026  17.271  1.00 12.22 ? 332  ASN A CB  1 
ATOM   2542 C  CG  . ASN A 1 332  ? 28.556 34.350  17.349  1.00 14.80 ? 332  ASN A CG  1 
ATOM   2543 O  OD1 . ASN A 1 332  ? 29.347 34.378  16.425  1.00 16.38 ? 332  ASN A OD1 1 
ATOM   2544 N  ND2 . ASN A 1 332  ? 28.844 33.663  18.490  1.00 18.96 ? 332  ASN A ND2 1 
ATOM   2545 N  N   . VAL A 1 333  ? 28.910 38.046  15.981  1.00 9.37  ? 333  VAL A N   1 
ATOM   2546 C  CA  . VAL A 1 333  ? 29.945 39.042  16.359  1.00 10.24 ? 333  VAL A CA  1 
ATOM   2547 C  C   . VAL A 1 333  ? 29.394 40.413  15.949  1.00 9.22  ? 333  VAL A C   1 
ATOM   2548 O  O   . VAL A 1 333  ? 29.072 40.585  14.753  1.00 10.27 ? 333  VAL A O   1 
ATOM   2549 C  CB  . VAL A 1 333  ? 31.215 38.776  15.616  1.00 10.33 ? 333  VAL A CB  1 
ATOM   2550 C  CG1 . VAL A 1 333  ? 32.248 39.808  16.058  1.00 11.48 ? 333  VAL A CG1 1 
ATOM   2551 C  CG2 . VAL A 1 333  ? 31.675 37.322  15.863  1.00 11.89 ? 333  VAL A CG2 1 
ATOM   2552 N  N   . LEU A 1 334  ? 29.241 41.364  16.876  1.00 7.99  ? 334  LEU A N   1 
ATOM   2553 C  CA  . LEU A 1 334  ? 28.621 42.650  16.616  1.00 8.10  ? 334  LEU A CA  1 
ATOM   2554 C  C   . LEU A 1 334  ? 29.600 43.809  16.803  1.00 7.88  ? 334  LEU A C   1 
ATOM   2555 O  O   . LEU A 1 334  ? 30.341 43.897  17.784  1.00 8.69  ? 334  LEU A O   1 
ATOM   2556 C  CB  . LEU A 1 334  ? 27.465 42.837  17.619  1.00 8.46  ? 334  LEU A CB  1 
ATOM   2557 C  CG  . LEU A 1 334  ? 26.655 44.128  17.430  1.00 8.74  ? 334  LEU A CG  1 
ATOM   2558 C  CD1 . LEU A 1 334  ? 25.838 44.040  16.104  1.00 10.11 ? 334  LEU A CD1 1 
ATOM   2559 C  CD2 . LEU A 1 334  ? 25.671 44.289  18.628  1.00 9.29  ? 334  LEU A CD2 1 
ATOM   2560 N  N   . LEU A 1 335  ? 29.626 44.709  15.822  1.00 8.08  ? 335  LEU A N   1 
ATOM   2561 C  CA  . LEU A 1 335  ? 30.462 45.909  15.845  1.00 7.82  ? 335  LEU A CA  1 
ATOM   2562 C  C   . LEU A 1 335  ? 29.662 47.077  16.399  1.00 7.14  ? 335  LEU A C   1 
ATOM   2563 O  O   . LEU A 1 335  ? 28.615 47.422  15.840  1.00 9.02  ? 335  LEU A O   1 
ATOM   2564 C  CB  . LEU A 1 335  ? 30.904 46.251  14.399  1.00 8.00  ? 335  LEU A CB  1 
ATOM   2565 C  CG  . LEU A 1 335  ? 31.788 47.512  14.324  1.00 7.35  ? 335  LEU A CG  1 
ATOM   2566 C  CD1 . LEU A 1 335  ? 33.083 47.339  15.022  1.00 10.02 ? 335  LEU A CD1 1 
ATOM   2567 C  CD2 . LEU A 1 335  ? 31.997 47.829  12.862  1.00 9.85  ? 335  LEU A CD2 1 
ATOM   2568 N  N   . ILE A 1 336  ? 30.162 47.715  17.456  1.00 7.11  ? 336  ILE A N   1 
ATOM   2569 C  CA  . ILE A 1 336  ? 29.559 48.889  18.047  1.00 7.18  ? 336  ILE A CA  1 
ATOM   2570 C  C   . ILE A 1 336  ? 30.592 50.039  18.089  1.00 7.06  ? 336  ILE A C   1 
ATOM   2571 O  O   . ILE A 1 336  ? 31.383 50.154  19.019  1.00 7.67  ? 336  ILE A O   1 
ATOM   2572 C  CB  . ILE A 1 336  ? 29.033 48.616  19.498  1.00 8.39  ? 336  ILE A CB  1 
ATOM   2573 C  CG1 . ILE A 1 336  ? 27.991 47.493  19.496  1.00 7.61  ? 336  ILE A CG1 1 
ATOM   2574 C  CG2 . ILE A 1 336  ? 28.489 49.939  20.069  1.00 9.47  ? 336  ILE A CG2 1 
ATOM   2575 C  CD1 . ILE A 1 336  ? 26.706 47.813  18.724  1.00 9.18  ? 336  ILE A CD1 1 
ATOM   2576 N  N   . PRO A 1 337  ? 30.624 50.887  17.052  1.00 7.56  ? 337  PRO A N   1 
ATOM   2577 C  CA  . PRO A 1 337  ? 31.552 52.038  17.101  1.00 7.28  ? 337  PRO A CA  1 
ATOM   2578 C  C   . PRO A 1 337  ? 31.136 52.955  18.283  1.00 7.60  ? 337  PRO A C   1 
ATOM   2579 O  O   . PRO A 1 337  ? 29.946 53.090  18.580  1.00 9.08  ? 337  PRO A O   1 
ATOM   2580 C  CB  . PRO A 1 337  ? 31.265 52.760  15.771  1.00 8.14  ? 337  PRO A CB  1 
ATOM   2581 C  CG  . PRO A 1 337  ? 30.832 51.634  14.836  1.00 8.40  ? 337  PRO A CG  1 
ATOM   2582 C  CD  . PRO A 1 337  ? 29.884 50.822  15.777  1.00 8.16  ? 337  PRO A CD  1 
ATOM   2583 N  N   . LEU A 1 338  ? 32.121 53.588  18.926  1.00 6.96  ? 338  LEU A N   1 
ATOM   2584 C  CA  . LEU A 1 338  ? 31.886 54.520  20.022  1.00 7.70  ? 338  LEU A CA  1 
ATOM   2585 C  C   . LEU A 1 338  ? 32.694 55.804  19.792  1.00 7.54  ? 338  LEU A C   1 
ATOM   2586 O  O   . LEU A 1 338  ? 33.850 55.895  20.211  1.00 7.19  ? 338  LEU A O   1 
ATOM   2587 C  CB  . LEU A 1 338  ? 32.231 53.854  21.356  1.00 8.93  ? 338  LEU A CB  1 
ATOM   2588 C  CG  . LEU A 1 338  ? 31.862 54.754  22.529  1.00 8.50  ? 338  LEU A CG  1 
ATOM   2589 C  CD1 . LEU A 1 338  ? 30.351 54.668  22.832  1.00 11.67 ? 338  LEU A CD1 1 
ATOM   2590 C  CD2 . LEU A 1 338  ? 32.650 54.272  23.798  1.00 11.71 ? 338  LEU A CD2 1 
ATOM   2591 N  N   . GLY A 1 339  ? 32.093 56.784  19.111  1.00 6.83  ? 339  GLY A N   1 
ATOM   2592 C  CA  . GLY A 1 339  ? 32.869 57.986  18.818  1.00 7.30  ? 339  GLY A CA  1 
ATOM   2593 C  C   . GLY A 1 339  ? 32.064 58.983  18.020  1.00 7.79  ? 339  GLY A C   1 
ATOM   2594 O  O   . GLY A 1 339  ? 30.888 58.769  17.729  1.00 9.16  ? 339  GLY A O   1 
ATOM   2595 N  N   . ASP A 1 340  ? 32.722 60.107  17.674  1.00 7.75  ? 340  ASP A N   1 
ATOM   2596 C  CA  . ASP A 1 340  ? 32.088 61.201  16.927  1.00 7.04  ? 340  ASP A CA  1 
ATOM   2597 C  C   . ASP A 1 340  ? 33.261 62.127  16.552  1.00 6.50  ? 340  ASP A C   1 
ATOM   2598 O  O   . ASP A 1 340  ? 34.428 61.826  16.759  1.00 7.36  ? 340  ASP A O   1 
ATOM   2599 C  CB  . ASP A 1 340  ? 31.025 61.869  17.854  1.00 8.20  ? 340  ASP A CB  1 
ATOM   2600 C  CG  . ASP A 1 340  ? 29.939 62.631  17.135  1.00 9.31  ? 340  ASP A CG  1 
ATOM   2601 O  OD1 . ASP A 1 340  ? 30.096 62.954  15.911  1.00 9.89  ? 340  ASP A OD1 1 
ATOM   2602 O  OD2 . ASP A 1 340  ? 28.917 62.918  17.820  1.00 9.90  ? 340  ASP A OD2 1 
ATOM   2603 N  N   . ASP A 1 341  ? 32.889 63.297  16.055  1.00 7.36  ? 341  ASP A N   1 
ATOM   2604 C  CA  . ASP A 1 341  ? 33.893 64.267  15.522  1.00 7.37  ? 341  ASP A CA  1 
ATOM   2605 C  C   . ASP A 1 341  ? 34.759 64.814  16.625  1.00 7.09  ? 341  ASP A C   1 
ATOM   2606 O  O   . ASP A 1 341  ? 34.228 65.292  17.659  1.00 8.93  ? 341  ASP A O   1 
ATOM   2607 C  CB  . ASP A 1 341  ? 33.187 65.460  14.831  1.00 8.54  ? 341  ASP A CB  1 
ATOM   2608 C  CG  . ASP A 1 341  ? 32.464 65.067  13.562  1.00 8.77  ? 341  ASP A CG  1 
ATOM   2609 O  OD1 . ASP A 1 341  ? 32.434 63.858  13.223  1.00 11.02 ? 341  ASP A OD1 1 
ATOM   2610 O  OD2 . ASP A 1 341  ? 31.993 66.028  12.876  1.00 11.97 ? 341  ASP A OD2 1 
ATOM   2611 N  N   . PHE A 1 342  ? 36.070 64.712  16.427  1.00 7.23  ? 342  PHE A N   1 
ATOM   2612 C  CA  . PHE A 1 342  ? 37.039 65.248  17.374  1.00 7.34  ? 342  PHE A CA  1 
ATOM   2613 C  C   . PHE A 1 342  ? 36.742 64.862  18.840  1.00 7.89  ? 342  PHE A C   1 
ATOM   2614 O  O   . PHE A 1 342  ? 36.978 65.672  19.776  1.00 10.33 ? 342  PHE A O   1 
ATOM   2615 C  CB  . PHE A 1 342  ? 37.158 66.781  17.173  1.00 7.65  ? 342  PHE A CB  1 
ATOM   2616 C  CG  . PHE A 1 342  ? 37.745 67.181  15.819  1.00 7.96  ? 342  PHE A CG  1 
ATOM   2617 C  CD1 . PHE A 1 342  ? 39.115 67.160  15.603  1.00 7.44  ? 342  PHE A CD1 1 
ATOM   2618 C  CD2 . PHE A 1 342  ? 36.900 67.594  14.762  1.00 7.95  ? 342  PHE A CD2 1 
ATOM   2619 C  CE1 . PHE A 1 342  ? 39.656 67.546  14.353  1.00 8.30  ? 342  PHE A CE1 1 
ATOM   2620 C  CE2 . PHE A 1 342  ? 37.437 67.986  13.486  1.00 8.60  ? 342  PHE A CE2 1 
ATOM   2621 C  CZ  . PHE A 1 342  ? 38.797 67.959  13.308  1.00 8.46  ? 342  PHE A CZ  1 
ATOM   2622 N  N   . ARG A 1 343  ? 36.309 63.606  19.011  1.00 7.64  ? 343  ARG A N   1 
ATOM   2623 C  CA  . ARG A 1 343  ? 36.087 63.109  20.375  1.00 8.18  ? 343  ARG A CA  1 
ATOM   2624 C  C   . ARG A 1 343  ? 37.405 62.678  21.025  1.00 10.03 ? 343  ARG A C   1 
ATOM   2625 O  O   . ARG A 1 343  ? 38.497 62.585  20.414  1.00 8.61  ? 343  ARG A O   1 
ATOM   2626 C  CB  . ARG A 1 343  ? 35.107 61.932  20.352  1.00 8.29  ? 343  ARG A CB  1 
ATOM   2627 C  CG  . ARG A 1 343  ? 33.685 62.354  20.120  1.00 8.60  ? 343  ARG A CG  1 
ATOM   2628 C  CD  . ARG A 1 343  ? 33.186 63.315  21.228  1.00 8.33  ? 343  ARG A CD  1 
ATOM   2629 N  NE  . ARG A 1 343  ? 31.742 63.575  21.120  1.00 8.46  ? 343  ARG A NE  1 
ATOM   2630 C  CZ  . ARG A 1 343  ? 30.801 62.867  21.751  1.00 8.38  ? 343  ARG A CZ  1 
ATOM   2631 N  NH1 . ARG A 1 343  ? 31.133 61.802  22.523  1.00 8.14  ? 343  ARG A NH1 1 
ATOM   2632 N  NH2 . ARG A 1 343  ? 29.532 63.266  21.682  1.00 8.13  ? 343  ARG A NH2 1 
ATOM   2633 N  N   . PHE A 1 344  ? 37.267 62.361  22.311  1.00 10.78 ? 344  PHE A N   1 
ATOM   2634 C  CA  . PHE A 1 344  ? 38.388 61.909  23.186  1.00 9.80  ? 344  PHE A CA  1 
ATOM   2635 C  C   . PHE A 1 344  ? 39.483 62.940  23.313  1.00 11.27 ? 344  PHE A C   1 
ATOM   2636 O  O   . PHE A 1 344  ? 40.684 62.642  23.324  1.00 12.86 ? 344  PHE A O   1 
ATOM   2637 C  CB  . PHE A 1 344  ? 38.835 60.532  22.707  1.00 11.56 ? 344  PHE A CB  1 
ATOM   2638 C  CG  . PHE A 1 344  ? 37.796 59.475  22.894  1.00 10.30 ? 344  PHE A CG  1 
ATOM   2639 C  CD1 . PHE A 1 344  ? 37.548 58.933  24.190  1.00 12.04 ? 344  PHE A CD1 1 
ATOM   2640 C  CD2 . PHE A 1 344  ? 37.013 59.023  21.857  1.00 10.05 ? 344  PHE A CD2 1 
ATOM   2641 C  CE1 . PHE A 1 344  ? 36.549 57.987  24.360  1.00 12.71 ? 344  PHE A CE1 1 
ATOM   2642 C  CE2 . PHE A 1 344  ? 36.023 58.092  22.026  1.00 11.34 ? 344  PHE A CE2 1 
ATOM   2643 C  CZ  . PHE A 1 344  ? 35.786 57.567  23.306  1.00 10.89 ? 344  PHE A CZ  1 
ATOM   2644 N  N   . LYS A 1 345  ? 39.081 64.176  23.487  1.00 11.41 ? 345  LYS A N   1 
ATOM   2645 C  CA  . LYS A 1 345  ? 39.973 65.287  23.615  1.00 12.29 ? 345  LYS A CA  1 
ATOM   2646 C  C   . LYS A 1 345  ? 40.481 65.581  25.033  1.00 14.24 ? 345  LYS A C   1 
ATOM   2647 O  O   . LYS A 1 345  ? 41.659 65.960  25.178  1.00 18.10 ? 345  LYS A O   1 
ATOM   2648 C  CB  . LYS A 1 345  ? 39.269 66.536  23.086  1.00 16.07 ? 345  LYS A CB  1 
ATOM   2649 C  CG  . LYS A 1 345  ? 40.076 67.730  23.210  1.00 15.95 ? 345  LYS A CG  1 
ATOM   2650 C  CD  . LYS A 1 345  ? 39.293 68.878  22.618  1.00 21.80 ? 345  LYS A CD  1 
ATOM   2651 C  CE  . LYS A 1 345  ? 40.021 70.155  22.774  1.00 22.07 ? 345  LYS A CE  1 
ATOM   2652 N  NZ  . LYS A 1 345  ? 39.184 71.287  22.200  1.00 22.71 ? 345  LYS A NZ  1 
ATOM   2653 N  N   . GLN A 1 346  ? 39.572 65.492  25.994  1.00 14.74 ? 346  GLN A N   1 
ATOM   2654 C  CA  . GLN A 1 346  ? 39.903 65.736  27.400  1.00 15.98 ? 346  GLN A CA  1 
ATOM   2655 C  C   . GLN A 1 346  ? 40.047 64.455  28.185  1.00 15.39 ? 346  GLN A C   1 
ATOM   2656 O  O   . GLN A 1 346  ? 39.326 63.486  27.949  1.00 11.98 ? 346  GLN A O   1 
ATOM   2657 C  CB  . GLN A 1 346  ? 38.786 66.542  28.040  1.00 17.41 ? 346  GLN A CB  1 
ATOM   2658 C  CG  . GLN A 1 346  ? 38.643 67.965  27.467  1.00 28.01 ? 346  GLN A CG  1 
ATOM   2659 C  CD  . GLN A 1 346  ? 37.268 68.562  27.772  1.00 28.64 ? 346  GLN A CD  1 
ATOM   2660 O  OE1 . GLN A 1 346  ? 36.946 68.839  28.931  1.00 43.57 ? 346  GLN A OE1 1 
ATOM   2661 N  NE2 . GLN A 1 346  ? 36.434 68.734  26.736  1.00 35.94 ? 346  GLN A NE2 1 
ATOM   2662 N  N   . ASN A 1 347  ? 40.941 64.464  29.161  1.00 15.60 ? 347  ASN A N   1 
ATOM   2663 C  CA  . ASN A 1 347  ? 41.099 63.376  30.104  1.00 15.16 ? 347  ASN A CA  1 
ATOM   2664 C  C   . ASN A 1 347  ? 39.795 62.937  30.740  1.00 13.33 ? 347  ASN A C   1 
ATOM   2665 O  O   . ASN A 1 347  ? 39.527 61.759  30.864  1.00 13.15 ? 347  ASN A O   1 
ATOM   2666 C  CB  . ASN A 1 347  ? 42.029 63.845  31.216  1.00 20.11 ? 347  ASN A CB  1 
ATOM   2667 C  CG  . ASN A 1 347  ? 43.375 64.115  30.709  1.00 28.01 ? 347  ASN A CG  1 
ATOM   2668 O  OD1 . ASN A 1 347  ? 43.969 65.166  30.953  1.00 31.11 ? 347  ASN A OD1 1 
ATOM   2669 N  ND2 . ASN A 1 347  ? 43.887 63.163  29.969  1.00 34.32 ? 347  ASN A ND2 1 
ATOM   2670 N  N   . THR A 1 348  ? 39.006 63.926  31.128  1.00 10.98 ? 348  THR A N   1 
ATOM   2671 C  CA  . THR A 1 348  ? 37.743 63.673  31.789  1.00 12.29 ? 348  THR A CA  1 
ATOM   2672 C  C   . THR A 1 348  ? 36.765 62.926  30.865  1.00 12.57 ? 348  THR A C   1 
ATOM   2673 O  O   . THR A 1 348  ? 35.888 62.174  31.316  1.00 12.22 ? 348  THR A O   1 
ATOM   2674 C  CB  . THR A 1 348  ? 37.077 64.949  32.257  1.00 15.96 ? 348  THR A CB  1 
ATOM   2675 O  OG1 . THR A 1 348  ? 37.080 65.892  31.181  1.00 18.30 ? 348  THR A OG1 1 
ATOM   2676 C  CG2 . THR A 1 348  ? 37.843 65.543  33.463  1.00 16.05 ? 348  THR A CG2 1 
ATOM   2677 N  N   . GLU A 1 349  ? 36.870 63.145  29.558  1.00 10.21 ? 349  GLU A N   1 
ATOM   2678 C  CA  . GLU A 1 349  ? 36.018 62.435  28.600  1.00 10.50 ? 349  GLU A CA  1 
ATOM   2679 C  C   . GLU A 1 349  ? 36.428 60.979  28.458  1.00 8.42  ? 349  GLU A C   1 
ATOM   2680 O  O   . GLU A 1 349  ? 35.594 60.108  28.427  1.00 9.16  ? 349  GLU A O   1 
ATOM   2681 C  CB  . GLU A 1 349  ? 36.068 63.139  27.240  1.00 9.59  ? 349  GLU A CB  1 
ATOM   2682 C  CG  . GLU A 1 349  ? 35.272 62.418  26.170  1.00 11.26 ? 349  GLU A CG  1 
ATOM   2683 C  CD  . GLU A 1 349  ? 35.491 63.046  24.776  1.00 10.06 ? 349  GLU A CD  1 
ATOM   2684 O  OE1 . GLU A 1 349  ? 36.148 64.074  24.634  1.00 13.05 ? 349  GLU A OE1 1 
ATOM   2685 O  OE2 . GLU A 1 349  ? 34.977 62.422  23.860  1.00 13.03 ? 349  GLU A OE2 1 
ATOM   2686 N  N   . TRP A 1 350  ? 37.739 60.753  28.372  1.00 8.66  ? 350  TRP A N   1 
ATOM   2687 C  CA  . TRP A 1 350  ? 38.225 59.379  28.344  1.00 8.19  ? 350  TRP A CA  1 
ATOM   2688 C  C   . TRP A 1 350  ? 37.688 58.635  29.581  1.00 9.15  ? 350  TRP A C   1 
ATOM   2689 O  O   . TRP A 1 350  ? 37.172 57.528  29.495  1.00 9.77  ? 350  TRP A O   1 
ATOM   2690 C  CB  . TRP A 1 350  ? 39.755 59.325  28.410  1.00 8.09  ? 350  TRP A CB  1 
ATOM   2691 C  CG  . TRP A 1 350  ? 40.390 59.576  27.085  1.00 8.73  ? 350  TRP A CG  1 
ATOM   2692 C  CD1 . TRP A 1 350  ? 40.733 60.782  26.585  1.00 9.52  ? 350  TRP A CD1 1 
ATOM   2693 C  CD2 . TRP A 1 350  ? 40.692 58.587  26.094  1.00 9.54  ? 350  TRP A CD2 1 
ATOM   2694 N  NE1 . TRP A 1 350  ? 41.262 60.617  25.301  1.00 8.81  ? 350  TRP A NE1 1 
ATOM   2695 C  CE2 . TRP A 1 350  ? 41.211 59.286  24.981  1.00 8.79  ? 350  TRP A CE2 1 
ATOM   2696 C  CE3 . TRP A 1 350  ? 40.560 57.188  26.021  1.00 11.70 ? 350  TRP A CE3 1 
ATOM   2697 C  CZ2 . TRP A 1 350  ? 41.579 58.630  23.795  1.00 11.67 ? 350  TRP A CZ2 1 
ATOM   2698 C  CZ3 . TRP A 1 350  ? 40.941 56.553  24.815  1.00 12.73 ? 350  TRP A CZ3 1 
ATOM   2699 C  CH2 . TRP A 1 350  ? 41.425 57.289  23.736  1.00 12.07 ? 350  TRP A CH2 1 
ATOM   2700 N  N   . ASP A 1 351  ? 37.765 59.273  30.762  1.00 9.98  ? 351  ASP A N   1 
ATOM   2701 C  CA  . ASP A 1 351  ? 37.291 58.598  31.993  1.00 11.12 ? 351  ASP A CA  1 
ATOM   2702 C  C   . ASP A 1 351  ? 35.800 58.376  31.983  1.00 9.35  ? 351  ASP A C   1 
ATOM   2703 O  O   . ASP A 1 351  ? 35.349 57.265  32.351  1.00 11.04 ? 351  ASP A O   1 
ATOM   2704 C  CB  . ASP A 1 351  ? 37.639 59.431  33.229  1.00 14.36 ? 351  ASP A CB  1 
ATOM   2705 C  CG  . ASP A 1 351  ? 39.104 59.388  33.575  1.00 20.18 ? 351  ASP A CG  1 
ATOM   2706 O  OD1 . ASP A 1 351  ? 39.769 58.357  33.303  1.00 23.17 ? 351  ASP A OD1 1 
ATOM   2707 O  OD2 . ASP A 1 351  ? 39.558 60.374  34.193  1.00 29.32 ? 351  ASP A OD2 1 
ATOM   2708 N  N   . VAL A 1 352  ? 35.013 59.356  31.587  1.00 9.44  ? 352  VAL A N   1 
ATOM   2709 C  CA  . VAL A 1 352  ? 33.579 59.173  31.653  1.00 9.98  ? 352  VAL A CA  1 
ATOM   2710 C  C   . VAL A 1 352  ? 33.084 58.081  30.704  1.00 10.46 ? 352  VAL A C   1 
ATOM   2711 O  O   . VAL A 1 352  ? 32.205 57.290  31.055  1.00 12.24 ? 352  VAL A O   1 
ATOM   2712 C  CB  . VAL A 1 352  ? 32.863 60.579  31.501  1.00 13.16 ? 352  VAL A CB  1 
ATOM   2713 C  CG1 . VAL A 1 352  ? 32.659 60.977  30.079  1.00 12.18 ? 352  VAL A CG1 1 
ATOM   2714 C  CG2 . VAL A 1 352  ? 31.575 60.587  32.319  1.00 16.15 ? 352  VAL A CG2 1 
ATOM   2715 N  N   . GLN A 1 353  ? 33.683 57.971  29.506  1.00 8.67  ? 353  GLN A N   1 
ATOM   2716 C  CA  . GLN A 1 353  ? 33.269 56.900  28.613  1.00 7.73  ? 353  GLN A CA  1 
ATOM   2717 C  C   . GLN A 1 353  ? 33.800 55.551  29.098  1.00 8.86  ? 353  GLN A C   1 
ATOM   2718 O  O   . GLN A 1 353  ? 33.018 54.589  29.210  1.00 9.78  ? 353  GLN A O   1 
ATOM   2719 C  CB  . GLN A 1 353  ? 33.773 57.170  27.177  1.00 8.26  ? 353  GLN A CB  1 
ATOM   2720 C  CG  . GLN A 1 353  ? 33.240 58.493  26.534  1.00 9.02  ? 353  GLN A CG  1 
ATOM   2721 C  CD  . GLN A 1 353  ? 31.789 58.418  26.070  1.00 9.15  ? 353  GLN A CD  1 
ATOM   2722 O  OE1 . GLN A 1 353  ? 30.932 57.742  26.655  1.00 9.62  ? 353  GLN A OE1 1 
ATOM   2723 N  NE2 . GLN A 1 353  ? 31.456 59.195  25.035  1.00 9.68  ? 353  GLN A NE2 1 
ATOM   2724 N  N   . ARG A 1 354  ? 35.080 55.475  29.420  1.00 7.83  ? 354  ARG A N   1 
ATOM   2725 C  CA  . ARG A 1 354  ? 35.624 54.197  29.818  1.00 8.74  ? 354  ARG A CA  1 
ATOM   2726 C  C   . ARG A 1 354  ? 34.997 53.627  31.083  1.00 10.30 ? 354  ARG A C   1 
ATOM   2727 O  O   . ARG A 1 354  ? 34.630 52.444  31.096  1.00 9.71  ? 354  ARG A O   1 
ATOM   2728 C  CB  . ARG A 1 354  ? 37.122 54.309  30.044  1.00 9.77  ? 354  ARG A CB  1 
ATOM   2729 C  CG  . ARG A 1 354  ? 37.765 52.966  30.503  1.00 9.42  ? 354  ARG A CG  1 
ATOM   2730 C  CD  . ARG A 1 354  ? 39.302 53.141  30.696  1.00 11.81 ? 354  ARG A CD  1 
ATOM   2731 N  NE  . ARG A 1 354  ? 39.600 54.168  31.712  1.00 12.03 ? 354  ARG A NE  1 
ATOM   2732 C  CZ  . ARG A 1 354  ? 39.487 54.006  33.034  1.00 14.47 ? 354  ARG A CZ  1 
ATOM   2733 N  NH1 . ARG A 1 354  ? 39.081 52.847  33.547  1.00 15.80 ? 354  ARG A NH1 1 
ATOM   2734 N  NH2 . ARG A 1 354  ? 39.825 54.996  33.823  1.00 15.19 ? 354  ARG A NH2 1 
ATOM   2735 N  N   . VAL A 1 355  ? 34.873 54.434  32.132  1.00 9.49  ? 355  VAL A N   1 
ATOM   2736 C  CA  . VAL A 1 355  ? 34.399 53.873  33.423  1.00 10.67 ? 355  VAL A CA  1 
ATOM   2737 C  C   . VAL A 1 355  ? 32.943 53.435  33.315  1.00 10.79 ? 355  VAL A C   1 
ATOM   2738 O  O   . VAL A 1 355  ? 32.588 52.338  33.813  1.00 11.11 ? 355  VAL A O   1 
ATOM   2739 C  CB  . VAL A 1 355  ? 34.621 54.883  34.538  1.00 11.56 ? 355  VAL A CB  1 
ATOM   2740 C  CG1 . VAL A 1 355  ? 33.904 54.454  35.853  1.00 17.04 ? 355  VAL A CG1 1 
ATOM   2741 C  CG2 . VAL A 1 355  ? 36.154 55.075  34.815  1.00 14.38 ? 355  VAL A CG2 1 
ATOM   2742 N  N   . ASN A 1 356  ? 32.076 54.251  32.701  1.00 9.23  ? 356  ASN A N   1 
ATOM   2743 C  CA  . ASN A 1 356  ? 30.695 53.856  32.556  1.00 8.49  ? 356  ASN A CA  1 
ATOM   2744 C  C   . ASN A 1 356  ? 30.537 52.588  31.695  1.00 9.44  ? 356  ASN A C   1 
ATOM   2745 O  O   . ASN A 1 356  ? 29.783 51.651  32.072  1.00 9.37  ? 356  ASN A O   1 
ATOM   2746 C  CB  . ASN A 1 356  ? 29.887 55.040  32.068  1.00 9.92  ? 356  ASN A CB  1 
ATOM   2747 C  CG  . ASN A 1 356  ? 29.646 56.042  33.153  1.00 10.61 ? 356  ASN A CG  1 
ATOM   2748 O  OD1 . ASN A 1 356  ? 28.938 55.704  34.147  1.00 11.55 ? 356  ASN A OD1 1 
ATOM   2749 N  ND2 . ASN A 1 356  ? 30.273 57.237  33.083  1.00 11.45 ? 356  ASN A ND2 1 
ATOM   2750 N  N   . TYR A 1 357  ? 31.260 52.473  30.575  1.00 8.54  ? 357  TYR A N   1 
ATOM   2751 C  CA  . TYR A 1 357  ? 31.167 51.259  29.777  1.00 10.05 ? 357  TYR A CA  1 
ATOM   2752 C  C   . TYR A 1 357  ? 31.736 50.094  30.542  1.00 8.88  ? 357  TYR A C   1 
ATOM   2753 O  O   . TYR A 1 357  ? 31.160 48.987  30.439  1.00 9.71  ? 357  TYR A O   1 
ATOM   2754 C  CB  . TYR A 1 357  ? 31.837 51.444  28.379  1.00 8.69  ? 357  TYR A CB  1 
ATOM   2755 C  CG  . TYR A 1 357  ? 30.850 51.981  27.382  1.00 7.67  ? 357  TYR A CG  1 
ATOM   2756 C  CD1 . TYR A 1 357  ? 30.038 51.094  26.660  1.00 8.42  ? 357  TYR A CD1 1 
ATOM   2757 C  CD2 . TYR A 1 357  ? 30.692 53.359  27.207  1.00 8.07  ? 357  TYR A CD2 1 
ATOM   2758 C  CE1 . TYR A 1 357  ? 29.056 51.566  25.778  1.00 8.35  ? 357  TYR A CE1 1 
ATOM   2759 C  CE2 . TYR A 1 357  ? 29.716 53.866  26.321  1.00 8.81  ? 357  TYR A CE2 1 
ATOM   2760 C  CZ  . TYR A 1 357  ? 28.906 52.956  25.624  1.00 8.11  ? 357  TYR A CZ  1 
ATOM   2761 O  OH  . TYR A 1 357  ? 27.931 53.378  24.786  1.00 10.02 ? 357  TYR A OH  1 
ATOM   2762 N  N   . GLU A 1 358  ? 32.808 50.269  31.322  1.00 9.17  ? 358  GLU A N   1 
ATOM   2763 C  CA  . GLU A 1 358  ? 33.305 49.101  32.083  1.00 9.39  ? 358  GLU A CA  1 
ATOM   2764 C  C   . GLU A 1 358  ? 32.303 48.616  33.141  1.00 9.96  ? 358  GLU A C   1 
ATOM   2765 O  O   . GLU A 1 358  ? 32.205 47.402  33.332  1.00 10.02 ? 358  GLU A O   1 
ATOM   2766 C  CB  . GLU A 1 358  ? 34.652 49.404  32.715  1.00 10.37 ? 358  GLU A CB  1 
ATOM   2767 C  CG  . GLU A 1 358  ? 35.635 49.416  31.540  1.00 14.07 ? 358  GLU A CG  1 
ATOM   2768 C  CD  . GLU A 1 358  ? 37.051 49.704  31.861  1.00 19.60 ? 358  GLU A CD  1 
ATOM   2769 O  OE1 . GLU A 1 358  ? 37.385 50.220  32.925  1.00 17.41 ? 358  GLU A OE1 1 
ATOM   2770 O  OE2 . GLU A 1 358  ? 37.888 49.450  30.954  1.00 21.91 ? 358  GLU A OE2 1 
ATOM   2771 N  N   . ARG A 1 359  ? 31.563 49.512  33.779  1.00 9.07  ? 359  ARG A N   1 
ATOM   2772 C  CA  . ARG A 1 359  ? 30.514 49.074  34.692  1.00 10.43 ? 359  ARG A CA  1 
ATOM   2773 C  C   . ARG A 1 359  ? 29.442 48.259  33.953  1.00 10.04 ? 359  ARG A C   1 
ATOM   2774 O  O   . ARG A 1 359  ? 28.997 47.227  34.441  1.00 10.42 ? 359  ARG A O   1 
ATOM   2775 C  CB  . ARG A 1 359  ? 29.899 50.273  35.402  1.00 10.16 ? 359  ARG A CB  1 
ATOM   2776 C  CG  . ARG A 1 359  ? 30.813 50.943  36.402  1.00 12.45 ? 359  ARG A CG  1 
ATOM   2777 C  CD  . ARG A 1 359  ? 30.133 52.182  36.954  1.00 18.79 ? 359  ARG A CD  1 
ATOM   2778 N  NE  . ARG A 1 359  ? 31.012 52.938  37.833  1.00 20.55 ? 359  ARG A NE  1 
ATOM   2779 C  CZ  . ARG A 1 359  ? 31.079 54.264  37.856  1.00 23.59 ? 359  ARG A CZ  1 
ATOM   2780 N  NH1 . ARG A 1 359  ? 30.316 54.991  37.041  1.00 21.16 ? 359  ARG A NH1 1 
ATOM   2781 N  NH2 . ARG A 1 359  ? 31.914 54.861  38.689  1.00 27.63 ? 359  ARG A NH2 1 
ATOM   2782 N  N   . LEU A 1 360  ? 29.049 48.715  32.770  1.00 9.67  ? 360  LEU A N   1 
ATOM   2783 C  CA  . LEU A 1 360  ? 28.085 47.994  31.972  1.00 8.67  ? 360  LEU A CA  1 
ATOM   2784 C  C   . LEU A 1 360  ? 28.633 46.635  31.577  1.00 8.64  ? 360  LEU A C   1 
ATOM   2785 O  O   . LEU A 1 360  ? 27.927 45.609  31.701  1.00 10.82 ? 360  LEU A O   1 
ATOM   2786 C  CB  . LEU A 1 360  ? 27.698 48.810  30.713  1.00 9.71  ? 360  LEU A CB  1 
ATOM   2787 C  CG  . LEU A 1 360  ? 26.853 50.029  31.088  1.00 9.60  ? 360  LEU A CG  1 
ATOM   2788 C  CD1 . LEU A 1 360  ? 26.953 51.054  29.925  1.00 10.79 ? 360  LEU A CD1 1 
ATOM   2789 C  CD2 . LEU A 1 360  ? 25.375 49.680  31.208  1.00 11.88 ? 360  LEU A CD2 1 
ATOM   2790 N  N   . PHE A 1 361  ? 29.884 46.545  31.115  1.00 9.68  ? 361  PHE A N   1 
ATOM   2791 C  CA  . PHE A 1 361  ? 30.426 45.247  30.729  1.00 8.69  ? 361  PHE A CA  1 
ATOM   2792 C  C   . PHE A 1 361  ? 30.465 44.277  31.928  1.00 8.89  ? 361  PHE A C   1 
ATOM   2793 O  O   . PHE A 1 361  ? 30.192 43.084  31.776  1.00 10.17 ? 361  PHE A O   1 
ATOM   2794 C  CB  . PHE A 1 361  ? 31.883 45.343  30.200  1.00 8.67  ? 361  PHE A CB  1 
ATOM   2795 C  CG  . PHE A 1 361  ? 32.030 46.189  28.929  1.00 9.84  ? 361  PHE A CG  1 
ATOM   2796 C  CD1 . PHE A 1 361  ? 30.980 46.402  28.043  1.00 9.51  ? 361  PHE A CD1 1 
ATOM   2797 C  CD2 . PHE A 1 361  ? 33.270 46.750  28.659  1.00 8.85  ? 361  PHE A CD2 1 
ATOM   2798 C  CE1 . PHE A 1 361  ? 31.184 47.201  26.863  1.00 10.34 ? 361  PHE A CE1 1 
ATOM   2799 C  CE2 . PHE A 1 361  ? 33.486 47.545  27.471  1.00 10.00 ? 361  PHE A CE2 1 
ATOM   2800 C  CZ  . PHE A 1 361  ? 32.441 47.749  26.603  1.00 11.25 ? 361  PHE A CZ  1 
ATOM   2801 N  N   . GLU A 1 362  ? 30.894 44.757  33.074  1.00 10.15 ? 362  GLU A N   1 
ATOM   2802 C  CA  . GLU A 1 362  ? 31.030 43.834  34.205  1.00 10.65 ? 362  GLU A CA  1 
ATOM   2803 C  C   . GLU A 1 362  ? 29.661 43.249  34.560  1.00 10.18 ? 362  GLU A C   1 
ATOM   2804 O  O   . GLU A 1 362  ? 29.540 42.032  34.812  1.00 11.54 ? 362  GLU A O   1 
ATOM   2805 C  CB  . GLU A 1 362  ? 31.598 44.529  35.449  1.00 14.71 ? 362  GLU A CB  1 
ATOM   2806 C  CG  . GLU A 1 362  ? 31.708 43.450  36.589  1.00 17.29 ? 362  GLU A CG  1 
ATOM   2807 C  CD  . GLU A 1 362  ? 32.339 43.941  37.880  1.00 24.85 ? 362  GLU A CD  1 
ATOM   2808 O  OE1 . GLU A 1 362  ? 32.908 45.042  37.859  1.00 24.35 ? 362  GLU A OE1 1 
ATOM   2809 O  OE2 . GLU A 1 362  ? 32.262 43.204  38.909  1.00 25.21 ? 362  GLU A OE2 1 
ATOM   2810 N  N   . HIS A 1 363  ? 28.631 44.070  34.531  1.00 9.73  ? 363  HIS A N   1 
ATOM   2811 C  CA  . HIS A 1 363  ? 27.282 43.562  34.789  1.00 9.95  ? 363  HIS A CA  1 
ATOM   2812 C  C   . HIS A 1 363  ? 26.804 42.627  33.695  1.00 10.51 ? 363  HIS A C   1 
ATOM   2813 O  O   . HIS A 1 363  ? 26.380 41.485  33.922  1.00 11.90 ? 363  HIS A O   1 
ATOM   2814 C  CB  . HIS A 1 363  ? 26.299 44.715  34.974  1.00 12.29 ? 363  HIS A CB  1 
ATOM   2815 C  CG  . HIS A 1 363  ? 24.887 44.267  35.216  1.00 10.60 ? 363  HIS A CG  1 
ATOM   2816 N  ND1 . HIS A 1 363  ? 24.453 43.801  36.452  1.00 16.27 ? 363  HIS A ND1 1 
ATOM   2817 C  CD2 . HIS A 1 363  ? 23.836 44.158  34.377  1.00 13.33 ? 363  HIS A CD2 1 
ATOM   2818 C  CE1 . HIS A 1 363  ? 23.189 43.418  36.338  1.00 15.11 ? 363  HIS A CE1 1 
ATOM   2819 N  NE2 . HIS A 1 363  ? 22.788 43.627  35.097  1.00 15.52 ? 363  HIS A NE2 1 
ATOM   2820 N  N   . ILE A 1 364  ? 26.822 43.084  32.443  1.00 10.23 ? 364  ILE A N   1 
ATOM   2821 C  CA  . ILE A 1 364  ? 26.314 42.299  31.351  1.00 10.77 ? 364  ILE A CA  1 
ATOM   2822 C  C   . ILE A 1 364  ? 27.001 40.956  31.206  1.00 9.00  ? 364  ILE A C   1 
ATOM   2823 O  O   . ILE A 1 364  ? 26.329 39.916  31.015  1.00 11.21 ? 364  ILE A O   1 
ATOM   2824 C  CB  . ILE A 1 364  ? 26.441 43.123  30.022  1.00 10.31 ? 364  ILE A CB  1 
ATOM   2825 C  CG1 . ILE A 1 364  ? 25.453 44.288  30.041  1.00 10.73 ? 364  ILE A CG1 1 
ATOM   2826 C  CG2 . ILE A 1 364  ? 26.227 42.180  28.828  1.00 11.76 ? 364  ILE A CG2 1 
ATOM   2827 C  CD1 . ILE A 1 364  ? 25.776 45.379  28.987  1.00 11.38 ? 364  ILE A CD1 1 
ATOM   2828 N  N   . ASN A 1 365  ? 28.305 40.944  31.307  1.00 8.88  ? 365  ASN A N   1 
ATOM   2829 C  CA  . ASN A 1 365  ? 29.067 39.715  31.062  1.00 10.52 ? 365  ASN A CA  1 
ATOM   2830 C  C   . ASN A 1 365  ? 28.860 38.706  32.192  1.00 13.78 ? 365  ASN A C   1 
ATOM   2831 O  O   . ASN A 1 365  ? 29.144 37.516  31.993  1.00 15.63 ? 365  ASN A O   1 
ATOM   2832 C  CB  . ASN A 1 365  ? 30.557 40.000  30.868  1.00 10.73 ? 365  ASN A CB  1 
ATOM   2833 C  CG  . ASN A 1 365  ? 30.822 40.870  29.629  1.00 9.43  ? 365  ASN A CG  1 
ATOM   2834 O  OD1 . ASN A 1 365  ? 29.908 41.086  28.793  1.00 11.05 ? 365  ASN A OD1 1 
ATOM   2835 N  ND2 . ASN A 1 365  ? 32.042 41.344  29.517  1.00 9.48  ? 365  ASN A ND2 1 
ATOM   2836 N  N   . SER A 1 366  ? 28.367 39.143  33.338  1.00 13.30 ? 366  SER A N   1 
ATOM   2837 C  CA  . SER A 1 366  ? 28.118 38.225  34.454  1.00 14.76 ? 366  SER A CA  1 
ATOM   2838 C  C   . SER A 1 366  ? 26.665 37.802  34.583  1.00 17.40 ? 366  SER A C   1 
ATOM   2839 O  O   . SER A 1 366  ? 26.354 36.979  35.442  1.00 21.15 ? 366  SER A O   1 
ATOM   2840 C  CB  . SER A 1 366  ? 28.630 38.806  35.768  1.00 19.33 ? 366  SER A CB  1 
ATOM   2841 O  OG  . SER A 1 366  ? 27.883 39.931  36.133  1.00 19.64 ? 366  SER A OG  1 
ATOM   2842 N  N   . GLN A 1 367  ? 25.782 38.346  33.757  1.00 17.66 ? 367  GLN A N   1 
ATOM   2843 C  CA  . GLN A 1 367  ? 24.360 37.994  33.831  1.00 18.19 ? 367  GLN A CA  1 
ATOM   2844 C  C   . GLN A 1 367  ? 24.122 36.981  32.728  1.00 17.82 ? 367  GLN A C   1 
ATOM   2845 O  O   . GLN A 1 367  ? 23.937 37.311  31.549  1.00 16.78 ? 367  GLN A O   1 
ATOM   2846 C  CB  . GLN A 1 367  ? 23.485 39.237  33.607  1.00 18.97 ? 367  GLN A CB  1 
ATOM   2847 C  CG  . GLN A 1 367  ? 23.487 40.178  34.836  1.00 25.46 ? 367  GLN A CG  1 
ATOM   2848 C  CD  . GLN A 1 367  ? 22.876 39.493  36.058  1.00 28.54 ? 367  GLN A CD  1 
ATOM   2849 O  OE1 . GLN A 1 367  ? 21.715 39.142  36.046  1.00 32.84 ? 367  GLN A OE1 1 
ATOM   2850 N  NE2 . GLN A 1 367  ? 23.669 39.280  37.091  1.00 35.51 ? 367  GLN A NE2 1 
ATOM   2851 N  N   . ALA A 1 368  ? 24.149 35.700  33.076  1.00 18.75 ? 368  ALA A N   1 
ATOM   2852 C  CA  . ALA A 1 368  ? 23.977 34.661  32.052  1.00 17.83 ? 368  ALA A CA  1 
ATOM   2853 C  C   . ALA A 1 368  ? 22.788 34.861  31.127  1.00 17.90 ? 368  ALA A C   1 
ATOM   2854 O  O   . ALA A 1 368  ? 22.912 34.569  29.921  1.00 18.72 ? 368  ALA A O   1 
ATOM   2855 C  CB  . ALA A 1 368  ? 23.861 33.268  32.737  1.00 19.70 ? 368  ALA A CB  1 
ATOM   2856 N  N   . HIS A 1 369  ? 21.656 35.316  31.659  1.00 16.47 ? 369  HIS A N   1 
ATOM   2857 C  CA  . HIS A 1 369  ? 20.469 35.505  30.851  1.00 15.90 ? 369  HIS A CA  1 
ATOM   2858 C  C   . HIS A 1 369  ? 20.621 36.379  29.608  1.00 16.26 ? 369  HIS A C   1 
ATOM   2859 O  O   . HIS A 1 369  ? 19.844 36.271  28.689  1.00 18.09 ? 369  HIS A O   1 
ATOM   2860 C  CB  . HIS A 1 369  ? 19.273 35.973  31.689  1.00 21.05 ? 369  HIS A CB  1 
ATOM   2861 C  CG  . HIS A 1 369  ? 19.353 37.400  32.123  1.00 24.41 ? 369  HIS A CG  1 
ATOM   2862 N  ND1 . HIS A 1 369  ? 19.948 37.779  33.300  1.00 28.53 ? 369  HIS A ND1 1 
ATOM   2863 C  CD2 . HIS A 1 369  ? 18.909 38.538  31.543  1.00 25.66 ? 369  HIS A CD2 1 
ATOM   2864 C  CE1 . HIS A 1 369  ? 19.879 39.091  33.425  1.00 25.52 ? 369  HIS A CE1 1 
ATOM   2865 N  NE2 . HIS A 1 369  ? 19.248 39.572  32.373  1.00 28.83 ? 369  HIS A NE2 1 
ATOM   2866 N  N   . PHE A 1 370  ? 21.589 37.284  29.588  1.00 17.09 ? 370  PHE A N   1 
ATOM   2867 C  CA  . PHE A 1 370  ? 21.839 38.086  28.384  1.00 15.17 ? 370  PHE A CA  1 
ATOM   2868 C  C   . PHE A 1 370  ? 22.534 37.288  27.297  1.00 13.59 ? 370  PHE A C   1 
ATOM   2869 O  O   . PHE A 1 370  ? 22.356 37.583  26.140  1.00 13.37 ? 370  PHE A O   1 
ATOM   2870 C  CB  . PHE A 1 370  ? 22.715 39.295  28.698  1.00 14.74 ? 370  PHE A CB  1 
ATOM   2871 C  CG  . PHE A 1 370  ? 22.016 40.405  29.433  1.00 15.51 ? 370  PHE A CG  1 
ATOM   2872 C  CD1 . PHE A 1 370  ? 20.819 40.932  28.992  1.00 16.61 ? 370  PHE A CD1 1 
ATOM   2873 C  CD2 . PHE A 1 370  ? 22.596 40.954  30.542  1.00 14.01 ? 370  PHE A CD2 1 
ATOM   2874 C  CE1 . PHE A 1 370  ? 20.230 41.968  29.673  1.00 18.79 ? 370  PHE A CE1 1 
ATOM   2875 C  CE2 . PHE A 1 370  ? 22.000 41.982  31.218  1.00 18.02 ? 370  PHE A CE2 1 
ATOM   2876 C  CZ  . PHE A 1 370  ? 20.832 42.492  30.771  1.00 18.26 ? 370  PHE A CZ  1 
ATOM   2877 N  N   . ASN A 1 371  ? 23.370 36.326  27.689  1.00 12.47 ? 371  ASN A N   1 
ATOM   2878 C  CA  . ASN A 1 371  ? 24.185 35.542  26.780  1.00 12.05 ? 371  ASN A CA  1 
ATOM   2879 C  C   . ASN A 1 371  ? 25.010 36.455  25.866  1.00 11.23 ? 371  ASN A C   1 
ATOM   2880 O  O   . ASN A 1 371  ? 25.061 36.242  24.641  1.00 12.46 ? 371  ASN A O   1 
ATOM   2881 C  CB  . ASN A 1 371  ? 23.317 34.576  25.963  1.00 13.89 ? 371  ASN A CB  1 
ATOM   2882 C  CG  . ASN A 1 371  ? 22.638 33.528  26.876  1.00 14.72 ? 371  ASN A CG  1 
ATOM   2883 O  OD1 . ASN A 1 371  ? 23.320 32.688  27.456  1.00 18.40 ? 371  ASN A OD1 1 
ATOM   2884 N  ND2 . ASN A 1 371  ? 21.327 33.658  27.033  1.00 17.21 ? 371  ASN A ND2 1 
ATOM   2885 N  N   . VAL A 1 372  ? 25.625 37.450  26.488  1.00 10.32 ? 372  VAL A N   1 
ATOM   2886 C  CA  . VAL A 1 372  ? 26.491 38.424  25.764  1.00 10.41 ? 372  VAL A CA  1 
ATOM   2887 C  C   . VAL A 1 372  ? 27.847 38.493  26.412  1.00 9.85  ? 372  VAL A C   1 
ATOM   2888 O  O   . VAL A 1 372  ? 28.003 38.370  27.666  1.00 11.49 ? 372  VAL A O   1 
ATOM   2889 C  CB  . VAL A 1 372  ? 25.880 39.831  25.872  1.00 11.29 ? 372  VAL A CB  1 
ATOM   2890 C  CG1 . VAL A 1 372  ? 26.890 40.934  25.381  1.00 10.76 ? 372  VAL A CG1 1 
ATOM   2891 C  CG2 . VAL A 1 372  ? 24.613 39.923  25.018  1.00 12.88 ? 372  VAL A CG2 1 
ATOM   2892 N  N   . GLN A 1 373  ? 28.896 38.616  25.602  1.00 9.71  ? 373  GLN A N   1 
ATOM   2893 C  CA  . GLN A 1 373  ? 30.248 38.876  26.100  1.00 9.42  ? 373  GLN A CA  1 
ATOM   2894 C  C   . GLN A 1 373  ? 30.677 40.206  25.383  1.00 9.12  ? 373  GLN A C   1 
ATOM   2895 O  O   . GLN A 1 373  ? 30.939 40.189  24.146  1.00 10.27 ? 373  GLN A O   1 
ATOM   2896 C  CB  . GLN A 1 373  ? 31.196 37.709  25.780  1.00 10.57 ? 373  GLN A CB  1 
ATOM   2897 C  CG  . GLN A 1 373  ? 32.664 38.020  26.098  1.00 11.94 ? 373  GLN A CG  1 
ATOM   2898 C  CD  . GLN A 1 373  ? 32.899 38.400  27.600  1.00 15.33 ? 373  GLN A CD  1 
ATOM   2899 O  OE1 . GLN A 1 373  ? 32.189 37.909  28.489  1.00 16.24 ? 373  GLN A OE1 1 
ATOM   2900 N  NE2 . GLN A 1 373  ? 33.887 39.206  27.867  1.00 15.05 ? 373  GLN A NE2 1 
ATOM   2901 N  N   . ALA A 1 374  ? 30.750 41.307  26.107  1.00 8.18  ? 374  ALA A N   1 
ATOM   2902 C  CA  . ALA A 1 374  ? 31.053 42.620  25.521  1.00 9.25  ? 374  ALA A CA  1 
ATOM   2903 C  C   . ALA A 1 374  ? 32.384 43.121  26.000  1.00 9.55  ? 374  ALA A C   1 
ATOM   2904 O  O   . ALA A 1 374  ? 32.753 42.952  27.192  1.00 9.52  ? 374  ALA A O   1 
ATOM   2905 C  CB  . ALA A 1 374  ? 29.975 43.558  25.913  1.00 10.08 ? 374  ALA A CB  1 
ATOM   2906 N  N   . GLN A 1 375  ? 33.111 43.813  25.135  1.00 8.79  ? 375  GLN A N   1 
ATOM   2907 C  CA  . GLN A 1 375  ? 34.424 44.359  25.506  1.00 9.04  ? 375  GLN A CA  1 
ATOM   2908 C  C   . GLN A 1 375  ? 34.839 45.454  24.546  1.00 8.51  ? 375  GLN A C   1 
ATOM   2909 O  O   . GLN A 1 375  ? 34.259 45.570  23.453  1.00 9.42  ? 375  GLN A O   1 
ATOM   2910 C  CB  . GLN A 1 375  ? 35.513 43.291  25.430  1.00 12.17 ? 375  GLN A CB  1 
ATOM   2911 C  CG  . GLN A 1 375  ? 35.519 42.496  24.108  1.00 13.58 ? 375  GLN A CG  1 
ATOM   2912 C  CD  . GLN A 1 375  ? 34.667 41.208  24.221  1.00 22.82 ? 375  GLN A CD  1 
ATOM   2913 O  OE1 . GLN A 1 375  ? 34.937 40.363  25.116  1.00 21.01 ? 375  GLN A OE1 1 
ATOM   2914 N  NE2 . GLN A 1 375  ? 33.637 41.035  23.345  1.00 17.39 ? 375  GLN A NE2 1 
ATOM   2915 N  N   . PHE A 1 376  ? 35.771 46.288  24.976  1.00 8.13  ? 376  PHE A N   1 
ATOM   2916 C  CA  . PHE A 1 376  ? 36.381 47.229  24.006  1.00 8.14  ? 376  PHE A CA  1 
ATOM   2917 C  C   . PHE A 1 376  ? 37.146 46.388  23.000  1.00 10.41 ? 376  PHE A C   1 
ATOM   2918 O  O   . PHE A 1 376  ? 37.814 45.388  23.339  1.00 11.46 ? 376  PHE A O   1 
ATOM   2919 C  CB  . PHE A 1 376  ? 37.357 48.173  24.711  1.00 8.77  ? 376  PHE A CB  1 
ATOM   2920 C  CG  . PHE A 1 376  ? 36.687 49.111  25.634  1.00 9.60  ? 376  PHE A CG  1 
ATOM   2921 C  CD1 . PHE A 1 376  ? 35.680 49.944  25.200  1.00 9.83  ? 376  PHE A CD1 1 
ATOM   2922 C  CD2 . PHE A 1 376  ? 37.066 49.135  26.991  1.00 10.38 ? 376  PHE A CD2 1 
ATOM   2923 C  CE1 . PHE A 1 376  ? 35.050 50.809  26.149  1.00 11.89 ? 376  PHE A CE1 1 
ATOM   2924 C  CE2 . PHE A 1 376  ? 36.444 49.990  27.884  1.00 12.60 ? 376  PHE A CE2 1 
ATOM   2925 C  CZ  . PHE A 1 376  ? 35.468 50.802  27.482  1.00 11.61 ? 376  PHE A CZ  1 
ATOM   2926 N  N   . GLY A 1 377  ? 37.153 46.856  21.753  1.00 8.98  ? 377  GLY A N   1 
ATOM   2927 C  CA  . GLY A 1 377  ? 37.902 46.143  20.720  1.00 8.83  ? 377  GLY A CA  1 
ATOM   2928 C  C   . GLY A 1 377  ? 38.385 47.119  19.664  1.00 8.41  ? 377  GLY A C   1 
ATOM   2929 O  O   . GLY A 1 377  ? 38.083 48.295  19.710  1.00 9.20  ? 377  GLY A O   1 
ATOM   2930 N  N   . THR A 1 378  ? 39.176 46.571  18.721  1.00 10.22 ? 378  THR A N   1 
ATOM   2931 C  CA  . THR A 1 378  ? 39.612 47.330  17.561  1.00 10.84 ? 378  THR A CA  1 
ATOM   2932 C  C   . THR A 1 378  ? 38.835 46.795  16.358  1.00 9.38  ? 378  THR A C   1 
ATOM   2933 O  O   . THR A 1 378  ? 38.108 45.790  16.392  1.00 9.93  ? 378  THR A O   1 
ATOM   2934 C  CB  . THR A 1 378  ? 41.102 47.222  17.290  1.00 11.71 ? 378  THR A CB  1 
ATOM   2935 O  OG1 . THR A 1 378  ? 41.404 45.877  16.889  1.00 11.56 ? 378  THR A OG1 1 
ATOM   2936 C  CG2 . THR A 1 378  ? 41.930 47.644  18.518  1.00 12.22 ? 378  THR A CG2 1 
ATOM   2937 N  N   . LEU A 1 379  ? 38.972 47.539  15.252  1.00 9.53  ? 379  LEU A N   1 
ATOM   2938 C  CA  . LEU A 1 379  ? 38.293 47.134  14.020  1.00 8.52  ? 379  LEU A CA  1 
ATOM   2939 C  C   . LEU A 1 379  ? 38.778 45.770  13.480  1.00 7.79  ? 379  LEU A C   1 
ATOM   2940 O  O   . LEU A 1 379  ? 37.988 44.922  13.062  1.00 8.47  ? 379  LEU A O   1 
ATOM   2941 C  CB  . LEU A 1 379  ? 38.458 48.260  12.970  1.00 8.05  ? 379  LEU A CB  1 
ATOM   2942 C  CG  . LEU A 1 379  ? 37.690 48.015  11.658  1.00 7.79  ? 379  LEU A CG  1 
ATOM   2943 C  CD1 . LEU A 1 379  ? 36.199 48.026  11.927  1.00 10.26 ? 379  LEU A CD1 1 
ATOM   2944 C  CD2 . LEU A 1 379  ? 38.065 49.110  10.619  1.00 10.45 ? 379  LEU A CD2 1 
ATOM   2945 N  N   . GLN A 1 380  ? 40.101 45.559  13.497  1.00 8.17  ? 380  GLN A N   1 
ATOM   2946 C  CA  . GLN A 1 380  ? 40.625 44.273  13.040  1.00 9.09  ? 380  GLN A CA  1 
ATOM   2947 C  C   . GLN A 1 380  ? 40.135 43.140  13.933  1.00 10.12 ? 380  GLN A C   1 
ATOM   2948 O  O   . GLN A 1 380  ? 39.884 42.029  13.425  1.00 9.53  ? 380  GLN A O   1 
ATOM   2949 C  CB  . GLN A 1 380  ? 42.163 44.311  12.993  1.00 10.13 ? 380  GLN A CB  1 
ATOM   2950 C  CG  . GLN A 1 380  ? 42.815 43.027  12.455  1.00 14.35 ? 380  GLN A CG  1 
ATOM   2951 C  CD  . GLN A 1 380  ? 42.456 42.853  11.022  1.00 16.37 ? 380  GLN A CD  1 
ATOM   2952 O  OE1 . GLN A 1 380  ? 42.580 43.810  10.241  1.00 17.35 ? 380  GLN A OE1 1 
ATOM   2953 N  NE2 . GLN A 1 380  ? 41.971 41.643  10.637  1.00 19.73 ? 380  GLN A NE2 1 
ATOM   2954 N  N   . GLU A 1 381  ? 39.998 43.376  15.239  1.00 8.90  ? 381  GLU A N   1 
ATOM   2955 C  CA  . GLU A 1 381  ? 39.496 42.318  16.115  1.00 9.67  ? 381  GLU A CA  1 
ATOM   2956 C  C   . GLU A 1 381  ? 38.070 41.917  15.707  1.00 8.09  ? 381  GLU A C   1 
ATOM   2957 O  O   . GLU A 1 381  ? 37.723 40.735  15.734  1.00 11.26 ? 381  GLU A O   1 
ATOM   2958 C  CB  . GLU A 1 381  ? 39.430 42.807  17.552  1.00 11.77 ? 381  GLU A CB  1 
ATOM   2959 C  CG  . GLU A 1 381  ? 40.692 42.774  18.371  1.00 17.80 ? 381  GLU A CG  1 
ATOM   2960 C  CD  . GLU A 1 381  ? 40.312 43.090  19.811  1.00 21.22 ? 381  GLU A CD  1 
ATOM   2961 O  OE1 . GLU A 1 381  ? 39.955 42.175  20.608  1.00 27.32 ? 381  GLU A OE1 1 
ATOM   2962 O  OE2 . GLU A 1 381  ? 40.329 44.258  20.131  1.00 19.37 ? 381  GLU A OE2 1 
ATOM   2963 N  N   . TYR A 1 382  ? 37.248 42.902  15.366  1.00 8.56  ? 382  TYR A N   1 
ATOM   2964 C  CA  . TYR A 1 382  ? 35.908 42.600  14.916  1.00 7.97  ? 382  TYR A CA  1 
ATOM   2965 C  C   . TYR A 1 382  ? 35.960 41.707  13.643  1.00 8.62  ? 382  TYR A C   1 
ATOM   2966 O  O   . TYR A 1 382  ? 35.324 40.663  13.566  1.00 8.57  ? 382  TYR A O   1 
ATOM   2967 C  CB  . TYR A 1 382  ? 35.137 43.898  14.587  1.00 8.74  ? 382  TYR A CB  1 
ATOM   2968 C  CG  . TYR A 1 382  ? 33.842 43.646  13.883  1.00 7.47  ? 382  TYR A CG  1 
ATOM   2969 C  CD1 . TYR A 1 382  ? 32.764 43.062  14.540  1.00 8.21  ? 382  TYR A CD1 1 
ATOM   2970 C  CD2 . TYR A 1 382  ? 33.726 43.887  12.503  1.00 8.44  ? 382  TYR A CD2 1 
ATOM   2971 C  CE1 . TYR A 1 382  ? 31.591 42.715  13.865  1.00 9.22  ? 382  TYR A CE1 1 
ATOM   2972 C  CE2 . TYR A 1 382  ? 32.559 43.555  11.813  1.00 9.96  ? 382  TYR A CE2 1 
ATOM   2973 C  CZ  . TYR A 1 382  ? 31.496 42.960  12.513  1.00 8.33  ? 382  TYR A CZ  1 
ATOM   2974 O  OH  . TYR A 1 382  ? 30.293 42.626  11.897  1.00 10.18 ? 382  TYR A OH  1 
ATOM   2975 N  N   . PHE A 1 383  ? 36.714 42.149  12.644  1.00 7.69  ? 383  PHE A N   1 
ATOM   2976 C  CA  . PHE A 1 383  ? 36.734 41.366  11.389  1.00 8.16  ? 383  PHE A CA  1 
ATOM   2977 C  C   . PHE A 1 383  ? 37.335 39.973  11.598  1.00 8.76  ? 383  PHE A C   1 
ATOM   2978 O  O   . PHE A 1 383  ? 36.854 39.018  10.972  1.00 9.51  ? 383  PHE A O   1 
ATOM   2979 C  CB  . PHE A 1 383  ? 37.498 42.141  10.296  1.00 8.20  ? 383  PHE A CB  1 
ATOM   2980 C  CG  . PHE A 1 383  ? 36.719 43.310  9.701   1.00 8.10  ? 383  PHE A CG  1 
ATOM   2981 C  CD1 . PHE A 1 383  ? 35.520 43.107  9.034   1.00 8.89  ? 383  PHE A CD1 1 
ATOM   2982 C  CD2 . PHE A 1 383  ? 37.237 44.608  9.776   1.00 7.80  ? 383  PHE A CD2 1 
ATOM   2983 C  CE1 . PHE A 1 383  ? 34.792 44.195  8.432   1.00 9.30  ? 383  PHE A CE1 1 
ATOM   2984 C  CE2 . PHE A 1 383  ? 36.508 45.674  9.170   1.00 8.77  ? 383  PHE A CE2 1 
ATOM   2985 C  CZ  . PHE A 1 383  ? 35.337 45.484  8.526   1.00 9.51  ? 383  PHE A CZ  1 
ATOM   2986 N  N   . ASP A 1 384  ? 38.401 39.901  12.392  1.00 9.25  ? 384  ASP A N   1 
ATOM   2987 C  CA  . ASP A 1 384  ? 38.957 38.561  12.647  1.00 10.29 ? 384  ASP A CA  1 
ATOM   2988 C  C   . ASP A 1 384  ? 37.892 37.625  13.252  1.00 9.91  ? 384  ASP A C   1 
ATOM   2989 O  O   . ASP A 1 384  ? 37.772 36.439  12.824  1.00 10.37 ? 384  ASP A O   1 
ATOM   2990 C  CB  . ASP A 1 384  ? 40.141 38.649  13.617  1.00 12.64 ? 384  ASP A CB  1 
ATOM   2991 C  CG  . ASP A 1 384  ? 41.368 39.258  12.990  1.00 14.69 ? 384  ASP A CG  1 
ATOM   2992 O  OD1 . ASP A 1 384  ? 41.447 39.411  11.759  1.00 17.50 ? 384  ASP A OD1 1 
ATOM   2993 O  OD2 . ASP A 1 384  ? 42.279 39.575  13.778  1.00 20.41 ? 384  ASP A OD2 1 
ATOM   2994 N  N   . ALA A 1 385  ? 37.094 38.120  14.193  1.00 9.69  ? 385  ALA A N   1 
ATOM   2995 C  CA  . ALA A 1 385  ? 36.055 37.254  14.787  1.00 9.49  ? 385  ALA A CA  1 
ATOM   2996 C  C   . ALA A 1 385  ? 34.953 36.925  13.786  1.00 10.91 ? 385  ALA A C   1 
ATOM   2997 O  O   . ALA A 1 385  ? 34.449 35.776  13.772  1.00 10.82 ? 385  ALA A O   1 
ATOM   2998 C  CB  . ALA A 1 385  ? 35.514 37.937  16.035  1.00 9.93  ? 385  ALA A CB  1 
ATOM   2999 N  N   . VAL A 1 386  ? 34.543 37.891  12.939  1.00 9.85  ? 386  VAL A N   1 
ATOM   3000 C  CA  . VAL A 1 386  ? 33.564 37.580  11.911  1.00 10.52 ? 386  VAL A CA  1 
ATOM   3001 C  C   . VAL A 1 386  ? 34.055 36.457  10.990  1.00 10.98 ? 386  VAL A C   1 
ATOM   3002 O  O   . VAL A 1 386  ? 33.270 35.508  10.679  1.00 11.21 ? 386  VAL A O   1 
ATOM   3003 C  CB  . VAL A 1 386  ? 33.278 38.842  11.044  1.00 10.20 ? 386  VAL A CB  1 
ATOM   3004 C  CG1 . VAL A 1 386  ? 32.469 38.503  9.767   1.00 12.95 ? 386  VAL A CG1 1 
ATOM   3005 C  CG2 . VAL A 1 386  ? 32.546 39.877  11.857  1.00 11.31 ? 386  VAL A CG2 1 
ATOM   3006 N  N   . HIS A 1 387  ? 35.308 36.517  10.552  1.00 10.99 ? 387  HIS A N   1 
ATOM   3007 C  CA  . HIS A 1 387  ? 35.804 35.477  9.650   1.00 11.17 ? 387  HIS A CA  1 
ATOM   3008 C  C   . HIS A 1 387  ? 36.026 34.133  10.377  1.00 11.81 ? 387  HIS A C   1 
ATOM   3009 O  O   . HIS A 1 387  ? 35.934 33.081  9.707   1.00 11.63 ? 387  HIS A O   1 
ATOM   3010 C  CB  . HIS A 1 387  ? 37.040 35.950  8.897   1.00 11.33 ? 387  HIS A CB  1 
ATOM   3011 C  CG  . HIS A 1 387  ? 36.727 37.083  7.959   1.00 9.61  ? 387  HIS A CG  1 
ATOM   3012 N  ND1 . HIS A 1 387  ? 35.814 36.960  6.926   1.00 13.41 ? 387  HIS A ND1 1 
ATOM   3013 C  CD2 . HIS A 1 387  ? 37.166 38.368  7.939   1.00 10.17 ? 387  HIS A CD2 1 
ATOM   3014 C  CE1 . HIS A 1 387  ? 35.723 38.132  6.295   1.00 13.58 ? 387  HIS A CE1 1 
ATOM   3015 N  NE2 . HIS A 1 387  ? 36.528 38.992  6.892   1.00 12.92 ? 387  HIS A NE2 1 
ATOM   3016 N  N   . GLN A 1 388  ? 36.308 34.162  11.665  1.00 12.30 ? 388  GLN A N   1 
ATOM   3017 C  CA  . GLN A 1 388  ? 36.360 32.921  12.436  1.00 12.90 ? 388  GLN A CA  1 
ATOM   3018 C  C   . GLN A 1 388  ? 34.988 32.237  12.397  1.00 14.95 ? 388  GLN A C   1 
ATOM   3019 O  O   . GLN A 1 388  ? 34.874 31.045  12.195  1.00 16.07 ? 388  GLN A O   1 
ATOM   3020 C  CB  . GLN A 1 388  ? 36.805 33.234  13.857  1.00 14.56 ? 388  GLN A CB  1 
ATOM   3021 C  CG  . GLN A 1 388  ? 38.313 33.477  13.961  1.00 21.72 ? 388  GLN A CG  1 
ATOM   3022 C  CD  . GLN A 1 388  ? 38.709 34.241  15.224  1.00 30.75 ? 388  GLN A CD  1 
ATOM   3023 O  OE1 . GLN A 1 388  ? 37.936 34.342  16.172  1.00 34.00 ? 388  GLN A OE1 1 
ATOM   3024 N  NE2 . GLN A 1 388  ? 39.913 34.776  15.235  1.00 31.61 ? 388  GLN A NE2 1 
ATOM   3025 N  N   . ALA A 1 389  ? 33.947 33.014  12.551  1.00 12.27 ? 389  ALA A N   1 
ATOM   3026 C  CA  . ALA A 1 389  ? 32.564 32.489  12.519  1.00 14.44 ? 389  ALA A CA  1 
ATOM   3027 C  C   . ALA A 1 389  ? 32.281 31.950  11.121  1.00 16.64 ? 389  ALA A C   1 
ATOM   3028 O  O   . ALA A 1 389  ? 31.726 30.852  10.960  1.00 18.08 ? 389  ALA A O   1 
ATOM   3029 C  CB  . ALA A 1 389  ? 31.586 33.562  12.890  1.00 14.41 ? 389  ALA A CB  1 
ATOM   3030 N  N   . GLU A 1 390  ? 32.684 32.692  10.078  1.00 15.06 ? 390  GLU A N   1 
ATOM   3031 C  CA  . GLU A 1 390  ? 32.488 32.252  8.686   1.00 15.01 ? 390  GLU A CA  1 
ATOM   3032 C  C   . GLU A 1 390  ? 33.175 30.917  8.435   1.00 17.71 ? 390  GLU A C   1 
ATOM   3033 O  O   . GLU A 1 390  ? 32.568 29.994  7.846   1.00 20.54 ? 390  GLU A O   1 
ATOM   3034 C  CB  . GLU A 1 390  ? 33.079 33.323  7.735   1.00 14.97 ? 390  GLU A CB  1 
ATOM   3035 C  CG  . GLU A 1 390  ? 32.867 33.038  6.245   1.00 17.78 ? 390  GLU A CG  1 
ATOM   3036 C  CD  . GLU A 1 390  ? 33.616 34.054  5.399   1.00 21.13 ? 390  GLU A CD  1 
ATOM   3037 O  OE1 . GLU A 1 390  ? 34.486 34.764  5.963   1.00 21.71 ? 390  GLU A OE1 1 
ATOM   3038 O  OE2 . GLU A 1 390  ? 33.362 34.155  4.184   1.00 21.58 ? 390  GLU A OE2 1 
ATOM   3039 N  N   . ARG A 1 391  ? 34.436 30.797  8.854   1.00 16.89 ? 391  ARG A N   1 
ATOM   3040 C  CA  . ARG A 1 391  ? 35.177 29.549  8.633   1.00 20.28 ? 391  ARG A CA  1 
ATOM   3041 C  C   . ARG A 1 391  ? 34.565 28.394  9.434   1.00 21.36 ? 391  ARG A C   1 
ATOM   3042 O  O   . ARG A 1 391  ? 34.682 27.210  9.017   1.00 26.05 ? 391  ARG A O   1 
ATOM   3043 C  CB  . ARG A 1 391  ? 36.647 29.745  9.017   1.00 22.31 ? 391  ARG A CB  1 
ATOM   3044 C  CG  . ARG A 1 391  ? 37.426 30.657  8.069   1.00 28.52 ? 391  ARG A CG  1 
ATOM   3045 C  CD  . ARG A 1 391  ? 38.922 30.498  8.308   1.00 30.52 ? 391  ARG A CD  1 
ATOM   3046 N  NE  . ARG A 1 391  ? 39.353 30.997  9.611   1.00 32.59 ? 391  ARG A NE  1 
ATOM   3047 C  CZ  . ARG A 1 391  ? 39.530 32.291  9.891   1.00 28.15 ? 391  ARG A CZ  1 
ATOM   3048 N  NH1 . ARG A 1 391  ? 39.317 33.211  8.955   1.00 29.66 ? 391  ARG A NH1 1 
ATOM   3049 N  NH2 . ARG A 1 391  ? 39.912 32.645  11.101  1.00 32.73 ? 391  ARG A NH2 1 
ATOM   3050 N  N   . ALA A 1 392  ? 33.902 28.690  10.538  1.00 19.61 ? 392  ALA A N   1 
ATOM   3051 C  CA  . ALA A 1 392  ? 33.267 27.613  11.320  1.00 22.19 ? 392  ALA A CA  1 
ATOM   3052 C  C   . ALA A 1 392  ? 31.917 27.229  10.657  1.00 24.72 ? 392  ALA A C   1 
ATOM   3053 O  O   . ALA A 1 392  ? 31.146 26.415  11.212  1.00 27.28 ? 392  ALA A O   1 
ATOM   3054 C  CB  . ALA A 1 392  ? 33.041 28.058  12.741  1.00 20.69 ? 392  ALA A CB  1 
ATOM   3055 N  N   . GLY A 1 393  ? 31.606 27.817  9.493   1.00 22.33 ? 393  GLY A N   1 
ATOM   3056 C  CA  . GLY A 1 393  ? 30.360 27.470  8.827   1.00 23.72 ? 393  GLY A CA  1 
ATOM   3057 C  C   . GLY A 1 393  ? 29.130 28.109  9.421   1.00 18.56 ? 393  GLY A C   1 
ATOM   3058 O  O   . GLY A 1 393  ? 27.995 27.729  9.107   1.00 22.74 ? 393  GLY A O   1 
ATOM   3059 N  N   . GLN A 1 394  ? 29.347 29.152  10.204  1.00 19.23 ? 394  GLN A N   1 
ATOM   3060 C  CA  . GLN A 1 394  ? 28.269 29.854  10.873  1.00 20.99 ? 394  GLN A CA  1 
ATOM   3061 C  C   . GLN A 1 394  ? 27.509 30.874  10.003  1.00 17.77 ? 394  GLN A C   1 
ATOM   3062 O  O   . GLN A 1 394  ? 26.444 31.285  10.355  1.00 22.73 ? 394  GLN A O   1 
ATOM   3063 C  CB  . GLN A 1 394  ? 28.839 30.538  12.125  1.00 24.63 ? 394  GLN A CB  1 
ATOM   3064 C  CG  . GLN A 1 394  ? 27.850 30.957  13.157  1.00 34.84 ? 394  GLN A CG  1 
ATOM   3065 C  CD  . GLN A 1 394  ? 28.338 32.087  14.025  1.00 33.62 ? 394  GLN A CD  1 
ATOM   3066 O  OE1 . GLN A 1 394  ? 28.005 33.247  13.801  1.00 36.02 ? 394  GLN A OE1 1 
ATOM   3067 N  NE2 . GLN A 1 394  ? 29.111 31.748  15.042  1.00 18.21 ? 394  GLN A NE2 1 
ATOM   3068 N  N   . ALA A 1 395  ? 28.076 31.279  8.873   1.00 17.93 ? 395  ALA A N   1 
ATOM   3069 C  CA  . ALA A 1 395  ? 27.499 32.298  8.008   1.00 16.54 ? 395  ALA A CA  1 
ATOM   3070 C  C   . ALA A 1 395  ? 28.193 32.248  6.631   1.00 14.79 ? 395  ALA A C   1 
ATOM   3071 O  O   . ALA A 1 395  ? 29.334 31.823  6.518   1.00 17.67 ? 395  ALA A O   1 
ATOM   3072 C  CB  . ALA A 1 395  ? 27.718 33.695  8.670   1.00 20.96 ? 395  ALA A CB  1 
ATOM   3073 N  N   . GLU A 1 396  ? 27.472 32.645  5.578   1.00 16.85 ? 396  GLU A N   1 
ATOM   3074 C  CA  . GLU A 1 396  ? 28.051 32.762  4.224   1.00 15.21 ? 396  GLU A CA  1 
ATOM   3075 C  C   . GLU A 1 396  ? 27.588 34.161  3.801   1.00 14.49 ? 396  GLU A C   1 
ATOM   3076 O  O   . GLU A 1 396  ? 26.494 34.604  4.197   1.00 17.46 ? 396  GLU A O   1 
ATOM   3077 C  CB  . GLU A 1 396  ? 27.499 31.685  3.290   1.00 22.24 ? 396  GLU A CB  1 
ATOM   3078 C  CG  . GLU A 1 396  ? 26.006 31.697  3.143   1.00 30.83 ? 396  GLU A CG  1 
ATOM   3079 C  CD  . GLU A 1 396  ? 25.521 30.546  2.274   1.00 38.98 ? 396  GLU A CD  1 
ATOM   3080 O  OE1 . GLU A 1 396  ? 26.361 29.680  1.924   1.00 39.93 ? 396  GLU A OE1 1 
ATOM   3081 O  OE2 . GLU A 1 396  ? 24.312 30.510  1.944   1.00 44.58 ? 396  GLU A OE2 1 
ATOM   3082 N  N   . PHE A 1 397  ? 28.431 34.824  3.021   1.00 12.81 ? 397  PHE A N   1 
ATOM   3083 C  CA  . PHE A 1 397  ? 28.137 36.194  2.664   1.00 9.68  ? 397  PHE A CA  1 
ATOM   3084 C  C   . PHE A 1 397  ? 27.829 36.355  1.195   1.00 9.78  ? 397  PHE A C   1 
ATOM   3085 O  O   . PHE A 1 397  ? 28.387 35.661  0.360   1.00 12.84 ? 397  PHE A O   1 
ATOM   3086 C  CB  . PHE A 1 397  ? 29.352 37.059  3.029   1.00 11.53 ? 397  PHE A CB  1 
ATOM   3087 C  CG  . PHE A 1 397  ? 29.662 37.081  4.517   1.00 11.98 ? 397  PHE A CG  1 
ATOM   3088 C  CD1 . PHE A 1 397  ? 28.824 37.746  5.381   1.00 9.35  ? 397  PHE A CD1 1 
ATOM   3089 C  CD2 . PHE A 1 397  ? 30.756 36.397  5.018   1.00 13.31 ? 397  PHE A CD2 1 
ATOM   3090 C  CE1 . PHE A 1 397  ? 29.057 37.719  6.748   1.00 11.33 ? 397  PHE A CE1 1 
ATOM   3091 C  CE2 . PHE A 1 397  ? 30.989 36.366  6.429   1.00 12.89 ? 397  PHE A CE2 1 
ATOM   3092 C  CZ  . PHE A 1 397  ? 30.146 37.015  7.235   1.00 10.76 ? 397  PHE A CZ  1 
ATOM   3093 N  N   . PRO A 1 398  ? 26.940 37.258  0.902   1.00 8.97  ? 398  PRO A N   1 
ATOM   3094 C  CA  . PRO A 1 398  ? 26.564 37.533  -0.473  1.00 9.07  ? 398  PRO A CA  1 
ATOM   3095 C  C   . PRO A 1 398  ? 27.631 38.290  -1.227  1.00 9.39  ? 398  PRO A C   1 
ATOM   3096 O  O   . PRO A 1 398  ? 28.469 38.988  -0.612  1.00 10.25 ? 398  PRO A O   1 
ATOM   3097 C  CB  . PRO A 1 398  ? 25.327 38.365  -0.305  1.00 11.53 ? 398  PRO A CB  1 
ATOM   3098 C  CG  . PRO A 1 398  ? 25.558 39.168  0.962   1.00 11.87 ? 398  PRO A CG  1 
ATOM   3099 C  CD  . PRO A 1 398  ? 26.217 38.110  1.842   1.00 10.50 ? 398  PRO A CD  1 
ATOM   3100 N  N   . THR A 1 399  ? 27.607 38.150  -2.532  1.00 8.92  ? 399  THR A N   1 
ATOM   3101 C  CA  . THR A 1 399  ? 28.523 38.891  -3.427  1.00 8.10  ? 399  THR A CA  1 
ATOM   3102 C  C   . THR A 1 399  ? 27.743 40.109  -3.939  1.00 8.45  ? 399  THR A C   1 
ATOM   3103 O  O   . THR A 1 399  ? 26.532 40.096  -4.106  1.00 9.03  ? 399  THR A O   1 
ATOM   3104 C  CB  . THR A 1 399  ? 28.937 38.009  -4.565  1.00 9.29  ? 399  THR A CB  1 
ATOM   3105 O  OG1 . THR A 1 399  ? 27.765 37.585  -5.288  1.00 10.72 ? 399  THR A OG1 1 
ATOM   3106 C  CG2 . THR A 1 399  ? 29.756 36.796  -4.028  1.00 10.11 ? 399  THR A CG2 1 
ATOM   3107 N  N   . LEU A 1 400  ? 28.495 41.192  -4.202  1.00 8.09  ? 400  LEU A N   1 
ATOM   3108 C  CA  . LEU A 1 400  ? 27.888 42.453  -4.638  1.00 7.15  ? 400  LEU A CA  1 
ATOM   3109 C  C   . LEU A 1 400  ? 28.826 43.175  -5.591  1.00 6.60  ? 400  LEU A C   1 
ATOM   3110 O  O   . LEU A 1 400  ? 30.056 43.129  -5.446  1.00 7.11  ? 400  LEU A O   1 
ATOM   3111 C  CB  . LEU A 1 400  ? 27.626 43.364  -3.415  1.00 8.10  ? 400  LEU A CB  1 
ATOM   3112 C  CG  . LEU A 1 400  ? 26.955 44.748  -3.631  1.00 7.36  ? 400  LEU A CG  1 
ATOM   3113 C  CD1 . LEU A 1 400  ? 26.096 45.139  -2.393  1.00 9.91  ? 400  LEU A CD1 1 
ATOM   3114 C  CD2 . LEU A 1 400  ? 27.993 45.825  -3.970  1.00 8.16  ? 400  LEU A CD2 1 
ATOM   3115 N  N   . SER A 1 401  ? 28.212 43.804  -6.615  1.00 7.08  ? 401  SER A N   1 
ATOM   3116 C  CA  . SER A 1 401  ? 28.973 44.750  -7.449  1.00 6.88  ? 401  SER A CA  1 
ATOM   3117 C  C   . SER A 1 401  ? 28.103 45.982  -7.647  1.00 6.50  ? 401  SER A C   1 
ATOM   3118 O  O   . SER A 1 401  ? 26.895 45.962  -7.451  1.00 6.61  ? 401  SER A O   1 
ATOM   3119 C  CB  . SER A 1 401  ? 29.372 44.153  -8.797  1.00 8.19  ? 401  SER A CB  1 
ATOM   3120 O  OG  . SER A 1 401  ? 28.259 44.129  -9.694  1.00 7.60  ? 401  SER A OG  1 
ATOM   3121 N  N   . GLY A 1 402  ? 28.780 47.082  -7.984  1.00 7.01  ? 402  GLY A N   1 
ATOM   3122 C  CA  . GLY A 1 402  ? 28.128 48.371  -8.226  1.00 6.60  ? 402  GLY A CA  1 
ATOM   3123 C  C   . GLY A 1 402  ? 28.722 49.455  -7.319  1.00 6.45  ? 402  GLY A C   1 
ATOM   3124 O  O   . GLY A 1 402  ? 29.795 49.251  -6.694  1.00 8.49  ? 402  GLY A O   1 
ATOM   3125 N  N   . ASP A 1 403  ? 28.110 50.627  -7.297  1.00 6.10  ? 403  ASP A N   1 
ATOM   3126 C  CA  . ASP A 1 403  ? 28.586 51.733  -6.455  1.00 6.32  ? 403  ASP A CA  1 
ATOM   3127 C  C   . ASP A 1 403  ? 27.464 52.185  -5.556  1.00 7.34  ? 403  ASP A C   1 
ATOM   3128 O  O   . ASP A 1 403  ? 26.335 51.640  -5.567  1.00 8.22  ? 403  ASP A O   1 
ATOM   3129 C  CB  . ASP A 1 403  ? 29.105 52.902  -7.342  1.00 7.27  ? 403  ASP A CB  1 
ATOM   3130 C  CG  . ASP A 1 403  ? 28.023 53.629  -8.065  1.00 9.14  ? 403  ASP A CG  1 
ATOM   3131 O  OD1 . ASP A 1 403  ? 26.891 53.186  -8.132  1.00 12.07 ? 403  ASP A OD1 1 
ATOM   3132 O  OD2 . ASP A 1 403  ? 28.378 54.708  -8.566  1.00 11.87 ? 403  ASP A OD2 1 
ATOM   3133 N  N   . PHE A 1 404  ? 27.765 53.213  -4.768  1.00 6.05  ? 404  PHE A N   1 
ATOM   3134 C  CA  . PHE A 1 404  ? 26.812 53.782  -3.810  1.00 6.35  ? 404  PHE A CA  1 
ATOM   3135 C  C   . PHE A 1 404  ? 26.705 55.273  -3.986  1.00 6.32  ? 404  PHE A C   1 
ATOM   3136 O  O   . PHE A 1 404  ? 26.820 56.039  -3.056  1.00 7.33  ? 404  PHE A O   1 
ATOM   3137 C  CB  . PHE A 1 404  ? 27.156 53.354  -2.341  1.00 6.86  ? 404  PHE A CB  1 
ATOM   3138 C  CG  . PHE A 1 404  ? 27.121 51.843  -2.149  1.00 6.20  ? 404  PHE A CG  1 
ATOM   3139 C  CD1 . PHE A 1 404  ? 25.874 51.221  -2.052  1.00 6.68  ? 404  PHE A CD1 1 
ATOM   3140 C  CD2 . PHE A 1 404  ? 28.279 51.100  -2.111  1.00 7.09  ? 404  PHE A CD2 1 
ATOM   3141 C  CE1 . PHE A 1 404  ? 25.815 49.804  -1.909  1.00 6.56  ? 404  PHE A CE1 1 
ATOM   3142 C  CE2 . PHE A 1 404  ? 28.204 49.685  -1.973  1.00 7.65  ? 404  PHE A CE2 1 
ATOM   3143 C  CZ  . PHE A 1 404  ? 26.968 49.076  -1.872  1.00 7.50  ? 404  PHE A CZ  1 
ATOM   3144 N  N   . PHE A 1 405  ? 26.423 55.664  -5.235  1.00 6.99  ? 405  PHE A N   1 
ATOM   3145 C  CA  . PHE A 1 405  ? 26.096 57.069  -5.546  1.00 5.94  ? 405  PHE A CA  1 
ATOM   3146 C  C   . PHE A 1 405  ? 24.734 57.048  -6.255  1.00 7.26  ? 405  PHE A C   1 
ATOM   3147 O  O   . PHE A 1 405  ? 24.408 56.048  -6.950  1.00 8.17  ? 405  PHE A O   1 
ATOM   3148 C  CB  . PHE A 1 405  ? 27.130 57.685  -6.519  1.00 7.28  ? 405  PHE A CB  1 
ATOM   3149 C  CG  . PHE A 1 405  ? 28.514 57.785  -5.976  1.00 6.38  ? 405  PHE A CG  1 
ATOM   3150 C  CD1 . PHE A 1 405  ? 28.754 58.591  -4.871  1.00 7.63  ? 405  PHE A CD1 1 
ATOM   3151 C  CD2 . PHE A 1 405  ? 29.554 57.080  -6.567  1.00 7.63  ? 405  PHE A CD2 1 
ATOM   3152 C  CE1 . PHE A 1 405  ? 30.095 58.689  -4.324  1.00 7.38  ? 405  PHE A CE1 1 
ATOM   3153 C  CE2 . PHE A 1 405  ? 30.873 57.156  -6.024  1.00 7.23  ? 405  PHE A CE2 1 
ATOM   3154 C  CZ  . PHE A 1 405  ? 31.111 57.969  -4.899  1.00 6.12  ? 405  PHE A CZ  1 
ATOM   3155 N  N   . THR A 1 406  ? 23.930 58.096  -6.157  1.00 7.62  ? 406  THR A N   1 
ATOM   3156 C  CA  . THR A 1 406  ? 24.161 59.308  -5.381  1.00 6.82  ? 406  THR A CA  1 
ATOM   3157 C  C   . THR A 1 406  ? 23.510 59.168  -4.014  1.00 6.78  ? 406  THR A C   1 
ATOM   3158 O  O   . THR A 1 406  ? 22.342 58.776  -3.858  1.00 8.27  ? 406  THR A O   1 
ATOM   3159 C  CB  . THR A 1 406  ? 23.620 60.541  -6.151  1.00 6.36  ? 406  THR A CB  1 
ATOM   3160 O  OG1 . THR A 1 406  ? 24.538 60.703  -7.224  1.00 8.22  ? 406  THR A OG1 1 
ATOM   3161 C  CG2 . THR A 1 406  ? 23.501 61.817  -5.336  1.00 6.95  ? 406  THR A CG2 1 
ATOM   3162 N  N   . TYR A 1 407  ? 24.259 59.533  -2.993  1.00 6.40  ? 407  TYR A N   1 
ATOM   3163 C  CA  . TYR A 1 407  ? 23.848 59.442  -1.602  1.00 6.06  ? 407  TYR A CA  1 
ATOM   3164 C  C   . TYR A 1 407  ? 22.727 60.426  -1.280  1.00 7.85  ? 407  TYR A C   1 
ATOM   3165 O  O   . TYR A 1 407  ? 22.758 61.560  -1.718  1.00 8.06  ? 407  TYR A O   1 
ATOM   3166 C  CB  . TYR A 1 407  ? 25.062 59.784  -0.736  1.00 7.36  ? 407  TYR A CB  1 
ATOM   3167 C  CG  . TYR A 1 407  ? 24.862 59.880  0.765   1.00 6.38  ? 407  TYR A CG  1 
ATOM   3168 C  CD1 . TYR A 1 407  ? 24.400 58.801  1.519   1.00 7.52  ? 407  TYR A CD1 1 
ATOM   3169 C  CD2 . TYR A 1 407  ? 25.174 61.042  1.427   1.00 8.11  ? 407  TYR A CD2 1 
ATOM   3170 C  CE1 . TYR A 1 407  ? 24.245 58.914  2.879   1.00 7.81  ? 407  TYR A CE1 1 
ATOM   3171 C  CE2 . TYR A 1 407  ? 25.035 61.147  2.770   1.00 8.13  ? 407  TYR A CE2 1 
ATOM   3172 C  CZ  . TYR A 1 407  ? 24.569 60.080  3.492   1.00 7.84  ? 407  TYR A CZ  1 
ATOM   3173 O  OH  . TYR A 1 407  ? 24.471 60.234  4.837   1.00 9.05  ? 407  TYR A OH  1 
ATOM   3174 N  N   . ALA A 1 408  ? 21.755 59.958  -0.491  1.00 8.77  ? 408  ALA A N   1 
ATOM   3175 C  CA  . ALA A 1 408  ? 20.828 60.850  0.203   1.00 7.65  ? 408  ALA A CA  1 
ATOM   3176 C  C   . ALA A 1 408  ? 20.752 60.386  1.649   1.00 7.07  ? 408  ALA A C   1 
ATOM   3177 O  O   . ALA A 1 408  ? 20.637 59.193  1.884   1.00 8.42  ? 408  ALA A O   1 
ATOM   3178 C  CB  . ALA A 1 408  ? 19.403 60.809  -0.452  1.00 8.78  ? 408  ALA A CB  1 
ATOM   3179 N  N   . ASP A 1 409  ? 20.856 61.328  2.586   1.00 7.94  ? 409  ASP A N   1 
ATOM   3180 C  CA  . ASP A 1 409  ? 20.772 60.970  4.012   1.00 9.30  ? 409  ASP A CA  1 
ATOM   3181 C  C   . ASP A 1 409  ? 19.352 61.034  4.532   1.00 10.38 ? 409  ASP A C   1 
ATOM   3182 O  O   . ASP A 1 409  ? 19.051 60.374  5.555   1.00 11.12 ? 409  ASP A O   1 
ATOM   3183 C  CB  . ASP A 1 409  ? 21.673 61.866  4.890   1.00 8.05  ? 409  ASP A CB  1 
ATOM   3184 C  CG  . ASP A 1 409  ? 21.397 63.358  4.800   1.00 7.55  ? 409  ASP A CG  1 
ATOM   3185 O  OD1 . ASP A 1 409  ? 20.809 63.870  3.806   1.00 8.45  ? 409  ASP A OD1 1 
ATOM   3186 O  OD2 . ASP A 1 409  ? 21.871 64.088  5.732   1.00 11.28 ? 409  ASP A OD2 1 
ATOM   3187 N  N   . ARG A 1 410  ? 18.447 61.739  3.846   1.00 9.18  ? 410  ARG A N   1 
ATOM   3188 C  CA  . ARG A 1 410  ? 17.025 61.831  4.291   1.00 9.42  ? 410  ARG A CA  1 
ATOM   3189 C  C   . ARG A 1 410  ? 16.224 62.466  3.166   1.00 9.99  ? 410  ARG A C   1 
ATOM   3190 O  O   . ARG A 1 410  ? 16.785 63.220  2.300   1.00 10.38 ? 410  ARG A O   1 
ATOM   3191 C  CB  . ARG A 1 410  ? 16.865 62.679  5.553   1.00 11.53 ? 410  ARG A CB  1 
ATOM   3192 C  CG  . ARG A 1 410  ? 17.246 64.142  5.386   1.00 13.47 ? 410  ARG A CG  1 
ATOM   3193 C  CD  . ARG A 1 410  ? 17.076 64.773  6.769   1.00 22.81 ? 410  ARG A CD  1 
ATOM   3194 N  NE  . ARG A 1 410  ? 17.821 66.000  7.010   1.00 26.18 ? 410  ARG A NE  1 
ATOM   3195 C  CZ  . ARG A 1 410  ? 17.378 67.223  6.778   1.00 32.06 ? 410  ARG A CZ  1 
ATOM   3196 N  NH1 . ARG A 1 410  ? 16.150 67.411  6.263   1.00 31.30 ? 410  ARG A NH1 1 
ATOM   3197 N  NH2 . ARG A 1 410  ? 18.165 68.253  7.102   1.00 25.06 ? 410  ARG A NH2 1 
ATOM   3198 N  N   . SER A 1 411  ? 14.945 62.111  3.095   1.00 10.99 ? 411  SER A N   1 
ATOM   3199 C  CA  . SER A 1 411  ? 13.984 62.726  2.168   1.00 10.22 ? 411  SER A CA  1 
ATOM   3200 C  C   . SER A 1 411  ? 14.495 62.762  0.734   1.00 9.56  ? 411  SER A C   1 
ATOM   3201 O  O   . SER A 1 411  ? 14.934 61.749  0.203   1.00 11.40 ? 411  SER A O   1 
ATOM   3202 C  CB  A SER A 1 411  ? 13.359 63.936  2.668   0.50 19.03 ? 411  SER A CB  1 
ATOM   3203 C  CB  B SER A 1 411  ? 13.646 64.155  2.713   0.50 18.60 ? 411  SER A CB  1 
ATOM   3204 O  OG  A SER A 1 411  ? 14.308 64.946  2.893   0.50 25.20 ? 411  SER A OG  1 
ATOM   3205 O  OG  B SER A 1 411  ? 12.512 64.647  2.025   0.50 25.78 ? 411  SER A OG  1 
ATOM   3206 N  N   . ASP A 1 412  ? 14.455 63.951  0.141   1.00 10.01 ? 412  ASP A N   1 
ATOM   3207 C  CA  . ASP A 1 412  ? 14.931 64.176  -1.219  1.00 9.55  ? 412  ASP A CA  1 
ATOM   3208 C  C   . ASP A 1 412  ? 16.268 64.915  -1.212  1.00 8.49  ? 412  ASP A C   1 
ATOM   3209 O  O   . ASP A 1 412  ? 16.639 65.540  -2.188  1.00 9.68  ? 412  ASP A O   1 
ATOM   3210 C  CB  . ASP A 1 412  ? 13.883 64.965  -2.026  1.00 11.28 ? 412  ASP A CB  1 
ATOM   3211 C  CG  . ASP A 1 412  ? 13.707 66.388  -1.524  1.00 10.53 ? 412  ASP A CG  1 
ATOM   3212 O  OD1 . ASP A 1 412  ? 14.188 66.707  -0.427  1.00 11.25 ? 412  ASP A OD1 1 
ATOM   3213 O  OD2 . ASP A 1 412  ? 13.078 67.188  -2.237  1.00 13.67 ? 412  ASP A OD2 1 
ATOM   3214 N  N   . ASN A 1 413  ? 16.971 64.852  -0.088  1.00 8.70  ? 413  ASN A N   1 
ATOM   3215 C  CA  . ASN A 1 413  ? 18.226 65.617  0.075   1.00 8.43  ? 413  ASN A CA  1 
ATOM   3216 C  C   . ASN A 1 413  ? 19.381 64.755  -0.481  1.00 7.50  ? 413  ASN A C   1 
ATOM   3217 O  O   . ASN A 1 413  ? 20.077 64.051  0.307   1.00 8.11  ? 413  ASN A O   1 
ATOM   3218 C  CB  . ASN A 1 413  ? 18.475 65.913  1.540   1.00 8.80  ? 413  ASN A CB  1 
ATOM   3219 C  CG  . ASN A 1 413  ? 17.565 67.005  2.138   1.00 9.30  ? 413  ASN A CG  1 
ATOM   3220 O  OD1 . ASN A 1 413  ? 17.845 67.477  3.223   1.00 11.79 ? 413  ASN A OD1 1 
ATOM   3221 N  ND2 . ASN A 1 413  ? 16.488 67.393  1.459   1.00 10.31 ? 413  ASN A ND2 1 
ATOM   3222 N  N   . TYR A 1 414  ? 19.558 64.802  -1.798  1.00 7.66  ? 414  TYR A N   1 
ATOM   3223 C  CA  . TYR A 1 414  ? 20.649 64.073  -2.521  1.00 8.32  ? 414  TYR A CA  1 
ATOM   3224 C  C   . TYR A 1 414  ? 21.871 64.983  -2.579  1.00 7.83  ? 414  TYR A C   1 
ATOM   3225 O  O   . TYR A 1 414  ? 21.791 66.154  -2.927  1.00 8.37  ? 414  TYR A O   1 
ATOM   3226 C  CB  . TYR A 1 414  ? 20.186 63.735  -3.945  1.00 7.91  ? 414  TYR A CB  1 
ATOM   3227 C  CG  . TYR A 1 414  ? 19.181 62.597  -3.968  1.00 7.39  ? 414  TYR A CG  1 
ATOM   3228 C  CD1 . TYR A 1 414  ? 17.816 62.851  -3.734  1.00 9.00  ? 414  TYR A CD1 1 
ATOM   3229 C  CD2 . TYR A 1 414  ? 19.601 61.275  -4.166  1.00 7.98  ? 414  TYR A CD2 1 
ATOM   3230 C  CE1 . TYR A 1 414  ? 16.904 61.760  -3.696  1.00 8.73  ? 414  TYR A CE1 1 
ATOM   3231 C  CE2 . TYR A 1 414  ? 18.712 60.188  -4.119  1.00 8.62  ? 414  TYR A CE2 1 
ATOM   3232 C  CZ  . TYR A 1 414  ? 17.373 60.466  -3.887  1.00 8.83  ? 414  TYR A CZ  1 
ATOM   3233 O  OH  . TYR A 1 414  ? 16.526 59.348  -3.852  1.00 8.95  ? 414  TYR A OH  1 
ATOM   3234 N  N   . TRP A 1 415  ? 22.998 64.349  -2.274  1.00 6.98  ? 415  TRP A N   1 
ATOM   3235 C  CA  . TRP A 1 415  ? 24.259 65.067  -2.167  1.00 7.09  ? 415  TRP A CA  1 
ATOM   3236 C  C   . TRP A 1 415  ? 24.992 65.125  -3.505  1.00 7.10  ? 415  TRP A C   1 
ATOM   3237 O  O   . TRP A 1 415  ? 26.111 64.654  -3.605  1.00 10.16 ? 415  TRP A O   1 
ATOM   3238 C  CB  . TRP A 1 415  ? 25.118 64.414  -1.074  1.00 7.52  ? 415  TRP A CB  1 
ATOM   3239 C  CG  . TRP A 1 415  ? 24.542 64.507  0.310   1.00 7.46  ? 415  TRP A CG  1 
ATOM   3240 C  CD1 . TRP A 1 415  ? 23.212 64.255  0.716   1.00 7.12  ? 415  TRP A CD1 1 
ATOM   3241 C  CD2 . TRP A 1 415  ? 25.278 64.742  1.496   1.00 7.42  ? 415  TRP A CD2 1 
ATOM   3242 N  NE1 . TRP A 1 415  ? 23.131 64.343  2.086   1.00 7.32  ? 415  TRP A NE1 1 
ATOM   3243 C  CE2 . TRP A 1 415  ? 24.378 64.630  2.584   1.00 8.27  ? 415  TRP A CE2 1 
ATOM   3244 C  CE3 . TRP A 1 415  ? 26.638 65.022  1.768   1.00 8.29  ? 415  TRP A CE3 1 
ATOM   3245 C  CZ2 . TRP A 1 415  ? 24.789 64.780  3.934   1.00 9.22  ? 415  TRP A CZ2 1 
ATOM   3246 C  CZ3 . TRP A 1 415  ? 27.053 65.175  3.086   1.00 8.56  ? 415  TRP A CZ3 1 
ATOM   3247 C  CH2 . TRP A 1 415  ? 26.136 65.047  4.157   1.00 9.34  ? 415  TRP A CH2 1 
ATOM   3248 N  N   . SER A 1 416  ? 24.364 65.666  -4.534  1.00 7.16  ? 416  SER A N   1 
ATOM   3249 C  CA  . SER A 1 416  ? 25.014 65.801  -5.815  1.00 7.46  ? 416  SER A CA  1 
ATOM   3250 C  C   . SER A 1 416  ? 25.601 67.217  -6.018  1.00 6.28  ? 416  SER A C   1 
ATOM   3251 O  O   . SER A 1 416  ? 26.282 67.425  -6.991  1.00 7.45  ? 416  SER A O   1 
ATOM   3252 C  CB  . SER A 1 416  ? 24.034 65.430  -6.945  1.00 6.82  ? 416  SER A CB  1 
ATOM   3253 O  OG  . SER A 1 416  ? 22.746 65.989  -6.754  1.00 8.27  ? 416  SER A OG  1 
ATOM   3254 N  N   . GLY A 1 417  ? 25.368 68.141  -5.098  1.00 5.84  ? 417  GLY A N   1 
ATOM   3255 C  CA  . GLY A 1 417  ? 25.949 69.492  -5.250  1.00 7.17  ? 417  GLY A CA  1 
ATOM   3256 C  C   . GLY A 1 417  ? 27.475 69.480  -5.164  1.00 5.85  ? 417  GLY A C   1 
ATOM   3257 O  O   . GLY A 1 417  ? 28.159 70.205  -5.906  1.00 6.47  ? 417  GLY A O   1 
ATOM   3258 N  N   . TYR A 1 418  ? 28.019 68.647  -4.268  1.00 6.12  ? 418  TYR A N   1 
ATOM   3259 C  CA  . TYR A 1 418  ? 29.479 68.665  -4.064  1.00 5.03  ? 418  TYR A CA  1 
ATOM   3260 C  C   . TYR A 1 418  ? 30.242 68.054  -5.250  1.00 5.66  ? 418  TYR A C   1 
ATOM   3261 O  O   . TYR A 1 418  ? 31.476 68.058  -5.281  1.00 6.28  ? 418  TYR A O   1 
ATOM   3262 C  CB  . TYR A 1 418  ? 29.856 67.972  -2.728  1.00 5.91  ? 418  TYR A CB  1 
ATOM   3263 C  CG  . TYR A 1 418  ? 29.976 66.450  -2.785  1.00 6.05  ? 418  TYR A CG  1 
ATOM   3264 C  CD1 . TYR A 1 418  ? 28.866 65.638  -2.657  1.00 7.27  ? 418  TYR A CD1 1 
ATOM   3265 C  CD2 . TYR A 1 418  ? 31.240 65.857  -2.941  1.00 5.94  ? 418  TYR A CD2 1 
ATOM   3266 C  CE1 . TYR A 1 418  ? 28.969 64.215  -2.671  1.00 6.41  ? 418  TYR A CE1 1 
ATOM   3267 C  CE2 . TYR A 1 418  ? 31.366 64.473  -2.952  1.00 6.35  ? 418  TYR A CE2 1 
ATOM   3268 C  CZ  . TYR A 1 418  ? 30.223 63.695  -2.819  1.00 5.68  ? 418  TYR A CZ  1 
ATOM   3269 O  OH  . TYR A 1 418  ? 30.409 62.322  -2.793  1.00 6.99  ? 418  TYR A OH  1 
ATOM   3270 N  N   . TYR A 1 419  ? 29.531 67.463  -6.227  1.00 5.94  ? 419  TYR A N   1 
ATOM   3271 C  CA  . TYR A 1 419  ? 30.214 67.015  -7.450  1.00 5.97  ? 419  TYR A CA  1 
ATOM   3272 C  C   . TYR A 1 419  ? 30.739 68.233  -8.244  1.00 6.07  ? 419  TYR A C   1 
ATOM   3273 O  O   . TYR A 1 419  ? 31.567 68.059  -9.109  1.00 6.18  ? 419  TYR A O   1 
ATOM   3274 C  CB  . TYR A 1 419  ? 29.279 66.216  -8.339  1.00 5.60  ? 419  TYR A CB  1 
ATOM   3275 C  CG  . TYR A 1 419  ? 28.628 65.032  -7.698  1.00 5.29  ? 419  TYR A CG  1 
ATOM   3276 C  CD1 . TYR A 1 419  ? 29.209 64.349  -6.599  1.00 5.54  ? 419  TYR A CD1 1 
ATOM   3277 C  CD2 . TYR A 1 419  ? 27.450 64.529  -8.260  1.00 5.61  ? 419  TYR A CD2 1 
ATOM   3278 C  CE1 . TYR A 1 419  ? 28.631 63.183  -6.080  1.00 6.13  ? 419  TYR A CE1 1 
ATOM   3279 C  CE2 . TYR A 1 419  ? 26.845 63.374  -7.734  1.00 5.69  ? 419  TYR A CE2 1 
ATOM   3280 C  CZ  . TYR A 1 419  ? 27.473 62.716  -6.644  1.00 6.53  ? 419  TYR A CZ  1 
ATOM   3281 O  OH  . TYR A 1 419  ? 26.889 61.547  -6.115  1.00 7.12  ? 419  TYR A OH  1 
ATOM   3282 N  N   . THR A 1 420  ? 30.273 69.438  -7.916  1.00 5.64  ? 420  THR A N   1 
ATOM   3283 C  CA  . THR A 1 420  ? 30.647 70.671  -8.621  1.00 6.02  ? 420  THR A CA  1 
ATOM   3284 C  C   . THR A 1 420  ? 31.169 71.765  -7.720  1.00 6.79  ? 420  THR A C   1 
ATOM   3285 O  O   . THR A 1 420  ? 31.953 72.595  -8.198  1.00 7.38  ? 420  THR A O   1 
ATOM   3286 C  CB  . THR A 1 420  ? 29.402 71.190  -9.404  1.00 5.99  ? 420  THR A CB  1 
ATOM   3287 O  OG1 . THR A 1 420  ? 28.970 70.137  -10.270 1.00 6.81  ? 420  THR A OG1 1 
ATOM   3288 C  CG2 . THR A 1 420  ? 29.729 72.433  -10.317 1.00 9.56  ? 420  THR A CG2 1 
ATOM   3289 N  N   . SER A 1 421  ? 30.803 71.791  -6.430  1.00 5.88  ? 421  SER A N   1 
ATOM   3290 C  CA  . SER A 1 421  ? 31.183 72.911  -5.565  1.00 5.69  ? 421  SER A CA  1 
ATOM   3291 C  C   . SER A 1 421  ? 32.665 73.248  -5.598  1.00 5.86  ? 421  SER A C   1 
ATOM   3292 O  O   . SER A 1 421  ? 33.528 72.355  -5.543  1.00 6.67  ? 421  SER A O   1 
ATOM   3293 C  CB  . SER A 1 421  ? 30.814 72.565  -4.119  1.00 5.88  ? 421  SER A CB  1 
ATOM   3294 O  OG  . SER A 1 421  ? 29.423 72.439  -4.029  1.00 7.00  ? 421  SER A OG  1 
ATOM   3295 N  N   . ARG A 1 422  ? 32.979 74.537  -5.623  1.00 5.84  ? 422  ARG A N   1 
ATOM   3296 C  CA  . ARG A 1 422  ? 34.371 75.016  -5.711  1.00 5.83  ? 422  ARG A CA  1 
ATOM   3297 C  C   . ARG A 1 422  ? 35.126 74.388  -6.904  1.00 6.46  ? 422  ARG A C   1 
ATOM   3298 O  O   . ARG A 1 422  ? 36.117 73.692  -6.747  1.00 6.15  ? 422  ARG A O   1 
ATOM   3299 C  CB  . ARG A 1 422  ? 35.115 74.822  -4.376  1.00 7.52  ? 422  ARG A CB  1 
ATOM   3300 C  CG  . ARG A 1 422  ? 34.875 75.933  -3.357  1.00 8.12  ? 422  ARG A CG  1 
ATOM   3301 C  CD  . ARG A 1 422  ? 33.436 76.027  -2.815  1.00 7.59  ? 422  ARG A CD  1 
ATOM   3302 N  NE  . ARG A 1 422  ? 33.459 76.999  -1.721  1.00 8.24  ? 422  ARG A NE  1 
ATOM   3303 C  CZ  . ARG A 1 422  ? 33.526 76.679  -0.437  1.00 8.17  ? 422  ARG A CZ  1 
ATOM   3304 N  NH1 . ARG A 1 422  ? 33.486 75.425  -0.035  1.00 8.51  ? 422  ARG A NH1 1 
ATOM   3305 N  NH2 . ARG A 1 422  ? 33.637 77.630  0.457   1.00 9.01  ? 422  ARG A NH2 1 
ATOM   3306 N  N   . PRO A 1 423  ? 34.622 74.610  -8.104  1.00 5.63  ? 423  PRO A N   1 
ATOM   3307 C  CA  . PRO A 1 423  ? 35.230 73.972  -9.276  1.00 5.65  ? 423  PRO A CA  1 
ATOM   3308 C  C   . PRO A 1 423  ? 36.634 74.433  -9.609  1.00 6.01  ? 423  PRO A C   1 
ATOM   3309 O  O   . PRO A 1 423  ? 37.355 73.705  -10.280 1.00 6.57  ? 423  PRO A O   1 
ATOM   3310 C  CB  . PRO A 1 423  ? 34.184 74.232  -10.388 1.00 7.27  ? 423  PRO A CB  1 
ATOM   3311 C  CG  . PRO A 1 423  ? 33.635 75.608  -10.007 1.00 7.03  ? 423  PRO A CG  1 
ATOM   3312 C  CD  . PRO A 1 423  ? 33.468 75.465  -8.478  1.00 6.88  ? 423  PRO A CD  1 
ATOM   3313 N  N   . TYR A 1 424  ? 37.029 75.636  -9.196  1.00 6.37  ? 424  TYR A N   1 
ATOM   3314 C  CA  . TYR A 1 424  ? 38.407 76.058  -9.478  1.00 6.54  ? 424  TYR A CA  1 
ATOM   3315 C  C   . TYR A 1 424  ? 39.374 75.035  -8.864  1.00 6.47  ? 424  TYR A C   1 
ATOM   3316 O  O   . TYR A 1 424  ? 40.371 74.675  -9.489  1.00 6.69  ? 424  TYR A O   1 
ATOM   3317 C  CB  . TYR A 1 424  ? 38.655 77.454  -8.828  1.00 6.56  ? 424  TYR A CB  1 
ATOM   3318 C  CG  . TYR A 1 424  ? 40.027 77.972  -9.059  1.00 6.62  ? 424  TYR A CG  1 
ATOM   3319 C  CD1 . TYR A 1 424  ? 40.280 78.744  -10.180 1.00 9.04  ? 424  TYR A CD1 1 
ATOM   3320 C  CD2 . TYR A 1 424  ? 41.062 77.716  -8.180  1.00 7.67  ? 424  TYR A CD2 1 
ATOM   3321 C  CE1 . TYR A 1 424  ? 41.533 79.251  -10.433 1.00 9.53  ? 424  TYR A CE1 1 
ATOM   3322 C  CE2 . TYR A 1 424  ? 42.361 78.228  -8.463  1.00 10.24 ? 424  TYR A CE2 1 
ATOM   3323 C  CZ  . TYR A 1 424  ? 42.564 79.002  -9.606  1.00 8.34  ? 424  TYR A CZ  1 
ATOM   3324 O  OH  . TYR A 1 424  ? 43.801 79.573  -9.923  1.00 11.96 ? 424  TYR A OH  1 
ATOM   3325 N  N   . HIS A 1 425  ? 39.106 74.613  -7.638  1.00 6.47  ? 425  HIS A N   1 
ATOM   3326 C  CA  . HIS A 1 425  ? 40.023 73.726  -6.910  1.00 5.45  ? 425  HIS A CA  1 
ATOM   3327 C  C   . HIS A 1 425  ? 39.910 72.291  -7.371  1.00 6.29  ? 425  HIS A C   1 
ATOM   3328 O  O   . HIS A 1 425  ? 40.868 71.544  -7.310  1.00 5.56  ? 425  HIS A O   1 
ATOM   3329 C  CB  . HIS A 1 425  ? 39.808 73.891  -5.410  1.00 7.06  ? 425  HIS A CB  1 
ATOM   3330 C  CG  . HIS A 1 425  ? 39.867 75.320  -4.993  1.00 8.16  ? 425  HIS A CG  1 
ATOM   3331 N  ND1 . HIS A 1 425  ? 38.765 76.146  -5.009  1.00 11.64 ? 425  HIS A ND1 1 
ATOM   3332 C  CD2 . HIS A 1 425  ? 40.920 76.098  -4.664  1.00 6.49  ? 425  HIS A CD2 1 
ATOM   3333 C  CE1 . HIS A 1 425  ? 39.134 77.365  -4.659  1.00 7.50  ? 425  HIS A CE1 1 
ATOM   3334 N  NE2 . HIS A 1 425  ? 40.433 77.358  -4.436  1.00 12.23 ? 425  HIS A NE2 1 
ATOM   3335 N  N   . LYS A 1 426  ? 38.734 71.923  -7.880  1.00 5.32  ? 426  LYS A N   1 
ATOM   3336 C  CA  . LYS A 1 426  ? 38.581 70.610  -8.502  1.00 6.37  ? 426  LYS A CA  1 
ATOM   3337 C  C   . LYS A 1 426  ? 39.488 70.547  -9.756  1.00 5.41  ? 426  LYS A C   1 
ATOM   3338 O  O   . LYS A 1 426  ? 40.094 69.500  -10.028 1.00 6.08  ? 426  LYS A O   1 
ATOM   3339 C  CB  . LYS A 1 426  ? 37.103 70.425  -8.891  1.00 6.03  ? 426  LYS A CB  1 
ATOM   3340 C  CG  . LYS A 1 426  ? 36.215 70.029  -7.720  1.00 5.76  ? 426  LYS A CG  1 
ATOM   3341 C  CD  . LYS A 1 426  ? 34.716 70.063  -8.068  1.00 7.30  ? 426  LYS A CD  1 
ATOM   3342 C  CE  . LYS A 1 426  ? 33.816 69.151  -7.189  1.00 5.71  ? 426  LYS A CE  1 
ATOM   3343 N  NZ  . LYS A 1 426  ? 33.838 69.612  -5.734  1.00 6.73  ? 426  LYS A NZ  1 
ATOM   3344 N  N   . ARG A 1 427  ? 39.524 71.607  -10.547 1.00 5.31  ? 427  ARG A N   1 
ATOM   3345 C  CA  . ARG A 1 427  ? 40.395 71.634  -11.710 1.00 5.43  ? 427  ARG A CA  1 
ATOM   3346 C  C   . ARG A 1 427  ? 41.860 71.686  -11.276 1.00 6.10  ? 427  ARG A C   1 
ATOM   3347 O  O   . ARG A 1 427  ? 42.683 70.994  -11.843 1.00 6.17  ? 427  ARG A O   1 
ATOM   3348 C  CB  . ARG A 1 427  ? 40.016 72.818  -12.610 1.00 7.10  ? 427  ARG A CB  1 
ATOM   3349 C  CG  . ARG A 1 427  ? 41.015 73.138  -13.706 1.00 7.96  ? 427  ARG A CG  1 
ATOM   3350 C  CD  . ARG A 1 427  ? 41.152 72.028  -14.743 1.00 8.54  ? 427  ARG A CD  1 
ATOM   3351 N  NE  . ARG A 1 427  ? 42.170 72.419  -15.715 1.00 9.74  ? 427  ARG A NE  1 
ATOM   3352 C  CZ  . ARG A 1 427  ? 42.996 71.593  -16.339 1.00 9.10  ? 427  ARG A CZ  1 
ATOM   3353 N  NH1 . ARG A 1 427  ? 42.943 70.289  -16.154 1.00 9.33  ? 427  ARG A NH1 1 
ATOM   3354 N  NH2 . ARG A 1 427  ? 43.889 72.101  -17.167 1.00 10.33 ? 427  ARG A NH2 1 
ATOM   3355 N  N   . MET A 1 428  ? 42.163 72.473  -10.244 1.00 5.64  ? 428  MET A N   1 
ATOM   3356 C  CA  . MET A 1 428  ? 43.538 72.536  -9.742  1.00 5.71  ? 428  MET A CA  1 
ATOM   3357 C  C   . MET A 1 428  ? 44.030 71.111  -9.320  1.00 5.11  ? 428  MET A C   1 
ATOM   3358 O  O   . MET A 1 428  ? 45.209 70.789  -9.509  1.00 5.87  ? 428  MET A O   1 
ATOM   3359 C  CB  . MET A 1 428  ? 43.613 73.509  -8.560  1.00 7.51  ? 428  MET A CB  1 
ATOM   3360 C  CG  . MET A 1 428  ? 45.048 73.885  -8.189  1.00 7.04  ? 428  MET A CG  1 
ATOM   3361 S  SD  . MET A 1 428  ? 44.960 75.189  -6.915  1.00 8.94  ? 428  MET A SD  1 
ATOM   3362 C  CE  . MET A 1 428  ? 46.701 75.683  -6.843  1.00 10.30 ? 428  MET A CE  1 
ATOM   3363 N  N   . ASP A 1 429  ? 43.151 70.324  -8.693  1.00 6.16  ? 429  ASP A N   1 
ATOM   3364 C  CA  . ASP A 1 429  ? 43.504 68.936  -8.318  1.00 5.55  ? 429  ASP A CA  1 
ATOM   3365 C  C   . ASP A 1 429  ? 44.082 68.139  -9.496  1.00 6.38  ? 429  ASP A C   1 
ATOM   3366 O  O   . ASP A 1 429  ? 45.076 67.441  -9.333  1.00 5.42  ? 429  ASP A O   1 
ATOM   3367 C  CB  . ASP A 1 429  ? 42.247 68.229  -7.784  1.00 7.12  ? 429  ASP A CB  1 
ATOM   3368 C  CG  . ASP A 1 429  ? 42.514 66.750  -7.478  1.00 6.82  ? 429  ASP A CG  1 
ATOM   3369 O  OD1 . ASP A 1 429  ? 43.030 66.528  -6.360  1.00 7.43  ? 429  ASP A OD1 1 
ATOM   3370 O  OD2 . ASP A 1 429  ? 42.215 65.877  -8.346  1.00 7.02  ? 429  ASP A OD2 1 
ATOM   3371 N  N   . ARG A 1 430  ? 43.434 68.238  -10.658 1.00 4.96  ? 430  ARG A N   1 
ATOM   3372 C  CA  . ARG A 1 430  ? 43.876 67.474  -11.811 1.00 5.60  ? 430  ARG A CA  1 
ATOM   3373 C  C   . ARG A 1 430  ? 45.186 68.008  -12.375 1.00 4.78  ? 430  ARG A C   1 
ATOM   3374 O  O   . ARG A 1 430  ? 46.026 67.206  -12.864 1.00 6.05  ? 430  ARG A O   1 
ATOM   3375 C  CB  . ARG A 1 430  ? 42.805 67.487  -12.900 1.00 5.14  ? 430  ARG A CB  1 
ATOM   3376 C  CG  . ARG A 1 430  ? 41.544 66.777  -12.500 1.00 6.80  ? 430  ARG A CG  1 
ATOM   3377 C  CD  . ARG A 1 430  ? 41.795 65.303  -12.032 1.00 5.80  ? 430  ARG A CD  1 
ATOM   3378 N  NE  . ARG A 1 430  ? 40.557 64.547  -12.041 1.00 6.83  ? 430  ARG A NE  1 
ATOM   3379 C  CZ  . ARG A 1 430  ? 39.833 64.201  -10.967 1.00 5.45  ? 430  ARG A CZ  1 
ATOM   3380 N  NH1 . ARG A 1 430  ? 40.216 64.533  -9.746  1.00 6.29  ? 430  ARG A NH1 1 
ATOM   3381 N  NH2 . ARG A 1 430  ? 38.714 63.521  -11.132 1.00 6.62  ? 430  ARG A NH2 1 
ATOM   3382 N  N   . VAL A 1 431  ? 45.387 69.325  -12.313 1.00 5.18  ? 431  VAL A N   1 
ATOM   3383 C  CA  . VAL A 1 431  ? 46.664 69.915  -12.787 1.00 5.44  ? 431  VAL A CA  1 
ATOM   3384 C  C   . VAL A 1 431  ? 47.792 69.391  -11.844 1.00 6.46  ? 431  VAL A C   1 
ATOM   3385 O  O   . VAL A 1 431  ? 48.822 68.901  -12.314 1.00 5.78  ? 431  VAL A O   1 
ATOM   3386 C  CB  . VAL A 1 431  ? 46.533 71.430  -12.752 1.00 5.20  ? 431  VAL A CB  1 
ATOM   3387 C  CG1 . VAL A 1 431  ? 47.899 72.047  -13.085 1.00 7.16  ? 431  VAL A CG1 1 
ATOM   3388 C  CG2 . VAL A 1 431  ? 45.508 71.868  -13.813 1.00 6.72  ? 431  VAL A CG2 1 
ATOM   3389 N  N   . LEU A 1 432  ? 47.599 69.514  -10.529 1.00 5.45  ? 432  LEU A N   1 
ATOM   3390 C  CA  . LEU A 1 432  ? 48.639 69.065  -9.596  1.00 5.75  ? 432  LEU A CA  1 
ATOM   3391 C  C   . LEU A 1 432  ? 48.828 67.546  -9.691  1.00 5.27  ? 432  LEU A C   1 
ATOM   3392 O  O   . LEU A 1 432  ? 49.968 67.070  -9.573  1.00 6.07  ? 432  LEU A O   1 
ATOM   3393 C  CB  . LEU A 1 432  ? 48.307 69.540  -8.191  1.00 6.74  ? 432  LEU A CB  1 
ATOM   3394 C  CG  . LEU A 1 432  ? 49.309 69.147  -7.092  1.00 6.66  ? 432  LEU A CG  1 
ATOM   3395 C  CD1 . LEU A 1 432  ? 50.729 69.662  -7.402  1.00 6.74  ? 432  LEU A CD1 1 
ATOM   3396 C  CD2 . LEU A 1 432  ? 48.821 69.748  -5.776  1.00 7.40  ? 432  LEU A CD2 1 
ATOM   3397 N  N   . MET A 1 433  ? 47.750 66.777  -9.931  1.00 4.78  ? 433  MET A N   1 
ATOM   3398 C  CA  . MET A 1 433  ? 47.921 65.326  -10.116 1.00 5.57  ? 433  MET A CA  1 
ATOM   3399 C  C   . MET A 1 433  ? 49.006 65.028  -11.144 1.00 5.63  ? 433  MET A C   1 
ATOM   3400 O  O   . MET A 1 433  ? 49.869 64.175  -10.986 1.00 5.47  ? 433  MET A O   1 
ATOM   3401 C  CB  . MET A 1 433  ? 46.577 64.729  -10.630 1.00 5.65  ? 433  MET A CB  1 
ATOM   3402 C  CG  . MET A 1 433  ? 46.669 63.235  -10.870 1.00 6.04  ? 433  MET A CG  1 
ATOM   3403 S  SD  . MET A 1 433  ? 45.099 62.570  -11.570 1.00 8.49  ? 433  MET A SD  1 
ATOM   3404 C  CE  . MET A 1 433  ? 45.122 63.232  -13.252 1.00 10.54 ? 433  MET A CE  1 
ATOM   3405 N  N   . HIS A 1 434  ? 48.867 65.698  -12.293 1.00 5.24  ? 434  HIS A N   1 
ATOM   3406 C  CA  . HIS A 1 434  ? 49.781 65.516  -13.420 1.00 5.55  ? 434  HIS A CA  1 
ATOM   3407 C  C   . HIS A 1 434  ? 51.177 66.030  -13.112 1.00 5.55  ? 434  HIS A C   1 
ATOM   3408 O  O   . HIS A 1 434  ? 52.122 65.372  -13.435 1.00 5.98  ? 434  HIS A O   1 
ATOM   3409 C  CB  . HIS A 1 434  ? 49.260 66.194  -14.683 1.00 7.13  ? 434  HIS A CB  1 
ATOM   3410 C  CG  . HIS A 1 434  ? 50.289 66.229  -15.766 1.00 5.55  ? 434  HIS A CG  1 
ATOM   3411 N  ND1 . HIS A 1 434  ? 50.661 65.101  -16.458 1.00 10.47 ? 434  HIS A ND1 1 
ATOM   3412 C  CD2 . HIS A 1 434  ? 51.099 67.224  -16.194 1.00 4.52  ? 434  HIS A CD2 1 
ATOM   3413 C  CE1 . HIS A 1 434  ? 51.626 65.415  -17.304 1.00 5.31  ? 434  HIS A CE1 1 
ATOM   3414 N  NE2 . HIS A 1 434  ? 51.916 66.693  -17.157 1.00 9.62  ? 434  HIS A NE2 1 
ATOM   3415 N  N   A TYR A 1 435  ? 51.277 67.189  -12.471 0.50 20.00 ? 435  TYR A N   1 
ATOM   3416 N  N   B TYR A 1 435  ? 51.274 67.179  -12.466 0.50 20.00 ? 435  TYR A N   1 
ATOM   3417 C  CA  A TYR A 1 435  ? 52.586 67.744  -12.134 0.50 20.00 ? 435  TYR A CA  1 
ATOM   3418 C  CA  B TYR A 1 435  ? 52.584 67.702  -12.144 0.50 20.00 ? 435  TYR A CA  1 
ATOM   3419 C  C   A TYR A 1 435  ? 53.338 66.852  -11.136 0.50 20.00 ? 435  TYR A C   1 
ATOM   3420 C  C   B TYR A 1 435  ? 53.341 66.863  -11.122 0.50 20.00 ? 435  TYR A C   1 
ATOM   3421 O  O   A TYR A 1 435  ? 54.551 66.734  -11.220 0.50 6.10  ? 435  TYR A O   1 
ATOM   3422 O  O   B TYR A 1 435  ? 54.555 66.751  -11.202 0.50 6.10  ? 435  TYR A O   1 
ATOM   3423 C  CB  A TYR A 1 435  ? 52.456 69.155  -11.552 0.50 20.00 ? 435  TYR A CB  1 
ATOM   3424 C  CB  B TYR A 1 435  ? 52.516 69.184  -11.802 0.50 20.00 ? 435  TYR A CB  1 
ATOM   3425 C  CG  A TYR A 1 435  ? 52.347 70.306  -12.532 0.50 20.00 ? 435  TYR A CG  1 
ATOM   3426 C  CG  B TYR A 1 435  ? 52.414 70.024  -13.060 0.50 20.00 ? 435  TYR A CG  1 
ATOM   3427 C  CD1 A TYR A 1 435  ? 51.326 70.362  -13.473 0.50 20.00 ? 435  TYR A CD1 1 
ATOM   3428 C  CD1 B TYR A 1 435  ? 53.415 69.989  -14.038 0.50 20.00 ? 435  TYR A CD1 1 
ATOM   3429 C  CD2 A TYR A 1 435  ? 53.210 71.388  -12.447 0.50 20.00 ? 435  TYR A CD2 1 
ATOM   3430 C  CD2 B TYR A 1 435  ? 51.293 70.782  -13.318 0.50 20.00 ? 435  TYR A CD2 1 
ATOM   3431 C  CE1 A TYR A 1 435  ? 51.204 71.430  -14.344 0.50 20.00 ? 435  TYR A CE1 1 
ATOM   3432 C  CE1 B TYR A 1 435  ? 53.308 70.743  -15.205 0.50 20.00 ? 435  TYR A CE1 1 
ATOM   3433 C  CE2 A TYR A 1 435  ? 53.098 72.459  -13.319 0.50 20.00 ? 435  TYR A CE2 1 
ATOM   3434 C  CE2 B TYR A 1 435  ? 51.185 71.543  -14.464 0.50 20.00 ? 435  TYR A CE2 1 
ATOM   3435 C  CZ  A TYR A 1 435  ? 52.090 72.473  -14.264 0.50 20.00 ? 435  TYR A CZ  1 
ATOM   3436 C  CZ  B TYR A 1 435  ? 52.193 71.523  -15.408 0.50 20.00 ? 435  TYR A CZ  1 
ATOM   3437 O  OH  A TYR A 1 435  ? 51.963 73.541  -15.128 0.50 20.00 ? 435  TYR A OH  1 
ATOM   3438 O  OH  B TYR A 1 435  ? 52.092 72.271  -16.563 0.50 20.00 ? 435  TYR A OH  1 
ATOM   3439 N  N   . VAL A 1 436  ? 52.626 66.240  -10.191 1.00 4.92  ? 436  VAL A N   1 
ATOM   3440 C  CA  . VAL A 1 436  ? 53.302 65.349  -9.260  1.00 5.59  ? 436  VAL A CA  1 
ATOM   3441 C  C   . VAL A 1 436  ? 53.805 64.111  -10.047 1.00 5.57  ? 436  VAL A C   1 
ATOM   3442 O  O   . VAL A 1 436  ? 54.967 63.658  -9.875  1.00 5.78  ? 436  VAL A O   1 
ATOM   3443 C  CB  . VAL A 1 436  ? 52.360 64.892  -8.131  1.00 5.99  ? 436  VAL A CB  1 
ATOM   3444 C  CG1 . VAL A 1 436  ? 52.878 63.659  -7.371  1.00 7.69  ? 436  VAL A CG1 1 
ATOM   3445 C  CG2 . VAL A 1 436  ? 52.182 66.050  -7.132  1.00 6.52  ? 436  VAL A CG2 1 
ATOM   3446 N  N   . ARG A 1 437  ? 52.953 63.543  -10.917 1.00 5.03  ? 437  ARG A N   1 
ATOM   3447 C  CA  . ARG A 1 437  ? 53.422 62.388  -11.671 1.00 6.43  ? 437  ARG A CA  1 
ATOM   3448 C  C   . ARG A 1 437  ? 54.658 62.761  -12.511 1.00 6.37  ? 437  ARG A C   1 
ATOM   3449 O  O   . ARG A 1 437  ? 55.659 61.991  -12.584 1.00 6.15  ? 437  ARG A O   1 
ATOM   3450 C  CB  . ARG A 1 437  ? 52.322 61.889  -12.618 1.00 6.94  ? 437  ARG A CB  1 
ATOM   3451 C  CG  . ARG A 1 437  ? 52.844 60.880  -13.680 1.00 7.63  ? 437  ARG A CG  1 
ATOM   3452 C  CD  . ARG A 1 437  ? 51.671 60.417  -14.556 1.00 7.46  ? 437  ARG A CD  1 
ATOM   3453 N  NE  . ARG A 1 437  ? 52.231 59.699  -15.719 1.00 7.15  ? 437  ARG A NE  1 
ATOM   3454 C  CZ  . ARG A 1 437  ? 51.466 58.880  -16.446 1.00 6.90  ? 437  ARG A CZ  1 
ATOM   3455 N  NH1 . ARG A 1 437  ? 50.202 58.652  -16.138 1.00 8.13  ? 437  ARG A NH1 1 
ATOM   3456 N  NH2 . ARG A 1 437  ? 51.974 58.321  -17.556 1.00 7.91  ? 437  ARG A NH2 1 
ATOM   3457 N  N   . ALA A 1 438  ? 54.596 63.923  -13.218 1.00 5.44  ? 438  ALA A N   1 
ATOM   3458 C  CA  . ALA A 1 438  ? 55.721 64.282  -14.092 1.00 5.63  ? 438  ALA A CA  1 
ATOM   3459 C  C   . ALA A 1 438  ? 57.004 64.576  -13.303 1.00 5.69  ? 438  ALA A C   1 
ATOM   3460 O  O   . ALA A 1 438  ? 58.112 64.230  -13.739 1.00 6.26  ? 438  ALA A O   1 
ATOM   3461 C  CB  . ALA A 1 438  ? 55.323 65.508  -14.973 1.00 7.53  ? 438  ALA A CB  1 
ATOM   3462 N  N   . ALA A 1 439  ? 56.875 65.265  -12.139 1.00 6.37  ? 439  ALA A N   1 
ATOM   3463 C  CA  . ALA A 1 439  ? 58.039 65.530  -11.314 1.00 6.11  ? 439  ALA A CA  1 
ATOM   3464 C  C   . ALA A 1 439  ? 58.650 64.240  -10.776 1.00 5.66  ? 439  ALA A C   1 
ATOM   3465 O  O   . ALA A 1 439  ? 59.896 64.113  -10.753 1.00 6.35  ? 439  ALA A O   1 
ATOM   3466 C  CB  . ALA A 1 439  ? 57.680 66.471  -10.200 1.00 6.87  ? 439  ALA A CB  1 
ATOM   3467 N  N   . GLU A 1 440  ? 57.831 63.317  -10.293 1.00 5.79  ? 440  GLU A N   1 
ATOM   3468 C  CA  . GLU A 1 440  ? 58.401 62.075  -9.765  1.00 6.14  ? 440  GLU A CA  1 
ATOM   3469 C  C   . GLU A 1 440  ? 59.035 61.267  -10.915 1.00 5.67  ? 440  GLU A C   1 
ATOM   3470 O  O   . GLU A 1 440  ? 60.135 60.676  -10.708 1.00 6.49  ? 440  GLU A O   1 
ATOM   3471 C  CB  . GLU A 1 440  ? 57.328 61.236  -9.050  1.00 6.93  ? 440  GLU A CB  1 
ATOM   3472 C  CG  . GLU A 1 440  ? 56.775 61.889  -7.788  1.00 7.91  ? 440  GLU A CG  1 
ATOM   3473 C  CD  . GLU A 1 440  ? 56.110 60.878  -6.870  1.00 9.52  ? 440  GLU A CD  1 
ATOM   3474 O  OE1 . GLU A 1 440  ? 55.002 60.411  -7.161  1.00 10.92 ? 440  GLU A OE1 1 
ATOM   3475 O  OE2 . GLU A 1 440  ? 56.761 60.587  -5.848  1.00 11.17 ? 440  GLU A OE2 1 
ATOM   3476 N  N   . MET A 1 441  ? 58.436 61.245  -12.113 1.00 5.74  ? 441  MET A N   1 
ATOM   3477 C  CA  . MET A 1 441  ? 58.996 60.477  -13.205 1.00 5.71  ? 441  MET A CA  1 
ATOM   3478 C  C   . MET A 1 441  ? 60.301 61.082  -13.757 1.00 6.35  ? 441  MET A C   1 
ATOM   3479 O  O   . MET A 1 441  ? 61.311 60.385  -13.877 1.00 7.11  ? 441  MET A O   1 
ATOM   3480 C  CB  . MET A 1 441  ? 57.941 60.352  -14.305 1.00 6.66  ? 441  MET A CB  1 
ATOM   3481 C  CG  . MET A 1 441  ? 58.433 59.598  -15.533 1.00 6.31  ? 441  MET A CG  1 
ATOM   3482 S  SD  . MET A 1 441  ? 57.186 59.343  -16.814 1.00 7.14  ? 441  MET A SD  1 
ATOM   3483 C  CE  . MET A 1 441  ? 56.045 58.158  -15.972 1.00 8.89  ? 441  MET A CE  1 
ATOM   3484 N  N   . LEU A 1 442  ? 60.292 62.403  -13.993 1.00 6.16  ? 442  LEU A N   1 
ATOM   3485 C  CA  . LEU A 1 442  ? 61.484 63.068  -14.548 1.00 6.43  ? 442  LEU A CA  1 
ATOM   3486 C  C   . LEU A 1 442  ? 62.662 62.950  -13.640 1.00 7.01  ? 442  LEU A C   1 
ATOM   3487 O  O   . LEU A 1 442  ? 63.785 62.771  -14.133 1.00 7.69  ? 442  LEU A O   1 
ATOM   3488 C  CB  . LEU A 1 442  ? 61.191 64.562  -14.860 1.00 7.05  ? 442  LEU A CB  1 
ATOM   3489 C  CG  . LEU A 1 442  ? 60.528 64.764  -16.229 1.00 6.79  ? 442  LEU A CG  1 
ATOM   3490 C  CD1 . LEU A 1 442  ? 59.939 66.165  -16.283 1.00 8.29  ? 442  LEU A CD1 1 
ATOM   3491 C  CD2 . LEU A 1 442  ? 61.583 64.610  -17.353 1.00 9.95  ? 442  LEU A CD2 1 
ATOM   3492 N  N   . SER A 1 443  ? 62.433 63.024  -12.316 1.00 5.91  ? 443  SER A N   1 
ATOM   3493 C  CA  . SER A 1 443  ? 63.560 62.979  -11.385 1.00 6.95  ? 443  SER A CA  1 
ATOM   3494 C  C   . SER A 1 443  ? 63.949 61.554  -11.030 1.00 7.23  ? 443  SER A C   1 
ATOM   3495 O  O   . SER A 1 443  ? 65.056 61.369  -10.529 1.00 8.43  ? 443  SER A O   1 
ATOM   3496 C  CB  . SER A 1 443  ? 63.278 63.783  -10.139 1.00 6.74  ? 443  SER A CB  1 
ATOM   3497 O  OG  . SER A 1 443  ? 62.181 63.241  -9.387  1.00 8.04  ? 443  SER A OG  1 
ATOM   3498 N  N   . ALA A 1 444  ? 63.137 60.563  -11.337 1.00 6.56  ? 444  ALA A N   1 
ATOM   3499 C  CA  . ALA A 1 444  ? 63.448 59.175  -10.986 1.00 6.92  ? 444  ALA A CA  1 
ATOM   3500 C  C   . ALA A 1 444  ? 64.592 58.638  -11.803 1.00 7.62  ? 444  ALA A C   1 
ATOM   3501 O  O   . ALA A 1 444  ? 65.226 57.628  -11.371 1.00 8.50  ? 444  ALA A O   1 
ATOM   3502 C  CB  . ALA A 1 444  ? 62.229 58.259  -11.228 1.00 8.04  ? 444  ALA A CB  1 
ATOM   3503 N  N   . TRP A 1 445  ? 64.855 59.173  -12.988 1.00 7.96  ? 445  TRP A N   1 
ATOM   3504 C  CA  . TRP A 1 445  ? 65.892 58.601  -13.870 1.00 9.31  ? 445  TRP A CA  1 
ATOM   3505 C  C   . TRP A 1 445  ? 67.289 58.649  -13.264 1.00 9.48  ? 445  TRP A C   1 
ATOM   3506 O  O   . TRP A 1 445  ? 68.142 57.880  -13.629 1.00 11.33 ? 445  TRP A O   1 
ATOM   3507 C  CB  . TRP A 1 445  ? 65.893 59.353  -15.208 1.00 8.55  ? 445  TRP A CB  1 
ATOM   3508 C  CG  . TRP A 1 445  ? 64.618 59.196  -15.975 1.00 6.86  ? 445  TRP A CG  1 
ATOM   3509 C  CD1 . TRP A 1 445  ? 63.645 60.144  -16.116 1.00 7.96  ? 445  TRP A CD1 1 
ATOM   3510 C  CD2 . TRP A 1 445  ? 64.135 58.024  -16.655 1.00 6.28  ? 445  TRP A CD2 1 
ATOM   3511 N  NE1 . TRP A 1 445  ? 62.585 59.638  -16.831 1.00 7.30  ? 445  TRP A NE1 1 
ATOM   3512 C  CE2 . TRP A 1 445  ? 62.865 58.340  -17.177 1.00 6.17  ? 445  TRP A CE2 1 
ATOM   3513 C  CE3 . TRP A 1 445  ? 64.664 56.727  -16.891 1.00 7.46  ? 445  TRP A CE3 1 
ATOM   3514 C  CZ2 . TRP A 1 445  ? 62.115 57.427  -17.916 1.00 7.46  ? 445  TRP A CZ2 1 
ATOM   3515 C  CZ3 . TRP A 1 445  ? 63.933 55.819  -17.631 1.00 8.58  ? 445  TRP A CZ3 1 
ATOM   3516 C  CH2 . TRP A 1 445  ? 62.657 56.153  -18.141 1.00 8.51  ? 445  TRP A CH2 1 
ATOM   3517 N  N   . HIS A 1 446  ? 67.533 59.588  -12.376 1.00 9.41  ? 446  HIS A N   1 
ATOM   3518 C  CA  . HIS A 1 446  ? 68.823 59.746  -11.727 1.00 10.56 ? 446  HIS A CA  1 
ATOM   3519 C  C   . HIS A 1 446  ? 68.678 59.666  -10.236 1.00 9.90  ? 446  HIS A C   1 
ATOM   3520 O  O   . HIS A 1 446  ? 67.639 59.885  -9.646  1.00 10.08 ? 446  HIS A O   1 
ATOM   3521 C  CB  . HIS A 1 446  ? 69.416 61.138  -11.956 1.00 11.63 ? 446  HIS A CB  1 
ATOM   3522 C  CG  . HIS A 1 446  ? 69.848 61.402  -13.367 1.00 14.63 ? 446  HIS A CG  1 
ATOM   3523 N  ND1 . HIS A 1 446  ? 69.077 62.124  -14.261 1.00 16.48 ? 446  HIS A ND1 1 
ATOM   3524 C  CD2 . HIS A 1 446  ? 70.980 61.065  -14.031 1.00 19.38 ? 446  HIS A CD2 1 
ATOM   3525 C  CE1 . HIS A 1 446  ? 69.712 62.222  -15.412 1.00 22.91 ? 446  HIS A CE1 1 
ATOM   3526 N  NE2 . HIS A 1 446  ? 70.862 61.596  -15.305 1.00 19.16 ? 446  HIS A NE2 1 
ATOM   3527 N  N   . SER A 1 447  ? 69.820 59.401  -9.605  1.00 11.46 ? 447  SER A N   1 
ATOM   3528 C  CA  . SER A 1 447  ? 69.964 59.487  -8.167  1.00 10.10 ? 447  SER A CA  1 
ATOM   3529 C  C   . SER A 1 447  ? 70.430 60.963  -7.907  1.00 10.64 ? 447  SER A C   1 
ATOM   3530 O  O   . SER A 1 447  ? 71.295 61.493  -8.674  1.00 13.51 ? 447  SER A O   1 
ATOM   3531 C  CB  . SER A 1 447  ? 71.064 58.532  -7.778  1.00 17.62 ? 447  SER A CB  1 
ATOM   3532 O  OG  . SER A 1 447  ? 71.029 58.397  -6.412  1.00 21.06 ? 447  SER A OG  1 
ATOM   3533 N  N   . TRP A 1 448  ? 69.936 61.641  -6.893  1.00 9.65  ? 448  TRP A N   1 
ATOM   3534 C  CA  . TRP A 1 448  ? 70.292 63.035  -6.670  1.00 10.97 ? 448  TRP A CA  1 
ATOM   3535 C  C   . TRP A 1 448  ? 70.989 63.230  -5.349  1.00 11.98 ? 448  TRP A C   1 
ATOM   3536 O  O   . TRP A 1 448  ? 70.611 62.609  -4.355  1.00 13.41 ? 448  TRP A O   1 
ATOM   3537 C  CB  . TRP A 1 448  ? 69.030 63.923  -6.663  1.00 10.99 ? 448  TRP A CB  1 
ATOM   3538 C  CG  . TRP A 1 448  ? 68.356 63.956  -8.051  1.00 8.97  ? 448  TRP A CG  1 
ATOM   3539 C  CD1 . TRP A 1 448  ? 67.512 63.042  -8.553  1.00 10.01 ? 448  TRP A CD1 1 
ATOM   3540 C  CD2 . TRP A 1 448  ? 68.521 64.966  -9.060  1.00 8.79  ? 448  TRP A CD2 1 
ATOM   3541 N  NE1 . TRP A 1 448  ? 67.106 63.383  -9.825  1.00 9.46  ? 448  TRP A NE1 1 
ATOM   3542 C  CE2 . TRP A 1 448  ? 67.710 64.573  -10.158 1.00 8.33  ? 448  TRP A CE2 1 
ATOM   3543 C  CE3 . TRP A 1 448  ? 69.266 66.169  -9.142  1.00 10.96 ? 448  TRP A CE3 1 
ATOM   3544 C  CZ2 . TRP A 1 448  ? 67.602 65.345  -11.314 1.00 10.29 ? 448  TRP A CZ2 1 
ATOM   3545 C  CZ3 . TRP A 1 448  ? 69.154 66.936  -10.291 1.00 9.71  ? 448  TRP A CZ3 1 
ATOM   3546 C  CH2 . TRP A 1 448  ? 68.328 66.519  -11.356 1.00 10.08 ? 448  TRP A CH2 1 
ATOM   3547 N  N   . ASP A 1 449  ? 71.968 64.138  -5.329  1.00 13.51 ? 449  ASP A N   1 
ATOM   3548 C  CA  . ASP A 1 449  ? 72.624 64.481  -4.098  1.00 16.03 ? 449  ASP A CA  1 
ATOM   3549 C  C   . ASP A 1 449  ? 71.603 65.118  -3.166  1.00 16.26 ? 449  ASP A C   1 
ATOM   3550 O  O   . ASP A 1 449  ? 70.685 65.812  -3.616  1.00 14.79 ? 449  ASP A O   1 
ATOM   3551 C  CB  . ASP A 1 449  ? 73.755 65.475  -4.386  1.00 22.62 ? 449  ASP A CB  1 
ATOM   3552 C  CG  . ASP A 1 449  ? 74.547 65.812  -3.116  1.00 27.74 ? 449  ASP A CG  1 
ATOM   3553 O  OD1 . ASP A 1 449  ? 75.406 64.981  -2.702  1.00 35.46 ? 449  ASP A OD1 1 
ATOM   3554 O  OD2 . ASP A 1 449  ? 74.283 66.845  -2.498  1.00 27.69 ? 449  ASP A OD2 1 
ATOM   3555 N  N   . GLY A 1 450  ? 71.755 64.918  -1.856  1.00 15.17 ? 450  GLY A N   1 
ATOM   3556 C  CA  . GLY A 1 450  ? 70.803 65.519  -0.932  1.00 17.00 ? 450  GLY A CA  1 
ATOM   3557 C  C   . GLY A 1 450  ? 70.733 67.046  -1.023  1.00 16.94 ? 450  GLY A C   1 
ATOM   3558 O  O   . GLY A 1 450  ? 69.698 67.675  -0.684  1.00 17.18 ? 450  GLY A O   1 
ATOM   3559 N  N   . MET A 1 451  ? 71.808 67.688  -1.452  1.00 16.22 ? 451  MET A N   1 
ATOM   3560 C  CA  . MET A 1 451  ? 71.800 69.139  -1.554  1.00 17.85 ? 451  MET A CA  1 
ATOM   3561 C  C   . MET A 1 451  ? 70.843 69.653  -2.627  1.00 13.73 ? 451  MET A C   1 
ATOM   3562 O  O   . MET A 1 451  ? 70.512 70.827  -2.653  1.00 17.40 ? 451  MET A O   1 
ATOM   3563 C  CB  . MET A 1 451  ? 73.227 69.673  -1.845  1.00 24.64 ? 451  MET A CB  1 
ATOM   3564 C  CG  . MET A 1 451  ? 74.213 69.454  -0.690  1.00 34.04 ? 451  MET A CG  1 
ATOM   3565 S  SD  . MET A 1 451  ? 73.762 70.291  0.851   1.00 49.10 ? 451  MET A SD  1 
ATOM   3566 C  CE  . MET A 1 451  ? 72.892 69.060  1.848   1.00 39.89 ? 451  MET A CE  1 
ATOM   3567 N  N   . ALA A 1 452  ? 70.425 68.767  -3.535  1.00 12.94 ? 452  ALA A N   1 
ATOM   3568 C  CA  . ALA A 1 452  ? 69.486 69.159  -4.588  1.00 12.87 ? 452  ALA A CA  1 
ATOM   3569 C  C   . ALA A 1 452  ? 68.042 69.275  -4.054  1.00 12.74 ? 452  ALA A C   1 
ATOM   3570 O  O   . ALA A 1 452  ? 67.195 69.798  -4.768  1.00 13.69 ? 452  ALA A O   1 
ATOM   3571 C  CB  . ALA A 1 452  ? 69.526 68.185  -5.702  1.00 13.52 ? 452  ALA A CB  1 
ATOM   3572 N  N   . ARG A 1 453  ? 67.766 68.758  -2.846  1.00 11.35 ? 453  ARG A N   1 
ATOM   3573 C  CA  . ARG A 1 453  ? 66.450 68.870  -2.186  1.00 12.01 ? 453  ARG A CA  1 
ATOM   3574 C  C   . ARG A 1 453  ? 65.322 68.289  -3.051  1.00 10.92 ? 453  ARG A C   1 
ATOM   3575 O  O   . ARG A 1 453  ? 64.184 68.753  -2.960  1.00 12.60 ? 453  ARG A O   1 
ATOM   3576 C  CB  . ARG A 1 453  ? 66.140 70.330  -1.837  1.00 13.91 ? 453  ARG A CB  1 
ATOM   3577 C  CG  . ARG A 1 453  ? 67.244 70.933  -0.977  1.00 14.33 ? 453  ARG A CG  1 
ATOM   3578 C  CD  . ARG A 1 453  ? 67.088 72.442  -0.818  1.00 22.98 ? 453  ARG A CD  1 
ATOM   3579 N  NE  . ARG A 1 453  ? 65.933 72.706  0.016   1.00 20.54 ? 453  ARG A NE  1 
ATOM   3580 C  CZ  . ARG A 1 453  ? 65.430 73.920  0.233   1.00 28.13 ? 453  ARG A CZ  1 
ATOM   3581 N  NH1 . ARG A 1 453  ? 65.984 75.008  -0.335  1.00 24.30 ? 453  ARG A NH1 1 
ATOM   3582 N  NH2 . ARG A 1 453  ? 64.368 74.046  1.019   1.00 23.65 ? 453  ARG A NH2 1 
ATOM   3583 N  N   . ILE A 1 454  ? 65.608 67.260  -3.827  1.00 9.35  ? 454  ILE A N   1 
ATOM   3584 C  CA  . ILE A 1 454  ? 64.606 66.667  -4.699  1.00 9.11  ? 454  ILE A CA  1 
ATOM   3585 C  C   . ILE A 1 454  ? 63.601 65.907  -3.845  1.00 10.11 ? 454  ILE A C   1 
ATOM   3586 O  O   . ILE A 1 454  ? 62.380 66.113  -3.972  1.00 9.24  ? 454  ILE A O   1 
ATOM   3587 C  CB  . ILE A 1 454  ? 65.284 65.710  -5.705  1.00 9.19  ? 454  ILE A CB  1 
ATOM   3588 C  CG1 . ILE A 1 454  ? 66.219 66.510  -6.640  1.00 11.26 ? 454  ILE A CG1 1 
ATOM   3589 C  CG2 . ILE A 1 454  ? 64.227 64.899  -6.475  1.00 10.73 ? 454  ILE A CG2 1 
ATOM   3590 C  CD1 . ILE A 1 454  ? 65.559 67.560  -7.513  1.00 13.52 ? 454  ILE A CD1 1 
ATOM   3591 N  N   . GLU A 1 455  ? 64.054 65.035  -2.969  1.00 10.26 ? 455  GLU A N   1 
ATOM   3592 C  CA  . GLU A 1 455  ? 63.121 64.243  -2.134  1.00 9.49  ? 455  GLU A CA  1 
ATOM   3593 C  C   . GLU A 1 455  ? 62.316 65.193  -1.245  1.00 9.53  ? 455  GLU A C   1 
ATOM   3594 O  O   . GLU A 1 455  ? 61.106 64.937  -1.034  1.00 9.70  ? 455  GLU A O   1 
ATOM   3595 C  CB  . GLU A 1 455  ? 63.876 63.251  -1.224  1.00 13.02 ? 455  GLU A CB  1 
ATOM   3596 C  CG  . GLU A 1 455  ? 64.484 62.052  -1.932  1.00 13.39 ? 455  GLU A CG  1 
ATOM   3597 C  CD  . GLU A 1 455  ? 65.897 62.332  -2.536  1.00 13.09 ? 455  GLU A CD  1 
ATOM   3598 O  OE1 . GLU A 1 455  ? 66.396 63.499  -2.400  1.00 14.38 ? 455  GLU A OE1 1 
ATOM   3599 O  OE2 . GLU A 1 455  ? 66.447 61.373  -3.110  1.00 12.52 ? 455  GLU A OE2 1 
ATOM   3600 N  N   . GLU A 1 456  ? 62.889 66.260  -0.706  1.00 10.23 ? 456  GLU A N   1 
ATOM   3601 C  CA  . GLU A 1 456  ? 62.174 67.186  0.114   1.00 8.68  ? 456  GLU A CA  1 
ATOM   3602 C  C   . GLU A 1 456  ? 61.024 67.822  -0.668  1.00 9.48  ? 456  GLU A C   1 
ATOM   3603 O  O   . GLU A 1 456  ? 59.878 67.922  -0.196  1.00 9.34  ? 456  GLU A O   1 
ATOM   3604 C  CB  . GLU A 1 456  ? 63.163 68.298  0.550   1.00 12.40 ? 456  GLU A CB  1 
ATOM   3605 C  CG  . GLU A 1 456  ? 62.535 69.391  1.340   1.00 15.59 ? 456  GLU A CG  1 
ATOM   3606 C  CD  . GLU A 1 456  ? 63.458 70.591  1.566   1.00 21.92 ? 456  GLU A CD  1 
ATOM   3607 O  OE1 . GLU A 1 456  ? 64.683 70.457  1.319   1.00 20.68 ? 456  GLU A OE1 1 
ATOM   3608 O  OE2 . GLU A 1 456  ? 62.954 71.676  1.983   1.00 23.30 ? 456  GLU A OE2 1 
ATOM   3609 N  N   . ARG A 1 457  ? 61.312 68.312  -1.873  1.00 8.04  ? 457  ARG A N   1 
ATOM   3610 C  CA  . ARG A 1 457  ? 60.235 68.974  -2.638  1.00 8.50  ? 457  ARG A CA  1 
ATOM   3611 C  C   . ARG A 1 457  ? 59.140 67.997  -3.109  1.00 6.83  ? 457  ARG A C   1 
ATOM   3612 O  O   . ARG A 1 457  ? 57.970 68.359  -3.063  1.00 7.76  ? 457  ARG A O   1 
ATOM   3613 C  CB  . ARG A 1 457  ? 60.861 69.744  -3.843  1.00 8.12  ? 457  ARG A CB  1 
ATOM   3614 C  CG  . ARG A 1 457  ? 61.188 71.205  -3.583  1.00 11.22 ? 457  ARG A CG  1 
ATOM   3615 C  CD  . ARG A 1 457  ? 62.145 71.398  -2.475  1.00 14.29 ? 457  ARG A CD  1 
ATOM   3616 N  NE  . ARG A 1 457  ? 62.449 72.834  -2.216  1.00 14.98 ? 457  ARG A NE  1 
ATOM   3617 C  CZ  . ARG A 1 457  ? 63.376 73.571  -2.855  1.00 18.64 ? 457  ARG A CZ  1 
ATOM   3618 N  NH1 . ARG A 1 457  ? 64.137 73.062  -3.836  1.00 14.36 ? 457  ARG A NH1 1 
ATOM   3619 N  NH2 . ARG A 1 457  ? 63.546 74.855  -2.494  1.00 18.50 ? 457  ARG A NH2 1 
ATOM   3620 N  N   . LEU A 1 458  ? 59.536 66.779  -3.485  1.00 7.21  ? 458  LEU A N   1 
ATOM   3621 C  CA  . LEU A 1 458  ? 58.544 65.794  -3.900  1.00 7.85  ? 458  LEU A CA  1 
ATOM   3622 C  C   . LEU A 1 458  ? 57.692 65.382  -2.702  1.00 8.44  ? 458  LEU A C   1 
ATOM   3623 O  O   . LEU A 1 458  ? 56.467 65.182  -2.896  1.00 8.58  ? 458  LEU A O   1 
ATOM   3624 C  CB  . LEU A 1 458  ? 59.250 64.567  -4.490  1.00 8.41  ? 458  LEU A CB  1 
ATOM   3625 C  CG  . LEU A 1 458  ? 59.919 64.895  -5.875  1.00 7.38  ? 458  LEU A CG  1 
ATOM   3626 C  CD1 . LEU A 1 458  ? 60.647 63.657  -6.321  1.00 10.09 ? 458  LEU A CD1 1 
ATOM   3627 C  CD2 . LEU A 1 458  ? 58.864 65.290  -6.957  1.00 9.57  ? 458  LEU A CD2 1 
ATOM   3628 N  N   . GLU A 1 459  ? 58.281 65.244  -1.497  1.00 7.74  ? 459  GLU A N   1 
ATOM   3629 C  CA  . GLU A 1 459  ? 57.457 64.862  -0.352  1.00 7.72  ? 459  GLU A CA  1 
ATOM   3630 C  C   . GLU A 1 459  ? 56.451 65.981  -0.054  1.00 7.40  ? 459  GLU A C   1 
ATOM   3631 O  O   . GLU A 1 459  ? 55.265 65.697  0.203   1.00 7.90  ? 459  GLU A O   1 
ATOM   3632 C  CB  . GLU A 1 459  ? 58.345 64.598  0.847   1.00 9.78  ? 459  GLU A CB  1 
ATOM   3633 C  CG  . GLU A 1 459  ? 57.543 64.292  2.139   1.00 11.67 ? 459  GLU A CG  1 
ATOM   3634 C  CD  . GLU A 1 459  ? 58.425 63.637  3.200   1.00 16.34 ? 459  GLU A CD  1 
ATOM   3635 O  OE1 . GLU A 1 459  ? 59.058 64.400  3.952   1.00 21.90 ? 459  GLU A OE1 1 
ATOM   3636 O  OE2 . GLU A 1 459  ? 58.503 62.380  3.269   1.00 20.09 ? 459  GLU A OE2 1 
ATOM   3637 N  N   . GLN A 1 460  ? 56.876 67.230  -0.103  1.00 7.58  ? 460  GLN A N   1 
ATOM   3638 C  CA  . GLN A 1 460  ? 55.945 68.326  0.061   1.00 8.09  ? 460  GLN A CA  1 
ATOM   3639 C  C   . GLN A 1 460  ? 54.809 68.261  -0.952  1.00 7.32  ? 460  GLN A C   1 
ATOM   3640 O  O   . GLN A 1 460  ? 53.657 68.382  -0.574  1.00 8.61  ? 460  GLN A O   1 
ATOM   3641 C  CB  . GLN A 1 460  ? 56.699 69.654  -0.035  1.00 11.63 ? 460  GLN A CB  1 
ATOM   3642 C  CG  . GLN A 1 460  ? 55.814 70.857  0.028   1.00 15.47 ? 460  GLN A CG  1 
ATOM   3643 C  CD  . GLN A 1 460  ? 56.552 72.106  -0.347  1.00 21.72 ? 460  GLN A CD  1 
ATOM   3644 O  OE1 . GLN A 1 460  ? 57.572 72.053  -1.015  1.00 31.57 ? 460  GLN A OE1 1 
ATOM   3645 N  NE2 . GLN A 1 460  ? 56.050 73.227  0.085   1.00 24.80 ? 460  GLN A NE2 1 
ATOM   3646 N  N   . ALA A 1 461  ? 55.143 68.069  -2.224  1.00 6.87  ? 461  ALA A N   1 
ATOM   3647 C  CA  . ALA A 1 461  ? 54.097 68.065  -3.247  1.00 7.97  ? 461  ALA A CA  1 
ATOM   3648 C  C   . ALA A 1 461  ? 53.133 66.903  -3.050  1.00 7.24  ? 461  ALA A C   1 
ATOM   3649 O  O   . ALA A 1 461  ? 51.904 67.088  -3.148  1.00 7.54  ? 461  ALA A O   1 
ATOM   3650 C  CB  . ALA A 1 461  ? 54.756 68.002  -4.612  1.00 7.80  ? 461  ALA A CB  1 
ATOM   3651 N  N   . ARG A 1 462  ? 53.655 65.706  -2.756  1.00 6.88  ? 462  ARG A N   1 
ATOM   3652 C  CA  . ARG A 1 462  ? 52.771 64.565  -2.554  1.00 6.31  ? 462  ARG A CA  1 
ATOM   3653 C  C   . ARG A 1 462  ? 51.858 64.792  -1.360  1.00 7.09  ? 462  ARG A C   1 
ATOM   3654 O  O   . ARG A 1 462  ? 50.676 64.424  -1.408  1.00 7.00  ? 462  ARG A O   1 
ATOM   3655 C  CB  . ARG A 1 462  ? 53.547 63.254  -2.286  1.00 7.71  ? 462  ARG A CB  1 
ATOM   3656 C  CG  . ARG A 1 462  ? 54.317 62.702  -3.549  1.00 7.21  ? 462  ARG A CG  1 
ATOM   3657 C  CD  . ARG A 1 462  ? 54.767 61.268  -3.269  1.00 8.04  ? 462  ARG A CD  1 
ATOM   3658 N  NE  . ARG A 1 462  ? 55.657 61.178  -2.077  1.00 8.03  ? 462  ARG A NE  1 
ATOM   3659 C  CZ  . ARG A 1 462  ? 56.972 61.326  -2.167  1.00 10.09 ? 462  ARG A CZ  1 
ATOM   3660 N  NH1 . ARG A 1 462  ? 57.576 61.531  -3.340  1.00 9.04  ? 462  ARG A NH1 1 
ATOM   3661 N  NH2 . ARG A 1 462  ? 57.735 61.327  -1.073  1.00 11.80 ? 462  ARG A NH2 1 
ATOM   3662 N  N   . ARG A 1 463  ? 52.384 65.389  -0.282  1.00 6.81  ? 463  ARG A N   1 
ATOM   3663 C  CA  . ARG A 1 463  ? 51.558 65.532  0.916   1.00 6.12  ? 463  ARG A CA  1 
ATOM   3664 C  C   . ARG A 1 463  ? 50.501 66.606  0.744   1.00 7.21  ? 463  ARG A C   1 
ATOM   3665 O  O   . ARG A 1 463  ? 49.402 66.434  1.266   1.00 7.60  ? 463  ARG A O   1 
ATOM   3666 C  CB  . ARG A 1 463  ? 52.461 65.808  2.121   1.00 6.96  ? 463  ARG A CB  1 
ATOM   3667 C  CG  . ARG A 1 463  ? 53.119 64.511  2.552   1.00 8.45  ? 463  ARG A CG  1 
ATOM   3668 C  CD  . ARG A 1 463  ? 54.188 64.749  3.633   1.00 9.69  ? 463  ARG A CD  1 
ATOM   3669 N  NE  . ARG A 1 463  ? 54.688 63.400  3.960   1.00 11.43 ? 463  ARG A NE  1 
ATOM   3670 C  CZ  . ARG A 1 463  ? 55.463 63.129  5.019   1.00 14.38 ? 463  ARG A CZ  1 
ATOM   3671 N  NH1 . ARG A 1 463  ? 55.826 64.136  5.800   1.00 13.95 ? 463  ARG A NH1 1 
ATOM   3672 N  NH2 . ARG A 1 463  ? 55.778 61.867  5.287   1.00 15.53 ? 463  ARG A NH2 1 
ATOM   3673 N  N   . GLU A 1 464  ? 50.755 67.705  0.019   1.00 6.73  ? 464  GLU A N   1 
ATOM   3674 C  CA  . GLU A 1 464  ? 49.726 68.727  -0.167  1.00 7.40  ? 464  GLU A CA  1 
ATOM   3675 C  C   . GLU A 1 464  ? 48.626 68.201  -1.091  1.00 7.43  ? 464  GLU A C   1 
ATOM   3676 O  O   . GLU A 1 464  ? 47.450 68.448  -0.842  1.00 7.79  ? 464  GLU A O   1 
ATOM   3677 C  CB  . GLU A 1 464  ? 50.277 70.015  -0.776  1.00 9.60  ? 464  GLU A CB  1 
ATOM   3678 C  CG  . GLU A 1 464  ? 51.427 70.698  0.056   1.00 11.08 ? 464  GLU A CG  1 
ATOM   3679 C  CD  . GLU A 1 464  ? 51.121 71.136  1.458   1.00 16.91 ? 464  GLU A CD  1 
ATOM   3680 O  OE1 . GLU A 1 464  ? 50.133 70.757  2.079   1.00 15.33 ? 464  GLU A OE1 1 
ATOM   3681 O  OE2 . GLU A 1 464  ? 51.970 71.903  1.976   1.00 21.49 ? 464  GLU A OE2 1 
ATOM   3682 N  N   . LEU A 1 465  ? 49.008 67.464  -2.148  1.00 6.17  ? 465  LEU A N   1 
ATOM   3683 C  CA  . LEU A 1 465  ? 47.973 66.908  -3.039  1.00 6.12  ? 465  LEU A CA  1 
ATOM   3684 C  C   . LEU A 1 465  ? 47.181 65.817  -2.252  1.00 5.76  ? 465  LEU A C   1 
ATOM   3685 O  O   . LEU A 1 465  ? 45.959 65.723  -2.366  1.00 6.23  ? 465  LEU A O   1 
ATOM   3686 C  CB  . LEU A 1 465  ? 48.622 66.270  -4.284  1.00 7.05  ? 465  LEU A CB  1 
ATOM   3687 C  CG  . LEU A 1 465  ? 47.638 65.615  -5.273  1.00 6.62  ? 465  LEU A CG  1 
ATOM   3688 C  CD1 . LEU A 1 465  ? 46.560 66.590  -5.714  1.00 7.17  ? 465  LEU A CD1 1 
ATOM   3689 C  CD2 . LEU A 1 465  ? 48.450 65.053  -6.448  1.00 7.95  ? 465  LEU A CD2 1 
ATOM   3690 N  N   . SER A 1 466  ? 47.886 65.012  -1.449  1.00 5.71  ? 466  SER A N   1 
ATOM   3691 C  CA  . SER A 1 466  ? 47.213 63.975  -0.658  1.00 6.33  ? 466  SER A CA  1 
ATOM   3692 C  C   . SER A 1 466  ? 46.210 64.590  0.350   1.00 5.48  ? 466  SER A C   1 
ATOM   3693 O  O   . SER A 1 466  ? 45.089 64.084  0.484   1.00 5.81  ? 466  SER A O   1 
ATOM   3694 C  CB  . SER A 1 466  ? 48.228 63.142  0.093   1.00 6.09  ? 466  SER A CB  1 
ATOM   3695 O  OG  . SER A 1 466  ? 49.008 62.331  -0.752  1.00 6.72  ? 466  SER A OG  1 
ATOM   3696 N  N   . LEU A 1 467  ? 46.606 65.690  0.998   1.00 5.29  ? 467  LEU A N   1 
ATOM   3697 C  CA  . LEU A 1 467  ? 45.715 66.349  1.955   1.00 5.24  ? 467  LEU A CA  1 
ATOM   3698 C  C   . LEU A 1 467  ? 44.405 66.774  1.256   1.00 5.64  ? 467  LEU A C   1 
ATOM   3699 O  O   . LEU A 1 467  ? 43.323 66.676  1.826   1.00 5.82  ? 467  LEU A O   1 
ATOM   3700 C  CB  . LEU A 1 467  ? 46.456 67.575  2.524   1.00 6.37  ? 467  LEU A CB  1 
ATOM   3701 C  CG  . LEU A 1 467  ? 45.675 68.212  3.659   1.00 10.44 ? 467  LEU A CG  1 
ATOM   3702 C  CD1 . LEU A 1 467  ? 45.836 67.325  4.898   1.00 16.46 ? 467  LEU A CD1 1 
ATOM   3703 C  CD2 . LEU A 1 467  ? 46.310 69.616  3.946   1.00 12.56 ? 467  LEU A CD2 1 
ATOM   3704 N  N   . PHE A 1 468  ? 44.545 67.284  0.026   1.00 5.33  ? 468  PHE A N   1 
ATOM   3705 C  CA  . PHE A 1 468  ? 43.361 67.791  -0.682  1.00 6.00  ? 468  PHE A CA  1 
ATOM   3706 C  C   . PHE A 1 468  ? 42.373 66.687  -1.089  1.00 5.56  ? 468  PHE A C   1 
ATOM   3707 O  O   . PHE A 1 468  ? 41.210 67.004  -1.387  1.00 6.59  ? 468  PHE A O   1 
ATOM   3708 C  CB  . PHE A 1 468  ? 43.776 68.612  -1.923  1.00 6.47  ? 468  PHE A CB  1 
ATOM   3709 C  CG  . PHE A 1 468  ? 42.659 69.439  -2.472  1.00 5.05  ? 468  PHE A CG  1 
ATOM   3710 C  CD1 . PHE A 1 468  ? 42.044 70.398  -1.689  1.00 6.98  ? 468  PHE A CD1 1 
ATOM   3711 C  CD2 . PHE A 1 468  ? 42.215 69.233  -3.802  1.00 6.63  ? 468  PHE A CD2 1 
ATOM   3712 C  CE1 . PHE A 1 468  ? 41.001 71.145  -2.182  1.00 6.15  ? 468  PHE A CE1 1 
ATOM   3713 C  CE2 . PHE A 1 468  ? 41.141 70.013  -4.302  1.00 6.35  ? 468  PHE A CE2 1 
ATOM   3714 C  CZ  . PHE A 1 468  ? 40.555 70.954  -3.488  1.00 6.43  ? 468  PHE A CZ  1 
ATOM   3715 N  N   . GLN A 1 469  ? 42.769 65.425  -1.068  1.00 4.77  ? 469  GLN A N   1 
ATOM   3716 C  CA  . GLN A 1 469  ? 41.839 64.324  -1.316  1.00 5.53  ? 469  GLN A CA  1 
ATOM   3717 C  C   . GLN A 1 469  ? 40.826 64.144  -0.200  1.00 5.53  ? 469  GLN A C   1 
ATOM   3718 O  O   . GLN A 1 469  ? 39.895 63.395  -0.376  1.00 5.80  ? 469  GLN A O   1 
ATOM   3719 C  CB  . GLN A 1 469  ? 42.603 63.012  -1.523  1.00 5.27  ? 469  GLN A CB  1 
ATOM   3720 C  CG  . GLN A 1 469  ? 43.688 63.068  -2.627  1.00 5.36  ? 469  GLN A CG  1 
ATOM   3721 C  CD  . GLN A 1 469  ? 43.169 63.729  -3.892  1.00 6.10  ? 469  GLN A CD  1 
ATOM   3722 O  OE1 . GLN A 1 469  ? 42.189 63.282  -4.486  1.00 8.82  ? 469  GLN A OE1 1 
ATOM   3723 N  NE2 . GLN A 1 469  ? 43.824 64.786  -4.300  1.00 4.09  ? 469  GLN A NE2 1 
ATOM   3724 N  N   . HIS A 1 470  ? 41.028 64.793  0.931   1.00 5.29  ? 470  HIS A N   1 
ATOM   3725 C  CA  . HIS A 1 470  ? 40.106 64.747  2.062   1.00 4.85  ? 470  HIS A CA  1 
ATOM   3726 C  C   . HIS A 1 470  ? 38.688 65.056  1.595   1.00 5.68  ? 470  HIS A C   1 
ATOM   3727 O  O   . HIS A 1 470  ? 38.474 65.810  0.666   1.00 6.36  ? 470  HIS A O   1 
ATOM   3728 C  CB  . HIS A 1 470  ? 40.564 65.776  3.100   1.00 5.77  ? 470  HIS A CB  1 
ATOM   3729 C  CG  . HIS A 1 470  ? 39.581 66.023  4.197   1.00 5.34  ? 470  HIS A CG  1 
ATOM   3730 N  ND1 . HIS A 1 470  ? 38.978 65.011  4.907   1.00 9.13  ? 470  HIS A ND1 1 
ATOM   3731 C  CD2 . HIS A 1 470  ? 39.103 67.179  4.710   1.00 4.29  ? 470  HIS A CD2 1 
ATOM   3732 C  CE1 . HIS A 1 470  ? 38.157 65.533  5.797   1.00 5.27  ? 470  HIS A CE1 1 
ATOM   3733 N  NE2 . HIS A 1 470  ? 38.217 66.844  5.701   1.00 9.83  ? 470  HIS A NE2 1 
ATOM   3734 N  N   . HIS A 1 471  ? 37.733 64.454  2.290   1.00 5.97  ? 471  HIS A N   1 
ATOM   3735 C  CA  . HIS A 1 471  ? 36.300 64.600  1.938   1.00 6.19  ? 471  HIS A CA  1 
ATOM   3736 C  C   . HIS A 1 471  ? 35.715 65.981  2.260   1.00 6.02  ? 471  HIS A C   1 
ATOM   3737 O  O   . HIS A 1 471  ? 34.539 66.157  2.004   1.00 7.08  ? 471  HIS A O   1 
ATOM   3738 C  CB  . HIS A 1 471  ? 35.453 63.450  2.572   1.00 6.17  ? 471  HIS A CB  1 
ATOM   3739 C  CG  . HIS A 1 471  ? 35.528 63.384  4.085   1.00 5.25  ? 471  HIS A CG  1 
ATOM   3740 N  ND1 . HIS A 1 471  ? 36.471 62.635  4.776   1.00 5.96  ? 471  HIS A ND1 1 
ATOM   3741 C  CD2 . HIS A 1 471  ? 34.789 64.010  5.038   1.00 5.10  ? 471  HIS A CD2 1 
ATOM   3742 C  CE1 . HIS A 1 471  ? 36.306 62.812  6.097   1.00 5.48  ? 471  HIS A CE1 1 
ATOM   3743 N  NE2 . HIS A 1 471  ? 35.293 63.643  6.293   1.00 5.60  ? 471  HIS A NE2 1 
ATOM   3744 N  N   . ASP A 1 472  ? 36.545 66.941  2.721   1.00 6.47  ? 472  ASP A N   1 
ATOM   3745 C  CA  . ASP A 1 472  ? 36.129 68.361  2.722   1.00 6.12  ? 472  ASP A CA  1 
ATOM   3746 C  C   . ASP A 1 472  ? 37.088 69.199  1.872   1.00 6.56  ? 472  ASP A C   1 
ATOM   3747 O  O   . ASP A 1 472  ? 36.999 70.442  1.891   1.00 7.60  ? 472  ASP A O   1 
ATOM   3748 C  CB  . ASP A 1 472  ? 36.008 68.969  4.134   1.00 6.10  ? 472  ASP A CB  1 
ATOM   3749 C  CG  . ASP A 1 472  ? 34.952 68.248  4.942   1.00 6.81  ? 472  ASP A CG  1 
ATOM   3750 O  OD1 . ASP A 1 472  ? 33.785 68.243  4.480   1.00 6.67  ? 472  ASP A OD1 1 
ATOM   3751 O  OD2 . ASP A 1 472  ? 35.311 67.670  6.007   1.00 6.86  ? 472  ASP A OD2 1 
ATOM   3752 N  N   . GLY A 1 473  ? 38.005 68.565  1.135   1.00 6.15  ? 473  GLY A N   1 
ATOM   3753 C  CA  . GLY A 1 473  ? 38.964 69.274  0.287   1.00 6.90  ? 473  GLY A CA  1 
ATOM   3754 C  C   . GLY A 1 473  ? 38.413 69.375  -1.135  1.00 5.98  ? 473  GLY A C   1 
ATOM   3755 O  O   . GLY A 1 473  ? 37.698 70.311  -1.475  1.00 5.77  ? 473  GLY A O   1 
ATOM   3756 N  N   . ILE A 1 474  ? 38.734 68.363  -1.942  1.00 6.12  ? 474  ILE A N   1 
ATOM   3757 C  CA  . ILE A 1 474  ? 38.297 68.362  -3.335  1.00 5.79  ? 474  ILE A CA  1 
ATOM   3758 C  C   . ILE A 1 474  ? 36.793 68.463  -3.488  1.00 6.70  ? 474  ILE A C   1 
ATOM   3759 O  O   . ILE A 1 474  ? 36.287 68.958  -4.527  1.00 7.65  ? 474  ILE A O   1 
ATOM   3760 C  CB  . ILE A 1 474  ? 38.879 67.083  -4.045  1.00 5.54  ? 474  ILE A CB  1 
ATOM   3761 C  CG1 . ILE A 1 474  ? 38.615 67.149  -5.535  1.00 6.91  ? 474  ILE A CG1 1 
ATOM   3762 C  CG2 . ILE A 1 474  ? 38.336 65.770  -3.391  1.00 7.11  ? 474  ILE A CG2 1 
ATOM   3763 C  CD1 . ILE A 1 474  ? 39.380 66.016  -6.302  1.00 7.66  ? 474  ILE A CD1 1 
ATOM   3764 N  N   . THR A 1 475  ? 36.048 68.028  -2.473  1.00 5.52  ? 475  THR A N   1 
ATOM   3765 C  CA  . THR A 1 475  ? 34.574 68.105  -2.483  1.00 6.23  ? 475  THR A CA  1 
ATOM   3766 C  C   . THR A 1 475  ? 34.059 69.569  -2.494  1.00 5.46  ? 475  THR A C   1 
ATOM   3767 O  O   . THR A 1 475  ? 32.880 69.779  -2.812  1.00 5.96  ? 475  THR A O   1 
ATOM   3768 C  CB  . THR A 1 475  ? 34.024 67.463  -1.218  1.00 6.23  ? 475  THR A CB  1 
ATOM   3769 O  OG1 . THR A 1 475  ? 34.578 68.213  -0.112  1.00 6.55  ? 475  THR A OG1 1 
ATOM   3770 C  CG2 . THR A 1 475  ? 34.355 65.989  -1.123  1.00 7.41  ? 475  THR A CG2 1 
ATOM   3771 N  N   . GLY A 1 476  ? 34.878 70.562  -2.104  1.00 5.48  ? 476  GLY A N   1 
ATOM   3772 C  CA  . GLY A 1 476  ? 34.366 71.917  -2.084  1.00 6.07  ? 476  GLY A CA  1 
ATOM   3773 C  C   . GLY A 1 476  ? 33.384 72.168  -0.946  1.00 6.54  ? 476  GLY A C   1 
ATOM   3774 O  O   . GLY A 1 476  ? 32.515 73.004  -1.086  1.00 6.88  ? 476  GLY A O   1 
ATOM   3775 N  N   . THR A 1 477  ? 33.543 71.439  0.175   1.00 6.23  ? 477  THR A N   1 
ATOM   3776 C  CA  . THR A 1 477  ? 32.629 71.562  1.291   1.00 6.33  ? 477  THR A CA  1 
ATOM   3777 C  C   . THR A 1 477  ? 33.304 72.174  2.508   1.00 6.49  ? 477  THR A C   1 
ATOM   3778 O  O   . THR A 1 477  ? 32.747 72.041  3.639   1.00 9.15  ? 477  THR A O   1 
ATOM   3779 C  CB  . THR A 1 477  ? 31.972 70.208  1.650   1.00 6.19  ? 477  THR A CB  1 
ATOM   3780 O  OG1 . THR A 1 477  ? 32.988 69.219  1.930   1.00 7.25  ? 477  THR A OG1 1 
ATOM   3781 C  CG2 . THR A 1 477  ? 31.131 69.722  0.441   1.00 7.03  ? 477  THR A CG2 1 
ATOM   3782 N  N   . ALA A 1 478  ? 34.405 72.906  2.374   1.00 6.45  ? 478  ALA A N   1 
ATOM   3783 C  CA  . ALA A 1 478  ? 35.030 73.560  3.556   1.00 6.67  ? 478  ALA A CA  1 
ATOM   3784 C  C   . ALA A 1 478  ? 34.713 75.046  3.606   1.00 7.05  ? 478  ALA A C   1 
ATOM   3785 O  O   . ALA A 1 478  ? 34.213 75.691  2.664   1.00 7.86  ? 478  ALA A O   1 
ATOM   3786 C  CB  . ALA A 1 478  ? 36.559 73.339  3.502   1.00 8.18  ? 478  ALA A CB  1 
ATOM   3787 N  N   . LYS A 1 479  ? 34.961 75.658  4.764   1.00 6.88  ? 479  LYS A N   1 
ATOM   3788 C  CA  . LYS A 1 479  ? 34.753 77.121  4.892   1.00 7.71  ? 479  LYS A CA  1 
ATOM   3789 C  C   . LYS A 1 479  ? 35.709 77.827  3.949   1.00 7.46  ? 479  LYS A C   1 
ATOM   3790 O  O   . LYS A 1 479  ? 36.803 77.338  3.623   1.00 7.37  ? 479  LYS A O   1 
ATOM   3791 C  CB  . LYS A 1 479  ? 35.015 77.586  6.328   1.00 9.02  ? 479  LYS A CB  1 
ATOM   3792 C  CG  . LYS A 1 479  ? 33.766 77.246  7.216   1.00 12.63 ? 479  LYS A CG  1 
ATOM   3793 C  CD  . LYS A 1 479  ? 33.791 78.074  8.519   1.00 18.71 ? 479  LYS A CD  1 
ATOM   3794 C  CE  . LYS A 1 479  ? 32.513 77.944  9.350   1.00 16.69 ? 479  LYS A CE  1 
ATOM   3795 N  NZ  . LYS A 1 479  ? 31.242 78.531  8.778   1.00 17.13 ? 479  LYS A NZ  1 
ATOM   3796 N  N   . THR A 1 480  ? 35.356 79.067  3.592   1.00 8.65  ? 480  THR A N   1 
ATOM   3797 C  CA  . THR A 1 480  ? 36.178 79.830  2.664   1.00 8.45  ? 480  THR A CA  1 
ATOM   3798 C  C   . THR A 1 480  ? 37.644 79.957  3.064   1.00 7.71  ? 480  THR A C   1 
ATOM   3799 O  O   . THR A 1 480  ? 38.532 79.766  2.248   1.00 9.44  ? 480  THR A O   1 
ATOM   3800 C  CB  . THR A 1 480  ? 35.604 81.237  2.488   1.00 11.21 ? 480  THR A CB  1 
ATOM   3801 O  OG1 . THR A 1 480  ? 34.282 81.117  1.966   1.00 14.17 ? 480  THR A OG1 1 
ATOM   3802 C  CG2 . THR A 1 480  ? 36.462 82.117  1.523   1.00 13.88 ? 480  THR A CG2 1 
ATOM   3803 N  N   . HIS A 1 481  ? 37.948 80.239  4.353   1.00 8.75  ? 481  HIS A N   1 
ATOM   3804 C  CA  . HIS A 1 481  ? 39.362 80.376  4.703   1.00 9.01  ? 481  HIS A CA  1 
ATOM   3805 C  C   . HIS A 1 481  ? 40.122 79.063  4.647   1.00 8.35  ? 481  HIS A C   1 
ATOM   3806 O  O   . HIS A 1 481  ? 41.321 79.057  4.472   1.00 9.52  ? 481  HIS A O   1 
ATOM   3807 C  CB  . HIS A 1 481  ? 39.571 81.076  6.080   1.00 12.47 ? 481  HIS A CB  1 
ATOM   3808 C  CG  . HIS A 1 481  ? 39.442 80.188  7.283   1.00 11.62 ? 481  HIS A CG  1 
ATOM   3809 N  ND1 . HIS A 1 481  ? 38.233 79.681  7.736   1.00 14.30 ? 481  HIS A ND1 1 
ATOM   3810 C  CD2 . HIS A 1 481  ? 40.393 79.707  8.121   1.00 10.56 ? 481  HIS A CD2 1 
ATOM   3811 C  CE1 . HIS A 1 481  ? 38.461 78.938  8.813   1.00 13.75 ? 481  HIS A CE1 1 
ATOM   3812 N  NE2 . HIS A 1 481  ? 39.766 78.939  9.058   1.00 11.89 ? 481  HIS A NE2 1 
ATOM   3813 N  N   . VAL A 1 482  ? 39.401 77.941  4.750   1.00 8.23  ? 482  VAL A N   1 
ATOM   3814 C  CA  . VAL A 1 482  ? 40.019 76.606  4.644   1.00 8.25  ? 482  VAL A CA  1 
ATOM   3815 C  C   . VAL A 1 482  ? 40.292 76.287  3.172   1.00 6.07  ? 482  VAL A C   1 
ATOM   3816 O  O   . VAL A 1 482  ? 41.353 75.778  2.849   1.00 7.50  ? 482  VAL A O   1 
ATOM   3817 C  CB  . VAL A 1 482  ? 39.063 75.582  5.305   1.00 6.30  ? 482  VAL A CB  1 
ATOM   3818 C  CG1 . VAL A 1 482  ? 39.739 74.173  5.250   1.00 7.34  ? 482  VAL A CG1 1 
ATOM   3819 C  CG2 . VAL A 1 482  ? 38.867 75.916  6.818   1.00 8.06  ? 482  VAL A CG2 1 
ATOM   3820 N  N   . VAL A 1 483  ? 39.350 76.612  2.296   1.00 6.77  ? 483  VAL A N   1 
ATOM   3821 C  CA  . VAL A 1 483  ? 39.596 76.484  0.879   1.00 7.11  ? 483  VAL A CA  1 
ATOM   3822 C  C   . VAL A 1 483  ? 40.838 77.284  0.476   1.00 6.76  ? 483  VAL A C   1 
ATOM   3823 O  O   . VAL A 1 483  ? 41.683 76.786  -0.297  1.00 7.79  ? 483  VAL A O   1 
ATOM   3824 C  CB  . VAL A 1 483  ? 38.364 76.992  0.044   1.00 7.19  ? 483  VAL A CB  1 
ATOM   3825 C  CG1 . VAL A 1 483  ? 38.662 76.979  -1.460  1.00 9.58  ? 483  VAL A CG1 1 
ATOM   3826 C  CG2 . VAL A 1 483  ? 37.135 76.087  0.345   1.00 9.25  ? 483  VAL A CG2 1 
ATOM   3827 N  N   . VAL A 1 484  ? 40.984 78.507  1.027   1.00 8.38  ? 484  VAL A N   1 
ATOM   3828 C  CA  . VAL A 1 484  ? 42.177 79.292  0.719   1.00 9.49  ? 484  VAL A CA  1 
ATOM   3829 C  C   . VAL A 1 484  ? 43.448 78.589  1.193   1.00 9.82  ? 484  VAL A C   1 
ATOM   3830 O  O   . VAL A 1 484  ? 44.460 78.579  0.451   1.00 9.08  ? 484  VAL A O   1 
ATOM   3831 C  CB  . VAL A 1 484  ? 42.046 80.704  1.314   1.00 10.41 ? 484  VAL A CB  1 
ATOM   3832 C  CG1 . VAL A 1 484  ? 43.424 81.433  1.234   1.00 13.22 ? 484  VAL A CG1 1 
ATOM   3833 C  CG2 . VAL A 1 484  ? 40.935 81.469  0.577   1.00 14.05 ? 484  VAL A CG2 1 
ATOM   3834 N  N   . ASP A 1 485  ? 43.406 77.960  2.367   1.00 8.30  ? 485  ASP A N   1 
ATOM   3835 C  CA  . ASP A 1 485  ? 44.568 77.230  2.824   1.00 7.40  ? 485  ASP A CA  1 
ATOM   3836 C  C   . ASP A 1 485  ? 44.919 76.072  1.882   1.00 7.74  ? 485  ASP A C   1 
ATOM   3837 O  O   . ASP A 1 485  ? 46.098 75.854  1.588   1.00 7.55  ? 485  ASP A O   1 
ATOM   3838 C  CB  . ASP A 1 485  ? 44.311 76.700  4.269   1.00 8.99  ? 485  ASP A CB  1 
ATOM   3839 C  CG  . ASP A 1 485  ? 45.550 76.070  4.889   1.00 9.52  ? 485  ASP A CG  1 
ATOM   3840 O  OD1 . ASP A 1 485  ? 46.565 76.794  4.988   1.00 14.12 ? 485  ASP A OD1 1 
ATOM   3841 O  OD2 . ASP A 1 485  ? 45.525 74.912  5.256   1.00 10.13 ? 485  ASP A OD2 1 
ATOM   3842 N  N   . TYR A 1 486  ? 43.917 75.301  1.465   1.00 7.25  ? 486  TYR A N   1 
ATOM   3843 C  CA  . TYR A 1 486  ? 44.200 74.208  0.518   1.00 6.44  ? 486  TYR A CA  1 
ATOM   3844 C  C   . TYR A 1 486  ? 44.782 74.770  -0.778  1.00 7.49  ? 486  TYR A C   1 
ATOM   3845 O  O   . TYR A 1 486  ? 45.699 74.147  -1.340  1.00 7.68  ? 486  TYR A O   1 
ATOM   3846 C  CB  . TYR A 1 486  ? 42.937 73.416  0.155   1.00 7.64  ? 486  TYR A CB  1 
ATOM   3847 C  CG  . TYR A 1 486  ? 42.332 72.560  1.283   1.00 7.07  ? 486  TYR A CG  1 
ATOM   3848 C  CD1 . TYR A 1 486  ? 43.139 71.688  2.055   1.00 10.01 ? 486  TYR A CD1 1 
ATOM   3849 C  CD2 . TYR A 1 486  ? 40.970 72.600  1.503   1.00 7.12  ? 486  TYR A CD2 1 
ATOM   3850 C  CE1 . TYR A 1 486  ? 42.528 70.873  3.046   1.00 8.94  ? 486  TYR A CE1 1 
ATOM   3851 C  CE2 . TYR A 1 486  ? 40.343 71.780  2.489   1.00 7.62  ? 486  TYR A CE2 1 
ATOM   3852 C  CZ  . TYR A 1 486  ? 41.144 70.959  3.217   1.00 8.01  ? 486  TYR A CZ  1 
ATOM   3853 O  OH  . TYR A 1 486  ? 40.528 70.140  4.178   1.00 9.33  ? 486  TYR A OH  1 
ATOM   3854 N  N   . GLU A 1 487  ? 44.252 75.908  -1.262  1.00 7.01  ? 487  GLU A N   1 
ATOM   3855 C  CA  . GLU A 1 487  ? 44.751 76.473  -2.508  1.00 8.23  ? 487  GLU A CA  1 
ATOM   3856 C  C   . GLU A 1 487  ? 46.231 76.887  -2.347  1.00 9.05  ? 487  GLU A C   1 
ATOM   3857 O  O   . GLU A 1 487  ? 47.070 76.624  -3.232  1.00 8.91  ? 487  GLU A O   1 
ATOM   3858 C  CB  . GLU A 1 487  ? 43.903 77.682  -2.910  1.00 8.61  ? 487  GLU A CB  1 
ATOM   3859 C  CG  . GLU A 1 487  ? 44.292 78.205  -4.306  1.00 10.08 ? 487  GLU A CG  1 
ATOM   3860 C  CD  . GLU A 1 487  ? 43.440 79.366  -4.773  1.00 16.70 ? 487  GLU A CD  1 
ATOM   3861 O  OE1 . GLU A 1 487  ? 42.317 79.549  -4.297  1.00 16.65 ? 487  GLU A OE1 1 
ATOM   3862 O  OE2 . GLU A 1 487  ? 43.947 80.118  -5.644  1.00 18.84 ? 487  GLU A OE2 1 
ATOM   3863 N  N   . GLN A 1 488  ? 46.535 77.541  -1.237  1.00 8.01  ? 488  GLN A N   1 
ATOM   3864 C  CA  . GLN A 1 488  ? 47.917 77.970  -0.946  1.00 8.40  ? 488  GLN A CA  1 
ATOM   3865 C  C   . GLN A 1 488  ? 48.859 76.777  -0.903  1.00 8.15  ? 488  GLN A C   1 
ATOM   3866 O  O   . GLN A 1 488  ? 49.927 76.825  -1.476  1.00 9.24  ? 488  GLN A O   1 
ATOM   3867 C  CB  . GLN A 1 488  ? 47.991 78.704  0.398   1.00 11.70 ? 488  GLN A CB  1 
ATOM   3868 C  CG  . GLN A 1 488  ? 47.356 80.069  0.436   1.00 23.14 ? 488  GLN A CG  1 
ATOM   3869 C  CD  . GLN A 1 488  ? 47.483 80.721  1.808   1.00 29.84 ? 488  GLN A CD  1 
ATOM   3870 O  OE1 . GLN A 1 488  ? 47.712 80.050  2.815   1.00 41.29 ? 488  GLN A OE1 1 
ATOM   3871 N  NE2 . GLN A 1 488  ? 47.316 82.031  1.848   1.00 37.06 ? 488  GLN A NE2 1 
ATOM   3872 N  N   . ARG A 1 489  ? 48.446 75.704  -0.234  1.00 6.71  ? 489  ARG A N   1 
ATOM   3873 C  CA  . ARG A 1 489  ? 49.260 74.495  -0.135  1.00 7.79  ? 489  ARG A CA  1 
ATOM   3874 C  C   . ARG A 1 489  ? 49.469 73.897  -1.528  1.00 7.74  ? 489  ARG A C   1 
ATOM   3875 O  O   . ARG A 1 489  ? 50.584 73.502  -1.880  1.00 7.13  ? 489  ARG A O   1 
ATOM   3876 C  CB  . ARG A 1 489  ? 48.547 73.495  0.787   1.00 7.30  ? 489  ARG A CB  1 
ATOM   3877 C  CG  . ARG A 1 489  ? 48.651 73.896  2.222   1.00 8.44  ? 489  ARG A CG  1 
ATOM   3878 C  CD  . ARG A 1 489  ? 47.676 72.977  3.024   1.00 10.80 ? 489  ARG A CD  1 
ATOM   3879 N  NE  . ARG A 1 489  ? 47.753 73.140  4.498   1.00 10.03 ? 489  ARG A NE  1 
ATOM   3880 C  CZ  . ARG A 1 489  ? 48.624 72.494  5.268   1.00 12.05 ? 489  ARG A CZ  1 
ATOM   3881 N  NH1 . ARG A 1 489  ? 49.509 71.639  4.780   1.00 13.53 ? 489  ARG A NH1 1 
ATOM   3882 N  NH2 . ARG A 1 489  ? 48.601 72.709  6.590   1.00 12.14 ? 489  ARG A NH2 1 
ATOM   3883 N  N   . MET A 1 490  ? 48.411 73.829  -2.353  1.00 7.60  ? 490  MET A N   1 
ATOM   3884 C  CA  . MET A 1 490  ? 48.588 73.292  -3.693  1.00 7.16  ? 490  MET A CA  1 
ATOM   3885 C  C   . MET A 1 490  ? 49.469 74.187  -4.580  1.00 7.42  ? 490  MET A C   1 
ATOM   3886 O  O   . MET A 1 490  ? 50.199 73.674  -5.428  1.00 7.96  ? 490  MET A O   1 
ATOM   3887 C  CB  . MET A 1 490  ? 47.242 73.013  -4.390  1.00 7.90  ? 490  MET A CB  1 
ATOM   3888 C  CG  . MET A 1 490  ? 46.529 71.837  -3.701  1.00 8.55  ? 490  MET A CG  1 
ATOM   3889 S  SD  . MET A 1 490  ? 45.175 71.147  -4.810  1.00 11.20 ? 490  MET A SD  1 
ATOM   3890 C  CE  . MET A 1 490  ? 43.882 72.365  -4.456  1.00 13.23 ? 490  MET A CE  1 
ATOM   3891 N  N   . GLN A 1 491  ? 49.409 75.504  -4.401  1.00 7.09  ? 491  GLN A N   1 
ATOM   3892 C  CA  . GLN A 1 491  ? 50.290 76.397  -5.170  1.00 7.90  ? 491  GLN A CA  1 
ATOM   3893 C  C   . GLN A 1 491  ? 51.747 76.142  -4.817  1.00 8.10  ? 491  GLN A C   1 
ATOM   3894 O  O   . GLN A 1 491  ? 52.625 76.079  -5.690  1.00 9.13  ? 491  GLN A O   1 
ATOM   3895 C  CB  . GLN A 1 491  ? 49.959 77.865  -4.859  1.00 10.56 ? 491  GLN A CB  1 
ATOM   3896 C  CG  . GLN A 1 491  ? 50.784 78.779  -5.774  1.00 17.24 ? 491  GLN A CG  1 
ATOM   3897 C  CD  . GLN A 1 491  ? 50.568 78.486  -7.264  1.00 28.37 ? 491  GLN A CD  1 
ATOM   3898 O  OE1 . GLN A 1 491  ? 49.445 78.338  -7.696  1.00 32.73 ? 491  GLN A OE1 1 
ATOM   3899 N  NE2 . GLN A 1 491  ? 51.654 78.381  -8.038  1.00 35.86 ? 491  GLN A NE2 1 
ATOM   3900 N  N   . GLU A 1 492  ? 52.038 75.952  -3.527  1.00 8.04  ? 492  GLU A N   1 
ATOM   3901 C  CA  . GLU A 1 492  ? 53.405 75.630  -3.130  1.00 8.68  ? 492  GLU A CA  1 
ATOM   3902 C  C   . GLU A 1 492  ? 53.800 74.280  -3.715  1.00 8.61  ? 492  GLU A C   1 
ATOM   3903 O  O   . GLU A 1 492  ? 54.945 74.101  -4.143  1.00 9.60  ? 492  GLU A O   1 
ATOM   3904 C  CB  . GLU A 1 492  ? 53.520 75.565  -1.596  1.00 11.70 ? 492  GLU A CB  1 
ATOM   3905 C  CG  . GLU A 1 492  ? 53.445 76.984  -0.923  1.00 17.17 ? 492  GLU A CG  1 
ATOM   3906 C  CD  . GLU A 1 492  ? 54.425 78.010  -1.555  1.00 24.87 ? 492  GLU A CD  1 
ATOM   3907 O  OE1 . GLU A 1 492  ? 55.681 77.783  -1.548  1.00 28.14 ? 492  GLU A OE1 1 
ATOM   3908 O  OE2 . GLU A 1 492  ? 53.933 79.051  -2.066  1.00 28.14 ? 492  GLU A OE2 1 
ATOM   3909 N  N   . ALA A 1 493  ? 52.870 73.313  -3.728  1.00 7.60  ? 493  ALA A N   1 
ATOM   3910 C  CA  . ALA A 1 493  ? 53.182 72.018  -4.322  1.00 6.04  ? 493  ALA A CA  1 
ATOM   3911 C  C   . ALA A 1 493  ? 53.499 72.163  -5.828  1.00 6.97  ? 493  ALA A C   1 
ATOM   3912 O  O   . ALA A 1 493  ? 54.401 71.490  -6.338  1.00 6.96  ? 493  ALA A O   1 
ATOM   3913 C  CB  . ALA A 1 493  ? 51.998 71.077  -4.083  1.00 6.80  ? 493  ALA A CB  1 
ATOM   3914 N  N   . LEU A 1 494  ? 52.725 72.976  -6.564  1.00 6.42  ? 494  LEU A N   1 
ATOM   3915 C  CA  . LEU A 1 494  ? 53.016 73.181  -7.988  1.00 7.36  ? 494  LEU A CA  1 
ATOM   3916 C  C   . LEU A 1 494  ? 54.405 73.790  -8.158  1.00 7.41  ? 494  LEU A C   1 
ATOM   3917 O  O   . LEU A 1 494  ? 55.137 73.369  -9.076  1.00 8.06  ? 494  LEU A O   1 
ATOM   3918 C  CB  . LEU A 1 494  ? 51.953 74.097  -8.610  1.00 8.23  ? 494  LEU A CB  1 
ATOM   3919 C  CG  . LEU A 1 494  ? 50.602 73.428  -8.808  1.00 8.08  ? 494  LEU A CG  1 
ATOM   3920 C  CD1 . LEU A 1 494  ? 49.583 74.555  -9.142  1.00 10.10 ? 494  LEU A CD1 1 
ATOM   3921 C  CD2 . LEU A 1 494  ? 50.639 72.383  -9.929  1.00 9.24  ? 494  LEU A CD2 1 
ATOM   3922 N  N   . LYS A 1 495  ? 54.790 74.754  -7.322  1.00 7.93  ? 495  LYS A N   1 
ATOM   3923 C  CA  . LYS A 1 495  ? 56.145 75.362  -7.420  1.00 7.87  ? 495  LYS A CA  1 
ATOM   3924 C  C   . LYS A 1 495  ? 57.206 74.296  -7.121  1.00 8.14  ? 495  LYS A C   1 
ATOM   3925 O  O   . LYS A 1 495  ? 58.266 74.249  -7.795  1.00 7.92  ? 495  LYS A O   1 
ATOM   3926 C  CB  . LYS A 1 495  ? 56.288 76.523  -6.419  1.00 11.18 ? 495  LYS A CB  1 
ATOM   3927 C  CG  . LYS A 1 495  ? 55.429 77.702  -6.834  1.00 15.00 ? 495  LYS A CG  1 
ATOM   3928 C  CD  . LYS A 1 495  ? 55.600 78.931  -5.970  1.00 23.45 ? 495  LYS A CD  1 
ATOM   3929 C  CE  . LYS A 1 495  ? 55.254 78.733  -4.545  1.00 28.89 ? 495  LYS A CE  1 
ATOM   3930 N  NZ  . LYS A 1 495  ? 55.562 80.037  -3.795  1.00 35.29 ? 495  LYS A NZ  1 
ATOM   3931 N  N   . ALA A 1 496  ? 56.981 73.430  -6.147  1.00 6.35  ? 496  ALA A N   1 
ATOM   3932 C  CA  . ALA A 1 496  ? 57.907 72.330  -5.887  1.00 7.04  ? 496  ALA A CA  1 
ATOM   3933 C  C   . ALA A 1 496  ? 58.073 71.398  -7.082  1.00 6.92  ? 496  ALA A C   1 
ATOM   3934 O  O   . ALA A 1 496  ? 59.164 71.018  -7.421  1.00 7.19  ? 496  ALA A O   1 
ATOM   3935 C  CB  . ALA A 1 496  ? 57.446 71.539  -4.669  1.00 7.80  ? 496  ALA A CB  1 
ATOM   3936 N  N   . CYS A 1 497  ? 56.965 71.026  -7.711  1.00 5.94  ? 497  CYS A N   1 
ATOM   3937 C  CA  . CYS A 1 497  ? 56.997 70.164  -8.899  1.00 7.42  ? 497  CYS A CA  1 
ATOM   3938 C  C   . CYS A 1 497  ? 57.761 70.852  -10.037 1.00 7.12  ? 497  CYS A C   1 
ATOM   3939 O  O   . CYS A 1 497  ? 58.582 70.220  -10.693 1.00 6.89  ? 497  CYS A O   1 
ATOM   3940 C  CB  . CYS A 1 497  ? 55.577 69.832  -9.378  1.00 6.91  ? 497  CYS A CB  1 
ATOM   3941 S  SG  . CYS A 1 497  ? 54.711 68.685  -8.306  1.00 8.45  ? 497  CYS A SG  1 
ATOM   3942 N  N   . GLN A 1 498  ? 57.524 72.135  -10.249 1.00 6.59  ? 498  GLN A N   1 
ATOM   3943 C  CA  . GLN A 1 498  ? 58.230 72.866  -11.295 1.00 6.75  ? 498  GLN A CA  1 
ATOM   3944 C  C   . GLN A 1 498  ? 59.733 72.831  -11.048 1.00 7.06  ? 498  GLN A C   1 
ATOM   3945 O  O   . GLN A 1 498  ? 60.498 72.566  -11.969 1.00 8.17  ? 498  GLN A O   1 
ATOM   3946 C  CB  . GLN A 1 498  ? 57.756 74.317  -11.400 1.00 7.69  ? 498  GLN A CB  1 
ATOM   3947 C  CG  . GLN A 1 498  ? 58.593 75.111  -12.393 1.00 12.75 ? 498  GLN A CG  1 
ATOM   3948 C  CD  . GLN A 1 498  ? 58.136 76.533  -12.579 1.00 14.67 ? 498  GLN A CD  1 
ATOM   3949 O  OE1 . GLN A 1 498  ? 57.878 76.975  -13.694 1.00 18.66 ? 498  GLN A OE1 1 
ATOM   3950 N  NE2 . GLN A 1 498  ? 58.067 77.274  -11.483 1.00 13.61 ? 498  GLN A NE2 1 
ATOM   3951 N  N   . MET A 1 499  ? 60.150 73.094  -9.810  1.00 6.94  ? 499  MET A N   1 
ATOM   3952 C  CA  . MET A 1 499  ? 61.568 73.089  -9.516  1.00 8.31  ? 499  MET A CA  1 
ATOM   3953 C  C   . MET A 1 499  ? 62.200 71.753  -9.842  1.00 7.29  ? 499  MET A C   1 
ATOM   3954 O  O   . MET A 1 499  ? 63.244 71.672  -10.495 1.00 8.16  ? 499  MET A O   1 
ATOM   3955 C  CB  . MET A 1 499  ? 61.760 73.440  -8.032  1.00 8.90  ? 499  MET A CB  1 
ATOM   3956 C  CG  . MET A 1 499  ? 63.213 73.295  -7.504  1.00 11.52 ? 499  MET A CG  1 
ATOM   3957 S  SD  . MET A 1 499  ? 64.520 74.214  -8.381  1.00 16.37 ? 499  MET A SD  1 
ATOM   3958 C  CE  . MET A 1 499  ? 63.844 75.723  -7.867  1.00 15.04 ? 499  MET A CE  1 
ATOM   3959 N  N   . VAL A 1 500  ? 61.588 70.659  -9.383  1.00 7.10  ? 500  VAL A N   1 
ATOM   3960 C  CA  . VAL A 1 500  ? 62.131 69.341  -9.602  1.00 5.81  ? 500  VAL A CA  1 
ATOM   3961 C  C   . VAL A 1 500  ? 62.127 69.011  -11.089 1.00 6.76  ? 500  VAL A C   1 
ATOM   3962 O  O   . VAL A 1 500  ? 63.131 68.471  -11.614 1.00 6.90  ? 500  VAL A O   1 
ATOM   3963 C  CB  . VAL A 1 500  ? 61.316 68.297  -8.815  1.00 6.85  ? 500  VAL A CB  1 
ATOM   3964 C  CG1 . VAL A 1 500  ? 61.753 66.869  -9.222  1.00 7.79  ? 500  VAL A CG1 1 
ATOM   3965 C  CG2 . VAL A 1 500  ? 61.559 68.507  -7.298  1.00 8.21  ? 500  VAL A CG2 1 
ATOM   3966 N  N   . MET A 1 501  ? 61.032 69.305  -11.792 1.00 6.50  ? 501  MET A N   1 
ATOM   3967 C  CA  . MET A 1 501  ? 60.970 69.012  -13.226 1.00 7.13  ? 501  MET A CA  1 
ATOM   3968 C  C   . MET A 1 501  ? 62.066 69.760  -13.985 1.00 7.59  ? 501  MET A C   1 
ATOM   3969 O  O   . MET A 1 501  ? 62.711 69.143  -14.831 1.00 7.29  ? 501  MET A O   1 
ATOM   3970 C  CB  . MET A 1 501  ? 59.604 69.432  -13.773 1.00 7.32  ? 501  MET A CB  1 
ATOM   3971 C  CG  . MET A 1 501  ? 58.494 68.495  -13.276 1.00 7.66  ? 501  MET A CG  1 
ATOM   3972 S  SD  . MET A 1 501  ? 56.802 69.143  -13.535 1.00 12.49 ? 501  MET A SD  1 
ATOM   3973 C  CE  . MET A 1 501  ? 56.758 68.863  -15.238 1.00 14.05 ? 501  MET A CE  1 
ATOM   3974 N  N   . GLN A 1 502  ? 62.239 71.062  -13.733 1.00 7.60  ? 502  GLN A N   1 
ATOM   3975 C  CA  . GLN A 1 502  ? 63.201 71.824  -14.552 1.00 6.91  ? 502  GLN A CA  1 
ATOM   3976 C  C   . GLN A 1 502  ? 64.631 71.444  -14.222 1.00 9.09  ? 502  GLN A C   1 
ATOM   3977 O  O   . GLN A 1 502  ? 65.454 71.368  -15.149 1.00 8.37  ? 502  GLN A O   1 
ATOM   3978 C  CB  . GLN A 1 502  ? 62.919 73.320  -14.446 1.00 9.08  ? 502  GLN A CB  1 
ATOM   3979 C  CG  . GLN A 1 502  ? 63.135 73.937  -13.080 1.00 9.35  ? 502  GLN A CG  1 
ATOM   3980 C  CD  . GLN A 1 502  ? 64.560 74.443  -12.885 1.00 12.45 ? 502  GLN A CD  1 
ATOM   3981 O  OE1 . GLN A 1 502  ? 65.341 74.577  -13.861 1.00 10.91 ? 502  GLN A OE1 1 
ATOM   3982 N  NE2 . GLN A 1 502  ? 64.923 74.738  -11.638 1.00 11.83 ? 502  GLN A NE2 1 
ATOM   3983 N  N   . GLN A 1 503  ? 64.949 71.112  -12.959 1.00 7.18  ? 503  GLN A N   1 
ATOM   3984 C  CA  . GLN A 1 503  ? 66.300 70.610  -12.681 1.00 8.14  ? 503  GLN A CA  1 
ATOM   3985 C  C   . GLN A 1 503  ? 66.507 69.291  -13.415 1.00 8.14  ? 503  GLN A C   1 
ATOM   3986 O  O   . GLN A 1 503  ? 67.619 69.000  -13.930 1.00 8.47  ? 503  GLN A O   1 
ATOM   3987 C  CB  . GLN A 1 503  ? 66.507 70.347  -11.170 1.00 9.11  ? 503  GLN A CB  1 
ATOM   3988 C  CG  . GLN A 1 503  ? 66.611 71.632  -10.340 1.00 11.09 ? 503  GLN A CG  1 
ATOM   3989 C  CD  . GLN A 1 503  ? 67.991 72.299  -10.481 1.00 11.39 ? 503  GLN A CD  1 
ATOM   3990 O  OE1 . GLN A 1 503  ? 68.973 71.653  -10.796 1.00 13.42 ? 503  GLN A OE1 1 
ATOM   3991 N  NE2 . GLN A 1 503  ? 68.062 73.593  -10.196 1.00 13.01 ? 503  GLN A NE2 1 
ATOM   3992 N  N   . SER A 1 504  ? 65.467 68.439  -13.505 1.00 6.61  ? 504  SER A N   1 
ATOM   3993 C  CA  . SER A 1 504  ? 65.627 67.128  -14.131 1.00 6.83  ? 504  SER A CA  1 
ATOM   3994 C  C   . SER A 1 504  ? 65.819 67.265  -15.648 1.00 7.91  ? 504  SER A C   1 
ATOM   3995 O  O   . SER A 1 504  ? 66.655 66.552  -16.229 1.00 7.46  ? 504  SER A O   1 
ATOM   3996 C  CB  . SER A 1 504  ? 64.364 66.253  -13.869 1.00 7.70  ? 504  SER A CB  1 
ATOM   3997 O  OG  . SER A 1 504  ? 64.222 65.982  -12.461 1.00 8.31  ? 504  SER A OG  1 
ATOM   3998 N  N   . VAL A 1 505  ? 65.066 68.164  -16.291 1.00 6.57  ? 505  VAL A N   1 
ATOM   3999 C  CA  . VAL A 1 505  ? 65.221 68.384  -17.738 1.00 7.95  ? 505  VAL A CA  1 
ATOM   4000 C  C   . VAL A 1 505  ? 66.657 68.883  -18.027 1.00 7.52  ? 505  VAL A C   1 
ATOM   4001 O  O   . VAL A 1 505  ? 67.316 68.398  -18.981 1.00 8.58  ? 505  VAL A O   1 
ATOM   4002 C  CB  . VAL A 1 505  ? 64.178 69.400  -18.240 1.00 7.97  ? 505  VAL A CB  1 
ATOM   4003 C  CG1 . VAL A 1 505  ? 64.533 69.873  -19.658 1.00 10.16 ? 505  VAL A CG1 1 
ATOM   4004 C  CG2 . VAL A 1 505  ? 62.750 68.800  -18.182 1.00 9.92  ? 505  VAL A CG2 1 
ATOM   4005 N  N   . TYR A 1 506  ? 67.148 69.817  -17.232 1.00 7.69  ? 506  TYR A N   1 
ATOM   4006 C  CA  . TYR A 1 506  ? 68.518 70.301  -17.448 1.00 8.29  ? 506  TYR A CA  1 
ATOM   4007 C  C   . TYR A 1 506  ? 69.539 69.135  -17.359 1.00 9.12  ? 506  TYR A C   1 
ATOM   4008 O  O   . TYR A 1 506  ? 70.426 69.015  -18.183 1.00 9.83  ? 506  TYR A O   1 
ATOM   4009 C  CB  . TYR A 1 506  ? 68.846 71.475  -16.498 1.00 8.28  ? 506  TYR A CB  1 
ATOM   4010 C  CG  . TYR A 1 506  ? 70.288 71.968  -16.605 1.00 9.31  ? 506  TYR A CG  1 
ATOM   4011 C  CD1 . TYR A 1 506  ? 70.822 72.398  -17.814 1.00 13.77 ? 506  TYR A CD1 1 
ATOM   4012 C  CD2 . TYR A 1 506  ? 71.116 71.967  -15.492 1.00 10.36 ? 506  TYR A CD2 1 
ATOM   4013 C  CE1 . TYR A 1 506  ? 72.159 72.828  -17.905 1.00 12.54 ? 506  TYR A CE1 1 
ATOM   4014 C  CE2 . TYR A 1 506  ? 72.470 72.392  -15.579 1.00 14.39 ? 506  TYR A CE2 1 
ATOM   4015 C  CZ  . TYR A 1 506  ? 72.964 72.813  -16.785 1.00 11.88 ? 506  TYR A CZ  1 
ATOM   4016 O  OH  . TYR A 1 506  ? 74.292 73.216  -16.892 1.00 14.51 ? 506  TYR A OH  1 
ATOM   4017 N  N   . ARG A 1 507  ? 69.389 68.263  -16.385 1.00 8.45  ? 507  ARG A N   1 
ATOM   4018 C  CA  . ARG A 1 507  ? 70.293 67.128  -16.272 1.00 7.85  ? 507  ARG A CA  1 
ATOM   4019 C  C   . ARG A 1 507  ? 70.141 66.115  -17.408 1.00 9.39  ? 507  ARG A C   1 
ATOM   4020 O  O   . ARG A 1 507  ? 71.102 65.578  -17.900 1.00 9.59  ? 507  ARG A O   1 
ATOM   4021 C  CB  . ARG A 1 507  ? 70.096 66.452  -14.920 1.00 9.11  ? 507  ARG A CB  1 
ATOM   4022 C  CG  . ARG A 1 507  ? 71.213 65.463  -14.578 1.00 11.12 ? 507  ARG A CG  1 
ATOM   4023 C  CD  . ARG A 1 507  ? 71.091 65.013  -13.149 1.00 11.50 ? 507  ARG A CD  1 
ATOM   4024 N  NE  . ARG A 1 507  ? 72.081 63.991  -12.795 1.00 14.04 ? 507  ARG A NE  1 
ATOM   4025 C  CZ  . ARG A 1 507  ? 72.138 63.412  -11.602 1.00 12.82 ? 507  ARG A CZ  1 
ATOM   4026 N  NH1 . ARG A 1 507  ? 71.307 63.765  -10.656 1.00 14.89 ? 507  ARG A NH1 1 
ATOM   4027 N  NH2 . ARG A 1 507  ? 73.043 62.488  -11.348 1.00 18.98 ? 507  ARG A NH2 1 
ATOM   4028 N  N   . LEU A 1 508  ? 68.913 65.841  -17.806 1.00 7.71  ? 508  LEU A N   1 
ATOM   4029 C  CA  . LEU A 1 508  ? 68.676 64.837  -18.826 1.00 7.96  ? 508  LEU A CA  1 
ATOM   4030 C  C   . LEU A 1 508  ? 69.075 65.243  -20.235 1.00 7.25  ? 508  LEU A C   1 
ATOM   4031 O  O   . LEU A 1 508  ? 69.289 64.357  -21.082 1.00 9.94  ? 508  LEU A O   1 
ATOM   4032 C  CB  . LEU A 1 508  ? 67.168 64.475  -18.845 1.00 7.42  ? 508  LEU A CB  1 
ATOM   4033 C  CG  . LEU A 1 508  ? 66.740 63.599  -17.612 1.00 7.50  ? 508  LEU A CG  1 
ATOM   4034 C  CD1 . LEU A 1 508  ? 65.204 63.676  -17.500 1.00 8.53  ? 508  LEU A CD1 1 
ATOM   4035 C  CD2 . LEU A 1 508  ? 67.182 62.153  -17.759 1.00 9.67  ? 508  LEU A CD2 1 
ATOM   4036 N  N   . LEU A 1 509  ? 69.164 66.546  -20.502 1.00 7.87  ? 509  LEU A N   1 
ATOM   4037 C  CA  . LEU A 1 509  ? 69.434 67.039  -21.855 1.00 8.19  ? 509  LEU A CA  1 
ATOM   4038 C  C   . LEU A 1 509  ? 70.707 67.829  -21.967 1.00 8.05  ? 509  LEU A C   1 
ATOM   4039 O  O   . LEU A 1 509  ? 70.872 68.565  -22.956 1.00 10.08 ? 509  LEU A O   1 
ATOM   4040 C  CB  . LEU A 1 509  ? 68.198 67.844  -22.372 1.00 8.17  ? 509  LEU A CB  1 
ATOM   4041 C  CG  . LEU A 1 509  ? 66.981 66.976  -22.671 1.00 7.67  ? 509  LEU A CG  1 
ATOM   4042 C  CD1 . LEU A 1 509  ? 65.857 67.956  -23.087 1.00 7.40  ? 509  LEU A CD1 1 
ATOM   4043 C  CD2 . LEU A 1 509  ? 67.234 65.967  -23.783 1.00 10.20 ? 509  LEU A CD2 1 
ATOM   4044 N  N   . THR A 1 510  ? 71.625 67.746  -20.999 1.00 8.13  ? 510  THR A N   1 
ATOM   4045 C  CA  . THR A 1 510  ? 72.906 68.468  -21.137 1.00 8.16  ? 510  THR A CA  1 
ATOM   4046 C  C   . THR A 1 510  ? 74.037 67.429  -21.146 1.00 9.39  ? 510  THR A C   1 
ATOM   4047 O  O   . THR A 1 510  ? 74.016 66.472  -20.364 1.00 10.15 ? 510  THR A O   1 
ATOM   4048 C  CB  . THR A 1 510  ? 73.076 69.425  -19.964 1.00 9.14  ? 510  THR A CB  1 
ATOM   4049 O  OG1 . THR A 1 510  ? 71.960 70.353  -19.957 1.00 9.88  ? 510  THR A OG1 1 
ATOM   4050 C  CG2 . THR A 1 510  ? 74.383 70.283  -20.081 1.00 10.02 ? 510  THR A CG2 1 
ATOM   4051 N  N   . LYS A 1 511  ? 75.027 67.651  -22.017 1.00 9.71  ? 511  LYS A N   1 
ATOM   4052 C  CA  . LYS A 1 511  ? 76.202 66.741  -22.085 1.00 10.90 ? 511  LYS A CA  1 
ATOM   4053 C  C   . LYS A 1 511  ? 76.699 66.615  -20.662 1.00 10.80 ? 511  LYS A C   1 
ATOM   4054 O  O   . LYS A 1 511  ? 76.963 67.601  -19.979 1.00 9.71  ? 511  LYS A O   1 
ATOM   4055 C  CB  . LYS A 1 511  ? 77.239 67.384  -22.999 1.00 13.62 ? 511  LYS A CB  1 
ATOM   4056 C  CG  . LYS A 1 511  ? 78.431 66.414  -23.153 1.00 18.99 ? 511  LYS A CG  1 
ATOM   4057 C  CD  . LYS A 1 511  ? 79.568 66.883  -24.055 1.00 21.46 ? 511  LYS A CD  1 
ATOM   4058 C  CE  . LYS A 1 511  ? 80.717 65.782  -24.047 1.00 25.01 ? 511  LYS A CE  1 
ATOM   4059 N  NZ  . LYS A 1 511  ? 81.991 66.051  -24.822 1.00 30.19 ? 511  LYS A NZ  1 
ATOM   4060 N  N   . PRO A 1 512  ? 76.941 65.361  -20.193 1.00 11.35 ? 512  PRO A N   1 
ATOM   4061 C  CA  . PRO A 1 512  ? 77.351 65.206  -18.789 1.00 12.18 ? 512  PRO A CA  1 
ATOM   4062 C  C   . PRO A 1 512  ? 78.582 65.933  -18.300 1.00 11.32 ? 512  PRO A C   1 
ATOM   4063 O  O   . PRO A 1 512  ? 78.608 66.416  -17.174 1.00 13.07 ? 512  PRO A O   1 
ATOM   4064 C  CB  . PRO A 1 512  ? 77.477 63.695  -18.621 1.00 15.14 ? 512  PRO A CB  1 
ATOM   4065 C  CG  . PRO A 1 512  ? 76.482 63.169  -19.617 1.00 19.04 ? 512  PRO A CG  1 
ATOM   4066 C  CD  . PRO A 1 512  ? 76.562 64.064  -20.809 1.00 14.65 ? 512  PRO A CD  1 
ATOM   4067 N  N   . SER A 1 513  ? 79.568 66.032  -19.177 1.00 11.37 ? 513  SER A N   1 
ATOM   4068 C  CA  . SER A 1 513  ? 80.825 66.730  -18.789 1.00 11.41 ? 513  SER A CA  1 
ATOM   4069 C  C   . SER A 1 513  ? 80.678 68.239  -18.800 1.00 11.42 ? 513  SER A C   1 
ATOM   4070 O  O   . SER A 1 513  ? 81.610 68.951  -18.411 1.00 13.32 ? 513  SER A O   1 
ATOM   4071 C  CB  . SER A 1 513  ? 81.987 66.292  -19.725 1.00 12.06 ? 513  SER A CB  1 
ATOM   4072 O  OG  . SER A 1 513  ? 81.675 66.635  -21.052 1.00 13.29 ? 513  SER A OG  1 
ATOM   4073 N  N   . ILE A 1 514  ? 79.525 68.763  -19.251 1.00 11.28 ? 514  ILE A N   1 
ATOM   4074 C  CA  . ILE A 1 514  ? 79.242 70.192  -19.282 1.00 11.78 ? 514  ILE A CA  1 
ATOM   4075 C  C   . ILE A 1 514  ? 78.233 70.559  -18.178 1.00 11.28 ? 514  ILE A C   1 
ATOM   4076 O  O   . ILE A 1 514  ? 78.294 71.635  -17.647 1.00 12.59 ? 514  ILE A O   1 
ATOM   4077 C  CB  . ILE A 1 514  ? 78.680 70.599  -20.711 1.00 13.20 ? 514  ILE A CB  1 
ATOM   4078 C  CG1 . ILE A 1 514  ? 79.816 70.520  -21.741 1.00 17.17 ? 514  ILE A CG1 1 
ATOM   4079 C  CG2 . ILE A 1 514  ? 78.033 71.980  -20.643 1.00 15.58 ? 514  ILE A CG2 1 
ATOM   4080 C  CD1 . ILE A 1 514  ? 79.356 70.742  -23.191 1.00 21.73 ? 514  ILE A CD1 1 
ATOM   4081 N  N   . TYR A 1 515  ? 77.358 69.616  -17.801 1.00 10.92 ? 515  TYR A N   1 
ATOM   4082 C  CA  . TYR A 1 515  ? 76.315 69.825  -16.779 1.00 9.98  ? 515  TYR A CA  1 
ATOM   4083 C  C   . TYR A 1 515  ? 76.902 70.458  -15.531 1.00 10.48 ? 515  TYR A C   1 
ATOM   4084 O  O   . TYR A 1 515  ? 77.789 69.853  -14.897 1.00 11.87 ? 515  TYR A O   1 
ATOM   4085 C  CB  . TYR A 1 515  ? 75.711 68.456  -16.518 1.00 11.13 ? 515  TYR A CB  1 
ATOM   4086 C  CG  . TYR A 1 515  ? 74.709 68.414  -15.416 1.00 11.16 ? 515  TYR A CG  1 
ATOM   4087 C  CD1 . TYR A 1 515  ? 73.532 69.144  -15.465 1.00 9.78  ? 515  TYR A CD1 1 
ATOM   4088 C  CD2 . TYR A 1 515  ? 74.951 67.613  -14.324 1.00 10.68 ? 515  TYR A CD2 1 
ATOM   4089 C  CE1 . TYR A 1 515  ? 72.576 69.072  -14.399 1.00 9.06  ? 515  TYR A CE1 1 
ATOM   4090 C  CE2 . TYR A 1 515  ? 74.023 67.514  -13.253 1.00 10.43 ? 515  TYR A CE2 1 
ATOM   4091 C  CZ  . TYR A 1 515  ? 72.865 68.249  -13.318 1.00 11.34 ? 515  TYR A CZ  1 
ATOM   4092 O  OH  . TYR A 1 515  ? 71.965 68.168  -12.278 1.00 10.85 ? 515  TYR A OH  1 
ATOM   4093 N  N   . SER A 1 516  ? 76.399 71.618  -15.143 1.00 11.37 ? 516  SER A N   1 
ATOM   4094 C  CA  . SER A 1 516  ? 76.938 72.329  -13.996 1.00 12.33 ? 516  SER A CA  1 
ATOM   4095 C  C   . SER A 1 516  ? 75.815 72.910  -13.158 1.00 14.52 ? 516  SER A C   1 
ATOM   4096 O  O   . SER A 1 516  ? 75.546 74.098  -13.236 1.00 14.91 ? 516  SER A O   1 
ATOM   4097 C  CB  . SER A 1 516  ? 77.864 73.452  -14.461 1.00 12.35 ? 516  SER A CB  1 
ATOM   4098 O  OG  . SER A 1 516  ? 78.623 73.950  -13.372 1.00 19.41 ? 516  SER A OG  1 
ATOM   4099 N  N   . PRO A 1 517  ? 75.158 72.069  -12.365 1.00 14.38 ? 517  PRO A N   1 
ATOM   4100 C  CA  . PRO A 1 517  ? 73.927 72.488  -11.698 1.00 14.73 ? 517  PRO A CA  1 
ATOM   4101 C  C   . PRO A 1 517  ? 74.192 73.413  -10.534 1.00 13.67 ? 517  PRO A C   1 
ATOM   4102 O  O   . PRO A 1 517  ? 75.103 73.190  -9.753  1.00 17.74 ? 517  PRO A O   1 
ATOM   4103 C  CB  . PRO A 1 517  ? 73.323 71.175  -11.203 1.00 17.37 ? 517  PRO A CB  1 
ATOM   4104 C  CG  . PRO A 1 517  ? 74.428 70.251  -11.114 1.00 15.61 ? 517  PRO A CG  1 
ATOM   4105 C  CD  . PRO A 1 517  ? 75.373 70.624  -12.222 1.00 13.97 ? 517  PRO A CD  1 
ATOM   4106 N  N   . ASP A 1 518  ? 73.393 74.459  -10.454 1.00 14.73 ? 518  ASP A N   1 
ATOM   4107 C  CA  . ASP A 1 518  ? 73.080 75.128  -9.210  1.00 15.41 ? 518  ASP A CA  1 
ATOM   4108 C  C   . ASP A 1 518  ? 71.663 74.730  -8.827  1.00 12.52 ? 518  ASP A C   1 
ATOM   4109 O  O   . ASP A 1 518  ? 70.720 75.073  -9.512  1.00 13.11 ? 518  ASP A O   1 
ATOM   4110 C  CB  . ASP A 1 518  ? 73.154 76.639  -9.451  1.00 17.93 ? 518  ASP A CB  1 
ATOM   4111 C  CG  . ASP A 1 518  ? 72.755 77.456  -8.248  1.00 23.25 ? 518  ASP A CG  1 
ATOM   4112 O  OD1 . ASP A 1 518  ? 72.088 76.938  -7.346  1.00 19.06 ? 518  ASP A OD1 1 
ATOM   4113 O  OD2 . ASP A 1 518  ? 73.099 78.650  -8.227  1.00 27.19 ? 518  ASP A OD2 1 
ATOM   4114 N  N   . PHE A 1 519  ? 71.525 73.984  -7.744  1.00 14.51 ? 519  PHE A N   1 
ATOM   4115 C  CA  . PHE A 1 519  ? 70.226 73.432  -7.385  1.00 13.43 ? 519  PHE A CA  1 
ATOM   4116 C  C   . PHE A 1 519  ? 69.166 74.409  -6.977  1.00 14.61 ? 519  PHE A C   1 
ATOM   4117 O  O   . PHE A 1 519  ? 68.010 74.004  -6.794  1.00 15.82 ? 519  PHE A O   1 
ATOM   4118 C  CB  . PHE A 1 519  ? 70.407 72.333  -6.351  1.00 14.09 ? 519  PHE A CB  1 
ATOM   4119 C  CG  . PHE A 1 519  ? 71.258 71.177  -6.855  1.00 13.22 ? 519  PHE A CG  1 
ATOM   4120 C  CD1 . PHE A 1 519  ? 70.963 70.499  -8.068  1.00 13.70 ? 519  PHE A CD1 1 
ATOM   4121 C  CD2 . PHE A 1 519  ? 72.340 70.756  -6.079  1.00 15.75 ? 519  PHE A CD2 1 
ATOM   4122 C  CE1 . PHE A 1 519  ? 71.734 69.431  -8.491  1.00 14.61 ? 519  PHE A CE1 1 
ATOM   4123 C  CE2 . PHE A 1 519  ? 73.117 69.690  -6.479  1.00 14.67 ? 519  PHE A CE2 1 
ATOM   4124 C  CZ  . PHE A 1 519  ? 72.829 69.017  -7.689  1.00 15.65 ? 519  PHE A CZ  1 
ATOM   4125 N  N   . SER A 1 520  ? 69.497 75.694  -6.854  1.00 14.39 ? 520  SER A N   1 
ATOM   4126 C  CA  . SER A 1 520  ? 68.471 76.715  -6.513  1.00 16.91 ? 520  SER A CA  1 
ATOM   4127 C  C   . SER A 1 520  ? 68.113 77.538  -7.771  1.00 14.76 ? 520  SER A C   1 
ATOM   4128 O  O   . SER A 1 520  ? 67.201 78.349  -7.718  1.00 16.35 ? 520  SER A O   1 
ATOM   4129 C  CB  . SER A 1 520  ? 69.019 77.732  -5.496  1.00 17.70 ? 520  SER A CB  1 
ATOM   4130 O  OG  . SER A 1 520  ? 70.111 78.437  -6.108  1.00 22.20 ? 520  SER A OG  1 
ATOM   4131 N  N   . PHE A 1 521  ? 68.813 77.283  -8.887  1.00 14.10 ? 521  PHE A N   1 
ATOM   4132 C  CA  . PHE A 1 521  ? 68.626 78.083  -10.104 1.00 14.38 ? 521  PHE A CA  1 
ATOM   4133 C  C   . PHE A 1 521  ? 67.518 77.582  -11.000 1.00 12.47 ? 521  PHE A C   1 
ATOM   4134 O  O   . PHE A 1 521  ? 67.261 76.385  -11.044 1.00 15.39 ? 521  PHE A O   1 
ATOM   4135 C  CB  . PHE A 1 521  ? 69.961 78.086  -10.896 1.00 14.61 ? 521  PHE A CB  1 
ATOM   4136 C  CG  . PHE A 1 521  ? 69.986 79.073  -12.036 1.00 16.23 ? 521  PHE A CG  1 
ATOM   4137 C  CD1 . PHE A 1 521  ? 70.146 80.449  -11.771 1.00 20.17 ? 521  PHE A CD1 1 
ATOM   4138 C  CD2 . PHE A 1 521  ? 69.800 78.659  -13.365 1.00 16.63 ? 521  PHE A CD2 1 
ATOM   4139 C  CE1 . PHE A 1 521  ? 70.105 81.397  -12.812 1.00 25.11 ? 521  PHE A CE1 1 
ATOM   4140 C  CE2 . PHE A 1 521  ? 69.754 79.580  -14.412 1.00 20.03 ? 521  PHE A CE2 1 
ATOM   4141 C  CZ  . PHE A 1 521  ? 69.904 80.957  -14.146 1.00 25.65 ? 521  PHE A CZ  1 
ATOM   4142 N  N   . SER A 1 522  ? 66.872 78.495  -11.696 1.00 14.60 ? 522  SER A N   1 
ATOM   4143 C  CA  . SER A 1 522  ? 65.817 78.160  -12.655 1.00 14.38 ? 522  SER A CA  1 
ATOM   4144 C  C   . SER A 1 522  ? 66.383 78.113  -14.069 1.00 12.76 ? 522  SER A C   1 
ATOM   4145 O  O   . SER A 1 522  ? 66.512 79.152  -14.747 1.00 16.78 ? 522  SER A O   1 
ATOM   4146 C  CB  . SER A 1 522  ? 64.695 79.205  -12.591 1.00 20.83 ? 522  SER A CB  1 
ATOM   4147 O  OG  . SER A 1 522  ? 63.916 78.977  -11.417 1.00 30.03 ? 522  SER A OG  1 
ATOM   4148 N  N   . TYR A 1 523  ? 66.707 76.911  -14.527 1.00 9.48  ? 523  TYR A N   1 
ATOM   4149 C  CA  . TYR A 1 523  ? 67.161 76.677  -15.898 1.00 8.92  ? 523  TYR A CA  1 
ATOM   4150 C  C   . TYR A 1 523  ? 66.047 76.768  -16.925 1.00 10.25 ? 523  TYR A C   1 
ATOM   4151 O  O   . TYR A 1 523  ? 66.240 77.167  -18.046 1.00 10.26 ? 523  TYR A O   1 
ATOM   4152 C  CB  . TYR A 1 523  ? 67.857 75.305  -16.001 1.00 10.56 ? 523  TYR A CB  1 
ATOM   4153 C  CG  . TYR A 1 523  ? 69.131 75.293  -15.199 1.00 9.67  ? 523  TYR A CG  1 
ATOM   4154 C  CD1 . TYR A 1 523  ? 70.288 75.871  -15.707 1.00 12.93 ? 523  TYR A CD1 1 
ATOM   4155 C  CD2 . TYR A 1 523  ? 69.159 74.777  -13.918 1.00 11.15 ? 523  TYR A CD2 1 
ATOM   4156 C  CE1 . TYR A 1 523  ? 71.446 75.890  -14.976 1.00 13.81 ? 523  TYR A CE1 1 
ATOM   4157 C  CE2 . TYR A 1 523  ? 70.311 74.791  -13.185 1.00 12.77 ? 523  TYR A CE2 1 
ATOM   4158 C  CZ  . TYR A 1 523  ? 71.448 75.358  -13.715 1.00 16.98 ? 523  TYR A CZ  1 
ATOM   4159 O  OH  . TYR A 1 523  ? 72.582 75.380  -12.938 1.00 16.37 ? 523  TYR A OH  1 
ATOM   4160 N  N   . PHE A 1 524  ? 64.862 76.360  -16.509 1.00 8.78  ? 524  PHE A N   1 
ATOM   4161 C  CA  . PHE A 1 524  ? 63.681 76.424  -17.372 1.00 7.95  ? 524  PHE A CA  1 
ATOM   4162 C  C   . PHE A 1 524  ? 62.487 76.877  -16.540 1.00 10.96 ? 524  PHE A C   1 
ATOM   4163 O  O   . PHE A 1 524  ? 62.415 76.632  -15.321 1.00 11.72 ? 524  PHE A O   1 
ATOM   4164 C  CB  . PHE A 1 524  ? 63.250 75.032  -17.942 1.00 8.86  ? 524  PHE A CB  1 
ATOM   4165 C  CG  . PHE A 1 524  ? 64.292 74.375  -18.802 1.00 8.33  ? 524  PHE A CG  1 
ATOM   4166 C  CD1 . PHE A 1 524  ? 65.310 73.614  -18.218 1.00 9.70  ? 524  PHE A CD1 1 
ATOM   4167 C  CD2 . PHE A 1 524  ? 64.253 74.535  -20.197 1.00 9.10  ? 524  PHE A CD2 1 
ATOM   4168 C  CE1 . PHE A 1 524  ? 66.283 73.024  -19.035 1.00 10.56 ? 524  PHE A CE1 1 
ATOM   4169 C  CE2 . PHE A 1 524  ? 65.238 73.926  -21.019 1.00 9.21  ? 524  PHE A CE2 1 
ATOM   4170 C  CZ  . PHE A 1 524  ? 66.235 73.190  -20.438 1.00 9.36  ? 524  PHE A CZ  1 
ATOM   4171 N  N   . THR A 1 525  ? 61.546 77.500  -17.234 1.00 10.54 ? 525  THR A N   1 
ATOM   4172 C  CA  . THR A 1 525  ? 60.266 77.779  -16.599 1.00 14.84 ? 525  THR A CA  1 
ATOM   4173 C  C   . THR A 1 525  ? 59.204 76.992  -17.356 1.00 10.83 ? 525  THR A C   1 
ATOM   4174 O  O   . THR A 1 525  ? 59.273 76.828  -18.609 1.00 12.56 ? 525  THR A O   1 
ATOM   4175 C  CB  . THR A 1 525  ? 59.894 79.229  -16.583 1.00 17.19 ? 525  THR A CB  1 
ATOM   4176 O  OG1 . THR A 1 525  ? 59.831 79.683  -17.897 1.00 20.35 ? 525  THR A OG1 1 
ATOM   4177 C  CG2 . THR A 1 525  ? 60.976 80.066  -15.861 1.00 20.59 ? 525  THR A CG2 1 
ATOM   4178 N  N   . LEU A 1 526  ? 58.212 76.509  -16.627 1.00 10.59 ? 526  LEU A N   1 
ATOM   4179 C  CA  . LEU A 1 526  ? 57.144 75.787  -17.230 1.00 11.59 ? 526  LEU A CA  1 
ATOM   4180 C  C   . LEU A 1 526  ? 56.198 76.762  -17.904 1.00 11.77 ? 526  LEU A C   1 
ATOM   4181 O  O   . LEU A 1 526  ? 55.977 77.892  -17.419 1.00 14.95 ? 526  LEU A O   1 
ATOM   4182 C  CB  . LEU A 1 526  ? 56.341 75.002  -16.159 1.00 14.56 ? 526  LEU A CB  1 
ATOM   4183 C  CG  . LEU A 1 526  ? 56.822 73.609  -15.773 1.00 15.80 ? 526  LEU A CG  1 
ATOM   4184 C  CD1 . LEU A 1 526  ? 55.988 73.102  -14.555 1.00 20.64 ? 526  LEU A CD1 1 
ATOM   4185 C  CD2 . LEU A 1 526  ? 56.653 72.674  -16.963 1.00 16.44 ? 526  LEU A CD2 1 
ATOM   4186 N  N   . ASP A 1 527  ? 55.614 76.338  -18.999 1.00 8.62  ? 527  ASP A N   1 
ATOM   4187 C  CA  . ASP A 1 527  ? 54.633 77.132  -19.671 1.00 10.19 ? 527  ASP A CA  1 
ATOM   4188 C  C   . ASP A 1 527  ? 53.382 76.257  -19.717 1.00 9.54  ? 527  ASP A C   1 
ATOM   4189 O  O   . ASP A 1 527  ? 53.424 75.155  -20.245 1.00 15.32 ? 527  ASP A O   1 
ATOM   4190 C  CB  . ASP A 1 527  ? 55.102 77.521  -21.095 1.00 10.77 ? 527  ASP A CB  1 
ATOM   4191 C  CG  . ASP A 1 527  ? 54.086 78.388  -21.817 1.00 15.66 ? 527  ASP A CG  1 
ATOM   4192 O  OD1 . ASP A 1 527  ? 53.771 79.490  -21.322 1.00 16.21 ? 527  ASP A OD1 1 
ATOM   4193 O  OD2 . ASP A 1 527  ? 53.582 77.973  -22.885 1.00 17.92 ? 527  ASP A OD2 1 
ATOM   4194 N  N   . ASP A 1 528  ? 52.281 76.690  -19.157 1.00 9.98  ? 528  ASP A N   1 
ATOM   4195 C  CA  . ASP A 1 528  ? 51.067 75.875  -19.151 1.00 9.44  ? 528  ASP A CA  1 
ATOM   4196 C  C   . ASP A 1 528  ? 49.973 76.717  -19.760 1.00 10.13 ? 528  ASP A C   1 
ATOM   4197 O  O   . ASP A 1 528  ? 49.624 77.763  -19.241 1.00 11.39 ? 528  ASP A O   1 
ATOM   4198 C  CB  . ASP A 1 528  ? 50.736 75.465  -17.711 1.00 10.07 ? 528  ASP A CB  1 
ATOM   4199 C  CG  . ASP A 1 528  ? 49.657 74.417  -17.635 1.00 10.38 ? 528  ASP A CG  1 
ATOM   4200 O  OD1 . ASP A 1 528  ? 48.656 74.487  -18.354 1.00 11.71 ? 528  ASP A OD1 1 
ATOM   4201 O  OD2 . ASP A 1 528  ? 49.853 73.469  -16.815 1.00 13.22 ? 528  ASP A OD2 1 
ATOM   4202 N  N   . SER A 1 529  ? 49.435 76.267  -20.892 1.00 10.36 ? 529  SER A N   1 
ATOM   4203 C  CA  . SER A 1 529  ? 48.408 77.045  -21.589 1.00 11.00 ? 529  SER A CA  1 
ATOM   4204 C  C   . SER A 1 529  ? 47.032 76.922  -20.996 1.00 10.44 ? 529  SER A C   1 
ATOM   4205 O  O   . SER A 1 529  ? 46.159 77.685  -21.334 1.00 14.15 ? 529  SER A O   1 
ATOM   4206 C  CB  . SER A 1 529  ? 48.227 76.599  -23.049 1.00 13.42 ? 529  SER A CB  1 
ATOM   4207 O  OG  . SER A 1 529  ? 49.469 76.567  -23.702 1.00 17.80 ? 529  SER A OG  1 
ATOM   4208 N  N   . ARG A 1 530  ? 46.790 75.956  -20.084 1.00 8.44  ? 530  ARG A N   1 
ATOM   4209 C  CA  . ARG A 1 530  ? 45.446 75.769  -19.576 1.00 9.51  ? 530  ARG A CA  1 
ATOM   4210 C  C   . ARG A 1 530  ? 45.328 75.876  -18.083 1.00 10.66 ? 530  ARG A C   1 
ATOM   4211 O  O   . ARG A 1 530  ? 44.261 75.532  -17.553 1.00 15.49 ? 530  ARG A O   1 
ATOM   4212 C  CB  . ARG A 1 530  ? 44.899 74.409  -20.091 1.00 8.65  ? 530  ARG A CB  1 
ATOM   4213 C  CG  . ARG A 1 530  ? 44.946 74.349  -21.642 1.00 10.11 ? 530  ARG A CG  1 
ATOM   4214 C  CD  . ARG A 1 530  ? 44.258 73.103  -22.259 1.00 9.88  ? 530  ARG A CD  1 
ATOM   4215 N  NE  . ARG A 1 530  ? 44.933 71.907  -21.810 1.00 10.30 ? 530  ARG A NE  1 
ATOM   4216 C  CZ  . ARG A 1 530  ? 44.722 70.689  -22.327 1.00 10.83 ? 530  ARG A CZ  1 
ATOM   4217 N  NH1 . ARG A 1 530  ? 43.872 70.535  -23.314 1.00 12.60 ? 530  ARG A NH1 1 
ATOM   4218 N  NH2 . ARG A 1 530  ? 45.365 69.645  -21.826 1.00 13.87 ? 530  ARG A NH2 1 
ATOM   4219 N  N   . TRP A 1 531  ? 46.372 76.265  -17.379 1.00 8.68  ? 531  TRP A N   1 
ATOM   4220 C  CA  . TRP A 1 531  ? 46.224 76.520  -15.947 1.00 9.27  ? 531  TRP A CA  1 
ATOM   4221 C  C   . TRP A 1 531  ? 47.147 77.621  -15.521 1.00 9.01  ? 531  TRP A C   1 
ATOM   4222 O  O   . TRP A 1 531  ? 48.308 77.545  -15.812 1.00 10.88 ? 531  TRP A O   1 
ATOM   4223 C  CB  . TRP A 1 531  ? 46.557 75.296  -15.105 1.00 10.42 ? 531  TRP A CB  1 
ATOM   4224 C  CG  . TRP A 1 531  ? 46.459 75.651  -13.671 1.00 11.18 ? 531  TRP A CG  1 
ATOM   4225 C  CD1 . TRP A 1 531  ? 47.472 76.042  -12.841 1.00 15.36 ? 531  TRP A CD1 1 
ATOM   4226 C  CD2 . TRP A 1 531  ? 45.266 75.719  -12.909 1.00 13.49 ? 531  TRP A CD2 1 
ATOM   4227 N  NE1 . TRP A 1 531  ? 46.974 76.313  -11.599 1.00 19.29 ? 531  TRP A NE1 1 
ATOM   4228 C  CE2 . TRP A 1 531  ? 45.620 76.135  -11.614 1.00 11.62 ? 531  TRP A CE2 1 
ATOM   4229 C  CE3 . TRP A 1 531  ? 43.941 75.440  -13.185 1.00 11.63 ? 531  TRP A CE3 1 
ATOM   4230 C  CZ2 . TRP A 1 531  ? 44.685 76.291  -10.602 1.00 17.51 ? 531  TRP A CZ2 1 
ATOM   4231 C  CZ3 . TRP A 1 531  ? 43.011 75.604  -12.186 1.00 14.69 ? 531  TRP A CZ3 1 
ATOM   4232 C  CH2 . TRP A 1 531  ? 43.388 76.017  -10.910 1.00 16.45 ? 531  TRP A CH2 1 
ATOM   4233 N  N   . PRO A 1 532  ? 46.633 78.633  -14.831 1.00 9.85  ? 532  PRO A N   1 
ATOM   4234 C  CA  . PRO A 1 532  ? 45.233 78.827  -14.437 1.00 10.18 ? 532  PRO A CA  1 
ATOM   4235 C  C   . PRO A 1 532  ? 44.356 79.095  -15.656 1.00 11.95 ? 532  PRO A C   1 
ATOM   4236 O  O   . PRO A 1 532  ? 43.132 78.952  -15.607 1.00 13.17 ? 532  PRO A O   1 
ATOM   4237 C  CB  . PRO A 1 532  ? 45.280 80.061  -13.471 1.00 12.58 ? 532  PRO A CB  1 
ATOM   4238 C  CG  . PRO A 1 532  ? 46.678 79.932  -12.851 1.00 14.18 ? 532  PRO A CG  1 
ATOM   4239 C  CD  . PRO A 1 532  ? 47.544 79.547  -14.076 1.00 11.61 ? 532  PRO A CD  1 
ATOM   4240 N  N   . GLY A 1 533  ? 44.990 79.470  -16.767 1.00 11.21 ? 533  GLY A N   1 
ATOM   4241 C  CA  . GLY A 1 533  ? 44.247 79.671  -18.001 1.00 13.54 ? 533  GLY A CA  1 
ATOM   4242 C  C   . GLY A 1 533  ? 44.045 81.129  -18.376 1.00 18.37 ? 533  GLY A C   1 
ATOM   4243 O  O   . GLY A 1 533  ? 44.050 82.047  -17.535 1.00 18.08 ? 533  GLY A O   1 
ATOM   4244 N  N   . SER A 1 534  ? 43.936 81.315  -19.694 1.00 20.99 ? 534  SER A N   1 
ATOM   4245 C  CA  . SER A 1 534  ? 43.741 82.632  -20.290 1.00 21.31 ? 534  SER A CA  1 
ATOM   4246 C  C   . SER A 1 534  ? 42.472 83.181  -19.670 1.00 21.40 ? 534  SER A C   1 
ATOM   4247 O  O   . SER A 1 534  ? 41.420 82.507  -19.661 1.00 24.57 ? 534  SER A O   1 
ATOM   4248 C  CB  . SER A 1 534  ? 43.602 82.476  -21.802 1.00 28.92 ? 534  SER A CB  1 
ATOM   4249 O  OG  . SER A 1 534  ? 43.632 83.736  -22.450 1.00 34.63 ? 534  SER A OG  1 
ATOM   4250 N  N   . GLY A 1 535  ? 42.543 84.402  -19.141 1.00 23.98 ? 535  GLY A N   1 
ATOM   4251 C  CA  . GLY A 1 535  ? 41.370 84.977  -18.514 1.00 24.06 ? 535  GLY A CA  1 
ATOM   4252 C  C   . GLY A 1 535  ? 41.239 84.694  -17.032 1.00 24.86 ? 535  GLY A C   1 
ATOM   4253 O  O   . GLY A 1 535  ? 40.347 85.249  -16.323 1.00 27.27 ? 535  GLY A O   1 
ATOM   4254 N  N   . VAL A 1 536  ? 42.112 83.823  -16.520 1.00 23.08 ? 536  VAL A N   1 
ATOM   4255 C  CA  . VAL A 1 536  ? 42.060 83.478  -15.096 1.00 21.62 ? 536  VAL A CA  1 
ATOM   4256 C  C   . VAL A 1 536  ? 43.247 84.167  -14.407 1.00 21.79 ? 536  VAL A C   1 
ATOM   4257 O  O   . VAL A 1 536  ? 43.058 84.865  -13.404 1.00 21.03 ? 536  VAL A O   1 
ATOM   4258 C  CB  . VAL A 1 536  ? 42.064 81.912  -14.937 1.00 20.97 ? 536  VAL A CB  1 
ATOM   4259 C  CG1 . VAL A 1 536  ? 41.898 81.482  -13.473 1.00 21.13 ? 536  VAL A CG1 1 
ATOM   4260 C  CG2 . VAL A 1 536  ? 40.865 81.343  -15.706 1.00 20.32 ? 536  VAL A CG2 1 
ATOM   4261 N  N   . GLU A 1 537  ? 44.449 83.954  -14.924 1.00 20.50 ? 537  GLU A N   1 
ATOM   4262 C  CA  . GLU A 1 537  ? 45.622 84.686  -14.454 1.00 21.21 ? 537  GLU A CA  1 
ATOM   4263 C  C   . GLU A 1 537  ? 46.528 84.979  -15.645 1.00 21.23 ? 537  GLU A C   1 
ATOM   4264 O  O   . GLU A 1 537  ? 46.616 84.182  -16.574 1.00 24.00 ? 537  GLU A O   1 
ATOM   4265 C  CB  . GLU A 1 537  ? 46.372 83.871  -13.391 1.00 23.09 ? 537  GLU A CB  1 
ATOM   4266 C  CG  . GLU A 1 537  ? 45.511 83.436  -12.204 1.00 26.84 ? 537  GLU A CG  1 
ATOM   4267 C  CD  . GLU A 1 537  ? 45.220 84.556  -11.225 1.00 36.64 ? 537  GLU A CD  1 
ATOM   4268 O  OE1 . GLU A 1 537  ? 45.570 85.715  -11.508 1.00 38.91 ? 537  GLU A OE1 1 
ATOM   4269 O  OE2 . GLU A 1 537  ? 44.635 84.277  -10.165 1.00 34.25 ? 537  GLU A OE2 1 
ATOM   4270 N  N   . ASP A 1 538  ? 47.202 86.123  -15.625 1.00 24.65 ? 538  ASP A N   1 
ATOM   4271 C  CA  . ASP A 1 538  ? 48.314 86.309  -16.549 1.00 30.94 ? 538  ASP A CA  1 
ATOM   4272 C  C   . ASP A 1 538  ? 49.595 85.778  -15.951 1.00 30.37 ? 538  ASP A C   1 
ATOM   4273 O  O   . ASP A 1 538  ? 50.292 86.468  -15.225 1.00 31.57 ? 538  ASP A O   1 
ATOM   4274 C  CB  . ASP A 1 538  ? 48.487 87.760  -17.003 1.00 35.50 ? 538  ASP A CB  1 
ATOM   4275 C  CG  . ASP A 1 538  ? 49.612 87.915  -18.027 1.00 42.84 ? 538  ASP A CG  1 
ATOM   4276 O  OD1 . ASP A 1 538  ? 50.773 87.643  -17.675 1.00 41.45 ? 538  ASP A OD1 1 
ATOM   4277 O  OD2 . ASP A 1 538  ? 49.342 88.304  -19.182 1.00 43.19 ? 538  ASP A OD2 1 
ATOM   4278 N  N   . SER A 1 539  ? 49.881 84.522  -16.251 1.00 26.81 ? 539  SER A N   1 
ATOM   4279 C  CA  . SER A 1 539  ? 50.991 83.817  -15.587 1.00 24.70 ? 539  SER A CA  1 
ATOM   4280 C  C   . SER A 1 539  ? 52.099 83.365  -16.527 1.00 24.22 ? 539  SER A C   1 
ATOM   4281 O  O   . SER A 1 539  ? 53.227 83.090  -16.083 1.00 26.16 ? 539  SER A O   1 
ATOM   4282 C  CB  . SER A 1 539  ? 50.432 82.563  -14.874 1.00 25.73 ? 539  SER A CB  1 
ATOM   4283 O  OG  . SER A 1 539  ? 49.824 81.679  -15.825 1.00 30.70 ? 539  SER A OG  1 
ATOM   4284 N  N   . ARG A 1 540  ? 51.755 83.283  -17.807 1.00 22.49 ? 540  ARG A N   1 
ATOM   4285 C  CA  . ARG A 1 540  ? 52.632 82.801  -18.862 1.00 24.05 ? 540  ARG A CA  1 
ATOM   4286 C  C   . ARG A 1 540  ? 53.644 83.805  -19.309 1.00 20.19 ? 540  ARG A C   1 
ATOM   4287 O  O   . ARG A 1 540  ? 53.322 84.974  -19.512 1.00 24.47 ? 540  ARG A O   1 
ATOM   4288 C  CB  . ARG A 1 540  ? 51.811 82.405  -20.066 1.00 23.54 ? 540  ARG A CB  1 
ATOM   4289 C  CG  . ARG A 1 540  ? 51.012 81.101  -19.837 1.00 19.49 ? 540  ARG A CG  1 
ATOM   4290 C  CD  . ARG A 1 540  ? 50.194 80.792  -21.076 1.00 16.84 ? 540  ARG A CD  1 
ATOM   4291 N  NE  . ARG A 1 540  ? 51.010 80.136  -22.116 1.00 14.70 ? 540  ARG A NE  1 
ATOM   4292 C  CZ  . ARG A 1 540  ? 50.566 79.776  -23.318 1.00 14.74 ? 540  ARG A CZ  1 
ATOM   4293 N  NH1 . ARG A 1 540  ? 49.319 79.970  -23.716 1.00 15.74 ? 540  ARG A NH1 1 
ATOM   4294 N  NH2 . ARG A 1 540  ? 51.407 79.209  -24.156 1.00 13.30 ? 540  ARG A NH2 1 
ATOM   4295 N  N   . THR A 1 541  ? 54.842 83.318  -19.502 1.00 20.08 ? 541  THR A N   1 
ATOM   4296 C  CA  . THR A 1 541  ? 55.890 84.207  -19.925 1.00 20.48 ? 541  THR A CA  1 
ATOM   4297 C  C   . THR A 1 541  ? 55.920 84.250  -21.447 1.00 18.62 ? 541  THR A C   1 
ATOM   4298 O  O   . THR A 1 541  ? 55.617 83.297  -22.159 1.00 22.46 ? 541  THR A O   1 
ATOM   4299 C  CB  . THR A 1 541  ? 57.238 83.763  -19.398 1.00 28.05 ? 541  THR A CB  1 
ATOM   4300 O  OG1 . THR A 1 541  ? 57.667 82.674  -20.175 1.00 31.20 ? 541  THR A OG1 1 
ATOM   4301 C  CG2 . THR A 1 541  ? 57.168 83.316  -17.916 1.00 22.93 ? 541  THR A CG2 1 
ATOM   4302 N  N   . THR A 1 542  ? 56.229 85.432  -21.935 1.00 15.67 ? 542  THR A N   1 
ATOM   4303 C  CA  . THR A 1 542  ? 56.371 85.627  -23.354 1.00 12.84 ? 542  THR A CA  1 
ATOM   4304 C  C   . THR A 1 542  ? 57.849 85.416  -23.653 1.00 10.54 ? 542  THR A C   1 
ATOM   4305 O  O   . THR A 1 542  ? 58.740 85.879  -22.901 1.00 14.04 ? 542  THR A O   1 
ATOM   4306 C  CB  . THR A 1 542  ? 56.050 87.072  -23.717 1.00 13.68 ? 542  THR A CB  1 
ATOM   4307 O  OG1 . THR A 1 542  ? 54.681 87.308  -23.414 1.00 19.29 ? 542  THR A OG1 1 
ATOM   4308 C  CG2 . THR A 1 542  ? 56.318 87.374  -25.172 1.00 13.91 ? 542  THR A CG2 1 
ATOM   4309 N  N   . ILE A 1 543  ? 58.111 84.640  -24.702 1.00 9.95  ? 543  ILE A N   1 
ATOM   4310 C  CA  . ILE A 1 543  ? 59.495 84.440  -25.147 1.00 9.77  ? 543  ILE A CA  1 
ATOM   4311 C  C   . ILE A 1 543  ? 59.867 85.742  -25.914 1.00 10.16 ? 543  ILE A C   1 
ATOM   4312 O  O   . ILE A 1 543  ? 59.224 86.052  -26.927 1.00 11.44 ? 543  ILE A O   1 
ATOM   4313 C  CB  . ILE A 1 543  ? 59.565 83.217  -26.044 1.00 10.28 ? 543  ILE A CB  1 
ATOM   4314 C  CG1 . ILE A 1 543  ? 59.266 81.939  -25.178 1.00 9.73  ? 543  ILE A CG1 1 
ATOM   4315 C  CG2 . ILE A 1 543  ? 60.936 83.142  -26.756 1.00 10.72 ? 543  ILE A CG2 1 
ATOM   4316 C  CD1 . ILE A 1 543  ? 59.134 80.691  -26.035 1.00 9.57  ? 543  ILE A CD1 1 
ATOM   4317 N  N   . ILE A 1 544  ? 60.853 86.447  -25.381 1.00 10.63 ? 544  ILE A N   1 
ATOM   4318 C  CA  . ILE A 1 544  ? 61.270 87.743  -25.964 1.00 10.45 ? 544  ILE A CA  1 
ATOM   4319 C  C   . ILE A 1 544  ? 62.452 87.555  -26.898 1.00 11.96 ? 544  ILE A C   1 
ATOM   4320 O  O   . ILE A 1 544  ? 63.584 87.176  -26.473 1.00 12.77 ? 544  ILE A O   1 
ATOM   4321 C  CB  . ILE A 1 544  ? 61.605 88.696  -24.819 1.00 13.00 ? 544  ILE A CB  1 
ATOM   4322 C  CG1 . ILE A 1 544  ? 60.335 88.871  -23.991 1.00 16.68 ? 544  ILE A CG1 1 
ATOM   4323 C  CG2 . ILE A 1 544  ? 62.110 90.033  -25.362 1.00 16.76 ? 544  ILE A CG2 1 
ATOM   4324 C  CD1 . ILE A 1 544  ? 60.412 89.904  -22.876 1.00 25.38 ? 544  ILE A CD1 1 
ATOM   4325 N  N   . LEU A 1 545  ? 62.173 87.783  -28.172 1.00 10.79 ? 545  LEU A N   1 
ATOM   4326 C  CA  . LEU A 1 545  ? 63.170 87.642  -29.222 1.00 10.52 ? 545  LEU A CA  1 
ATOM   4327 C  C   . LEU A 1 545  ? 63.283 89.003  -29.910 1.00 12.90 ? 545  LEU A C   1 
ATOM   4328 O  O   . LEU A 1 545  ? 62.328 89.781  -29.941 1.00 14.41 ? 545  LEU A O   1 
ATOM   4329 C  CB  . LEU A 1 545  ? 62.745 86.582  -30.239 1.00 9.92  ? 545  LEU A CB  1 
ATOM   4330 C  CG  . LEU A 1 545  ? 62.558 85.162  -29.662 1.00 9.87  ? 545  LEU A CG  1 
ATOM   4331 C  CD1 . LEU A 1 545  ? 62.080 84.227  -30.794 1.00 14.66 ? 545  LEU A CD1 1 
ATOM   4332 C  CD2 . LEU A 1 545  ? 63.819 84.674  -29.021 1.00 11.76 ? 545  LEU A CD2 1 
ATOM   4333 N  N   . GLY A 1 546  ? 64.434 89.276  -30.493 1.00 11.47 ? 546  GLY A N   1 
ATOM   4334 C  CA  . GLY A 1 546  ? 64.598 90.548  -31.203 1.00 11.61 ? 546  GLY A CA  1 
ATOM   4335 C  C   . GLY A 1 546  ? 65.989 90.564  -31.761 1.00 11.34 ? 546  GLY A C   1 
ATOM   4336 O  O   . GLY A 1 546  ? 66.932 90.052  -31.144 1.00 11.21 ? 546  GLY A O   1 
ATOM   4337 N  N   . GLU A 1 547  ? 66.134 91.260  -32.891 1.00 13.67 ? 547  GLU A N   1 
ATOM   4338 C  CA  . GLU A 1 547  ? 67.450 91.348  -33.546 1.00 17.73 ? 547  GLU A CA  1 
ATOM   4339 C  C   . GLU A 1 547  ? 68.502 92.021  -32.665 1.00 18.27 ? 547  GLU A C   1 
ATOM   4340 O  O   . GLU A 1 547  ? 69.701 91.692  -32.751 1.00 20.78 ? 547  GLU A O   1 
ATOM   4341 C  CB  . GLU A 1 547  ? 67.273 92.120  -34.854 1.00 23.06 ? 547  GLU A CB  1 
ATOM   4342 C  CG  . GLU A 1 547  ? 68.527 92.359  -35.699 1.00 36.38 ? 547  GLU A CG  1 
ATOM   4343 C  CD  . GLU A 1 547  ? 68.190 93.173  -36.967 1.00 39.82 ? 547  GLU A CD  1 
ATOM   4344 O  OE1 . GLU A 1 547  ? 67.208 92.803  -37.668 1.00 43.82 ? 547  GLU A OE1 1 
ATOM   4345 O  OE2 . GLU A 1 547  ? 68.900 94.173  -37.272 1.00 43.10 ? 547  GLU A OE2 1 
ATOM   4346 N  N   . ASP A 1 548  ? 68.043 92.909  -31.783 1.00 14.49 ? 548  ASP A N   1 
ATOM   4347 C  CA  . ASP A 1 548  ? 68.959 93.609  -30.894 1.00 14.52 ? 548  ASP A CA  1 
ATOM   4348 C  C   . ASP A 1 548  ? 68.933 93.054  -29.481 1.00 16.99 ? 548  ASP A C   1 
ATOM   4349 O  O   . ASP A 1 548  ? 69.347 93.744  -28.537 1.00 21.15 ? 548  ASP A O   1 
ATOM   4350 C  CB  . ASP A 1 548  ? 68.604 95.113  -30.870 1.00 17.26 ? 548  ASP A CB  1 
ATOM   4351 C  CG  . ASP A 1 548  ? 68.758 95.759  -32.224 1.00 20.06 ? 548  ASP A CG  1 
ATOM   4352 O  OD1 . ASP A 1 548  ? 69.899 95.780  -32.727 1.00 25.52 ? 548  ASP A OD1 1 
ATOM   4353 O  OD2 . ASP A 1 548  ? 67.763 96.235  -32.819 1.00 22.18 ? 548  ASP A OD2 1 
ATOM   4354 N  N   . ILE A 1 549  ? 68.433 91.832  -29.288 1.00 14.36 ? 549  ILE A N   1 
ATOM   4355 C  CA  . ILE A 1 549  ? 68.387 91.247  -27.945 1.00 13.82 ? 549  ILE A CA  1 
ATOM   4356 C  C   . ILE A 1 549  ? 68.689 89.743  -27.869 1.00 14.61 ? 549  ILE A C   1 
ATOM   4357 O  O   . ILE A 1 549  ? 69.504 89.333  -27.064 1.00 15.07 ? 549  ILE A O   1 
ATOM   4358 C  CB  . ILE A 1 549  ? 67.090 91.627  -27.150 1.00 14.93 ? 549  ILE A CB  1 
ATOM   4359 C  CG1 . ILE A 1 549  ? 67.115 91.051  -25.733 1.00 17.93 ? 549  ILE A CG1 1 
ATOM   4360 C  CG2 . ILE A 1 549  ? 65.825 91.193  -27.865 1.00 13.72 ? 549  ILE A CG2 1 
ATOM   4361 C  CD1 . ILE A 1 549  ? 67.673 91.952  -24.705 1.00 29.22 ? 549  ILE A CD1 1 
ATOM   4362 N  N   . LEU A 1 550  ? 68.015 88.952  -28.701 1.00 12.92 ? 550  LEU A N   1 
ATOM   4363 C  CA  . LEU A 1 550  ? 68.152 87.484  -28.610 1.00 11.67 ? 550  LEU A CA  1 
ATOM   4364 C  C   . LEU A 1 550  ? 67.498 86.930  -29.856 1.00 10.32 ? 550  LEU A C   1 
ATOM   4365 O  O   . LEU A 1 550  ? 66.312 87.118  -30.073 1.00 12.41 ? 550  LEU A O   1 
ATOM   4366 C  CB  . LEU A 1 550  ? 67.391 87.023  -27.350 1.00 13.06 ? 550  LEU A CB  1 
ATOM   4367 C  CG  . LEU A 1 550  ? 67.462 85.505  -27.169 1.00 12.42 ? 550  LEU A CG  1 
ATOM   4368 C  CD1 . LEU A 1 550  ? 68.897 85.117  -26.969 1.00 14.97 ? 550  LEU A CD1 1 
ATOM   4369 C  CD2 . LEU A 1 550  ? 66.662 85.118  -25.954 1.00 14.57 ? 550  LEU A CD2 1 
ATOM   4370 N  N   . PRO A 1 551  ? 68.266 86.235  -30.694 1.00 10.56 ? 551  PRO A N   1 
ATOM   4371 C  CA  . PRO A 1 551  ? 67.652 85.723  -31.907 1.00 11.44 ? 551  PRO A CA  1 
ATOM   4372 C  C   . PRO A 1 551  ? 66.826 84.449  -31.794 1.00 10.34 ? 551  PRO A C   1 
ATOM   4373 O  O   . PRO A 1 551  ? 65.955 84.221  -32.633 1.00 12.00 ? 551  PRO A O   1 
ATOM   4374 C  CB  . PRO A 1 551  ? 68.833 85.499  -32.882 1.00 15.26 ? 551  PRO A CB  1 
ATOM   4375 C  CG  . PRO A 1 551  ? 69.982 85.392  -32.102 1.00 19.12 ? 551  PRO A CG  1 
ATOM   4376 C  CD  . PRO A 1 551  ? 69.742 86.167  -30.747 1.00 14.27 ? 551  PRO A CD  1 
ATOM   4377 N  N   . SER A 1 552  ? 67.076 83.646  -30.749 1.00 9.81  ? 552  SER A N   1 
ATOM   4378 C  CA  . SER A 1 552  ? 66.390 82.353  -30.680 1.00 8.45  ? 552  SER A CA  1 
ATOM   4379 C  C   . SER A 1 552  ? 66.263 81.868  -29.250 1.00 8.52  ? 552  SER A C   1 
ATOM   4380 O  O   . SER A 1 552  ? 66.942 82.354  -28.350 1.00 9.58  ? 552  SER A O   1 
ATOM   4381 C  CB  . SER A 1 552  ? 67.112 81.301  -31.529 1.00 9.94  ? 552  SER A CB  1 
ATOM   4382 O  OG  . SER A 1 552  ? 68.339 80.931  -30.970 1.00 12.32 ? 552  SER A OG  1 
ATOM   4383 N  N   . LYS A 1 553  ? 65.413 80.842  -29.096 1.00 8.48  ? 553  LYS A N   1 
ATOM   4384 C  CA  . LYS A 1 553  ? 65.140 80.264  -27.795 1.00 7.82  ? 553  LYS A CA  1 
ATOM   4385 C  C   . LYS A 1 553  ? 64.864 78.750  -27.908 1.00 7.05  ? 553  LYS A C   1 
ATOM   4386 O  O   . LYS A 1 553  ? 64.046 78.334  -28.747 1.00 8.14  ? 553  LYS A O   1 
ATOM   4387 C  CB  . LYS A 1 553  ? 63.850 80.925  -27.227 1.00 8.72  ? 553  LYS A CB  1 
ATOM   4388 C  CG  . LYS A 1 553  ? 63.371 80.342  -25.816 1.00 8.59  ? 553  LYS A CG  1 
ATOM   4389 C  CD  . LYS A 1 553  ? 64.409 80.505  -24.784 1.00 9.07  ? 553  LYS A CD  1 
ATOM   4390 C  CE  . LYS A 1 553  ? 64.614 81.962  -24.391 1.00 10.35 ? 553  LYS A CE  1 
ATOM   4391 N  NZ  . LYS A 1 553  ? 65.800 82.078  -23.460 1.00 12.32 ? 553  LYS A NZ  1 
ATOM   4392 N  N   . HIS A 1 554  ? 65.503 77.984  -27.036 1.00 7.88  ? 554  HIS A N   1 
ATOM   4393 C  CA  . HIS A 1 554  ? 65.235 76.564  -26.907 1.00 7.50  ? 554  HIS A CA  1 
ATOM   4394 C  C   . HIS A 1 554  ? 64.031 76.328  -25.994 1.00 6.48  ? 554  HIS A C   1 
ATOM   4395 O  O   . HIS A 1 554  ? 63.899 76.938  -24.953 1.00 8.98  ? 554  HIS A O   1 
ATOM   4396 C  CB  . HIS A 1 554  ? 66.439 75.857  -26.302 1.00 9.53  ? 554  HIS A CB  1 
ATOM   4397 C  CG  . HIS A 1 554  ? 67.581 75.666  -27.249 1.00 10.90 ? 554  HIS A CG  1 
ATOM   4398 N  ND1 . HIS A 1 554  ? 68.113 76.683  -28.013 1.00 16.81 ? 554  HIS A ND1 1 
ATOM   4399 C  CD2 . HIS A 1 554  ? 68.305 74.562  -27.536 1.00 10.60 ? 554  HIS A CD2 1 
ATOM   4400 C  CE1 . HIS A 1 554  ? 69.117 76.211  -28.729 1.00 10.53 ? 554  HIS A CE1 1 
ATOM   4401 N  NE2 . HIS A 1 554  ? 69.248 74.925  -28.460 1.00 19.01 ? 554  HIS A NE2 1 
ATOM   4402 N  N   . VAL A 1 555  ? 63.173 75.412  -26.408 1.00 6.65  ? 555  VAL A N   1 
ATOM   4403 C  CA  . VAL A 1 555  ? 62.046 74.952  -25.609 1.00 7.65  ? 555  VAL A CA  1 
ATOM   4404 C  C   . VAL A 1 555  ? 62.114 73.414  -25.606 1.00 8.00  ? 555  VAL A C   1 
ATOM   4405 O  O   . VAL A 1 555  ? 62.644 72.781  -26.541 1.00 7.92  ? 555  VAL A O   1 
ATOM   4406 C  CB  . VAL A 1 555  ? 60.681 75.417  -26.143 1.00 6.50  ? 555  VAL A CB  1 
ATOM   4407 C  CG1 . VAL A 1 555  ? 60.571 76.940  -26.069 1.00 8.87  ? 555  VAL A CG1 1 
ATOM   4408 C  CG2 . VAL A 1 555  ? 60.433 74.979  -27.571 1.00 7.70  ? 555  VAL A CG2 1 
ATOM   4409 N  N   . VAL A 1 556  ? 61.558 72.800  -24.547 1.00 6.75  ? 556  VAL A N   1 
ATOM   4410 C  CA  . VAL A 1 556  ? 61.612 71.346  -24.439 1.00 6.33  ? 556  VAL A CA  1 
ATOM   4411 C  C   . VAL A 1 556  ? 60.219 70.840  -24.033 1.00 6.11  ? 556  VAL A C   1 
ATOM   4412 O  O   . VAL A 1 556  ? 59.568 71.427  -23.149 1.00 6.60  ? 556  VAL A O   1 
ATOM   4413 C  CB  . VAL A 1 556  ? 62.604 70.938  -23.308 1.00 6.40  ? 556  VAL A CB  1 
ATOM   4414 C  CG1 . VAL A 1 556  ? 62.530 69.416  -23.064 1.00 7.46  ? 556  VAL A CG1 1 
ATOM   4415 C  CG2 . VAL A 1 556  ? 64.050 71.320  -23.648 1.00 8.78  ? 556  VAL A CG2 1 
ATOM   4416 N  N   . MET A 1 557  ? 59.776 69.744  -24.653 1.00 6.18  ? 557  MET A N   1 
ATOM   4417 C  CA  . MET A 1 557  ? 58.528 69.090  -24.257 1.00 6.27  ? 557  MET A CA  1 
ATOM   4418 C  C   . MET A 1 557  ? 58.806 67.746  -23.608 1.00 7.21  ? 557  MET A C   1 
ATOM   4419 O  O   . MET A 1 557  ? 59.701 67.020  -24.027 1.00 7.75  ? 557  MET A O   1 
ATOM   4420 C  CB  . MET A 1 557  ? 57.620 68.809  -25.469 1.00 6.01  ? 557  MET A CB  1 
ATOM   4421 C  CG  . MET A 1 557  ? 56.644 69.974  -25.807 1.00 7.34  ? 557  MET A CG  1 
ATOM   4422 S  SD  . MET A 1 557  ? 57.300 71.616  -25.976 1.00 8.78  ? 557  MET A SD  1 
ATOM   4423 C  CE  . MET A 1 557  ? 58.255 71.629  -27.492 1.00 28.99 ? 557  MET A CE  1 
ATOM   4424 N  N   . HIS A 1 558  ? 58.031 67.458  -22.556 1.00 6.01  ? 558  HIS A N   1 
ATOM   4425 C  CA  . HIS A 1 558  ? 58.077 66.164  -21.888 1.00 5.31  ? 558  HIS A CA  1 
ATOM   4426 C  C   . HIS A 1 558  ? 56.773 65.429  -22.102 1.00 5.76  ? 558  HIS A C   1 
ATOM   4427 O  O   . HIS A 1 558  ? 55.681 66.003  -22.085 1.00 6.71  ? 558  HIS A O   1 
ATOM   4428 C  CB  . HIS A 1 558  ? 58.265 66.355  -20.376 1.00 6.78  ? 558  HIS A CB  1 
ATOM   4429 C  CG  . HIS A 1 558  ? 58.194 65.076  -19.584 1.00 6.02  ? 558  HIS A CG  1 
ATOM   4430 N  ND1 . HIS A 1 558  ? 57.248 64.909  -18.579 1.00 6.93  ? 558  HIS A ND1 1 
ATOM   4431 C  CD2 . HIS A 1 558  ? 58.934 63.934  -19.613 1.00 6.74  ? 558  HIS A CD2 1 
ATOM   4432 C  CE1 . HIS A 1 558  ? 57.442 63.719  -18.011 1.00 6.30  ? 558  HIS A CE1 1 
ATOM   4433 N  NE2 . HIS A 1 558  ? 58.449 63.096  -18.620 1.00 7.36  ? 558  HIS A NE2 1 
ATOM   4434 N  N   . ASN A 1 559  ? 56.915 64.102  -22.350 1.00 5.26  ? 559  ASN A N   1 
ATOM   4435 C  CA  . ASN A 1 559  ? 55.756 63.215  -22.525 1.00 5.69  ? 559  ASN A CA  1 
ATOM   4436 C  C   . ASN A 1 559  ? 55.778 62.129  -21.438 1.00 5.46  ? 559  ASN A C   1 
ATOM   4437 O  O   . ASN A 1 559  ? 56.540 61.176  -21.562 1.00 6.90  ? 559  ASN A O   1 
ATOM   4438 C  CB  . ASN A 1 559  ? 55.838 62.577  -23.914 1.00 6.07  ? 559  ASN A CB  1 
ATOM   4439 C  CG  . ASN A 1 559  ? 54.842 61.484  -24.117 1.00 6.07  ? 559  ASN A CG  1 
ATOM   4440 O  OD1 . ASN A 1 559  ? 53.750 61.488  -23.549 1.00 7.47  ? 559  ASN A OD1 1 
ATOM   4441 N  ND2 . ASN A 1 559  ? 55.213 60.507  -24.984 1.00 7.38  ? 559  ASN A ND2 1 
ATOM   4442 N  N   . THR A 1 560  ? 54.907 62.246  -20.437 1.00 5.51  ? 560  THR A N   1 
ATOM   4443 C  CA  . THR A 1 560  ? 54.924 61.252  -19.353 1.00 5.87  ? 560  THR A CA  1 
ATOM   4444 C  C   . THR A 1 560  ? 54.345 59.886  -19.749 1.00 7.00  ? 560  THR A C   1 
ATOM   4445 O  O   . THR A 1 560  ? 54.527 58.908  -19.018 1.00 7.33  ? 560  THR A O   1 
ATOM   4446 C  CB  . THR A 1 560  ? 54.181 61.864  -18.168 1.00 5.44  ? 560  THR A CB  1 
ATOM   4447 O  OG1 . THR A 1 560  ? 54.467 61.128  -16.935 1.00 6.62  ? 560  THR A OG1 1 
ATOM   4448 C  CG2 . THR A 1 560  ? 52.676 61.916  -18.362 1.00 6.83  ? 560  THR A CG2 1 
ATOM   4449 N  N   . LEU A 1 561  ? 53.606 59.826  -20.843 1.00 6.49  ? 561  LEU A N   1 
ATOM   4450 C  CA  . LEU A 1 561  ? 52.992 58.545  -21.270 1.00 6.69  ? 561  LEU A CA  1 
ATOM   4451 C  C   . LEU A 1 561  ? 53.996 57.638  -21.953 1.00 5.90  ? 561  LEU A C   1 
ATOM   4452 O  O   . LEU A 1 561  ? 54.889 58.090  -22.670 1.00 6.90  ? 561  LEU A O   1 
ATOM   4453 C  CB  . LEU A 1 561  ? 51.885 58.853  -22.265 1.00 6.53  ? 561  LEU A CB  1 
ATOM   4454 C  CG  . LEU A 1 561  ? 50.761 59.756  -21.697 1.00 7.31  ? 561  LEU A CG  1 
ATOM   4455 C  CD1 . LEU A 1 561  ? 49.712 59.935  -22.822 1.00 9.41  ? 561  LEU A CD1 1 
ATOM   4456 C  CD2 . LEU A 1 561  ? 50.075 59.161  -20.437 1.00 8.58  ? 561  LEU A CD2 1 
ATOM   4457 N  N   . PRO A 1 562  ? 53.855 56.329  -21.791 1.00 6.45  ? 562  PRO A N   1 
ATOM   4458 C  CA  . PRO A 1 562  ? 54.805 55.369  -22.376 1.00 6.58  ? 562  PRO A CA  1 
ATOM   4459 C  C   . PRO A 1 562  ? 54.633 54.990  -23.834 1.00 6.70  ? 562  PRO A C   1 
ATOM   4460 O  O   . PRO A 1 562  ? 54.782 53.818  -24.182 1.00 8.10  ? 562  PRO A O   1 
ATOM   4461 C  CB  . PRO A 1 562  ? 54.696 54.168  -21.396 1.00 7.59  ? 562  PRO A CB  1 
ATOM   4462 C  CG  . PRO A 1 562  ? 53.173 54.173  -21.150 1.00 7.14  ? 562  PRO A CG  1 
ATOM   4463 C  CD  . PRO A 1 562  ? 52.882 55.654  -20.886 1.00 6.39  ? 562  PRO A CD  1 
ATOM   4464 N  N   . HIS A 1 563  ? 54.280 55.963  -24.672 1.00 7.35  ? 563  HIS A N   1 
ATOM   4465 C  CA  . HIS A 1 563  ? 54.225 55.713  -26.107 1.00 7.26  ? 563  HIS A CA  1 
ATOM   4466 C  C   . HIS A 1 563  ? 54.616 56.999  -26.784 1.00 7.79  ? 563  HIS A C   1 
ATOM   4467 O  O   . HIS A 1 563  ? 54.468 58.092  -26.204 1.00 8.08  ? 563  HIS A O   1 
ATOM   4468 C  CB  . HIS A 1 563  ? 52.813 55.249  -26.578 1.00 8.44  ? 563  HIS A CB  1 
ATOM   4469 C  CG  . HIS A 1 563  ? 51.682 56.120  -26.130 1.00 8.41  ? 563  HIS A CG  1 
ATOM   4470 N  ND1 . HIS A 1 563  ? 50.874 55.788  -25.061 1.00 8.34  ? 563  HIS A ND1 1 
ATOM   4471 C  CD2 . HIS A 1 563  ? 51.176 57.282  -26.628 1.00 9.29  ? 563  HIS A CD2 1 
ATOM   4472 C  CE1 . HIS A 1 563  ? 49.923 56.693  -24.917 1.00 9.20  ? 563  HIS A CE1 1 
ATOM   4473 N  NE2 . HIS A 1 563  ? 50.090 57.624  -25.846 1.00 9.81  ? 563  HIS A NE2 1 
ATOM   4474 N  N   . TRP A 1 564  ? 55.131 56.904  -27.997 1.00 8.27  ? 564  TRP A N   1 
ATOM   4475 C  CA  . TRP A 1 564  ? 55.463 58.106  -28.776 1.00 6.67  ? 564  TRP A CA  1 
ATOM   4476 C  C   . TRP A 1 564  ? 54.190 58.927  -28.908 1.00 8.85  ? 564  TRP A C   1 
ATOM   4477 O  O   . TRP A 1 564  ? 53.062 58.413  -29.095 1.00 8.72  ? 564  TRP A O   1 
ATOM   4478 C  CB  . TRP A 1 564  ? 55.927 57.701  -30.195 1.00 9.24  ? 564  TRP A CB  1 
ATOM   4479 C  CG  . TRP A 1 564  ? 57.356 57.304  -30.271 1.00 8.64  ? 564  TRP A CG  1 
ATOM   4480 C  CD1 . TRP A 1 564  ? 57.869 56.023  -30.122 1.00 10.47 ? 564  TRP A CD1 1 
ATOM   4481 C  CD2 . TRP A 1 564  ? 58.481 58.174  -30.439 1.00 10.11 ? 564  TRP A CD2 1 
ATOM   4482 N  NE1 . TRP A 1 564  ? 59.228 56.080  -30.187 1.00 11.99 ? 564  TRP A NE1 1 
ATOM   4483 C  CE2 . TRP A 1 564  ? 59.643 57.377  -30.376 1.00 10.42 ? 564  TRP A CE2 1 
ATOM   4484 C  CE3 . TRP A 1 564  ? 58.617 59.566  -30.631 1.00 11.75 ? 564  TRP A CE3 1 
ATOM   4485 C  CZ2 . TRP A 1 564  ? 60.953 57.921  -30.503 1.00 12.44 ? 564  TRP A CZ2 1 
ATOM   4486 C  CZ3 . TRP A 1 564  ? 59.929 60.106  -30.769 1.00 11.46 ? 564  TRP A CZ3 1 
ATOM   4487 C  CH2 . TRP A 1 564  ? 61.054 59.281  -30.699 1.00 13.78 ? 564  TRP A CH2 1 
ATOM   4488 N  N   . ARG A 1 565  ? 54.332 60.246  -28.820 1.00 8.33  ? 565  ARG A N   1 
ATOM   4489 C  CA  . ARG A 1 565  ? 53.128 61.066  -28.882 1.00 9.29  ? 565  ARG A CA  1 
ATOM   4490 C  C   . ARG A 1 565  ? 53.404 62.359  -29.604 1.00 7.88  ? 565  ARG A C   1 
ATOM   4491 O  O   . ARG A 1 565  ? 54.449 62.997  -29.388 1.00 9.30  ? 565  ARG A O   1 
ATOM   4492 C  CB  . ARG A 1 565  ? 52.601 61.382  -27.428 1.00 10.15 ? 565  ARG A CB  1 
ATOM   4493 C  CG  . ARG A 1 565  ? 51.309 62.222  -27.467 1.00 10.67 ? 565  ARG A CG  1 
ATOM   4494 C  CD  . ARG A 1 565  ? 50.458 62.213  -26.141 1.00 14.69 ? 565  ARG A CD  1 
ATOM   4495 N  NE  . ARG A 1 565  ? 51.251 62.495  -24.971 1.00 14.15 ? 565  ARG A NE  1 
ATOM   4496 C  CZ  . ARG A 1 565  ? 50.724 63.040  -23.859 1.00 10.71 ? 565  ARG A CZ  1 
ATOM   4497 N  NH1 . ARG A 1 565  ? 49.416 63.400  -23.802 1.00 10.89 ? 565  ARG A NH1 1 
ATOM   4498 N  NH2 . ARG A 1 565  ? 51.516 63.172  -22.816 1.00 10.33 ? 565  ARG A NH2 1 
ATOM   4499 N  N   . GLU A 1 566  ? 52.475 62.722  -30.475 1.00 9.02  ? 566  GLU A N   1 
ATOM   4500 C  CA  . GLU A 1 566  ? 52.463 64.067  -31.100 1.00 10.28 ? 566  GLU A CA  1 
ATOM   4501 C  C   . GLU A 1 566  ? 51.323 64.869  -30.502 1.00 10.15 ? 566  GLU A C   1 
ATOM   4502 O  O   . GLU A 1 566  ? 50.262 64.356  -30.231 1.00 11.28 ? 566  GLU A O   1 
ATOM   4503 C  CB  . GLU A 1 566  ? 52.201 63.958  -32.592 1.00 12.42 ? 566  GLU A CB  1 
ATOM   4504 C  CG  . GLU A 1 566  ? 53.309 63.352  -33.352 1.00 13.92 ? 566  GLU A CG  1 
ATOM   4505 C  CD  . GLU A 1 566  ? 52.993 63.309  -34.867 1.00 16.59 ? 566  GLU A CD  1 
ATOM   4506 O  OE1 . GLU A 1 566  ? 51.816 63.081  -35.257 1.00 21.77 ? 566  GLU A OE1 1 
ATOM   4507 O  OE2 . GLU A 1 566  ? 53.961 63.500  -35.612 1.00 23.07 ? 566  GLU A OE2 1 
ATOM   4508 N  N   . GLN A 1 567  ? 51.561 66.155  -30.266 1.00 8.59  ? 567  GLN A N   1 
ATOM   4509 C  CA  . GLN A 1 567  ? 50.508 67.037  -29.752 1.00 8.23  ? 567  GLN A CA  1 
ATOM   4510 C  C   . GLN A 1 567  ? 50.875 68.450  -30.170 1.00 8.11  ? 567  GLN A C   1 
ATOM   4511 O  O   . GLN A 1 567  ? 52.086 68.806  -30.212 1.00 8.19  ? 567  GLN A O   1 
ATOM   4512 C  CB  . GLN A 1 567  ? 50.471 66.986  -28.231 1.00 9.46  ? 567  GLN A CB  1 
ATOM   4513 C  CG  . GLN A 1 567  ? 49.310 67.790  -27.624 1.00 9.58  ? 567  GLN A CG  1 
ATOM   4514 C  CD  . GLN A 1 567  ? 49.715 68.249  -26.228 1.00 14.24 ? 567  GLN A CD  1 
ATOM   4515 O  OE1 . GLN A 1 567  ? 49.715 67.452  -25.276 1.00 11.67 ? 567  GLN A OE1 1 
ATOM   4516 N  NE2 . GLN A 1 567  ? 50.155 69.518  -26.099 1.00 15.42 ? 567  GLN A NE2 1 
ATOM   4517 N  N   . LEU A 1 568  ? 49.893 69.241  -30.587 1.00 9.39  ? 568  LEU A N   1 
ATOM   4518 C  CA  . LEU A 1 568  ? 50.234 70.658  -30.838 1.00 8.17  ? 568  LEU A CA  1 
ATOM   4519 C  C   . LEU A 1 568  ? 50.551 71.354  -29.531 1.00 8.18  ? 568  LEU A C   1 
ATOM   4520 O  O   . LEU A 1 568  ? 49.899 71.104  -28.465 1.00 9.24  ? 568  LEU A O   1 
ATOM   4521 C  CB  . LEU A 1 568  ? 49.068 71.441  -31.458 1.00 11.00 ? 568  LEU A CB  1 
ATOM   4522 C  CG  . LEU A 1 568  ? 48.574 71.008  -32.837 1.00 11.61 ? 568  LEU A CG  1 
ATOM   4523 C  CD1 . LEU A 1 568  ? 47.664 72.121  -33.415 1.00 13.67 ? 568  LEU A CD1 1 
ATOM   4524 C  CD2 . LEU A 1 568  ? 49.725 70.858  -33.768 1.00 14.06 ? 568  LEU A CD2 1 
ATOM   4525 N  N   . VAL A 1 569  ? 51.538 72.209  -29.551 1.00 7.59  ? 569  VAL A N   1 
ATOM   4526 C  CA  . VAL A 1 569  ? 51.926 72.999  -28.389 1.00 8.30  ? 569  VAL A CA  1 
ATOM   4527 C  C   . VAL A 1 569  ? 52.005 74.451  -28.811 1.00 8.41  ? 569  VAL A C   1 
ATOM   4528 O  O   . VAL A 1 569  ? 52.264 74.774  -29.988 1.00 9.70  ? 569  VAL A O   1 
ATOM   4529 C  CB  . VAL A 1 569  ? 53.319 72.593  -27.800 1.00 7.33  ? 569  VAL A CB  1 
ATOM   4530 C  CG1 . VAL A 1 569  ? 53.200 71.175  -27.157 1.00 10.19 ? 569  VAL A CG1 1 
ATOM   4531 C  CG2 . VAL A 1 569  ? 54.424 72.597  -28.919 1.00 8.67  ? 569  VAL A CG2 1 
ATOM   4532 N  N   . ASP A 1 570  ? 51.745 75.341  -27.877 1.00 8.23  ? 570  ASP A N   1 
ATOM   4533 C  CA  . ASP A 1 570  ? 51.812 76.770  -28.200 1.00 9.42  ? 570  ASP A CA  1 
ATOM   4534 C  C   . ASP A 1 570  ? 52.634 77.519  -27.185 1.00 10.59 ? 570  ASP A C   1 
ATOM   4535 O  O   . ASP A 1 570  ? 52.715 77.160  -25.989 1.00 11.44 ? 570  ASP A O   1 
ATOM   4536 C  CB  . ASP A 1 570  ? 50.416 77.386  -28.348 1.00 10.76 ? 570  ASP A CB  1 
ATOM   4537 C  CG  . ASP A 1 570  ? 49.694 77.503  -27.043 1.00 16.84 ? 570  ASP A CG  1 
ATOM   4538 O  OD1 . ASP A 1 570  ? 49.610 76.512  -26.306 1.00 22.55 ? 570  ASP A OD1 1 
ATOM   4539 O  OD2 . ASP A 1 570  ? 49.201 78.588  -26.724 1.00 24.60 ? 570  ASP A OD2 1 
ATOM   4540 N  N   . PHE A 1 571  ? 53.261 78.597  -27.652 1.00 8.01  ? 571  PHE A N   1 
ATOM   4541 C  CA  . PHE A 1 571  ? 54.055 79.485  -26.790 1.00 9.00  ? 571  PHE A CA  1 
ATOM   4542 C  C   . PHE A 1 571  ? 53.706 80.941  -27.186 1.00 8.54  ? 571  PHE A C   1 
ATOM   4543 O  O   . PHE A 1 571  ? 53.369 81.195  -28.338 1.00 10.12 ? 571  PHE A O   1 
ATOM   4544 C  CB  . PHE A 1 571  ? 55.577 79.309  -27.036 1.00 9.32  ? 571  PHE A CB  1 
ATOM   4545 C  CG  . PHE A 1 571  ? 56.080 77.944  -26.644 1.00 6.90  ? 571  PHE A CG  1 
ATOM   4546 C  CD1 . PHE A 1 571  ? 56.067 76.871  -27.525 1.00 8.36  ? 571  PHE A CD1 1 
ATOM   4547 C  CD2 . PHE A 1 571  ? 56.525 77.783  -25.347 1.00 8.75  ? 571  PHE A CD2 1 
ATOM   4548 C  CE1 . PHE A 1 571  ? 56.510 75.603  -27.077 1.00 9.08  ? 571  PHE A CE1 1 
ATOM   4549 C  CE2 . PHE A 1 571  ? 56.957 76.529  -24.892 1.00 8.53  ? 571  PHE A CE2 1 
ATOM   4550 C  CZ  . PHE A 1 571  ? 56.949 75.436  -25.774 1.00 9.16  ? 571  PHE A CZ  1 
ATOM   4551 N  N   . TYR A 1 572  ? 53.824 81.838  -26.221 1.00 7.75  ? 572  TYR A N   1 
ATOM   4552 C  CA  . TYR A 1 572  ? 53.694 83.273  -26.523 1.00 8.31  ? 572  TYR A CA  1 
ATOM   4553 C  C   . TYR A 1 572  ? 55.086 83.746  -26.927 1.00 10.20 ? 572  TYR A C   1 
ATOM   4554 O  O   . TYR A 1 572  ? 56.075 83.449  -26.262 1.00 9.18  ? 572  TYR A O   1 
ATOM   4555 C  CB  . TYR A 1 572  ? 53.254 84.054  -25.282 1.00 10.64 ? 572  TYR A CB  1 
ATOM   4556 C  CG  . TYR A 1 572  ? 51.818 83.912  -24.855 1.00 12.23 ? 572  TYR A CG  1 
ATOM   4557 C  CD1 . TYR A 1 572  ? 50.867 83.249  -25.613 1.00 11.64 ? 572  TYR A CD1 1 
ATOM   4558 C  CD2 . TYR A 1 572  ? 51.423 84.473  -23.653 1.00 22.54 ? 572  TYR A CD2 1 
ATOM   4559 C  CE1 . TYR A 1 572  ? 49.529 83.148  -25.189 1.00 13.12 ? 572  TYR A CE1 1 
ATOM   4560 C  CE2 . TYR A 1 572  ? 50.107 84.391  -23.229 1.00 22.07 ? 572  TYR A CE2 1 
ATOM   4561 C  CZ  . TYR A 1 572  ? 49.182 83.742  -24.000 1.00 18.76 ? 572  TYR A CZ  1 
ATOM   4562 O  OH  . TYR A 1 572  ? 47.856 83.741  -23.560 1.00 19.38 ? 572  TYR A OH  1 
ATOM   4563 N  N   . VAL A 1 573  ? 55.130 84.574  -27.959 1.00 9.30  ? 573  VAL A N   1 
ATOM   4564 C  CA  . VAL A 1 573  ? 56.384 85.145  -28.515 1.00 9.33  ? 573  VAL A CA  1 
ATOM   4565 C  C   . VAL A 1 573  ? 56.166 86.618  -28.815 1.00 8.97  ? 573  VAL A C   1 
ATOM   4566 O  O   . VAL A 1 573  ? 55.038 87.052  -29.109 1.00 10.51 ? 573  VAL A O   1 
ATOM   4567 C  CB  . VAL A 1 573  ? 56.843 84.415  -29.772 1.00 9.52  ? 573  VAL A CB  1 
ATOM   4568 C  CG1 . VAL A 1 573  ? 57.340 83.013  -29.443 1.00 12.83 ? 573  VAL A CG1 1 
ATOM   4569 C  CG2 . VAL A 1 573  ? 55.748 84.305  -30.790 1.00 12.82 ? 573  VAL A CG2 1 
ATOM   4570 N  N   . SER A 1 574  ? 57.268 87.376  -28.765 1.00 9.66  ? 574  SER A N   1 
ATOM   4571 C  CA  . SER A 1 574  ? 57.158 88.842  -28.943 1.00 9.93  ? 574  SER A CA  1 
ATOM   4572 C  C   . SER A 1 574  ? 57.186 89.326  -30.375 1.00 11.74 ? 574  SER A C   1 
ATOM   4573 O  O   . SER A 1 574  ? 57.184 90.564  -30.581 1.00 16.10 ? 574  SER A O   1 
ATOM   4574 C  CB  . SER A 1 574  ? 58.258 89.513  -28.164 1.00 12.93 ? 574  SER A CB  1 
ATOM   4575 O  OG  . SER A 1 574  ? 59.552 89.170  -28.651 1.00 11.90 ? 574  SER A OG  1 
ATOM   4576 N  N   . SER A 1 575  ? 57.179 88.436  -31.352 1.00 12.13 ? 575  SER A N   1 
ATOM   4577 C  CA  . SER A 1 575  ? 57.105 88.767  -32.763 1.00 13.36 ? 575  SER A CA  1 
ATOM   4578 C  C   . SER A 1 575  ? 56.310 87.729  -33.487 1.00 13.91 ? 575  SER A C   1 
ATOM   4579 O  O   . SER A 1 575  ? 56.332 86.547  -33.091 1.00 12.58 ? 575  SER A O   1 
ATOM   4580 C  CB  . SER A 1 575  ? 58.523 88.737  -33.369 1.00 15.68 ? 575  SER A CB  1 
ATOM   4581 O  OG  . SER A 1 575  ? 58.521 88.840  -34.788 1.00 14.34 ? 575  SER A OG  1 
ATOM   4582 N  N   . PRO A 1 576  ? 55.603 88.108  -34.552 1.00 13.33 ? 576  PRO A N   1 
ATOM   4583 C  CA  . PRO A 1 576  ? 54.861 87.098  -35.297 1.00 11.58 ? 576  PRO A CA  1 
ATOM   4584 C  C   . PRO A 1 576  ? 55.791 86.373  -36.297 1.00 10.81 ? 576  PRO A C   1 
ATOM   4585 O  O   . PRO A 1 576  ? 55.410 85.370  -36.905 1.00 12.77 ? 576  PRO A O   1 
ATOM   4586 C  CB  . PRO A 1 576  ? 53.783 87.892  -36.044 1.00 14.57 ? 576  PRO A CB  1 
ATOM   4587 C  CG  . PRO A 1 576  ? 54.482 89.269  -36.234 1.00 17.91 ? 576  PRO A CG  1 
ATOM   4588 C  CD  . PRO A 1 576  ? 55.357 89.485  -35.046 1.00 14.08 ? 576  PRO A CD  1 
ATOM   4589 N  N   . PHE A 1 577  ? 57.029 86.883  -36.496 1.00 11.60 ? 577  PHE A N   1 
ATOM   4590 C  CA  . PHE A 1 577  ? 57.913 86.320  -37.513 1.00 11.70 ? 577  PHE A CA  1 
ATOM   4591 C  C   . PHE A 1 577  ? 58.888 85.369  -36.855 1.00 12.85 ? 577  PHE A C   1 
ATOM   4592 O  O   . PHE A 1 577  ? 60.036 85.684  -36.626 1.00 13.32 ? 577  PHE A O   1 
ATOM   4593 C  CB  . PHE A 1 577  ? 58.650 87.461  -38.244 1.00 13.41 ? 577  PHE A CB  1 
ATOM   4594 C  CG  . PHE A 1 577  ? 57.722 88.471  -38.837 1.00 16.80 ? 577  PHE A CG  1 
ATOM   4595 C  CD1 . PHE A 1 577  ? 56.686 88.053  -39.635 1.00 14.77 ? 577  PHE A CD1 1 
ATOM   4596 C  CD2 . PHE A 1 577  ? 57.924 89.821  -38.616 1.00 22.01 ? 577  PHE A CD2 1 
ATOM   4597 C  CE1 . PHE A 1 577  ? 55.830 88.981  -40.242 1.00 20.35 ? 577  PHE A CE1 1 
ATOM   4598 C  CE2 . PHE A 1 577  ? 57.073 90.764  -39.215 1.00 24.74 ? 577  PHE A CE2 1 
ATOM   4599 C  CZ  . PHE A 1 577  ? 56.046 90.335  -40.016 1.00 21.01 ? 577  PHE A CZ  1 
ATOM   4600 N  N   . VAL A 1 578  ? 58.363 84.182  -36.563 1.00 11.17 ? 578  VAL A N   1 
ATOM   4601 C  CA  . VAL A 1 578  ? 59.135 83.166  -35.821 1.00 11.87 ? 578  VAL A CA  1 
ATOM   4602 C  C   . VAL A 1 578  ? 58.988 81.830  -36.523 1.00 11.88 ? 578  VAL A C   1 
ATOM   4603 O  O   . VAL A 1 578  ? 57.951 81.513  -37.060 1.00 12.05 ? 578  VAL A O   1 
ATOM   4604 C  CB  . VAL A 1 578  ? 58.585 83.064  -34.361 1.00 12.37 ? 578  VAL A CB  1 
ATOM   4605 C  CG1 . VAL A 1 578  ? 59.320 81.926  -33.573 1.00 12.63 ? 578  VAL A CG1 1 
ATOM   4606 C  CG2 . VAL A 1 578  ? 58.827 84.333  -33.630 1.00 12.49 ? 578  VAL A CG2 1 
ATOM   4607 N  N   . SER A 1 579  ? 60.113 81.131  -36.597 1.00 12.99 ? 579  SER A N   1 
ATOM   4608 C  CA  . SER A 1 579  ? 60.065 79.810  -37.181 1.00 13.66 ? 579  SER A CA  1 
ATOM   4609 C  C   . SER A 1 579  ? 60.610 78.779  -36.197 1.00 10.01 ? 579  SER A C   1 
ATOM   4610 O  O   . SER A 1 579  ? 61.394 79.092  -35.302 1.00 11.28 ? 579  SER A O   1 
ATOM   4611 C  CB  . SER A 1 579  ? 60.734 79.725  -38.534 1.00 21.06 ? 579  SER A CB  1 
ATOM   4612 O  OG  . SER A 1 579  ? 61.971 80.280  -38.467 1.00 23.97 ? 579  SER A OG  1 
ATOM   4613 N  N   . VAL A 1 580  ? 60.194 77.564  -36.431 1.00 8.45  ? 580  VAL A N   1 
ATOM   4614 C  CA  . VAL A 1 580  ? 60.545 76.470  -35.533 1.00 8.17  ? 580  VAL A CA  1 
ATOM   4615 C  C   . VAL A 1 580  ? 61.421 75.451  -36.254 1.00 8.96  ? 580  VAL A C   1 
ATOM   4616 O  O   . VAL A 1 580  ? 61.160 75.081  -37.413 1.00 10.28 ? 580  VAL A O   1 
ATOM   4617 C  CB  . VAL A 1 580  ? 59.277 75.777  -35.049 1.00 8.06  ? 580  VAL A CB  1 
ATOM   4618 C  CG1 . VAL A 1 580  ? 59.610 74.633  -34.064 1.00 9.95  ? 580  VAL A CG1 1 
ATOM   4619 C  CG2 . VAL A 1 580  ? 58.310 76.802  -34.386 1.00 10.14 ? 580  VAL A CG2 1 
ATOM   4620 N  N   . THR A 1 581  ? 62.396 74.963  -35.510 1.00 8.35  ? 581  THR A N   1 
ATOM   4621 C  CA  . THR A 1 581  ? 63.261 73.864  -35.981 1.00 8.57  ? 581  THR A CA  1 
ATOM   4622 C  C   . THR A 1 581  ? 63.448 72.844  -34.841 1.00 9.71  ? 581  THR A C   1 
ATOM   4623 O  O   . THR A 1 581  ? 63.243 73.143  -33.637 1.00 9.56  ? 581  THR A O   1 
ATOM   4624 C  CB  . THR A 1 581  ? 64.679 74.357  -36.384 1.00 9.89  ? 581  THR A CB  1 
ATOM   4625 O  OG1 . THR A 1 581  ? 65.220 75.244  -35.402 1.00 12.60 ? 581  THR A OG1 1 
ATOM   4626 C  CG2 . THR A 1 581  ? 64.589 75.150  -37.732 1.00 11.14 ? 581  THR A CG2 1 
ATOM   4627 N  N   . ASP A 1 582  ? 63.738 71.595  -35.206 1.00 10.94 ? 582  ASP A N   1 
ATOM   4628 C  CA  . ASP A 1 582  ? 64.177 70.567  -34.230 1.00 12.58 ? 582  ASP A CA  1 
ATOM   4629 C  C   . ASP A 1 582  ? 65.689 70.687  -33.977 1.00 11.93 ? 582  ASP A C   1 
ATOM   4630 O  O   . ASP A 1 582  ? 66.296 71.569  -34.526 1.00 14.36 ? 582  ASP A O   1 
ATOM   4631 C  CB  . ASP A 1 582  ? 63.728 69.139  -34.598 1.00 17.09 ? 582  ASP A CB  1 
ATOM   4632 C  CG  . ASP A 1 582  ? 64.360 68.603  -35.878 1.00 14.45 ? 582  ASP A CG  1 
ATOM   4633 O  OD1 . ASP A 1 582  ? 65.403 69.098  -36.298 1.00 15.23 ? 582  ASP A OD1 1 
ATOM   4634 O  OD2 . ASP A 1 582  ? 63.782 67.672  -36.430 1.00 19.01 ? 582  ASP A OD2 1 
ATOM   4635 N  N   . LEU A 1 583  ? 66.303 69.872  -33.109 1.00 21.15 ? 583  LEU A N   1 
ATOM   4636 C  CA  . LEU A 1 583  ? 67.726 70.168  -32.896 1.00 23.25 ? 583  LEU A CA  1 
ATOM   4637 C  C   . LEU A 1 583  ? 68.659 69.620  -33.981 1.00 23.88 ? 583  LEU A C   1 
ATOM   4638 O  O   . LEU A 1 583  ? 69.876 69.740  -33.839 1.00 26.87 ? 583  LEU A O   1 
ATOM   4639 C  CB  . LEU A 1 583  ? 68.203 69.773  -31.458 1.00 22.20 ? 583  LEU A CB  1 
ATOM   4640 C  CG  . LEU A 1 583  ? 69.083 70.806  -30.698 1.00 20.05 ? 583  LEU A CG  1 
ATOM   4641 C  CD1 . LEU A 1 583  ? 68.352 72.104  -30.654 1.00 25.91 ? 583  LEU A CD1 1 
ATOM   4642 C  CD2 . LEU A 1 583  ? 69.475 70.401  -29.232 1.00 22.06 ? 583  LEU A CD2 1 
ATOM   4643 N  N   . ALA A 1 584  ? 68.088 69.047  -35.066 1.00 18.47 ? 584  ALA A N   1 
ATOM   4644 C  CA  . ALA A 1 584  ? 68.928 68.675  -36.219 1.00 13.93 ? 584  ALA A CA  1 
ATOM   4645 C  C   . ALA A 1 584  ? 68.705 69.775  -37.217 1.00 12.96 ? 584  ALA A C   1 
ATOM   4646 O  O   . ALA A 1 584  ? 69.105 69.696  -38.395 1.00 12.86 ? 584  ALA A O   1 
ATOM   4647 C  CB  . ALA A 1 584  ? 68.518 67.377  -36.834 1.00 15.94 ? 584  ALA A CB  1 
ATOM   4648 N  N   . ASN A 1 585  ? 68.065 70.858  -36.775 1.00 12.74 ? 585  ASN A N   1 
ATOM   4649 C  CA  . ASN A 1 585  ? 67.798 71.978  -37.636 1.00 12.06 ? 585  ASN A CA  1 
ATOM   4650 C  C   . ASN A 1 585  ? 66.832 71.770  -38.771 1.00 12.07 ? 585  ASN A C   1 
ATOM   4651 O  O   . ASN A 1 585  ? 66.820 72.559  -39.758 1.00 16.53 ? 585  ASN A O   1 
ATOM   4652 C  CB  . ASN A 1 585  ? 69.072 72.621  -38.160 1.00 16.74 ? 585  ASN A CB  1 
ATOM   4653 C  CG  . ASN A 1 585  ? 69.270 73.940  -37.550 1.00 30.86 ? 585  ASN A CG  1 
ATOM   4654 O  OD1 . ASN A 1 585  ? 68.549 74.929  -37.872 1.00 24.03 ? 585  ASN A OD1 1 
ATOM   4655 N  ND2 . ASN A 1 585  ? 70.174 73.983  -36.575 1.00 31.49 ? 585  ASN A ND2 1 
ATOM   4656 N  N   . ASN A 1 586  ? 66.000 70.749  -38.672 1.00 9.50  ? 586  ASN A N   1 
ATOM   4657 C  CA  . ASN A 1 586  ? 64.966 70.465  -39.673 1.00 12.24 ? 586  ASN A CA  1 
ATOM   4658 C  C   . ASN A 1 586  ? 63.791 71.431  -39.366 1.00 12.92 ? 586  ASN A C   1 
ATOM   4659 O  O   . ASN A 1 586  ? 63.364 71.582  -38.213 1.00 11.82 ? 586  ASN A O   1 
ATOM   4660 C  CB  . ASN A 1 586  ? 64.383 69.070  -39.518 1.00 14.34 ? 586  ASN A CB  1 
ATOM   4661 C  CG  . ASN A 1 586  ? 65.433 67.962  -39.581 1.00 17.38 ? 586  ASN A CG  1 
ATOM   4662 O  OD1 . ASN A 1 586  ? 66.277 67.999  -40.456 1.00 18.36 ? 586  ASN A OD1 1 
ATOM   4663 N  ND2 . ASN A 1 586  ? 65.375 66.977  -38.659 1.00 16.06 ? 586  ASN A ND2 1 
ATOM   4664 N  N   . PRO A 1 587  ? 63.249 72.081  -40.377 1.00 11.98 ? 587  PRO A N   1 
ATOM   4665 C  CA  . PRO A 1 587  ? 62.114 72.991  -40.176 1.00 11.00 ? 587  PRO A CA  1 
ATOM   4666 C  C   . PRO A 1 587  ? 60.899 72.200  -39.727 1.00 11.00 ? 587  PRO A C   1 
ATOM   4667 O  O   . PRO A 1 587  ? 60.671 71.029  -40.103 1.00 13.20 ? 587  PRO A O   1 
ATOM   4668 C  CB  . PRO A 1 587  ? 61.897 73.640  -41.561 1.00 14.60 ? 587  PRO A CB  1 
ATOM   4669 C  CG  . PRO A 1 587  ? 62.562 72.678  -42.523 1.00 22.14 ? 587  PRO A CG  1 
ATOM   4670 C  CD  . PRO A 1 587  ? 63.768 72.097  -41.765 1.00 14.20 ? 587  PRO A CD  1 
ATOM   4671 N  N   . VAL A 1 588  ? 60.086 72.855  -38.882 1.00 10.15 ? 588  VAL A N   1 
ATOM   4672 C  CA  . VAL A 1 588  ? 58.857 72.265  -38.370 1.00 10.11 ? 588  VAL A CA  1 
ATOM   4673 C  C   . VAL A 1 588  ? 57.739 73.266  -38.744 1.00 10.25 ? 588  VAL A C   1 
ATOM   4674 O  O   . VAL A 1 588  ? 57.884 74.472  -38.507 1.00 11.13 ? 588  VAL A O   1 
ATOM   4675 C  CB  . VAL A 1 588  ? 58.917 72.159  -36.825 1.00 10.54 ? 588  VAL A CB  1 
ATOM   4676 C  CG1 . VAL A 1 588  ? 57.619 71.654  -36.298 1.00 12.63 ? 588  VAL A CG1 1 
ATOM   4677 C  CG2 . VAL A 1 588  ? 60.061 71.161  -36.403 1.00 12.28 ? 588  VAL A CG2 1 
ATOM   4678 N  N   . GLU A 1 589  ? 56.692 72.757  -39.370 1.00 10.75 ? 589  GLU A N   1 
ATOM   4679 C  CA  . GLU A 1 589  ? 55.570 73.625  -39.781 1.00 10.55 ? 589  GLU A CA  1 
ATOM   4680 C  C   . GLU A 1 589  ? 54.923 74.284  -38.556 1.00 10.61 ? 589  GLU A C   1 
ATOM   4681 O  O   . GLU A 1 589  ? 54.689 73.584  -37.514 1.00 11.84 ? 589  GLU A O   1 
ATOM   4682 C  CB  . GLU A 1 589  ? 54.519 72.804  -40.515 1.00 13.44 ? 589  GLU A CB  1 
ATOM   4683 C  CG  . GLU A 1 589  ? 53.414 73.728  -41.073 1.00 22.90 ? 589  GLU A CG  1 
ATOM   4684 C  CD  . GLU A 1 589  ? 52.267 73.018  -41.793 1.00 31.63 ? 589  GLU A CD  1 
ATOM   4685 O  OE1 . GLU A 1 589  ? 52.391 71.804  -42.060 1.00 32.46 ? 589  GLU A OE1 1 
ATOM   4686 O  OE2 . GLU A 1 589  ? 51.222 73.691  -42.088 1.00 29.23 ? 589  GLU A OE2 1 
ATOM   4687 N  N   . ALA A 1 590  ? 54.664 75.573  -38.613 1.00 9.17  ? 590  ALA A N   1 
ATOM   4688 C  CA  . ALA A 1 590  ? 54.109 76.273  -37.469 1.00 9.01  ? 590  ALA A CA  1 
ATOM   4689 C  C   . ALA A 1 590  ? 52.990 77.195  -37.917 1.00 10.69 ? 590  ALA A C   1 
ATOM   4690 O  O   . ALA A 1 590  ? 52.900 77.524  -39.140 1.00 10.77 ? 590  ALA A O   1 
ATOM   4691 C  CB  . ALA A 1 590  ? 55.173 77.102  -36.764 1.00 10.65 ? 590  ALA A CB  1 
ATOM   4692 N  N   . GLN A 1 591  ? 52.165 77.621  -36.979 1.00 9.78  ? 591  GLN A N   1 
ATOM   4693 C  CA  . GLN A 1 591  ? 51.080 78.575  -37.239 1.00 8.15  ? 591  GLN A CA  1 
ATOM   4694 C  C   . GLN A 1 591  ? 51.174 79.648  -36.187 1.00 8.93  ? 591  GLN A C   1 
ATOM   4695 O  O   . GLN A 1 591  ? 51.411 79.371  -34.995 1.00 10.38 ? 591  GLN A O   1 
ATOM   4696 C  CB  . GLN A 1 591  ? 49.716 77.886  -37.128 1.00 8.95  ? 591  GLN A CB  1 
ATOM   4697 C  CG  . GLN A 1 591  ? 48.550 78.909  -37.180 1.00 9.40  ? 591  GLN A CG  1 
ATOM   4698 C  CD  . GLN A 1 591  ? 47.212 78.184  -36.989 1.00 9.76  ? 591  GLN A CD  1 
ATOM   4699 O  OE1 . GLN A 1 591  ? 46.983 77.108  -37.550 1.00 10.41 ? 591  GLN A OE1 1 
ATOM   4700 N  NE2 . GLN A 1 591  ? 46.332 78.745  -36.162 1.00 10.97 ? 591  GLN A NE2 1 
ATOM   4701 N  N   . VAL A 1 592  ? 51.036 80.929  -36.559 1.00 9.08  ? 592  VAL A N   1 
ATOM   4702 C  CA  . VAL A 1 592  ? 50.989 82.033  -35.603 1.00 9.50  ? 592  VAL A CA  1 
ATOM   4703 C  C   . VAL A 1 592  ? 49.569 82.566  -35.634 1.00 8.33  ? 592  VAL A C   1 
ATOM   4704 O  O   . VAL A 1 592  ? 48.939 82.646  -36.708 1.00 10.79 ? 592  VAL A O   1 
ATOM   4705 C  CB  . VAL A 1 592  ? 52.047 83.111  -35.985 1.00 9.02  ? 592  VAL A CB  1 
ATOM   4706 C  CG1 . VAL A 1 592  ? 51.848 84.375  -35.169 1.00 11.57 ? 592  VAL A CG1 1 
ATOM   4707 C  CG2 . VAL A 1 592  ? 53.442 82.581  -35.678 1.00 10.72 ? 592  VAL A CG2 1 
ATOM   4708 N  N   . SER A 1 593  ? 49.040 82.803  -34.440 1.00 11.05 ? 593  SER A N   1 
ATOM   4709 C  CA  . SER A 1 593  ? 47.699 83.345  -34.203 1.00 10.74 ? 593  SER A CA  1 
ATOM   4710 C  C   . SER A 1 593  ? 47.852 84.521  -33.262 1.00 10.37 ? 593  SER A C   1 
ATOM   4711 O  O   . SER A 1 593  ? 48.845 84.621  -32.558 1.00 12.15 ? 593  SER A O   1 
ATOM   4712 C  CB  . SER A 1 593  ? 46.825 82.289  -33.510 1.00 12.31 ? 593  SER A CB  1 
ATOM   4713 O  OG  . SER A 1 593  ? 46.505 81.208  -34.368 1.00 13.07 ? 593  SER A OG  1 
ATOM   4714 N  N   . PRO A 1 594  ? 46.871 85.414  -33.207 1.00 10.50 ? 594  PRO A N   1 
ATOM   4715 C  CA  . PRO A 1 594  ? 46.975 86.492  -32.215 1.00 10.02 ? 594  PRO A CA  1 
ATOM   4716 C  C   . PRO A 1 594  ? 46.735 86.029  -30.767 1.00 9.58  ? 594  PRO A C   1 
ATOM   4717 O  O   . PRO A 1 594  ? 46.291 84.868  -30.530 1.00 10.50 ? 594  PRO A O   1 
ATOM   4718 C  CB  . PRO A 1 594  ? 45.833 87.458  -32.605 1.00 11.29 ? 594  PRO A CB  1 
ATOM   4719 C  CG  . PRO A 1 594  ? 45.425 87.010  -34.007 1.00 11.06 ? 594  PRO A CG  1 
ATOM   4720 C  CD  . PRO A 1 594  ? 45.664 85.558  -34.056 1.00 9.63  ? 594  PRO A CD  1 
ATOM   4721 N  N   . VAL A 1 595  ? 47.048 86.873  -29.781 1.00 9.74  ? 595  VAL A N   1 
ATOM   4722 C  CA  . VAL A 1 595  ? 46.702 86.558  -28.415 1.00 10.55 ? 595  VAL A CA  1 
ATOM   4723 C  C   . VAL A 1 595  ? 45.433 87.371  -28.149 1.00 10.19 ? 595  VAL A C   1 
ATOM   4724 O  O   . VAL A 1 595  ? 45.441 88.616  -28.225 1.00 12.13 ? 595  VAL A O   1 
ATOM   4725 C  CB  . VAL A 1 595  ? 47.800 86.959  -27.408 1.00 11.09 ? 595  VAL A CB  1 
ATOM   4726 C  CG1 . VAL A 1 595  ? 47.257 86.820  -25.987 1.00 12.64 ? 595  VAL A CG1 1 
ATOM   4727 C  CG2 . VAL A 1 595  ? 49.025 86.067  -27.650 1.00 11.66 ? 595  VAL A CG2 1 
ATOM   4728 N  N   . TRP A 1 596  ? 44.337 86.662  -27.906 1.00 10.68 ? 596  TRP A N   1 
ATOM   4729 C  CA  . TRP A 1 596  ? 43.021 87.267  -27.741 1.00 10.81 ? 596  TRP A CA  1 
ATOM   4730 C  C   . TRP A 1 596  ? 42.623 87.172  -26.271 1.00 11.38 ? 596  TRP A C   1 
ATOM   4731 O  O   . TRP A 1 596  ? 42.659 86.103  -25.689 1.00 15.12 ? 596  TRP A O   1 
ATOM   4732 C  CB  . TRP A 1 596  ? 41.990 86.499  -28.577 1.00 10.47 ? 596  TRP A CB  1 
ATOM   4733 C  CG  . TRP A 1 596  ? 42.102 86.691  -30.055 1.00 10.78 ? 596  TRP A CG  1 
ATOM   4734 C  CD1 . TRP A 1 596  ? 42.503 85.771  -30.975 1.00 9.59  ? 596  TRP A CD1 1 
ATOM   4735 C  CD2 . TRP A 1 596  ? 41.782 87.875  -30.786 1.00 10.07 ? 596  TRP A CD2 1 
ATOM   4736 N  NE1 . TRP A 1 596  ? 42.458 86.311  -32.233 1.00 11.70 ? 596  TRP A NE1 1 
ATOM   4737 C  CE2 . TRP A 1 596  ? 42.021 87.604  -32.141 1.00 11.42 ? 596  TRP A CE2 1 
ATOM   4738 C  CE3 . TRP A 1 596  ? 41.321 89.141  -30.422 1.00 10.67 ? 596  TRP A CE3 1 
ATOM   4739 C  CZ2 . TRP A 1 596  ? 41.813 88.550  -33.132 1.00 12.34 ? 596  TRP A CZ2 1 
ATOM   4740 C  CZ3 . TRP A 1 596  ? 41.122 90.077  -31.407 1.00 11.42 ? 596  TRP A CZ3 1 
ATOM   4741 C  CH2 . TRP A 1 596  ? 41.362 89.776  -32.744 1.00 13.44 ? 596  TRP A CH2 1 
ATOM   4742 N  N   . SER A 1 597  ? 42.228 88.289  -25.683 1.00 12.02 ? 597  SER A N   1 
ATOM   4743 C  CA  . SER A 1 597  ? 41.725 88.298  -24.320 1.00 14.59 ? 597  SER A CA  1 
ATOM   4744 C  C   . SER A 1 597  ? 40.326 88.894  -24.273 1.00 17.49 ? 597  SER A C   1 
ATOM   4745 O  O   . SER A 1 597  ? 40.048 89.904  -24.917 1.00 19.44 ? 597  SER A O   1 
ATOM   4746 C  CB  A SER A 1 597  ? 42.644 88.993  -23.317 0.50 21.03 ? 597  SER A CB  1 
ATOM   4747 C  CB  B SER A 1 597  ? 42.542 89.254  -23.450 0.50 22.19 ? 597  SER A CB  1 
ATOM   4748 O  OG  A SER A 1 597  ? 42.605 90.359  -23.631 0.50 25.45 ? 597  SER A OG  1 
ATOM   4749 O  OG  B SER A 1 597  ? 43.925 89.086  -23.677 0.50 34.87 ? 597  SER A OG  1 
ATOM   4750 N  N   . TRP A 1 598  ? 39.451 88.266  -23.503 1.00 13.13 ? 598  TRP A N   1 
ATOM   4751 C  CA  . TRP A 1 598  ? 38.057 88.681  -23.450 1.00 11.75 ? 598  TRP A CA  1 
ATOM   4752 C  C   . TRP A 1 598  ? 37.811 89.578  -22.256 1.00 13.52 ? 598  TRP A C   1 
ATOM   4753 O  O   . TRP A 1 598  ? 38.342 89.361  -21.181 1.00 18.25 ? 598  TRP A O   1 
ATOM   4754 C  CB  . TRP A 1 598  ? 37.124 87.470  -23.388 1.00 13.42 ? 598  TRP A CB  1 
ATOM   4755 C  CG  . TRP A 1 598  ? 37.053 86.731  -24.671 1.00 11.20 ? 598  TRP A CG  1 
ATOM   4756 C  CD1 . TRP A 1 598  ? 37.957 85.839  -25.145 1.00 12.01 ? 598  TRP A CD1 1 
ATOM   4757 C  CD2 . TRP A 1 598  ? 36.030 86.831  -25.659 1.00 10.50 ? 598  TRP A CD2 1 
ATOM   4758 N  NE1 . TRP A 1 598  ? 37.562 85.366  -26.365 1.00 11.50 ? 598  TRP A NE1 1 
ATOM   4759 C  CE2 . TRP A 1 598  ? 36.377 85.958  -26.704 1.00 9.69  ? 598  TRP A CE2 1 
ATOM   4760 C  CE3 . TRP A 1 598  ? 34.842 87.560  -25.755 1.00 11.46 ? 598  TRP A CE3 1 
ATOM   4761 C  CZ2 . TRP A 1 598  ? 35.587 85.798  -27.835 1.00 10.83 ? 598  TRP A CZ2 1 
ATOM   4762 C  CZ3 . TRP A 1 598  ? 34.054 87.400  -26.878 1.00 10.12 ? 598  TRP A CZ3 1 
ATOM   4763 C  CH2 . TRP A 1 598  ? 34.432 86.529  -27.905 1.00 12.65 ? 598  TRP A CH2 1 
ATOM   4764 N  N   . HIS A 1 599  ? 36.987 90.587  -22.461 1.00 15.58 ? 599  HIS A N   1 
ATOM   4765 C  CA  . HIS A 1 599  ? 36.751 91.571  -21.448 1.00 19.86 ? 599  HIS A CA  1 
ATOM   4766 C  C   . HIS A 1 599  ? 35.290 91.783  -21.271 1.00 19.14 ? 599  HIS A C   1 
ATOM   4767 O  O   . HIS A 1 599  ? 34.556 91.881  -22.231 1.00 18.43 ? 599  HIS A O   1 
ATOM   4768 C  CB  . HIS A 1 599  ? 37.507 92.832  -21.799 1.00 23.45 ? 599  HIS A CB  1 
ATOM   4769 C  CG  . HIS A 1 599  ? 38.981 92.600  -21.830 1.00 30.32 ? 599  HIS A CG  1 
ATOM   4770 N  ND1 . HIS A 1 599  ? 39.713 92.318  -20.695 1.00 34.65 ? 599  HIS A ND1 1 
ATOM   4771 C  CD2 . HIS A 1 599  ? 39.843 92.511  -22.864 1.00 34.85 ? 599  HIS A CD2 1 
ATOM   4772 C  CE1 . HIS A 1 599  ? 40.972 92.107  -21.031 1.00 33.80 ? 599  HIS A CE1 1 
ATOM   4773 N  NE2 . HIS A 1 599  ? 41.075 92.217  -22.340 1.00 32.49 ? 599  HIS A NE2 1 
ATOM   4774 N  N   . HIS A 1 600  ? 34.847 91.765  -20.024 1.00 21.83 ? 600  HIS A N   1 
ATOM   4775 C  CA  . HIS A 1 600  ? 33.515 92.237  -19.732 1.00 23.27 ? 600  HIS A CA  1 
ATOM   4776 C  C   . HIS A 1 600  ? 33.546 93.745  -19.647 1.00 20.45 ? 600  HIS A C   1 
ATOM   4777 O  O   . HIS A 1 600  ? 33.981 94.309  -18.650 1.00 25.96 ? 600  HIS A O   1 
ATOM   4778 C  CB  . HIS A 1 600  ? 32.950 91.656  -18.447 1.00 27.82 ? 600  HIS A CB  1 
ATOM   4779 C  CG  . HIS A 1 600  ? 31.620 92.233  -18.080 1.00 38.86 ? 600  HIS A CG  1 
ATOM   4780 N  ND1 . HIS A 1 600  ? 31.068 92.103  -16.824 1.00 41.92 ? 600  HIS A ND1 1 
ATOM   4781 C  CD2 . HIS A 1 600  ? 30.742 92.967  -18.804 1.00 40.96 ? 600  HIS A CD2 1 
ATOM   4782 C  CE1 . HIS A 1 600  ? 29.902 92.721  -16.794 1.00 41.03 ? 600  HIS A CE1 1 
ATOM   4783 N  NE2 . HIS A 1 600  ? 29.680 93.253  -17.983 1.00 45.58 ? 600  HIS A NE2 1 
ATOM   4784 N  N   . ASP A 1 601  ? 33.098 94.380  -20.715 1.00 19.57 ? 601  ASP A N   1 
ATOM   4785 C  CA  . ASP A 1 601  ? 33.217 95.816  -20.853 1.00 21.02 ? 601  ASP A CA  1 
ATOM   4786 C  C   . ASP A 1 601  ? 32.079 96.505  -20.083 1.00 22.70 ? 601  ASP A C   1 
ATOM   4787 O  O   . ASP A 1 601  ? 30.948 96.488  -20.539 1.00 22.03 ? 601  ASP A O   1 
ATOM   4788 C  CB  . ASP A 1 601  ? 33.212 96.139  -22.343 1.00 22.61 ? 601  ASP A CB  1 
ATOM   4789 C  CG  . ASP A 1 601  ? 33.574 97.568  -22.641 1.00 28.33 ? 601  ASP A CG  1 
ATOM   4790 O  OD1 . ASP A 1 601  ? 33.355 98.429  -21.761 1.00 26.05 ? 601  ASP A OD1 1 
ATOM   4791 O  OD2 . ASP A 1 601  ? 34.058 97.835  -23.766 1.00 30.47 ? 601  ASP A OD2 1 
ATOM   4792 N  N   . THR A 1 602  ? 32.394 97.099  -18.921 1.00 25.57 ? 602  THR A N   1 
ATOM   4793 C  CA  . THR A 1 602  ? 31.352 97.736  -18.114 1.00 27.47 ? 602  THR A CA  1 
ATOM   4794 C  C   . THR A 1 602  ? 30.863 99.052  -18.675 1.00 26.14 ? 602  THR A C   1 
ATOM   4795 O  O   . THR A 1 602  ? 29.879 99.596  -18.167 1.00 26.83 ? 602  THR A O   1 
ATOM   4796 C  CB  . THR A 1 602  ? 31.756 97.967  -16.621 1.00 29.94 ? 602  THR A CB  1 
ATOM   4797 O  OG1 . THR A 1 602  ? 32.899 98.843  -16.542 1.00 32.52 ? 602  THR A OG1 1 
ATOM   4798 C  CG2 . THR A 1 602  ? 32.045 96.633  -15.925 1.00 32.36 ? 602  THR A CG2 1 
ATOM   4799 N  N   . LEU A 1 603  ? 31.521 99.564  -19.704 1.00 21.51 ? 603  LEU A N   1 
ATOM   4800 C  CA  . LEU A 1 603  ? 31.080 100.776 -20.368 1.00 23.37 ? 603  LEU A CA  1 
ATOM   4801 C  C   . LEU A 1 603  ? 30.077 100.452 -21.502 1.00 24.72 ? 603  LEU A C   1 
ATOM   4802 O  O   . LEU A 1 603  ? 28.967 100.963 -21.515 1.00 21.67 ? 603  LEU A O   1 
ATOM   4803 C  CB  . LEU A 1 603  ? 32.271 101.560 -20.913 1.00 29.68 ? 603  LEU A CB  1 
ATOM   4804 C  CG  . LEU A 1 603  ? 32.991 102.425 -19.873 1.00 34.37 ? 603  LEU A CG  1 
ATOM   4805 C  CD1 . LEU A 1 603  ? 31.988 103.442 -19.279 1.00 36.15 ? 603  LEU A CD1 1 
ATOM   4806 C  CD2 . LEU A 1 603  ? 33.582 101.552 -18.782 1.00 38.99 ? 603  LEU A CD2 1 
ATOM   4807 N  N   . THR A 1 604  ? 30.434 99.575  -22.445 1.00 22.05 ? 604  THR A N   1 
ATOM   4808 C  CA  . THR A 1 604  ? 29.526 99.215  -23.515 1.00 18.56 ? 604  THR A CA  1 
ATOM   4809 C  C   . THR A 1 604  ? 28.539 98.091  -23.100 1.00 13.23 ? 604  THR A C   1 
ATOM   4810 O  O   . THR A 1 604  ? 27.594 97.830  -23.860 1.00 16.63 ? 604  THR A O   1 
ATOM   4811 C  CB  . THR A 1 604  ? 30.300 98.653  -24.757 1.00 20.51 ? 604  THR A CB  1 
ATOM   4812 O  OG1 . THR A 1 604  ? 31.077 97.508  -24.317 1.00 21.81 ? 604  THR A OG1 1 
ATOM   4813 C  CG2 . THR A 1 604  ? 31.216 99.739  -25.382 1.00 22.81 ? 604  THR A CG2 1 
ATOM   4814 N  N   . LYS A 1 605  ? 28.812 97.427  -21.973 1.00 15.62 ? 605  LYS A N   1 
ATOM   4815 C  CA  . LYS A 1 605  ? 27.961 96.315  -21.503 1.00 17.95 ? 605  LYS A CA  1 
ATOM   4816 C  C   . LYS A 1 605  ? 27.960 95.175  -22.514 1.00 19.68 ? 605  LYS A C   1 
ATOM   4817 O  O   . LYS A 1 605  ? 26.915 94.635  -22.892 1.00 21.66 ? 605  LYS A O   1 
ATOM   4818 C  CB  . LYS A 1 605  ? 26.525 96.782  -21.296 1.00 19.55 ? 605  LYS A CB  1 
ATOM   4819 C  CG  . LYS A 1 605  ? 26.428 97.984  -20.369 1.00 20.29 ? 605  LYS A CG  1 
ATOM   4820 C  CD  . LYS A 1 605  ? 26.745 97.593  -18.941 1.00 20.01 ? 605  LYS A CD  1 
ATOM   4821 C  CE  . LYS A 1 605  ? 26.760 98.847  -18.034 1.00 21.22 ? 605  LYS A CE  1 
ATOM   4822 N  NZ  . LYS A 1 605  ? 26.926 98.395  -16.635 1.00 29.21 ? 605  LYS A NZ  1 
ATOM   4823 N  N   . THR A 1 606  ? 29.142 94.889  -23.029 1.00 15.57 ? 606  THR A N   1 
ATOM   4824 C  CA  . THR A 1 606  ? 29.308 93.745  -23.939 1.00 16.40 ? 606  THR A CA  1 
ATOM   4825 C  C   . THR A 1 606  ? 30.537 92.998  -23.475 1.00 14.61 ? 606  THR A C   1 
ATOM   4826 O  O   . THR A 1 606  ? 31.342 93.487  -22.687 1.00 16.79 ? 606  THR A O   1 
ATOM   4827 C  CB  . THR A 1 606  ? 29.554 94.191  -25.378 1.00 20.36 ? 606  THR A CB  1 
ATOM   4828 O  OG1 . THR A 1 606  ? 30.725 95.030  -25.399 1.00 22.50 ? 606  THR A OG1 1 
ATOM   4829 C  CG2 . THR A 1 606  ? 28.271 94.872  -25.975 1.00 21.54 ? 606  THR A CG2 1 
ATOM   4830 N  N   . ILE A 1 607  ? 30.618 91.724  -23.894 1.00 14.83 ? 607  ILE A N   1 
ATOM   4831 C  CA  . ILE A 1 607  ? 31.750 90.854  -23.598 1.00 12.73 ? 607  ILE A CA  1 
ATOM   4832 C  C   . ILE A 1 607  ? 32.433 90.670  -24.956 1.00 11.92 ? 607  ILE A C   1 
ATOM   4833 O  O   . ILE A 1 607  ? 31.836 90.092  -25.891 1.00 12.08 ? 607  ILE A O   1 
ATOM   4834 C  CB  . ILE A 1 607  ? 31.245 89.540  -23.080 1.00 12.33 ? 607  ILE A CB  1 
ATOM   4835 C  CG1 . ILE A 1 607  ? 30.402 89.797  -21.823 1.00 16.19 ? 607  ILE A CG1 1 
ATOM   4836 C  CG2 . ILE A 1 607  ? 32.449 88.620  -22.769 1.00 14.77 ? 607  ILE A CG2 1 
ATOM   4837 C  CD1 . ILE A 1 607  ? 29.613 88.593  -21.401 1.00 17.93 ? 607  ILE A CD1 1 
ATOM   4838 N  N   . HIS A 1 608  ? 33.641 91.176  -25.122 1.00 12.63 ? 608  HIS A N   1 
ATOM   4839 C  CA  . HIS A 1 608  ? 34.238 91.171  -26.444 1.00 12.99 ? 608  HIS A CA  1 
ATOM   4840 C  C   . HIS A 1 608  ? 35.754 91.016  -26.311 1.00 11.95 ? 608  HIS A C   1 
ATOM   4841 O  O   . HIS A 1 608  ? 36.316 91.289  -25.275 1.00 15.49 ? 608  HIS A O   1 
ATOM   4842 C  CB  . HIS A 1 608  ? 33.904 92.451  -27.197 1.00 15.75 ? 608  HIS A CB  1 
ATOM   4843 C  CG  . HIS A 1 608  ? 34.390 93.681  -26.521 1.00 17.54 ? 608  HIS A CG  1 
ATOM   4844 N  ND1 . HIS A 1 608  ? 35.567 94.304  -26.870 1.00 22.23 ? 608  HIS A ND1 1 
ATOM   4845 C  CD2 . HIS A 1 608  ? 33.852 94.422  -25.531 1.00 21.38 ? 608  HIS A CD2 1 
ATOM   4846 C  CE1 . HIS A 1 608  ? 35.728 95.380  -26.123 1.00 22.68 ? 608  HIS A CE1 1 
ATOM   4847 N  NE2 . HIS A 1 608  ? 34.702 95.472  -25.299 1.00 26.37 ? 608  HIS A NE2 1 
ATOM   4848 N  N   . PRO A 1 609  ? 36.400 90.542  -27.358 1.00 11.73 ? 609  PRO A N   1 
ATOM   4849 C  CA  . PRO A 1 609  ? 37.829 90.299  -27.321 1.00 12.37 ? 609  PRO A CA  1 
ATOM   4850 C  C   . PRO A 1 609  ? 38.719 91.401  -27.778 1.00 14.85 ? 609  PRO A C   1 
ATOM   4851 O  O   . PRO A 1 609  ? 38.377 92.153  -28.699 1.00 18.80 ? 609  PRO A O   1 
ATOM   4852 C  CB  . PRO A 1 609  ? 37.974 89.089  -28.243 1.00 13.68 ? 609  PRO A CB  1 
ATOM   4853 C  CG  . PRO A 1 609  ? 36.982 89.356  -29.309 1.00 16.27 ? 609  PRO A CG  1 
ATOM   4854 C  CD  . PRO A 1 609  ? 35.814 90.035  -28.631 1.00 12.33 ? 609  PRO A CD  1 
ATOM   4855 N  N   . GLN A 1 610  ? 39.873 91.452  -27.150 1.00 12.63 ? 610  GLN A N   1 
ATOM   4856 C  CA  . GLN A 1 610  ? 40.874 92.431  -27.531 1.00 15.06 ? 610  GLN A CA  1 
ATOM   4857 C  C   . GLN A 1 610  ? 42.115 91.670  -27.967 1.00 11.43 ? 610  GLN A C   1 
ATOM   4858 O  O   . GLN A 1 610  ? 42.446 90.685  -27.290 1.00 13.13 ? 610  GLN A O   1 
ATOM   4859 C  CB  . GLN A 1 610  ? 41.238 93.322  -26.353 1.00 17.97 ? 610  GLN A CB  1 
ATOM   4860 C  CG  . GLN A 1 610  ? 40.046 93.966  -25.737 1.00 32.63 ? 610  GLN A CG  1 
ATOM   4861 C  CD  . GLN A 1 610  ? 39.626 95.214  -26.472 1.00 37.58 ? 610  GLN A CD  1 
ATOM   4862 O  OE1 . GLN A 1 610  ? 39.383 95.193  -27.690 1.00 41.32 ? 610  GLN A OE1 1 
ATOM   4863 N  NE2 . GLN A 1 610  ? 39.533 96.325  -25.733 1.00 41.45 ? 610  GLN A NE2 1 
ATOM   4864 N  N   . GLY A 1 611  ? 42.771 92.108  -29.027 1.00 12.16 ? 611  GLY A N   1 
ATOM   4865 C  CA  . GLY A 1 611  ? 43.983 91.414  -29.450 1.00 13.79 ? 611  GLY A CA  1 
ATOM   4866 C  C   . GLY A 1 611  ? 45.245 92.169  -29.033 1.00 13.91 ? 611  GLY A C   1 
ATOM   4867 O  O   . GLY A 1 611  ? 45.285 93.397  -28.908 1.00 17.11 ? 611  GLY A O   1 
ATOM   4868 N  N   . SER A 1 612  ? 46.319 91.438  -28.807 1.00 14.58 ? 612  SER A N   1 
ATOM   4869 C  CA  . SER A 1 612  ? 47.592 92.075  -28.467 1.00 12.66 ? 612  SER A CA  1 
ATOM   4870 C  C   . SER A 1 612  ? 48.274 92.523  -29.718 1.00 11.08 ? 612  SER A C   1 
ATOM   4871 O  O   . SER A 1 612  ? 48.179 91.931  -30.771 1.00 15.94 ? 612  SER A O   1 
ATOM   4872 C  CB  . SER A 1 612  ? 48.431 91.014  -27.765 1.00 13.63 ? 612  SER A CB  1 
ATOM   4873 O  OG  . SER A 1 612  ? 49.716 91.578  -27.445 1.00 15.58 ? 612  SER A OG  1 
ATOM   4874 N  N   . THR A 1 613  ? 48.995 93.688  -29.631 1.00 18.20 ? 613  THR A N   1 
ATOM   4875 C  CA  . THR A 1 613  ? 49.724 94.191  -30.799 1.00 18.82 ? 613  THR A CA  1 
ATOM   4876 C  C   . THR A 1 613  ? 51.238 93.979  -30.620 1.00 22.11 ? 613  THR A C   1 
ATOM   4877 O  O   . THR A 1 613  ? 52.042 94.473  -31.428 1.00 21.05 ? 613  THR A O   1 
ATOM   4878 C  CB  . THR A 1 613  ? 49.506 95.684  -31.001 1.00 20.52 ? 613  THR A CB  1 
ATOM   4879 O  OG1 . THR A 1 613  ? 49.982 96.341  -29.810 1.00 18.07 ? 613  THR A OG1 1 
ATOM   4880 C  CG2 . THR A 1 613  ? 47.991 96.006  -31.107 1.00 22.16 ? 613  THR A CG2 1 
ATOM   4881 N  N   . THR A 1 614  ? 51.607 93.248  -29.565 1.00 18.39 ? 614  THR A N   1 
ATOM   4882 C  CA  . THR A 1 614  ? 53.009 92.901  -29.258 1.00 20.30 ? 614  THR A CA  1 
ATOM   4883 C  C   . THR A 1 614  ? 53.318 91.463  -28.786 1.00 22.21 ? 614  THR A C   1 
ATOM   4884 O  O   . THR A 1 614  ? 54.483 91.128  -28.677 1.00 23.72 ? 614  THR A O   1 
ATOM   4885 C  CB  . THR A 1 614  ? 53.590 93.785  -28.170 1.00 18.90 ? 614  THR A CB  1 
ATOM   4886 O  OG1 . THR A 1 614  ? 52.832 93.612  -26.979 1.00 18.99 ? 614  THR A OG1 1 
ATOM   4887 C  CG2 . THR A 1 614  ? 53.618 95.252  -28.592 1.00 19.59 ? 614  THR A CG2 1 
ATOM   4888 N  N   . LYS A 1 615  ? 52.305 90.668  -28.442 1.00 17.44 ? 615  LYS A N   1 
ATOM   4889 C  CA  . LYS A 1 615  ? 52.437 89.240  -28.072 1.00 15.05 ? 615  LYS A CA  1 
ATOM   4890 C  C   . LYS A 1 615  ? 51.686 88.452  -29.143 1.00 14.47 ? 615  LYS A C   1 
ATOM   4891 O  O   . LYS A 1 615  ? 50.626 88.860  -29.561 1.00 14.70 ? 615  LYS A O   1 
ATOM   4892 C  CB  . LYS A 1 615  ? 51.661 88.910  -26.775 1.00 21.37 ? 615  LYS A CB  1 
ATOM   4893 C  CG  . LYS A 1 615  ? 52.153 89.443  -25.436 1.00 29.57 ? 615  LYS A CG  1 
ATOM   4894 C  CD  . LYS A 1 615  ? 52.075 88.364  -24.322 1.00 29.96 ? 615  LYS A CD  1 
ATOM   4895 C  CE  . LYS A 1 615  ? 50.691 87.986  -23.816 1.00 24.21 ? 615  LYS A CE  1 
ATOM   4896 N  NZ  . LYS A 1 615  ? 50.653 87.844  -22.318 1.00 24.75 ? 615  LYS A NZ  1 
ATOM   4897 N  N   . TYR A 1 616  ? 52.207 87.294  -29.531 1.00 11.74 ? 616  TYR A N   1 
ATOM   4898 C  CA  . TYR A 1 616  ? 51.570 86.416  -30.495 1.00 12.32 ? 616  TYR A CA  1 
ATOM   4899 C  C   . TYR A 1 616  ? 51.688 84.978  -30.017 1.00 9.76  ? 616  TYR A C   1 
ATOM   4900 O  O   . TYR A 1 616  ? 52.532 84.685  -29.191 1.00 11.91 ? 616  TYR A O   1 
ATOM   4901 C  CB  . TYR A 1 616  ? 52.243 86.599  -31.855 1.00 12.01 ? 616  TYR A CB  1 
ATOM   4902 C  CG  . TYR A 1 616  ? 52.193 88.047  -32.260 1.00 15.88 ? 616  TYR A CG  1 
ATOM   4903 C  CD1 . TYR A 1 616  ? 51.046 88.557  -32.843 1.00 14.80 ? 616  TYR A CD1 1 
ATOM   4904 C  CD2 . TYR A 1 616  ? 53.229 88.909  -31.972 1.00 16.04 ? 616  TYR A CD2 1 
ATOM   4905 C  CE1 . TYR A 1 616  ? 50.949 89.861  -33.175 1.00 21.28 ? 616  TYR A CE1 1 
ATOM   4906 C  CE2 . TYR A 1 616  ? 53.138 90.253  -32.306 1.00 19.47 ? 616  TYR A CE2 1 
ATOM   4907 C  CZ  . TYR A 1 616  ? 51.974 90.712  -32.899 1.00 17.95 ? 616  TYR A CZ  1 
ATOM   4908 O  OH  . TYR A 1 616  ? 51.801 92.027  -33.259 1.00 20.37 ? 616  TYR A OH  1 
ATOM   4909 N  N   . ARG A 1 617  ? 50.839 84.098  -30.533 1.00 10.49 ? 617  ARG A N   1 
ATOM   4910 C  CA  . ARG A 1 617  ? 50.952 82.663  -30.203 1.00 9.98  ? 617  ARG A CA  1 
ATOM   4911 C  C   . ARG A 1 617  ? 51.577 81.918  -31.348 1.00 11.32 ? 617  ARG A C   1 
ATOM   4912 O  O   . ARG A 1 617  ? 51.094 82.040  -32.486 1.00 12.32 ? 617  ARG A O   1 
ATOM   4913 C  CB  . ARG A 1 617  ? 49.577 82.038  -29.982 1.00 13.54 ? 617  ARG A CB  1 
ATOM   4914 C  CG  . ARG A 1 617  ? 48.899 82.423  -28.718 1.00 18.17 ? 617  ARG A CG  1 
ATOM   4915 C  CD  . ARG A 1 617  ? 47.496 81.740  -28.645 1.00 17.38 ? 617  ARG A CD  1 
ATOM   4916 N  NE  . ARG A 1 617  ? 47.486 80.273  -28.639 1.00 16.78 ? 617  ARG A NE  1 
ATOM   4917 C  CZ  . ARG A 1 617  ? 46.786 79.525  -29.497 1.00 20.30 ? 617  ARG A CZ  1 
ATOM   4918 N  NH1 . ARG A 1 617  ? 46.013 80.084  -30.452 1.00 17.17 ? 617  ARG A NH1 1 
ATOM   4919 N  NH2 . ARG A 1 617  ? 46.862 78.214  -29.432 1.00 16.63 ? 617  ARG A NH2 1 
ATOM   4920 N  N   . ILE A 1 618  ? 52.615 81.124  -31.102 1.00 9.92  ? 618  ILE A N   1 
ATOM   4921 C  CA  . ILE A 1 618  ? 53.171 80.268  -32.151 1.00 10.48 ? 618  ILE A CA  1 
ATOM   4922 C  C   . ILE A 1 618  ? 52.775 78.819  -31.756 1.00 9.38  ? 618  ILE A C   1 
ATOM   4923 O  O   . ILE A 1 618  ? 52.924 78.434  -30.563 1.00 10.63 ? 618  ILE A O   1 
ATOM   4924 C  CB  . ILE A 1 618  ? 54.644 80.449  -32.373 1.00 11.57 ? 618  ILE A CB  1 
ATOM   4925 C  CG1 . ILE A 1 618  ? 55.017 79.537  -33.547 1.00 15.44 ? 618  ILE A CG1 1 
ATOM   4926 C  CG2 . ILE A 1 618  ? 55.428 80.186  -31.156 1.00 13.81 ? 618  ILE A CG2 1 
ATOM   4927 C  CD1 . ILE A 1 618  ? 56.168 79.987  -34.346 1.00 15.44 ? 618  ILE A CD1 1 
ATOM   4928 N  N   . ILE A 1 619  ? 52.313 78.046  -32.708 1.00 9.15  ? 619  ILE A N   1 
ATOM   4929 C  CA  . ILE A 1 619  ? 51.766 76.706  -32.492 1.00 8.58  ? 619  ILE A CA  1 
ATOM   4930 C  C   . ILE A 1 619  ? 52.472 75.756  -33.433 1.00 7.98  ? 619  ILE A C   1 
ATOM   4931 O  O   . ILE A 1 619  ? 52.639 76.048  -34.653 1.00 9.62  ? 619  ILE A O   1 
ATOM   4932 C  CB  . ILE A 1 619  ? 50.249 76.712  -32.881 1.00 11.80 ? 619  ILE A CB  1 
ATOM   4933 C  CG1 . ILE A 1 619  ? 49.529 77.772  -32.036 1.00 13.44 ? 619  ILE A CG1 1 
ATOM   4934 C  CG2 . ILE A 1 619  ? 49.604 75.316  -32.800 1.00 12.82 ? 619  ILE A CG2 1 
ATOM   4935 C  CD1 . ILE A 1 619  ? 48.258 78.346  -32.822 1.00 14.31 ? 619  ILE A CD1 1 
ATOM   4936 N  N   . PHE A 1 620  ? 52.897 74.578  -32.967 1.00 8.24  ? 620  PHE A N   1 
ATOM   4937 C  CA  . PHE A 1 620  ? 53.494 73.603  -33.859 1.00 7.91  ? 620  PHE A CA  1 
ATOM   4938 C  C   . PHE A 1 620  ? 53.297 72.225  -33.254 1.00 7.68  ? 620  PHE A C   1 
ATOM   4939 O  O   . PHE A 1 620  ? 53.001 72.118  -32.034 1.00 8.52  ? 620  PHE A O   1 
ATOM   4940 C  CB  . PHE A 1 620  ? 54.990 73.836  -34.088 1.00 8.78  ? 620  PHE A CB  1 
ATOM   4941 C  CG  . PHE A 1 620  ? 55.833 73.770  -32.819 1.00 7.38  ? 620  PHE A CG  1 
ATOM   4942 C  CD1 . PHE A 1 620  ? 56.019 74.880  -32.015 1.00 8.04  ? 620  PHE A CD1 1 
ATOM   4943 C  CD2 . PHE A 1 620  ? 56.494 72.580  -32.489 1.00 9.75  ? 620  PHE A CD2 1 
ATOM   4944 C  CE1 . PHE A 1 620  ? 56.873 74.829  -30.900 1.00 9.11  ? 620  PHE A CE1 1 
ATOM   4945 C  CE2 . PHE A 1 620  ? 57.348 72.511  -31.363 1.00 9.04  ? 620  PHE A CE2 1 
ATOM   4946 C  CZ  . PHE A 1 620  ? 57.539 73.634  -30.589 1.00 9.31  ? 620  PHE A CZ  1 
ATOM   4947 N  N   . LYS A 1 621  ? 53.473 71.195  -34.053 1.00 8.17  ? 621  LYS A N   1 
ATOM   4948 C  CA  . LYS A 1 621  ? 53.331 69.826  -33.575 1.00 9.50  ? 621  LYS A CA  1 
ATOM   4949 C  C   . LYS A 1 621  ? 54.621 69.306  -32.989 1.00 10.07 ? 621  LYS A C   1 
ATOM   4950 O  O   . LYS A 1 621  ? 55.667 69.255  -33.657 1.00 11.27 ? 621  LYS A O   1 
ATOM   4951 C  CB  . LYS A 1 621  ? 52.908 68.960  -34.764 1.00 10.07 ? 621  LYS A CB  1 
ATOM   4952 C  CG  . LYS A 1 621  ? 52.584 67.507  -34.351 1.00 12.51 ? 621  LYS A CG  1 
ATOM   4953 C  CD  . LYS A 1 621  ? 51.778 66.790  -35.492 1.00 16.32 ? 621  LYS A CD  1 
ATOM   4954 C  CE  . LYS A 1 621  ? 52.468 66.840  -36.790 1.00 20.85 ? 621  LYS A CE  1 
ATOM   4955 N  NZ  . LYS A 1 621  ? 51.638 66.126  -37.872 1.00 25.70 ? 621  LYS A NZ  1 
ATOM   4956 N  N   . ALA A 1 622  ? 54.589 69.019  -31.696 1.00 9.35  ? 622  ALA A N   1 
ATOM   4957 C  CA  . ALA A 1 622  ? 55.760 68.389  -31.045 1.00 8.49  ? 622  ALA A CA  1 
ATOM   4958 C  C   . ALA A 1 622  ? 55.637 66.862  -31.090 1.00 9.18  ? 622  ALA A C   1 
ATOM   4959 O  O   . ALA A 1 622  ? 54.519 66.339  -30.960 1.00 11.20 ? 622  ALA A O   1 
ATOM   4960 C  CB  . ALA A 1 622  ? 55.875 68.810  -29.571 1.00 8.59  ? 622  ALA A CB  1 
ATOM   4961 N  N   . ARG A 1 623  ? 56.747 66.179  -31.310 1.00 8.04  ? 623  ARG A N   1 
ATOM   4962 C  CA  . ARG A 1 623  ? 56.739 64.684  -31.336 1.00 8.55  ? 623  ARG A CA  1 
ATOM   4963 C  C   . ARG A 1 623  ? 57.762 64.282  -30.299 1.00 7.54  ? 623  ARG A C   1 
ATOM   4964 O  O   . ARG A 1 623  ? 58.930 64.659  -30.375 1.00 9.31  ? 623  ARG A O   1 
ATOM   4965 C  CB  . ARG A 1 623  ? 57.117 64.188  -32.747 1.00 9.76  ? 623  ARG A CB  1 
ATOM   4966 C  CG  . ARG A 1 623  ? 57.145 62.663  -32.759 1.00 11.97 ? 623  ARG A CG  1 
ATOM   4967 C  CD  . ARG A 1 623  ? 57.068 62.054  -34.233 1.00 15.98 ? 623  ARG A CD  1 
ATOM   4968 N  NE  . ARG A 1 623  ? 57.151 60.567  -34.220 1.00 16.36 ? 623  ARG A NE  1 
ATOM   4969 C  CZ  . ARG A 1 623  ? 58.314 59.946  -34.173 1.00 19.96 ? 623  ARG A CZ  1 
ATOM   4970 N  NH1 . ARG A 1 623  ? 59.458 60.616  -34.158 1.00 21.54 ? 623  ARG A NH1 1 
ATOM   4971 N  NH2 . ARG A 1 623  ? 58.335 58.639  -34.045 1.00 20.04 ? 623  ARG A NH2 1 
ATOM   4972 N  N   . VAL A 1 624  ? 57.273 63.511  -29.307 1.00 7.13  ? 624  VAL A N   1 
ATOM   4973 C  CA  . VAL A 1 624  ? 58.095 63.221  -28.116 1.00 7.56  ? 624  VAL A CA  1 
ATOM   4974 C  C   . VAL A 1 624  ? 58.138 61.739  -27.847 1.00 6.10  ? 624  VAL A C   1 
ATOM   4975 O  O   . VAL A 1 624  ? 57.116 61.057  -27.902 1.00 7.54  ? 624  VAL A O   1 
ATOM   4976 C  CB  . VAL A 1 624  ? 57.479 64.017  -26.907 1.00 7.56  ? 624  VAL A CB  1 
ATOM   4977 C  CG1 . VAL A 1 624  ? 58.465 63.966  -25.726 1.00 8.71  ? 624  VAL A CG1 1 
ATOM   4978 C  CG2 . VAL A 1 624  ? 57.130 65.519  -27.324 1.00 8.55  ? 624  VAL A CG2 1 
ATOM   4979 N  N   . PRO A 1 625  ? 59.347 61.254  -27.439 1.00 6.33  ? 625  PRO A N   1 
ATOM   4980 C  CA  . PRO A 1 625  ? 59.466 59.808  -27.180 1.00 7.00  ? 625  PRO A CA  1 
ATOM   4981 C  C   . PRO A 1 625  ? 58.643 59.351  -25.965 1.00 7.20  ? 625  PRO A C   1 
ATOM   4982 O  O   . PRO A 1 625  ? 58.215 60.158  -25.133 1.00 7.21  ? 625  PRO A O   1 
ATOM   4983 C  CB  . PRO A 1 625  ? 60.945 59.624  -26.812 1.00 8.70  ? 625  PRO A CB  1 
ATOM   4984 C  CG  . PRO A 1 625  ? 61.689 60.818  -27.488 1.00 9.27  ? 625  PRO A CG  1 
ATOM   4985 C  CD  . PRO A 1 625  ? 60.656 61.936  -27.337 1.00 8.28  ? 625  PRO A CD  1 
ATOM   4986 N  N   . PRO A 1 626  ? 58.437 58.054  -25.828 1.00 7.23  ? 626  PRO A N   1 
ATOM   4987 C  CA  . PRO A 1 626  ? 57.716 57.505  -24.655 1.00 6.75  ? 626  PRO A CA  1 
ATOM   4988 C  C   . PRO A 1 626  ? 58.524 57.930  -23.395 1.00 6.39  ? 626  PRO A C   1 
ATOM   4989 O  O   . PRO A 1 626  ? 59.742 57.763  -23.327 1.00 6.72  ? 626  PRO A O   1 
ATOM   4990 C  CB  . PRO A 1 626  ? 57.883 55.988  -24.819 1.00 7.82  ? 626  PRO A CB  1 
ATOM   4991 C  CG  . PRO A 1 626  ? 58.169 55.797  -26.343 1.00 7.23  ? 626  PRO A CG  1 
ATOM   4992 C  CD  . PRO A 1 626  ? 59.035 56.984  -26.675 1.00 8.30  ? 626  PRO A CD  1 
ATOM   4993 N  N   . MET A 1 627  ? 57.813 58.474  -22.391 1.00 5.60  ? 627  MET A N   1 
ATOM   4994 C  CA  . MET A 1 627  ? 58.437 58.893  -21.102 1.00 5.66  ? 627  MET A CA  1 
ATOM   4995 C  C   . MET A 1 627  ? 59.707 59.667  -21.374 1.00 6.46  ? 627  MET A C   1 
ATOM   4996 O  O   . MET A 1 627  ? 60.745 59.506  -20.701 1.00 7.60  ? 627  MET A O   1 
ATOM   4997 C  CB  . MET A 1 627  ? 58.757 57.649  -20.249 1.00 7.44  ? 627  MET A CB  1 
ATOM   4998 C  CG  . MET A 1 627  ? 57.468 56.901  -19.885 1.00 7.16  ? 627  MET A CG  1 
ATOM   4999 S  SD  . MET A 1 627  ? 57.649 55.270  -19.166 1.00 9.85  ? 627  MET A SD  1 
ATOM   5000 C  CE  . MET A 1 627  ? 58.482 55.552  -17.677 1.00 9.91  ? 627  MET A CE  1 
ATOM   5001 N  N   . GLY A 1 628  ? 59.610 60.578  -22.359 1.00 6.99  ? 628  GLY A N   1 
ATOM   5002 C  CA  . GLY A 1 628  ? 60.812 61.251  -22.869 1.00 7.35  ? 628  GLY A CA  1 
ATOM   5003 C  C   . GLY A 1 628  ? 60.711 62.741  -23.082 1.00 6.00  ? 628  GLY A C   1 
ATOM   5004 O  O   . GLY A 1 628  ? 59.724 63.381  -22.669 1.00 6.85  ? 628  GLY A O   1 
ATOM   5005 N  N   . LEU A 1 629  ? 61.751 63.289  -23.716 1.00 6.60  ? 629  LEU A N   1 
ATOM   5006 C  CA  . LEU A 1 629  ? 61.863 64.760  -23.936 1.00 6.32  ? 629  LEU A CA  1 
ATOM   5007 C  C   . LEU A 1 629  ? 62.278 65.031  -25.355 1.00 7.07  ? 629  LEU A C   1 
ATOM   5008 O  O   . LEU A 1 629  ? 63.037 64.238  -25.969 1.00 7.32  ? 629  LEU A O   1 
ATOM   5009 C  CB  . LEU A 1 629  ? 62.964 65.330  -23.022 1.00 6.64  ? 629  LEU A CB  1 
ATOM   5010 C  CG  . LEU A 1 629  ? 62.725 65.173  -21.516 1.00 7.13  ? 629  LEU A CG  1 
ATOM   5011 C  CD1 . LEU A 1 629  ? 64.008 65.392  -20.699 1.00 8.59  ? 629  LEU A CD1 1 
ATOM   5012 C  CD2 . LEU A 1 629  ? 61.670 66.194  -21.086 1.00 7.89  ? 629  LEU A CD2 1 
ATOM   5013 N  N   . ALA A 1 630  ? 61.842 66.164  -25.874 1.00 6.80  ? 630  ALA A N   1 
ATOM   5014 C  CA  . ALA A 1 630  ? 62.238 66.596  -27.249 1.00 7.01  ? 630  ALA A CA  1 
ATOM   5015 C  C   . ALA A 1 630  ? 62.453 68.100  -27.218 1.00 6.72  ? 630  ALA A C   1 
ATOM   5016 O  O   . ALA A 1 630  ? 61.632 68.867  -26.671 1.00 7.89  ? 630  ALA A O   1 
ATOM   5017 C  CB  . ALA A 1 630  ? 61.131 66.236  -28.252 1.00 9.47  ? 630  ALA A CB  1 
ATOM   5018 N  N   . THR A 1 631  ? 63.551 68.542  -27.828 1.00 7.71  ? 631  THR A N   1 
ATOM   5019 C  CA  . THR A 1 631  ? 63.955 69.955  -27.836 1.00 7.03  ? 631  THR A CA  1 
ATOM   5020 C  C   . THR A 1 631  ? 63.675 70.601  -29.189 1.00 7.23  ? 631  THR A C   1 
ATOM   5021 O  O   . THR A 1 631  ? 63.935 69.999  -30.224 1.00 8.65  ? 631  THR A O   1 
ATOM   5022 C  CB  . THR A 1 631  ? 65.467 70.077  -27.522 1.00 7.71  ? 631  THR A CB  1 
ATOM   5023 O  OG1 . THR A 1 631  ? 65.750 69.343  -26.331 1.00 8.31  ? 631  THR A OG1 1 
ATOM   5024 C  CG2 . THR A 1 631  ? 65.911 71.524  -27.355 1.00 8.51  ? 631  THR A CG2 1 
ATOM   5025 N  N   . TYR A 1 632  ? 63.176 71.831  -29.168 1.00 6.65  ? 632  TYR A N   1 
ATOM   5026 C  CA  . TYR A 1 632  ? 62.948 72.601  -30.407 1.00 6.88  ? 632  TYR A CA  1 
ATOM   5027 C  C   . TYR A 1 632  ? 63.523 73.977  -30.181 1.00 8.19  ? 632  TYR A C   1 
ATOM   5028 O  O   . TYR A 1 632  ? 63.820 74.431  -29.053 1.00 7.95  ? 632  TYR A O   1 
ATOM   5029 C  CB  . TYR A 1 632  ? 61.464 72.712  -30.742 1.00 8.62  ? 632  TYR A CB  1 
ATOM   5030 C  CG  . TYR A 1 632  ? 60.821 71.396  -31.087 1.00 7.73  ? 632  TYR A CG  1 
ATOM   5031 C  CD1 . TYR A 1 632  ? 60.404 70.476  -30.103 1.00 8.66  ? 632  TYR A CD1 1 
ATOM   5032 C  CD2 . TYR A 1 632  ? 60.632 71.044  -32.417 1.00 8.90  ? 632  TYR A CD2 1 
ATOM   5033 C  CE1 . TYR A 1 632  ? 59.842 69.262  -30.463 1.00 9.32  ? 632  TYR A CE1 1 
ATOM   5034 C  CE2 . TYR A 1 632  ? 60.054 69.813  -32.793 1.00 9.52  ? 632  TYR A CE2 1 
ATOM   5035 C  CZ  . TYR A 1 632  ? 59.671 68.935  -31.801 1.00 8.08  ? 632  TYR A CZ  1 
ATOM   5036 O  OH  . TYR A 1 632  ? 59.125 67.698  -32.156 1.00 12.19 ? 632  TYR A OH  1 
ATOM   5037 N  N   . VAL A 1 633  ? 63.668 74.693  -31.294 1.00 7.96  ? 633  VAL A N   1 
ATOM   5038 C  CA  . VAL A 1 633  ? 64.210 76.046  -31.276 1.00 8.20  ? 633  VAL A CA  1 
ATOM   5039 C  C   . VAL A 1 633  ? 63.259 77.013  -32.021 1.00 7.72  ? 633  VAL A C   1 
ATOM   5040 O  O   . VAL A 1 633  ? 62.765 76.677  -33.118 1.00 8.42  ? 633  VAL A O   1 
ATOM   5041 C  CB  . VAL A 1 633  ? 65.617 76.091  -31.971 1.00 8.56  ? 633  VAL A CB  1 
ATOM   5042 C  CG1 . VAL A 1 633  ? 66.232 77.511  -31.886 1.00 12.19 ? 633  VAL A CG1 1 
ATOM   5043 C  CG2 . VAL A 1 633  ? 66.549 75.118  -31.260 1.00 10.44 ? 633  VAL A CG2 1 
ATOM   5044 N  N   . LEU A 1 634  ? 62.995 78.143  -31.401 1.00 8.55  ? 634  LEU A N   1 
ATOM   5045 C  CA  . LEU A 1 634  ? 62.156 79.223  -32.020 1.00 8.86  ? 634  LEU A CA  1 
ATOM   5046 C  C   . LEU A 1 634  ? 63.136 80.349  -32.371 1.00 9.11  ? 634  LEU A C   1 
ATOM   5047 O  O   . LEU A 1 634  ? 63.917 80.808  -31.533 1.00 10.42 ? 634  LEU A O   1 
ATOM   5048 C  CB  . LEU A 1 634  ? 61.138 79.764  -31.002 1.00 9.90  ? 634  LEU A CB  1 
ATOM   5049 C  CG  . LEU A 1 634  ? 60.299 78.750  -30.213 1.00 17.52 ? 634  LEU A CG  1 
ATOM   5050 C  CD1 . LEU A 1 634  ? 59.154 79.559  -29.523 1.00 17.56 ? 634  LEU A CD1 1 
ATOM   5051 C  CD2 . LEU A 1 634  ? 59.786 77.616  -31.019 1.00 19.43 ? 634  LEU A CD2 1 
ATOM   5052 N  N   . THR A 1 635  ? 63.098 80.754  -33.670 1.00 9.00  ? 635  THR A N   1 
ATOM   5053 C  CA  . THR A 1 635  ? 64.043 81.792  -34.171 1.00 9.18  ? 635  THR A CA  1 
ATOM   5054 C  C   . THR A 1 635  ? 63.278 82.921  -34.833 1.00 10.34 ? 635  THR A C   1 
ATOM   5055 O  O   . THR A 1 635  ? 62.347 82.689  -35.613 1.00 11.27 ? 635  THR A O   1 
ATOM   5056 C  CB  . THR A 1 635  ? 64.956 81.137  -35.221 1.00 10.46 ? 635  THR A CB  1 
ATOM   5057 O  OG1 . THR A 1 635  ? 65.636 80.004  -34.615 1.00 11.28 ? 635  THR A OG1 1 
ATOM   5058 C  CG2 . THR A 1 635  ? 65.990 82.142  -35.733 1.00 11.01 ? 635  THR A CG2 1 
ATOM   5059 N  N   . ILE A 1 636  ? 63.725 84.139  -34.549 1.00 11.03 ? 636  ILE A N   1 
ATOM   5060 C  CA  . ILE A 1 636  ? 63.005 85.283  -35.156 1.00 12.92 ? 636  ILE A CA  1 
ATOM   5061 C  C   . ILE A 1 636  ? 63.630 85.608  -36.517 1.00 13.66 ? 636  ILE A C   1 
ATOM   5062 O  O   . ILE A 1 636  ? 64.775 85.250  -36.793 1.00 13.87 ? 636  ILE A O   1 
ATOM   5063 C  CB  . ILE A 1 636  ? 63.121 86.501  -34.235 1.00 12.27 ? 636  ILE A CB  1 
ATOM   5064 C  CG1 . ILE A 1 636  ? 62.168 87.639  -34.678 1.00 12.91 ? 636  ILE A CG1 1 
ATOM   5065 C  CG2 . ILE A 1 636  ? 64.568 86.985  -34.181 1.00 14.19 ? 636  ILE A CG2 1 
ATOM   5066 C  CD1 . ILE A 1 636  ? 62.123 88.801  -33.653 1.00 16.54 ? 636  ILE A CD1 1 
ATOM   5067 N  N   . SER A 1 637  ? 62.791 86.129  -37.422 1.00 14.18 ? 637  SER A N   1 
ATOM   5068 C  CA  . SER A 1 637  ? 63.307 86.620  -38.730 1.00 16.87 ? 637  SER A CA  1 
ATOM   5069 C  C   . SER A 1 637  ? 62.688 87.990  -38.944 1.00 18.35 ? 637  SER A C   1 
ATOM   5070 O  O   . SER A 1 637  ? 61.840 88.412  -38.202 1.00 16.70 ? 637  SER A O   1 
ATOM   5071 C  CB  . SER A 1 637  ? 62.995 85.694  -39.919 1.00 25.09 ? 637  SER A CB  1 
ATOM   5072 O  OG  . SER A 1 637  ? 61.661 85.290  -39.926 1.00 29.14 ? 637  SER A OG  1 
ATOM   5073 N  N   . ASP A 1 638  ? 63.153 88.700  -39.963 1.00 22.64 ? 638  ASP A N   1 
ATOM   5074 C  CA  . ASP A 1 638  ? 62.613 90.038  -40.171 1.00 27.41 ? 638  ASP A CA  1 
ATOM   5075 C  C   . ASP A 1 638  ? 61.319 90.080  -40.997 1.00 27.46 ? 638  ASP A C   1 
ATOM   5076 O  O   . ASP A 1 638  ? 60.705 91.151  -41.139 1.00 33.42 ? 638  ASP A O   1 
ATOM   5077 C  CB  . ASP A 1 638  ? 63.687 90.916  -40.804 1.00 32.77 ? 638  ASP A CB  1 
ATOM   5078 C  CG  . ASP A 1 638  ? 63.804 90.673  -42.270 1.00 38.99 ? 638  ASP A CG  1 
ATOM   5079 O  OD1 . ASP A 1 638  ? 63.913 89.479  -42.673 1.00 43.06 ? 638  ASP A OD1 1 
ATOM   5080 O  OD2 . ASP A 1 638  ? 63.767 91.678  -43.021 1.00 46.36 ? 638  ASP A OD2 1 
ATOM   5081 N  N   . SER A 1 639  ? 60.885 88.933  -41.529 1.00 23.88 ? 639  SER A N   1 
ATOM   5082 C  CA  . SER A 1 639  ? 59.667 88.879  -42.305 1.00 24.31 ? 639  SER A CA  1 
ATOM   5083 C  C   . SER A 1 639  ? 59.104 87.467  -42.243 1.00 24.73 ? 639  SER A C   1 
ATOM   5084 O  O   . SER A 1 639  ? 59.714 86.576  -41.610 1.00 21.34 ? 639  SER A O   1 
ATOM   5085 C  CB  . SER A 1 639  ? 59.954 89.297  -43.759 1.00 24.59 ? 639  SER A CB  1 
ATOM   5086 O  OG  . SER A 1 639  ? 60.970 88.474  -44.302 1.00 30.57 ? 639  SER A OG  1 
ATOM   5087 N  N   . LYS A 1 640  ? 57.965 87.248  -42.882 1.00 21.71 ? 640  LYS A N   1 
ATOM   5088 C  CA  . LYS A 1 640  ? 57.309 85.930  -42.847 1.00 23.60 ? 640  LYS A CA  1 
ATOM   5089 C  C   . LYS A 1 640  ? 58.239 84.772  -43.215 1.00 21.44 ? 640  LYS A C   1 
ATOM   5090 O  O   . LYS A 1 640  ? 58.780 84.704  -44.305 1.00 24.37 ? 640  LYS A O   1 
ATOM   5091 C  CB  . LYS A 1 640  ? 56.073 85.859  -43.772 1.00 23.89 ? 640  LYS A CB  1 
ATOM   5092 C  CG  . LYS A 1 640  ? 54.895 86.786  -43.386 1.00 33.97 ? 640  LYS A CG  1 
ATOM   5093 C  CD  . LYS A 1 640  ? 53.537 86.367  -44.037 1.00 36.11 ? 640  LYS A CD  1 
ATOM   5094 C  CE  . LYS A 1 640  ? 53.489 86.486  -45.549 1.00 40.21 ? 640  LYS A CE  1 
ATOM   5095 N  NZ  . LYS A 1 640  ? 53.587 87.885  -46.080 1.00 40.79 ? 640  LYS A NZ  1 
ATOM   5096 N  N   . PRO A 1 641  ? 58.404 83.806  -42.306 1.00 18.37 ? 641  PRO A N   1 
ATOM   5097 C  CA  . PRO A 1 641  ? 59.245 82.629  -42.487 1.00 19.35 ? 641  PRO A CA  1 
ATOM   5098 C  C   . PRO A 1 641  ? 58.581 81.666  -43.446 1.00 15.60 ? 641  PRO A C   1 
ATOM   5099 O  O   . PRO A 1 641  ? 57.355 81.537  -43.489 1.00 17.78 ? 641  PRO A O   1 
ATOM   5100 C  CB  . PRO A 1 641  ? 59.263 81.983  -41.081 1.00 21.88 ? 641  PRO A CB  1 
ATOM   5101 C  CG  . PRO A 1 641  ? 58.942 83.038  -40.189 1.00 18.87 ? 641  PRO A CG  1 
ATOM   5102 C  CD  . PRO A 1 641  ? 57.980 83.941  -40.900 1.00 18.68 ? 641  PRO A CD  1 
ATOM   5103 N  N   . GLU A 1 642  ? 59.372 80.897  -44.169 1.00 15.67 ? 642  GLU A N   1 
ATOM   5104 C  CA  . GLU A 1 642  ? 58.821 79.947  -45.111 1.00 16.27 ? 642  GLU A CA  1 
ATOM   5105 C  C   . GLU A 1 642  ? 57.881 78.855  -44.570 1.00 17.02 ? 642  GLU A C   1 
ATOM   5106 O  O   . GLU A 1 642  ? 56.943 78.403  -45.222 1.00 20.72 ? 642  GLU A O   1 
ATOM   5107 C  CB  . GLU A 1 642  ? 59.981 79.229  -45.821 1.00 21.26 ? 642  GLU A CB  1 
ATOM   5108 C  CG  . GLU A 1 642  ? 59.570 78.105  -46.736 1.00 24.98 ? 642  GLU A CG  1 
ATOM   5109 C  CD  . GLU A 1 642  ? 60.790 77.480  -47.438 1.00 34.13 ? 642  GLU A CD  1 
ATOM   5110 O  OE1 . GLU A 1 642  ? 61.860 78.141  -47.504 1.00 35.61 ? 642  GLU A OE1 1 
ATOM   5111 O  OE2 . GLU A 1 642  ? 60.671 76.324  -47.914 1.00 40.67 ? 642  GLU A OE2 1 
ATOM   5112 N  N   . HIS A 1 643  ? 58.156 78.408  -43.351 1.00 14.17 ? 643  HIS A N   1 
ATOM   5113 C  CA  . HIS A 1 643  ? 57.395 77.303  -42.769 1.00 13.57 ? 643  HIS A CA  1 
ATOM   5114 C  C   . HIS A 1 643  ? 56.422 77.707  -41.664 1.00 13.48 ? 643  HIS A C   1 
ATOM   5115 O  O   . HIS A 1 643  ? 56.005 76.831  -40.907 1.00 13.74 ? 643  HIS A O   1 
ATOM   5116 C  CB  . HIS A 1 643  ? 58.361 76.256  -42.210 1.00 14.00 ? 643  HIS A CB  1 
ATOM   5117 C  CG  . HIS A 1 643  ? 59.242 75.655  -43.253 1.00 16.99 ? 643  HIS A CG  1 
ATOM   5118 N  ND1 . HIS A 1 643  ? 58.813 74.642  -44.069 1.00 23.23 ? 643  HIS A ND1 1 
ATOM   5119 C  CD2 . HIS A 1 643  ? 60.482 75.990  -43.670 1.00 18.06 ? 643  HIS A CD2 1 
ATOM   5120 C  CE1 . HIS A 1 643  ? 59.749 74.382  -44.971 1.00 20.29 ? 643  HIS A CE1 1 
ATOM   5121 N  NE2 . HIS A 1 643  ? 60.765 75.190  -44.751 1.00 19.51 ? 643  HIS A NE2 1 
ATOM   5122 N  N   . THR A 1 644  ? 56.074 78.978  -41.598 1.00 11.04 ? 644  THR A N   1 
ATOM   5123 C  CA  . THR A 1 644  ? 55.088 79.494  -40.641 1.00 11.08 ? 644  THR A CA  1 
ATOM   5124 C  C   . THR A 1 644  ? 53.934 80.147  -41.380 1.00 13.01 ? 644  THR A C   1 
ATOM   5125 O  O   . THR A 1 644  ? 54.152 80.977  -42.260 1.00 15.11 ? 644  THR A O   1 
ATOM   5126 C  CB  . THR A 1 644  ? 55.740 80.490  -39.695 1.00 12.66 ? 644  THR A CB  1 
ATOM   5127 O  OG1 . THR A 1 644  ? 56.778 79.823  -38.969 1.00 12.38 ? 644  THR A OG1 1 
ATOM   5128 C  CG2 . THR A 1 644  ? 54.747 81.042  -38.687 1.00 12.20 ? 644  THR A CG2 1 
ATOM   5129 N  N   . SER A 1 645  ? 52.717 79.729  -41.053 1.00 10.92 ? 645  SER A N   1 
ATOM   5130 C  CA  . SER A 1 645  ? 51.510 80.323  -41.663 1.00 11.05 ? 645  SER A CA  1 
ATOM   5131 C  C   . SER A 1 645  ? 50.821 81.166  -40.618 1.00 10.38 ? 645  SER A C   1 
ATOM   5132 O  O   . SER A 1 645  ? 51.169 81.124  -39.441 1.00 11.58 ? 645  SER A O   1 
ATOM   5133 C  CB  . SER A 1 645  ? 50.541 79.285  -42.171 1.00 12.70 ? 645  SER A CB  1 
ATOM   5134 O  OG  . SER A 1 645  ? 50.066 78.521  -41.046 1.00 13.25 ? 645  SER A OG  1 
ATOM   5135 N  N   . TYR A 1 646  ? 49.873 81.986  -41.058 1.00 10.02 ? 646  TYR A N   1 
ATOM   5136 C  CA  . TYR A 1 646  ? 49.185 82.926  -40.173 1.00 9.84  ? 646  TYR A CA  1 
ATOM   5137 C  C   . TYR A 1 646  ? 47.678 82.711  -40.229 1.00 11.32 ? 646  TYR A C   1 
ATOM   5138 O  O   . TYR A 1 646  ? 47.116 82.641  -41.300 1.00 14.52 ? 646  TYR A O   1 
ATOM   5139 C  CB  . TYR A 1 646  ? 49.546 84.377  -40.545 1.00 13.52 ? 646  TYR A CB  1 
ATOM   5140 C  CG  . TYR A 1 646  ? 51.019 84.585  -40.309 1.00 12.00 ? 646  TYR A CG  1 
ATOM   5141 C  CD1 . TYR A 1 646  ? 51.942 84.283  -41.294 1.00 12.97 ? 646  TYR A CD1 1 
ATOM   5142 C  CD2 . TYR A 1 646  ? 51.488 84.951  -39.072 1.00 11.20 ? 646  TYR A CD2 1 
ATOM   5143 C  CE1 . TYR A 1 646  ? 53.277 84.397  -41.060 1.00 14.45 ? 646  TYR A CE1 1 
ATOM   5144 C  CE2 . TYR A 1 646  ? 52.824 85.072  -38.834 1.00 14.09 ? 646  TYR A CE2 1 
ATOM   5145 C  CZ  . TYR A 1 646  ? 53.707 84.795  -39.835 1.00 12.93 ? 646  TYR A CZ  1 
ATOM   5146 O  OH  . TYR A 1 646  ? 55.039 84.905  -39.569 1.00 16.57 ? 646  TYR A OH  1 
ATOM   5147 N  N   . ALA A 1 647  ? 47.030 82.632  -39.072 1.00 9.57  ? 647  ALA A N   1 
ATOM   5148 C  CA  . ALA A 1 647  ? 45.576 82.439  -39.006 1.00 9.89  ? 647  ALA A CA  1 
ATOM   5149 C  C   . ALA A 1 647  ? 44.814 83.664  -39.525 1.00 10.89 ? 647  ALA A C   1 
ATOM   5150 O  O   . ALA A 1 647  ? 45.211 84.782  -39.302 1.00 11.03 ? 647  ALA A O   1 
ATOM   5151 C  CB  . ALA A 1 647  ? 45.148 82.135  -37.569 1.00 11.20 ? 647  ALA A CB  1 
ATOM   5152 N  N   . SER A 1 648  ? 43.709 83.432  -40.212 1.00 10.75 ? 648  SER A N   1 
ATOM   5153 C  CA  . SER A 1 648  ? 42.719 84.492  -40.416 1.00 10.35 ? 648  SER A CA  1 
ATOM   5154 C  C   . SER A 1 648  ? 41.843 84.656  -39.171 1.00 9.20  ? 648  SER A C   1 
ATOM   5155 O  O   . SER A 1 648  ? 41.692 83.724  -38.402 1.00 9.88  ? 648  SER A O   1 
ATOM   5156 C  CB  A SER A 1 648  ? 41.983 84.221  -41.661 0.50 14.79 ? 648  SER A CB  1 
ATOM   5157 C  CB  B SER A 1 648  ? 41.835 83.991  -41.561 0.50 15.90 ? 648  SER A CB  1 
ATOM   5158 O  OG  A SER A 1 648  ? 41.204 83.065  -41.541 0.50 19.06 ? 648  SER A OG  1 
ATOM   5159 O  OG  B SER A 1 648  ? 42.546 83.946  -42.784 0.50 28.03 ? 648  SER A OG  1 
ATOM   5160 N  N   . ASN A 1 649  ? 41.272 85.838  -38.986 1.00 9.90  ? 649  ASN A N   1 
ATOM   5161 C  CA  . ASN A 1 649  ? 40.403 86.117  -37.845 1.00 9.45  ? 649  ASN A CA  1 
ATOM   5162 C  C   . ASN A 1 649  ? 39.188 86.892  -38.286 1.00 9.55  ? 649  ASN A C   1 
ATOM   5163 O  O   . ASN A 1 649  ? 39.297 87.855  -39.030 1.00 10.79 ? 649  ASN A O   1 
ATOM   5164 C  CB  . ASN A 1 649  ? 41.140 86.902  -36.767 1.00 9.51  ? 649  ASN A CB  1 
ATOM   5165 C  CG  . ASN A 1 649  ? 42.320 86.129  -36.194 1.00 11.29 ? 649  ASN A CG  1 
ATOM   5166 O  OD1 . ASN A 1 649  ? 42.188 85.415  -35.213 1.00 11.56 ? 649  ASN A OD1 1 
ATOM   5167 N  ND2 . ASN A 1 649  ? 43.458 86.259  -36.826 1.00 11.56 ? 649  ASN A ND2 1 
ATOM   5168 N  N   . LEU A 1 650  ? 38.036 86.449  -37.820 1.00 9.40  ? 650  LEU A N   1 
ATOM   5169 C  CA  . LEU A 1 650  ? 36.739 87.065  -38.204 1.00 9.08  ? 650  LEU A CA  1 
ATOM   5170 C  C   . LEU A 1 650  ? 35.957 87.327  -36.959 1.00 9.47  ? 650  LEU A C   1 
ATOM   5171 O  O   . LEU A 1 650  ? 35.671 86.404  -36.172 1.00 10.43 ? 650  LEU A O   1 
ATOM   5172 C  CB  . LEU A 1 650  ? 36.010 86.107  -39.120 1.00 10.33 ? 650  LEU A CB  1 
ATOM   5173 C  CG  . LEU A 1 650  ? 34.557 86.423  -39.478 1.00 10.55 ? 650  LEU A CG  1 
ATOM   5174 C  CD1 . LEU A 1 650  ? 34.509 87.758  -40.309 1.00 12.07 ? 650  LEU A CD1 1 
ATOM   5175 C  CD2 . LEU A 1 650  ? 33.957 85.283  -40.291 1.00 15.20 ? 650  LEU A CD2 1 
ATOM   5176 N  N   . LEU A 1 651  ? 35.587 88.577  -36.719 1.00 11.02 ? 651  LEU A N   1 
ATOM   5177 C  CA  . LEU A 1 651  ? 34.783 88.978  -35.567 1.00 10.51 ? 651  LEU A CA  1 
ATOM   5178 C  C   . LEU A 1 651  ? 33.336 89.190  -36.026 1.00 9.51  ? 651  LEU A C   1 
ATOM   5179 O  O   . LEU A 1 651  ? 33.088 90.073  -36.886 1.00 12.75 ? 651  LEU A O   1 
ATOM   5180 C  CB  . LEU A 1 651  ? 35.384 90.261  -34.994 1.00 13.66 ? 651  LEU A CB  1 
ATOM   5181 C  CG  . LEU A 1 651  ? 34.943 90.716  -33.596 1.00 21.99 ? 651  LEU A CG  1 
ATOM   5182 C  CD1 . LEU A 1 651  ? 33.582 91.310  -33.649 1.00 27.86 ? 651  LEU A CD1 1 
ATOM   5183 C  CD2 . LEU A 1 651  ? 35.076 89.551  -32.606 1.00 19.42 ? 651  LEU A CD2 1 
ATOM   5184 N  N   . LEU A 1 652  ? 32.395 88.418  -35.538 1.00 9.76  ? 652  LEU A N   1 
ATOM   5185 C  CA  . LEU A 1 652  ? 31.003 88.496  -35.914 1.00 10.22 ? 652  LEU A CA  1 
ATOM   5186 C  C   . LEU A 1 652  ? 30.216 89.174  -34.821 1.00 12.58 ? 652  LEU A C   1 
ATOM   5187 O  O   . LEU A 1 652  ? 30.105 88.707  -33.667 1.00 12.17 ? 652  LEU A O   1 
ATOM   5188 C  CB  . LEU A 1 652  ? 30.482 87.088  -36.219 1.00 9.78  ? 652  LEU A CB  1 
ATOM   5189 C  CG  . LEU A 1 652  ? 31.199 86.369  -37.330 1.00 10.95 ? 652  LEU A CG  1 
ATOM   5190 C  CD1 . LEU A 1 652  ? 30.669 84.894  -37.499 1.00 11.60 ? 652  LEU A CD1 1 
ATOM   5191 C  CD2 . LEU A 1 652  ? 31.067 87.124  -38.682 1.00 12.53 ? 652  LEU A CD2 1 
ATOM   5192 N  N   . ARG A 1 653  ? 29.712 90.349  -35.163 1.00 12.75 ? 653  ARG A N   1 
ATOM   5193 C  CA  . ARG A 1 653  ? 28.939 91.152  -34.239 1.00 14.39 ? 653  ARG A CA  1 
ATOM   5194 C  C   . ARG A 1 653  ? 28.327 92.335  -34.963 1.00 15.16 ? 653  ARG A C   1 
ATOM   5195 O  O   . ARG A 1 653  ? 28.818 92.777  -35.987 1.00 17.00 ? 653  ARG A O   1 
ATOM   5196 C  CB  . ARG A 1 653  ? 29.788 91.635  -33.069 1.00 15.08 ? 653  ARG A CB  1 
ATOM   5197 C  CG  . ARG A 1 653  ? 30.794 92.703  -33.442 1.00 18.23 ? 653  ARG A CG  1 
ATOM   5198 C  CD  . ARG A 1 653  ? 31.423 93.294  -32.200 1.00 33.60 ? 653  ARG A CD  1 
ATOM   5199 N  NE  . ARG A 1 653  ? 30.456 94.084  -31.457 1.00 27.95 ? 653  ARG A NE  1 
ATOM   5200 C  CZ  . ARG A 1 653  ? 30.719 94.695  -30.314 1.00 28.19 ? 653  ARG A CZ  1 
ATOM   5201 N  NH1 . ARG A 1 653  ? 31.922 94.607  -29.787 1.00 31.10 ? 653  ARG A NH1 1 
ATOM   5202 N  NH2 . ARG A 1 653  ? 29.781 95.400  -29.706 1.00 31.02 ? 653  ARG A NH2 1 
ATOM   5203 N  N   . LYS A 1 654  ? 27.234 92.823  -34.405 1.00 20.09 ? 654  LYS A N   1 
ATOM   5204 C  CA  . LYS A 1 654  ? 26.701 94.140  -34.756 1.00 23.43 ? 654  LYS A CA  1 
ATOM   5205 C  C   . LYS A 1 654  ? 27.632 95.208  -34.212 1.00 20.85 ? 654  LYS A C   1 
ATOM   5206 O  O   . LYS A 1 654  ? 28.213 95.042  -33.155 1.00 23.11 ? 654  LYS A O   1 
ATOM   5207 C  CB  . LYS A 1 654  ? 25.332 94.352  -34.101 1.00 29.24 ? 654  LYS A CB  1 
ATOM   5208 C  CG  . LYS A 1 654  ? 24.416 93.157  -34.114 1.00 29.56 ? 654  LYS A CG  1 
ATOM   5209 C  CD  . LYS A 1 654  ? 23.962 92.856  -35.505 1.00 35.16 ? 654  LYS A CD  1 
ATOM   5210 C  CE  . LYS A 1 654  ? 24.403 93.915  -36.460 1.00 37.30 ? 654  LYS A CE  1 
ATOM   5211 N  NZ  . LYS A 1 654  ? 23.636 93.849  -37.725 1.00 39.33 ? 654  LYS A NZ  1 
ATOM   5212 N  N   . ASN A 1 655  ? 27.737 96.321  -34.915 1.00 22.15 ? 655  ASN A N   1 
ATOM   5213 C  CA  . ASN A 1 655  ? 28.463 97.444  -34.346 1.00 22.48 ? 655  ASN A CA  1 
ATOM   5214 C  C   . ASN A 1 655  ? 29.924 97.128  -34.074 1.00 20.09 ? 655  ASN A C   1 
ATOM   5215 O  O   . ASN A 1 655  ? 30.377 97.335  -32.974 1.00 22.05 ? 655  ASN A O   1 
ATOM   5216 C  CB  . ASN A 1 655  ? 27.829 97.887  -33.021 1.00 25.51 ? 655  ASN A CB  1 
ATOM   5217 C  CG  . ASN A 1 655  ? 28.271 99.285  -32.586 1.00 31.22 ? 655  ASN A CG  1 
ATOM   5218 O  OD1 . ASN A 1 655  ? 28.800 100.062 -33.375 1.00 34.25 ? 655  ASN A OD1 1 
ATOM   5219 N  ND2 . ASN A 1 655  ? 28.017 99.616  -31.329 1.00 26.84 ? 655  ASN A ND2 1 
ATOM   5220 N  N   . PRO A 1 656  ? 30.658 96.621  -35.063 1.00 18.03 ? 656  PRO A N   1 
ATOM   5221 C  CA  . PRO A 1 656  ? 32.058 96.326  -34.755 1.00 16.92 ? 656  PRO A CA  1 
ATOM   5222 C  C   . PRO A 1 656  ? 32.929 97.590  -34.757 1.00 15.78 ? 656  PRO A C   1 
ATOM   5223 O  O   . PRO A 1 656  ? 32.587 98.642  -35.320 1.00 15.23 ? 656  PRO A O   1 
ATOM   5224 C  CB  . PRO A 1 656  ? 32.479 95.434  -35.913 1.00 15.37 ? 656  PRO A CB  1 
ATOM   5225 C  CG  . PRO A 1 656  ? 31.695 96.066  -37.078 1.00 15.98 ? 656  PRO A CG  1 
ATOM   5226 C  CD  . PRO A 1 656  ? 30.312 96.224  -36.448 1.00 18.68 ? 656  PRO A CD  1 
ATOM   5227 N  N   . THR A 1 657  ? 34.069 97.464  -34.102 1.00 14.23 ? 657  THR A N   1 
ATOM   5228 C  CA  . THR A 1 657  ? 35.089 98.501  -34.121 1.00 14.68 ? 657  THR A CA  1 
ATOM   5229 C  C   . THR A 1 657  ? 36.397 97.779  -34.504 1.00 14.38 ? 657  THR A C   1 
ATOM   5230 O  O   . THR A 1 657  ? 36.504 96.531  -34.382 1.00 16.45 ? 657  THR A O   1 
ATOM   5231 C  CB  . THR A 1 657  ? 35.278 99.190  -32.787 1.00 16.11 ? 657  THR A CB  1 
ATOM   5232 O  OG1 . THR A 1 657  ? 35.395 98.188  -31.755 1.00 20.53 ? 657  THR A OG1 1 
ATOM   5233 C  CG2 . THR A 1 657  ? 34.063 100.104 -32.474 1.00 19.31 ? 657  THR A CG2 1 
ATOM   5234 N  N   . SER A 1 658  ? 37.391 98.536  -34.937 1.00 13.71 ? 658  SER A N   1 
ATOM   5235 C  CA  . SER A 1 658  ? 38.652 98.000  -35.393 1.00 14.39 ? 658  SER A CA  1 
ATOM   5236 C  C   . SER A 1 658  ? 39.400 97.210  -34.301 1.00 16.77 ? 658  SER A C   1 
ATOM   5237 O  O   . SER A 1 658  ? 39.234 97.436  -33.103 1.00 17.74 ? 658  SER A O   1 
ATOM   5238 C  CB  . SER A 1 658  ? 39.511 99.149  -35.864 1.00 18.52 ? 658  SER A CB  1 
ATOM   5239 O  OG  . SER A 1 658  ? 39.816 99.903  -34.712 1.00 22.27 ? 658  SER A OG  1 
ATOM   5240 N  N   . LEU A 1 659  ? 40.232 96.274  -34.767 1.00 15.18 ? 659  LEU A N   1 
ATOM   5241 C  CA  . LEU A 1 659  ? 41.030 95.404  -33.845 1.00 16.27 ? 659  LEU A CA  1 
ATOM   5242 C  C   . LEU A 1 659  ? 42.432 95.257  -34.467 1.00 17.09 ? 659  LEU A C   1 
ATOM   5243 O  O   . LEU A 1 659  ? 42.740 94.302  -35.184 1.00 18.05 ? 659  LEU A O   1 
ATOM   5244 C  CB  . LEU A 1 659  ? 40.395 94.001  -33.718 1.00 16.85 ? 659  LEU A CB  1 
ATOM   5245 C  CG  . LEU A 1 659  ? 39.031 93.869  -33.044 1.00 18.77 ? 659  LEU A CG  1 
ATOM   5246 C  CD1 . LEU A 1 659  ? 38.480 92.434  -33.216 1.00 23.31 ? 659  LEU A CD1 1 
ATOM   5247 C  CD2 . LEU A 1 659  ? 39.131 94.180  -31.605 1.00 21.59 ? 659  LEU A CD2 1 
ATOM   5248 N  N   . PRO A 1 660  ? 43.264 96.263  -34.298 1.00 17.17 ? 660  PRO A N   1 
ATOM   5249 C  CA  . PRO A 1 660  ? 44.633 96.228  -34.845 1.00 17.56 ? 660  PRO A CA  1 
ATOM   5250 C  C   . PRO A 1 660  ? 45.490 95.151  -34.099 1.00 15.99 ? 660  PRO A C   1 
ATOM   5251 O  O   . PRO A 1 660  ? 45.262 94.894  -32.923 1.00 16.99 ? 660  PRO A O   1 
ATOM   5252 C  CB  . PRO A 1 660  ? 45.128 97.664  -34.643 1.00 19.39 ? 660  PRO A CB  1 
ATOM   5253 C  CG  . PRO A 1 660  ? 44.393 98.146  -33.459 1.00 21.01 ? 660  PRO A CG  1 
ATOM   5254 C  CD  . PRO A 1 660  ? 43.008 97.452  -33.472 1.00 21.23 ? 660  PRO A CD  1 
ATOM   5255 N  N   . LEU A 1 661  ? 46.416 94.570  -34.836 1.00 16.58 ? 661  LEU A N   1 
ATOM   5256 C  CA  . LEU A 1 661  ? 47.234 93.493  -34.235 1.00 17.52 ? 661  LEU A CA  1 
ATOM   5257 C  C   . LEU A 1 661  ? 48.741 93.714  -34.469 1.00 22.68 ? 661  LEU A C   1 
ATOM   5258 O  O   . LEU A 1 661  ? 49.503 92.740  -34.574 1.00 18.43 ? 661  LEU A O   1 
ATOM   5259 C  CB  . LEU A 1 661  ? 46.824 92.157  -34.874 1.00 15.76 ? 661  LEU A CB  1 
ATOM   5260 C  CG  . LEU A 1 661  ? 45.373 91.713  -34.629 1.00 13.71 ? 661  LEU A CG  1 
ATOM   5261 C  CD1 . LEU A 1 661  ? 45.118 90.427  -35.435 1.00 13.86 ? 661  LEU A CD1 1 
ATOM   5262 C  CD2 . LEU A 1 661  ? 45.169 91.475  -33.122 1.00 13.34 ? 661  LEU A CD2 1 
ATOM   5263 N  N   . GLY A 1 662  ? 49.180 94.975  -34.584 1.00 20.70 ? 662  GLY A N   1 
ATOM   5264 C  CA  . GLY A 1 662  ? 50.621 95.256  -34.821 1.00 17.41 ? 662  GLY A CA  1 
ATOM   5265 C  C   . GLY A 1 662  ? 51.197 94.653  -36.071 1.00 19.05 ? 662  GLY A C   1 
ATOM   5266 O  O   . GLY A 1 662  ? 50.619 94.796  -37.181 1.00 21.73 ? 662  GLY A O   1 
ATOM   5267 N  N   . GLN A 1 663  ? 52.283 93.862  -35.884 1.00 20.67 ? 663  GLN A N   1 
ATOM   5268 C  CA  . GLN A 1 663  ? 52.989 93.248  -36.991 1.00 23.63 ? 663  GLN A CA  1 
ATOM   5269 C  C   . GLN A 1 663  ? 52.310 92.062  -37.603 1.00 14.47 ? 663  GLN A C   1 
ATOM   5270 O  O   . GLN A 1 663  ? 52.675 91.629  -38.713 1.00 20.10 ? 663  GLN A O   1 
ATOM   5271 C  CB  . GLN A 1 663  ? 54.392 92.807  -36.564 1.00 25.41 ? 663  GLN A CB  1 
ATOM   5272 C  CG  . GLN A 1 663  ? 55.018 93.601  -35.393 1.00 33.81 ? 663  GLN A CG  1 
ATOM   5273 C  CD  . GLN A 1 663  ? 56.394 93.039  -34.994 1.00 34.83 ? 663  GLN A CD  1 
ATOM   5274 O  OE1 . GLN A 1 663  ? 57.254 92.814  -35.873 1.00 27.90 ? 663  GLN A OE1 1 
ATOM   5275 N  NE2 . GLN A 1 663  ? 56.606 92.804  -33.680 1.00 35.44 ? 663  GLN A NE2 1 
ATOM   5276 N  N   . TYR A 1 664  ? 51.266 91.561  -36.937 1.00 18.68 ? 664  TYR A N   1 
ATOM   5277 C  CA  . TYR A 1 664  ? 50.536 90.396  -37.443 1.00 18.85 ? 664  TYR A CA  1 
ATOM   5278 C  C   . TYR A 1 664  ? 50.187 90.653  -38.890 1.00 13.61 ? 664  TYR A C   1 
ATOM   5279 O  O   . TYR A 1 664  ? 49.519 91.672  -39.202 1.00 20.12 ? 664  TYR A O   1 
ATOM   5280 C  CB  . TYR A 1 664  ? 49.319 90.186  -36.549 1.00 17.63 ? 664  TYR A CB  1 
ATOM   5281 C  CG  . TYR A 1 664  ? 48.675 88.845  -36.744 1.00 14.07 ? 664  TYR A CG  1 
ATOM   5282 C  CD1 . TYR A 1 664  ? 49.203 87.683  -36.126 1.00 12.58 ? 664  TYR A CD1 1 
ATOM   5283 C  CD2 . TYR A 1 664  ? 47.575 88.704  -37.592 1.00 13.17 ? 664  TYR A CD2 1 
ATOM   5284 C  CE1 . TYR A 1 664  ? 48.640 86.460  -36.352 1.00 13.47 ? 664  TYR A CE1 1 
ATOM   5285 C  CE2 . TYR A 1 664  ? 46.990 87.450  -37.847 1.00 12.78 ? 664  TYR A CE2 1 
ATOM   5286 C  CZ  . TYR A 1 664  ? 47.552 86.318  -37.182 1.00 12.69 ? 664  TYR A CZ  1 
ATOM   5287 O  OH  . TYR A 1 664  ? 46.903 85.117  -37.333 1.00 12.84 ? 664  TYR A OH  1 
ATOM   5288 N  N   . PRO A 1 665  ? 50.411 89.744  -39.803 1.00 19.99 ? 665  PRO A N   1 
ATOM   5289 C  CA  . PRO A 1 665  ? 50.303 90.093  -41.218 1.00 21.09 ? 665  PRO A CA  1 
ATOM   5290 C  C   . PRO A 1 665  ? 48.932 89.958  -41.899 1.00 24.00 ? 665  PRO A C   1 
ATOM   5291 O  O   . PRO A 1 665  ? 48.847 90.324  -43.060 1.00 26.55 ? 665  PRO A O   1 
ATOM   5292 C  CB  . PRO A 1 665  ? 51.318 89.173  -41.880 1.00 20.89 ? 665  PRO A CB  1 
ATOM   5293 C  CG  . PRO A 1 665  ? 51.486 88.068  -40.920 1.00 21.74 ? 665  PRO A CG  1 
ATOM   5294 C  CD  . PRO A 1 665  ? 51.290 88.592  -39.585 1.00 17.08 ? 665  PRO A CD  1 
ATOM   5295 N  N   . GLU A 1 666  ? 47.902 89.441  -41.217 1.00 19.41 ? 666  GLU A N   1 
ATOM   5296 C  CA  . GLU A 1 666  ? 46.545 89.357  -41.782 1.00 17.93 ? 666  GLU A CA  1 
ATOM   5297 C  C   . GLU A 1 666  ? 45.655 90.289  -40.980 1.00 18.59 ? 666  GLU A C   1 
ATOM   5298 O  O   . GLU A 1 666  ? 45.618 90.253  -39.745 1.00 16.93 ? 666  GLU A O   1 
ATOM   5299 C  CB  . GLU A 1 666  ? 45.985 87.943  -41.682 1.00 21.22 ? 666  GLU A CB  1 
ATOM   5300 C  CG  A GLU A 1 666  ? 44.490 87.871  -42.018 0.50 36.03 ? 666  GLU A CG  1 
ATOM   5301 C  CG  B GLU A 1 666  ? 46.641 86.875  -42.481 0.50 32.93 ? 666  GLU A CG  1 
ATOM   5302 C  CD  A GLU A 1 666  ? 44.122 86.835  -43.079 0.50 34.07 ? 666  GLU A CD  1 
ATOM   5303 C  CD  B GLU A 1 666  ? 46.595 87.281  -43.941 0.50 34.00 ? 666  GLU A CD  1 
ATOM   5304 O  OE1 A GLU A 1 666  ? 44.994 86.037  -43.478 0.50 42.84 ? 666  GLU A OE1 1 
ATOM   5305 O  OE1 B GLU A 1 666  ? 45.513 87.656  -44.430 0.50 41.45 ? 666  GLU A OE1 1 
ATOM   5306 O  OE2 A GLU A 1 666  ? 42.956 86.815  -43.512 0.50 31.25 ? 666  GLU A OE2 1 
ATOM   5307 O  OE2 B GLU A 1 666  ? 47.651 87.211  -44.597 0.50 39.36 ? 666  GLU A OE2 1 
ATOM   5308 N  N   . ASP A 1 667  ? 44.928 91.153  -41.684 1.00 16.75 ? 667  ASP A N   1 
ATOM   5309 C  CA  . ASP A 1 667  ? 43.982 92.057  -41.033 1.00 17.18 ? 667  ASP A CA  1 
ATOM   5310 C  C   . ASP A 1 667  ? 42.717 91.292  -40.544 1.00 9.93  ? 667  ASP A C   1 
ATOM   5311 O  O   . ASP A 1 667  ? 42.196 90.443  -41.222 1.00 13.67 ? 667  ASP A O   1 
ATOM   5312 C  CB  . ASP A 1 667  ? 43.524 93.159  -42.006 1.00 18.77 ? 667  ASP A CB  1 
ATOM   5313 C  CG  . ASP A 1 667  ? 44.648 94.074  -42.458 1.00 27.03 ? 667  ASP A CG  1 
ATOM   5314 O  OD1 . ASP A 1 667  ? 45.676 94.192  -41.771 1.00 25.63 ? 667  ASP A OD1 1 
ATOM   5315 O  OD2 . ASP A 1 667  ? 44.455 94.713  -43.501 1.00 28.46 ? 667  ASP A OD2 1 
ATOM   5316 N  N   . VAL A 1 668  ? 42.241 91.661  -39.374 1.00 12.23 ? 668  VAL A N   1 
ATOM   5317 C  CA  . VAL A 1 668  ? 40.987 91.084  -38.828 1.00 13.15 ? 668  VAL A CA  1 
ATOM   5318 C  C   . VAL A 1 668  ? 39.829 91.472  -39.740 1.00 12.90 ? 668  VAL A C   1 
ATOM   5319 O  O   . VAL A 1 668  ? 39.802 92.641  -40.222 1.00 13.70 ? 668  VAL A O   1 
ATOM   5320 C  CB  . VAL A 1 668  ? 40.668 91.551  -37.410 1.00 13.64 ? 668  VAL A CB  1 
ATOM   5321 C  CG1 . VAL A 1 668  ? 39.348 90.949  -36.903 1.00 14.10 ? 668  VAL A CG1 1 
ATOM   5322 C  CG2 . VAL A 1 668  ? 41.834 91.143  -36.426 1.00 13.16 ? 668  VAL A CG2 1 
ATOM   5323 N  N   . LYS A 1 669  ? 38.942 90.525  -40.028 1.00 10.77 ? 669  LYS A N   1 
ATOM   5324 C  CA  . LYS A 1 669  ? 37.727 90.776  -40.804 1.00 10.82 ? 669  LYS A CA  1 
ATOM   5325 C  C   . LYS A 1 669  ? 36.505 90.822  -39.896 1.00 11.22 ? 669  LYS A C   1 
ATOM   5326 O  O   . LYS A 1 669  ? 36.525 90.288  -38.787 1.00 11.11 ? 669  LYS A O   1 
ATOM   5327 C  CB  . LYS A 1 669  ? 37.527 89.694  -41.872 1.00 15.01 ? 669  LYS A CB  1 
ATOM   5328 C  CG  . LYS A 1 669  ? 38.735 89.459  -42.770 1.00 26.97 ? 669  LYS A CG  1 
ATOM   5329 C  CD  . LYS A 1 669  ? 38.721 90.311  -44.022 1.00 36.23 ? 669  LYS A CD  1 
ATOM   5330 C  CE  . LYS A 1 669  ? 40.140 90.613  -44.503 1.00 31.09 ? 669  LYS A CE  1 
ATOM   5331 N  NZ  . LYS A 1 669  ? 40.260 92.041  -44.917 1.00 35.66 ? 669  LYS A NZ  1 
ATOM   5332 N  N   . PHE A 1 670  ? 35.443 91.462  -40.379 1.00 11.74 ? 670  PHE A N   1 
ATOM   5333 C  CA  . PHE A 1 670  ? 34.240 91.667  -39.577 1.00 11.34 ? 670  PHE A CA  1 
ATOM   5334 C  C   . PHE A 1 670  ? 33.009 91.255  -40.361 1.00 11.81 ? 670  PHE A C   1 
ATOM   5335 O  O   . PHE A 1 670  ? 33.007 91.184  -41.571 1.00 13.57 ? 670  PHE A O   1 
ATOM   5336 C  CB  . PHE A 1 670  ? 34.091 93.173  -39.131 1.00 13.14 ? 670  PHE A CB  1 
ATOM   5337 C  CG  . PHE A 1 670  ? 35.238 93.651  -38.328 1.00 11.20 ? 670  PHE A CG  1 
ATOM   5338 C  CD1 . PHE A 1 670  ? 36.390 94.133  -38.993 1.00 14.59 ? 670  PHE A CD1 1 
ATOM   5339 C  CD2 . PHE A 1 670  ? 35.269 93.541  -36.956 1.00 13.73 ? 670  PHE A CD2 1 
ATOM   5340 C  CE1 . PHE A 1 670  ? 37.531 94.486  -38.282 1.00 15.36 ? 670  PHE A CE1 1 
ATOM   5341 C  CE2 . PHE A 1 670  ? 36.421 93.896  -36.240 1.00 16.57 ? 670  PHE A CE2 1 
ATOM   5342 C  CZ  . PHE A 1 670  ? 37.559 94.377  -36.942 1.00 14.53 ? 670  PHE A CZ  1 
ATOM   5343 N  N   . GLY A 1 671  ? 31.933 90.943  -39.632 1.00 12.93 ? 671  GLY A N   1 
ATOM   5344 C  CA  . GLY A 1 671  ? 30.663 90.603  -40.278 1.00 13.41 ? 671  GLY A CA  1 
ATOM   5345 C  C   . GLY A 1 671  ? 29.537 90.540  -39.289 1.00 12.93 ? 671  GLY A C   1 
ATOM   5346 O  O   . GLY A 1 671  ? 29.757 90.512  -38.076 1.00 11.41 ? 671  GLY A O   1 
ATOM   5347 N  N   . ASP A 1 672  ? 28.317 90.564  -39.805 1.00 12.32 ? 672  ASP A N   1 
ATOM   5348 C  CA  . ASP A 1 672  ? 27.170 90.405  -38.927 1.00 13.24 ? 672  ASP A CA  1 
ATOM   5349 C  C   . ASP A 1 672  ? 27.136 88.893  -38.503 1.00 12.54 ? 672  ASP A C   1 
ATOM   5350 O  O   . ASP A 1 672  ? 27.626 88.013  -39.216 1.00 12.68 ? 672  ASP A O   1 
ATOM   5351 C  CB  . ASP A 1 672  ? 25.851 90.646  -39.694 1.00 15.80 ? 672  ASP A CB  1 
ATOM   5352 C  CG  . ASP A 1 672  ? 25.543 92.106  -39.937 1.00 23.82 ? 672  ASP A CG  1 
ATOM   5353 O  OD1 . ASP A 1 672  ? 26.204 92.988  -39.404 1.00 22.91 ? 672  ASP A OD1 1 
ATOM   5354 O  OD2 . ASP A 1 672  ? 24.564 92.353  -40.674 1.00 27.23 ? 672  ASP A OD2 1 
ATOM   5355 N  N   . PRO A 1 673  ? 26.536 88.601  -37.329 1.00 12.58 ? 673  PRO A N   1 
ATOM   5356 C  CA  . PRO A 1 673  ? 26.445 87.195  -36.874 1.00 12.63 ? 673  PRO A CA  1 
ATOM   5357 C  C   . PRO A 1 673  ? 25.846 86.340  -37.986 1.00 12.99 ? 673  PRO A C   1 
ATOM   5358 O  O   . PRO A 1 673  ? 24.925 86.779  -38.706 1.00 13.54 ? 673  PRO A O   1 
ATOM   5359 C  CB  . PRO A 1 673  ? 25.501 87.292  -35.692 1.00 14.20 ? 673  PRO A CB  1 
ATOM   5360 C  CG  . PRO A 1 673  ? 25.871 88.621  -35.077 1.00 16.48 ? 673  PRO A CG  1 
ATOM   5361 C  CD  . PRO A 1 673  ? 25.965 89.527  -36.327 1.00 15.18 ? 673  PRO A CD  1 
ATOM   5362 N  N   . ARG A 1 674  ? 26.358 85.130  -38.123 1.00 11.99 ? 674  ARG A N   1 
ATOM   5363 C  CA  . ARG A 1 674  ? 25.888 84.197  -39.159 1.00 12.21 ? 674  ARG A CA  1 
ATOM   5364 C  C   . ARG A 1 674  ? 26.368 82.806  -38.796 1.00 12.46 ? 674  ARG A C   1 
ATOM   5365 O  O   . ARG A 1 674  ? 27.341 82.664  -38.020 1.00 12.66 ? 674  ARG A O   1 
ATOM   5366 C  CB  . ARG A 1 674  ? 26.451 84.577  -40.552 1.00 12.51 ? 674  ARG A CB  1 
ATOM   5367 C  CG  . ARG A 1 674  ? 27.986 84.547  -40.682 1.00 15.81 ? 674  ARG A CG  1 
ATOM   5368 C  CD  . ARG A 1 674  ? 28.373 84.626  -42.178 1.00 18.45 ? 674  ARG A CD  1 
ATOM   5369 N  NE  . ARG A 1 674  ? 29.751 84.298  -42.526 1.00 22.29 ? 674  ARG A NE  1 
ATOM   5370 C  CZ  . ARG A 1 674  ? 30.744 85.181  -42.666 1.00 22.18 ? 674  ARG A CZ  1 
ATOM   5371 N  NH1 . ARG A 1 674  ? 30.552 86.509  -42.470 1.00 22.64 ? 674  ARG A NH1 1 
ATOM   5372 N  NH2 . ARG A 1 674  ? 31.945 84.721  -43.055 1.00 24.90 ? 674  ARG A NH2 1 
ATOM   5373 N  N   . GLU A 1 675  ? 25.725 81.793  -39.355 1.00 12.38 ? 675  GLU A N   1 
ATOM   5374 C  CA  . GLU A 1 675  ? 26.174 80.428  -39.181 1.00 11.73 ? 675  GLU A CA  1 
ATOM   5375 C  C   . GLU A 1 675  ? 27.512 80.240  -39.912 1.00 13.35 ? 675  GLU A C   1 
ATOM   5376 O  O   . GLU A 1 675  ? 27.809 80.892  -40.961 1.00 15.85 ? 675  GLU A O   1 
ATOM   5377 C  CB  . GLU A 1 675  ? 25.118 79.459  -39.710 1.00 16.84 ? 675  GLU A CB  1 
ATOM   5378 C  CG  . GLU A 1 675  ? 23.865 79.589  -38.905 1.00 18.46 ? 675  GLU A CG  1 
ATOM   5379 C  CD  . GLU A 1 675  ? 23.013 78.317  -38.849 1.00 26.92 ? 675  GLU A CD  1 
ATOM   5380 O  OE1 . GLU A 1 675  ? 23.126 77.493  -39.799 1.00 29.85 ? 675  GLU A OE1 1 
ATOM   5381 O  OE2 . GLU A 1 675  ? 22.242 78.166  -37.852 1.00 30.99 ? 675  GLU A OE2 1 
ATOM   5382 N  N   . ILE A 1 676  ? 28.368 79.402  -39.350 1.00 12.98 ? 676  ILE A N   1 
ATOM   5383 C  CA  . ILE A 1 676  ? 29.657 79.137  -39.965 1.00 13.27 ? 676  ILE A CA  1 
ATOM   5384 C  C   . ILE A 1 676  ? 30.031 77.673  -39.832 1.00 12.80 ? 676  ILE A C   1 
ATOM   5385 O  O   . ILE A 1 676  ? 29.547 76.988  -38.942 1.00 14.65 ? 676  ILE A O   1 
ATOM   5386 C  CB  . ILE A 1 676  ? 30.768 79.980  -39.352 1.00 21.16 ? 676  ILE A CB  1 
ATOM   5387 C  CG1 . ILE A 1 676  ? 30.866 79.726  -37.863 1.00 18.38 ? 676  ILE A CG1 1 
ATOM   5388 C  CG2 . ILE A 1 676  ? 30.593 81.473  -39.669 1.00 25.15 ? 676  ILE A CG2 1 
ATOM   5389 C  CD1 . ILE A 1 676  ? 32.275 79.601  -37.398 1.00 31.26 ? 676  ILE A CD1 1 
ATOM   5390 N  N   . SER A 1 677  ? 30.891 77.215  -40.728 1.00 11.55 ? 677  SER A N   1 
ATOM   5391 C  CA  . SER A 1 677  ? 31.417 75.860  -40.676 1.00 13.30 ? 677  SER A CA  1 
ATOM   5392 C  C   . SER A 1 677  ? 32.937 75.875  -40.821 1.00 14.41 ? 677  SER A C   1 
ATOM   5393 O  O   . SER A 1 677  ? 33.496 76.704  -41.519 1.00 15.86 ? 677  SER A O   1 
ATOM   5394 C  CB  A SER A 1 677  ? 30.461 75.072  -41.581 0.50 16.77 ? 677  SER A CB  1 
ATOM   5395 C  CB  B SER A 1 677  ? 30.867 74.983  -41.816 0.50 17.27 ? 677  SER A CB  1 
ATOM   5396 O  OG  A SER A 1 677  ? 31.108 73.975  -42.181 0.50 30.40 ? 677  SER A OG  1 
ATOM   5397 O  OG  B SER A 1 677  ? 29.500 74.719  -41.598 0.50 30.47 ? 677  SER A OG  1 
ATOM   5398 N  N   . LEU A 1 678  ? 33.590 74.943  -40.143 1.00 11.87 ? 678  LEU A N   1 
ATOM   5399 C  CA  . LEU A 1 678  ? 35.044 74.840  -40.161 1.00 11.28 ? 678  LEU A CA  1 
ATOM   5400 C  C   . LEU A 1 678  ? 35.447 73.380  -40.282 1.00 10.70 ? 678  LEU A C   1 
ATOM   5401 O  O   . LEU A 1 678  ? 34.774 72.495  -39.782 1.00 12.37 ? 678  LEU A O   1 
ATOM   5402 C  CB  . LEU A 1 678  ? 35.644 75.412  -38.877 1.00 13.46 ? 678  LEU A CB  1 
ATOM   5403 C  CG  . LEU A 1 678  ? 35.553 76.922  -38.671 1.00 16.24 ? 678  LEU A CG  1 
ATOM   5404 C  CD1 . LEU A 1 678  ? 35.855 77.245  -37.215 1.00 17.66 ? 678  LEU A CD1 1 
ATOM   5405 C  CD2 . LEU A 1 678  ? 36.540 77.599  -39.587 1.00 23.33 ? 678  LEU A CD2 1 
ATOM   5406 N  N   . ARG A 1 679  ? 36.569 73.162  -40.945 1.00 10.59 ? 679  ARG A N   1 
ATOM   5407 C  CA  . ARG A 1 679  ? 37.216 71.859  -40.979 1.00 12.06 ? 679  ARG A CA  1 
ATOM   5408 C  C   . ARG A 1 679  ? 38.721 72.073  -40.886 1.00 15.72 ? 679  ARG A C   1 
ATOM   5409 O  O   . ARG A 1 679  ? 39.286 72.821  -41.667 1.00 16.84 ? 679  ARG A O   1 
ATOM   5410 C  CB  . ARG A 1 679  ? 36.889 71.141  -42.293 1.00 14.65 ? 679  ARG A CB  1 
ATOM   5411 C  CG  . ARG A 1 679  ? 37.472 69.754  -42.392 1.00 17.78 ? 679  ARG A CG  1 
ATOM   5412 C  CD  . ARG A 1 679  ? 37.107 69.092  -43.702 1.00 21.07 ? 679  ARG A CD  1 
ATOM   5413 N  NE  . ARG A 1 679  ? 37.326 67.651  -43.632 1.00 24.93 ? 679  ARG A NE  1 
ATOM   5414 C  CZ  . ARG A 1 679  ? 37.298 66.830  -44.675 1.00 31.06 ? 679  ARG A CZ  1 
ATOM   5415 N  NH1 . ARG A 1 679  ? 37.054 67.297  -45.886 1.00 34.05 ? 679  ARG A NH1 1 
ATOM   5416 N  NH2 . ARG A 1 679  ? 37.505 65.534  -44.500 1.00 30.36 ? 679  ARG A NH2 1 
ATOM   5417 N  N   . VAL A 1 680  ? 39.364 71.419  -39.926 1.00 11.76 ? 680  VAL A N   1 
ATOM   5418 C  CA  . VAL A 1 680  ? 40.821 71.357  -39.893 1.00 12.55 ? 680  VAL A CA  1 
ATOM   5419 C  C   . VAL A 1 680  ? 41.346 69.996  -40.345 1.00 14.22 ? 680  VAL A C   1 
ATOM   5420 O  O   . VAL A 1 680  ? 40.861 68.964  -39.920 1.00 15.43 ? 680  VAL A O   1 
ATOM   5421 C  CB  . VAL A 1 680  ? 41.376 71.687  -38.491 1.00 11.48 ? 680  VAL A CB  1 
ATOM   5422 C  CG1 . VAL A 1 680  ? 42.896 71.485  -38.437 1.00 13.08 ? 680  VAL A CG1 1 
ATOM   5423 C  CG2 . VAL A 1 680  ? 41.021 73.124  -38.110 1.00 12.06 ? 680  VAL A CG2 1 
ATOM   5424 N  N   . GLY A 1 681  ? 42.341 70.023  -41.221 1.00 15.81 ? 681  GLY A N   1 
ATOM   5425 C  CA  . GLY A 1 681  ? 42.938 68.801  -41.729 1.00 19.97 ? 681  GLY A CA  1 
ATOM   5426 C  C   . GLY A 1 681  ? 41.939 67.897  -42.427 1.00 19.02 ? 681  GLY A C   1 
ATOM   5427 O  O   . GLY A 1 681  ? 41.132 68.358  -43.222 1.00 20.35 ? 681  GLY A O   1 
ATOM   5428 N  N   . ASN A 1 682  ? 42.006 66.606  -42.111 1.00 25.83 ? 682  ASN A N   1 
ATOM   5429 C  CA  . ASN A 1 682  ? 41.102 65.603  -42.666 1.00 26.13 ? 682  ASN A CA  1 
ATOM   5430 C  C   . ASN A 1 682  ? 39.885 65.422  -41.777 1.00 27.66 ? 682  ASN A C   1 
ATOM   5431 O  O   . ASN A 1 682  ? 39.029 64.590  -42.058 1.00 30.51 ? 682  ASN A O   1 
ATOM   5432 C  CB  . ASN A 1 682  ? 41.794 64.245  -42.778 1.00 30.76 ? 682  ASN A CB  1 
ATOM   5433 C  CG  . ASN A 1 682  ? 42.928 64.242  -43.767 1.00 35.30 ? 682  ASN A CG  1 
ATOM   5434 O  OD1 . ASN A 1 682  ? 42.942 65.017  -44.713 1.00 44.05 ? 682  ASN A OD1 1 
ATOM   5435 N  ND2 . ASN A 1 682  ? 43.888 63.355  -43.558 1.00 39.77 ? 682  ASN A ND2 1 
ATOM   5436 N  N   . GLY A 1 683  ? 39.832 66.181  -40.692 1.00 22.69 ? 683  GLY A N   1 
ATOM   5437 C  CA  . GLY A 1 683  ? 39.100 65.782  -39.506 1.00 21.43 ? 683  GLY A CA  1 
ATOM   5438 C  C   . GLY A 1 683  ? 37.648 66.136  -39.705 1.00 16.07 ? 683  GLY A C   1 
ATOM   5439 O  O   . GLY A 1 683  ? 37.244 66.363  -40.826 1.00 17.92 ? 683  GLY A O   1 
ATOM   5440 N  N   . PRO A 1 684  ? 36.871 66.209  -38.631 1.00 14.59 ? 684  PRO A N   1 
ATOM   5441 C  CA  . PRO A 1 684  ? 35.440 66.481  -38.787 1.00 13.32 ? 684  PRO A CA  1 
ATOM   5442 C  C   . PRO A 1 684  ? 35.165 67.918  -39.229 1.00 11.79 ? 684  PRO A C   1 
ATOM   5443 O  O   . PRO A 1 684  ? 35.972 68.810  -39.025 1.00 13.28 ? 684  PRO A O   1 
ATOM   5444 C  CB  . PRO A 1 684  ? 34.881 66.230  -37.385 1.00 15.70 ? 684  PRO A CB  1 
ATOM   5445 C  CG  . PRO A 1 684  ? 36.042 66.463  -36.476 1.00 20.38 ? 684  PRO A CG  1 
ATOM   5446 C  CD  . PRO A 1 684  ? 37.230 65.972  -37.223 1.00 16.67 ? 684  PRO A CD  1 
ATOM   5447 N  N   . THR A 1 685  ? 34.013 68.117  -39.848 1.00 11.55 ? 685  THR A N   1 
ATOM   5448 C  CA  . THR A 1 685  ? 33.524 69.447  -40.156 1.00 11.11 ? 685  THR A CA  1 
ATOM   5449 C  C   . THR A 1 685  ? 32.486 69.819  -39.108 1.00 11.74 ? 685  THR A C   1 
ATOM   5450 O  O   . THR A 1 685  ? 31.538 69.082  -38.891 1.00 12.50 ? 685  THR A O   1 
ATOM   5451 C  CB  . THR A 1 685  ? 32.888 69.476  -41.550 1.00 12.94 ? 685  THR A CB  1 
ATOM   5452 O  OG1 . THR A 1 685  ? 33.863 69.087  -42.517 1.00 15.65 ? 685  THR A OG1 1 
ATOM   5453 C  CG2 . THR A 1 685  ? 32.372 70.866  -41.886 1.00 14.92 ? 685  THR A CG2 1 
ATOM   5454 N  N   . LEU A 1 686  ? 32.691 70.951  -38.448 1.00 9.48  ? 686  LEU A N   1 
ATOM   5455 C  CA  . LEU A 1 686  ? 31.802 71.398  -37.385 1.00 10.25 ? 686  LEU A CA  1 
ATOM   5456 C  C   . LEU A 1 686  ? 31.008 72.610  -37.867 1.00 10.40 ? 686  LEU A C   1 
ATOM   5457 O  O   . LEU A 1 686  ? 31.575 73.535  -38.452 1.00 11.32 ? 686  LEU A O   1 
ATOM   5458 C  CB  . LEU A 1 686  ? 32.608 71.782  -36.139 1.00 10.26 ? 686  LEU A CB  1 
ATOM   5459 C  CG  . LEU A 1 686  ? 33.570 70.792  -35.467 1.00 16.50 ? 686  LEU A CG  1 
ATOM   5460 C  CD1 . LEU A 1 686  ? 33.765 71.121  -33.994 1.00 15.37 ? 686  LEU A CD1 1 
ATOM   5461 C  CD2 . LEU A 1 686  ? 33.230 69.348  -35.652 1.00 17.63 ? 686  LEU A CD2 1 
ATOM   5462 N  N   . ALA A 1 687  ? 29.704 72.608  -37.614 1.00 9.23  ? 687  ALA A N   1 
ATOM   5463 C  CA  . ALA A 1 687  ? 28.889 73.757  -37.967 1.00 10.17 ? 687  ALA A CA  1 
ATOM   5464 C  C   . ALA A 1 687  ? 28.429 74.430  -36.689 1.00 10.73 ? 687  ALA A C   1 
ATOM   5465 O  O   . ALA A 1 687  ? 28.098 73.741  -35.693 1.00 10.34 ? 687  ALA A O   1 
ATOM   5466 C  CB  . ALA A 1 687  ? 27.653 73.297  -38.815 1.00 11.44 ? 687  ALA A CB  1 
ATOM   5467 N  N   . PHE A 1 688  ? 28.386 75.763  -36.704 1.00 10.52 ? 688  PHE A N   1 
ATOM   5468 C  CA  . PHE A 1 688  ? 28.030 76.570  -35.552 1.00 8.86  ? 688  PHE A CA  1 
ATOM   5469 C  C   . PHE A 1 688  ? 26.857 77.490  -35.818 1.00 10.20 ? 688  PHE A C   1 
ATOM   5470 O  O   . PHE A 1 688  ? 26.710 77.973  -36.959 1.00 11.89 ? 688  PHE A O   1 
ATOM   5471 C  CB  . PHE A 1 688  ? 29.207 77.472  -35.152 1.00 10.19 ? 688  PHE A CB  1 
ATOM   5472 C  CG  . PHE A 1 688  ? 30.422 76.699  -34.776 1.00 8.90  ? 688  PHE A CG  1 
ATOM   5473 C  CD1 . PHE A 1 688  ? 31.268 76.208  -35.741 1.00 9.96  ? 688  PHE A CD1 1 
ATOM   5474 C  CD2 . PHE A 1 688  ? 30.693 76.406  -33.444 1.00 8.69  ? 688  PHE A CD2 1 
ATOM   5475 C  CE1 . PHE A 1 688  ? 32.394 75.392  -35.437 1.00 8.73  ? 688  PHE A CE1 1 
ATOM   5476 C  CE2 . PHE A 1 688  ? 31.817 75.599  -33.146 1.00 8.48  ? 688  PHE A CE2 1 
ATOM   5477 C  CZ  . PHE A 1 688  ? 32.655 75.096  -34.125 1.00 8.50  ? 688  PHE A CZ  1 
ATOM   5478 N  N   . SER A 1 689  ? 26.041 77.756  -34.834 1.00 10.68 ? 689  SER A N   1 
ATOM   5479 C  CA  . SER A 1 689  ? 24.917 78.688  -34.935 1.00 11.68 ? 689  SER A CA  1 
ATOM   5480 C  C   . SER A 1 689  ? 25.498 80.129  -34.969 1.00 11.49 ? 689  SER A C   1 
ATOM   5481 O  O   . SER A 1 689  ? 26.683 80.377  -34.729 1.00 10.77 ? 689  SER A O   1 
ATOM   5482 C  CB  . SER A 1 689  ? 24.023 78.570  -33.689 1.00 10.85 ? 689  SER A CB  1 
ATOM   5483 O  OG  . SER A 1 689  ? 24.638 79.144  -32.549 1.00 12.01 ? 689  SER A OG  1 
ATOM   5484 N  N   . GLU A 1 690  ? 24.621 81.092  -35.261 1.00 12.15 ? 690  GLU A N   1 
ATOM   5485 C  CA  . GLU A 1 690  ? 25.040 82.489  -35.225 1.00 11.45 ? 690  GLU A CA  1 
ATOM   5486 C  C   . GLU A 1 690  ? 25.416 82.960  -33.839 1.00 11.48 ? 690  GLU A C   1 
ATOM   5487 O  O   . GLU A 1 690  ? 25.986 84.049  -33.685 1.00 12.25 ? 690  GLU A O   1 
ATOM   5488 C  CB  . GLU A 1 690  ? 23.961 83.388  -35.829 1.00 17.18 ? 690  GLU A CB  1 
ATOM   5489 C  CG  . GLU A 1 690  ? 22.735 83.613  -35.080 1.00 19.62 ? 690  GLU A CG  1 
ATOM   5490 C  CD  . GLU A 1 690  ? 21.939 84.723  -35.765 1.00 26.73 ? 690  GLU A CD  1 
ATOM   5491 O  OE1 . GLU A 1 690  ? 21.472 84.453  -36.902 1.00 30.30 ? 690  GLU A OE1 1 
ATOM   5492 O  OE2 . GLU A 1 690  ? 21.811 85.860  -35.201 1.00 35.05 ? 690  GLU A OE2 1 
ATOM   5493 N  N   . GLN A 1 691  ? 25.064 82.172  -32.818 1.00 12.07 ? 691  GLN A N   1 
ATOM   5494 C  CA  . GLN A 1 691  ? 25.516 82.522  -31.461 1.00 12.17 ? 691  GLN A CA  1 
ATOM   5495 C  C   . GLN A 1 691  ? 26.861 81.842  -31.113 1.00 9.37  ? 691  GLN A C   1 
ATOM   5496 O  O   . GLN A 1 691  ? 27.272 81.920  -29.935 1.00 14.15 ? 691  GLN A O   1 
ATOM   5497 C  CB  . GLN A 1 691  ? 24.502 82.134  -30.377 1.00 13.31 ? 691  GLN A CB  1 
ATOM   5498 C  CG  . GLN A 1 691  ? 23.217 82.881  -30.457 1.00 19.08 ? 691  GLN A CG  1 
ATOM   5499 C  CD  . GLN A 1 691  ? 22.211 81.870  -30.623 1.00 32.90 ? 691  GLN A CD  1 
ATOM   5500 O  OE1 . GLN A 1 691  ? 21.759 81.227  -29.635 1.00 30.15 ? 691  GLN A OE1 1 
ATOM   5501 N  NE2 . GLN A 1 691  ? 21.889 81.606  -31.885 1.00 29.83 ? 691  GLN A NE2 1 
ATOM   5502 N  N   . GLY A 1 692  ? 27.509 81.185  -32.052 1.00 9.42  ? 692  GLY A N   1 
ATOM   5503 C  CA  . GLY A 1 692  ? 28.835 80.649  -31.792 1.00 11.23 ? 692  GLY A CA  1 
ATOM   5504 C  C   . GLY A 1 692  ? 28.839 79.299  -31.121 1.00 9.15  ? 692  GLY A C   1 
ATOM   5505 O  O   . GLY A 1 692  ? 29.875 78.870  -30.653 1.00 11.10 ? 692  GLY A O   1 
ATOM   5506 N  N   . LEU A 1 693  ? 27.703 78.613  -31.110 1.00 9.00  ? 693  LEU A N   1 
ATOM   5507 C  CA  . LEU A 1 693  ? 27.592 77.302  -30.444 1.00 9.73  ? 693  LEU A CA  1 
ATOM   5508 C  C   . LEU A 1 693  ? 27.459 76.210  -31.445 1.00 10.19 ? 693  LEU A C   1 
ATOM   5509 O  O   . LEU A 1 693  ? 26.733 76.332  -32.461 1.00 9.66  ? 693  LEU A O   1 
ATOM   5510 C  CB  . LEU A 1 693  ? 26.387 77.311  -29.529 1.00 11.45 ? 693  LEU A CB  1 
ATOM   5511 C  CG  . LEU A 1 693  ? 26.536 78.278  -28.349 1.00 12.91 ? 693  LEU A CG  1 
ATOM   5512 C  CD1 . LEU A 1 693  ? 25.136 78.772  -27.970 1.00 19.21 ? 693  LEU A CD1 1 
ATOM   5513 C  CD2 . LEU A 1 693  ? 27.145 77.613  -27.160 1.00 15.87 ? 693  LEU A CD2 1 
ATOM   5514 N  N   . LEU A 1 694  ? 28.133 75.093  -31.187 1.00 9.01  ? 694  LEU A N   1 
ATOM   5515 C  CA  . LEU A 1 694  ? 28.052 73.958  -32.091 1.00 8.36  ? 694  LEU A CA  1 
ATOM   5516 C  C   . LEU A 1 694  ? 26.619 73.557  -32.357 1.00 7.49  ? 694  LEU A C   1 
ATOM   5517 O  O   . LEU A 1 694  ? 25.776 73.544  -31.435 1.00 8.36  ? 694  LEU A O   1 
ATOM   5518 C  CB  . LEU A 1 694  ? 28.757 72.748  -31.390 1.00 10.88 ? 694  LEU A CB  1 
ATOM   5519 C  CG  . LEU A 1 694  ? 28.959 71.488  -32.239 1.00 10.83 ? 694  LEU A CG  1 
ATOM   5520 C  CD1 . LEU A 1 694  ? 29.947 71.753  -33.372 1.00 11.23 ? 694  LEU A CD1 1 
ATOM   5521 C  CD2 . LEU A 1 694  ? 29.502 70.352  -31.334 1.00 11.85 ? 694  LEU A CD2 1 
ATOM   5522 N  N   . LYS A 1 695  ? 26.345 73.210  -33.639 1.00 9.16  ? 695  LYS A N   1 
ATOM   5523 C  CA  . LYS A 1 695  ? 25.039 72.652  -33.995 1.00 9.77  ? 695  LYS A CA  1 
ATOM   5524 C  C   . LYS A 1 695  ? 25.159 71.325  -34.701 1.00 9.62  ? 695  LYS A C   1 
ATOM   5525 O  O   . LYS A 1 695  ? 24.173 70.571  -34.635 1.00 11.04 ? 695  LYS A O   1 
ATOM   5526 C  CB  . LYS A 1 695  ? 24.171 73.638  -34.813 1.00 14.80 ? 695  LYS A CB  1 
ATOM   5527 C  CG  . LYS A 1 695  ? 24.751 74.009  -36.101 1.00 23.52 ? 695  LYS A CG  1 
ATOM   5528 C  CD  . LYS A 1 695  ? 23.933 75.212  -36.685 1.00 29.86 ? 695  LYS A CD  1 
ATOM   5529 C  CE  . LYS A 1 695  ? 22.440 75.044  -36.478 1.00 35.26 ? 695  LYS A CE  1 
ATOM   5530 N  NZ  . LYS A 1 695  ? 21.908 74.251  -37.628 1.00 39.70 ? 695  LYS A NZ  1 
ATOM   5531 N  N   . SER A 1 696  ? 26.272 70.989  -35.312 1.00 8.97  ? 696  SER A N   1 
ATOM   5532 C  CA  . SER A 1 696  ? 26.389 69.650  -35.967 1.00 10.51 ? 696  SER A CA  1 
ATOM   5533 C  C   . SER A 1 696  ? 27.817 69.262  -36.180 1.00 11.51 ? 696  SER A C   1 
ATOM   5534 O  O   . SER A 1 696  ? 28.729 70.151  -36.241 1.00 10.61 ? 696  SER A O   1 
ATOM   5535 C  CB  . SER A 1 696  ? 25.639 69.617  -37.337 1.00 11.02 ? 696  SER A CB  1 
ATOM   5536 O  OG  . SER A 1 696  ? 26.244 70.411  -38.333 1.00 13.72 ? 696  SER A OG  1 
ATOM   5537 N  N   . ILE A 1 697  ? 28.062 67.939  -36.334 1.00 10.23 ? 697  ILE A N   1 
ATOM   5538 C  CA  . ILE A 1 697  ? 29.378 67.399  -36.601 1.00 11.96 ? 697  ILE A CA  1 
ATOM   5539 C  C   . ILE A 1 697  ? 29.243 66.453  -37.780 1.00 12.97 ? 697  ILE A C   1 
ATOM   5540 O  O   . ILE A 1 697  ? 28.362 65.571  -37.749 1.00 12.98 ? 697  ILE A O   1 
ATOM   5541 C  CB  . ILE A 1 697  ? 29.937 66.595  -35.369 1.00 11.63 ? 697  ILE A CB  1 
ATOM   5542 C  CG1 . ILE A 1 697  ? 30.034 67.519  -34.158 1.00 10.93 ? 697  ILE A CG1 1 
ATOM   5543 C  CG2 . ILE A 1 697  ? 31.283 65.932  -35.702 1.00 11.76 ? 697  ILE A CG2 1 
ATOM   5544 C  CD1 . ILE A 1 697  ? 30.527 66.750  -32.864 1.00 11.84 ? 697  ILE A CD1 1 
ATOM   5545 N  N   . GLN A 1 698  ? 30.060 66.662  -38.786 1.00 11.32 ? 698  GLN A N   1 
ATOM   5546 C  CA  . GLN A 1 698  ? 30.083 65.773  -39.911 1.00 12.14 ? 698  GLN A CA  1 
ATOM   5547 C  C   . GLN A 1 698  ? 31.409 65.052  -39.923 1.00 13.28 ? 698  GLN A C   1 
ATOM   5548 O  O   . GLN A 1 698  ? 32.415 65.673  -40.137 1.00 13.91 ? 698  GLN A O   1 
ATOM   5549 C  CB  . GLN A 1 698  ? 29.911 66.570  -41.198 1.00 14.40 ? 698  GLN A CB  1 
ATOM   5550 C  CG  . GLN A 1 698  ? 29.926 65.675  -42.436 1.00 18.06 ? 698  GLN A CG  1 
ATOM   5551 C  CD  . GLN A 1 698  ? 30.071 66.454  -43.719 1.00 19.44 ? 698  GLN A CD  1 
ATOM   5552 O  OE1 . GLN A 1 698  ? 30.726 67.477  -43.761 1.00 25.75 ? 698  GLN A OE1 1 
ATOM   5553 N  NE2 . GLN A 1 698  ? 29.438 65.973  -44.768 1.00 21.36 ? 698  GLN A NE2 1 
ATOM   5554 N  N   . LEU A 1 699  ? 31.413 63.741  -39.716 1.00 14.21 ? 699  LEU A N   1 
ATOM   5555 C  CA  . LEU A 1 699  ? 32.686 63.054  -39.560 1.00 15.57 ? 699  LEU A CA  1 
ATOM   5556 C  C   . LEU A 1 699  ? 33.594 63.006  -40.801 1.00 19.75 ? 699  LEU A C   1 
ATOM   5557 O  O   . LEU A 1 699  ? 34.811 63.186  -40.684 1.00 22.18 ? 699  LEU A O   1 
ATOM   5558 C  CB  . LEU A 1 699  ? 32.427 61.640  -38.991 1.00 18.76 ? 699  LEU A CB  1 
ATOM   5559 C  CG  . LEU A 1 699  ? 31.809 61.644  -37.578 1.00 17.28 ? 699  LEU A CG  1 
ATOM   5560 C  CD1 . LEU A 1 699  ? 31.598 60.186  -37.122 1.00 20.15 ? 699  LEU A CD1 1 
ATOM   5561 C  CD2 . LEU A 1 699  ? 32.694 62.359  -36.585 1.00 19.52 ? 699  LEU A CD2 1 
ATOM   5562 N  N   . THR A 1 700  ? 32.987 62.836  -41.975 1.00 20.25 ? 700  THR A N   1 
ATOM   5563 C  CA  . THR A 1 700  ? 33.777 62.807  -43.204 1.00 27.44 ? 700  THR A CA  1 
ATOM   5564 C  C   . THR A 1 700  ? 33.031 63.527  -44.305 1.00 27.59 ? 700  THR A C   1 
ATOM   5565 O  O   . THR A 1 700  ? 31.890 63.949  -44.119 1.00 28.16 ? 700  THR A O   1 
ATOM   5566 C  CB  . THR A 1 700  ? 34.079 61.350  -43.654 1.00 28.06 ? 700  THR A CB  1 
ATOM   5567 O  OG1 . THR A 1 700  ? 32.846 60.630  -43.811 1.00 33.82 ? 700  THR A OG1 1 
ATOM   5568 C  CG2 . THR A 1 700  ? 34.953 60.648  -42.618 1.00 28.65 ? 700  THR A CG2 1 
ATOM   5569 N  N   . GLN A 1 701  ? 33.683 63.664  -45.458 1.00 33.69 ? 701  GLN A N   1 
ATOM   5570 C  CA  . GLN A 1 701  ? 33.126 64.370  -46.620 1.00 36.45 ? 701  GLN A CA  1 
ATOM   5571 C  C   . GLN A 1 701  ? 31.756 63.830  -47.039 1.00 36.02 ? 701  GLN A C   1 
ATOM   5572 O  O   . GLN A 1 701  ? 30.856 64.598  -47.329 1.00 38.67 ? 701  GLN A O   1 
ATOM   5573 C  CB  . GLN A 1 701  ? 34.105 64.357  -47.810 1.00 39.82 ? 701  GLN A CB  1 
ATOM   5574 C  CG  . GLN A 1 701  ? 35.343 65.213  -47.632 1.00 42.97 ? 701  GLN A CG  1 
ATOM   5575 C  CD  . GLN A 1 701  ? 35.122 66.661  -48.002 1.00 46.11 ? 701  GLN A CD  1 
ATOM   5576 O  OE1 . GLN A 1 701  ? 34.081 67.245  -47.705 1.00 46.00 ? 701  GLN A OE1 1 
ATOM   5577 N  NE2 . GLN A 1 701  ? 36.111 67.256  -48.635 1.00 46.69 ? 701  GLN A NE2 1 
ATOM   5578 N  N   . ASP A 1 702  ? 31.592 62.515  -47.021 1.00 36.96 ? 702  ASP A N   1 
ATOM   5579 C  CA  . ASP A 1 702  ? 30.334 61.885  -47.436 1.00 41.32 ? 702  ASP A CA  1 
ATOM   5580 C  C   . ASP A 1 702  ? 29.204 61.837  -46.419 1.00 41.01 ? 702  ASP A C   1 
ATOM   5581 O  O   . ASP A 1 702  ? 28.020 61.856  -46.774 1.00 41.01 ? 702  ASP A O   1 
ATOM   5582 C  CB  . ASP A 1 702  ? 30.608 60.438  -47.903 1.00 43.85 ? 702  ASP A CB  1 
ATOM   5583 C  CG  . ASP A 1 702  ? 31.108 59.524  -46.768 1.00 47.43 ? 702  ASP A CG  1 
ATOM   5584 O  OD1 . ASP A 1 702  ? 32.190 59.813  -46.193 1.00 49.18 ? 702  ASP A OD1 1 
ATOM   5585 O  OD2 . ASP A 1 702  ? 30.420 58.513  -46.463 1.00 49.67 ? 702  ASP A OD2 1 
ATOM   5586 N  N   . SER A 1 703  ? 29.546 62.006  -45.144 1.00 36.88 ? 703  SER A N   1 
ATOM   5587 C  CA  . SER A 1 703  ? 28.645 61.643  -44.068 1.00 30.36 ? 703  SER A CA  1 
ATOM   5588 C  C   . SER A 1 703  ? 27.625 62.711  -43.664 1.00 24.00 ? 703  SER A C   1 
ATOM   5589 O  O   . SER A 1 703  ? 27.744 63.863  -44.039 1.00 24.46 ? 703  SER A O   1 
ATOM   5590 C  CB  . SER A 1 703  ? 29.441 61.135  -42.870 1.00 31.98 ? 703  SER A CB  1 
ATOM   5591 O  OG  . SER A 1 703  ? 30.216 62.173  -42.312 1.00 28.34 ? 703  SER A OG  1 
ATOM   5592 N  N   . PRO A 1 704  ? 26.622 62.289  -42.906 1.00 23.53 ? 704  PRO A N   1 
ATOM   5593 C  CA  . PRO A 1 704  ? 25.563 63.151  -42.405 1.00 22.20 ? 704  PRO A CA  1 
ATOM   5594 C  C   . PRO A 1 704  ? 26.095 64.238  -41.435 1.00 18.71 ? 704  PRO A C   1 
ATOM   5595 O  O   . PRO A 1 704  ? 27.121 64.036  -40.722 1.00 20.54 ? 704  PRO A O   1 
ATOM   5596 C  CB  . PRO A 1 704  ? 24.669 62.185  -41.629 1.00 25.44 ? 704  PRO A CB  1 
ATOM   5597 C  CG  . PRO A 1 704  ? 24.923 60.878  -42.323 1.00 23.86 ? 704  PRO A CG  1 
ATOM   5598 C  CD  . PRO A 1 704  ? 26.365 60.873  -42.566 1.00 26.03 ? 704  PRO A CD  1 
ATOM   5599 N  N   . HIS A 1 705  ? 25.447 65.402  -41.493 1.00 18.67 ? 705  HIS A N   1 
ATOM   5600 C  CA  . HIS A 1 705  ? 25.739 66.442  -40.498 1.00 16.69 ? 705  HIS A CA  1 
ATOM   5601 C  C   . HIS A 1 705  ? 24.895 66.010  -39.293 1.00 17.91 ? 705  HIS A C   1 
ATOM   5602 O  O   . HIS A 1 705  ? 23.699 66.262  -39.213 1.00 19.35 ? 705  HIS A O   1 
ATOM   5603 C  CB  . HIS A 1 705  ? 25.323 67.816  -41.033 1.00 19.91 ? 705  HIS A CB  1 
ATOM   5604 C  CG  . HIS A 1 705  ? 26.190 68.294  -42.159 1.00 23.20 ? 705  HIS A CG  1 
ATOM   5605 N  ND1 . HIS A 1 705  ? 27.313 69.076  -41.966 1.00 24.30 ? 705  HIS A ND1 1 
ATOM   5606 C  CD2 . HIS A 1 705  ? 26.129 68.047  -43.490 1.00 29.26 ? 705  HIS A CD2 1 
ATOM   5607 C  CE1 . HIS A 1 705  ? 27.908 69.286  -43.130 1.00 31.19 ? 705  HIS A CE1 1 
ATOM   5608 N  NE2 . HIS A 1 705  ? 27.207 68.673  -44.072 1.00 28.54 ? 705  HIS A NE2 1 
ATOM   5609 N  N   . VAL A 1 706  ? 25.546 65.375  -38.300 1.00 13.26 ? 706  VAL A N   1 
ATOM   5610 C  CA  . VAL A 1 706  ? 24.821 64.860  -37.143 1.00 12.92 ? 706  VAL A CA  1 
ATOM   5611 C  C   . VAL A 1 706  ? 24.484 65.962  -36.154 1.00 10.95 ? 706  VAL A C   1 
ATOM   5612 O  O   . VAL A 1 706  ? 25.407 66.674  -35.763 1.00 11.82 ? 706  VAL A O   1 
ATOM   5613 C  CB  . VAL A 1 706  ? 25.719 63.792  -36.408 1.00 12.09 ? 706  VAL A CB  1 
ATOM   5614 C  CG1 . VAL A 1 706  ? 24.971 63.271  -35.161 1.00 12.35 ? 706  VAL A CG1 1 
ATOM   5615 C  CG2 . VAL A 1 706  ? 26.164 62.663  -37.404 1.00 14.07 ? 706  VAL A CG2 1 
ATOM   5616 N  N   . PRO A 1 707  ? 23.219 66.168  -35.779 1.00 10.04 ? 707  PRO A N   1 
ATOM   5617 C  CA  . PRO A 1 707  ? 22.861 67.221  -34.821 1.00 12.04 ? 707  PRO A CA  1 
ATOM   5618 C  C   . PRO A 1 707  ? 23.516 66.996  -33.470 1.00 11.36 ? 707  PRO A C   1 
ATOM   5619 O  O   . PRO A 1 707  ? 23.355 65.941  -32.850 1.00 12.24 ? 707  PRO A O   1 
ATOM   5620 C  CB  . PRO A 1 707  ? 21.336 67.134  -34.706 1.00 12.03 ? 707  PRO A CB  1 
ATOM   5621 C  CG  . PRO A 1 707  ? 20.919 66.431  -36.008 1.00 16.20 ? 707  PRO A CG  1 
ATOM   5622 C  CD  . PRO A 1 707  ? 22.019 65.437  -36.269 1.00 12.31 ? 707  PRO A CD  1 
ATOM   5623 N  N   . VAL A 1 708  ? 24.328 67.985  -33.073 1.00 10.63 ? 708  VAL A N   1 
ATOM   5624 C  CA  . VAL A 1 708  ? 25.034 67.956  -31.759 1.00 9.99  ? 708  VAL A CA  1 
ATOM   5625 C  C   . VAL A 1 708  ? 25.012 69.435  -31.377 1.00 9.43  ? 708  VAL A C   1 
ATOM   5626 O  O   . VAL A 1 708  ? 25.759 70.266  -31.976 1.00 10.55 ? 708  VAL A O   1 
ATOM   5627 C  CB  . VAL A 1 708  ? 26.480 67.430  -31.878 1.00 10.48 ? 708  VAL A CB  1 
ATOM   5628 C  CG1 . VAL A 1 708  ? 27.154 67.445  -30.449 1.00 12.08 ? 708  VAL A CG1 1 
ATOM   5629 C  CG2 . VAL A 1 708  ? 26.490 65.954  -32.432 1.00 12.86 ? 708  VAL A CG2 1 
ATOM   5630 N  N   . HIS A 1 709  ? 24.182 69.801  -30.417 1.00 9.25  ? 709  HIS A N   1 
ATOM   5631 C  CA  . HIS A 1 709  ? 24.077 71.208  -30.073 1.00 10.46 ? 709  HIS A CA  1 
ATOM   5632 C  C   . HIS A 1 709  ? 24.480 71.496  -28.636 1.00 11.67 ? 709  HIS A C   1 
ATOM   5633 O  O   . HIS A 1 709  ? 23.989 70.843  -27.736 1.00 11.04 ? 709  HIS A O   1 
ATOM   5634 C  CB  A HIS A 1 709  ? 22.651 71.635  -30.364 0.50 14.05 ? 709  HIS A CB  1 
ATOM   5635 C  CB  B HIS A 1 709  ? 22.567 71.527  -30.258 0.50 14.10 ? 709  HIS A CB  1 
ATOM   5636 C  CG  A HIS A 1 709  ? 22.392 73.084  -30.077 0.50 24.00 ? 709  HIS A CG  1 
ATOM   5637 C  CG  B HIS A 1 709  ? 22.039 71.805  -31.669 0.50 26.91 ? 709  HIS A CG  1 
ATOM   5638 N  ND1 A HIS A 1 709  ? 23.202 74.097  -30.546 0.50 32.24 ? 709  HIS A ND1 1 
ATOM   5639 N  ND1 B HIS A 1 709  ? 21.850 70.801  -32.592 0.50 36.18 ? 709  HIS A ND1 1 
ATOM   5640 C  CD2 A HIS A 1 709  ? 21.422 73.687  -29.356 0.50 28.07 ? 709  HIS A CD2 1 
ATOM   5641 C  CD2 B HIS A 1 709  ? 21.652 72.951  -32.282 0.50 34.76 ? 709  HIS A CD2 1 
ATOM   5642 C  CE1 A HIS A 1 709  ? 22.728 75.261  -30.145 0.50 25.05 ? 709  HIS A CE1 1 
ATOM   5643 C  CE1 B HIS A 1 709  ? 21.406 71.315  -33.723 0.50 33.34 ? 709  HIS A CE1 1 
ATOM   5644 N  NE2 A HIS A 1 709  ? 21.657 75.037  -29.411 0.50 31.39 ? 709  HIS A NE2 1 
ATOM   5645 N  NE2 B HIS A 1 709  ? 21.255 72.619  -33.555 0.50 28.82 ? 709  HIS A NE2 1 
ATOM   5646 N  N   . PHE A 1 710  ? 25.343 72.491  -28.434 1.00 9.30  ? 710  PHE A N   1 
ATOM   5647 C  CA  . PHE A 1 710  ? 25.667 72.939  -27.079 1.00 7.34  ? 710  PHE A CA  1 
ATOM   5648 C  C   . PHE A 1 710  ? 24.635 74.019  -26.672 1.00 9.33  ? 710  PHE A C   1 
ATOM   5649 O  O   . PHE A 1 710  ? 24.264 74.909  -27.506 1.00 10.09 ? 710  PHE A O   1 
ATOM   5650 C  CB  . PHE A 1 710  ? 27.065 73.583  -26.995 1.00 10.49 ? 710  PHE A CB  1 
ATOM   5651 C  CG  . PHE A 1 710  ? 28.174 72.604  -26.662 1.00 10.45 ? 710  PHE A CG  1 
ATOM   5652 C  CD1 . PHE A 1 710  ? 28.134 71.891  -25.462 1.00 12.19 ? 710  PHE A CD1 1 
ATOM   5653 C  CD2 . PHE A 1 710  ? 29.253 72.408  -27.526 1.00 12.81 ? 710  PHE A CD2 1 
ATOM   5654 C  CE1 . PHE A 1 710  ? 29.155 70.974  -25.078 1.00 13.36 ? 710  PHE A CE1 1 
ATOM   5655 C  CE2 . PHE A 1 710  ? 30.293 71.485  -27.133 1.00 12.15 ? 710  PHE A CE2 1 
ATOM   5656 C  CZ  . PHE A 1 710  ? 30.206 70.794  -25.896 1.00 13.77 ? 710  PHE A CZ  1 
ATOM   5657 N  N   . LYS A 1 711  ? 24.214 73.993  -25.419 1.00 8.15  ? 711  LYS A N   1 
ATOM   5658 C  CA  . LYS A 1 711  ? 23.298 74.959  -24.869 1.00 10.32 ? 711  LYS A CA  1 
ATOM   5659 C  C   . LYS A 1 711  ? 23.661 75.202  -23.427 1.00 10.22 ? 711  LYS A C   1 
ATOM   5660 O  O   . LYS A 1 711  ? 23.942 74.246  -22.705 1.00 12.34 ? 711  LYS A O   1 
ATOM   5661 C  CB  . LYS A 1 711  ? 21.851 74.400  -24.952 1.00 11.52 ? 711  LYS A CB  1 
ATOM   5662 C  CG  . LYS A 1 711  ? 20.784 75.387  -24.423 1.00 15.37 ? 711  LYS A CG  1 
ATOM   5663 C  CD  . LYS A 1 711  ? 19.377 74.836  -24.529 1.00 18.36 ? 711  LYS A CD  1 
ATOM   5664 C  CE  . LYS A 1 711  ? 18.986 74.755  -26.006 1.00 18.60 ? 711  LYS A CE  1 
ATOM   5665 N  NZ  . LYS A 1 711  ? 17.618 74.114  -26.052 1.00 21.23 ? 711  LYS A NZ  1 
ATOM   5666 N  N   . PHE A 1 712  ? 23.628 76.430  -22.961 1.00 8.45  ? 712  PHE A N   1 
ATOM   5667 C  CA  . PHE A 1 712  ? 23.842 76.753  -21.572 1.00 7.70  ? 712  PHE A CA  1 
ATOM   5668 C  C   . PHE A 1 712  ? 22.543 77.091  -20.891 1.00 7.67  ? 712  PHE A C   1 
ATOM   5669 O  O   . PHE A 1 712  ? 21.698 77.856  -21.442 1.00 9.58  ? 712  PHE A O   1 
ATOM   5670 C  CB  . PHE A 1 712  ? 24.836 77.933  -21.432 1.00 9.80  ? 712  PHE A CB  1 
ATOM   5671 C  CG  . PHE A 1 712  ? 26.253 77.527  -21.737 1.00 8.59  ? 712  PHE A CG  1 
ATOM   5672 C  CD1 . PHE A 1 712  ? 26.738 77.539  -23.039 1.00 9.47  ? 712  PHE A CD1 1 
ATOM   5673 C  CD2 . PHE A 1 712  ? 27.093 77.058  -20.709 1.00 9.25  ? 712  PHE A CD2 1 
ATOM   5674 C  CE1 . PHE A 1 712  ? 28.028 77.079  -23.338 1.00 9.09  ? 712  PHE A CE1 1 
ATOM   5675 C  CE2 . PHE A 1 712  ? 28.357 76.616  -20.990 1.00 8.28  ? 712  PHE A CE2 1 
ATOM   5676 C  CZ  . PHE A 1 712  ? 28.835 76.614  -22.285 1.00 8.87  ? 712  PHE A CZ  1 
ATOM   5677 N  N   . LEU A 1 713  ? 22.335 76.553  -19.707 1.00 7.59  ? 713  LEU A N   1 
ATOM   5678 C  CA  . LEU A 1 713  ? 21.106 76.763  -18.952 1.00 8.11  ? 713  LEU A CA  1 
ATOM   5679 C  C   . LEU A 1 713  ? 21.420 77.048  -17.506 1.00 9.06  ? 713  LEU A C   1 
ATOM   5680 O  O   . LEU A 1 713  ? 22.598 76.937  -17.058 1.00 8.56  ? 713  LEU A O   1 
ATOM   5681 C  CB  . LEU A 1 713  ? 20.175 75.525  -19.046 1.00 9.12  ? 713  LEU A CB  1 
ATOM   5682 C  CG  . LEU A 1 713  ? 19.834 75.078  -20.468 1.00 8.40  ? 713  LEU A CG  1 
ATOM   5683 C  CD1 . LEU A 1 713  ? 20.704 73.882  -20.854 1.00 11.96 ? 713  LEU A CD1 1 
ATOM   5684 C  CD2 . LEU A 1 713  ? 18.343 74.638  -20.544 1.00 12.10 ? 713  LEU A CD2 1 
ATOM   5685 N  N   . LYS A 1 714  ? 20.411 77.463  -16.762 1.00 8.84  ? 714  LYS A N   1 
ATOM   5686 C  CA  . LYS A 1 714  ? 20.586 77.727  -15.354 1.00 8.87  ? 714  LYS A CA  1 
ATOM   5687 C  C   . LYS A 1 714  ? 19.546 77.039  -14.492 1.00 9.86  ? 714  LYS A C   1 
ATOM   5688 O  O   . LYS A 1 714  ? 18.344 76.992  -14.850 1.00 11.33 ? 714  LYS A O   1 
ATOM   5689 C  CB  . LYS A 1 714  ? 20.508 79.243  -15.071 1.00 14.00 ? 714  LYS A CB  1 
ATOM   5690 C  CG  . LYS A 1 714  ? 19.390 79.935  -15.718 1.00 23.87 ? 714  LYS A CG  1 
ATOM   5691 C  CD  . LYS A 1 714  ? 19.347 81.415  -15.266 1.00 30.15 ? 714  LYS A CD  1 
ATOM   5692 C  CE  . LYS A 1 714  ? 20.634 82.182  -15.547 1.00 33.06 ? 714  LYS A CE  1 
ATOM   5693 N  NZ  . LYS A 1 714  ? 20.594 83.669  -15.113 1.00 39.20 ? 714  LYS A NZ  1 
ATOM   5694 N  N   . TYR A 1 715  ? 20.003 76.498  -13.368 1.00 8.63  ? 715  TYR A N   1 
ATOM   5695 C  CA  . TYR A 1 715  ? 19.130 75.989  -12.343 1.00 7.82  ? 715  TYR A CA  1 
ATOM   5696 C  C   . TYR A 1 715  ? 19.077 77.048  -11.240 1.00 10.01 ? 715  TYR A C   1 
ATOM   5697 O  O   . TYR A 1 715  ? 20.050 77.754  -10.975 1.00 10.28 ? 715  TYR A O   1 
ATOM   5698 C  CB  . TYR A 1 715  ? 19.666 74.684  -11.714 1.00 7.36  ? 715  TYR A CB  1 
ATOM   5699 C  CG  . TYR A 1 715  ? 19.598 73.475  -12.557 1.00 7.59  ? 715  TYR A CG  1 
ATOM   5700 C  CD1 . TYR A 1 715  ? 18.413 72.752  -12.635 1.00 7.85  ? 715  TYR A CD1 1 
ATOM   5701 C  CD2 . TYR A 1 715  ? 20.717 73.034  -13.288 1.00 8.49  ? 715  TYR A CD2 1 
ATOM   5702 C  CE1 . TYR A 1 715  ? 18.326 71.595  -13.404 1.00 7.94  ? 715  TYR A CE1 1 
ATOM   5703 C  CE2 . TYR A 1 715  ? 20.644 71.899  -14.090 1.00 8.31  ? 715  TYR A CE2 1 
ATOM   5704 C  CZ  . TYR A 1 715  ? 19.427 71.168  -14.130 1.00 7.95  ? 715  TYR A CZ  1 
ATOM   5705 O  OH  . TYR A 1 715  ? 19.350 69.994  -14.878 1.00 8.52  ? 715  TYR A OH  1 
ATOM   5706 N  N   . GLY A 1 716  ? 17.920 77.113  -10.558 1.00 9.57  ? 716  GLY A N   1 
ATOM   5707 C  CA  . GLY A 1 716  ? 17.753 78.010  -9.419  1.00 9.77  ? 716  GLY A CA  1 
ATOM   5708 C  C   . GLY A 1 716  ? 17.609 77.220  -8.124  1.00 11.65 ? 716  GLY A C   1 
ATOM   5709 O  O   . GLY A 1 716  ? 17.947 75.993  -8.047  1.00 12.19 ? 716  GLY A O   1 
ATOM   5710 N  N   . VAL A 1 717  ? 17.121 77.885  -7.091  1.00 11.30 ? 717  VAL A N   1 
ATOM   5711 C  CA  . VAL A 1 717  ? 16.976 77.312  -5.746  1.00 12.25 ? 717  VAL A CA  1 
ATOM   5712 C  C   . VAL A 1 717  ? 15.527 77.470  -5.313  1.00 13.32 ? 717  VAL A C   1 
ATOM   5713 O  O   . VAL A 1 717  ? 14.823 78.415  -5.761  1.00 16.84 ? 717  VAL A O   1 
ATOM   5714 C  CB  . VAL A 1 717  ? 17.899 78.073  -4.786  1.00 12.66 ? 717  VAL A CB  1 
ATOM   5715 C  CG1 . VAL A 1 717  ? 17.721 77.677  -3.332  1.00 17.94 ? 717  VAL A CG1 1 
ATOM   5716 C  CG2 . VAL A 1 717  ? 19.363 77.828  -5.197  1.00 12.66 ? 717  VAL A CG2 1 
ATOM   5717 N  N   . ARG A 1 718  ? 15.080 76.606  -4.416  1.00 11.17 ? 718  ARG A N   1 
ATOM   5718 C  CA  . ARG A 1 718  ? 13.673 76.619  -3.939  1.00 12.81 ? 718  ARG A CA  1 
ATOM   5719 C  C   . ARG A 1 718  ? 13.416 77.799  -3.056  1.00 18.65 ? 718  ARG A C   1 
ATOM   5720 O  O   . ARG A 1 718  ? 14.249 78.179  -2.275  1.00 20.30 ? 718  ARG A O   1 
ATOM   5721 C  CB  . ARG A 1 718  ? 13.343 75.295  -3.228  1.00 12.84 ? 718  ARG A CB  1 
ATOM   5722 C  CG  . ARG A 1 718  ? 13.417 74.187  -4.233  1.00 12.44 ? 718  ARG A CG  1 
ATOM   5723 C  CD  . ARG A 1 718  ? 13.443 72.813  -3.523  1.00 13.59 ? 718  ARG A CD  1 
ATOM   5724 N  NE  . ARG A 1 718  ? 13.647 71.810  -4.542  1.00 13.01 ? 718  ARG A NE  1 
ATOM   5725 C  CZ  . ARG A 1 718  ? 13.609 70.488  -4.337  1.00 12.91 ? 718  ARG A CZ  1 
ATOM   5726 N  NH1 . ARG A 1 718  ? 13.340 70.017  -3.121  1.00 14.24 ? 718  ARG A NH1 1 
ATOM   5727 N  NH2 . ARG A 1 718  ? 13.938 69.641  -5.296  1.00 16.23 ? 718  ARG A NH2 1 
ATOM   5728 N  N   . SER A 1 719  ? 12.244 78.413  -3.212  1.00 20.64 ? 719  SER A N   1 
ATOM   5729 C  CA  . SER A 1 719  ? 11.941 79.596  -2.411  1.00 25.62 ? 719  SER A CA  1 
ATOM   5730 C  C   . SER A 1 719  ? 11.342 79.288  -1.042  1.00 27.14 ? 719  SER A C   1 
ATOM   5731 O  O   . SER A 1 719  ? 11.180 80.174  -0.234  1.00 32.07 ? 719  SER A O   1 
ATOM   5732 C  CB  . SER A 1 719  ? 11.029 80.530  -3.200  1.00 23.96 ? 719  SER A CB  1 
ATOM   5733 O  OG  . SER A 1 719  ? 9.862  79.825  -3.531  1.00 29.67 ? 719  SER A OG  1 
ATOM   5734 N  N   . HIS A 1 720  ? 10.994 78.030  -0.806  1.00 30.23 ? 720  HIS A N   1 
ATOM   5735 C  CA  . HIS A 1 720  ? 10.530 77.579  0.495   1.00 33.10 ? 720  HIS A CA  1 
ATOM   5736 C  C   . HIS A 1 720  ? 10.999 76.106  0.594   1.00 33.12 ? 720  HIS A C   1 
ATOM   5737 O  O   . HIS A 1 720  ? 11.264 75.438  -0.426  1.00 33.64 ? 720  HIS A O   1 
ATOM   5738 C  CB  . HIS A 1 720  ? 9.009  77.749  0.631   1.00 35.40 ? 720  HIS A CB  1 
ATOM   5739 C  CG  . HIS A 1 720  ? 8.251  77.313  -0.574  1.00 38.04 ? 720  HIS A CG  1 
ATOM   5740 N  ND1 . HIS A 1 720  ? 8.103  75.983  -0.910  1.00 37.95 ? 720  HIS A ND1 1 
ATOM   5741 C  CD2 . HIS A 1 720  ? 7.692  78.027  -1.583  1.00 38.64 ? 720  HIS A CD2 1 
ATOM   5742 C  CE1 . HIS A 1 720  ? 7.491  75.897  -2.081  1.00 38.21 ? 720  HIS A CE1 1 
ATOM   5743 N  NE2 . HIS A 1 720  ? 7.233  77.122  -2.511  1.00 38.91 ? 720  HIS A NE2 1 
ATOM   5744 N  N   . GLY A 1 721  ? 11.157 75.611  1.816   1.00 29.85 ? 721  GLY A N   1 
ATOM   5745 C  CA  . GLY A 1 721  ? 11.634 74.246  1.958   1.00 27.92 ? 721  GLY A CA  1 
ATOM   5746 C  C   . GLY A 1 721  ? 13.164 74.257  1.917   1.00 26.24 ? 721  GLY A C   1 
ATOM   5747 O  O   . GLY A 1 721  ? 13.790 75.315  1.982   1.00 23.54 ? 721  GLY A O   1 
ATOM   5748 N  N   . ASP A 1 722  ? 13.753 73.076  1.733   1.00 22.36 ? 722  ASP A N   1 
ATOM   5749 C  CA  . ASP A 1 722  ? 15.207 72.928  1.779   1.00 17.87 ? 722  ASP A CA  1 
ATOM   5750 C  C   . ASP A 1 722  ? 15.924 73.626  0.609   1.00 14.06 ? 722  ASP A C   1 
ATOM   5751 O  O   . ASP A 1 722  ? 15.549 73.536  -0.540  1.00 15.22 ? 722  ASP A O   1 
ATOM   5752 C  CB  . ASP A 1 722  ? 15.550 71.452  1.808   1.00 15.55 ? 722  ASP A CB  1 
ATOM   5753 C  CG  . ASP A 1 722  ? 15.000 70.723  3.059   1.00 18.75 ? 722  ASP A CG  1 
ATOM   5754 O  OD1 . ASP A 1 722  ? 14.760 71.349  4.142   1.00 19.84 ? 722  ASP A OD1 1 
ATOM   5755 O  OD2 . ASP A 1 722  ? 14.825 69.489  2.965   1.00 16.77 ? 722  ASP A OD2 1 
ATOM   5756 N  N   . ARG A 1 723  ? 17.001 74.321  0.975   1.00 13.20 ? 723  ARG A N   1 
ATOM   5757 C  CA  . ARG A 1 723  ? 17.833 75.069  0.039   1.00 12.54 ? 723  ARG A CA  1 
ATOM   5758 C  C   . ARG A 1 723  ? 19.104 74.317  -0.353  1.00 13.04 ? 723  ARG A C   1 
ATOM   5759 O  O   . ARG A 1 723  ? 19.736 73.650  0.461   1.00 13.13 ? 723  ARG A O   1 
ATOM   5760 C  CB  . ARG A 1 723  ? 18.196 76.437  0.610   1.00 14.82 ? 723  ARG A CB  1 
ATOM   5761 C  CG  . ARG A 1 723  ? 16.993 77.358  0.825   1.00 27.65 ? 723  ARG A CG  1 
ATOM   5762 C  CD  . ARG A 1 723  ? 17.393 78.650  1.507   1.00 37.70 ? 723  ARG A CD  1 
ATOM   5763 N  NE  . ARG A 1 723  ? 16.248 79.523  1.713   1.00 40.06 ? 723  ARG A NE  1 
ATOM   5764 C  CZ  . ARG A 1 723  ? 16.332 80.743  2.219   1.00 42.28 ? 723  ARG A CZ  1 
ATOM   5765 N  NH1 . ARG A 1 723  ? 15.236 81.471  2.366   1.00 41.50 ? 723  ARG A NH1 1 
ATOM   5766 N  NH2 . ARG A 1 723  ? 17.512 81.238  2.582   1.00 42.10 ? 723  ARG A NH2 1 
ATOM   5767 N  N   . SER A 1 724  ? 19.459 74.447  -1.623  1.00 10.44 ? 724  SER A N   1 
ATOM   5768 C  CA  . SER A 1 724  ? 20.723 73.958  -2.142  1.00 9.45  ? 724  SER A CA  1 
ATOM   5769 C  C   . SER A 1 724  ? 21.836 74.650  -1.362  1.00 9.96  ? 724  SER A C   1 
ATOM   5770 O  O   . SER A 1 724  ? 21.750 75.855  -1.015  1.00 12.41 ? 724  SER A O   1 
ATOM   5771 C  CB  . SER A 1 724  ? 20.888 74.335  -3.627  1.00 10.02 ? 724  SER A CB  1 
ATOM   5772 O  OG  . SER A 1 724  ? 19.877 73.691  -4.355  1.00 10.57 ? 724  SER A OG  1 
ATOM   5773 N  N   . GLY A 1 725  ? 22.959 73.933  -1.187  1.00 9.06  ? 725  GLY A N   1 
ATOM   5774 C  CA  . GLY A 1 725  ? 24.148 74.478  -0.526  1.00 8.31  ? 725  GLY A CA  1 
ATOM   5775 C  C   . GLY A 1 725  ? 25.381 73.738  -1.072  1.00 8.03  ? 725  GLY A C   1 
ATOM   5776 O  O   . GLY A 1 725  ? 25.290 73.108  -2.161  1.00 8.58  ? 725  GLY A O   1 
ATOM   5777 N  N   . ALA A 1 726  ? 26.510 73.813  -0.367  1.00 8.19  ? 726  ALA A N   1 
ATOM   5778 C  CA  . ALA A 1 726  ? 27.697 73.144  -0.856  1.00 6.88  ? 726  ALA A CA  1 
ATOM   5779 C  C   . ALA A 1 726  ? 27.529 71.650  -1.107  1.00 7.78  ? 726  ALA A C   1 
ATOM   5780 O  O   . ALA A 1 726  ? 28.225 71.085  -1.988  1.00 7.74  ? 726  ALA A O   1 
ATOM   5781 C  CB  . ALA A 1 726  ? 28.892 73.346  0.119   1.00 8.16  ? 726  ALA A CB  1 
ATOM   5782 N  N   . TYR A 1 727  ? 26.712 70.973  -0.298  1.00 7.05  ? 727  TYR A N   1 
ATOM   5783 C  CA  . TYR A 1 727  ? 26.486 69.533  -0.444  1.00 7.05  ? 727  TYR A CA  1 
ATOM   5784 C  C   . TYR A 1 727  ? 25.329 69.166  -1.341  1.00 6.96  ? 727  TYR A C   1 
ATOM   5785 O  O   . TYR A 1 727  ? 25.434 68.319  -2.220  1.00 8.26  ? 727  TYR A O   1 
ATOM   5786 C  CB  . TYR A 1 727  ? 26.206 68.897  0.926   1.00 7.23  ? 727  TYR A CB  1 
ATOM   5787 C  CG  . TYR A 1 727  ? 27.262 69.204  1.989   1.00 7.40  ? 727  TYR A CG  1 
ATOM   5788 C  CD1 . TYR A 1 727  ? 27.142 70.344  2.775   1.00 7.96  ? 727  TYR A CD1 1 
ATOM   5789 C  CD2 . TYR A 1 727  ? 28.368 68.358  2.194   1.00 7.67  ? 727  TYR A CD2 1 
ATOM   5790 C  CE1 . TYR A 1 727  ? 28.108 70.642  3.759   1.00 8.21  ? 727  TYR A CE1 1 
ATOM   5791 C  CE2 . TYR A 1 727  ? 29.323 68.649  3.166   1.00 6.52  ? 727  TYR A CE2 1 
ATOM   5792 C  CZ  . TYR A 1 727  ? 29.171 69.782  3.932   1.00 6.76  ? 727  TYR A CZ  1 
ATOM   5793 O  OH  . TYR A 1 727  ? 30.056 70.051  4.980   1.00 7.61  ? 727  TYR A OH  1 
ATOM   5794 N  N   . LEU A 1 728  ? 24.191 69.829  -1.088  1.00 7.44  ? 728  LEU A N   1 
ATOM   5795 C  CA  . LEU A 1 728  ? 22.923 69.439  -1.706  1.00 8.10  ? 728  LEU A CA  1 
ATOM   5796 C  C   . LEU A 1 728  ? 22.563 70.208  -2.943  1.00 7.27  ? 728  LEU A C   1 
ATOM   5797 O  O   . LEU A 1 728  ? 22.738 71.405  -2.987  1.00 8.58  ? 728  LEU A O   1 
ATOM   5798 C  CB  . LEU A 1 728  ? 21.734 69.642  -0.702  1.00 9.50  ? 728  LEU A CB  1 
ATOM   5799 C  CG  . LEU A 1 728  ? 21.912 69.002  0.698   1.00 7.72  ? 728  LEU A CG  1 
ATOM   5800 C  CD1 . LEU A 1 728  ? 20.623 69.283  1.501   1.00 11.88 ? 728  LEU A CD1 1 
ATOM   5801 C  CD2 . LEU A 1 728  ? 22.235 67.534  0.627   1.00 9.45  ? 728  LEU A CD2 1 
ATOM   5802 N  N   . PHE A 1 729  ? 22.022 69.478  -3.923  1.00 7.49  ? 729  PHE A N   1 
ATOM   5803 C  CA  . PHE A 1 729  ? 21.479 70.084  -5.146  1.00 7.82  ? 729  PHE A CA  1 
ATOM   5804 C  C   . PHE A 1 729  ? 19.949 69.866  -5.043  1.00 8.51  ? 729  PHE A C   1 
ATOM   5805 O  O   . PHE A 1 729  ? 19.465 68.729  -5.154  1.00 8.79  ? 729  PHE A O   1 
ATOM   5806 C  CB  . PHE A 1 729  ? 22.086 69.353  -6.346  1.00 8.47  ? 729  PHE A CB  1 
ATOM   5807 C  CG  . PHE A 1 729  ? 21.537 69.784  -7.694  1.00 7.58  ? 729  PHE A CG  1 
ATOM   5808 C  CD1 . PHE A 1 729  ? 21.223 71.120  -7.944  1.00 9.04  ? 729  PHE A CD1 1 
ATOM   5809 C  CD2 . PHE A 1 729  ? 21.447 68.863  -8.721  1.00 7.43  ? 729  PHE A CD2 1 
ATOM   5810 C  CE1 . PHE A 1 729  ? 20.815 71.534  -9.249  1.00 7.89  ? 729  PHE A CE1 1 
ATOM   5811 C  CE2 . PHE A 1 729  ? 21.043 69.269  -10.021 1.00 9.22  ? 729  PHE A CE2 1 
ATOM   5812 C  CZ  . PHE A 1 729  ? 20.728 70.603  -10.280 1.00 8.64  ? 729  PHE A CZ  1 
ATOM   5813 N  N   . LEU A 1 730  ? 19.242 70.986  -4.863  1.00 9.12  ? 730  LEU A N   1 
ATOM   5814 C  CA  . LEU A 1 730  ? 17.757 70.978  -4.669  1.00 9.78  ? 730  LEU A CA  1 
ATOM   5815 C  C   . LEU A 1 730  ? 17.170 72.000  -5.642  1.00 9.58  ? 730  LEU A C   1 
ATOM   5816 O  O   . LEU A 1 730  ? 16.743 73.089  -5.255  1.00 9.78  ? 730  LEU A O   1 
ATOM   5817 C  CB  . LEU A 1 730  ? 17.438 71.336  -3.190  1.00 10.65 ? 730  LEU A CB  1 
ATOM   5818 C  CG  . LEU A 1 730  ? 17.827 70.204  -2.210  1.00 10.96 ? 730  LEU A CG  1 
ATOM   5819 C  CD1 . LEU A 1 730  ? 17.862 70.748  -0.808  1.00 11.19 ? 730  LEU A CD1 1 
ATOM   5820 C  CD2 . LEU A 1 730  ? 16.832 69.050  -2.311  1.00 14.04 ? 730  LEU A CD2 1 
ATOM   5821 N  N   . PRO A 1 731  ? 17.209 71.686  -6.930  1.00 10.10 ? 731  PRO A N   1 
ATOM   5822 C  CA  . PRO A 1 731  ? 16.714 72.632  -7.933  1.00 10.11 ? 731  PRO A CA  1 
ATOM   5823 C  C   . PRO A 1 731  ? 15.254 72.926  -7.830  1.00 10.03 ? 731  PRO A C   1 
ATOM   5824 O  O   . PRO A 1 731  ? 14.459 72.092  -7.376  1.00 11.46 ? 731  PRO A O   1 
ATOM   5825 C  CB  . PRO A 1 731  ? 17.073 71.941  -9.232  1.00 11.12 ? 731  PRO A CB  1 
ATOM   5826 C  CG  . PRO A 1 731  ? 16.991 70.465  -8.941  1.00 9.88  ? 731  PRO A CG  1 
ATOM   5827 C  CD  . PRO A 1 731  ? 17.609 70.396  -7.536  1.00 8.59  ? 731  PRO A CD  1 
ATOM   5828 N  N   . ASN A 1 732  ? 14.938 74.137  -8.298  1.00 11.63 ? 732  ASN A N   1 
ATOM   5829 C  CA  . ASN A 1 732  ? 13.505 74.541  -8.357  1.00 12.19 ? 732  ASN A CA  1 
ATOM   5830 C  C   . ASN A 1 732  ? 13.012 74.144  -9.744  1.00 13.04 ? 732  ASN A C   1 
ATOM   5831 O  O   . ASN A 1 732  ? 12.611 75.019  -10.542 1.00 18.52 ? 732  ASN A O   1 
ATOM   5832 C  CB  . ASN A 1 732  ? 13.357 76.059  -8.102  1.00 14.51 ? 732  ASN A CB  1 
ATOM   5833 C  CG  . ASN A 1 732  ? 14.103 76.922  -9.106  1.00 20.62 ? 732  ASN A CG  1 
ATOM   5834 O  OD1 . ASN A 1 732  ? 15.060 76.517  -9.714  1.00 18.84 ? 732  ASN A OD1 1 
ATOM   5835 N  ND2 . ASN A 1 732  ? 13.638 78.173  -9.261  1.00 22.61 ? 732  ASN A ND2 1 
ATOM   5836 N  N   . GLY A 1 733  ? 13.114 72.886  -10.101 1.00 11.34 ? 733  GLY A N   1 
ATOM   5837 C  CA  . GLY A 1 733  ? 12.658 72.404  -11.401 1.00 12.87 ? 733  GLY A CA  1 
ATOM   5838 C  C   . GLY A 1 733  ? 13.754 72.340  -12.474 1.00 10.45 ? 733  GLY A C   1 
ATOM   5839 O  O   . GLY A 1 733  ? 14.923 72.721  -12.213 1.00 10.78 ? 733  GLY A O   1 
ATOM   5840 N  N   . PRO A 1 734  ? 13.419 71.849  -13.670 1.00 9.47  ? 734  PRO A N   1 
ATOM   5841 C  CA  . PRO A 1 734  ? 14.371 71.756  -14.778 1.00 10.28 ? 734  PRO A CA  1 
ATOM   5842 C  C   . PRO A 1 734  ? 14.987 73.134  -15.077 1.00 10.10 ? 734  PRO A C   1 
ATOM   5843 O  O   . PRO A 1 734  ? 14.425 74.194  -14.827 1.00 10.47 ? 734  PRO A O   1 
ATOM   5844 C  CB  . PRO A 1 734  ? 13.532 71.284  -15.954 1.00 11.33 ? 734  PRO A CB  1 
ATOM   5845 C  CG  . PRO A 1 734  ? 12.452 70.420  -15.265 1.00 16.90 ? 734  PRO A CG  1 
ATOM   5846 C  CD  . PRO A 1 734  ? 12.110 71.264  -14.039 1.00 12.19 ? 734  PRO A CD  1 
ATOM   5847 N  N   . ALA A 1 735  ? 16.189 73.076  -15.642 1.00 9.30  ? 735  ALA A N   1 
ATOM   5848 C  CA  . ALA A 1 735  ? 16.914 74.298  -15.981 1.00 9.17  ? 735  ALA A CA  1 
ATOM   5849 C  C   . ALA A 1 735  ? 16.245 75.134  -17.072 1.00 9.22  ? 735  ALA A C   1 
ATOM   5850 O  O   . ALA A 1 735  ? 15.558 74.588  -17.925 1.00 11.66 ? 735  ALA A O   1 
ATOM   5851 C  CB  . ALA A 1 735  ? 18.308 73.873  -16.392 1.00 10.01 ? 735  ALA A CB  1 
ATOM   5852 N  N   . SER A 1 736  ? 16.494 76.438  -17.001 1.00 10.53 ? 736  SER A N   1 
ATOM   5853 C  CA  . SER A 1 736  ? 15.957 77.402  -17.978 1.00 11.24 ? 736  SER A CA  1 
ATOM   5854 C  C   . SER A 1 736  ? 17.117 77.894  -18.830 1.00 11.63 ? 736  SER A C   1 
ATOM   5855 O  O   . SER A 1 736  ? 18.190 78.140  -18.312 1.00 11.22 ? 736  SER A O   1 
ATOM   5856 C  CB  . SER A 1 736  ? 15.365 78.570  -17.233 1.00 14.31 ? 736  SER A CB  1 
ATOM   5857 O  OG  . SER A 1 736  ? 14.444 78.121  -16.258 1.00 26.24 ? 736  SER A OG  1 
ATOM   5858 N  N   . PRO A 1 737  ? 16.910 78.108  -20.127 1.00 13.37 ? 737  PRO A N   1 
ATOM   5859 C  CA  . PRO A 1 737  ? 18.026 78.568  -20.976 1.00 14.80 ? 737  PRO A CA  1 
ATOM   5860 C  C   . PRO A 1 737  ? 18.585 79.909  -20.519 1.00 14.80 ? 737  PRO A C   1 
ATOM   5861 O  O   . PRO A 1 737  ? 17.832 80.822  -20.105 1.00 16.16 ? 737  PRO A O   1 
ATOM   5862 C  CB  . PRO A 1 737  ? 17.396 78.730  -22.378 1.00 18.39 ? 737  PRO A CB  1 
ATOM   5863 C  CG  . PRO A 1 737  ? 16.206 77.814  -22.330 1.00 20.01 ? 737  PRO A CG  1 
ATOM   5864 C  CD  . PRO A 1 737  ? 15.665 77.960  -20.903 1.00 15.45 ? 737  PRO A CD  1 
ATOM   5865 N  N   . VAL A 1 738  ? 19.915 80.060  -20.573 1.00 13.77 ? 738  VAL A N   1 
ATOM   5866 C  CA  . VAL A 1 738  ? 20.528 81.372  -20.311 1.00 11.12 ? 738  VAL A CA  1 
ATOM   5867 C  C   . VAL A 1 738  ? 20.124 82.259  -21.539 1.00 12.12 ? 738  VAL A C   1 
ATOM   5868 O  O   . VAL A 1 738  ? 20.222 81.836  -22.689 1.00 14.78 ? 738  VAL A O   1 
ATOM   5869 C  CB  . VAL A 1 738  ? 22.075 81.230  -20.241 1.00 12.85 ? 738  VAL A CB  1 
ATOM   5870 C  CG1 . VAL A 1 738  ? 22.733 82.646  -20.212 1.00 16.45 ? 738  VAL A CG1 1 
ATOM   5871 C  CG2 . VAL A 1 738  ? 22.526 80.434  -18.964 1.00 14.82 ? 738  VAL A CG2 1 
ATOM   5872 N  N   . GLU A 1 739  ? 19.667 83.474  -21.262 1.00 14.63 ? 739  GLU A N   1 
ATOM   5873 C  CA  . GLU A 1 739  ? 19.272 84.427  -22.320 1.00 16.61 ? 739  GLU A CA  1 
ATOM   5874 C  C   . GLU A 1 739  ? 20.610 84.953  -22.872 1.00 13.93 ? 739  GLU A C   1 
ATOM   5875 O  O   . GLU A 1 739  ? 21.376 85.576  -22.139 1.00 16.49 ? 739  GLU A O   1 
ATOM   5876 C  CB  . GLU A 1 739  ? 18.495 85.573  -21.689 1.00 20.71 ? 739  GLU A CB  1 
ATOM   5877 C  CG  . GLU A 1 739  ? 17.157 85.164  -21.195 1.00 31.74 ? 739  GLU A CG  1 
ATOM   5878 C  CD  . GLU A 1 739  ? 16.223 86.359  -20.938 1.00 40.12 ? 739  GLU A CD  1 
ATOM   5879 O  OE1 . GLU A 1 739  ? 16.555 87.497  -21.330 1.00 39.86 ? 739  GLU A OE1 1 
ATOM   5880 O  OE2 . GLU A 1 739  ? 15.147 86.135  -20.346 1.00 44.78 ? 739  GLU A OE2 1 
ATOM   5881 N  N   . LEU A 1 740  ? 20.855 84.704  -24.146 1.00 16.55 ? 740  LEU A N   1 
ATOM   5882 C  CA  . LEU A 1 740  ? 22.168 85.021  -24.730 1.00 17.03 ? 740  LEU A CA  1 
ATOM   5883 C  C   . LEU A 1 740  ? 22.355 86.407  -25.318 1.00 19.80 ? 740  LEU A C   1 
ATOM   5884 O  O   . LEU A 1 740  ? 23.483 86.853  -25.484 1.00 21.82 ? 740  LEU A O   1 
ATOM   5885 C  CB  . LEU A 1 740  ? 22.495 84.000  -25.820 1.00 18.98 ? 740  LEU A CB  1 
ATOM   5886 C  CG  . LEU A 1 740  ? 22.521 82.537  -25.345 1.00 14.78 ? 740  LEU A CG  1 
ATOM   5887 C  CD1 . LEU A 1 740  ? 22.993 81.642  -26.465 1.00 16.49 ? 740  LEU A CD1 1 
ATOM   5888 C  CD2 . LEU A 1 740  ? 23.499 82.377  -24.117 1.00 18.14 ? 740  LEU A CD2 1 
ATOM   5889 N  N   . GLY A 1 741  ? 21.255 87.068  -25.632 1.00 21.12 ? 741  GLY A N   1 
ATOM   5890 C  CA  . GLY A 1 741  ? 21.379 88.372  -26.289 1.00 19.57 ? 741  GLY A CA  1 
ATOM   5891 C  C   . GLY A 1 741  ? 21.939 88.170  -27.713 1.00 20.01 ? 741  GLY A C   1 
ATOM   5892 O  O   . GLY A 1 741  ? 21.587 87.213  -28.374 1.00 21.82 ? 741  GLY A O   1 
ATOM   5893 N  N   . GLN A 1 742  ? 22.735 89.108  -28.212 1.00 21.15 ? 742  GLN A N   1 
ATOM   5894 C  CA  . GLN A 1 742  ? 23.412 88.888  -29.482 1.00 17.81 ? 742  GLN A CA  1 
ATOM   5895 C  C   . GLN A 1 742  ? 24.907 88.862  -29.178 1.00 17.74 ? 742  GLN A C   1 
ATOM   5896 O  O   . GLN A 1 742  ? 25.569 89.884  -29.229 1.00 18.45 ? 742  GLN A O   1 
ATOM   5897 C  CB  . GLN A 1 742  ? 23.114 89.997  -30.513 1.00 23.57 ? 742  GLN A CB  1 
ATOM   5898 C  CG  . GLN A 1 742  ? 23.336 89.577  -31.965 1.00 31.46 ? 742  GLN A CG  1 
ATOM   5899 C  CD  . GLN A 1 742  ? 22.603 90.450  -32.990 1.00 40.05 ? 742  GLN A CD  1 
ATOM   5900 O  OE1 . GLN A 1 742  ? 22.891 90.381  -34.177 1.00 40.30 ? 742  GLN A OE1 1 
ATOM   5901 N  NE2 . GLN A 1 742  ? 21.635 91.248  -32.530 1.00 39.36 ? 742  GLN A NE2 1 
ATOM   5902 N  N   . PRO A 1 743  ? 25.416 87.696  -28.802 1.00 15.09 ? 743  PRO A N   1 
ATOM   5903 C  CA  . PRO A 1 743  ? 26.831 87.656  -28.414 1.00 11.57 ? 743  PRO A CA  1 
ATOM   5904 C  C   . PRO A 1 743  ? 27.892 87.838  -29.501 1.00 12.20 ? 743  PRO A C   1 
ATOM   5905 O  O   . PRO A 1 743  ? 27.662 87.602  -30.678 1.00 13.92 ? 743  PRO A O   1 
ATOM   5906 C  CB  . PRO A 1 743  ? 26.940 86.315  -27.674 1.00 14.69 ? 743  PRO A CB  1 
ATOM   5907 C  CG  . PRO A 1 743  ? 25.957 85.432  -28.397 1.00 13.85 ? 743  PRO A CG  1 
ATOM   5908 C  CD  . PRO A 1 743  ? 24.787 86.359  -28.777 1.00 12.80 ? 743  PRO A CD  1 
ATOM   5909 N  N   . VAL A 1 744  ? 29.047 88.335  -29.067 1.00 10.44 ? 744  VAL A N   1 
ATOM   5910 C  CA  . VAL A 1 744  ? 30.186 88.532  -29.988 1.00 10.06 ? 744  VAL A CA  1 
ATOM   5911 C  C   . VAL A 1 744  ? 30.866 87.188  -30.211 1.00 8.31  ? 744  VAL A C   1 
ATOM   5912 O  O   . VAL A 1 744  ? 31.204 86.470  -29.239 1.00 9.81  ? 744  VAL A O   1 
ATOM   5913 C  CB  . VAL A 1 744  ? 31.185 89.519  -29.360 1.00 9.55  ? 744  VAL A CB  1 
ATOM   5914 C  CG1 . VAL A 1 744  ? 32.380 89.705  -30.285 1.00 11.55 ? 744  VAL A CG1 1 
ATOM   5915 C  CG2 . VAL A 1 744  ? 30.488 90.941  -29.156 1.00 12.62 ? 744  VAL A CG2 1 
ATOM   5916 N  N   . VAL A 1 745  ? 31.066 86.825  -31.446 1.00 7.67  ? 745  VAL A N   1 
ATOM   5917 C  CA  . VAL A 1 745  ? 31.681 85.539  -31.851 1.00 8.09  ? 745  VAL A CA  1 
ATOM   5918 C  C   . VAL A 1 745  ? 32.981 85.765  -32.568 1.00 7.91  ? 745  VAL A C   1 
ATOM   5919 O  O   . VAL A 1 745  ? 33.054 86.595  -33.509 1.00 9.78  ? 745  VAL A O   1 
ATOM   5920 C  CB  . VAL A 1 745  ? 30.711 84.749  -32.763 1.00 8.65  ? 745  VAL A CB  1 
ATOM   5921 C  CG1 . VAL A 1 745  ? 31.367 83.413  -33.197 1.00 10.38 ? 745  VAL A CG1 1 
ATOM   5922 C  CG2 . VAL A 1 745  ? 29.401 84.522  -32.031 1.00 9.13  ? 745  VAL A CG2 1 
ATOM   5923 N  N   . LEU A 1 746  ? 34.086 85.126  -32.171 1.00 7.75  ? 746  LEU A N   1 
ATOM   5924 C  CA  . LEU A 1 746  ? 35.372 85.271  -32.803 1.00 7.84  ? 746  LEU A CA  1 
ATOM   5925 C  C   . LEU A 1 746  ? 35.781 83.987  -33.455 1.00 8.37  ? 746  LEU A C   1 
ATOM   5926 O  O   . LEU A 1 746  ? 35.831 82.927  -32.780 1.00 8.41  ? 746  LEU A O   1 
ATOM   5927 C  CB  . LEU A 1 746  ? 36.400 85.654  -31.723 1.00 9.47  ? 746  LEU A CB  1 
ATOM   5928 C  CG  . LEU A 1 746  ? 37.852 85.615  -32.225 1.00 11.53 ? 746  LEU A CG  1 
ATOM   5929 C  CD1 . LEU A 1 746  ? 38.160 86.729  -33.278 1.00 14.00 ? 746  LEU A CD1 1 
ATOM   5930 C  CD2 . LEU A 1 746  ? 38.759 85.773  -30.950 1.00 15.15 ? 746  LEU A CD2 1 
ATOM   5931 N  N   . VAL A 1 747  ? 36.046 84.009  -34.731 1.00 7.81  ? 747  VAL A N   1 
ATOM   5932 C  CA  . VAL A 1 747  ? 36.450 82.820  -35.486 1.00 7.93  ? 747  VAL A CA  1 
ATOM   5933 C  C   . VAL A 1 747  ? 37.883 82.950  -35.919 1.00 9.48  ? 747  VAL A C   1 
ATOM   5934 O  O   . VAL A 1 747  ? 38.265 83.924  -36.596 1.00 10.40 ? 747  VAL A O   1 
ATOM   5935 C  CB  . VAL A 1 747  ? 35.559 82.667  -36.747 1.00 10.04 ? 747  VAL A CB  1 
ATOM   5936 C  CG1 . VAL A 1 747  ? 35.923 81.347  -37.502 1.00 11.25 ? 747  VAL A CG1 1 
ATOM   5937 C  CG2 . VAL A 1 747  ? 34.113 82.706  -36.371 1.00 10.32 ? 747  VAL A CG2 1 
ATOM   5938 N  N   . THR A 1 748  ? 38.747 82.014  -35.557 1.00 8.70  ? 748  THR A N   1 
ATOM   5939 C  CA  . THR A 1 748  ? 40.117 82.014  -35.999 1.00 9.83  ? 748  THR A CA  1 
ATOM   5940 C  C   . THR A 1 748  ? 40.316 80.806  -36.857 1.00 9.65  ? 748  THR A C   1 
ATOM   5941 O  O   . THR A 1 748  ? 39.994 79.674  -36.433 1.00 12.09 ? 748  THR A O   1 
ATOM   5942 C  CB  . THR A 1 748  ? 41.058 82.033  -34.767 1.00 11.44 ? 748  THR A CB  1 
ATOM   5943 O  OG1 . THR A 1 748  ? 40.828 83.250  -34.006 1.00 13.13 ? 748  THR A OG1 1 
ATOM   5944 C  CG2 . THR A 1 748  ? 42.497 81.945  -35.195 1.00 12.65 ? 748  THR A CG2 1 
ATOM   5945 N  N   . LYS A 1 749  ? 40.804 80.965  -38.086 1.00 9.28  ? 749  LYS A N   1 
ATOM   5946 C  CA  . LYS A 1 749  ? 40.967 79.847  -39.009 1.00 9.63  ? 749  LYS A CA  1 
ATOM   5947 C  C   . LYS A 1 749  ? 42.412 79.709  -39.387 1.00 10.87 ? 749  LYS A C   1 
ATOM   5948 O  O   . LYS A 1 749  ? 43.044 80.646  -39.946 1.00 10.55 ? 749  LYS A O   1 
ATOM   5949 C  CB  . LYS A 1 749  ? 40.145 80.047  -40.286 1.00 12.42 ? 749  LYS A CB  1 
ATOM   5950 C  CG  . LYS A 1 749  ? 40.335 78.879  -41.298 1.00 14.63 ? 749  LYS A CG  1 
ATOM   5951 C  CD  . LYS A 1 749  ? 39.399 79.100  -42.540 1.00 17.67 ? 749  LYS A CD  1 
ATOM   5952 C  CE  . LYS A 1 749  ? 39.762 78.264  -43.733 1.00 24.26 ? 749  LYS A CE  1 
ATOM   5953 N  NZ  . LYS A 1 749  ? 38.879 78.835  -44.817 1.00 33.26 ? 749  LYS A NZ  1 
ATOM   5954 N  N   . GLY A 1 750  ? 42.986 78.554  -39.069 1.00 10.10 ? 750  GLY A N   1 
ATOM   5955 C  CA  . GLY A 1 750  ? 44.368 78.287  -39.387 1.00 11.14 ? 750  GLY A CA  1 
ATOM   5956 C  C   . GLY A 1 750  ? 44.563 76.899  -39.964 1.00 11.09 ? 750  GLY A C   1 
ATOM   5957 O  O   . GLY A 1 750  ? 43.679 76.022  -39.880 1.00 12.54 ? 750  GLY A O   1 
ATOM   5958 N  N   . LYS A 1 751  ? 45.747 76.702  -40.545 1.00 11.88 ? 751  LYS A N   1 
ATOM   5959 C  CA  . LYS A 1 751  ? 46.067 75.415  -41.133 1.00 11.88 ? 751  LYS A CA  1 
ATOM   5960 C  C   . LYS A 1 751  ? 46.199 74.325  -40.047 1.00 10.90 ? 751  LYS A C   1 
ATOM   5961 O  O   . LYS A 1 751  ? 45.807 73.169  -40.287 1.00 12.07 ? 751  LYS A O   1 
ATOM   5962 C  CB  . LYS A 1 751  ? 47.374 75.491  -41.901 1.00 15.43 ? 751  LYS A CB  1 
ATOM   5963 C  CG  . LYS A 1 751  ? 47.685 74.165  -42.617 1.00 24.91 ? 751  LYS A CG  1 
ATOM   5964 C  CD  . LYS A 1 751  ? 48.709 74.335  -43.751 1.00 32.07 ? 751  LYS A CD  1 
ATOM   5965 C  CE  . LYS A 1 751  ? 48.908 72.985  -44.436 1.00 34.98 ? 751  LYS A CE  1 
ATOM   5966 N  NZ  . LYS A 1 751  ? 47.583 72.344  -44.790 1.00 42.34 ? 751  LYS A NZ  1 
ATOM   5967 N  N   . LEU A 1 752  ? 46.772 74.670  -38.896 1.00 9.75  ? 752  LEU A N   1 
ATOM   5968 C  CA  . LEU A 1 752  ? 46.971 73.670  -37.814 1.00 9.57  ? 752  LEU A CA  1 
ATOM   5969 C  C   . LEU A 1 752  ? 45.890 73.709  -36.745 1.00 10.83 ? 752  LEU A C   1 
ATOM   5970 O  O   . LEU A 1 752  ? 45.579 72.696  -36.133 1.00 10.07 ? 752  LEU A O   1 
ATOM   5971 C  CB  . LEU A 1 752  ? 48.318 73.892  -37.132 1.00 10.04 ? 752  LEU A CB  1 
ATOM   5972 C  CG  . LEU A 1 752  ? 49.549 73.820  -38.059 1.00 11.66 ? 752  LEU A CG  1 
ATOM   5973 C  CD1 . LEU A 1 752  ? 50.815 73.921  -37.209 1.00 13.31 ? 752  LEU A CD1 1 
ATOM   5974 C  CD2 . LEU A 1 752  ? 49.503 72.632  -38.982 1.00 16.08 ? 752  LEU A CD2 1 
ATOM   5975 N  N   . GLU A 1 753  ? 45.288 74.873  -36.507 1.00 10.50 ? 753  GLU A N   1 
ATOM   5976 C  CA  . GLU A 1 753  ? 44.313 75.014  -35.437 1.00 9.44  ? 753  GLU A CA  1 
ATOM   5977 C  C   . GLU A 1 753  ? 43.323 76.102  -35.806 1.00 9.36  ? 753  GLU A C   1 
ATOM   5978 O  O   . GLU A 1 753  ? 43.736 77.212  -36.235 1.00 10.08 ? 753  GLU A O   1 
ATOM   5979 C  CB  . GLU A 1 753  ? 45.038 75.384  -34.133 1.00 9.43  ? 753  GLU A CB  1 
ATOM   5980 C  CG  . GLU A 1 753  ? 44.087 75.595  -32.914 1.00 12.67 ? 753  GLU A CG  1 
ATOM   5981 C  CD  . GLU A 1 753  ? 44.829 76.016  -31.641 1.00 17.57 ? 753  GLU A CD  1 
ATOM   5982 O  OE1 . GLU A 1 753  ? 45.150 77.215  -31.532 1.00 22.80 ? 753  GLU A OE1 1 
ATOM   5983 O  OE2 . GLU A 1 753  ? 45.063 75.125  -30.807 1.00 21.13 ? 753  GLU A OE2 1 
ATOM   5984 N  N   . SER A 1 754  ? 42.060 75.816  -35.591 1.00 8.80  ? 754  SER A N   1 
ATOM   5985 C  CA  . SER A 1 754  ? 40.994 76.817  -35.808 1.00 8.15  ? 754  SER A CA  1 
ATOM   5986 C  C   . SER A 1 754  ? 40.130 76.822  -34.567 1.00 8.74  ? 754  SER A C   1 
ATOM   5987 O  O   . SER A 1 754  ? 40.132 75.864  -33.748 1.00 9.29  ? 754  SER A O   1 
ATOM   5988 C  CB  . SER A 1 754  ? 40.167 76.458  -37.013 1.00 8.47  ? 754  SER A CB  1 
ATOM   5989 O  OG  . SER A 1 754  ? 40.940 76.583  -38.208 1.00 9.17  ? 754  SER A OG  1 
ATOM   5990 N  N   . SER A 1 755  ? 39.355 77.877  -34.363 1.00 7.94  ? 755  SER A N   1 
ATOM   5991 C  CA  . SER A 1 755  ? 38.486 77.907  -33.197 1.00 9.67  ? 755  SER A CA  1 
ATOM   5992 C  C   . SER A 1 755  ? 37.371 78.911  -33.338 1.00 8.39  ? 755  SER A C   1 
ATOM   5993 O  O   . SER A 1 755  ? 37.491 79.886  -34.121 1.00 9.12  ? 755  SER A O   1 
ATOM   5994 C  CB  A SER A 1 755  ? 39.282 78.270  -31.959 0.50 13.92 ? 755  SER A CB  1 
ATOM   5995 C  CB  B SER A 1 755  ? 39.453 78.357  -32.036 0.50 16.75 ? 755  SER A CB  1 
ATOM   5996 O  OG  A SER A 1 755  ? 39.793 79.584  -32.087 0.50 14.76 ? 755  SER A OG  1 
ATOM   5997 O  OG  B SER A 1 755  ? 38.910 79.286  -31.123 0.50 37.39 ? 755  SER A OG  1 
ATOM   5998 N  N   . VAL A 1 756  ? 36.295 78.691  -32.604 1.00 7.09  ? 756  VAL A N   1 
ATOM   5999 C  CA  . VAL A 1 756  ? 35.144 79.590  -32.527 1.00 8.06  ? 756  VAL A CA  1 
ATOM   6000 C  C   . VAL A 1 756  ? 34.996 79.902  -31.034 1.00 8.05  ? 756  VAL A C   1 
ATOM   6001 O  O   . VAL A 1 756  ? 34.831 78.952  -30.208 1.00 9.50  ? 756  VAL A O   1 
ATOM   6002 C  CB  . VAL A 1 756  ? 33.855 78.950  -33.054 1.00 8.10  ? 756  VAL A CB  1 
ATOM   6003 C  CG1 . VAL A 1 756  ? 32.651 79.920  -32.824 1.00 10.01 ? 756  VAL A CG1 1 
ATOM   6004 C  CG2 . VAL A 1 756  ? 34.084 78.615  -34.557 1.00 10.40 ? 756  VAL A CG2 1 
ATOM   6005 N  N   . SER A 1 757  ? 35.007 81.170  -30.657 1.00 7.82  ? 757  SER A N   1 
ATOM   6006 C  CA  . SER A 1 757  ? 34.861 81.556  -29.255 1.00 8.81  ? 757  SER A CA  1 
ATOM   6007 C  C   . SER A 1 757  ? 33.733 82.538  -29.127 1.00 9.63  ? 757  SER A C   1 
ATOM   6008 O  O   . SER A 1 757  ? 33.612 83.422  -30.013 1.00 11.02 ? 757  SER A O   1 
ATOM   6009 C  CB  . SER A 1 757  ? 36.153 82.243  -28.759 1.00 10.56 ? 757  SER A CB  1 
ATOM   6010 O  OG  . SER A 1 757  ? 37.288 81.387  -28.907 1.00 12.46 ? 757  SER A OG  1 
ATOM   6011 N  N   . VAL A 1 758  ? 32.932 82.466  -28.079 1.00 7.84  ? 758  VAL A N   1 
ATOM   6012 C  CA  . VAL A 1 758  ? 31.788 83.403  -27.930 1.00 7.45  ? 758  VAL A CA  1 
ATOM   6013 C  C   . VAL A 1 758  ? 31.683 83.862  -26.507 1.00 7.82  ? 758  VAL A C   1 
ATOM   6014 O  O   . VAL A 1 758  ? 31.845 83.041  -25.561 1.00 8.36  ? 758  VAL A O   1 
ATOM   6015 C  CB  . VAL A 1 758  ? 30.474 82.754  -28.458 1.00 8.81  ? 758  VAL A CB  1 
ATOM   6016 C  CG1 . VAL A 1 758  ? 30.148 81.408  -27.731 1.00 10.16 ? 758  VAL A CG1 1 
ATOM   6017 C  CG2 . VAL A 1 758  ? 29.332 83.727  -28.272 1.00 9.49  ? 758  VAL A CG2 1 
ATOM   6018 N  N   . GLY A 1 759  ? 31.419 85.140  -26.322 1.00 8.20  ? 759  GLY A N   1 
ATOM   6019 C  CA  . GLY A 1 759  ? 31.276 85.702  -24.971 1.00 9.72  ? 759  GLY A CA  1 
ATOM   6020 C  C   . GLY A 1 759  ? 29.856 85.670  -24.519 1.00 9.72  ? 759  GLY A C   1 
ATOM   6021 O  O   . GLY A 1 759  ? 29.052 86.547  -24.846 1.00 10.66 ? 759  GLY A O   1 
ATOM   6022 N  N   . LEU A 1 760  ? 29.462 84.646  -23.796 1.00 9.79  ? 760  LEU A N   1 
ATOM   6023 C  CA  . LEU A 1 760  ? 28.119 84.502  -23.259 1.00 9.58  ? 760  LEU A CA  1 
ATOM   6024 C  C   . LEU A 1 760  ? 28.062 85.002  -21.863 1.00 9.52  ? 760  LEU A C   1 
ATOM   6025 O  O   . LEU A 1 760  ? 29.109 85.150  -21.212 1.00 11.12 ? 760  LEU A O   1 
ATOM   6026 C  CB  . LEU A 1 760  ? 27.762 82.986  -23.246 1.00 11.50 ? 760  LEU A CB  1 
ATOM   6027 C  CG  . LEU A 1 760  ? 27.925 82.290  -24.596 1.00 12.12 ? 760  LEU A CG  1 
ATOM   6028 C  CD1 . LEU A 1 760  ? 27.674 80.775  -24.473 1.00 14.42 ? 760  LEU A CD1 1 
ATOM   6029 C  CD2 . LEU A 1 760  ? 26.976 82.881  -25.633 1.00 14.82 ? 760  LEU A CD2 1 
ATOM   6030 N  N   . PRO A 1 761  ? 26.879 85.244  -21.321 1.00 11.10 ? 761  PRO A N   1 
ATOM   6031 C  CA  . PRO A 1 761  ? 26.815 85.697  -19.925 1.00 11.47 ? 761  PRO A CA  1 
ATOM   6032 C  C   . PRO A 1 761  ? 27.375 84.553  -19.039 1.00 13.32 ? 761  PRO A C   1 
ATOM   6033 O  O   . PRO A 1 761  ? 26.939 83.387  -19.133 1.00 14.02 ? 761  PRO A O   1 
ATOM   6034 C  CB  . PRO A 1 761  ? 25.305 85.913  -19.681 1.00 13.80 ? 761  PRO A CB  1 
ATOM   6035 C  CG  . PRO A 1 761  ? 24.754 86.161  -21.100 1.00 14.86 ? 761  PRO A CG  1 
ATOM   6036 C  CD  . PRO A 1 761  ? 25.568 85.260  -21.989 1.00 12.88 ? 761  PRO A CD  1 
ATOM   6037 N  N   . SER A 1 762  ? 28.345 84.924  -18.222 1.00 10.66 ? 762  SER A N   1 
ATOM   6038 C  CA  . SER A 1 762  ? 29.085 84.062  -17.298 1.00 10.58 ? 762  SER A CA  1 
ATOM   6039 C  C   . SER A 1 762  ? 30.026 83.066  -17.944 1.00 9.74  ? 762  SER A C   1 
ATOM   6040 O  O   . SER A 1 762  ? 30.716 82.361  -17.191 1.00 9.89  ? 762  SER A O   1 
ATOM   6041 C  CB  . SER A 1 762  ? 28.162 83.220  -16.401 1.00 13.13 ? 762  SER A CB  1 
ATOM   6042 O  OG  . SER A 1 762  ? 27.197 83.993  -15.714 1.00 15.62 ? 762  SER A OG  1 
ATOM   6043 N  N   . VAL A 1 763  ? 30.100 82.971  -19.260 1.00 8.92  ? 763  VAL A N   1 
ATOM   6044 C  CA  . VAL A 1 763  ? 30.976 81.986  -19.847 1.00 8.74  ? 763  VAL A CA  1 
ATOM   6045 C  C   . VAL A 1 763  ? 31.571 82.413  -21.182 1.00 8.95  ? 763  VAL A C   1 
ATOM   6046 O  O   . VAL A 1 763  ? 30.805 82.745  -22.122 1.00 10.05 ? 763  VAL A O   1 
ATOM   6047 C  CB  . VAL A 1 763  ? 30.231 80.640  -20.142 1.00 10.69 ? 763  VAL A CB  1 
ATOM   6048 C  CG1 . VAL A 1 763  ? 31.220 79.582  -20.699 1.00 10.52 ? 763  VAL A CG1 1 
ATOM   6049 C  CG2 . VAL A 1 763  ? 29.602 80.090  -18.900 1.00 14.78 ? 763  VAL A CG2 1 
ATOM   6050 N  N   . VAL A 1 764  ? 32.886 82.390  -21.305 1.00 7.30  ? 764  VAL A N   1 
ATOM   6051 C  CA  . VAL A 1 764  ? 33.479 82.523  -22.635 1.00 7.11  ? 764  VAL A CA  1 
ATOM   6052 C  C   . VAL A 1 764  ? 33.662 81.071  -23.092 1.00 8.10  ? 764  VAL A C   1 
ATOM   6053 O  O   . VAL A 1 764  ? 34.464 80.298  -22.499 1.00 7.28  ? 764  VAL A O   1 
ATOM   6054 C  CB  . VAL A 1 764  ? 34.834 83.260  -22.665 1.00 7.90  ? 764  VAL A CB  1 
ATOM   6055 C  CG1 . VAL A 1 764  ? 35.372 83.329  -24.132 1.00 10.54 ? 764  VAL A CG1 1 
ATOM   6056 C  CG2 . VAL A 1 764  ? 34.617 84.695  -22.101 1.00 10.71 ? 764  VAL A CG2 1 
ATOM   6057 N  N   . HIS A 1 765  ? 32.944 80.682  -24.124 1.00 7.19  ? 765  HIS A N   1 
ATOM   6058 C  CA  . HIS A 1 765  ? 32.864 79.280  -24.557 1.00 6.91  ? 765  HIS A CA  1 
ATOM   6059 C  C   . HIS A 1 765  ? 33.669 79.175  -25.842 1.00 7.65  ? 765  HIS A C   1 
ATOM   6060 O  O   . HIS A 1 765  ? 33.498 79.980  -26.727 1.00 8.17  ? 765  HIS A O   1 
ATOM   6061 C  CB  . HIS A 1 765  ? 31.383 78.921  -24.784 1.00 8.35  ? 765  HIS A CB  1 
ATOM   6062 C  CG  . HIS A 1 765  ? 31.138 77.616  -25.479 1.00 7.22  ? 765  HIS A CG  1 
ATOM   6063 N  ND1 . HIS A 1 765  ? 31.321 76.385  -24.886 1.00 11.16 ? 765  HIS A ND1 1 
ATOM   6064 C  CD2 . HIS A 1 765  ? 30.656 77.365  -26.717 1.00 5.48  ? 765  HIS A CD2 1 
ATOM   6065 C  CE1 . HIS A 1 765  ? 30.986 75.434  -25.741 1.00 6.59  ? 765  HIS A CE1 1 
ATOM   6066 N  NE2 . HIS A 1 765  ? 30.579 76.002  -26.860 1.00 11.70 ? 765  HIS A NE2 1 
ATOM   6067 N  N   . GLN A 1 766  ? 34.580 78.214  -25.911 1.00 7.60  ? 766  GLN A N   1 
ATOM   6068 C  CA  . GLN A 1 766  ? 35.502 78.085  -27.024 1.00 7.72  ? 766  GLN A CA  1 
ATOM   6069 C  C   . GLN A 1 766  ? 35.564 76.659  -27.555 1.00 8.02  ? 766  GLN A C   1 
ATOM   6070 O  O   . GLN A 1 766  ? 35.739 75.701  -26.802 1.00 8.81  ? 766  GLN A O   1 
ATOM   6071 C  CB  . GLN A 1 766  ? 36.908 78.489  -26.548 1.00 9.35  ? 766  GLN A CB  1 
ATOM   6072 C  CG  A GLN A 1 766  ? 36.967 79.817  -25.768 0.50 19.37 ? 766  GLN A CG  1 
ATOM   6073 C  CG  B GLN A 1 766  ? 37.861 78.306  -27.813 0.50 18.20 ? 766  GLN A CG  1 
ATOM   6074 C  CD  A GLN A 1 766  ? 38.067 79.833  -24.671 0.50 29.04 ? 766  GLN A CD  1 
ATOM   6075 C  CD  B GLN A 1 766  ? 39.274 78.725  -27.410 0.50 22.91 ? 766  GLN A CD  1 
ATOM   6076 O  OE1 A GLN A 1 766  ? 39.215 79.505  -24.960 0.50 26.71 ? 766  GLN A OE1 1 
ATOM   6077 O  OE1 B GLN A 1 766  ? 39.672 78.546  -26.267 0.50 27.14 ? 766  GLN A OE1 1 
ATOM   6078 N  NE2 A GLN A 1 766  ? 37.709 80.219  -23.411 0.50 19.72 ? 766  GLN A NE2 1 
ATOM   6079 N  NE2 B GLN A 1 766  ? 40.033 79.276  -28.360 0.50 26.40 ? 766  GLN A NE2 1 
ATOM   6080 N  N   . THR A 1 767  ? 35.380 76.498  -28.862 1.00 6.65  ? 767  THR A N   1 
ATOM   6081 C  CA  . THR A 1 767  ? 35.496 75.198  -29.525 1.00 7.23  ? 767  THR A CA  1 
ATOM   6082 C  C   . THR A 1 767  ? 36.746 75.241  -30.375 1.00 7.58  ? 767  THR A C   1 
ATOM   6083 O  O   . THR A 1 767  ? 36.848 76.122  -31.277 1.00 9.17  ? 767  THR A O   1 
ATOM   6084 C  CB  . THR A 1 767  ? 34.286 74.898  -30.426 1.00 8.16  ? 767  THR A CB  1 
ATOM   6085 O  OG1 . THR A 1 767  ? 33.113 74.978  -29.638 1.00 10.96 ? 767  THR A OG1 1 
ATOM   6086 C  CG2 . THR A 1 767  ? 34.400 73.491  -31.037 1.00 9.20  ? 767  THR A CG2 1 
ATOM   6087 N  N   . ILE A 1 768  ? 37.713 74.375  -30.126 1.00 7.88  ? 768  ILE A N   1 
ATOM   6088 C  CA  . ILE A 1 768  ? 39.011 74.352  -30.796 1.00 7.93  ? 768  ILE A CA  1 
ATOM   6089 C  C   . ILE A 1 768  ? 39.169 73.112  -31.613 1.00 9.57  ? 768  ILE A C   1 
ATOM   6090 O  O   . ILE A 1 768  ? 38.871 72.003  -31.129 1.00 9.95  ? 768  ILE A O   1 
ATOM   6091 C  CB  . ILE A 1 768  ? 40.134 74.436  -29.759 1.00 9.04  ? 768  ILE A CB  1 
ATOM   6092 C  CG1 . ILE A 1 768  ? 39.956 75.695  -28.937 1.00 11.05 ? 768  ILE A CG1 1 
ATOM   6093 C  CG2 . ILE A 1 768  ? 41.468 74.549  -30.482 1.00 11.88 ? 768  ILE A CG2 1 
ATOM   6094 C  CD1 . ILE A 1 768  ? 40.807 75.687  -27.567 1.00 14.91 ? 768  ILE A CD1 1 
ATOM   6095 N  N   . MET A 1 769  ? 39.618 73.261  -32.853 1.00 8.88  ? 769  MET A N   1 
ATOM   6096 C  CA  . MET A 1 769  ? 39.789 72.150  -33.803 1.00 8.43  ? 769  MET A CA  1 
ATOM   6097 C  C   . MET A 1 769  ? 41.232 72.022  -34.225 1.00 9.67  ? 769  MET A C   1 
ATOM   6098 O  O   . MET A 1 769  ? 41.843 72.994  -34.680 1.00 9.42  ? 769  MET A O   1 
ATOM   6099 C  CB  . MET A 1 769  ? 38.974 72.426  -35.054 1.00 10.60 ? 769  MET A CB  1 
ATOM   6100 C  CG  A MET A 1 769  ? 37.489 72.307  -34.821 0.50 11.54 ? 769  MET A CG  1 
ATOM   6101 C  CG  B MET A 1 769  ? 37.472 72.690  -34.544 0.50 11.61 ? 769  MET A CG  1 
ATOM   6102 S  SD  A MET A 1 769  ? 36.499 73.382  -35.934 0.50 15.15 ? 769  MET A SD  1 
ATOM   6103 S  SD  B MET A 1 769  ? 36.398 73.005  -35.966 0.50 15.03 ? 769  MET A SD  1 
ATOM   6104 C  CE  A MET A 1 769  ? 36.528 74.978  -35.024 0.50 25.62 ? 769  MET A CE  1 
ATOM   6105 C  CE  B MET A 1 769  ? 36.830 71.676  -37.083 0.50 20.62 ? 769  MET A CE  1 
ATOM   6106 N  N   . ARG A 1 770  ? 41.776 70.813  -34.138 1.00 9.77  ? 770  ARG A N   1 
ATOM   6107 C  CA  . ARG A 1 770  ? 43.140 70.566  -34.536 1.00 10.23 ? 770  ARG A CA  1 
ATOM   6108 C  C   . ARG A 1 770  ? 43.233 69.373  -35.462 1.00 11.33 ? 770  ARG A C   1 
ATOM   6109 O  O   . ARG A 1 770  ? 44.330 68.888  -35.739 1.00 15.30 ? 770  ARG A O   1 
ATOM   6110 C  CB  . ARG A 1 770  ? 44.034 70.344  -33.320 1.00 11.61 ? 770  ARG A CB  1 
ATOM   6111 C  CG  . ARG A 1 770  ? 44.192 71.577  -32.476 1.00 13.66 ? 770  ARG A CG  1 
ATOM   6112 C  CD  . ARG A 1 770  ? 44.952 71.282  -31.190 1.00 16.77 ? 770  ARG A CD  1 
ATOM   6113 N  NE  A ARG A 1 770  ? 45.044 72.505  -30.418 0.50 22.09 ? 770  ARG A NE  1 
ATOM   6114 N  NE  B ARG A 1 770  ? 44.908 72.414  -30.223 0.50 24.05 ? 770  ARG A NE  1 
ATOM   6115 C  CZ  A ARG A 1 770  ? 45.563 72.594  -29.199 0.50 35.39 ? 770  ARG A CZ  1 
ATOM   6116 C  CZ  B ARG A 1 770  ? 44.098 72.336  -29.168 0.50 32.65 ? 770  ARG A CZ  1 
ATOM   6117 N  NH1 A ARG A 1 770  ? 46.053 71.515  -28.601 0.50 37.63 ? 770  ARG A NH1 1 
ATOM   6118 N  NH1 B ARG A 1 770  ? 43.390 71.240  -28.960 0.50 36.15 ? 770  ARG A NH1 1 
ATOM   6119 N  NH2 A ARG A 1 770  ? 45.574 73.766  -28.572 0.50 37.82 ? 770  ARG A NH2 1 
ATOM   6120 N  NH2 B ARG A 1 770  ? 43.994 73.352  -28.322 0.50 39.95 ? 770  ARG A NH2 1 
ATOM   6121 N  N   . GLY A 1 771  ? 42.103 68.901  -35.937 1.00 11.32 ? 771  GLY A N   1 
ATOM   6122 C  CA  . GLY A 1 771  ? 42.161 67.783  -36.841 1.00 14.68 ? 771  GLY A CA  1 
ATOM   6123 C  C   . GLY A 1 771  ? 41.491 66.548  -36.389 1.00 18.13 ? 771  GLY A C   1 
ATOM   6124 O  O   . GLY A 1 771  ? 41.286 65.663  -37.237 1.00 19.32 ? 771  GLY A O   1 
ATOM   6125 N  N   . GLY A 1 772  ? 41.163 66.475  -35.095 1.00 14.86 ? 772  GLY A N   1 
ATOM   6126 C  CA  . GLY A 1 772  ? 40.443 65.310  -34.547 1.00 16.89 ? 772  GLY A CA  1 
ATOM   6127 C  C   . GLY A 1 772  ? 39.234 65.813  -33.763 1.00 14.63 ? 772  GLY A C   1 
ATOM   6128 O  O   . GLY A 1 772  ? 38.630 66.834  -34.100 1.00 13.12 ? 772  GLY A O   1 
ATOM   6129 N  N   . ALA A 1 773  ? 38.849 65.097  -32.708 1.00 11.26 ? 773  ALA A N   1 
ATOM   6130 C  CA  . ALA A 1 773  ? 37.730 65.545  -31.887 1.00 10.40 ? 773  ALA A CA  1 
ATOM   6131 C  C   . ALA A 1 773  ? 38.034 66.929  -31.328 1.00 9.18  ? 773  ALA A C   1 
ATOM   6132 O  O   . ALA A 1 773  ? 39.162 67.198  -30.923 1.00 9.19  ? 773  ALA A O   1 
ATOM   6133 C  CB  . ALA A 1 773  ? 37.528 64.580  -30.750 1.00 12.40 ? 773  ALA A CB  1 
ATOM   6134 N  N   . PRO A 1 774  ? 37.058 67.806  -31.345 1.00 7.98  ? 774  PRO A N   1 
ATOM   6135 C  CA  . PRO A 1 774  ? 37.347 69.151  -30.813 1.00 8.57  ? 774  PRO A CA  1 
ATOM   6136 C  C   . PRO A 1 774  ? 37.648 69.192  -29.324 1.00 7.99  ? 774  PRO A C   1 
ATOM   6137 O  O   . PRO A 1 774  ? 37.293 68.274  -28.547 1.00 8.16  ? 774  PRO A O   1 
ATOM   6138 C  CB  . PRO A 1 774  ? 36.068 69.952  -31.101 1.00 10.90 ? 774  PRO A CB  1 
ATOM   6139 C  CG  . PRO A 1 774  ? 35.016 68.937  -31.131 1.00 13.58 ? 774  PRO A CG  1 
ATOM   6140 C  CD  . PRO A 1 774  ? 35.700 67.694  -31.852 1.00 9.04  ? 774  PRO A CD  1 
ATOM   6141 N  N   . GLU A 1 775  ? 38.291 70.264  -28.943 1.00 8.49  ? 775  GLU A N   1 
ATOM   6142 C  CA  . GLU A 1 775  ? 38.542 70.568  -27.533 1.00 6.95  ? 775  GLU A CA  1 
ATOM   6143 C  C   . GLU A 1 775  ? 37.585 71.691  -27.175 1.00 7.35  ? 775  GLU A C   1 
ATOM   6144 O  O   . GLU A 1 775  ? 37.359 72.637  -28.000 1.00 9.98  ? 775  GLU A O   1 
ATOM   6145 C  CB  . GLU A 1 775  ? 39.959 71.042  -27.317 1.00 8.64  ? 775  GLU A CB  1 
ATOM   6146 C  CG  . GLU A 1 775  ? 40.236 71.455  -25.826 1.00 8.85  ? 775  GLU A CG  1 
ATOM   6147 C  CD  . GLU A 1 775  ? 41.670 71.977  -25.546 1.00 16.22 ? 775  GLU A CD  1 
ATOM   6148 O  OE1 . GLU A 1 775  ? 42.512 71.989  -26.454 1.00 24.03 ? 775  GLU A OE1 1 
ATOM   6149 O  OE2 . GLU A 1 775  ? 41.956 72.388  -24.402 1.00 15.85 ? 775  GLU A OE2 1 
ATOM   6150 N  N   . ILE A 1 776  ? 36.914 71.628  -26.053 1.00 7.15  ? 776  ILE A N   1 
ATOM   6151 C  CA  . ILE A 1 776  ? 36.037 72.709  -25.603 1.00 7.40  ? 776  ILE A CA  1 
ATOM   6152 C  C   . ILE A 1 776  ? 36.675 73.347  -24.379 1.00 6.93  ? 776  ILE A C   1 
ATOM   6153 O  O   . ILE A 1 776  ? 37.152 72.612  -23.460 1.00 7.31  ? 776  ILE A O   1 
ATOM   6154 C  CB  . ILE A 1 776  ? 34.649 72.161  -25.186 1.00 8.91  ? 776  ILE A CB  1 
ATOM   6155 C  CG1 . ILE A 1 776  ? 34.088 71.210  -26.239 1.00 11.05 ? 776  ILE A CG1 1 
ATOM   6156 C  CG2 . ILE A 1 776  ? 33.725 73.328  -24.745 1.00 11.34 ? 776  ILE A CG2 1 
ATOM   6157 C  CD1 . ILE A 1 776  ? 34.026 71.758  -27.686 1.00 14.51 ? 776  ILE A CD1 1 
ATOM   6158 N  N   . ARG A 1 777  ? 36.720 74.670  -24.330 1.00 7.44  ? 777  ARG A N   1 
ATOM   6159 C  CA  . ARG A 1 777  ? 37.200 75.357  -23.123 1.00 7.89  ? 777  ARG A CA  1 
ATOM   6160 C  C   . ARG A 1 777  ? 36.143 76.353  -22.692 1.00 8.20  ? 777  ARG A C   1 
ATOM   6161 O  O   . ARG A 1 777  ? 35.612 77.119  -23.543 1.00 8.76  ? 777  ARG A O   1 
ATOM   6162 C  CB  . ARG A 1 777  ? 38.496 76.111  -23.374 1.00 9.53  ? 777  ARG A CB  1 
ATOM   6163 C  CG  . ARG A 1 777  ? 39.615 75.234  -23.758 1.00 8.28  ? 777  ARG A CG  1 
ATOM   6164 C  CD  . ARG A 1 777  ? 40.949 76.002  -23.868 1.00 9.84  ? 777  ARG A CD  1 
ATOM   6165 N  NE  . ARG A 1 777  ? 42.020 75.146  -24.366 1.00 12.15 ? 777  ARG A NE  1 
ATOM   6166 C  CZ  . ARG A 1 777  ? 43.200 75.566  -24.813 1.00 13.37 ? 777  ARG A CZ  1 
ATOM   6167 N  NH1 . ARG A 1 777  ? 43.459 76.880  -24.765 1.00 15.38 ? 777  ARG A NH1 1 
ATOM   6168 N  NH2 . ARG A 1 777  ? 44.059 74.720  -25.381 1.00 15.68 ? 777  ARG A NH2 1 
ATOM   6169 N  N   . ASN A 1 778  ? 35.775 76.365  -21.418 1.00 6.08  ? 778  ASN A N   1 
ATOM   6170 C  CA  . ASN A 1 778  ? 34.845 77.355  -20.930 1.00 6.66  ? 778  ASN A CA  1 
ATOM   6171 C  C   . ASN A 1 778  ? 35.528 78.173  -19.832 1.00 6.69  ? 778  ASN A C   1 
ATOM   6172 O  O   . ASN A 1 778  ? 35.962 77.587  -18.795 1.00 7.42  ? 778  ASN A O   1 
ATOM   6173 C  CB  . ASN A 1 778  ? 33.631 76.679  -20.245 1.00 8.16  ? 778  ASN A CB  1 
ATOM   6174 C  CG  . ASN A 1 778  ? 32.690 75.984  -21.186 1.00 8.32  ? 778  ASN A CG  1 
ATOM   6175 O  OD1 . ASN A 1 778  ? 32.635 76.353  -22.375 1.00 9.27  ? 778  ASN A OD1 1 
ATOM   6176 N  ND2 . ASN A 1 778  ? 31.913 75.037  -20.677 1.00 7.91  ? 778  ASN A ND2 1 
ATOM   6177 N  N   . LEU A 1 779  ? 35.591 79.494  -20.007 1.00 7.34  ? 779  LEU A N   1 
ATOM   6178 C  CA  . LEU A 1 779  ? 36.110 80.366  -18.910 1.00 7.61  ? 779  LEU A CA  1 
ATOM   6179 C  C   . LEU A 1 779  ? 34.859 80.797  -18.188 1.00 6.67  ? 779  LEU A C   1 
ATOM   6180 O  O   . LEU A 1 779  ? 34.054 81.593  -18.719 1.00 7.85  ? 779  LEU A O   1 
ATOM   6181 C  CB  . LEU A 1 779  ? 36.844 81.548  -19.537 1.00 8.90  ? 779  LEU A CB  1 
ATOM   6182 C  CG  . LEU A 1 779  ? 37.381 82.547  -18.493 1.00 11.76 ? 779  LEU A CG  1 
ATOM   6183 C  CD1 . LEU A 1 779  ? 38.344 81.929  -17.601 1.00 16.56 ? 779  LEU A CD1 1 
ATOM   6184 C  CD2 . LEU A 1 779  ? 37.973 83.768  -19.294 1.00 19.02 ? 779  LEU A CD2 1 
ATOM   6185 N  N   . VAL A 1 780  ? 34.643 80.192  -17.019 1.00 7.61  ? 780  VAL A N   1 
ATOM   6186 C  CA  . VAL A 1 780  ? 33.385 80.380  -16.285 1.00 8.46  ? 780  VAL A CA  1 
ATOM   6187 C  C   . VAL A 1 780  ? 33.523 81.378  -15.148 1.00 8.12  ? 780  VAL A C   1 
ATOM   6188 O  O   . VAL A 1 780  ? 34.339 81.173  -14.223 1.00 9.41  ? 780  VAL A O   1 
ATOM   6189 C  CB  . VAL A 1 780  ? 32.916 78.992  -15.728 1.00 7.83  ? 780  VAL A CB  1 
ATOM   6190 C  CG1 . VAL A 1 780  ? 31.589 79.135  -15.004 1.00 10.37 ? 780  VAL A CG1 1 
ATOM   6191 C  CG2 . VAL A 1 780  ? 32.829 77.964  -16.854 1.00 8.77  ? 780  VAL A CG2 1 
ATOM   6192 N  N   . ASP A 1 781  ? 32.758 82.473  -15.231 1.00 7.99  ? 781  ASP A N   1 
ATOM   6193 C  CA  . ASP A 1 781  ? 32.756 83.483  -14.155 1.00 9.80  ? 781  ASP A CA  1 
ATOM   6194 C  C   . ASP A 1 781  ? 31.331 83.787  -13.786 1.00 9.33  ? 781  ASP A C   1 
ATOM   6195 O  O   . ASP A 1 781  ? 30.664 84.635  -14.444 1.00 9.99  ? 781  ASP A O   1 
ATOM   6196 C  CB  . ASP A 1 781  ? 33.458 84.757  -14.635 1.00 11.42 ? 781  ASP A CB  1 
ATOM   6197 C  CG  . ASP A 1 781  ? 33.518 85.796  -13.549 1.00 14.20 ? 781  ASP A CG  1 
ATOM   6198 O  OD1 . ASP A 1 781  ? 33.087 85.571  -12.395 1.00 13.54 ? 781  ASP A OD1 1 
ATOM   6199 O  OD2 . ASP A 1 781  ? 34.036 86.909  -13.868 1.00 20.77 ? 781  ASP A OD2 1 
ATOM   6200 N  N   . ILE A 1 782  ? 30.790 83.075  -12.809 1.00 9.64  ? 782  ILE A N   1 
ATOM   6201 C  CA  . ILE A 1 782  ? 29.388 83.219  -12.399 1.00 11.03 ? 782  ILE A CA  1 
ATOM   6202 C  C   . ILE A 1 782  ? 29.140 84.562  -11.738 1.00 14.80 ? 782  ILE A C   1 
ATOM   6203 O  O   . ILE A 1 782  ? 27.988 84.941  -11.481 1.00 15.99 ? 782  ILE A O   1 
ATOM   6204 C  CB  . ILE A 1 782  ? 29.022 82.016  -11.508 1.00 11.47 ? 782  ILE A CB  1 
ATOM   6205 C  CG1 . ILE A 1 782  ? 27.537 81.860  -11.356 1.00 12.47 ? 782  ILE A CG1 1 
ATOM   6206 C  CG2 . ILE A 1 782  ? 29.723 82.171  -10.130 1.00 13.80 ? 782  ILE A CG2 1 
ATOM   6207 C  CD1 . ILE A 1 782  ? 27.229 80.390  -10.902 1.00 14.98 ? 782  ILE A CD1 1 
ATOM   6208 N  N   . GLY A 1 783  ? 30.207 85.294  -11.455 1.00 13.09 ? 783  GLY A N   1 
ATOM   6209 C  CA  . GLY A 1 783  ? 30.032 86.678  -11.006 1.00 15.88 ? 783  GLY A CA  1 
ATOM   6210 C  C   . GLY A 1 783  ? 29.200 86.795  -9.760  1.00 16.13 ? 783  GLY A C   1 
ATOM   6211 O  O   . GLY A 1 783  ? 29.422 86.034  -8.794  1.00 18.55 ? 783  GLY A O   1 
ATOM   6212 N  N   . SER A 1 784  ? 28.230 87.690  -9.788  1.00 18.87 ? 784  SER A N   1 
ATOM   6213 C  CA  . SER A 1 784  ? 27.397 87.868  -8.597  1.00 18.78 ? 784  SER A CA  1 
ATOM   6214 C  C   . SER A 1 784  ? 26.027 87.219  -8.742  1.00 20.64 ? 784  SER A C   1 
ATOM   6215 O  O   . SER A 1 784  ? 25.086 87.629  -8.034  1.00 21.13 ? 784  SER A O   1 
ATOM   6216 C  CB  . SER A 1 784  ? 27.241 89.363  -8.283  1.00 23.50 ? 784  SER A CB  1 
ATOM   6217 O  OG  . SER A 1 784  ? 26.667 90.034  -9.382  1.00 31.45 ? 784  SER A OG  1 
ATOM   6218 N  N   . LEU A 1 785  ? 25.881 86.225  -9.629  1.00 18.32 ? 785  LEU A N   1 
ATOM   6219 C  CA  . LEU A 1 785  ? 24.578 85.581  -9.808  1.00 16.55 ? 785  LEU A CA  1 
ATOM   6220 C  C   . LEU A 1 785  ? 24.222 84.621  -8.661  1.00 18.60 ? 785  LEU A C   1 
ATOM   6221 O  O   . LEU A 1 785  ? 24.396 83.367  -8.758  1.00 18.68 ? 785  LEU A O   1 
ATOM   6222 C  CB  . LEU A 1 785  ? 24.559 84.795  -11.129 1.00 16.14 ? 785  LEU A CB  1 
ATOM   6223 C  CG  . LEU A 1 785  ? 24.779 85.626  -12.421 1.00 18.08 ? 785  LEU A CG  1 
ATOM   6224 C  CD1 . LEU A 1 785  ? 24.729 84.755  -13.626 1.00 21.25 ? 785  LEU A CD1 1 
ATOM   6225 C  CD2 . LEU A 1 785  ? 23.726 86.751  -12.538 1.00 21.50 ? 785  LEU A CD2 1 
ATOM   6226 N  N   . ASP A 1 786  ? 23.636 85.150  -7.585  1.00 18.03 ? 786  ASP A N   1 
ATOM   6227 C  CA  . ASP A 1 786  ? 23.313 84.322  -6.436  1.00 15.92 ? 786  ASP A CA  1 
ATOM   6228 C  C   . ASP A 1 786  ? 22.194 83.295  -6.812  1.00 12.07 ? 786  ASP A C   1 
ATOM   6229 O  O   . ASP A 1 786  ? 21.370 83.486  -7.707  1.00 14.36 ? 786  ASP A O   1 
ATOM   6230 C  CB  . ASP A 1 786  ? 22.815 85.157  -5.235  1.00 19.37 ? 786  ASP A CB  1 
ATOM   6231 C  CG  . ASP A 1 786  ? 23.936 85.892  -4.501  1.00 23.83 ? 786  ASP A CG  1 
ATOM   6232 O  OD1 . ASP A 1 786  ? 25.104 86.038  -4.980  1.00 20.58 ? 786  ASP A OD1 1 
ATOM   6233 O  OD2 . ASP A 1 786  ? 23.618 86.349  -3.385  1.00 27.35 ? 786  ASP A OD2 1 
ATOM   6234 N  N   . ASN A 1 787  ? 22.280 82.204  -6.088  1.00 13.73 ? 787  ASN A N   1 
ATOM   6235 C  CA  . ASN A 1 787  ? 21.345 81.098  -6.211  1.00 11.79 ? 787  ASN A CA  1 
ATOM   6236 C  C   . ASN A 1 787  ? 21.142 80.645  -7.639  1.00 11.07 ? 787  ASN A C   1 
ATOM   6237 O  O   . ASN A 1 787  ? 20.025 80.470  -8.121  1.00 11.27 ? 787  ASN A O   1 
ATOM   6238 C  CB  . ASN A 1 787  ? 20.007 81.478  -5.545  1.00 11.53 ? 787  ASN A CB  1 
ATOM   6239 C  CG  . ASN A 1 787  ? 20.195 81.706  -4.099  1.00 17.13 ? 787  ASN A CG  1 
ATOM   6240 O  OD1 . ASN A 1 787  ? 20.973 80.972  -3.448  1.00 18.25 ? 787  ASN A OD1 1 
ATOM   6241 N  ND2 . ASN A 1 787  ? 19.536 82.744  -3.561  1.00 24.18 ? 787  ASN A ND2 1 
ATOM   6242 N  N   . THR A 1 788  ? 22.281 80.426  -8.296  1.00 9.55  ? 788  THR A N   1 
ATOM   6243 C  CA  . THR A 1 788  ? 22.280 79.987  -9.680  1.00 10.51 ? 788  THR A CA  1 
ATOM   6244 C  C   . THR A 1 788  ? 23.330 78.864  -9.902  1.00 8.84  ? 788  THR A C   1 
ATOM   6245 O  O   . THR A 1 788  ? 24.442 78.964  -9.342  1.00 9.09  ? 788  THR A O   1 
ATOM   6246 C  CB  . THR A 1 788  ? 22.711 81.184  -10.594 1.00 12.81 ? 788  THR A CB  1 
ATOM   6247 O  OG1 . THR A 1 788  ? 21.763 82.267  -10.452 1.00 13.82 ? 788  THR A OG1 1 
ATOM   6248 C  CG2 . THR A 1 788  ? 22.679 80.795  -12.089 1.00 14.19 ? 788  THR A CG2 1 
ATOM   6249 N  N   . GLU A 1 789  ? 22.968 77.857  -10.683 1.00 8.55  ? 789  GLU A N   1 
ATOM   6250 C  CA  . GLU A 1 789  ? 23.927 76.808  -11.067 1.00 7.38  ? 789  GLU A CA  1 
ATOM   6251 C  C   . GLU A 1 789  ? 23.927 76.838  -12.589 1.00 7.50  ? 789  GLU A C   1 
ATOM   6252 O  O   . GLU A 1 789  ? 22.835 76.754  -13.207 1.00 9.33  ? 789  GLU A O   1 
ATOM   6253 C  CB  . GLU A 1 789  ? 23.548 75.408  -10.519 1.00 8.28  ? 789  GLU A CB  1 
ATOM   6254 C  CG  . GLU A 1 789  ? 23.117 75.447  -9.053  1.00 9.39  ? 789  GLU A CG  1 
ATOM   6255 C  CD  . GLU A 1 789  ? 23.316 74.169  -8.280  1.00 8.67  ? 789  GLU A CD  1 
ATOM   6256 O  OE1 . GLU A 1 789  ? 24.159 73.344  -8.754  1.00 9.34  ? 789  GLU A OE1 1 
ATOM   6257 O  OE2 . GLU A 1 789  ? 22.684 74.042  -7.202  1.00 8.81  ? 789  GLU A OE2 1 
ATOM   6258 N  N   . ILE A 1 790  ? 25.085 77.014  -13.214 1.00 6.79  ? 790  ILE A N   1 
ATOM   6259 C  CA  . ILE A 1 790  ? 25.181 77.076  -14.664 1.00 8.10  ? 790  ILE A CA  1 
ATOM   6260 C  C   . ILE A 1 790  ? 25.535 75.695  -15.208 1.00 7.50  ? 790  ILE A C   1 
ATOM   6261 O  O   . ILE A 1 790  ? 26.530 75.094  -14.764 1.00 8.23  ? 790  ILE A O   1 
ATOM   6262 C  CB  . ILE A 1 790  ? 26.256 78.071  -15.096 1.00 9.67  ? 790  ILE A CB  1 
ATOM   6263 C  CG1 . ILE A 1 790  ? 25.860 79.516  -14.693 1.00 14.02 ? 790  ILE A CG1 1 
ATOM   6264 C  CG2 . ILE A 1 790  ? 26.491 77.981  -16.622 1.00 11.66 ? 790  ILE A CG2 1 
ATOM   6265 C  CD1 . ILE A 1 790  ? 27.064 80.469  -14.795 1.00 23.94 ? 790  ILE A CD1 1 
ATOM   6266 N  N   . VAL A 1 791  ? 24.741 75.185  -16.131 1.00 6.98  ? 791  VAL A N   1 
ATOM   6267 C  CA  . VAL A 1 791  ? 24.976 73.887  -16.732 1.00 7.31  ? 791  VAL A CA  1 
ATOM   6268 C  C   . VAL A 1 791  ? 25.234 73.971  -18.211 1.00 7.58  ? 791  VAL A C   1 
ATOM   6269 O  O   . VAL A 1 791  ? 24.647 74.859  -18.922 1.00 7.69  ? 791  VAL A O   1 
ATOM   6270 C  CB  . VAL A 1 791  ? 23.755 72.940  -16.440 1.00 7.52  ? 791  VAL A CB  1 
ATOM   6271 C  CG1 . VAL A 1 791  ? 22.498 73.412  -17.241 1.00 10.00 ? 791  VAL A CG1 1 
ATOM   6272 C  CG2 . VAL A 1 791  ? 24.102 71.468  -16.778 1.00 9.22  ? 791  VAL A CG2 1 
ATOM   6273 N  N   . MET A 1 792  ? 26.129 73.136  -18.708 1.00 6.68  ? 792  MET A N   1 
ATOM   6274 C  CA  . MET A 1 792  ? 26.387 73.019  -20.145 1.00 6.48  ? 792  MET A CA  1 
ATOM   6275 C  C   . MET A 1 792  ? 25.725 71.727  -20.601 1.00 6.88  ? 792  MET A C   1 
ATOM   6276 O  O   . MET A 1 792  ? 26.051 70.618  -20.092 1.00 8.16  ? 792  MET A O   1 
ATOM   6277 C  CB  . MET A 1 792  ? 27.893 72.997  -20.446 1.00 7.60  ? 792  MET A CB  1 
ATOM   6278 C  CG  . MET A 1 792  ? 28.188 72.837  -21.982 1.00 8.20  ? 792  MET A CG  1 
ATOM   6279 S  SD  . MET A 1 792  ? 29.964 72.873  -22.300 1.00 8.99  ? 792  MET A SD  1 
ATOM   6280 C  CE  . MET A 1 792  ? 30.497 71.373  -21.500 1.00 10.64 ? 792  MET A CE  1 
ATOM   6281 N  N   . ARG A 1 793  ? 24.791 71.812  -21.546 1.00 7.08  ? 793  ARG A N   1 
ATOM   6282 C  CA  . ARG A 1 793  ? 24.080 70.630  -22.050 1.00 8.02  ? 793  ARG A CA  1 
ATOM   6283 C  C   . ARG A 1 793  ? 24.406 70.413  -23.508 1.00 6.94  ? 793  ARG A C   1 
ATOM   6284 O  O   . ARG A 1 793  ? 24.624 71.363  -24.298 1.00 8.17  ? 793  ARG A O   1 
ATOM   6285 C  CB  . ARG A 1 793  ? 22.567 70.854  -21.888 1.00 7.91  ? 793  ARG A CB  1 
ATOM   6286 C  CG  . ARG A 1 793  ? 21.695 69.635  -22.322 1.00 7.65  ? 793  ARG A CG  1 
ATOM   6287 C  CD  . ARG A 1 793  ? 20.206 69.880  -22.059 1.00 8.63  ? 793  ARG A CD  1 
ATOM   6288 N  NE  . ARG A 1 793  ? 19.957 69.934  -20.614 1.00 8.88  ? 793  ARG A NE  1 
ATOM   6289 C  CZ  . ARG A 1 793  ? 18.899 70.524  -20.066 1.00 9.39  ? 793  ARG A CZ  1 
ATOM   6290 N  NH1 . ARG A 1 793  ? 17.975 71.104  -20.856 1.00 10.52 ? 793  ARG A NH1 1 
ATOM   6291 N  NH2 . ARG A 1 793  ? 18.760 70.585  -18.769 1.00 9.31  ? 793  ARG A NH2 1 
ATOM   6292 N  N   . LEU A 1 794  ? 24.475 69.154  -23.888 1.00 7.41  ? 794  LEU A N   1 
ATOM   6293 C  CA  . LEU A 1 794  ? 24.590 68.701  -25.287 1.00 8.05  ? 794  LEU A CA  1 
ATOM   6294 C  C   . LEU A 1 794  ? 23.274 68.028  -25.671 1.00 8.93  ? 794  LEU A C   1 
ATOM   6295 O  O   . LEU A 1 794  ? 22.785 67.112  -24.967 1.00 9.37  ? 794  LEU A O   1 
ATOM   6296 C  CB  . LEU A 1 794  ? 25.701 67.672  -25.448 1.00 10.05 ? 794  LEU A CB  1 
ATOM   6297 C  CG  . LEU A 1 794  ? 27.061 68.333  -25.526 1.00 10.10 ? 794  LEU A CG  1 
ATOM   6298 C  CD1 . LEU A 1 794  ? 28.178 67.380  -25.086 1.00 11.19 ? 794  LEU A CD1 1 
ATOM   6299 C  CD2 . LEU A 1 794  ? 27.247 68.792  -26.969 1.00 13.62 ? 794  LEU A CD2 1 
ATOM   6300 N  N   . GLU A 1 795  ? 22.679 68.489  -26.769 1.00 9.33  ? 795  GLU A N   1 
ATOM   6301 C  CA  . GLU A 1 795  ? 21.407 67.930  -27.265 1.00 9.06  ? 795  GLU A CA  1 
ATOM   6302 C  C   . GLU A 1 795  ? 21.691 67.221  -28.567 1.00 9.38  ? 795  GLU A C   1 
ATOM   6303 O  O   . GLU A 1 795  ? 22.261 67.798  -29.499 1.00 11.53 ? 795  GLU A O   1 
ATOM   6304 C  CB  . GLU A 1 795  ? 20.389 69.051  -27.517 1.00 10.76 ? 795  GLU A CB  1 
ATOM   6305 C  CG  . GLU A 1 795  ? 19.962 69.778  -26.261 1.00 13.78 ? 795  GLU A CG  1 
ATOM   6306 C  CD  . GLU A 1 795  ? 19.087 71.031  -26.516 1.00 18.24 ? 795  GLU A CD  1 
ATOM   6307 O  OE1 . GLU A 1 795  ? 19.159 71.640  -27.622 1.00 22.49 ? 795  GLU A OE1 1 
ATOM   6308 O  OE2 . GLU A 1 795  ? 18.368 71.458  -25.593 1.00 19.64 ? 795  GLU A OE2 1 
ATOM   6309 N  N   . THR A 1 796  ? 21.349 65.918  -28.621 1.00 8.95  ? 796  THR A N   1 
ATOM   6310 C  CA  . THR A 1 796  ? 21.537 65.135  -29.829 1.00 9.00  ? 796  THR A CA  1 
ATOM   6311 C  C   . THR A 1 796  ? 20.210 64.385  -30.035 1.00 8.60  ? 796  THR A C   1 
ATOM   6312 O  O   . THR A 1 796  ? 19.272 64.454  -29.233 1.00 11.24 ? 796  THR A O   1 
ATOM   6313 C  CB  . THR A 1 796  ? 22.690 64.070  -29.723 1.00 9.50  ? 796  THR A CB  1 
ATOM   6314 O  OG1 . THR A 1 796  ? 22.244 62.917  -28.977 1.00 8.90  ? 796  THR A OG1 1 
ATOM   6315 C  CG2 . THR A 1 796  ? 23.906 64.671  -29.016 1.00 11.82 ? 796  THR A CG2 1 
ATOM   6316 N  N   . HIS A 1 797  ? 20.223 63.651  -31.138 1.00 10.21 ? 797  HIS A N   1 
ATOM   6317 C  CA  . HIS A 1 797  ? 19.041 62.791  -31.452 1.00 9.20  ? 797  HIS A CA  1 
ATOM   6318 C  C   . HIS A 1 797  ? 19.406 61.335  -31.247 1.00 10.89 ? 797  HIS A C   1 
ATOM   6319 O  O   . HIS A 1 797  ? 18.635 60.445  -31.660 1.00 12.74 ? 797  HIS A O   1 
ATOM   6320 C  CB  . HIS A 1 797  ? 18.530 63.102  -32.880 1.00 10.02 ? 797  HIS A CB  1 
ATOM   6321 C  CG  . HIS A 1 797  ? 18.072 64.519  -33.015 1.00 9.41  ? 797  HIS A CG  1 
ATOM   6322 N  ND1 . HIS A 1 797  ? 17.808 65.135  -34.225 1.00 12.20 ? 797  HIS A ND1 1 
ATOM   6323 C  CD2 . HIS A 1 797  ? 17.809 65.440  -32.060 1.00 12.11 ? 797  HIS A CD2 1 
ATOM   6324 C  CE1 . HIS A 1 797  ? 17.403 66.368  -33.996 1.00 14.26 ? 797  HIS A CE1 1 
ATOM   6325 N  NE2 . HIS A 1 797  ? 17.396 66.586  -32.694 1.00 16.58 ? 797  HIS A NE2 1 
ATOM   6326 N  N   . ILE A 1 798  ? 20.537 61.021  -30.571 1.00 10.25 ? 798  ILE A N   1 
ATOM   6327 C  CA  . ILE A 1 798  ? 20.930 59.636  -30.275 1.00 8.61  ? 798  ILE A CA  1 
ATOM   6328 C  C   . ILE A 1 798  ? 19.827 59.034  -29.398 1.00 8.83  ? 798  ILE A C   1 
ATOM   6329 O  O   . ILE A 1 798  ? 19.315 59.633  -28.457 1.00 9.43  ? 798  ILE A O   1 
ATOM   6330 C  CB  . ILE A 1 798  ? 22.264 59.661  -29.497 1.00 8.91  ? 798  ILE A CB  1 
ATOM   6331 C  CG1 . ILE A 1 798  ? 23.352 60.183  -30.413 1.00 10.85 ? 798  ILE A CG1 1 
ATOM   6332 C  CG2 . ILE A 1 798  ? 22.592 58.231  -28.936 1.00 10.59 ? 798  ILE A CG2 1 
ATOM   6333 C  CD1 . ILE A 1 798  ? 24.804 60.373  -29.726 1.00 13.94 ? 798  ILE A CD1 1 
ATOM   6334 N  N   . ASP A 1 799  ? 19.392 57.802  -29.783 1.00 10.22 ? 799  ASP A N   1 
ATOM   6335 C  CA  . ASP A 1 799  ? 18.310 57.136  -29.059 1.00 9.64  ? 799  ASP A CA  1 
ATOM   6336 C  C   . ASP A 1 799  ? 18.824 56.340  -27.861 1.00 10.69 ? 799  ASP A C   1 
ATOM   6337 O  O   . ASP A 1 799  ? 18.857 55.129  -27.858 1.00 11.13 ? 799  ASP A O   1 
ATOM   6338 C  CB  . ASP A 1 799  ? 17.495 56.240  -30.033 1.00 12.22 ? 799  ASP A CB  1 
ATOM   6339 C  CG  . ASP A 1 799  ? 16.254 55.638  -29.357 1.00 13.43 ? 799  ASP A CG  1 
ATOM   6340 O  OD1 . ASP A 1 799  ? 15.877 55.967  -28.209 1.00 18.56 ? 799  ASP A OD1 1 
ATOM   6341 O  OD2 . ASP A 1 799  ? 15.717 54.711  -29.981 1.00 20.94 ? 799  ASP A OD2 1 
ATOM   6342 N  N   . SER A 1 800  ? 19.294 57.087  -26.860 1.00 10.08 ? 800  SER A N   1 
ATOM   6343 C  CA  . SER A 1 800  ? 19.873 56.483  -25.657 1.00 9.61  ? 800  SER A CA  1 
ATOM   6344 C  C   . SER A 1 800  ? 18.825 56.088  -24.666 1.00 10.43 ? 800  SER A C   1 
ATOM   6345 O  O   . SER A 1 800  ? 19.139 55.311  -23.731 1.00 9.62  ? 800  SER A O   1 
ATOM   6346 C  CB  . SER A 1 800  ? 20.886 57.501  -25.024 1.00 9.80  ? 800  SER A CB  1 
ATOM   6347 O  OG  . SER A 1 800  ? 20.271 58.726  -24.713 1.00 9.39  ? 800  SER A OG  1 
ATOM   6348 N  N   . GLY A 1 801  ? 17.605 56.598  -24.768 1.00 9.15  ? 801  GLY A N   1 
ATOM   6349 C  CA  . GLY A 1 801  ? 16.572 56.227  -23.821 1.00 9.96  ? 801  GLY A CA  1 
ATOM   6350 C  C   . GLY A 1 801  ? 16.869 56.742  -22.439 1.00 9.84  ? 801  GLY A C   1 
ATOM   6351 O  O   . GLY A 1 801  ? 16.974 57.956  -22.262 1.00 11.22 ? 801  GLY A O   1 
ATOM   6352 N  N   . ASP A 1 802  ? 16.947 55.861  -21.456 1.00 9.38  ? 802  ASP A N   1 
ATOM   6353 C  CA  . ASP A 1 802  ? 17.243 56.217  -20.074 1.00 9.08  ? 802  ASP A CA  1 
ATOM   6354 C  C   . ASP A 1 802  ? 18.636 55.765  -19.665 1.00 8.23  ? 802  ASP A C   1 
ATOM   6355 O  O   . ASP A 1 802  ? 18.940 55.807  -18.467 1.00 9.94  ? 802  ASP A O   1 
ATOM   6356 C  CB  . ASP A 1 802  ? 16.167 55.587  -19.126 1.00 11.12 ? 802  ASP A CB  1 
ATOM   6357 C  CG  . ASP A 1 802  ? 16.050 54.074  -19.260 1.00 11.75 ? 802  ASP A CG  1 
ATOM   6358 O  OD1 . ASP A 1 802  ? 16.801 53.417  -19.982 1.00 14.31 ? 802  ASP A OD1 1 
ATOM   6359 O  OD2 . ASP A 1 802  ? 15.142 53.571  -18.542 1.00 16.10 ? 802  ASP A OD2 1 
ATOM   6360 N  N   . ILE A 1 803  ? 19.504 55.410  -20.588 1.00 6.73  ? 803  ILE A N   1 
ATOM   6361 C  CA  . ILE A 1 803  ? 20.827 54.884  -20.244 1.00 7.62  ? 803  ILE A CA  1 
ATOM   6362 C  C   . ILE A 1 803  ? 21.920 55.910  -20.547 1.00 7.47  ? 803  ILE A C   1 
ATOM   6363 O  O   . ILE A 1 803  ? 21.884 56.595  -21.576 1.00 7.26  ? 803  ILE A O   1 
ATOM   6364 C  CB  . ILE A 1 803  ? 21.122 53.594  -21.082 1.00 7.53  ? 803  ILE A CB  1 
ATOM   6365 C  CG1 . ILE A 1 803  ? 20.092 52.467  -20.709 1.00 10.42 ? 803  ILE A CG1 1 
ATOM   6366 C  CG2 . ILE A 1 803  ? 22.567 53.082  -20.813 1.00 9.53  ? 803  ILE A CG2 1 
ATOM   6367 C  CD1 . ILE A 1 803  ? 20.064 52.122  -19.213 1.00 12.96 ? 803  ILE A CD1 1 
ATOM   6368 N  N   . PHE A 1 804  ? 22.917 56.008  -19.655 1.00 7.46  ? 804  PHE A N   1 
ATOM   6369 C  CA  . PHE A 1 804  ? 24.094 56.809  -19.923 1.00 6.54  ? 804  PHE A CA  1 
ATOM   6370 C  C   . PHE A 1 804  ? 25.240 56.187  -19.093 1.00 6.73  ? 804  PHE A C   1 
ATOM   6371 O  O   . PHE A 1 804  ? 24.978 55.298  -18.283 1.00 7.84  ? 804  PHE A O   1 
ATOM   6372 C  CB  . PHE A 1 804  ? 23.863 58.323  -19.595 1.00 6.53  ? 804  PHE A CB  1 
ATOM   6373 C  CG  . PHE A 1 804  ? 23.435 58.631  -18.190 1.00 6.33  ? 804  PHE A CG  1 
ATOM   6374 C  CD1 . PHE A 1 804  ? 22.164 58.432  -17.710 1.00 7.13  ? 804  PHE A CD1 1 
ATOM   6375 C  CD2 . PHE A 1 804  ? 24.384 59.250  -17.323 1.00 6.21  ? 804  PHE A CD2 1 
ATOM   6376 C  CE1 . PHE A 1 804  ? 21.803 58.815  -16.424 1.00 7.24  ? 804  PHE A CE1 1 
ATOM   6377 C  CE2 . PHE A 1 804  ? 24.043 59.650  -16.051 1.00 6.57  ? 804  PHE A CE2 1 
ATOM   6378 C  CZ  . PHE A 1 804  ? 22.759 59.449  -15.574 1.00 7.05  ? 804  PHE A CZ  1 
ATOM   6379 N  N   . TYR A 1 805  ? 26.442 56.634  -19.332 1.00 6.42  ? 805  TYR A N   1 
ATOM   6380 C  CA  . TYR A 1 805  ? 27.612 56.068  -18.649 1.00 5.91  ? 805  TYR A CA  1 
ATOM   6381 C  C   . TYR A 1 805  ? 28.445 57.195  -18.084 1.00 6.79  ? 805  TYR A C   1 
ATOM   6382 O  O   . TYR A 1 805  ? 28.587 58.235  -18.727 1.00 6.78  ? 805  TYR A O   1 
ATOM   6383 C  CB  . TYR A 1 805  ? 28.473 55.276  -19.646 1.00 7.25  ? 805  TYR A CB  1 
ATOM   6384 C  CG  . TYR A 1 805  ? 27.766 54.063  -20.219 1.00 6.02  ? 805  TYR A CG  1 
ATOM   6385 C  CD1 . TYR A 1 805  ? 26.817 54.189  -21.221 1.00 8.67  ? 805  TYR A CD1 1 
ATOM   6386 C  CD2 . TYR A 1 805  ? 28.045 52.800  -19.716 1.00 7.50  ? 805  TYR A CD2 1 
ATOM   6387 C  CE1 . TYR A 1 805  ? 26.173 53.033  -21.705 1.00 8.40  ? 805  TYR A CE1 1 
ATOM   6388 C  CE2 . TYR A 1 805  ? 27.404 51.639  -20.214 1.00 9.35  ? 805  TYR A CE2 1 
ATOM   6389 C  CZ  . TYR A 1 805  ? 26.487 51.821  -21.192 1.00 8.32  ? 805  TYR A CZ  1 
ATOM   6390 O  OH  . TYR A 1 805  ? 25.851 50.697  -21.742 1.00 10.75 ? 805  TYR A OH  1 
ATOM   6391 N  N   . THR A 1 806  ? 28.933 56.980  -16.862 1.00 6.63  ? 806  THR A N   1 
ATOM   6392 C  CA  . THR A 1 806  ? 29.822 57.969  -16.201 1.00 5.94  ? 806  THR A CA  1 
ATOM   6393 C  C   . THR A 1 806  ? 30.994 57.230  -15.632 1.00 6.68  ? 806  THR A C   1 
ATOM   6394 O  O   . THR A 1 806  ? 30.923 56.016  -15.410 1.00 7.72  ? 806  THR A O   1 
ATOM   6395 C  CB  . THR A 1 806  ? 29.100 58.784  -15.119 1.00 7.12  ? 806  THR A CB  1 
ATOM   6396 O  OG1 . THR A 1 806  ? 28.721 57.889  -14.075 1.00 7.35  ? 806  THR A OG1 1 
ATOM   6397 C  CG2 . THR A 1 806  ? 27.837 59.470  -15.656 1.00 7.22  ? 806  THR A CG2 1 
ATOM   6398 N  N   . ASP A 1 807  ? 32.122 57.894  -15.443 1.00 6.13  ? 807  ASP A N   1 
ATOM   6399 C  CA  . ASP A 1 807  ? 33.244 57.168  -14.859 1.00 6.77  ? 807  ASP A CA  1 
ATOM   6400 C  C   . ASP A 1 807  ? 33.306 57.248  -13.333 1.00 6.41  ? 807  ASP A C   1 
ATOM   6401 O  O   . ASP A 1 807  ? 32.652 58.078  -12.682 1.00 6.88  ? 807  ASP A O   1 
ATOM   6402 C  CB  . ASP A 1 807  ? 34.546 57.633  -15.451 1.00 9.22  ? 807  ASP A CB  1 
ATOM   6403 C  CG  . ASP A 1 807  ? 34.982 58.914  -14.943 1.00 8.64  ? 807  ASP A CG  1 
ATOM   6404 O  OD1 . ASP A 1 807  ? 34.239 59.916  -15.032 1.00 9.86  ? 807  ASP A OD1 1 
ATOM   6405 O  OD2 . ASP A 1 807  ? 36.151 58.974  -14.449 1.00 11.05 ? 807  ASP A OD2 1 
ATOM   6406 N  N   . LEU A 1 808  ? 34.052 56.301  -12.779 1.00 5.94  ? 808  LEU A N   1 
ATOM   6407 C  CA  . LEU A 1 808  ? 34.348 56.306  -11.319 1.00 5.55  ? 808  LEU A CA  1 
ATOM   6408 C  C   . LEU A 1 808  ? 35.844 56.504  -11.139 1.00 5.44  ? 808  LEU A C   1 
ATOM   6409 O  O   . LEU A 1 808  ? 36.637 55.684  -11.616 1.00 6.02  ? 808  LEU A O   1 
ATOM   6410 C  CB  . LEU A 1 808  ? 33.893 54.973  -10.692 1.00 6.40  ? 808  LEU A CB  1 
ATOM   6411 C  CG  . LEU A 1 808  ? 32.359 54.822  -10.604 1.00 6.96  ? 808  LEU A CG  1 
ATOM   6412 C  CD1 . LEU A 1 808  ? 32.046 53.357  -10.367 1.00 8.64  ? 808  LEU A CD1 1 
ATOM   6413 C  CD2 . LEU A 1 808  ? 31.799 55.646  -9.442  1.00 9.12  ? 808  LEU A CD2 1 
ATOM   6414 N  N   . ASN A 1 809  ? 36.201 57.671  -10.627 1.00 4.87  ? 809  ASN A N   1 
ATOM   6415 C  CA  . ASN A 1 809  ? 37.577 57.981  -10.256 1.00 5.56  ? 809  ASN A CA  1 
ATOM   6416 C  C   . ASN A 1 809  ? 38.546 57.890  -11.419 1.00 4.80  ? 809  ASN A C   1 
ATOM   6417 O  O   . ASN A 1 809  ? 39.714 57.644  -11.196 1.00 5.86  ? 809  ASN A O   1 
ATOM   6418 C  CB  . ASN A 1 809  ? 38.031 57.075  -9.092  1.00 4.70  ? 809  ASN A CB  1 
ATOM   6419 C  CG  . ASN A 1 809  ? 36.989 56.983  -8.014  1.00 5.58  ? 809  ASN A CG  1 
ATOM   6420 O  OD1 . ASN A 1 809  ? 36.153 56.105  -8.043  1.00 8.62  ? 809  ASN A OD1 1 
ATOM   6421 N  ND2 . ASN A 1 809  ? 37.009 57.918  -7.091  1.00 4.05  ? 809  ASN A ND2 1 
ATOM   6422 N  N   . GLY A 1 810  ? 38.072 58.076  -12.650 1.00 5.33  ? 810  GLY A N   1 
ATOM   6423 C  CA  . GLY A 1 810  ? 39.001 58.004  -13.794 1.00 6.73  ? 810  GLY A CA  1 
ATOM   6424 C  C   . GLY A 1 810  ? 39.471 56.574  -14.056 1.00 7.12  ? 810  GLY A C   1 
ATOM   6425 O  O   . GLY A 1 810  ? 40.446 56.399  -14.835 1.00 9.66  ? 810  GLY A O   1 
ATOM   6426 N  N   . LEU A 1 811  ? 38.861 55.581  -13.421 1.00 6.38  ? 811  LEU A N   1 
ATOM   6427 C  CA  . LEU A 1 811  ? 39.308 54.196  -13.535 1.00 6.48  ? 811  LEU A CA  1 
ATOM   6428 C  C   . LEU A 1 811  ? 38.407 53.294  -14.390 1.00 7.54  ? 811  LEU A C   1 
ATOM   6429 O  O   . LEU A 1 811  ? 38.938 52.388  -15.043 1.00 10.37 ? 811  LEU A O   1 
ATOM   6430 C  CB  . LEU A 1 811  ? 39.363 53.601  -12.113 1.00 8.04  ? 811  LEU A CB  1 
ATOM   6431 C  CG  . LEU A 1 811  ? 39.840 52.155  -11.933 1.00 9.49  ? 811  LEU A CG  1 
ATOM   6432 C  CD1 . LEU A 1 811  ? 41.285 52.020  -12.422 1.00 10.66 ? 811  LEU A CD1 1 
ATOM   6433 C  CD2 . LEU A 1 811  ? 39.713 51.697  -10.447 1.00 11.01 ? 811  LEU A CD2 1 
ATOM   6434 N  N   . GLN A 1 812  ? 37.113 53.516  -14.371 1.00 6.17  ? 812  GLN A N   1 
ATOM   6435 C  CA  . GLN A 1 812  ? 36.149 52.624  -15.032 1.00 7.18  ? 812  GLN A CA  1 
ATOM   6436 C  C   . GLN A 1 812  ? 34.903 53.357  -15.345 1.00 6.84  ? 812  GLN A C   1 
ATOM   6437 O  O   . GLN A 1 812  ? 34.642 54.421  -14.722 1.00 8.41  ? 812  GLN A O   1 
ATOM   6438 C  CB  . GLN A 1 812  ? 35.801 51.460  -14.062 1.00 7.91  ? 812  GLN A CB  1 
ATOM   6439 C  CG  . GLN A 1 812  ? 35.206 51.997  -12.710 1.00 10.23 ? 812  GLN A CG  1 
ATOM   6440 C  CD  . GLN A 1 812  ? 34.911 50.856  -11.731 1.00 11.95 ? 812  GLN A CD  1 
ATOM   6441 O  OE1 . GLN A 1 812  ? 33.983 50.114  -11.915 1.00 11.85 ? 812  GLN A OE1 1 
ATOM   6442 N  NE2 . GLN A 1 812  ? 35.751 50.738  -10.677 1.00 14.43 ? 812  GLN A NE2 1 
ATOM   6443 N  N   . PHE A 1 813  ? 34.161 52.900  -16.364 1.00 6.62  ? 813  PHE A N   1 
ATOM   6444 C  CA  . PHE A 1 813  ? 32.875 53.488  -16.705 1.00 6.03  ? 813  PHE A CA  1 
ATOM   6445 C  C   . PHE A 1 813  ? 31.759 52.594  -16.267 1.00 7.02  ? 813  PHE A C   1 
ATOM   6446 O  O   . PHE A 1 813  ? 31.775 51.363  -16.551 1.00 8.57  ? 813  PHE A O   1 
ATOM   6447 C  CB  . PHE A 1 813  ? 32.820 53.788  -18.208 1.00 7.03  ? 813  PHE A CB  1 
ATOM   6448 C  CG  . PHE A 1 813  ? 33.590 55.035  -18.590 1.00 6.97  ? 813  PHE A CG  1 
ATOM   6449 C  CD1 . PHE A 1 813  ? 34.971 54.988  -18.675 1.00 7.40  ? 813  PHE A CD1 1 
ATOM   6450 C  CD2 . PHE A 1 813  ? 32.915 56.255  -18.814 1.00 7.63  ? 813  PHE A CD2 1 
ATOM   6451 C  CE1 . PHE A 1 813  ? 35.707 56.178  -18.952 1.00 9.37  ? 813  PHE A CE1 1 
ATOM   6452 C  CE2 . PHE A 1 813  ? 33.642 57.416  -19.086 1.00 10.20 ? 813  PHE A CE2 1 
ATOM   6453 C  CZ  . PHE A 1 813  ? 35.010 57.338  -19.135 1.00 9.07  ? 813  PHE A CZ  1 
ATOM   6454 N  N   . ILE A 1 814  ? 30.796 53.165  -15.590 1.00 6.69  ? 814  ILE A N   1 
ATOM   6455 C  CA  . ILE A 1 814  ? 29.685 52.405  -15.066 1.00 6.01  ? 814  ILE A CA  1 
ATOM   6456 C  C   . ILE A 1 814  ? 28.384 52.835  -15.737 1.00 6.26  ? 814  ILE A C   1 
ATOM   6457 O  O   . ILE A 1 814  ? 28.134 54.041  -15.976 1.00 6.25  ? 814  ILE A O   1 
ATOM   6458 C  CB  . ILE A 1 814  ? 29.639 52.568  -13.512 1.00 6.22  ? 814  ILE A CB  1 
ATOM   6459 C  CG1 . ILE A 1 814  ? 28.561 51.647  -12.940 1.00 6.88  ? 814  ILE A CG1 1 
ATOM   6460 C  CG2 . ILE A 1 814  ? 29.365 54.044  -13.053 1.00 6.79  ? 814  ILE A CG2 1 
ATOM   6461 C  CD1 . ILE A 1 814  ? 28.714 51.462  -11.378 1.00 8.93  ? 814  ILE A CD1 1 
ATOM   6462 N  N   . LYS A 1 815  ? 27.531 51.842  -16.028 1.00 6.38  ? 815  LYS A N   1 
ATOM   6463 C  CA  . LYS A 1 815  ? 26.223 52.129  -16.618 1.00 6.62  ? 815  LYS A CA  1 
ATOM   6464 C  C   . LYS A 1 815  ? 25.288 52.753  -15.583 1.00 6.06  ? 815  LYS A C   1 
ATOM   6465 O  O   . LYS A 1 815  ? 25.133 52.275  -14.453 1.00 7.28  ? 815  LYS A O   1 
ATOM   6466 C  CB  . LYS A 1 815  ? 25.630 50.818  -17.116 1.00 7.86  ? 815  LYS A CB  1 
ATOM   6467 C  CG  . LYS A 1 815  ? 24.318 50.991  -17.902 1.00 9.27  ? 815  LYS A CG  1 
ATOM   6468 C  CD  . LYS A 1 815  ? 23.883 49.572  -18.437 1.00 13.06 ? 815  LYS A CD  1 
ATOM   6469 C  CE  . LYS A 1 815  ? 22.683 49.614  -19.324 1.00 19.59 ? 815  LYS A CE  1 
ATOM   6470 N  NZ  . LYS A 1 815  ? 22.483 48.162  -19.811 1.00 24.06 ? 815  LYS A NZ  1 
ATOM   6471 N  N   . ARG A 1 816  ? 24.642 53.844  -15.980 1.00 6.72  ? 816  ARG A N   1 
ATOM   6472 C  CA  . ARG A 1 816  ? 23.653 54.531  -15.213 1.00 6.21  ? 816  ARG A CA  1 
ATOM   6473 C  C   . ARG A 1 816  ? 22.287 54.424  -15.910 1.00 7.14  ? 816  ARG A C   1 
ATOM   6474 O  O   . ARG A 1 816  ? 22.211 54.375  -17.157 1.00 7.94  ? 816  ARG A O   1 
ATOM   6475 C  CB  . ARG A 1 816  ? 23.936 56.067  -15.083 1.00 7.57  ? 816  ARG A CB  1 
ATOM   6476 C  CG  . ARG A 1 816  ? 25.352 56.432  -14.564 1.00 7.76  ? 816  ARG A CG  1 
ATOM   6477 C  CD  . ARG A 1 816  ? 25.537 55.789  -13.217 1.00 7.42  ? 816  ARG A CD  1 
ATOM   6478 N  NE  . ARG A 1 816  ? 26.748 56.370  -12.582 1.00 6.78  ? 816  ARG A NE  1 
ATOM   6479 C  CZ  . ARG A 1 816  ? 27.136 55.979  -11.369 1.00 6.75  ? 816  ARG A CZ  1 
ATOM   6480 N  NH1 . ARG A 1 816  ? 26.445 55.042  -10.723 1.00 7.44  ? 816  ARG A NH1 1 
ATOM   6481 N  NH2 . ARG A 1 816  ? 28.185 56.554  -10.750 1.00 7.61  ? 816  ARG A NH2 1 
ATOM   6482 N  N   . ARG A 1 817  ? 21.241 54.373  -15.091 1.00 7.39  ? 817  ARG A N   1 
ATOM   6483 C  CA  . ARG A 1 817  ? 19.901 54.413  -15.674 1.00 7.05  ? 817  ARG A CA  1 
ATOM   6484 C  C   . ARG A 1 817  ? 19.162 55.558  -14.999 1.00 7.92  ? 817  ARG A C   1 
ATOM   6485 O  O   . ARG A 1 817  ? 19.035 55.612  -13.762 1.00 8.69  ? 817  ARG A O   1 
ATOM   6486 C  CB  . ARG A 1 817  ? 19.174 53.047  -15.432 1.00 8.75  ? 817  ARG A CB  1 
ATOM   6487 C  CG  . ARG A 1 817  ? 17.718 53.109  -15.922 1.00 10.44 ? 817  ARG A CG  1 
ATOM   6488 C  CD  . ARG A 1 817  ? 16.974 51.737  -15.723 1.00 11.04 ? 817  ARG A CD  1 
ATOM   6489 N  NE  . ARG A 1 817  ? 17.555 50.707  -16.561 1.00 11.84 ? 817  ARG A NE  1 
ATOM   6490 C  CZ  . ARG A 1 817  ? 18.286 49.672  -16.147 1.00 14.41 ? 817  ARG A CZ  1 
ATOM   6491 N  NH1 . ARG A 1 817  ? 18.554 49.534  -14.867 1.00 13.64 ? 817  ARG A NH1 1 
ATOM   6492 N  NH2 . ARG A 1 817  ? 18.734 48.757  -16.997 1.00 16.96 ? 817  ARG A NH2 1 
ATOM   6493 N  N   . ARG A 1 818  ? 18.687 56.501  -15.815 1.00 7.36  ? 818  ARG A N   1 
ATOM   6494 C  CA  . ARG A 1 818  ? 17.902 57.611  -15.313 1.00 8.99  ? 818  ARG A CA  1 
ATOM   6495 C  C   . ARG A 1 818  ? 16.589 57.016  -14.761 1.00 10.68 ? 818  ARG A C   1 
ATOM   6496 O  O   . ARG A 1 818  ? 15.951 56.222  -15.453 1.00 11.29 ? 818  ARG A O   1 
ATOM   6497 C  CB  . ARG A 1 818  ? 17.595 58.565  -16.481 1.00 8.48  ? 818  ARG A CB  1 
ATOM   6498 C  CG  A ARG A 1 818  ? 16.971 59.873  -16.018 0.50 9.75  ? 818  ARG A CG  1 
ATOM   6499 C  CG  B ARG A 1 818  ? 16.669 59.750  -15.998 0.50 10.35 ? 818  ARG A CG  1 
ATOM   6500 C  CD  . ARG A 1 818  ? 16.227 60.607  -17.178 1.00 10.32 ? 818  ARG A CD  1 
ATOM   6501 N  NE  A ARG A 1 818  ? 14.967 59.914  -17.517 0.50 14.40 ? 818  ARG A NE  1 
ATOM   6502 N  NE  B ARG A 1 818  ? 17.150 60.571  -18.253 0.50 27.14 ? 818  ARG A NE  1 
ATOM   6503 C  CZ  A ARG A 1 818  ? 14.679 59.335  -18.685 0.50 13.86 ? 818  ARG A CZ  1 
ATOM   6504 C  CZ  B ARG A 1 818  ? 16.985 59.977  -19.434 0.50 28.20 ? 818  ARG A CZ  1 
ATOM   6505 N  NH1 A ARG A 1 818  ? 15.536 59.318  -19.708 0.50 12.91 ? 818  ARG A NH1 1 
ATOM   6506 N  NH1 B ARG A 1 818  ? 15.829 59.390  -19.768 0.50 26.34 ? 818  ARG A NH1 1 
ATOM   6507 N  NH2 A ARG A 1 818  ? 13.476 58.760  -18.838 0.50 15.43 ? 818  ARG A NH2 1 
ATOM   6508 N  NH2 B ARG A 1 818  ? 18.038 59.857  -20.229 0.50 26.62 ? 818  ARG A NH2 1 
ATOM   6509 N  N   . LEU A 1 819  ? 16.211 57.388  -13.542 1.00 8.98  ? 819  LEU A N   1 
ATOM   6510 C  CA  . LEU A 1 819  ? 14.986 56.873  -12.889 1.00 10.60 ? 819  LEU A CA  1 
ATOM   6511 C  C   . LEU A 1 819  ? 14.009 57.994  -12.633 1.00 9.35  ? 819  LEU A C   1 
ATOM   6512 O  O   . LEU A 1 819  ? 14.259 58.869  -11.816 1.00 10.58 ? 819  LEU A O   1 
ATOM   6513 C  CB  . LEU A 1 819  ? 15.355 56.193  -11.564 1.00 11.80 ? 819  LEU A CB  1 
ATOM   6514 C  CG  . LEU A 1 819  ? 16.265 54.927  -11.732 1.00 11.98 ? 819  LEU A CG  1 
ATOM   6515 C  CD1 . LEU A 1 819  ? 16.759 54.469  -10.316 1.00 14.11 ? 819  LEU A CD1 1 
ATOM   6516 C  CD2 . LEU A 1 819  ? 15.648 53.795  -12.495 1.00 14.13 ? 819  LEU A CD2 1 
ATOM   6517 N  N   . ASP A 1 820  ? 12.887 57.948  -13.361 1.00 11.26 ? 820  ASP A N   1 
ATOM   6518 C  CA  . ASP A 1 820  ? 11.920 59.003  -13.148 1.00 12.88 ? 820  ASP A CA  1 
ATOM   6519 C  C   . ASP A 1 820  ? 11.186 58.869  -11.818 1.00 11.00 ? 820  ASP A C   1 
ATOM   6520 O  O   . ASP A 1 820  ? 10.551 59.824  -11.405 1.00 13.96 ? 820  ASP A O   1 
ATOM   6521 C  CB  . ASP A 1 820  ? 10.990 59.115  -14.367 1.00 15.50 ? 820  ASP A CB  1 
ATOM   6522 C  CG  . ASP A 1 820  ? 11.776 59.404  -15.668 1.00 18.32 ? 820  ASP A CG  1 
ATOM   6523 O  OD1 . ASP A 1 820  ? 12.853 60.059  -15.648 1.00 17.45 ? 820  ASP A OD1 1 
ATOM   6524 O  OD2 . ASP A 1 820  ? 11.334 58.978  -16.747 1.00 22.16 ? 820  ASP A OD2 1 
ATOM   6525 N  N   . LYS A 1 821  ? 11.343 57.734  -11.112 1.00 12.04 ? 821  LYS A N   1 
ATOM   6526 C  CA  . LYS A 1 821  ? 10.761 57.618  -9.777  1.00 12.05 ? 821  LYS A CA  1 
ATOM   6527 C  C   . LYS A 1 821  ? 11.600 58.399  -8.736  1.00 12.88 ? 821  LYS A C   1 
ATOM   6528 O  O   . LYS A 1 821  ? 11.126 58.625  -7.601  1.00 14.84 ? 821  LYS A O   1 
ATOM   6529 C  CB  . LYS A 1 821  ? 10.659 56.138  -9.397  1.00 11.20 ? 821  LYS A CB  1 
ATOM   6530 C  CG  . LYS A 1 821  ? 11.990 55.423  -9.165  1.00 11.19 ? 821  LYS A CG  1 
ATOM   6531 C  CD  . LYS A 1 821  ? 11.803 53.931  -9.055  1.00 11.20 ? 821  LYS A CD  1 
ATOM   6532 C  CE  . LYS A 1 821  ? 13.146 53.228  -8.963  1.00 13.77 ? 821  LYS A CE  1 
ATOM   6533 N  NZ  . LYS A 1 821  ? 13.071 51.759  -9.138  1.00 13.34 ? 821  LYS A NZ  1 
ATOM   6534 N  N   . LEU A 1 822  ? 12.791 58.878  -9.153  1.00 11.62 ? 822  LEU A N   1 
ATOM   6535 C  CA  . LEU A 1 822  ? 13.659 59.672  -8.242  1.00 12.20 ? 822  LEU A CA  1 
ATOM   6536 C  C   . LEU A 1 822  ? 13.677 61.119  -8.767  1.00 11.79 ? 822  LEU A C   1 
ATOM   6537 O  O   . LEU A 1 822  ? 13.487 61.345  -9.968  1.00 11.98 ? 822  LEU A O   1 
ATOM   6538 C  CB  . LEU A 1 822  ? 15.083 59.141  -8.255  1.00 12.13 ? 822  LEU A CB  1 
ATOM   6539 C  CG  . LEU A 1 822  ? 15.230 57.674  -7.752  1.00 12.11 ? 822  LEU A CG  1 
ATOM   6540 C  CD1 . LEU A 1 822  ? 16.690 57.302  -7.671  1.00 15.09 ? 822  LEU A CD1 1 
ATOM   6541 C  CD2 . LEU A 1 822  ? 14.515 57.453  -6.395  1.00 13.33 ? 822  LEU A CD2 1 
ATOM   6542 N  N   . PRO A 1 823  ? 13.905 62.093  -7.893  1.00 11.02 ? 823  PRO A N   1 
ATOM   6543 C  CA  . PRO A 1 823  ? 13.943 63.503  -8.335  1.00 10.48 ? 823  PRO A CA  1 
ATOM   6544 C  C   . PRO A 1 823  ? 15.186 63.779  -9.211  1.00 9.91  ? 823  PRO A C   1 
ATOM   6545 O  O   . PRO A 1 823  ? 16.180 63.007  -9.223  1.00 10.46 ? 823  PRO A O   1 
ATOM   6546 C  CB  . PRO A 1 823  ? 13.918 64.286  -7.041  1.00 13.43 ? 823  PRO A CB  1 
ATOM   6547 C  CG  . PRO A 1 823  ? 14.585 63.364  -6.030  1.00 13.34 ? 823  PRO A CG  1 
ATOM   6548 C  CD  . PRO A 1 823  ? 14.052 61.952  -6.434  1.00 11.51 ? 823  PRO A CD  1 
ATOM   6549 N  N   . LEU A 1 824  ? 15.141 64.915  -9.916  1.00 9.71  ? 824  LEU A N   1 
ATOM   6550 C  CA  . LEU A 1 824  ? 16.195 65.299  -10.829 1.00 9.97  ? 824  LEU A CA  1 
ATOM   6551 C  C   . LEU A 1 824  ? 17.611 65.177  -10.200 1.00 8.96  ? 824  LEU A C   1 
ATOM   6552 O  O   . LEU A 1 824  ? 18.496 64.585  -10.805 1.00 8.31  ? 824  LEU A O   1 
ATOM   6553 C  CB  . LEU A 1 824  ? 15.886 66.740  -11.262 1.00 11.88 ? 824  LEU A CB  1 
ATOM   6554 C  CG  . LEU A 1 824  ? 16.683 67.340  -12.384 1.00 10.40 ? 824  LEU A CG  1 
ATOM   6555 C  CD1 . LEU A 1 824  ? 15.915 68.586  -12.889 1.00 11.48 ? 824  LEU A CD1 1 
ATOM   6556 C  CD2 . LEU A 1 824  ? 18.134 67.766  -11.922 1.00 8.79  ? 824  LEU A CD2 1 
ATOM   6557 N  N   . GLN A 1 825  ? 17.747 65.720  -8.989  1.00 8.27  ? 825  GLN A N   1 
ATOM   6558 C  CA  . GLN A 1 825  ? 19.068 65.736  -8.320  1.00 7.49  ? 825  GLN A CA  1 
ATOM   6559 C  C   . GLN A 1 825  ? 19.610 64.342  -8.009  1.00 7.48  ? 825  GLN A C   1 
ATOM   6560 O  O   . GLN A 1 825  ? 20.864 64.197  -7.832  1.00 7.95  ? 825  GLN A O   1 
ATOM   6561 C  CB  . GLN A 1 825  ? 19.050 66.606  -7.076  1.00 8.57  ? 825  GLN A CB  1 
ATOM   6562 C  CG  . GLN A 1 825  ? 18.126 66.107  -5.966  1.00 8.15  ? 825  GLN A CG  1 
ATOM   6563 C  CD  . GLN A 1 825  ? 16.664 66.581  -6.067  1.00 9.82  ? 825  GLN A CD  1 
ATOM   6564 O  OE1 . GLN A 1 825  ? 16.228 67.052  -7.132  1.00 10.29 ? 825  GLN A OE1 1 
ATOM   6565 N  NE2 . GLN A 1 825  ? 15.933 66.485  -4.967  1.00 8.57  ? 825  GLN A NE2 1 
ATOM   6566 N  N   . ALA A 1 826  ? 18.732 63.316  -7.896  1.00 7.73  ? 826  ALA A N   1 
ATOM   6567 C  CA  . ALA A 1 826  ? 19.200 61.950  -7.649  1.00 7.51  ? 826  ALA A CA  1 
ATOM   6568 C  C   . ALA A 1 826  ? 19.769 61.359  -8.920  1.00 7.13  ? 826  ALA A C   1 
ATOM   6569 O  O   . ALA A 1 826  ? 20.514 60.361  -8.870  1.00 8.95  ? 826  ALA A O   1 
ATOM   6570 C  CB  . ALA A 1 826  ? 17.970 61.114  -7.180  1.00 9.39  ? 826  ALA A CB  1 
ATOM   6571 N  N   . ASN A 1 827  ? 19.433 61.907  -10.107 1.00 7.76  ? 827  ASN A N   1 
ATOM   6572 C  CA  . ASN A 1 827  ? 19.926 61.393  -11.383 1.00 7.85  ? 827  ASN A CA  1 
ATOM   6573 C  C   . ASN A 1 827  ? 21.243 62.044  -11.816 1.00 7.15  ? 827  ASN A C   1 
ATOM   6574 O  O   . ASN A 1 827  ? 21.743 61.739  -12.863 1.00 8.29  ? 827  ASN A O   1 
ATOM   6575 C  CB  . ASN A 1 827  ? 18.807 61.560  -12.456 1.00 8.53  ? 827  ASN A CB  1 
ATOM   6576 C  CG  . ASN A 1 827  ? 17.684 60.552  -12.214 1.00 9.69  ? 827  ASN A CG  1 
ATOM   6577 O  OD1 . ASN A 1 827  ? 17.926 59.361  -12.278 1.00 9.90  ? 827  ASN A OD1 1 
ATOM   6578 N  ND2 . ASN A 1 827  ? 16.475 60.999  -11.881 1.00 12.64 ? 827  ASN A ND2 1 
ATOM   6579 N  N   . TYR A 1 828  ? 21.741 62.958  -10.987 1.00 7.88  ? 828  TYR A N   1 
ATOM   6580 C  CA  . TYR A 1 828  ? 23.095 63.507  -11.127 1.00 6.95  ? 828  TYR A CA  1 
ATOM   6581 C  C   . TYR A 1 828  ? 24.135 62.576  -10.492 1.00 6.84  ? 828  TYR A C   1 
ATOM   6582 O  O   . TYR A 1 828  ? 23.937 62.072  -9.402  1.00 8.43  ? 828  TYR A O   1 
ATOM   6583 C  CB  . TYR A 1 828  ? 23.157 64.909  -10.480 1.00 7.21  ? 828  TYR A CB  1 
ATOM   6584 C  CG  . TYR A 1 828  ? 23.181 66.052  -11.488 1.00 6.53  ? 828  TYR A CG  1 
ATOM   6585 C  CD1 . TYR A 1 828  ? 22.132 66.274  -12.369 1.00 7.91  ? 828  TYR A CD1 1 
ATOM   6586 C  CD2 . TYR A 1 828  ? 24.259 66.906  -11.549 1.00 8.03  ? 828  TYR A CD2 1 
ATOM   6587 C  CE1 . TYR A 1 828  ? 22.178 67.301  -13.285 1.00 9.04  ? 828  TYR A CE1 1 
ATOM   6588 C  CE2 . TYR A 1 828  ? 24.304 67.939  -12.454 1.00 9.03  ? 828  TYR A CE2 1 
ATOM   6589 C  CZ  . TYR A 1 828  ? 23.269 68.129  -13.314 1.00 7.25  ? 828  TYR A CZ  1 
ATOM   6590 O  OH  . TYR A 1 828  ? 23.357 69.142  -14.211 1.00 9.31  ? 828  TYR A OH  1 
ATOM   6591 N  N   . TYR A 1 829  ? 25.247 62.399  -11.198 1.00 6.71  ? 829  TYR A N   1 
ATOM   6592 C  CA  . TYR A 1 829  ? 26.332 61.547  -10.748 1.00 6.54  ? 829  TYR A CA  1 
ATOM   6593 C  C   . TYR A 1 829  ? 27.642 62.271  -10.914 1.00 7.50  ? 829  TYR A C   1 
ATOM   6594 O  O   . TYR A 1 829  ? 27.730 63.279  -11.607 1.00 7.03  ? 829  TYR A O   1 
ATOM   6595 C  CB  . TYR A 1 829  ? 26.363 60.285  -11.628 1.00 6.61  ? 829  TYR A CB  1 
ATOM   6596 C  CG  . TYR A 1 829  ? 25.186 59.361  -11.346 1.00 7.24  ? 829  TYR A CG  1 
ATOM   6597 C  CD1 . TYR A 1 829  ? 25.214 58.469  -10.289 1.00 6.46  ? 829  TYR A CD1 1 
ATOM   6598 C  CD2 . TYR A 1 829  ? 24.029 59.418  -12.152 1.00 7.76  ? 829  TYR A CD2 1 
ATOM   6599 C  CE1 . TYR A 1 829  ? 24.141 57.651  -10.011 1.00 7.62  ? 829  TYR A CE1 1 
ATOM   6600 C  CE2 . TYR A 1 829  ? 22.945 58.594  -11.870 1.00 8.26  ? 829  TYR A CE2 1 
ATOM   6601 C  CZ  . TYR A 1 829  ? 23.003 57.716  -10.796 1.00 7.11  ? 829  TYR A CZ  1 
ATOM   6602 O  OH  . TYR A 1 829  ? 21.915 56.897  -10.480 1.00 9.21  ? 829  TYR A OH  1 
ATOM   6603 N  N   . PRO A 1 830  ? 28.713 61.795  -10.231 1.00 6.81  ? 830  PRO A N   1 
ATOM   6604 C  CA  . PRO A 1 830  ? 29.999 62.457  -10.419 1.00 7.12  ? 830  PRO A CA  1 
ATOM   6605 C  C   . PRO A 1 830  ? 30.460 62.169  -11.847 1.00 7.44  ? 830  PRO A C   1 
ATOM   6606 O  O   . PRO A 1 830  ? 30.255 61.066  -12.428 1.00 7.62  ? 830  PRO A O   1 
ATOM   6607 C  CB  . PRO A 1 830  ? 30.940 61.769  -9.398  1.00 10.83 ? 830  PRO A CB  1 
ATOM   6608 C  CG  . PRO A 1 830  ? 30.048 60.821  -8.573  1.00 10.68 ? 830  PRO A CG  1 
ATOM   6609 C  CD  . PRO A 1 830  ? 28.726 60.655  -9.289  1.00 6.98  ? 830  PRO A CD  1 
ATOM   6610 N  N   . ILE A 1 831  ? 31.114 63.156  -12.454 1.00 6.09  ? 831  ILE A N   1 
ATOM   6611 C  CA  . ILE A 1 831  ? 31.754 63.018  -13.784 1.00 6.53  ? 831  ILE A CA  1 
ATOM   6612 C  C   . ILE A 1 831  ? 33.224 63.321  -13.504 1.00 6.87  ? 831  ILE A C   1 
ATOM   6613 O  O   . ILE A 1 831  ? 33.723 64.410  -13.832 1.00 7.08  ? 831  ILE A O   1 
ATOM   6614 C  CB  . ILE A 1 831  ? 31.180 63.986  -14.842 1.00 6.39  ? 831  ILE A CB  1 
ATOM   6615 C  CG1 . ILE A 1 831  ? 29.657 64.041  -14.821 1.00 6.51  ? 831  ILE A CG1 1 
ATOM   6616 C  CG2 . ILE A 1 831  ? 31.739 63.545  -16.225 1.00 6.94  ? 831  ILE A CG2 1 
ATOM   6617 C  CD1 . ILE A 1 831  ? 28.909 62.683  -15.116 1.00 6.72  ? 831  ILE A CD1 1 
ATOM   6618 N  N   . PRO A 1 832  ? 33.955 62.370  -12.899 1.00 6.12  ? 832  PRO A N   1 
ATOM   6619 C  CA  . PRO A 1 832  ? 35.353 62.663  -12.591 1.00 6.83  ? 832  PRO A CA  1 
ATOM   6620 C  C   . PRO A 1 832  ? 36.221 62.796  -13.777 1.00 8.13  ? 832  PRO A C   1 
ATOM   6621 O  O   . PRO A 1 832  ? 37.192 63.553  -13.646 1.00 10.67 ? 832  PRO A O   1 
ATOM   6622 C  CB  . PRO A 1 832  ? 35.782 61.547  -11.588 1.00 6.34  ? 832  PRO A CB  1 
ATOM   6623 C  CG  . PRO A 1 832  ? 34.711 60.507  -11.762 1.00 8.94  ? 832  PRO A CG  1 
ATOM   6624 C  CD  . PRO A 1 832  ? 33.442 61.138  -12.252 1.00 6.85  ? 832  PRO A CD  1 
ATOM   6625 N  N   . SER A 1 833  ? 35.928 62.137  -14.895 1.00 6.81  ? 833  SER A N   1 
ATOM   6626 C  CA  . SER A 1 833  ? 36.746 62.250  -16.103 1.00 6.87  ? 833  SER A CA  1 
ATOM   6627 C  C   . SER A 1 833  ? 35.965 62.079  -17.420 1.00 6.29  ? 833  SER A C   1 
ATOM   6628 O  O   . SER A 1 833  ? 36.506 62.428  -18.471 1.00 5.98  ? 833  SER A O   1 
ATOM   6629 C  CB  . SER A 1 833  ? 37.946 61.330  -16.101 1.00 10.55 ? 833  SER A CB  1 
ATOM   6630 O  OG  . SER A 1 833  ? 37.603 60.046  -16.364 1.00 12.23 ? 833  SER A OG  1 
ATOM   6631 N  N   . GLY A 1 834  ? 34.741 61.550  -17.389 1.00 6.56  ? 834  GLY A N   1 
ATOM   6632 C  CA  . GLY A 1 834  ? 34.025 61.465  -18.666 1.00 5.88  ? 834  GLY A CA  1 
ATOM   6633 C  C   . GLY A 1 834  ? 32.678 60.837  -18.532 1.00 5.85  ? 834  GLY A C   1 
ATOM   6634 O  O   . GLY A 1 834  ? 32.284 60.281  -17.501 1.00 6.77  ? 834  GLY A O   1 
ATOM   6635 N  N   . MET A 1 835  ? 31.901 61.007  -19.606 1.00 6.08  ? 835  MET A N   1 
ATOM   6636 C  CA  . MET A 1 835  ? 30.537 60.461  -19.669 1.00 6.46  ? 835  MET A CA  1 
ATOM   6637 C  C   . MET A 1 835  ? 30.183 60.241  -21.127 1.00 5.34  ? 835  MET A C   1 
ATOM   6638 O  O   . MET A 1 835  ? 30.764 60.879  -22.022 1.00 6.42  ? 835  MET A O   1 
ATOM   6639 C  CB  . MET A 1 835  ? 29.535 61.431  -19.016 1.00 6.84  ? 835  MET A CB  1 
ATOM   6640 C  CG  . MET A 1 835  ? 29.444 62.791  -19.788 1.00 7.49  ? 835  MET A CG  1 
ATOM   6641 S  SD  . MET A 1 835  ? 28.572 64.089  -18.890 1.00 10.78 ? 835  MET A SD  1 
ATOM   6642 C  CE  . MET A 1 835  ? 27.046 63.381  -18.397 1.00 12.95 ? 835  MET A CE  1 
ATOM   6643 N  N   . PHE A 1 836  ? 29.228 59.327  -21.373 1.00 6.23  ? 836  PHE A N   1 
ATOM   6644 C  CA  . PHE A 1 836  ? 28.784 59.124  -22.758 1.00 6.02  ? 836  PHE A CA  1 
ATOM   6645 C  C   . PHE A 1 836  ? 27.397 58.585  -22.802 1.00 7.16  ? 836  PHE A C   1 
ATOM   6646 O  O   . PHE A 1 836  ? 26.856 58.017  -21.844 1.00 7.01  ? 836  PHE A O   1 
ATOM   6647 C  CB  . PHE A 1 836  ? 29.767 58.235  -23.580 1.00 7.14  ? 836  PHE A CB  1 
ATOM   6648 C  CG  . PHE A 1 836  ? 29.961 56.797  -23.130 1.00 7.69  ? 836  PHE A CG  1 
ATOM   6649 C  CD1 . PHE A 1 836  ? 29.105 55.765  -23.601 1.00 7.78  ? 836  PHE A CD1 1 
ATOM   6650 C  CD2 . PHE A 1 836  ? 31.069 56.444  -22.317 1.00 8.78  ? 836  PHE A CD2 1 
ATOM   6651 C  CE1 . PHE A 1 836  ? 29.367 54.420  -23.252 1.00 9.86  ? 836  PHE A CE1 1 
ATOM   6652 C  CE2 . PHE A 1 836  ? 31.316 55.110  -21.996 1.00 8.43  ? 836  PHE A CE2 1 
ATOM   6653 C  CZ  . PHE A 1 836  ? 30.474 54.113  -22.464 1.00 10.42 ? 836  PHE A CZ  1 
ATOM   6654 N  N   . ILE A 1 837  ? 26.788 58.801  -23.980 1.00 6.69  ? 837  ILE A N   1 
ATOM   6655 C  CA  . ILE A 1 837  ? 25.480 58.197  -24.365 1.00 7.45  ? 837  ILE A CA  1 
ATOM   6656 C  C   . ILE A 1 837  ? 25.680 57.541  -25.704 1.00 7.42  ? 837  ILE A C   1 
ATOM   6657 O  O   . ILE A 1 837  ? 26.539 57.938  -26.519 1.00 7.30  ? 837  ILE A O   1 
ATOM   6658 C  CB  . ILE A 1 837  ? 24.331 59.232  -24.425 1.00 8.16  ? 837  ILE A CB  1 
ATOM   6659 C  CG1 . ILE A 1 837  ? 24.741 60.448  -25.235 1.00 7.71  ? 837  ILE A CG1 1 
ATOM   6660 C  CG2 . ILE A 1 837  ? 23.840 59.557  -23.042 1.00 8.64  ? 837  ILE A CG2 1 
ATOM   6661 C  CD1 . ILE A 1 837  ? 23.508 61.323  -25.710 1.00 10.16 ? 837  ILE A CD1 1 
ATOM   6662 N  N   . GLU A 1 838  ? 24.884 56.476  -25.934 1.00 7.06  ? 838  GLU A N   1 
ATOM   6663 C  CA  . GLU A 1 838  ? 24.980 55.795  -27.217 1.00 7.19  ? 838  GLU A CA  1 
ATOM   6664 C  C   . GLU A 1 838  ? 23.668 55.042  -27.540 1.00 7.28  ? 838  GLU A C   1 
ATOM   6665 O  O   . GLU A 1 838  ? 22.815 54.811  -26.694 1.00 8.50  ? 838  GLU A O   1 
ATOM   6666 C  CB  . GLU A 1 838  ? 26.122 54.755  -27.250 1.00 8.34  ? 838  GLU A CB  1 
ATOM   6667 C  CG  . GLU A 1 838  ? 25.906 53.610  -26.262 1.00 10.31 ? 838  GLU A CG  1 
ATOM   6668 C  CD  . GLU A 1 838  ? 27.054 52.600  -26.217 1.00 10.43 ? 838  GLU A CD  1 
ATOM   6669 O  OE1 . GLU A 1 838  ? 28.048 52.706  -26.931 1.00 12.79 ? 838  GLU A OE1 1 
ATOM   6670 O  OE2 . GLU A 1 838  ? 26.866 51.607  -25.448 1.00 13.60 ? 838  GLU A OE2 1 
ATOM   6671 N  N   . ASP A 1 839  ? 23.532 54.793  -28.846 1.00 8.61  ? 839  ASP A N   1 
ATOM   6672 C  CA  . ASP A 1 839  ? 22.460 53.876  -29.304 1.00 8.27  ? 839  ASP A CA  1 
ATOM   6673 C  C   . ASP A 1 839  ? 23.187 52.774  -30.098 1.00 9.30  ? 839  ASP A C   1 
ATOM   6674 O  O   . ASP A 1 839  ? 24.372 52.570  -29.983 1.00 11.23 ? 839  ASP A O   1 
ATOM   6675 C  CB  . ASP A 1 839  ? 21.343 54.604  -30.099 1.00 9.26  ? 839  ASP A CB  1 
ATOM   6676 C  CG  . ASP A 1 839  ? 21.810 55.334  -31.345 1.00 10.87 ? 839  ASP A CG  1 
ATOM   6677 O  OD1 . ASP A 1 839  ? 22.826 54.992  -31.932 1.00 11.00 ? 839  ASP A OD1 1 
ATOM   6678 O  OD2 . ASP A 1 839  ? 21.061 56.316  -31.733 1.00 14.73 ? 839  ASP A OD2 1 
ATOM   6679 N  N   . ALA A 1 840  ? 22.429 52.055  -30.945 1.00 11.61 ? 840  ALA A N   1 
ATOM   6680 C  CA  . ALA A 1 840  ? 23.066 50.981  -31.687 1.00 12.61 ? 840  ALA A CA  1 
ATOM   6681 C  C   . ALA A 1 840  ? 24.152 51.445  -32.621 1.00 11.61 ? 840  ALA A C   1 
ATOM   6682 O  O   . ALA A 1 840  ? 25.129 50.720  -32.851 1.00 14.13 ? 840  ALA A O   1 
ATOM   6683 C  CB  . ALA A 1 840  ? 22.023 50.198  -32.478 1.00 13.91 ? 840  ALA A CB  1 
ATOM   6684 N  N   . ASN A 1 841  ? 24.028 52.689  -33.114 1.00 10.87 ? 841  ASN A N   1 
ATOM   6685 C  CA  . ASN A 1 841  ? 24.982 53.160  -34.120 1.00 9.94  ? 841  ASN A CA  1 
ATOM   6686 C  C   . ASN A 1 841  ? 25.966 54.260  -33.801 1.00 8.96  ? 841  ASN A C   1 
ATOM   6687 O  O   . ASN A 1 841  ? 26.990 54.340  -34.431 1.00 10.52 ? 841  ASN A O   1 
ATOM   6688 C  CB  . ASN A 1 841  ? 24.178 53.579  -35.408 1.00 12.22 ? 841  ASN A CB  1 
ATOM   6689 C  CG  . ASN A 1 841  ? 23.430 52.368  -36.003 1.00 13.44 ? 841  ASN A CG  1 
ATOM   6690 O  OD1 . ASN A 1 841  ? 24.010 51.308  -36.124 1.00 17.33 ? 841  ASN A OD1 1 
ATOM   6691 N  ND2 . ASN A 1 841  ? 22.158 52.530  -36.260 1.00 20.60 ? 841  ASN A ND2 1 
ATOM   6692 N  N   . THR A 1 842  ? 25.559 55.108  -32.873 1.00 9.14  ? 842  THR A N   1 
ATOM   6693 C  CA  . THR A 1 842  ? 26.270 56.341  -32.567 1.00 8.82  ? 842  THR A CA  1 
ATOM   6694 C  C   . THR A 1 842  ? 26.506 56.518  -31.074 1.00 8.10  ? 842  THR A C   1 
ATOM   6695 O  O   . THR A 1 842  ? 25.623 56.263  -30.257 1.00 9.21  ? 842  THR A O   1 
ATOM   6696 C  CB  . THR A 1 842  ? 25.398 57.551  -33.055 1.00 9.59  ? 842  THR A CB  1 
ATOM   6697 O  OG1 . THR A 1 842  ? 25.014 57.326  -34.458 1.00 12.28 ? 842  THR A OG1 1 
ATOM   6698 C  CG2 . THR A 1 842  ? 26.156 58.856  -33.057 1.00 11.12 ? 842  THR A CG2 1 
ATOM   6699 N  N   . ARG A 1 843  ? 27.680 57.074  -30.793 1.00 7.48  ? 843  ARG A N   1 
ATOM   6700 C  CA  . ARG A 1 843  ? 28.053 57.421  -29.398 1.00 7.74  ? 843  ARG A CA  1 
ATOM   6701 C  C   . ARG A 1 843  ? 28.589 58.866  -29.332 1.00 7.08  ? 843  ARG A C   1 
ATOM   6702 O  O   . ARG A 1 843  ? 29.276 59.309  -30.272 1.00 7.81  ? 843  ARG A O   1 
ATOM   6703 C  CB  . ARG A 1 843  ? 29.114 56.458  -28.879 1.00 7.85  ? 843  ARG A CB  1 
ATOM   6704 C  CG  . ARG A 1 843  ? 29.547 56.749  -27.422 1.00 7.92  ? 843  ARG A CG  1 
ATOM   6705 C  CD  . ARG A 1 843  ? 30.707 55.901  -26.942 1.00 6.98  ? 843  ARG A CD  1 
ATOM   6706 N  NE  . ARG A 1 843  ? 30.301 54.513  -26.706 1.00 7.97  ? 843  ARG A NE  1 
ATOM   6707 C  CZ  . ARG A 1 843  ? 31.112 53.670  -26.108 1.00 8.39  ? 843  ARG A CZ  1 
ATOM   6708 N  NH1 . ARG A 1 843  ? 32.334 54.007  -25.731 1.00 8.02  ? 843  ARG A NH1 1 
ATOM   6709 N  NH2 . ARG A 1 843  ? 30.651 52.454  -25.773 1.00 8.52  ? 843  ARG A NH2 1 
ATOM   6710 N  N   . LEU A 1 844  ? 28.218 59.565  -28.274 1.00 7.32  ? 844  LEU A N   1 
ATOM   6711 C  CA  . LEU A 1 844  ? 28.809 60.884  -27.997 1.00 6.50  ? 844  LEU A CA  1 
ATOM   6712 C  C   . LEU A 1 844  ? 29.457 60.784  -26.597 1.00 6.69  ? 844  LEU A C   1 
ATOM   6713 O  O   . LEU A 1 844  ? 28.759 60.479  -25.625 1.00 6.86  ? 844  LEU A O   1 
ATOM   6714 C  CB  . LEU A 1 844  ? 27.761 62.005  -28.019 1.00 8.21  ? 844  LEU A CB  1 
ATOM   6715 C  CG  . LEU A 1 844  ? 28.398 63.409  -27.881 1.00 8.56  ? 844  LEU A CG  1 
ATOM   6716 C  CD1 . LEU A 1 844  ? 29.253 63.729  -29.105 1.00 11.05 ? 844  LEU A CD1 1 
ATOM   6717 C  CD2 . LEU A 1 844  ? 27.285 64.426  -27.727 1.00 11.64 ? 844  LEU A CD2 1 
ATOM   6718 N  N   . THR A 1 845  ? 30.770 61.014  -26.584 1.00 6.83  ? 845  THR A N   1 
ATOM   6719 C  CA  . THR A 1 845  ? 31.532 60.965  -25.310 1.00 6.53  ? 845  THR A CA  1 
ATOM   6720 C  C   . THR A 1 845  ? 32.082 62.387  -25.033 1.00 7.20  ? 845  THR A C   1 
ATOM   6721 O  O   . THR A 1 845  ? 32.685 63.010  -25.919 1.00 7.55  ? 845  THR A O   1 
ATOM   6722 C  CB  . THR A 1 845  ? 32.738 60.020  -25.428 1.00 7.19  ? 845  THR A CB  1 
ATOM   6723 O  OG1 . THR A 1 845  ? 32.273 58.711  -25.829 1.00 7.85  ? 845  THR A OG1 1 
ATOM   6724 C  CG2 . THR A 1 845  ? 33.457 59.840  -24.094 1.00 7.39  ? 845  THR A CG2 1 
ATOM   6725 N  N   . LEU A 1 846  ? 31.897 62.838  -23.800 1.00 6.77  ? 846  LEU A N   1 
ATOM   6726 C  CA  . LEU A 1 846  ? 32.450 64.116  -23.337 1.00 5.81  ? 846  LEU A CA  1 
ATOM   6727 C  C   . LEU A 1 846  ? 33.520 63.769  -22.280 1.00 5.80  ? 846  LEU A C   1 
ATOM   6728 O  O   . LEU A 1 846  ? 33.152 63.164  -21.225 1.00 6.56  ? 846  LEU A O   1 
ATOM   6729 C  CB  . LEU A 1 846  ? 31.363 65.004  -22.733 1.00 8.15  ? 846  LEU A CB  1 
ATOM   6730 C  CG  . LEU A 1 846  ? 31.865 66.371  -22.233 1.00 8.02  ? 846  LEU A CG  1 
ATOM   6731 C  CD1 . LEU A 1 846  ? 32.277 67.272  -23.393 1.00 9.14  ? 846  LEU A CD1 1 
ATOM   6732 C  CD2 . LEU A 1 846  ? 30.775 67.072  -21.422 1.00 14.08 ? 846  LEU A CD2 1 
ATOM   6733 N  N   . LEU A 1 847  ? 34.789 64.049  -22.547 1.00 5.71  ? 847  LEU A N   1 
ATOM   6734 C  CA  . LEU A 1 847  ? 35.886 63.815  -21.582 1.00 5.19  ? 847  LEU A CA  1 
ATOM   6735 C  C   . LEU A 1 847  ? 36.133 65.140  -20.866 1.00 5.99  ? 847  LEU A C   1 
ATOM   6736 O  O   . LEU A 1 847  ? 35.997 66.228  -21.464 1.00 6.73  ? 847  LEU A O   1 
ATOM   6737 C  CB  . LEU A 1 847  ? 37.172 63.347  -22.256 1.00 6.77  ? 847  LEU A CB  1 
ATOM   6738 C  CG  . LEU A 1 847  ? 37.127 61.994  -22.969 1.00 6.34  ? 847  LEU A CG  1 
ATOM   6739 C  CD1 . LEU A 1 847  ? 36.465 60.893  -22.111 1.00 6.96  ? 847  LEU A CD1 1 
ATOM   6740 C  CD2 . LEU A 1 847  ? 36.424 62.095  -24.370 1.00 7.26  ? 847  LEU A CD2 1 
ATOM   6741 N  N   . THR A 1 848  ? 36.482 65.070  -19.582 1.00 5.85  ? 848  THR A N   1 
ATOM   6742 C  CA  . THR A 1 848  ? 36.708 66.296  -18.777 1.00 6.08  ? 848  THR A CA  1 
ATOM   6743 C  C   . THR A 1 848  ? 38.104 66.369  -18.171 1.00 7.47  ? 848  THR A C   1 
ATOM   6744 O  O   . THR A 1 848  ? 38.776 65.347  -17.914 1.00 8.99  ? 848  THR A O   1 
ATOM   6745 C  CB  . THR A 1 848  ? 35.745 66.399  -17.612 1.00 8.31  ? 848  THR A CB  1 
ATOM   6746 O  OG1 . THR A 1 848  ? 36.182 65.469  -16.569 1.00 12.85 ? 848  THR A OG1 1 
ATOM   6747 C  CG2 . THR A 1 848  ? 34.371 66.113  -17.984 1.00 10.33 ? 848  THR A CG2 1 
ATOM   6748 N  N   . GLY A 1 849  ? 38.580 67.604  -18.031 1.00 6.17  ? 849  GLY A N   1 
ATOM   6749 C  CA  . GLY A 1 849  ? 39.849 67.873  -17.368 1.00 5.88  ? 849  GLY A CA  1 
ATOM   6750 C  C   . GLY A 1 849  ? 39.655 68.205  -15.884 1.00 5.28  ? 849  GLY A C   1 
ATOM   6751 O  O   . GLY A 1 849  ? 40.624 68.629  -15.233 1.00 6.21  ? 849  GLY A O   1 
ATOM   6752 N  N   . GLN A 1 850  ? 38.469 68.024  -15.337 1.00 5.19  ? 850  GLN A N   1 
ATOM   6753 C  CA  . GLN A 1 850  ? 38.156 68.333  -13.938 1.00 5.62  ? 850  GLN A CA  1 
ATOM   6754 C  C   . GLN A 1 850  ? 36.892 67.603  -13.556 1.00 6.14  ? 850  GLN A C   1 
ATOM   6755 O  O   . GLN A 1 850  ? 35.987 67.402  -14.395 1.00 6.56  ? 850  GLN A O   1 
ATOM   6756 C  CB  . GLN A 1 850  ? 37.927 69.875  -13.766 1.00 6.38  ? 850  GLN A CB  1 
ATOM   6757 C  CG  . GLN A 1 850  ? 36.803 70.463  -14.702 1.00 5.96  ? 850  GLN A CG  1 
ATOM   6758 C  CD  . GLN A 1 850  ? 37.193 70.567  -16.148 1.00 6.25  ? 850  GLN A CD  1 
ATOM   6759 O  OE1 . GLN A 1 850  ? 38.310 70.966  -16.530 1.00 6.77  ? 850  GLN A OE1 1 
ATOM   6760 N  NE2 . GLN A 1 850  ? 36.242 70.203  -17.022 1.00 5.98  ? 850  GLN A NE2 1 
ATOM   6761 N  N   . PRO A 1 851  ? 36.763 67.194  -12.296 1.00 5.54  ? 851  PRO A N   1 
ATOM   6762 C  CA  . PRO A 1 851  ? 35.526 66.487  -11.883 1.00 5.12  ? 851  PRO A CA  1 
ATOM   6763 C  C   . PRO A 1 851  ? 34.427 67.496  -11.684 1.00 5.21  ? 851  PRO A C   1 
ATOM   6764 O  O   . PRO A 1 851  ? 34.622 68.562  -11.051 1.00 6.51  ? 851  PRO A O   1 
ATOM   6765 C  CB  . PRO A 1 851  ? 35.912 65.819  -10.528 1.00 5.89  ? 851  PRO A CB  1 
ATOM   6766 C  CG  . PRO A 1 851  ? 37.040 66.789  -9.973  1.00 5.55  ? 851  PRO A CG  1 
ATOM   6767 C  CD  . PRO A 1 851  ? 37.784 67.247  -11.220 1.00 5.24  ? 851  PRO A CD  1 
ATOM   6768 N  N   . LEU A 1 852  ? 33.241 67.194  -12.234 1.00 5.69  ? 852  LEU A N   1 
ATOM   6769 C  CA  . LEU A 1 852  ? 32.054 68.027  -12.128 1.00 7.18  ? 852  LEU A CA  1 
ATOM   6770 C  C   . LEU A 1 852  ? 30.828 67.108  -12.046 1.00 7.55  ? 852  LEU A C   1 
ATOM   6771 O  O   . LEU A 1 852  ? 30.939 65.909  -12.303 1.00 11.70 ? 852  LEU A O   1 
ATOM   6772 C  CB  . LEU A 1 852  ? 31.937 68.924  -13.389 1.00 7.33  ? 852  LEU A CB  1 
ATOM   6773 C  CG  . LEU A 1 852  ? 33.062 69.957  -13.519 1.00 6.35  ? 852  LEU A CG  1 
ATOM   6774 C  CD1 . LEU A 1 852  ? 33.033 70.548  -14.976 1.00 7.52  ? 852  LEU A CD1 1 
ATOM   6775 C  CD2 . LEU A 1 852  ? 32.940 71.068  -12.501 1.00 8.04  ? 852  LEU A CD2 1 
ATOM   6776 N  N   . GLY A 1 853  ? 29.669 67.618  -11.707 1.00 5.75  ? 853  GLY A N   1 
ATOM   6777 C  CA  . GLY A 1 853  ? 28.480 66.800  -11.694 1.00 6.73  ? 853  GLY A CA  1 
ATOM   6778 C  C   . GLY A 1 853  ? 27.730 66.780  -13.004 1.00 6.11  ? 853  GLY A C   1 
ATOM   6779 O  O   . GLY A 1 853  ? 27.775 67.787  -13.749 1.00 6.19  ? 853  GLY A O   1 
ATOM   6780 N  N   . GLY A 1 854  ? 27.043 65.693  -13.310 1.00 5.42  ? 854  GLY A N   1 
ATOM   6781 C  CA  . GLY A 1 854  ? 26.331 65.684  -14.584 1.00 7.02  ? 854  GLY A CA  1 
ATOM   6782 C  C   . GLY A 1 854  ? 25.343 64.558  -14.677 1.00 5.22  ? 854  GLY A C   1 
ATOM   6783 O  O   . GLY A 1 854  ? 25.170 63.729  -13.768 1.00 6.65  ? 854  GLY A O   1 
ATOM   6784 N  N   . SER A 1 855  ? 24.641 64.542  -15.814 1.00 6.86  ? 855  SER A N   1 
ATOM   6785 C  CA  . SER A 1 855  ? 23.586 63.564  -15.995 1.00 7.19  ? 855  SER A CA  1 
ATOM   6786 C  C   . SER A 1 855  ? 23.182 63.527  -17.459 1.00 7.07  ? 855  SER A C   1 
ATOM   6787 O  O   . SER A 1 855  ? 23.708 64.212  -18.339 1.00 7.93  ? 855  SER A O   1 
ATOM   6788 C  CB  . SER A 1 855  ? 22.322 64.021  -15.216 1.00 8.03  ? 855  SER A CB  1 
ATOM   6789 O  OG  . SER A 1 855  ? 21.315 62.980  -15.179 1.00 9.10  ? 855  SER A OG  1 
ATOM   6790 N  N   . SER A 1 856  ? 22.212 62.628  -17.724 1.00 7.49  ? 856  SER A N   1 
ATOM   6791 C  CA  . SER A 1 856  ? 21.476 62.591  -19.030 1.00 7.99  ? 856  SER A CA  1 
ATOM   6792 C  C   . SER A 1 856  ? 20.005 62.614  -18.594 1.00 8.55  ? 856  SER A C   1 
ATOM   6793 O  O   . SER A 1 856  ? 19.458 61.584  -18.182 1.00 9.38  ? 856  SER A O   1 
ATOM   6794 C  CB  . SER A 1 856  ? 21.807 61.341  -19.776 1.00 6.98  ? 856  SER A CB  1 
ATOM   6795 O  OG  . SER A 1 856  ? 20.972 61.279  -20.959 1.00 8.68  ? 856  SER A OG  1 
ATOM   6796 N  N   . LEU A 1 857  ? 19.353 63.773  -18.613 1.00 8.37  ? 857  LEU A N   1 
ATOM   6797 C  CA  . LEU A 1 857  ? 17.981 63.877  -18.097 1.00 7.94  ? 857  LEU A CA  1 
ATOM   6798 C  C   . LEU A 1 857  ? 16.896 63.549  -19.134 1.00 8.79  ? 857  LEU A C   1 
ATOM   6799 O  O   . LEU A 1 857  ? 15.719 63.514  -18.787 1.00 9.18  ? 857  LEU A O   1 
ATOM   6800 C  CB  . LEU A 1 857  ? 17.751 65.304  -17.503 1.00 9.08  ? 857  LEU A CB  1 
ATOM   6801 C  CG  . LEU A 1 857  ? 18.605 65.564  -16.278 1.00 9.71  ? 857  LEU A CG  1 
ATOM   6802 C  CD1 . LEU A 1 857  ? 18.477 67.066  -15.808 1.00 11.04 ? 857  LEU A CD1 1 
ATOM   6803 C  CD2 . LEU A 1 857  ? 18.199 64.599  -15.134 1.00 12.19 ? 857  LEU A CD2 1 
ATOM   6804 N  N   . ALA A 1 858  ? 17.313 63.354  -20.368 1.00 7.89  ? 858  ALA A N   1 
ATOM   6805 C  CA  . ALA A 1 858  ? 16.422 62.934  -21.430 1.00 8.25  ? 858  ALA A CA  1 
ATOM   6806 C  C   . ALA A 1 858  ? 17.231 62.218  -22.496 1.00 9.47  ? 858  ALA A C   1 
ATOM   6807 O  O   . ALA A 1 858  ? 18.412 62.481  -22.675 1.00 8.57  ? 858  ALA A O   1 
ATOM   6808 C  CB  . ALA A 1 858  ? 15.697 64.167  -22.040 1.00 9.57  ? 858  ALA A CB  1 
ATOM   6809 N  N   . SER A 1 859  ? 16.567 61.324  -23.215 1.00 9.70  ? 859  SER A N   1 
ATOM   6810 C  CA  . SER A 1 859  ? 17.198 60.617  -24.286 1.00 8.83  ? 859  SER A CA  1 
ATOM   6811 C  C   . SER A 1 859  ? 17.911 61.566  -25.222 1.00 7.60  ? 859  SER A C   1 
ATOM   6812 O  O   . SER A 1 859  ? 17.370 62.645  -25.536 1.00 9.70  ? 859  SER A O   1 
ATOM   6813 C  CB  . SER A 1 859  ? 16.099 59.802  -25.029 1.00 10.65 ? 859  SER A CB  1 
ATOM   6814 O  OG  . SER A 1 859  ? 16.638 59.054  -26.055 1.00 10.32 ? 859  SER A OG  1 
ATOM   6815 N  N   . GLY A 1 860  ? 19.122 61.226  -25.585 1.00 8.01  ? 860  GLY A N   1 
ATOM   6816 C  CA  . GLY A 1 860  ? 19.890 62.050  -26.488 1.00 9.19  ? 860  GLY A CA  1 
ATOM   6817 C  C   . GLY A 1 860  ? 20.666 63.208  -25.830 1.00 7.77  ? 860  GLY A C   1 
ATOM   6818 O  O   . GLY A 1 860  ? 21.434 63.886  -26.530 1.00 8.36  ? 860  GLY A O   1 
ATOM   6819 N  N   . GLU A 1 861  ? 20.520 63.403  -24.516 1.00 7.51  ? 861  GLU A N   1 
ATOM   6820 C  CA  . GLU A 1 861  ? 21.216 64.531  -23.865 1.00 8.20  ? 861  GLU A CA  1 
ATOM   6821 C  C   . GLU A 1 861  ? 22.345 64.145  -22.962 1.00 9.45  ? 861  GLU A C   1 
ATOM   6822 O  O   . GLU A 1 861  ? 22.365 63.023  -22.399 1.00 9.79  ? 861  GLU A O   1 
ATOM   6823 C  CB  . GLU A 1 861  ? 20.279 65.329  -22.969 1.00 11.05 ? 861  GLU A CB  1 
ATOM   6824 C  CG  . GLU A 1 861  ? 19.155 65.938  -23.686 1.00 11.46 ? 861  GLU A CG  1 
ATOM   6825 C  CD  . GLU A 1 861  ? 18.228 66.783  -22.791 1.00 12.95 ? 861  GLU A CD  1 
ATOM   6826 O  OE1 . GLU A 1 861  ? 18.345 66.864  -21.526 1.00 12.95 ? 861  GLU A OE1 1 
ATOM   6827 O  OE2 . GLU A 1 861  ? 17.278 67.423  -23.373 1.00 15.99 ? 861  GLU A OE2 1 
ATOM   6828 N  N   . LEU A 1 862  ? 23.289 65.055  -22.828 1.00 8.39  ? 862  LEU A N   1 
ATOM   6829 C  CA  . LEU A 1 862  ? 24.347 64.924  -21.775 1.00 8.68  ? 862  LEU A CA  1 
ATOM   6830 C  C   . LEU A 1 862  ? 24.367 66.314  -21.143 1.00 6.95  ? 862  LEU A C   1 
ATOM   6831 O  O   . LEU A 1 862  ? 24.207 67.330  -21.850 1.00 8.09  ? 862  LEU A O   1 
ATOM   6832 C  CB  . LEU A 1 862  ? 25.748 64.666  -22.381 1.00 9.30  ? 862  LEU A CB  1 
ATOM   6833 C  CG  . LEU A 1 862  ? 26.043 63.308  -22.983 1.00 9.96  ? 862  LEU A CG  1 
ATOM   6834 C  CD1 . LEU A 1 862  ? 27.373 63.327  -23.704 1.00 11.02 ? 862  LEU A CD1 1 
ATOM   6835 C  CD2 . LEU A 1 862  ? 26.006 62.254  -21.889 1.00 11.75 ? 862  LEU A CD2 1 
ATOM   6836 N  N   . GLU A 1 863  ? 24.636 66.437  -19.850 1.00 6.38  ? 863  GLU A N   1 
ATOM   6837 C  CA  . GLU A 1 863  ? 24.829 67.772  -19.295 1.00 6.66  ? 863  GLU A CA  1 
ATOM   6838 C  C   . GLU A 1 863  ? 25.822 67.687  -18.152 1.00 7.21  ? 863  GLU A C   1 
ATOM   6839 O  O   . GLU A 1 863  ? 25.951 66.666  -17.474 1.00 6.66  ? 863  GLU A O   1 
ATOM   6840 C  CB  . GLU A 1 863  ? 23.550 68.426  -18.831 1.00 8.20  ? 863  GLU A CB  1 
ATOM   6841 C  CG  . GLU A 1 863  ? 22.922 67.808  -17.580 1.00 8.79  ? 863  GLU A CG  1 
ATOM   6842 C  CD  . GLU A 1 863  ? 21.631 68.538  -17.210 1.00 8.58  ? 863  GLU A CD  1 
ATOM   6843 O  OE1 . GLU A 1 863  ? 20.695 68.584  -18.088 1.00 9.93  ? 863  GLU A OE1 1 
ATOM   6844 O  OE2 . GLU A 1 863  ? 21.508 69.099  -16.087 1.00 8.72  ? 863  GLU A OE2 1 
ATOM   6845 N  N   . ILE A 1 864  ? 26.533 68.786  -17.948 1.00 6.50  ? 864  ILE A N   1 
ATOM   6846 C  CA  . ILE A 1 864  ? 27.577 68.837  -16.889 1.00 6.87  ? 864  ILE A CA  1 
ATOM   6847 C  C   . ILE A 1 864  ? 27.587 70.227  -16.285 1.00 6.15  ? 864  ILE A C   1 
ATOM   6848 O  O   . ILE A 1 864  ? 27.609 71.251  -17.030 1.00 6.20  ? 864  ILE A O   1 
ATOM   6849 C  CB  . ILE A 1 864  ? 28.952 68.405  -17.498 1.00 8.48  ? 864  ILE A CB  1 
ATOM   6850 C  CG1 . ILE A 1 864  ? 30.026 68.334  -16.403 1.00 9.87  ? 864  ILE A CG1 1 
ATOM   6851 C  CG2 . ILE A 1 864  ? 29.348 69.247  -18.696 1.00 11.04 ? 864  ILE A CG2 1 
ATOM   6852 C  CD1 . ILE A 1 864  ? 31.143 67.377  -16.926 1.00 9.85  ? 864  ILE A CD1 1 
ATOM   6853 N  N   . MET A 1 865  ? 27.537 70.283  -14.953 1.00 6.50  ? 865  MET A N   1 
ATOM   6854 C  CA  . MET A 1 865  ? 27.479 71.549  -14.243 1.00 6.41  ? 865  MET A CA  1 
ATOM   6855 C  C   . MET A 1 865  ? 28.837 72.233  -14.295 1.00 7.00  ? 865  MET A C   1 
ATOM   6856 O  O   . MET A 1 865  ? 29.893 71.602  -14.121 1.00 8.08  ? 865  MET A O   1 
ATOM   6857 C  CB  . MET A 1 865  ? 27.021 71.287  -12.803 1.00 7.06  ? 865  MET A CB  1 
ATOM   6858 C  CG  . MET A 1 865  ? 26.427 72.562  -12.134 1.00 7.24  ? 865  MET A CG  1 
ATOM   6859 S  SD  . MET A 1 865  ? 24.808 72.994  -12.879 1.00 9.14  ? 865  MET A SD  1 
ATOM   6860 C  CE  . MET A 1 865  ? 23.829 71.731  -11.954 1.00 9.51  ? 865  MET A CE  1 
ATOM   6861 N  N   . GLN A 1 866  ? 28.815 73.564  -14.495 1.00 6.93  ? 866  GLN A N   1 
ATOM   6862 C  CA  . GLN A 1 866  ? 30.043 74.357  -14.613 1.00 6.32  ? 866  GLN A CA  1 
ATOM   6863 C  C   . GLN A 1 866  ? 30.437 75.048  -13.313 1.00 7.10  ? 866  GLN A C   1 
ATOM   6864 O  O   . GLN A 1 866  ? 31.613 75.078  -12.940 1.00 7.59  ? 866  GLN A O   1 
ATOM   6865 C  CB  . GLN A 1 866  ? 29.865 75.415  -15.718 1.00 7.24  ? 866  GLN A CB  1 
ATOM   6866 C  CG  . GLN A 1 866  ? 29.541 74.778  -17.095 1.00 7.72  ? 866  GLN A CG  1 
ATOM   6867 C  CD  . GLN A 1 866  ? 30.581 73.801  -17.518 1.00 6.62  ? 866  GLN A CD  1 
ATOM   6868 O  OE1 . GLN A 1 866  ? 31.696 74.175  -17.861 1.00 8.50  ? 866  GLN A OE1 1 
ATOM   6869 N  NE2 . GLN A 1 866  ? 30.233 72.521  -17.490 1.00 8.28  ? 866  GLN A NE2 1 
ATOM   6870 N  N   . ASP A 1 867  ? 29.443 75.686  -12.655 1.00 7.41  ? 867  ASP A N   1 
ATOM   6871 C  CA  . ASP A 1 867  ? 29.673 76.323  -11.349 1.00 6.74  ? 867  ASP A CA  1 
ATOM   6872 C  C   . ASP A 1 867  ? 28.341 76.535  -10.679 1.00 5.94  ? 867  ASP A C   1 
ATOM   6873 O  O   . ASP A 1 867  ? 27.285 76.454  -11.347 1.00 7.42  ? 867  ASP A O   1 
ATOM   6874 C  CB  . ASP A 1 867  ? 30.494 77.652  -11.475 1.00 8.74  ? 867  ASP A CB  1 
ATOM   6875 C  CG  . ASP A 1 867  ? 31.180 78.048  -10.145 1.00 8.05  ? 867  ASP A CG  1 
ATOM   6876 O  OD1 . ASP A 1 867  ? 31.046 77.367  -9.123  1.00 8.41  ? 867  ASP A OD1 1 
ATOM   6877 O  OD2 . ASP A 1 867  ? 31.914 79.052  -10.188 1.00 8.64  ? 867  ASP A OD2 1 
ATOM   6878 N  N   . ARG A 1 868  ? 28.372 76.798  -9.388  1.00 7.14  ? 868  ARG A N   1 
ATOM   6879 C  CA  . ARG A 1 868  ? 27.158 77.054  -8.628  1.00 6.96  ? 868  ARG A CA  1 
ATOM   6880 C  C   . ARG A 1 868  ? 27.458 78.063  -7.530  1.00 7.12  ? 868  ARG A C   1 
ATOM   6881 O  O   . ARG A 1 868  ? 28.482 77.983  -6.872  1.00 7.89  ? 868  ARG A O   1 
ATOM   6882 C  CB  . ARG A 1 868  ? 26.622 75.739  -8.037  1.00 7.48  ? 868  ARG A CB  1 
ATOM   6883 C  CG  . ARG A 1 868  ? 27.651 74.925  -7.243  1.00 8.32  ? 868  ARG A CG  1 
ATOM   6884 C  CD  . ARG A 1 868  ? 27.341 73.411  -7.255  1.00 8.10  ? 868  ARG A CD  1 
ATOM   6885 N  NE  . ARG A 1 868  ? 25.979 73.180  -6.781  1.00 6.75  ? 868  ARG A NE  1 
ATOM   6886 C  CZ  . ARG A 1 868  ? 25.662 72.923  -5.520  1.00 6.70  ? 868  ARG A CZ  1 
ATOM   6887 N  NH1 . ARG A 1 868  ? 26.601 72.821  -4.587  1.00 7.87  ? 868  ARG A NH1 1 
ATOM   6888 N  NH2 . ARG A 1 868  ? 24.397 72.764  -5.188  1.00 8.16  ? 868  ARG A NH2 1 
ATOM   6889 N  N   . ARG A 1 869  ? 26.555 79.020  -7.353  1.00 8.17  ? 869  ARG A N   1 
ATOM   6890 C  CA  . ARG A 1 869  ? 26.729 80.104  -6.351  1.00 8.20  ? 869  ARG A CA  1 
ATOM   6891 C  C   . ARG A 1 869  ? 25.453 80.099  -5.551  1.00 8.64  ? 869  ARG A C   1 
ATOM   6892 O  O   . ARG A 1 869  ? 24.365 80.300  -6.096  1.00 9.58  ? 869  ARG A O   1 
ATOM   6893 C  CB  . ARG A 1 869  ? 26.980 81.425  -7.086  1.00 9.53  ? 869  ARG A CB  1 
ATOM   6894 C  CG  . ARG A 1 869  ? 27.187 82.566  -6.099  1.00 9.20  ? 869  ARG A CG  1 
ATOM   6895 C  CD  . ARG A 1 869  ? 27.478 83.848  -6.905  1.00 11.81 ? 869  ARG A CD  1 
ATOM   6896 N  NE  . ARG A 1 869  ? 27.608 85.026  -6.015  1.00 15.38 ? 869  ARG A NE  1 
ATOM   6897 C  CZ  . ARG A 1 869  ? 28.745 85.354  -5.417  1.00 13.26 ? 869  ARG A CZ  1 
ATOM   6898 N  NH1 . ARG A 1 869  ? 29.811 84.643  -5.577  1.00 13.08 ? 869  ARG A NH1 1 
ATOM   6899 N  NH2 . ARG A 1 869  ? 28.803 86.481  -4.665  1.00 16.73 ? 869  ARG A NH2 1 
ATOM   6900 N  N   . LEU A 1 870  ? 25.585 79.832  -4.261  1.00 10.02 ? 870  LEU A N   1 
ATOM   6901 C  CA  . LEU A 1 870  ? 24.427 79.593  -3.354  1.00 9.88  ? 870  LEU A CA  1 
ATOM   6902 C  C   . LEU A 1 870  ? 24.495 80.461  -2.137  1.00 10.89 ? 870  LEU A C   1 
ATOM   6903 O  O   . LEU A 1 870  ? 25.471 80.416  -1.403  1.00 12.36 ? 870  LEU A O   1 
ATOM   6904 C  CB  . LEU A 1 870  ? 24.436 78.100  -2.976  1.00 11.79 ? 870  LEU A CB  1 
ATOM   6905 C  CG  . LEU A 1 870  ? 24.410 77.296  -4.277  1.00 18.77 ? 870  LEU A CG  1 
ATOM   6906 C  CD1 . LEU A 1 870  ? 25.024 76.013  -4.045  1.00 20.08 ? 870  LEU A CD1 1 
ATOM   6907 C  CD2 . LEU A 1 870  ? 23.067 77.266  -4.934  1.00 14.17 ? 870  LEU A CD2 1 
ATOM   6908 N  N   . ALA A 1 871  ? 23.416 81.201  -1.889  1.00 12.29 ? 871  ALA A N   1 
ATOM   6909 C  CA  . ALA A 1 871  ? 23.472 82.107  -0.745  1.00 14.56 ? 871  ALA A CA  1 
ATOM   6910 C  C   . ALA A 1 871  ? 23.150 81.450  0.602   1.00 17.69 ? 871  ALA A C   1 
ATOM   6911 O  O   . ALA A 1 871  ? 23.498 81.984  1.648   1.00 20.99 ? 871  ALA A O   1 
ATOM   6912 C  CB  . ALA A 1 871  ? 22.515 83.285  -0.976  1.00 18.40 ? 871  ALA A CB  1 
ATOM   6913 N  N   . SER A 1 872  ? 22.509 80.307  0.573   1.00 14.24 ? 872  SER A N   1 
ATOM   6914 C  CA  . SER A 1 872  ? 22.107 79.651  1.823   1.00 16.03 ? 872  SER A CA  1 
ATOM   6915 C  C   . SER A 1 872  ? 22.965 78.463  2.200   1.00 13.46 ? 872  SER A C   1 
ATOM   6916 O  O   . SER A 1 872  ? 23.607 77.848  1.351   1.00 13.74 ? 872  SER A O   1 
ATOM   6917 C  CB  . SER A 1 872  ? 20.645 79.179  1.671   1.00 19.50 ? 872  SER A CB  1 
ATOM   6918 O  OG  . SER A 1 872  ? 19.791 80.321  1.659   1.00 26.31 ? 872  SER A OG  1 
ATOM   6919 N  N   . ASP A 1 873  ? 23.003 78.204  3.501   1.00 14.61 ? 873  ASP A N   1 
ATOM   6920 C  CA  . ASP A 1 873  ? 23.657 77.035  4.083   1.00 14.17 ? 873  ASP A CA  1 
ATOM   6921 C  C   . ASP A 1 873  ? 22.646 75.881  3.949   1.00 14.03 ? 873  ASP A C   1 
ATOM   6922 O  O   . ASP A 1 873  ? 21.408 76.101  4.059   1.00 15.53 ? 873  ASP A O   1 
ATOM   6923 C  CB  . ASP A 1 873  ? 23.957 77.259  5.574   1.00 13.24 ? 873  ASP A CB  1 
ATOM   6924 C  CG  . ASP A 1 873  ? 24.446 75.989  6.244   1.00 15.30 ? 873  ASP A CG  1 
ATOM   6925 O  OD1 . ASP A 1 873  ? 25.545 75.530  5.842   1.00 15.63 ? 873  ASP A OD1 1 
ATOM   6926 O  OD2 . ASP A 1 873  ? 23.731 75.444  7.120   1.00 16.10 ? 873  ASP A OD2 1 
ATOM   6927 N  N   . ASP A 1 874  ? 23.139 74.657  3.740   1.00 12.75 ? 874  ASP A N   1 
ATOM   6928 C  CA  . ASP A 1 874  ? 22.263 73.480  3.586   1.00 10.68 ? 874  ASP A CA  1 
ATOM   6929 C  C   . ASP A 1 874  ? 22.216 72.557  4.794   1.00 10.59 ? 874  ASP A C   1 
ATOM   6930 O  O   . ASP A 1 874  ? 21.944 71.342  4.683   1.00 13.96 ? 874  ASP A O   1 
ATOM   6931 C  CB  . ASP A 1 874  ? 22.575 72.694  2.311   1.00 10.52 ? 874  ASP A CB  1 
ATOM   6932 C  CG  . ASP A 1 874  ? 24.056 72.379  2.165   1.00 9.43  ? 874  ASP A CG  1 
ATOM   6933 O  OD1 . ASP A 1 874  ? 24.883 72.773  3.052   1.00 12.07 ? 874  ASP A OD1 1 
ATOM   6934 O  OD2 . ASP A 1 874  ? 24.352 71.751  1.127   1.00 9.37  ? 874  ASP A OD2 1 
ATOM   6935 N  N   . GLU A 1 875  ? 22.548 73.118  5.951   1.00 12.12 ? 875  GLU A N   1 
ATOM   6936 C  CA  . GLU A 1 875  ? 22.291 72.404  7.199   1.00 13.72 ? 875  GLU A CA  1 
ATOM   6937 C  C   . GLU A 1 875  ? 22.999 71.112  7.452   1.00 13.57 ? 875  GLU A C   1 
ATOM   6938 O  O   . GLU A 1 875  ? 22.452 70.193  8.080   1.00 14.35 ? 875  GLU A O   1 
ATOM   6939 C  CB  . GLU A 1 875  ? 20.762 72.200  7.394   1.00 19.74 ? 875  GLU A CB  1 
ATOM   6940 C  CG  . GLU A 1 875  ? 19.924 73.494  7.439   1.00 24.22 ? 875  GLU A CG  1 
ATOM   6941 C  CD  . GLU A 1 875  ? 18.424 73.148  7.608   1.00 31.38 ? 875  GLU A CD  1 
ATOM   6942 O  OE1 . GLU A 1 875  ? 18.055 72.497  8.604   1.00 39.92 ? 875  GLU A OE1 1 
ATOM   6943 O  OE2 . GLU A 1 875  ? 17.621 73.505  6.716   1.00 42.63 ? 875  GLU A OE2 1 
ATOM   6944 N  N   . ARG A 1 876  ? 24.229 71.010  6.947   1.00 10.86 ? 876  ARG A N   1 
ATOM   6945 C  CA  . ARG A 1 876  ? 25.051 69.828  7.228   1.00 12.51 ? 876  ARG A CA  1 
ATOM   6946 C  C   . ARG A 1 876  ? 26.279 70.189  8.055   1.00 12.01 ? 876  ARG A C   1 
ATOM   6947 O  O   . ARG A 1 876  ? 27.151 69.333  8.221   1.00 13.07 ? 876  ARG A O   1 
ATOM   6948 C  CB  . ARG A 1 876  ? 25.440 69.090  5.933   1.00 11.68 ? 876  ARG A CB  1 
ATOM   6949 C  CG  . ARG A 1 876  ? 24.220 68.544  5.178   1.00 11.42 ? 876  ARG A CG  1 
ATOM   6950 C  CD  . ARG A 1 876  ? 23.358 67.602  6.049   1.00 12.07 ? 876  ARG A CD  1 
ATOM   6951 N  NE  . ARG A 1 876  ? 22.314 66.870  5.295   1.00 11.02 ? 876  ARG A NE  1 
ATOM   6952 C  CZ  . ARG A 1 876  ? 21.144 67.420  4.943   1.00 11.38 ? 876  ARG A CZ  1 
ATOM   6953 N  NH1 . ARG A 1 876  ? 20.904 68.706  5.210   1.00 10.38 ? 876  ARG A NH1 1 
ATOM   6954 N  NH2 . ARG A 1 876  ? 20.213 66.655  4.403   1.00 9.79  ? 876  ARG A NH2 1 
ATOM   6955 N  N   . GLY A 1 877  ? 26.358 71.422  8.557   1.00 11.63 ? 877  GLY A N   1 
ATOM   6956 C  CA  . GLY A 1 877  ? 27.440 71.812  9.458   1.00 11.78 ? 877  GLY A CA  1 
ATOM   6957 C  C   . GLY A 1 877  ? 28.427 72.805  8.910   1.00 10.72 ? 877  GLY A C   1 
ATOM   6958 O  O   . GLY A 1 877  ? 29.243 73.319  9.700   1.00 12.98 ? 877  GLY A O   1 
ATOM   6959 N  N   . LEU A 1 878  ? 28.382 73.102  7.608   1.00 10.35 ? 878  LEU A N   1 
ATOM   6960 C  CA  . LEU A 1 878  ? 29.365 74.026  7.047   1.00 11.62 ? 878  LEU A CA  1 
ATOM   6961 C  C   . LEU A 1 878  ? 29.112 75.462  7.523   1.00 12.36 ? 878  LEU A C   1 
ATOM   6962 O  O   . LEU A 1 878  ? 30.070 76.227  7.717   1.00 13.67 ? 878  LEU A O   1 
ATOM   6963 C  CB  . LEU A 1 878  ? 29.345 73.910  5.517   1.00 10.42 ? 878  LEU A CB  1 
ATOM   6964 C  CG  . LEU A 1 878  ? 30.147 74.931  4.716   1.00 11.67 ? 878  LEU A CG  1 
ATOM   6965 C  CD1 . LEU A 1 878  ? 31.651 74.931  5.150   1.00 11.77 ? 878  LEU A CD1 1 
ATOM   6966 C  CD2 . LEU A 1 878  ? 30.004 74.601  3.207   1.00 14.55 ? 878  LEU A CD2 1 
ATOM   6967 N  N   . GLY A 1 879  ? 27.836 75.802  7.705   1.00 10.96 ? 879  GLY A N   1 
ATOM   6968 C  CA  . GLY A 1 879  ? 27.472 77.126  8.235   1.00 12.62 ? 879  GLY A CA  1 
ATOM   6969 C  C   . GLY A 1 879  ? 27.711 78.291  7.283   1.00 14.88 ? 879  GLY A C   1 
ATOM   6970 O  O   . GLY A 1 879  ? 27.977 79.399  7.731   1.00 15.70 ? 879  GLY A O   1 
ATOM   6971 N  N   . GLN A 1 880  ? 27.751 78.026  5.988   1.00 13.54 ? 880  GLN A N   1 
ATOM   6972 C  CA  . GLN A 1 880  ? 27.858 79.095  5.006   1.00 13.58 ? 880  GLN A CA  1 
ATOM   6973 C  C   . GLN A 1 880  ? 27.329 78.585  3.677   1.00 12.59 ? 880  GLN A C   1 
ATOM   6974 O  O   . GLN A 1 880  ? 27.239 77.393  3.474   1.00 14.58 ? 880  GLN A O   1 
ATOM   6975 C  CB  . GLN A 1 880  ? 29.299 79.628  4.873   1.00 12.53 ? 880  GLN A CB  1 
ATOM   6976 C  CG  . GLN A 1 880  ? 30.337 78.605  4.359   1.00 13.08 ? 880  GLN A CG  1 
ATOM   6977 C  CD  . GLN A 1 880  ? 31.623 79.252  3.849   1.00 13.78 ? 880  GLN A CD  1 
ATOM   6978 O  OE1 . GLN A 1 880  ? 32.533 79.516  4.604   1.00 18.47 ? 880  GLN A OE1 1 
ATOM   6979 N  NE2 . GLN A 1 880  ? 31.676 79.496  2.564   1.00 11.18 ? 880  GLN A NE2 1 
ATOM   6980 N  N   . GLY A 1 881  ? 26.983 79.498  2.777   1.00 14.27 ? 881  GLY A N   1 
ATOM   6981 C  CA  . GLY A 1 881  ? 26.637 79.113  1.406   1.00 16.98 ? 881  GLY A CA  1 
ATOM   6982 C  C   . GLY A 1 881  ? 27.958 79.048  0.628   1.00 15.72 ? 881  GLY A C   1 
ATOM   6983 O  O   . GLY A 1 881  ? 29.066 78.858  1.189   1.00 16.05 ? 881  GLY A O   1 
ATOM   6984 N  N   . VAL A 1 882  ? 27.839 79.164  -0.693  1.00 11.38 ? 882  VAL A N   1 
ATOM   6985 C  CA  . VAL A 1 882  ? 29.017 79.124  -1.567  1.00 10.61 ? 882  VAL A CA  1 
ATOM   6986 C  C   . VAL A 1 882  ? 28.934 80.420  -2.342  1.00 10.32 ? 882  VAL A C   1 
ATOM   6987 O  O   . VAL A 1 882  ? 28.200 80.564  -3.342  1.00 9.90  ? 882  VAL A O   1 
ATOM   6988 C  CB  . VAL A 1 882  ? 28.939 77.924  -2.490  1.00 10.73 ? 882  VAL A CB  1 
ATOM   6989 C  CG1 . VAL A 1 882  ? 30.076 77.982  -3.480  1.00 12.31 ? 882  VAL A CG1 1 
ATOM   6990 C  CG2 . VAL A 1 882  ? 29.024 76.637  -1.658  1.00 14.49 ? 882  VAL A CG2 1 
ATOM   6991 N  N   . LEU A 1 883  ? 29.705 81.392  -1.860  1.00 10.72 ? 883  LEU A N   1 
ATOM   6992 C  CA  . LEU A 1 883  ? 29.697 82.764  -2.448  1.00 11.38 ? 883  LEU A CA  1 
ATOM   6993 C  C   . LEU A 1 883  ? 31.100 83.230  -2.778  1.00 13.05 ? 883  LEU A C   1 
ATOM   6994 O  O   . LEU A 1 883  ? 31.326 84.450  -2.977  1.00 16.74 ? 883  LEU A O   1 
ATOM   6995 C  CB  . LEU A 1 883  ? 29.026 83.779  -1.464  1.00 12.76 ? 883  LEU A CB  1 
ATOM   6996 C  CG  . LEU A 1 883  ? 27.534 83.467  -1.236  1.00 12.89 ? 883  LEU A CG  1 
ATOM   6997 C  CD1 . LEU A 1 883  ? 26.908 84.352  -0.080  1.00 15.62 ? 883  LEU A CD1 1 
ATOM   6998 C  CD2 . LEU A 1 883  ? 26.737 83.689  -2.564  1.00 13.47 ? 883  LEU A CD2 1 
ATOM   6999 N  N   . ASP A 1 884  ? 32.040 82.321  -2.824  1.00 10.29 ? 884  ASP A N   1 
ATOM   7000 C  CA  . ASP A 1 884  ? 33.454 82.572  -3.074  1.00 10.51 ? 884  ASP A CA  1 
ATOM   7001 C  C   . ASP A 1 884  ? 33.953 82.127  -4.441  1.00 10.30 ? 884  ASP A C   1 
ATOM   7002 O  O   . ASP A 1 884  ? 35.141 81.869  -4.641  1.00 11.21 ? 884  ASP A O   1 
ATOM   7003 C  CB  . ASP A 1 884  ? 34.343 81.976  -1.954  1.00 12.44 ? 884  ASP A CB  1 
ATOM   7004 C  CG  . ASP A 1 884  ? 34.118 80.465  -1.733  1.00 14.34 ? 884  ASP A CG  1 
ATOM   7005 O  OD1 . ASP A 1 884  ? 33.302 79.816  -2.472  1.00 12.58 ? 884  ASP A OD1 1 
ATOM   7006 O  OD2 . ASP A 1 884  ? 34.774 79.948  -0.779  1.00 16.32 ? 884  ASP A OD2 1 
ATOM   7007 N  N   . ASN A 1 885  ? 33.052 82.108  -5.400  1.00 10.15 ? 885  ASN A N   1 
ATOM   7008 C  CA  . ASN A 1 885  ? 33.390 81.719  -6.749  1.00 9.91  ? 885  ASN A CA  1 
ATOM   7009 C  C   . ASN A 1 885  ? 34.480 82.579  -7.320  1.00 10.72 ? 885  ASN A C   1 
ATOM   7010 O  O   . ASN A 1 885  ? 34.611 83.732  -6.972  1.00 11.79 ? 885  ASN A O   1 
ATOM   7011 C  CB  . ASN A 1 885  ? 32.159 81.830  -7.636  1.00 9.94  ? 885  ASN A CB  1 
ATOM   7012 C  CG  . ASN A 1 885  ? 30.936 81.211  -6.995  1.00 10.87 ? 885  ASN A CG  1 
ATOM   7013 O  OD1 . ASN A 1 885  ? 30.298 81.785  -6.133  1.00 12.12 ? 885  ASN A OD1 1 
ATOM   7014 N  ND2 . ASN A 1 885  ? 30.614 80.017  -7.432  1.00 9.57  ? 885  ASN A ND2 1 
ATOM   7015 N  N   . LYS A 1 886  ? 35.252 81.996  -8.217  1.00 10.70 ? 886  LYS A N   1 
ATOM   7016 C  CA  . LYS A 1 886  ? 36.266 82.729  -8.952  1.00 11.99 ? 886  LYS A CA  1 
ATOM   7017 C  C   . LYS A 1 886  ? 36.357 82.151  -10.358 1.00 9.78  ? 886  LYS A C   1 
ATOM   7018 O  O   . LYS A 1 886  ? 35.981 80.982  -10.625 1.00 10.92 ? 886  LYS A O   1 
ATOM   7019 C  CB  . LYS A 1 886  ? 37.618 82.664  -8.227  1.00 16.77 ? 886  LYS A CB  1 
ATOM   7020 C  CG  . LYS A 1 886  ? 38.170 81.265  -8.062  1.00 16.32 ? 886  LYS A CG  1 
ATOM   7021 C  CD  . LYS A 1 886  ? 39.211 81.099  -6.887  1.00 22.38 ? 886  LYS A CD  1 
ATOM   7022 C  CE  . LYS A 1 886  ? 40.566 81.373  -7.421  1.00 17.07 ? 886  LYS A CE  1 
ATOM   7023 N  NZ  . LYS A 1 886  ? 41.683 81.687  -6.495  1.00 20.85 ? 886  LYS A NZ  1 
ATOM   7024 N  N   . PRO A 1 887  ? 36.865 82.922  -11.317 1.00 8.72  ? 887  PRO A N   1 
ATOM   7025 C  CA  . PRO A 1 887  ? 36.953 82.414  -12.689 1.00 9.30  ? 887  PRO A CA  1 
ATOM   7026 C  C   . PRO A 1 887  ? 37.732 81.135  -12.778 1.00 8.86  ? 887  PRO A C   1 
ATOM   7027 O  O   . PRO A 1 887  ? 38.785 80.993  -12.192 1.00 9.88  ? 887  PRO A O   1 
ATOM   7028 C  CB  . PRO A 1 887  ? 37.632 83.547  -13.458 1.00 10.83 ? 887  PRO A CB  1 
ATOM   7029 C  CG  . PRO A 1 887  ? 37.209 84.812  -12.654 1.00 11.57 ? 887  PRO A CG  1 
ATOM   7030 C  CD  . PRO A 1 887  ? 37.164 84.369  -11.231 1.00 10.77 ? 887  PRO A CD  1 
ATOM   7031 N  N   . VAL A 1 888  ? 37.208 80.183  -13.553 1.00 7.49  ? 888  VAL A N   1 
ATOM   7032 C  CA  . VAL A 1 888  ? 37.866 78.894  -13.740 1.00 7.34  ? 888  VAL A CA  1 
ATOM   7033 C  C   . VAL A 1 888  ? 37.816 78.523  -15.196 1.00 7.03  ? 888  VAL A C   1 
ATOM   7034 O  O   . VAL A 1 888  ? 36.783 78.781  -15.875 1.00 8.18  ? 888  VAL A O   1 
ATOM   7035 C  CB  . VAL A 1 888  ? 37.228 77.761  -12.838 1.00 7.67  ? 888  VAL A CB  1 
ATOM   7036 C  CG1 . VAL A 1 888  ? 35.738 77.650  -13.097 1.00 8.60  ? 888  VAL A CG1 1 
ATOM   7037 C  CG2 . VAL A 1 888  ? 37.915 76.426  -13.113 1.00 8.29  ? 888  VAL A CG2 1 
ATOM   7038 N  N   . LEU A 1 889  ? 38.879 77.959  -15.728 1.00 6.11  ? 889  LEU A N   1 
ATOM   7039 C  CA  . LEU A 1 889  ? 38.888 77.479  -17.116 1.00 6.55  ? 889  LEU A CA  1 
ATOM   7040 C  C   . LEU A 1 889  ? 38.688 75.943  -17.166 1.00 6.86  ? 889  LEU A C   1 
ATOM   7041 O  O   . LEU A 1 889  ? 39.581 75.157  -16.811 1.00 8.73  ? 889  LEU A O   1 
ATOM   7042 C  CB  . LEU A 1 889  ? 40.221 77.850  -17.798 1.00 8.36  ? 889  LEU A CB  1 
ATOM   7043 C  CG  . LEU A 1 889  ? 40.232 77.403  -19.291 1.00 8.98  ? 889  LEU A CG  1 
ATOM   7044 C  CD1 . LEU A 1 889  ? 39.391 78.376  -20.143 1.00 9.77  ? 889  LEU A CD1 1 
ATOM   7045 C  CD2 . LEU A 1 889  ? 41.704 77.328  -19.808 1.00 13.61 ? 889  LEU A CD2 1 
ATOM   7046 N  N   . HIS A 1 890  ? 37.465 75.548  -17.484 1.00 5.72  ? 890  HIS A N   1 
ATOM   7047 C  CA  . HIS A 1 890  ? 37.150 74.119  -17.616 1.00 6.42  ? 890  HIS A CA  1 
ATOM   7048 C  C   . HIS A 1 890  ? 37.539 73.633  -19.009 1.00 6.47  ? 890  HIS A C   1 
ATOM   7049 O  O   . HIS A 1 890  ? 37.293 74.357  -20.009 1.00 7.51  ? 890  HIS A O   1 
ATOM   7050 C  CB  . HIS A 1 890  ? 35.660 73.880  -17.405 1.00 7.01  ? 890  HIS A CB  1 
ATOM   7051 C  CG  . HIS A 1 890  ? 35.222 74.025  -15.996 1.00 6.84  ? 890  HIS A CG  1 
ATOM   7052 N  ND1 . HIS A 1 890  ? 36.061 73.674  -14.943 1.00 8.80  ? 890  HIS A ND1 1 
ATOM   7053 C  CD2 . HIS A 1 890  ? 34.050 74.450  -15.468 1.00 7.86  ? 890  HIS A CD2 1 
ATOM   7054 C  CE1 . HIS A 1 890  ? 35.386 73.884  -13.816 1.00 8.61  ? 890  HIS A CE1 1 
ATOM   7055 N  NE2 . HIS A 1 890  ? 34.175 74.354  -14.097 1.00 7.79  ? 890  HIS A NE2 1 
ATOM   7056 N  N   . ILE A 1 891  ? 38.054 72.424  -19.115 1.00 5.36  ? 891  ILE A N   1 
ATOM   7057 C  CA  . ILE A 1 891  ? 38.481 71.900  -20.426 1.00 5.82  ? 891  ILE A CA  1 
ATOM   7058 C  C   . ILE A 1 891  ? 37.835 70.548  -20.687 1.00 6.21  ? 891  ILE A C   1 
ATOM   7059 O  O   . ILE A 1 891  ? 37.557 69.765  -19.745 1.00 6.11  ? 891  ILE A O   1 
ATOM   7060 C  CB  . ILE A 1 891  ? 40.026 71.819  -20.537 1.00 5.77  ? 891  ILE A CB  1 
ATOM   7061 C  CG1 . ILE A 1 891  ? 40.639 70.833  -19.513 1.00 6.85  ? 891  ILE A CG1 1 
ATOM   7062 C  CG2 . ILE A 1 891  ? 40.588 73.261  -20.344 1.00 7.95  ? 891  ILE A CG2 1 
ATOM   7063 C  CD1 . ILE A 1 891  ? 42.188 70.635  -19.761 1.00 8.37  ? 891  ILE A CD1 1 
ATOM   7064 N  N   . TYR A 1 892  ? 37.607 70.264  -21.955 1.00 5.44  ? 892  TYR A N   1 
ATOM   7065 C  CA  . TYR A 1 892  ? 36.927 69.036  -22.389 1.00 5.46  ? 892  TYR A CA  1 
ATOM   7066 C  C   . TYR A 1 892  ? 37.351 68.603  -23.768 1.00 5.22  ? 892  TYR A C   1 
ATOM   7067 O  O   . TYR A 1 892  ? 37.951 69.354  -24.543 1.00 5.96  ? 892  TYR A O   1 
ATOM   7068 C  CB  . TYR A 1 892  ? 35.378 69.275  -22.526 1.00 5.76  ? 892  TYR A CB  1 
ATOM   7069 C  CG  . TYR A 1 892  ? 34.744 69.953  -21.370 1.00 4.83  ? 892  TYR A CG  1 
ATOM   7070 C  CD1 . TYR A 1 892  ? 34.735 71.336  -21.231 1.00 5.66  ? 892  TYR A CD1 1 
ATOM   7071 C  CD2 . TYR A 1 892  ? 34.126 69.180  -20.354 1.00 6.08  ? 892  TYR A CD2 1 
ATOM   7072 C  CE1 . TYR A 1 892  ? 34.125 71.926  -20.145 1.00 5.85  ? 892  TYR A CE1 1 
ATOM   7073 C  CE2 . TYR A 1 892  ? 33.548 69.751  -19.247 1.00 5.79  ? 892  TYR A CE2 1 
ATOM   7074 C  CZ  . TYR A 1 892  ? 33.536 71.124  -19.147 1.00 5.89  ? 892  TYR A CZ  1 
ATOM   7075 O  OH  . TYR A 1 892  ? 32.925 71.669  -18.033 1.00 7.55  ? 892  TYR A OH  1 
ATOM   7076 N  N   . ARG A 1 893  ? 37.042 67.331  -24.082 1.00 6.06  ? 893  ARG A N   1 
ATOM   7077 C  CA  . ARG A 1 893  ? 37.135 66.895  -25.516 1.00 6.27  ? 893  ARG A CA  1 
ATOM   7078 C  C   . ARG A 1 893  ? 35.775 66.269  -25.807 1.00 6.31  ? 893  ARG A C   1 
ATOM   7079 O  O   . ARG A 1 893  ? 35.154 65.630  -24.955 1.00 6.99  ? 893  ARG A O   1 
ATOM   7080 C  CB  . ARG A 1 893  ? 38.213 65.851  -25.726 1.00 6.54  ? 893  ARG A CB  1 
ATOM   7081 C  CG  . ARG A 1 893  ? 39.651 66.318  -25.577 1.00 7.82  ? 893  ARG A CG  1 
ATOM   7082 C  CD  . ARG A 1 893  ? 40.146 67.343  -26.677 1.00 7.89  ? 893  ARG A CD  1 
ATOM   7083 N  NE  . ARG A 1 893  ? 40.177 66.743  -28.010 1.00 8.46  ? 893  ARG A NE  1 
ATOM   7084 C  CZ  . ARG A 1 893  ? 41.113 65.922  -28.471 1.00 7.57  ? 893  ARG A CZ  1 
ATOM   7085 N  NH1 . ARG A 1 893  ? 42.143 65.525  -27.701 1.00 10.65 ? 893  ARG A NH1 1 
ATOM   7086 N  NH2 . ARG A 1 893  ? 41.078 65.509  -29.746 1.00 10.74 ? 893  ARG A NH2 1 
ATOM   7087 N  N   . LEU A 1 894  ? 35.290 66.471  -27.045 1.00 6.79  ? 894  LEU A N   1 
ATOM   7088 C  CA  . LEU A 1 894  ? 33.956 65.996  -27.476 1.00 8.41  ? 894  LEU A CA  1 
ATOM   7089 C  C   . LEU A 1 894  ? 34.152 65.043  -28.632 1.00 7.11  ? 894  LEU A C   1 
ATOM   7090 O  O   . LEU A 1 894  ? 34.620 65.451  -29.702 1.00 8.94  ? 894  LEU A O   1 
ATOM   7091 C  CB  . LEU A 1 894  ? 33.123 67.214  -27.876 1.00 8.59  ? 894  LEU A CB  1 
ATOM   7092 C  CG  . LEU A 1 894  ? 31.686 66.830  -28.283 1.00 9.70  ? 894  LEU A CG  1 
ATOM   7093 C  CD1 . LEU A 1 894  ? 30.933 66.252  -27.083 1.00 13.46 ? 894  LEU A CD1 1 
ATOM   7094 C  CD2 . LEU A 1 894  ? 30.982 68.082  -28.804 1.00 11.66 ? 894  LEU A CD2 1 
ATOM   7095 N  N   . VAL A 1 895  ? 33.853 63.749  -28.415 1.00 6.87  ? 895  VAL A N   1 
ATOM   7096 C  CA  . VAL A 1 895  ? 34.095 62.715  -29.403 1.00 7.80  ? 895  VAL A CA  1 
ATOM   7097 C  C   . VAL A 1 895  ? 32.802 62.066  -29.866 1.00 8.07  ? 895  VAL A C   1 
ATOM   7098 O  O   . VAL A 1 895  ? 32.117 61.351  -29.104 1.00 8.55  ? 895  VAL A O   1 
ATOM   7099 C  CB  . VAL A 1 895  ? 34.999 61.607  -28.759 1.00 8.65  ? 895  VAL A CB  1 
ATOM   7100 C  CG1 . VAL A 1 895  ? 35.372 60.620  -29.819 1.00 11.73 ? 895  VAL A CG1 1 
ATOM   7101 C  CG2 . VAL A 1 895  ? 36.238 62.219  -28.121 1.00 10.94 ? 895  VAL A CG2 1 
ATOM   7102 N  N   . LEU A 1 896  ? 32.412 62.344  -31.117 1.00 9.05  ? 896  LEU A N   1 
ATOM   7103 C  CA  . LEU A 1 896  ? 31.245 61.715  -31.763 1.00 8.93  ? 896  LEU A CA  1 
ATOM   7104 C  C   . LEU A 1 896  ? 31.810 60.574  -32.614 1.00 8.70  ? 896  LEU A C   1 
ATOM   7105 O  O   . LEU A 1 896  ? 32.754 60.773  -33.362 1.00 10.13 ? 896  LEU A O   1 
ATOM   7106 C  CB  . LEU A 1 896  ? 30.537 62.718  -32.679 1.00 9.97  ? 896  LEU A CB  1 
ATOM   7107 C  CG  . LEU A 1 896  ? 29.334 62.072  -33.438 1.00 10.70 ? 896  LEU A CG  1 
ATOM   7108 C  CD1 . LEU A 1 896  ? 28.192 61.854  -32.546 1.00 11.96 ? 896  LEU A CD1 1 
ATOM   7109 C  CD2 . LEU A 1 896  ? 28.954 63.026  -34.603 1.00 12.13 ? 896  LEU A CD2 1 
ATOM   7110 N  N   . GLU A 1 897  ? 31.255 59.363  -32.451 1.00 8.84  ? 897  GLU A N   1 
ATOM   7111 C  CA  . GLU A 1 897  ? 31.752 58.201  -33.187 1.00 9.67  ? 897  GLU A CA  1 
ATOM   7112 C  C   . GLU A 1 897  ? 30.662 57.253  -33.580 1.00 9.72  ? 897  GLU A C   1 
ATOM   7113 O  O   . GLU A 1 897  ? 29.617 57.176  -32.949 1.00 10.10 ? 897  GLU A O   1 
ATOM   7114 C  CB  . GLU A 1 897  ? 32.718 57.382  -32.293 1.00 15.04 ? 897  GLU A CB  1 
ATOM   7115 C  CG  . GLU A 1 897  ? 33.847 58.132  -31.615 1.00 17.12 ? 897  GLU A CG  1 
ATOM   7116 C  CD  . GLU A 1 897  ? 34.527 57.260  -30.472 1.00 12.47 ? 897  GLU A CD  1 
ATOM   7117 O  OE1 . GLU A 1 897  ? 33.895 57.067  -29.379 1.00 17.40 ? 897  GLU A OE1 1 
ATOM   7118 O  OE2 . GLU A 1 897  ? 35.687 56.911  -30.808 1.00 21.10 ? 897  GLU A OE2 1 
ATOM   7119 N  N   . LYS A 1 898  ? 30.935 56.529  -34.667 1.00 11.52 ? 898  LYS A N   1 
ATOM   7120 C  CA  . LYS A 1 898  ? 30.076 55.413  -35.070 1.00 11.33 ? 898  LYS A CA  1 
ATOM   7121 C  C   . LYS A 1 898  ? 30.518 54.201  -34.269 1.00 14.41 ? 898  LYS A C   1 
ATOM   7122 O  O   . LYS A 1 898  ? 31.710 53.888  -34.196 1.00 17.79 ? 898  LYS A O   1 
ATOM   7123 C  CB  . LYS A 1 898  ? 30.271 55.109  -36.533 1.00 15.46 ? 898  LYS A CB  1 
ATOM   7124 C  CG  . LYS A 1 898  ? 29.829 56.259  -37.423 1.00 19.16 ? 898  LYS A CG  1 
ATOM   7125 C  CD  . LYS A 1 898  ? 28.403 56.855  -37.143 1.00 25.56 ? 898  LYS A CD  1 
ATOM   7126 C  CE  . LYS A 1 898  ? 27.209 55.864  -36.854 1.00 30.71 ? 898  LYS A CE  1 
ATOM   7127 N  NZ  . LYS A 1 898  ? 27.043 54.620  -37.689 1.00 32.29 ? 898  LYS A NZ  1 
ATOM   7128 N  N   . VAL A 1 899  ? 29.571 53.520  -33.656 1.00 11.37 ? 899  VAL A N   1 
ATOM   7129 C  CA  . VAL A 1 899  ? 29.895 52.373  -32.839 1.00 12.11 ? 899  VAL A CA  1 
ATOM   7130 C  C   . VAL A 1 899  ? 29.178 51.067  -33.239 1.00 11.58 ? 899  VAL A C   1 
ATOM   7131 O  O   . VAL A 1 899  ? 29.218 50.077  -32.546 1.00 11.06 ? 899  VAL A O   1 
ATOM   7132 C  CB  . VAL A 1 899  ? 29.583 52.650  -31.324 1.00 12.01 ? 899  VAL A CB  1 
ATOM   7133 C  CG1 . VAL A 1 899  ? 30.584 53.675  -30.781 1.00 14.86 ? 899  VAL A CG1 1 
ATOM   7134 C  CG2 . VAL A 1 899  ? 28.178 53.175  -31.145 1.00 12.24 ? 899  VAL A CG2 1 
ATOM   7135 N  N   . ASN A 1 900  ? 28.560 51.078  -34.410 1.00 11.75 ? 900  ASN A N   1 
ATOM   7136 C  CA  . ASN A 1 900  ? 27.808 49.891  -34.850 1.00 13.20 ? 900  ASN A CA  1 
ATOM   7137 C  C   . ASN A 1 900  ? 28.749 48.674  -35.064 1.00 12.59 ? 900  ASN A C   1 
ATOM   7138 O  O   . ASN A 1 900  ? 28.281 47.538  -35.007 1.00 17.20 ? 900  ASN A O   1 
ATOM   7139 C  CB  . ASN A 1 900  ? 27.047 50.198  -36.177 1.00 14.53 ? 900  ASN A CB  1 
ATOM   7140 C  CG  . ASN A 1 900  ? 27.924 50.808  -37.226 1.00 17.96 ? 900  ASN A CG  1 
ATOM   7141 O  OD1 . ASN A 1 900  ? 28.512 51.878  -37.054 1.00 24.05 ? 900  ASN A OD1 1 
ATOM   7142 N  ND2 . ASN A 1 900  ? 28.036 50.106  -38.376 1.00 22.29 ? 900  ASN A ND2 1 
ATOM   7143 N  N   . ASN A 1 901  ? 30.027 48.910  -35.289 1.00 10.12 ? 901  ASN A N   1 
ATOM   7144 C  CA  . ASN A 1 901  ? 30.968 47.837  -35.505 1.00 12.01 ? 901  ASN A CA  1 
ATOM   7145 C  C   . ASN A 1 901  ? 31.708 47.421  -34.244 1.00 11.33 ? 901  ASN A C   1 
ATOM   7146 O  O   . ASN A 1 901  ? 32.460 46.477  -34.275 1.00 13.22 ? 901  ASN A O   1 
ATOM   7147 C  CB  . ASN A 1 901  ? 31.970 48.220  -36.588 1.00 15.62 ? 901  ASN A CB  1 
ATOM   7148 C  CG  . ASN A 1 901  ? 31.386 48.144  -37.965 1.00 22.55 ? 901  ASN A CG  1 
ATOM   7149 O  OD1 . ASN A 1 901  ? 30.707 47.197  -38.290 1.00 26.34 ? 901  ASN A OD1 1 
ATOM   7150 N  ND2 . ASN A 1 901  ? 31.640 49.154  -38.775 1.00 20.59 ? 901  ASN A ND2 1 
ATOM   7151 N  N   . CYS A 1 902  ? 31.495 48.124  -33.138 1.00 11.29 ? 902  CYS A N   1 
ATOM   7152 C  CA  . CYS A 1 902  ? 32.252 47.819  -31.917 1.00 11.90 ? 902  CYS A CA  1 
ATOM   7153 C  C   . CYS A 1 902  ? 31.708 46.629  -31.175 1.00 12.03 ? 902  CYS A C   1 
ATOM   7154 O  O   . CYS A 1 902  ? 30.493 46.448  -31.069 1.00 13.27 ? 902  CYS A O   1 
ATOM   7155 C  CB  . CYS A 1 902  ? 32.204 48.999  -30.935 1.00 12.39 ? 902  CYS A CB  1 
ATOM   7156 S  SG  . CYS A 1 902  ? 32.914 50.538  -31.554 1.00 14.99 ? 902  CYS A SG  1 
ATOM   7157 N  N   . VAL A 1 903  ? 32.612 45.839  -30.639 1.00 10.79 ? 903  VAL A N   1 
ATOM   7158 C  CA  . VAL A 1 903  ? 32.191 44.696  -29.784 1.00 10.83 ? 903  VAL A CA  1 
ATOM   7159 C  C   . VAL A 1 903  ? 31.921 45.251  -28.346 1.00 12.40 ? 903  VAL A C   1 
ATOM   7160 O  O   . VAL A 1 903  ? 32.839 45.557  -27.566 1.00 12.81 ? 903  VAL A O   1 
ATOM   7161 C  CB  . VAL A 1 903  ? 33.256 43.639  -29.787 1.00 10.04 ? 903  VAL A CB  1 
ATOM   7162 C  CG1 . VAL A 1 903  ? 32.818 42.487  -28.816 1.00 12.52 ? 903  VAL A CG1 1 
ATOM   7163 C  CG2 . VAL A 1 903  ? 33.420 43.120  -31.230 1.00 12.46 ? 903  VAL A CG2 1 
ATOM   7164 N  N   . ARG A 1 904  ? 30.667 45.462  -28.030 1.00 11.35 ? 904  ARG A N   1 
ATOM   7165 C  CA  . ARG A 1 904  ? 30.253 46.040  -26.761 1.00 11.09 ? 904  ARG A CA  1 
ATOM   7166 C  C   . ARG A 1 904  ? 29.694 44.982  -25.829 1.00 11.87 ? 904  ARG A C   1 
ATOM   7167 O  O   . ARG A 1 904  ? 29.350 43.850  -26.248 1.00 11.70 ? 904  ARG A O   1 
ATOM   7168 C  CB  . ARG A 1 904  ? 29.161 47.102  -27.012 1.00 11.63 ? 904  ARG A CB  1 
ATOM   7169 C  CG  . ARG A 1 904  ? 29.760 48.365  -27.676 1.00 13.09 ? 904  ARG A CG  1 
ATOM   7170 C  CD  . ARG A 1 904  ? 28.702 49.424  -27.948 1.00 16.67 ? 904  ARG A CD  1 
ATOM   7171 N  NE  . ARG A 1 904  ? 27.951 49.005  -29.114 1.00 15.36 ? 904  ARG A NE  1 
ATOM   7172 C  CZ  . ARG A 1 904  ? 27.007 49.753  -29.678 1.00 16.49 ? 904  ARG A CZ  1 
ATOM   7173 N  NH1 . ARG A 1 904  ? 26.697 50.933  -29.170 1.00 16.23 ? 904  ARG A NH1 1 
ATOM   7174 N  NH2 . ARG A 1 904  ? 26.395 49.301  -30.786 1.00 16.68 ? 904  ARG A NH2 1 
ATOM   7175 N  N   . PRO A 1 905  ? 29.636 45.271  -24.524 1.00 9.68  ? 905  PRO A N   1 
ATOM   7176 C  CA  . PRO A 1 905  ? 29.071 44.331  -23.560 1.00 10.08 ? 905  PRO A CA  1 
ATOM   7177 C  C   . PRO A 1 905  ? 27.591 44.109  -23.904 1.00 10.22 ? 905  PRO A C   1 
ATOM   7178 O  O   . PRO A 1 905  ? 26.960 44.957  -24.577 1.00 11.76 ? 905  PRO A O   1 
ATOM   7179 C  CB  . PRO A 1 905  ? 29.200 45.082  -22.219 1.00 10.76 ? 905  PRO A CB  1 
ATOM   7180 C  CG  . PRO A 1 905  ? 30.429 46.010  -22.441 1.00 9.58  ? 905  PRO A CG  1 
ATOM   7181 C  CD  . PRO A 1 905  ? 30.200 46.490  -23.882 1.00 9.20  ? 905  PRO A CD  1 
ATOM   7182 N  N   . SER A 1 906  ? 27.049 42.990  -23.413 1.00 11.53 ? 906  SER A N   1 
ATOM   7183 C  CA  . SER A 1 906  ? 25.632 42.736  -23.599 1.00 14.42 ? 906  SER A CA  1 
ATOM   7184 C  C   . SER A 1 906  ? 24.787 43.729  -22.800 1.00 13.96 ? 906  SER A C   1 
ATOM   7185 O  O   . SER A 1 906  ? 25.286 44.520  -21.971 1.00 14.83 ? 906  SER A O   1 
ATOM   7186 C  CB  . SER A 1 906  ? 25.331 41.323  -23.169 1.00 19.61 ? 906  SER A CB  1 
ATOM   7187 O  OG  . SER A 1 906  ? 25.023 41.324  -21.805 1.00 26.82 ? 906  SER A OG  1 
ATOM   7188 N  N   . LYS A 1 907  ? 23.493 43.721  -23.088 1.00 15.59 ? 907  LYS A N   1 
ATOM   7189 C  CA  . LYS A 1 907  ? 22.571 44.632  -22.422 1.00 17.89 ? 907  LYS A CA  1 
ATOM   7190 C  C   . LYS A 1 907  ? 22.537 44.497  -20.934 1.00 15.86 ? 907  LYS A C   1 
ATOM   7191 O  O   . LYS A 1 907  ? 22.174 45.433  -20.237 1.00 20.10 ? 907  LYS A O   1 
ATOM   7192 C  CB  . LYS A 1 907  ? 21.166 44.411  -22.971 1.00 24.18 ? 907  LYS A CB  1 
ATOM   7193 C  CG  . LYS A 1 907  ? 21.037 44.934  -24.359 1.00 31.10 ? 907  LYS A CG  1 
ATOM   7194 C  CD  . LYS A 1 907  ? 19.590 44.782  -24.809 1.00 37.32 ? 907  LYS A CD  1 
ATOM   7195 C  CE  . LYS A 1 907  ? 19.469 45.065  -26.291 1.00 36.43 ? 907  LYS A CE  1 
ATOM   7196 N  NZ  . LYS A 1 907  ? 18.085 44.759  -26.778 1.00 41.48 ? 907  LYS A NZ  1 
ATOM   7197 N  N   . LEU A 1 908  ? 22.854 43.340  -20.418 1.00 13.72 ? 908  LEU A N   1 
ATOM   7198 C  CA  . LEU A 1 908  ? 22.790 43.175  -18.968 1.00 15.70 ? 908  LEU A CA  1 
ATOM   7199 C  C   . LEU A 1 908  ? 24.109 43.467  -18.246 1.00 14.52 ? 908  LEU A C   1 
ATOM   7200 O  O   . LEU A 1 908  ? 24.190 43.407  -17.017 1.00 16.40 ? 908  LEU A O   1 
ATOM   7201 C  CB  . LEU A 1 908  ? 22.335 41.754  -18.602 1.00 18.87 ? 908  LEU A CB  1 
ATOM   7202 C  CG  . LEU A 1 908  ? 20.946 41.334  -19.130 1.00 22.29 ? 908  LEU A CG  1 
ATOM   7203 C  CD1 . LEU A 1 908  ? 20.661 39.882  -18.706 1.00 23.88 ? 908  LEU A CD1 1 
ATOM   7204 C  CD2 . LEU A 1 908  ? 19.855 42.278  -18.575 1.00 24.96 ? 908  LEU A CD2 1 
ATOM   7205 N  N   . HIS A 1 909  ? 25.161 43.777  -18.979 1.00 12.48 ? 909  HIS A N   1 
ATOM   7206 C  CA  . HIS A 1 909  ? 26.461 44.043  -18.345 1.00 11.66 ? 909  HIS A CA  1 
ATOM   7207 C  C   . HIS A 1 909  ? 26.423 45.449  -17.679 1.00 9.87  ? 909  HIS A C   1 
ATOM   7208 O  O   . HIS A 1 909  ? 25.945 46.393  -18.262 1.00 10.64 ? 909  HIS A O   1 
ATOM   7209 C  CB  . HIS A 1 909  ? 27.554 43.984  -19.399 1.00 10.26 ? 909  HIS A CB  1 
ATOM   7210 C  CG  . HIS A 1 909  ? 28.917 43.760  -18.835 1.00 10.15 ? 909  HIS A CG  1 
ATOM   7211 N  ND1 . HIS A 1 909  ? 29.613 44.735  -18.115 1.00 9.75  ? 909  HIS A ND1 1 
ATOM   7212 C  CD2 . HIS A 1 909  ? 29.719 42.675  -18.899 1.00 10.57 ? 909  HIS A CD2 1 
ATOM   7213 C  CE1 . HIS A 1 909  ? 30.785 44.231  -17.765 1.00 10.59 ? 909  HIS A CE1 1 
ATOM   7214 N  NE2 . HIS A 1 909  ? 30.877 42.973  -18.238 1.00 10.85 ? 909  HIS A NE2 1 
ATOM   7215 N  N   . PRO A 1 910  ? 26.953 45.579  -16.478 1.00 8.82  ? 910  PRO A N   1 
ATOM   7216 C  CA  . PRO A 1 910  ? 26.926 46.889  -15.792 1.00 9.14  ? 910  PRO A CA  1 
ATOM   7217 C  C   . PRO A 1 910  ? 28.003 47.870  -16.167 1.00 7.76  ? 910  PRO A C   1 
ATOM   7218 O  O   . PRO A 1 910  ? 27.967 49.006  -15.630 1.00 8.27  ? 910  PRO A O   1 
ATOM   7219 C  CB  . PRO A 1 910  ? 26.998 46.546  -14.294 1.00 11.81 ? 910  PRO A CB  1 
ATOM   7220 C  CG  . PRO A 1 910  ? 27.416 45.058  -14.234 1.00 12.09 ? 910  PRO A CG  1 
ATOM   7221 C  CD  . PRO A 1 910  ? 27.384 44.463  -15.592 1.00 10.65 ? 910  PRO A CD  1 
ATOM   7222 N  N   . ALA A 1 911  ? 28.971 47.465  -16.984 1.00 7.90  ? 911  ALA A N   1 
ATOM   7223 C  CA  . ALA A 1 911  ? 30.059 48.403  -17.388 1.00 8.41  ? 911  ALA A CA  1 
ATOM   7224 C  C   . ALA A 1 911  ? 29.946 48.873  -18.811 1.00 8.33  ? 911  ALA A C   1 
ATOM   7225 O  O   . ALA A 1 911  ? 29.206 48.300  -19.652 1.00 9.12  ? 911  ALA A O   1 
ATOM   7226 C  CB  . ALA A 1 911  ? 31.411 47.697  -17.246 1.00 9.79  ? 911  ALA A CB  1 
ATOM   7227 N  N   . GLY A 1 912  ? 30.695 49.948  -19.095 1.00 7.78  ? 912  GLY A N   1 
ATOM   7228 C  CA  . GLY A 1 912  ? 30.922 50.410  -20.447 1.00 9.19  ? 912  GLY A CA  1 
ATOM   7229 C  C   . GLY A 1 912  ? 32.408 50.662  -20.646 1.00 6.72  ? 912  GLY A C   1 
ATOM   7230 O  O   . GLY A 1 912  ? 33.139 50.729  -19.659 1.00 7.74  ? 912  GLY A O   1 
ATOM   7231 N  N   . TYR A 1 913  ? 32.858 50.829  -21.881 1.00 7.63  ? 913  TYR A N   1 
ATOM   7232 C  CA  . TYR A 1 913  ? 34.281 50.990  -22.185 1.00 8.06  ? 913  TYR A CA  1 
ATOM   7233 C  C   . TYR A 1 913  ? 34.460 52.034  -23.267 1.00 7.93  ? 913  TYR A C   1 
ATOM   7234 O  O   . TYR A 1 913  ? 33.659 52.134  -24.185 1.00 8.89  ? 913  TYR A O   1 
ATOM   7235 C  CB  . TYR A 1 913  ? 34.897 49.661  -22.624 1.00 8.40  ? 913  TYR A CB  1 
ATOM   7236 C  CG  . TYR A 1 913  ? 34.851 48.646  -21.502 1.00 7.18  ? 913  TYR A CG  1 
ATOM   7237 C  CD1 . TYR A 1 913  ? 35.738 48.723  -20.451 1.00 8.37  ? 913  TYR A CD1 1 
ATOM   7238 C  CD2 . TYR A 1 913  ? 33.885 47.648  -21.469 1.00 8.33  ? 913  TYR A CD2 1 
ATOM   7239 C  CE1 . TYR A 1 913  ? 35.684 47.840  -19.405 1.00 8.43  ? 913  TYR A CE1 1 
ATOM   7240 C  CE2 . TYR A 1 913  ? 33.828 46.745  -20.419 1.00 8.51  ? 913  TYR A CE2 1 
ATOM   7241 C  CZ  . TYR A 1 913  ? 34.731 46.858  -19.393 1.00 8.79  ? 913  TYR A CZ  1 
ATOM   7242 O  OH  . TYR A 1 913  ? 34.697 45.977  -18.361 1.00 9.76  ? 913  TYR A OH  1 
ATOM   7243 N  N   . LEU A 1 914  ? 35.532 52.803  -23.146 1.00 7.78  ? 914  LEU A N   1 
ATOM   7244 C  CA  . LEU A 1 914  ? 35.845 53.802  -24.157 1.00 7.98  ? 914  LEU A CA  1 
ATOM   7245 C  C   . LEU A 1 914  ? 36.457 53.179  -25.399 1.00 8.93  ? 914  LEU A C   1 
ATOM   7246 O  O   . LEU A 1 914  ? 36.969 52.047  -25.442 1.00 8.46  ? 914  LEU A O   1 
ATOM   7247 C  CB  . LEU A 1 914  ? 36.937 54.768  -23.607 1.00 7.89  ? 914  LEU A CB  1 
ATOM   7248 C  CG  . LEU A 1 914  ? 36.476 55.653  -22.432 1.00 7.86  ? 914  LEU A CG  1 
ATOM   7249 C  CD1 . LEU A 1 914  ? 37.580 56.675  -22.151 1.00 9.83  ? 914  LEU A CD1 1 
ATOM   7250 C  CD2 . LEU A 1 914  ? 35.141 56.378  -22.731 1.00 9.06  ? 914  LEU A CD2 1 
ATOM   7251 N  N   . THR A 1 915  ? 36.366 53.934  -26.496 1.00 8.74  ? 915  THR A N   1 
ATOM   7252 C  CA  . THR A 1 915  ? 37.104 53.645  -27.724 1.00 8.26  ? 915  THR A CA  1 
ATOM   7253 C  C   . THR A 1 915  ? 38.519 54.214  -27.591 1.00 8.31  ? 915  THR A C   1 
ATOM   7254 O  O   . THR A 1 915  ? 38.788 55.023  -26.700 1.00 9.45  ? 915  THR A O   1 
ATOM   7255 C  CB  . THR A 1 915  ? 36.456 54.366  -28.913 1.00 10.33 ? 915  THR A CB  1 
ATOM   7256 O  OG1 . THR A 1 915  ? 36.473 55.762  -28.629 1.00 12.19 ? 915  THR A OG1 1 
ATOM   7257 C  CG2 . THR A 1 915  ? 35.012 53.897  -29.144 1.00 11.51 ? 915  THR A CG2 1 
ATOM   7258 N  N   . SER A 1 916  ? 39.400 53.815  -28.509 1.00 9.05  ? 916  SER A N   1 
ATOM   7259 C  CA  . SER A 1 916  ? 40.724 54.357  -28.552 1.00 8.91  ? 916  SER A CA  1 
ATOM   7260 C  C   . SER A 1 916  ? 40.742 55.873  -28.647 1.00 9.10  ? 916  SER A C   1 
ATOM   7261 O  O   . SER A 1 916  ? 41.464 56.544  -27.887 1.00 9.15  ? 916  SER A O   1 
ATOM   7262 C  CB  . SER A 1 916  ? 41.443 53.813  -29.792 1.00 11.89 ? 916  SER A CB  1 
ATOM   7263 O  OG  . SER A 1 916  ? 42.660 54.502  -30.061 1.00 19.04 ? 916  SER A OG  1 
ATOM   7264 N  N   . ALA A 1 917  ? 39.929 56.450  -29.525 1.00 8.69  ? 917  ALA A N   1 
ATOM   7265 C  CA  . ALA A 1 917  ? 40.003 57.900  -29.676 1.00 8.58  ? 917  ALA A CA  1 
ATOM   7266 C  C   . ALA A 1 917  ? 39.555 58.593  -28.397 1.00 8.51  ? 917  ALA A C   1 
ATOM   7267 O  O   . ALA A 1 917  ? 40.079 59.680  -28.043 1.00 8.81  ? 917  ALA A O   1 
ATOM   7268 C  CB  . ALA A 1 917  ? 39.115 58.362  -30.848 1.00 10.85 ? 917  ALA A CB  1 
ATOM   7269 N  N   . ALA A 1 918  ? 38.540 58.058  -27.726 1.00 7.94  ? 918  ALA A N   1 
ATOM   7270 C  CA  . ALA A 1 918  ? 38.087 58.725  -26.483 1.00 7.95  ? 918  ALA A CA  1 
ATOM   7271 C  C   . ALA A 1 918  ? 39.117 58.598  -25.366 1.00 6.14  ? 918  ALA A C   1 
ATOM   7272 O  O   . ALA A 1 918  ? 39.289 59.545  -24.574 1.00 7.29  ? 918  ALA A O   1 
ATOM   7273 C  CB  . ALA A 1 918  ? 36.703 58.212  -26.043 1.00 8.74  ? 918  ALA A CB  1 
ATOM   7274 N  N   . HIS A 1 919  ? 39.777 57.451  -25.270 1.00 6.18  ? 919  HIS A N   1 
ATOM   7275 C  CA  . HIS A 1 919  ? 40.773 57.292  -24.234 1.00 6.35  ? 919  HIS A CA  1 
ATOM   7276 C  C   . HIS A 1 919  ? 41.929 58.247  -24.521 1.00 7.02  ? 919  HIS A C   1 
ATOM   7277 O  O   . HIS A 1 919  ? 42.458 58.903  -23.584 1.00 7.21  ? 919  HIS A O   1 
ATOM   7278 C  CB  . HIS A 1 919  ? 41.223 55.824  -24.247 1.00 7.90  ? 919  HIS A CB  1 
ATOM   7279 C  CG  . HIS A 1 919  ? 42.354 55.564  -23.295 1.00 9.55  ? 919  HIS A CG  1 
ATOM   7280 N  ND1 . HIS A 1 919  ? 43.594 55.171  -23.717 1.00 12.73 ? 919  HIS A ND1 1 
ATOM   7281 C  CD2 . HIS A 1 919  ? 42.412 55.666  -21.951 1.00 10.40 ? 919  HIS A CD2 1 
ATOM   7282 C  CE1 . HIS A 1 919  ? 44.394 55.024  -22.674 1.00 10.60 ? 919  HIS A CE1 1 
ATOM   7283 N  NE2 . HIS A 1 919  ? 43.719 55.324  -21.604 1.00 11.68 ? 919  HIS A NE2 1 
ATOM   7284 N  N   . LYS A 1 920  ? 42.403 58.307  -25.769 1.00 7.83  ? 920  LYS A N   1 
ATOM   7285 C  CA  . LYS A 1 920  ? 43.487 59.254  -26.082 1.00 7.87  ? 920  LYS A CA  1 
ATOM   7286 C  C   . LYS A 1 920  ? 43.046 60.683  -25.798 1.00 7.13  ? 920  LYS A C   1 
ATOM   7287 O  O   . LYS A 1 920  ? 43.858 61.487  -25.304 1.00 7.14  ? 920  LYS A O   1 
ATOM   7288 C  CB  . LYS A 1 920  ? 43.953 59.097  -27.542 1.00 11.52 ? 920  LYS A CB  1 
ATOM   7289 C  CG  . LYS A 1 920  ? 44.859 57.848  -27.654 1.00 13.28 ? 920  LYS A CG  1 
ATOM   7290 C  CD  . LYS A 1 920  ? 45.630 57.803  -28.956 1.00 15.42 ? 920  LYS A CD  1 
ATOM   7291 C  CE  . LYS A 1 920  ? 46.580 56.609  -28.998 1.00 14.09 ? 920  LYS A CE  1 
ATOM   7292 N  NZ  . LYS A 1 920  ? 47.733 56.673  -28.055 1.00 14.69 ? 920  LYS A NZ  1 
ATOM   7293 N  N   . ALA A 1 921  ? 41.787 61.019  -26.084 1.00 6.67  ? 921  ALA A N   1 
ATOM   7294 C  CA  . ALA A 1 921  ? 41.329 62.387  -25.789 1.00 6.75  ? 921  ALA A CA  1 
ATOM   7295 C  C   . ALA A 1 921  ? 41.353 62.659  -24.270 1.00 6.69  ? 921  ALA A C   1 
ATOM   7296 O  O   . ALA A 1 921  ? 41.717 63.745  -23.825 1.00 6.89  ? 921  ALA A O   1 
ATOM   7297 C  CB  . ALA A 1 921  ? 39.904 62.544  -26.379 1.00 7.56  ? 921  ALA A CB  1 
ATOM   7298 N  N   . SER A 1 922  ? 40.983 61.669  -23.454 1.00 6.53  ? 922  SER A N   1 
ATOM   7299 C  CA  . SER A 1 922  ? 41.048 61.843  -21.993 1.00 6.15  ? 922  SER A CA  1 
ATOM   7300 C  C   . SER A 1 922  ? 42.505 62.061  -21.568 1.00 7.30  ? 922  SER A C   1 
ATOM   7301 O  O   . SER A 1 922  ? 42.809 62.969  -20.787 1.00 7.90  ? 922  SER A O   1 
ATOM   7302 C  CB  . SER A 1 922  ? 40.473 60.619  -21.301 1.00 6.86  ? 922  SER A CB  1 
ATOM   7303 O  OG  . SER A 1 922  ? 40.628 60.753  -19.876 1.00 7.58  ? 922  SER A OG  1 
ATOM   7304 N  N   . GLN A 1 923  ? 43.429 61.275  -22.120 1.00 6.47  ? 923  GLN A N   1 
ATOM   7305 C  CA  . GLN A 1 923  ? 44.850 61.457  -21.788 1.00 6.34  ? 923  GLN A CA  1 
ATOM   7306 C  C   . GLN A 1 923  ? 45.336 62.841  -22.203 1.00 6.28  ? 923  GLN A C   1 
ATOM   7307 O  O   . GLN A 1 923  ? 46.229 63.405  -21.524 1.00 7.26  ? 923  GLN A O   1 
ATOM   7308 C  CB  . GLN A 1 923  ? 45.694 60.357  -22.458 1.00 6.87  ? 923  GLN A CB  1 
ATOM   7309 C  CG  . GLN A 1 923  ? 45.407 58.976  -21.885 1.00 6.71  ? 923  GLN A CG  1 
ATOM   7310 C  CD  . GLN A 1 923  ? 46.333 57.935  -22.481 1.00 8.14  ? 923  GLN A CD  1 
ATOM   7311 O  OE1 . GLN A 1 923  ? 46.477 57.862  -23.723 1.00 9.67  ? 923  GLN A OE1 1 
ATOM   7312 N  NE2 . GLN A 1 923  ? 46.960 57.096  -21.622 1.00 8.86  ? 923  GLN A NE2 1 
ATOM   7313 N  N   . SER A 1 924  ? 44.827 63.410  -23.303 1.00 6.42  ? 924  SER A N   1 
ATOM   7314 C  CA  . SER A 1 924  ? 45.267 64.728  -23.764 1.00 6.52  ? 924  SER A CA  1 
ATOM   7315 C  C   . SER A 1 924  ? 44.882 65.829  -22.777 1.00 6.72  ? 924  SER A C   1 
ATOM   7316 O  O   . SER A 1 924  ? 45.497 66.900  -22.745 1.00 9.59  ? 924  SER A O   1 
ATOM   7317 C  CB  . SER A 1 924  ? 44.652 65.051  -25.152 1.00 8.50  ? 924  SER A CB  1 
ATOM   7318 O  OG  . SER A 1 924  ? 43.260 65.481  -25.054 1.00 9.56  ? 924  SER A OG  1 
ATOM   7319 N  N   . LEU A 1 925  ? 43.824 65.568  -22.006 1.00 6.71  ? 925  LEU A N   1 
ATOM   7320 C  CA  . LEU A 1 925  ? 43.345 66.526  -21.002 1.00 7.50  ? 925  LEU A CA  1 
ATOM   7321 C  C   . LEU A 1 925  ? 44.067 66.342  -19.666 1.00 7.38  ? 925  LEU A C   1 
ATOM   7322 O  O   . LEU A 1 925  ? 44.460 67.318  -19.006 1.00 9.71  ? 925  LEU A O   1 
ATOM   7323 C  CB  . LEU A 1 925  ? 41.828 66.351  -20.705 1.00 7.25  ? 925  LEU A CB  1 
ATOM   7324 C  CG  . LEU A 1 925  ? 40.943 66.621  -21.935 1.00 6.74  ? 925  LEU A CG  1 
ATOM   7325 C  CD1 . LEU A 1 925  ? 39.522 66.241  -21.557 1.00 9.13  ? 925  LEU A CD1 1 
ATOM   7326 C  CD2 . LEU A 1 925  ? 40.978 68.114  -22.372 1.00 9.13  ? 925  LEU A CD2 1 
ATOM   7327 N  N   . LEU A 1 926  ? 44.232 65.092  -19.240 1.00 6.81  ? 926  LEU A N   1 
ATOM   7328 C  CA  . LEU A 1 926  ? 44.800 64.845  -17.912 1.00 6.74  ? 926  LEU A CA  1 
ATOM   7329 C  C   . LEU A 1 926  ? 46.295 64.804  -17.883 1.00 6.56  ? 926  LEU A C   1 
ATOM   7330 O  O   . LEU A 1 926  ? 46.863 65.213  -16.860 1.00 8.45  ? 926  LEU A O   1 
ATOM   7331 C  CB  . LEU A 1 926  ? 44.210 63.541  -17.356 1.00 9.22  ? 926  LEU A CB  1 
ATOM   7332 C  CG  . LEU A 1 926  ? 42.677 63.609  -17.103 1.00 9.93  ? 926  LEU A CG  1 
ATOM   7333 C  CD1 . LEU A 1 926  ? 42.195 62.214  -16.581 1.00 12.97 ? 926  LEU A CD1 1 
ATOM   7334 C  CD2 . LEU A 1 926  ? 42.382 64.745  -16.119 1.00 14.43 ? 926  LEU A CD2 1 
ATOM   7335 N  N   . ASP A 1 927  ? 46.935 64.332  -18.940 1.00 6.34  ? 927  ASP A N   1 
ATOM   7336 C  CA  . ASP A 1 927  ? 48.406 64.225  -18.948 1.00 7.08  ? 927  ASP A CA  1 
ATOM   7337 C  C   . ASP A 1 927  ? 48.966 64.758  -20.256 1.00 6.65  ? 927  ASP A C   1 
ATOM   7338 O  O   . ASP A 1 927  ? 49.520 64.026  -21.070 1.00 7.18  ? 927  ASP A O   1 
ATOM   7339 C  CB  . ASP A 1 927  ? 48.847 62.793  -18.700 1.00 7.86  ? 927  ASP A CB  1 
ATOM   7340 C  CG  . ASP A 1 927  ? 48.547 62.355  -17.250 1.00 8.59  ? 927  ASP A CG  1 
ATOM   7341 O  OD1 . ASP A 1 927  ? 49.251 62.758  -16.271 1.00 8.20  ? 927  ASP A OD1 1 
ATOM   7342 O  OD2 . ASP A 1 927  ? 47.530 61.662  -17.121 1.00 9.36  ? 927  ASP A OD2 1 
ATOM   7343 N  N   . PRO A 1 928  ? 48.783 66.057  -20.502 1.00 7.31  ? 928  PRO A N   1 
ATOM   7344 C  CA  . PRO A 1 928  ? 49.299 66.685  -21.738 1.00 6.70  ? 928  PRO A CA  1 
ATOM   7345 C  C   . PRO A 1 928  ? 50.809 66.687  -21.738 1.00 6.96  ? 928  PRO A C   1 
ATOM   7346 O  O   . PRO A 1 928  ? 51.454 66.409  -20.714 1.00 7.47  ? 928  PRO A O   1 
ATOM   7347 C  CB  . PRO A 1 928  ? 48.768 68.114  -21.623 1.00 8.96  ? 928  PRO A CB  1 
ATOM   7348 C  CG  . PRO A 1 928  ? 48.735 68.387  -20.152 1.00 10.77 ? 928  PRO A CG  1 
ATOM   7349 C  CD  . PRO A 1 928  ? 48.181 67.049  -19.580 1.00 8.65  ? 928  PRO A CD  1 
ATOM   7350 N  N   . LEU A 1 929  ? 51.430 67.040  -22.871 1.00 7.29  ? 929  LEU A N   1 
ATOM   7351 C  CA  . LEU A 1 929  ? 52.840 67.313  -22.833 1.00 5.98  ? 929  LEU A CA  1 
ATOM   7352 C  C   . LEU A 1 929  ? 53.147 68.468  -21.895 1.00 7.55  ? 929  LEU A C   1 
ATOM   7353 O  O   . LEU A 1 929  ? 52.368 69.403  -21.798 1.00 9.68  ? 929  LEU A O   1 
ATOM   7354 C  CB  . LEU A 1 929  ? 53.371 67.701  -24.243 1.00 7.79  ? 929  LEU A CB  1 
ATOM   7355 C  CG  . LEU A 1 929  ? 53.162 66.684  -25.369 1.00 6.95  ? 929  LEU A CG  1 
ATOM   7356 C  CD1 . LEU A 1 929  ? 53.768 67.288  -26.649 1.00 7.89  ? 929  LEU A CD1 1 
ATOM   7357 C  CD2 . LEU A 1 929  ? 53.875 65.364  -25.041 1.00 6.86  ? 929  LEU A CD2 1 
ATOM   7358 N  N   . ASP A 1 930  ? 54.279 68.391  -21.220 1.00 6.74  ? 930  ASP A N   1 
ATOM   7359 C  CA  . ASP A 1 930  ? 54.772 69.529  -20.389 1.00 6.92  ? 930  ASP A CA  1 
ATOM   7360 C  C   . ASP A 1 930  ? 55.685 70.372  -21.260 1.00 8.04  ? 930  ASP A C   1 
ATOM   7361 O  O   . ASP A 1 930  ? 56.428 69.812  -22.099 1.00 8.60  ? 930  ASP A O   1 
ATOM   7362 C  CB  . ASP A 1 930  ? 55.533 69.013  -19.172 1.00 7.03  ? 930  ASP A CB  1 
ATOM   7363 C  CG  . ASP A 1 930  ? 54.752 67.967  -18.457 1.00 8.85  ? 930  ASP A CG  1 
ATOM   7364 O  OD1 . ASP A 1 930  ? 53.667 68.374  -17.957 1.00 11.13 ? 930  ASP A OD1 1 
ATOM   7365 O  OD2 . ASP A 1 930  ? 55.101 66.767  -18.423 1.00 9.28  ? 930  ASP A OD2 1 
ATOM   7366 N  N   . LYS A 1 931  ? 55.674 71.679  -21.055 1.00 7.81  ? 931  LYS A N   1 
ATOM   7367 C  CA  . LYS A 1 931  ? 56.454 72.601  -21.879 1.00 7.32  ? 931  LYS A CA  1 
ATOM   7368 C  C   . LYS A 1 931  ? 57.412 73.399  -21.024 1.00 8.08  ? 931  LYS A C   1 
ATOM   7369 O  O   . LYS A 1 931  ? 57.009 74.011  -20.014 1.00 8.78  ? 931  LYS A O   1 
ATOM   7370 C  CB  . LYS A 1 931  ? 55.510 73.558  -22.619 1.00 9.83  ? 931  LYS A CB  1 
ATOM   7371 C  CG  . LYS A 1 931  ? 54.524 72.843  -23.567 1.00 9.36  ? 931  LYS A CG  1 
ATOM   7372 C  CD  . LYS A 1 931  ? 53.587 73.881  -24.257 1.00 15.74 ? 931  LYS A CD  1 
ATOM   7373 C  CE  . LYS A 1 931  ? 52.756 74.682  -23.263 1.00 20.39 ? 931  LYS A CE  1 
ATOM   7374 N  NZ  . LYS A 1 931  ? 51.983 75.680  -23.934 1.00 18.88 ? 931  LYS A NZ  1 
ATOM   7375 N  N   . PHE A 1 932  ? 58.670 73.459  -21.436 1.00 7.28  ? 932  PHE A N   1 
ATOM   7376 C  CA  . PHE A 1 932  ? 59.702 74.175  -20.683 1.00 6.95  ? 932  PHE A CA  1 
ATOM   7377 C  C   . PHE A 1 932  ? 60.371 75.201  -21.577 1.00 7.75  ? 932  PHE A C   1 
ATOM   7378 O  O   . PHE A 1 932  ? 60.723 74.878  -22.741 1.00 8.64  ? 932  PHE A O   1 
ATOM   7379 C  CB  . PHE A 1 932  ? 60.784 73.191  -20.235 1.00 6.86  ? 932  PHE A CB  1 
ATOM   7380 C  CG  . PHE A 1 932  ? 60.287 72.092  -19.324 1.00 7.77  ? 932  PHE A CG  1 
ATOM   7381 C  CD1 . PHE A 1 932  ? 59.700 70.936  -19.824 1.00 8.58  ? 932  PHE A CD1 1 
ATOM   7382 C  CD2 . PHE A 1 932  ? 60.438 72.230  -17.953 1.00 8.88  ? 932  PHE A CD2 1 
ATOM   7383 C  CE1 . PHE A 1 932  ? 59.247 69.869  -18.965 1.00 9.14  ? 932  PHE A CE1 1 
ATOM   7384 C  CE2 . PHE A 1 932  ? 60.007 71.197  -17.056 1.00 10.69 ? 932  PHE A CE2 1 
ATOM   7385 C  CZ  . PHE A 1 932  ? 59.411 70.028  -17.582 1.00 10.80 ? 932  PHE A CZ  1 
ATOM   7386 N  N   . ILE A 1 933  ? 60.587 76.395  -21.052 1.00 7.83  ? 933  ILE A N   1 
ATOM   7387 C  CA  . ILE A 1 933  ? 61.271 77.443  -21.825 1.00 7.58  ? 933  ILE A CA  1 
ATOM   7388 C  C   . ILE A 1 933  ? 62.634 77.677  -21.188 1.00 7.53  ? 933  ILE A C   1 
ATOM   7389 O  O   . ILE A 1 933  ? 62.692 77.955  -19.975 1.00 8.51  ? 933  ILE A O   1 
ATOM   7390 C  CB  . ILE A 1 933  ? 60.459 78.759  -21.767 1.00 7.86  ? 933  ILE A CB  1 
ATOM   7391 C  CG1 . ILE A 1 933  ? 59.072 78.553  -22.361 1.00 8.13  ? 933  ILE A CG1 1 
ATOM   7392 C  CG2 . ILE A 1 933  ? 61.231 79.879  -22.504 1.00 8.48  ? 933  ILE A CG2 1 
ATOM   7393 C  CD1 . ILE A 1 933  ? 58.123 79.745  -22.067 1.00 9.20  ? 933  ILE A CD1 1 
ATOM   7394 N  N   . PHE A 1 934  ? 63.745 77.570  -21.932 1.00 7.43  ? 934  PHE A N   1 
ATOM   7395 C  CA  . PHE A 1 934  ? 65.061 77.787  -21.318 1.00 8.97  ? 934  PHE A CA  1 
ATOM   7396 C  C   . PHE A 1 934  ? 65.144 79.268  -20.852 1.00 9.64  ? 934  PHE A C   1 
ATOM   7397 O  O   . PHE A 1 934  ? 64.812 80.183  -21.598 1.00 10.07 ? 934  PHE A O   1 
ATOM   7398 C  CB  . PHE A 1 934  ? 66.175 77.432  -22.313 1.00 9.72  ? 934  PHE A CB  1 
ATOM   7399 C  CG  . PHE A 1 934  ? 67.545 77.509  -21.682 1.00 9.26  ? 934  PHE A CG  1 
ATOM   7400 C  CD1 . PHE A 1 934  ? 67.941 76.553  -20.775 1.00 9.80  ? 934  PHE A CD1 1 
ATOM   7401 C  CD2 . PHE A 1 934  ? 68.378 78.580  -21.940 1.00 10.73 ? 934  PHE A CD2 1 
ATOM   7402 C  CE1 . PHE A 1 934  ? 69.185 76.668  -20.100 1.00 13.61 ? 934  PHE A CE1 1 
ATOM   7403 C  CE2 . PHE A 1 934  ? 69.604 78.716  -21.301 1.00 13.52 ? 934  PHE A CE2 1 
ATOM   7404 C  CZ  . PHE A 1 934  ? 70.020 77.782  -20.380 1.00 15.20 ? 934  PHE A CZ  1 
ATOM   7405 N  N   . ALA A 1 935  ? 65.580 79.477  -19.606 1.00 9.91  ? 935  ALA A N   1 
ATOM   7406 C  CA  . ALA A 1 935  ? 65.476 80.776  -18.994 1.00 11.38 ? 935  ALA A CA  1 
ATOM   7407 C  C   . ALA A 1 935  ? 66.577 81.749  -19.227 1.00 16.78 ? 935  ALA A C   1 
ATOM   7408 O  O   . ALA A 1 935  ? 66.340 82.943  -18.954 1.00 20.38 ? 935  ALA A O   1 
ATOM   7409 C  CB  . ALA A 1 935  ? 65.303 80.577  -17.501 1.00 15.00 ? 935  ALA A CB  1 
ATOM   7410 N  N   . GLU A 1 936  ? 67.728 81.315  -19.710 1.00 14.17 ? 936  GLU A N   1 
ATOM   7411 C  CA  . GLU A 1 936  ? 68.849 82.225  -19.956 1.00 16.81 ? 936  GLU A CA  1 
ATOM   7412 C  C   . GLU A 1 936  ? 69.097 82.325  -21.452 1.00 20.88 ? 936  GLU A C   1 
ATOM   7413 O  O   . GLU A 1 936  ? 68.363 81.763  -22.239 1.00 30.93 ? 936  GLU A O   1 
ATOM   7414 C  CB  A GLU A 1 936  ? 69.997 81.852  -19.023 0.50 22.03 ? 936  GLU A CB  1 
ATOM   7415 C  CB  B GLU A 1 936  ? 70.216 81.639  -19.431 0.50 19.75 ? 936  GLU A CB  1 
ATOM   7416 C  CG  A GLU A 1 936  ? 69.685 82.017  -17.543 0.50 27.82 ? 936  GLU A CG  1 
ATOM   7417 C  CG  B GLU A 1 936  ? 70.389 81.284  -17.939 0.50 30.39 ? 936  GLU A CG  1 
ATOM   7418 C  CD  A GLU A 1 936  ? 69.423 83.462  -17.149 0.50 36.43 ? 936  GLU A CD  1 
ATOM   7419 C  CD  B GLU A 1 936  ? 71.590 80.309  -17.680 0.50 36.89 ? 936  GLU A CD  1 
ATOM   7420 O  OE1 A GLU A 1 936  ? 68.669 83.688  -16.176 0.50 40.40 ? 936  GLU A OE1 1 
ATOM   7421 O  OE1 B GLU A 1 936  ? 71.389 79.078  -17.609 0.50 36.81 ? 936  GLU A OE1 1 
ATOM   7422 O  OE2 A GLU A 1 936  ? 69.951 84.367  -17.820 0.50 41.24 ? 936  GLU A OE2 1 
ATOM   7423 O  OE2 B GLU A 1 936  ? 72.749 80.774  -17.577 0.50 42.05 ? 936  GLU A OE2 1 
ATOM   7424 N  N   . ASN A 1 937  ? 70.113 83.080  -21.867 1.00 13.72 ? 937  ASN A N   1 
ATOM   7425 C  CA  . ASN A 1 937  ? 70.302 83.266  -23.292 1.00 12.89 ? 937  ASN A CA  1 
ATOM   7426 C  C   . ASN A 1 937  ? 70.829 82.120  -24.079 1.00 10.64 ? 937  ASN A C   1 
ATOM   7427 O  O   . ASN A 1 937  ? 70.412 81.918  -25.233 1.00 12.67 ? 937  ASN A O   1 
ATOM   7428 C  CB  . ASN A 1 937  ? 71.206 84.479  -23.515 1.00 14.30 ? 937  ASN A CB  1 
ATOM   7429 C  CG  . ASN A 1 937  ? 70.505 85.803  -23.189 1.00 17.98 ? 937  ASN A CG  1 
ATOM   7430 O  OD1 . ASN A 1 937  ? 69.277 85.888  -23.113 1.00 17.84 ? 937  ASN A OD1 1 
ATOM   7431 N  ND2 . ASN A 1 937  ? 71.302 86.843  -23.012 1.00 23.11 ? 937  ASN A ND2 1 
ATOM   7432 N  N   . GLU A 1 938  ? 71.719 81.349  -23.458 1.00 11.76 ? 938  GLU A N   1 
ATOM   7433 C  CA  . GLU A 1 938  ? 72.376 80.268  -24.142 1.00 13.18 ? 938  GLU A CA  1 
ATOM   7434 C  C   . GLU A 1 938  ? 72.477 79.026  -23.271 1.00 12.18 ? 938  GLU A C   1 
ATOM   7435 O  O   . GLU A 1 938  ? 72.920 79.086  -22.155 1.00 14.77 ? 938  GLU A O   1 
ATOM   7436 C  CB  . GLU A 1 938  ? 73.815 80.672  -24.563 1.00 18.18 ? 938  GLU A CB  1 
ATOM   7437 C  CG  . GLU A 1 938  ? 74.405 79.508  -25.385 1.00 22.86 ? 938  GLU A CG  1 
ATOM   7438 C  CD  . GLU A 1 938  ? 75.654 79.838  -26.193 1.00 33.71 ? 938  GLU A CD  1 
ATOM   7439 O  OE1 . GLU A 1 938  ? 76.340 80.834  -25.870 1.00 34.13 ? 938  GLU A OE1 1 
ATOM   7440 O  OE2 . GLU A 1 938  ? 75.947 79.066  -27.151 1.00 37.30 ? 938  GLU A OE2 1 
ATOM   7441 N  N   . TRP A 1 939  ? 72.033 77.910  -23.849 1.00 12.23 ? 939  TRP A N   1 
ATOM   7442 C  CA  . TRP A 1 939  ? 72.116 76.599  -23.130 1.00 11.47 ? 939  TRP A CA  1 
ATOM   7443 C  C   . TRP A 1 939  ? 73.304 75.842  -23.648 1.00 13.73 ? 939  TRP A C   1 
ATOM   7444 O  O   . TRP A 1 939  ? 73.268 75.266  -24.709 1.00 14.83 ? 939  TRP A O   1 
ATOM   7445 C  CB  . TRP A 1 939  ? 70.777 75.878  -23.373 1.00 10.84 ? 939  TRP A CB  1 
ATOM   7446 C  CG  . TRP A 1 939  ? 70.658 74.503  -22.755 1.00 9.02  ? 939  TRP A CG  1 
ATOM   7447 C  CD1 . TRP A 1 939  ? 71.535 73.844  -21.926 1.00 10.14 ? 939  TRP A CD1 1 
ATOM   7448 C  CD2 . TRP A 1 939  ? 69.577 73.617  -23.012 1.00 9.35  ? 939  TRP A CD2 1 
ATOM   7449 N  NE1 . TRP A 1 939  ? 71.043 72.577  -21.661 1.00 9.57  ? 939  TRP A NE1 1 
ATOM   7450 C  CE2 . TRP A 1 939  ? 69.844 72.417  -22.313 1.00 7.97  ? 939  TRP A CE2 1 
ATOM   7451 C  CE3 . TRP A 1 939  ? 68.417 73.712  -23.773 1.00 9.88  ? 939  TRP A CE3 1 
ATOM   7452 C  CZ2 . TRP A 1 939  ? 68.989 71.321  -22.359 1.00 9.56  ? 939  TRP A CZ2 1 
ATOM   7453 C  CZ3 . TRP A 1 939  ? 67.560 72.638  -23.822 1.00 9.38  ? 939  TRP A CZ3 1 
ATOM   7454 C  CH2 . TRP A 1 939  ? 67.852 71.431  -23.115 1.00 9.17  ? 939  TRP A CH2 1 
ATOM   7455 N  N   . ILE A 1 940  ? 74.389 75.875  -22.868 1.00 14.61 ? 940  ILE A N   1 
ATOM   7456 C  CA  . ILE A 1 940  ? 75.597 75.165  -23.324 1.00 17.02 ? 940  ILE A CA  1 
ATOM   7457 C  C   . ILE A 1 940  ? 75.477 73.622  -23.147 1.00 12.63 ? 940  ILE A C   1 
ATOM   7458 O  O   . ILE A 1 940  ? 75.052 73.173  -22.073 1.00 14.74 ? 940  ILE A O   1 
ATOM   7459 C  CB  . ILE A 1 940  ? 76.809 75.754  -22.582 1.00 20.58 ? 940  ILE A CB  1 
ATOM   7460 C  CG1 . ILE A 1 940  ? 76.868 77.268  -22.903 1.00 24.31 ? 940  ILE A CG1 1 
ATOM   7461 C  CG2 . ILE A 1 940  ? 78.092 75.115  -23.067 1.00 23.56 ? 940  ILE A CG2 1 
ATOM   7462 C  CD1 . ILE A 1 940  ? 77.886 78.035  -22.093 1.00 29.53 ? 940  ILE A CD1 1 
ATOM   7463 N  N   . GLY A 1 941  ? 75.795 72.870  -24.176 1.00 14.46 ? 941  GLY A N   1 
ATOM   7464 C  CA  . GLY A 1 941  ? 75.711 71.417  -24.040 1.00 12.74 ? 941  GLY A CA  1 
ATOM   7465 C  C   . GLY A 1 941  ? 74.333 70.810  -24.274 1.00 13.45 ? 941  GLY A C   1 
ATOM   7466 O  O   . GLY A 1 941  ? 74.131 69.601  -24.039 1.00 12.54 ? 941  GLY A O   1 
ATOM   7467 N  N   . ALA A 1 942  ? 73.388 71.584  -24.832 1.00 12.89 ? 942  ALA A N   1 
ATOM   7468 C  CA  . ALA A 1 942  ? 72.037 71.112  -25.063 1.00 11.93 ? 942  ALA A CA  1 
ATOM   7469 C  C   . ALA A 1 942  ? 71.953 69.938  -26.000 1.00 12.27 ? 942  ALA A C   1 
ATOM   7470 O  O   . ALA A 1 942  ? 72.673 69.850  -26.997 1.00 14.72 ? 942  ALA A O   1 
ATOM   7471 C  CB  . ALA A 1 942  ? 71.166 72.278  -25.621 1.00 13.56 ? 942  ALA A CB  1 
ATOM   7472 N  N   . GLN A 1 943  ? 71.097 68.972  -25.682 1.00 12.04 ? 943  GLN A N   1 
ATOM   7473 C  CA  . GLN A 1 943  ? 70.858 67.825  -26.490 1.00 12.84 ? 943  GLN A CA  1 
ATOM   7474 C  C   . GLN A 1 943  ? 69.427 67.798  -27.047 1.00 10.66 ? 943  GLN A C   1 
ATOM   7475 O  O   . GLN A 1 943  ? 68.496 68.405  -26.429 1.00 12.68 ? 943  GLN A O   1 
ATOM   7476 C  CB  . GLN A 1 943  ? 71.089 66.527  -25.695 1.00 13.19 ? 943  GLN A CB  1 
ATOM   7477 C  CG  . GLN A 1 943  ? 72.489 66.489  -25.131 1.00 17.85 ? 943  GLN A CG  1 
ATOM   7478 C  CD  . GLN A 1 943  ? 72.744 65.207  -24.319 1.00 23.06 ? 943  GLN A CD  1 
ATOM   7479 O  OE1 . GLN A 1 943  ? 71.828 64.718  -23.637 1.00 28.33 ? 943  GLN A OE1 1 
ATOM   7480 N  NE2 . GLN A 1 943  ? 73.988 64.682  -24.369 1.00 26.60 ? 943  GLN A NE2 1 
ATOM   7481 N  N   . GLY A 1 944  ? 69.179 67.063  -28.097 1.00 10.72 ? 944  GLY A N   1 
ATOM   7482 C  CA  . GLY A 1 944  ? 67.934 67.130  -28.784 1.00 9.96  ? 944  GLY A CA  1 
ATOM   7483 C  C   . GLY A 1 944  ? 66.795 66.266  -28.279 1.00 9.45  ? 944  GLY A C   1 
ATOM   7484 O  O   . GLY A 1 944  ? 65.621 66.551  -28.561 1.00 11.67 ? 944  GLY A O   1 
ATOM   7485 N  N   . GLN A 1 945  ? 67.114 65.170  -27.616 1.00 10.92 ? 945  GLN A N   1 
ATOM   7486 C  CA  . GLN A 1 945  ? 66.064 64.233  -27.216 1.00 10.36 ? 945  GLN A CA  1 
ATOM   7487 C  C   . GLN A 1 945  ? 66.554 63.344  -26.101 1.00 10.56 ? 945  GLN A C   1 
ATOM   7488 O  O   . GLN A 1 945  ? 67.770 63.151  -25.924 1.00 12.07 ? 945  GLN A O   1 
ATOM   7489 C  CB  . GLN A 1 945  ? 65.806 63.358  -28.417 1.00 11.18 ? 945  GLN A CB  1 
ATOM   7490 C  CG  . GLN A 1 945  ? 64.615 62.456  -28.383 1.00 15.76 ? 945  GLN A CG  1 
ATOM   7491 C  CD  . GLN A 1 945  ? 64.547 61.547  -29.617 1.00 19.68 ? 945  GLN A CD  1 
ATOM   7492 O  OE1 . GLN A 1 945  ? 63.759 61.764  -30.519 1.00 21.56 ? 945  GLN A OE1 1 
ATOM   7493 N  NE2 . GLN A 1 945  ? 65.383 60.550  -29.639 1.00 20.10 ? 945  GLN A NE2 1 
ATOM   7494 N  N   . PHE A 1 946  ? 65.591 62.891  -25.303 1.00 8.66  ? 946  PHE A N   1 
ATOM   7495 C  CA  . PHE A 1 946  ? 65.837 61.859  -24.258 1.00 8.16  ? 946  PHE A CA  1 
ATOM   7496 C  C   . PHE A 1 946  ? 64.722 60.839  -24.381 1.00 7.77  ? 946  PHE A C   1 
ATOM   7497 O  O   . PHE A 1 946  ? 63.580 61.166  -24.579 1.00 8.25  ? 946  PHE A O   1 
ATOM   7498 C  CB  . PHE A 1 946  ? 65.857 62.474  -22.847 1.00 9.17  ? 946  PHE A CB  1 
ATOM   7499 C  CG  . PHE A 1 946  ? 65.724 61.457  -21.737 1.00 9.23  ? 946  PHE A CG  1 
ATOM   7500 C  CD1 . PHE A 1 946  ? 66.765 60.616  -21.433 1.00 11.34 ? 946  PHE A CD1 1 
ATOM   7501 C  CD2 . PHE A 1 946  ? 64.488 61.337  -21.071 1.00 8.67  ? 946  PHE A CD2 1 
ATOM   7502 C  CE1 . PHE A 1 946  ? 66.585 59.587  -20.441 1.00 10.84 ? 946  PHE A CE1 1 
ATOM   7503 C  CE2 . PHE A 1 946  ? 64.314 60.316  -20.090 1.00 10.24 ? 946  PHE A CE2 1 
ATOM   7504 C  CZ  . PHE A 1 946  ? 65.349 59.456  -19.794 1.00 11.06 ? 946  PHE A CZ  1 
ATOM   7505 N  N   . GLY A 1 947  ? 65.069 59.542  -24.273 1.00 9.08  ? 947  GLY A N   1 
ATOM   7506 C  CA  . GLY A 1 947  ? 64.069 58.490  -24.307 1.00 9.77  ? 947  GLY A CA  1 
ATOM   7507 C  C   . GLY A 1 947  ? 63.760 57.902  -25.651 1.00 9.59  ? 947  GLY A C   1 
ATOM   7508 O  O   . GLY A 1 947  ? 62.836 57.139  -25.754 1.00 10.12 ? 947  GLY A O   1 
ATOM   7509 N  N   . GLY A 1 948  ? 64.509 58.240  -26.723 1.00 11.09 ? 948  GLY A N   1 
ATOM   7510 C  CA  . GLY A 1 948  ? 64.240 57.646  -28.014 1.00 11.57 ? 948  GLY A CA  1 
ATOM   7511 C  C   . GLY A 1 948  ? 64.331 56.134  -28.034 1.00 11.89 ? 948  GLY A C   1 
ATOM   7512 O  O   . GLY A 1 948  ? 63.697 55.530  -28.895 1.00 16.87 ? 948  GLY A O   1 
ATOM   7513 N  N   . ASP A 1 949  ? 65.072 55.540  -27.101 1.00 12.35 ? 949  ASP A N   1 
ATOM   7514 C  CA  . ASP A 1 949  ? 65.156 54.089  -27.018 1.00 16.10 ? 949  ASP A CA  1 
ATOM   7515 C  C   . ASP A 1 949  ? 64.147 53.473  -26.033 1.00 13.82 ? 949  ASP A C   1 
ATOM   7516 O  O   . ASP A 1 949  ? 64.152 52.251  -25.792 1.00 17.06 ? 949  ASP A O   1 
ATOM   7517 C  CB  . ASP A 1 949  ? 66.598 53.657  -26.637 1.00 15.73 ? 949  ASP A CB  1 
ATOM   7518 C  CG  . ASP A 1 949  ? 67.083 54.235  -25.316 1.00 22.81 ? 949  ASP A CG  1 
ATOM   7519 O  OD1 . ASP A 1 949  ? 66.502 55.186  -24.723 1.00 23.33 ? 949  ASP A OD1 1 
ATOM   7520 O  OD2 . ASP A 1 949  ? 68.136 53.738  -24.820 1.00 31.06 ? 949  ASP A OD2 1 
ATOM   7521 N  N   . HIS A 1 950  ? 63.271 54.277  -25.420 1.00 11.50 ? 950  HIS A N   1 
ATOM   7522 C  CA  . HIS A 1 950  ? 62.246 53.732  -24.510 1.00 10.11 ? 950  HIS A CA  1 
ATOM   7523 C  C   . HIS A 1 950  ? 61.189 52.979  -25.331 1.00 9.74  ? 950  HIS A C   1 
ATOM   7524 O  O   . HIS A 1 950  ? 60.813 53.452  -26.365 1.00 12.48 ? 950  HIS A O   1 
ATOM   7525 C  CB  . HIS A 1 950  ? 61.531 54.862  -23.742 1.00 10.34 ? 950  HIS A CB  1 
ATOM   7526 C  CG  . HIS A 1 950  ? 62.397 55.577  -22.758 1.00 9.27  ? 950  HIS A CG  1 
ATOM   7527 N  ND1 . HIS A 1 950  ? 62.013 56.743  -22.136 1.00 11.81 ? 950  HIS A ND1 1 
ATOM   7528 C  CD2 . HIS A 1 950  ? 63.629 55.291  -22.289 1.00 5.73  ? 950  HIS A CD2 1 
ATOM   7529 C  CE1 . HIS A 1 950  ? 62.970 57.141  -21.322 1.00 7.97  ? 950  HIS A CE1 1 
ATOM   7530 N  NE2 . HIS A 1 950  ? 63.967 56.279  -21.402 1.00 12.47 ? 950  HIS A NE2 1 
ATOM   7531 N  N   . PRO A 1 951  ? 60.716 51.820  -24.864 1.00 10.74 ? 951  PRO A N   1 
ATOM   7532 C  CA  . PRO A 1 951  ? 59.685 51.087  -25.590 1.00 10.92 ? 951  PRO A CA  1 
ATOM   7533 C  C   . PRO A 1 951  ? 58.405 51.891  -25.710 1.00 10.78 ? 951  PRO A C   1 
ATOM   7534 O  O   . PRO A 1 951  ? 58.000 52.575  -24.749 1.00 10.99 ? 951  PRO A O   1 
ATOM   7535 C  CB  . PRO A 1 951  ? 59.437 49.830  -24.732 1.00 14.14 ? 951  PRO A CB  1 
ATOM   7536 C  CG  . PRO A 1 951  ? 60.697 49.636  -24.035 1.00 16.52 ? 951  PRO A CG  1 
ATOM   7537 C  CD  . PRO A 1 951  ? 61.185 51.082  -23.688 1.00 14.42 ? 951  PRO A CD  1 
ATOM   7538 N  N   . SER A 1 952  ? 57.739 51.782  -26.842 1.00 10.26 ? 952  SER A N   1 
ATOM   7539 C  CA  . SER A 1 952  ? 56.480 52.457  -27.077 1.00 9.79  ? 952  SER A CA  1 
ATOM   7540 C  C   . SER A 1 952  ? 55.412 51.406  -26.881 1.00 10.08 ? 952  SER A C   1 
ATOM   7541 O  O   . SER A 1 952  ? 55.170 50.563  -27.766 1.00 11.51 ? 952  SER A O   1 
ATOM   7542 C  CB  . SER A 1 952  ? 56.453 53.043  -28.502 1.00 9.93  ? 952  SER A CB  1 
ATOM   7543 O  OG  . SER A 1 952  ? 55.415 54.009  -28.659 1.00 11.06 ? 952  SER A OG  1 
ATOM   7544 N  N   . ALA A 1 953  ? 54.761 51.448  -25.713 1.00 10.59 ? 953  ALA A N   1 
ATOM   7545 C  CA  . ALA A 1 953  ? 53.815 50.424  -25.309 1.00 8.90  ? 953  ALA A CA  1 
ATOM   7546 C  C   . ALA A 1 953  ? 52.446 50.543  -25.946 1.00 10.51 ? 953  ALA A C   1 
ATOM   7547 O  O   . ALA A 1 953  ? 52.027 51.629  -26.388 1.00 10.22 ? 953  ALA A O   1 
ATOM   7548 C  CB  . ALA A 1 953  ? 53.674 50.454  -23.784 1.00 11.68 ? 953  ALA A CB  1 
ATOM   7549 N  N   . ARG A 1 954  ? 51.710 49.436  -25.968 1.00 8.87  ? 954  ARG A N   1 
ATOM   7550 C  CA  . ARG A 1 954  ? 50.376 49.422  -26.526 1.00 9.86  ? 954  ARG A CA  1 
ATOM   7551 C  C   . ARG A 1 954  ? 49.563 50.565  -25.875 1.00 9.00  ? 954  ARG A C   1 
ATOM   7552 O  O   . ARG A 1 954  ? 49.697 50.847  -24.664 1.00 8.61  ? 954  ARG A O   1 
ATOM   7553 C  CB  . ARG A 1 954  ? 49.738 48.057  -26.309 1.00 12.32 ? 954  ARG A CB  1 
ATOM   7554 C  CG  . ARG A 1 954  ? 48.503 47.900  -27.260 1.00 15.83 ? 954  ARG A CG  1 
ATOM   7555 C  CD  . ARG A 1 954  ? 47.981 46.466  -27.399 1.00 20.49 ? 954  ARG A CD  1 
ATOM   7556 N  NE  . ARG A 1 954  ? 47.035 46.173  -26.349 1.00 20.59 ? 954  ARG A NE  1 
ATOM   7557 C  CZ  . ARG A 1 954  ? 46.418 45.016  -26.208 1.00 33.83 ? 954  ARG A CZ  1 
ATOM   7558 N  NH1 . ARG A 1 954  ? 46.668 44.016  -27.062 1.00 37.82 ? 954  ARG A NH1 1 
ATOM   7559 N  NH2 . ARG A 1 954  ? 45.516 44.879  -25.249 1.00 26.55 ? 954  ARG A NH2 1 
ATOM   7560 N  N   . GLU A 1 955  ? 48.627 51.127  -26.642 1.00 9.56  ? 955  GLU A N   1 
ATOM   7561 C  CA  . GLU A 1 955  ? 47.930 52.339  -26.230 1.00 9.33  ? 955  GLU A CA  1 
ATOM   7562 C  C   . GLU A 1 955  ? 47.114 52.199  -24.982 1.00 7.83  ? 955  GLU A C   1 
ATOM   7563 O  O   . GLU A 1 955  ? 46.774 53.232  -24.354 1.00 10.14 ? 955  GLU A O   1 
ATOM   7564 C  CB  . GLU A 1 955  ? 47.037 52.830  -27.393 1.00 13.20 ? 955  GLU A CB  1 
ATOM   7565 C  CG  . GLU A 1 955  ? 45.916 51.853  -27.764 1.00 13.27 ? 955  GLU A CG  1 
ATOM   7566 C  CD  . GLU A 1 955  ? 45.006 52.358  -28.838 1.00 19.51 ? 955  GLU A CD  1 
ATOM   7567 O  OE1 . GLU A 1 955  ? 44.739 53.577  -28.896 1.00 22.57 ? 955  GLU A OE1 1 
ATOM   7568 O  OE2 . GLU A 1 955  ? 44.503 51.521  -29.601 1.00 20.55 ? 955  GLU A OE2 1 
ATOM   7569 N  N   . ASP A 1 956  ? 46.673 50.992  -24.652 1.00 7.57  ? 956  ASP A N   1 
ATOM   7570 C  CA  . ASP A 1 956  ? 45.839 50.850  -23.432 1.00 9.39  ? 956  ASP A CA  1 
ATOM   7571 C  C   . ASP A 1 956  ? 46.676 50.732  -22.170 1.00 7.35  ? 956  ASP A C   1 
ATOM   7572 O  O   . ASP A 1 956  ? 46.079 50.653  -21.085 1.00 8.99  ? 956  ASP A O   1 
ATOM   7573 C  CB  . ASP A 1 956  ? 44.864 49.645  -23.555 1.00 10.27 ? 956  ASP A CB  1 
ATOM   7574 C  CG  . ASP A 1 956  ? 45.539 48.338  -23.935 1.00 10.78 ? 956  ASP A CG  1 
ATOM   7575 O  OD1 . ASP A 1 956  ? 46.749 48.243  -24.126 1.00 13.13 ? 956  ASP A OD1 1 
ATOM   7576 O  OD2 . ASP A 1 956  ? 44.776 47.340  -24.003 1.00 12.26 ? 956  ASP A OD2 1 
ATOM   7577 N  N   . LEU A 1 957  ? 47.996 50.723  -22.270 1.00 7.79  ? 957  LEU A N   1 
ATOM   7578 C  CA  . LEU A 1 957  ? 48.864 50.566  -21.075 1.00 8.51  ? 957  LEU A CA  1 
ATOM   7579 C  C   . LEU A 1 957  ? 49.418 51.923  -20.665 1.00 8.28  ? 957  LEU A C   1 
ATOM   7580 O  O   . LEU A 1 957  ? 49.837 52.723  -21.510 1.00 9.10  ? 957  LEU A O   1 
ATOM   7581 C  CB  . LEU A 1 957  ? 50.044 49.638  -21.436 1.00 9.32  ? 957  LEU A CB  1 
ATOM   7582 C  CG  . LEU A 1 957  ? 50.919 49.141  -20.286 1.00 13.70 ? 957  LEU A CG  1 
ATOM   7583 C  CD1 . LEU A 1 957  ? 50.064 48.265  -19.306 1.00 17.09 ? 957  LEU A CD1 1 
ATOM   7584 C  CD2 . LEU A 1 957  ? 52.040 48.241  -20.842 1.00 15.09 ? 957  LEU A CD2 1 
ATOM   7585 N  N   . ASP A 1 958  ? 49.432 52.169  -19.366 1.00 7.29  ? 958  ASP A N   1 
ATOM   7586 C  CA  . ASP A 1 958  ? 50.069 53.384  -18.840 1.00 7.04  ? 958  ASP A CA  1 
ATOM   7587 C  C   . ASP A 1 958  ? 50.990 53.057  -17.698 1.00 6.69  ? 958  ASP A C   1 
ATOM   7588 O  O   . ASP A 1 958  ? 50.755 52.096  -16.924 1.00 8.28  ? 958  ASP A O   1 
ATOM   7589 C  CB  . ASP A 1 958  ? 49.012 54.364  -18.343 1.00 7.22  ? 958  ASP A CB  1 
ATOM   7590 C  CG  . ASP A 1 958  ? 49.553 55.798  -18.150 1.00 8.23  ? 958  ASP A CG  1 
ATOM   7591 O  OD1 . ASP A 1 958  ? 50.654 56.109  -18.637 1.00 8.60  ? 958  ASP A OD1 1 
ATOM   7592 O  OD2 . ASP A 1 958  ? 48.827 56.583  -17.494 1.00 9.35  ? 958  ASP A OD2 1 
ATOM   7593 N  N   . VAL A 1 959  ? 52.052 53.843  -17.561 1.00 6.65  ? 959  VAL A N   1 
ATOM   7594 C  CA  . VAL A 1 959  ? 52.919 53.827  -16.367 1.00 6.24  ? 959  VAL A CA  1 
ATOM   7595 C  C   . VAL A 1 959  ? 52.367 54.961  -15.510 1.00 6.54  ? 959  VAL A C   1 
ATOM   7596 O  O   . VAL A 1 959  ? 52.781 56.125  -15.616 1.00 8.05  ? 959  VAL A O   1 
ATOM   7597 C  CB  . VAL A 1 959  ? 54.402 54.055  -16.728 1.00 6.43  ? 959  VAL A CB  1 
ATOM   7598 C  CG1 . VAL A 1 959  ? 55.255 54.154  -15.425 1.00 7.42  ? 959  VAL A CG1 1 
ATOM   7599 C  CG2 . VAL A 1 959  ? 54.936 52.861  -17.578 1.00 8.82  ? 959  VAL A CG2 1 
ATOM   7600 N  N   . SER A 1 960  ? 51.405 54.633  -14.663 1.00 7.11  ? 960  SER A N   1 
ATOM   7601 C  CA  . SER A 1 960  ? 50.712 55.596  -13.831 1.00 7.39  ? 960  SER A CA  1 
ATOM   7602 C  C   . SER A 1 960  ? 51.625 56.273  -12.866 1.00 7.62  ? 960  SER A C   1 
ATOM   7603 O  O   . SER A 1 960  ? 51.438 57.489  -12.584 1.00 8.46  ? 960  SER A O   1 
ATOM   7604 C  CB  . SER A 1 960  ? 49.598 54.921  -13.040 1.00 8.03  ? 960  SER A CB  1 
ATOM   7605 O  OG  . SER A 1 960  ? 48.771 54.112  -13.913 1.00 9.56  ? 960  SER A OG  1 
ATOM   7606 N  N   . VAL A 1 961  ? 52.597 55.534  -12.332 1.00 7.41  ? 961  VAL A N   1 
ATOM   7607 C  CA  . VAL A 1 961  ? 53.562 56.076  -11.380 1.00 6.74  ? 961  VAL A CA  1 
ATOM   7608 C  C   . VAL A 1 961  ? 54.944 55.498  -11.702 1.00 7.30  ? 961  VAL A C   1 
ATOM   7609 O  O   . VAL A 1 961  ? 55.089 54.284  -11.977 1.00 6.43  ? 961  VAL A O   1 
ATOM   7610 C  CB  . VAL A 1 961  ? 53.267 55.585  -9.923  1.00 7.37  ? 961  VAL A CB  1 
ATOM   7611 C  CG1 . VAL A 1 961  ? 54.419 56.037  -8.959  1.00 8.07  ? 961  VAL A CG1 1 
ATOM   7612 C  CG2 . VAL A 1 961  ? 51.941 56.145  -9.431  1.00 8.91  ? 961  VAL A CG2 1 
ATOM   7613 N  N   . MET A 1 962  ? 55.943 56.376  -11.710 1.00 6.35  ? 962  MET A N   1 
ATOM   7614 C  CA  . MET A 1 962  ? 57.340 55.991  -11.701 1.00 5.88  ? 962  MET A CA  1 
ATOM   7615 C  C   . MET A 1 962  ? 57.943 56.793  -10.544 1.00 6.67  ? 962  MET A C   1 
ATOM   7616 O  O   . MET A 1 962  ? 57.899 58.034  -10.556 1.00 7.83  ? 962  MET A O   1 
ATOM   7617 C  CB  . MET A 1 962  ? 58.082 56.292  -13.018 1.00 7.96  ? 962  MET A CB  1 
ATOM   7618 C  CG  . MET A 1 962  ? 59.583 55.936  -12.926 1.00 7.84  ? 962  MET A CG  1 
ATOM   7619 S  SD  . MET A 1 962  ? 60.291 56.237  -14.570 1.00 8.96  ? 962  MET A SD  1 
ATOM   7620 C  CE  . MET A 1 962  ? 62.070 55.776  -14.260 1.00 9.55  ? 962  MET A CE  1 
ATOM   7621 N  N   . ARG A 1 963  ? 58.497 56.107  -9.549  1.00 6.71  ? 963  ARG A N   1 
ATOM   7622 C  CA  . ARG A 1 963  ? 58.992 56.769  -8.355  1.00 6.17  ? 963  ARG A CA  1 
ATOM   7623 C  C   . ARG A 1 963  ? 60.262 56.101  -7.836  1.00 6.73  ? 963  ARG A C   1 
ATOM   7624 O  O   . ARG A 1 963  ? 60.216 54.925  -7.485  1.00 6.62  ? 963  ARG A O   1 
ATOM   7625 C  CB  . ARG A 1 963  ? 57.924 56.733  -7.241  1.00 7.17  ? 963  ARG A CB  1 
ATOM   7626 C  CG  . ARG A 1 963  ? 58.363 57.394  -5.895  1.00 8.03  ? 963  ARG A CG  1 
ATOM   7627 C  CD  . ARG A 1 963  ? 57.283 57.265  -4.778  1.00 9.35  ? 963  ARG A CD  1 
ATOM   7628 N  NE  . ARG A 1 963  ? 56.054 57.909  -5.224  1.00 8.94  ? 963  ARG A NE  1 
ATOM   7629 C  CZ  . ARG A 1 963  ? 54.838 57.387  -5.180  1.00 8.66  ? 963  ARG A CZ  1 
ATOM   7630 N  NH1 . ARG A 1 963  ? 54.610 56.212  -4.622  1.00 9.27  ? 963  ARG A NH1 1 
ATOM   7631 N  NH2 . ARG A 1 963  ? 53.836 58.088  -5.694  1.00 8.88  ? 963  ARG A NH2 1 
ATOM   7632 N  N   . ARG A 1 964  ? 61.369 56.857  -7.749  1.00 7.52  ? 964  ARG A N   1 
ATOM   7633 C  CA  . ARG A 1 964  ? 62.554 56.236  -7.083  1.00 8.05  ? 964  ARG A CA  1 
ATOM   7634 C  C   . ARG A 1 964  ? 62.252 56.209  -5.590  1.00 7.78  ? 964  ARG A C   1 
ATOM   7635 O  O   . ARG A 1 964  ? 61.841 57.175  -4.999  1.00 8.74  ? 964  ARG A O   1 
ATOM   7636 C  CB  . ARG A 1 964  ? 63.774 57.094  -7.408  1.00 7.76  ? 964  ARG A CB  1 
ATOM   7637 C  CG  . ARG A 1 964  ? 65.036 56.423  -6.793  1.00 8.76  ? 964  ARG A CG  1 
ATOM   7638 C  CD  . ARG A 1 964  ? 66.343 57.080  -7.283  1.00 8.78  ? 964  ARG A CD  1 
ATOM   7639 N  NE  . ARG A 1 964  ? 66.559 56.950  -8.701  1.00 9.02  ? 964  ARG A NE  1 
ATOM   7640 C  CZ  . ARG A 1 964  ? 67.419 56.156  -9.292  1.00 8.96  ? 964  ARG A CZ  1 
ATOM   7641 N  NH1 . ARG A 1 964  ? 68.192 55.362  -8.524  1.00 13.32 ? 964  ARG A NH1 1 
ATOM   7642 N  NH2 . ARG A 1 964  ? 67.521 56.102  -10.618 1.00 12.56 ? 964  ARG A NH2 1 
ATOM   7643 N  N   . LEU A 1 965  ? 62.504 55.049  -4.992  1.00 7.56  ? 965  LEU A N   1 
ATOM   7644 C  CA  . LEU A 1 965  ? 62.122 54.761  -3.603  1.00 7.08  ? 965  LEU A CA  1 
ATOM   7645 C  C   . LEU A 1 965  ? 63.289 54.891  -2.609  1.00 9.16  ? 965  LEU A C   1 
ATOM   7646 O  O   . LEU A 1 965  ? 63.058 54.849  -1.401  1.00 10.84 ? 965  LEU A O   1 
ATOM   7647 C  CB  . LEU A 1 965  ? 61.590 53.339  -3.514  1.00 9.16  ? 965  LEU A CB  1 
ATOM   7648 C  CG  . LEU A 1 965  ? 60.343 53.109  -4.390  1.00 7.99  ? 965  LEU A CG  1 
ATOM   7649 C  CD1 . LEU A 1 965  ? 59.960 51.603  -4.340  1.00 9.87  ? 965  LEU A CD1 1 
ATOM   7650 C  CD2 . LEU A 1 965  ? 59.158 53.997  -3.948  1.00 11.13 ? 965  LEU A CD2 1 
ATOM   7651 N  N   . THR A 1 966  ? 64.504 55.044  -3.145  1.00 9.16  ? 966  THR A N   1 
ATOM   7652 C  CA  . THR A 1 966  ? 65.728 55.150  -2.327  1.00 9.04  ? 966  THR A CA  1 
ATOM   7653 C  C   . THR A 1 966  ? 66.419 56.480  -2.509  1.00 9.18  ? 966  THR A C   1 
ATOM   7654 O  O   . THR A 1 966  ? 66.411 57.042  -3.612  1.00 10.33 ? 966  THR A O   1 
ATOM   7655 C  CB  . THR A 1 966  ? 66.746 54.071  -2.724  1.00 9.65  ? 966  THR A CB  1 
ATOM   7656 O  OG1 . THR A 1 966  ? 66.783 53.952  -4.130  1.00 9.95  ? 966  THR A OG1 1 
ATOM   7657 C  CG2 . THR A 1 966  ? 66.348 52.704  -2.113  1.00 11.94 ? 966  THR A CG2 1 
ATOM   7658 N  N   . LYS A 1 967  ? 67.066 56.961  -1.448  1.00 10.10 ? 967  LYS A N   1 
ATOM   7659 C  CA  . LYS A 1 967  ? 67.887 58.172  -1.491  1.00 10.23 ? 967  LYS A CA  1 
ATOM   7660 C  C   . LYS A 1 967  ? 69.276 57.727  -1.996  1.00 10.61 ? 967  LYS A C   1 
ATOM   7661 O  O   . LYS A 1 967  ? 69.564 56.524  -2.153  1.00 10.86 ? 967  LYS A O   1 
ATOM   7662 C  CB  . LYS A 1 967  ? 68.038 58.791  -0.102  1.00 12.60 ? 967  LYS A CB  1 
ATOM   7663 C  CG  . LYS A 1 967  ? 66.670 59.305  0.408   1.00 16.55 ? 967  LYS A CG  1 
ATOM   7664 C  CD  . LYS A 1 967  ? 66.828 60.208  1.633   1.00 21.24 ? 967  LYS A CD  1 
ATOM   7665 C  CE  . LYS A 1 967  ? 65.507 60.907  1.939   1.00 28.66 ? 967  LYS A CE  1 
ATOM   7666 N  NZ  . LYS A 1 967  ? 65.655 61.660  3.216   1.00 35.29 ? 967  LYS A NZ  1 
ATOM   7667 N  N   . SER A 1 968  ? 70.105 58.728  -2.320  1.00 11.51 ? 968  SER A N   1 
ATOM   7668 C  CA  . SER A 1 968  ? 71.404 58.429  -2.977  1.00 11.65 ? 968  SER A CA  1 
ATOM   7669 C  C   . SER A 1 968  ? 72.387 57.636  -2.128  1.00 12.10 ? 968  SER A C   1 
ATOM   7670 O  O   . SER A 1 968  ? 73.235 56.975  -2.727  1.00 16.30 ? 968  SER A O   1 
ATOM   7671 C  CB  . SER A 1 968  ? 72.105 59.731  -3.453  1.00 14.85 ? 968  SER A CB  1 
ATOM   7672 O  OG  . SER A 1 968  ? 72.426 60.545  -2.373  1.00 20.69 ? 968  SER A OG  1 
ATOM   7673 N  N   . SER A 1 969  ? 72.206 57.631  -0.818  1.00 12.93 ? 969  SER A N   1 
ATOM   7674 C  CA  . SER A 1 969  ? 73.146 56.842  0.020   1.00 13.66 ? 969  SER A CA  1 
ATOM   7675 C  C   . SER A 1 969  ? 72.921 55.330  0.009   1.00 14.53 ? 969  SER A C   1 
ATOM   7676 O  O   . SER A 1 969  ? 73.759 54.582  0.524   1.00 14.75 ? 969  SER A O   1 
ATOM   7677 C  CB  . SER A 1 969  ? 73.101 57.387  1.447   1.00 19.92 ? 969  SER A CB  1 
ATOM   7678 O  OG  . SER A 1 969  ? 71.774 57.290  1.932   1.00 29.17 ? 969  SER A OG  1 
ATOM   7679 N  N   . ALA A 1 970  ? 71.814 54.852  -0.553  1.00 11.85 ? 970  ALA A N   1 
ATOM   7680 C  CA  . ALA A 1 970  ? 71.531 53.444  -0.606  1.00 11.12 ? 970  ALA A CA  1 
ATOM   7681 C  C   . ALA A 1 970  ? 72.358 52.735  -1.645  1.00 12.81 ? 970  ALA A C   1 
ATOM   7682 O  O   . ALA A 1 970  ? 72.339 53.052  -2.846  1.00 14.71 ? 970  ALA A O   1 
ATOM   7683 C  CB  . ALA A 1 970  ? 70.026 53.193  -0.883  1.00 13.87 ? 970  ALA A CB  1 
ATOM   7684 N  N   . LYS A 1 971  ? 73.085 51.690  -1.204  1.00 13.60 ? 971  LYS A N   1 
ATOM   7685 C  CA  . LYS A 1 971  ? 73.886 50.905  -2.113  1.00 14.47 ? 971  LYS A CA  1 
ATOM   7686 C  C   . LYS A 1 971  ? 73.032 50.275  -3.202  1.00 14.12 ? 971  LYS A C   1 
ATOM   7687 O  O   . LYS A 1 971  ? 73.428 50.241  -4.366  1.00 16.19 ? 971  LYS A O   1 
ATOM   7688 C  CB  . LYS A 1 971  ? 74.619 49.797  -1.298  1.00 16.69 ? 971  LYS A CB  1 
ATOM   7689 C  CG  . LYS A 1 971  ? 75.489 48.884  -2.098  1.00 22.97 ? 971  LYS A CG  1 
ATOM   7690 C  CD  . LYS A 1 971  ? 76.433 48.088  -1.131  1.00 26.48 ? 971  LYS A CD  1 
ATOM   7691 C  CE  . LYS A 1 971  ? 77.237 47.057  -1.908  1.00 33.40 ? 971  LYS A CE  1 
ATOM   7692 N  NZ  . LYS A 1 971  ? 77.919 47.629  -3.113  1.00 39.04 ? 971  LYS A NZ  1 
ATOM   7693 N  N   . THR A 1 972  ? 71.865 49.752  -2.794  1.00 13.57 ? 972  THR A N   1 
ATOM   7694 C  CA  . THR A 1 972  ? 70.999 49.144  -3.788  1.00 13.06 ? 972  THR A CA  1 
ATOM   7695 C  C   . THR A 1 972  ? 69.841 50.152  -4.043  1.00 11.28 ? 972  THR A C   1 
ATOM   7696 O  O   . THR A 1 972  ? 69.049 50.413  -3.152  1.00 13.13 ? 972  THR A O   1 
ATOM   7697 C  CB  . THR A 1 972  ? 70.430 47.779  -3.328  1.00 17.58 ? 972  THR A CB  1 
ATOM   7698 O  OG1 . THR A 1 972  ? 71.531 46.865  -3.149  1.00 18.69 ? 972  THR A OG1 1 
ATOM   7699 C  CG2 . THR A 1 972  ? 69.501 47.151  -4.402  1.00 17.51 ? 972  THR A CG2 1 
ATOM   7700 N  N   . GLN A 1 973  ? 69.794 50.711  -5.233  1.00 10.98 ? 973  GLN A N   1 
ATOM   7701 C  CA  . GLN A 1 973  ? 68.735 51.652  -5.593  1.00 10.27 ? 973  GLN A CA  1 
ATOM   7702 C  C   . GLN A 1 973  ? 67.460 50.891  -5.953  1.00 10.94 ? 973  GLN A C   1 
ATOM   7703 O  O   . GLN A 1 973  ? 67.514 49.810  -6.509  1.00 11.81 ? 973  GLN A O   1 
ATOM   7704 C  CB  . GLN A 1 973  ? 69.189 52.534  -6.757  1.00 10.29 ? 973  GLN A CB  1 
ATOM   7705 C  CG  . GLN A 1 973  ? 70.263 53.543  -6.356  1.00 10.08 ? 973  GLN A CG  1 
ATOM   7706 C  CD  . GLN A 1 973  ? 69.759 54.598  -5.378  1.00 10.89 ? 973  GLN A CD  1 
ATOM   7707 O  OE1 . GLN A 1 973  ? 68.772 55.270  -5.635  1.00 12.30 ? 973  GLN A OE1 1 
ATOM   7708 N  NE2 . GLN A 1 973  ? 70.444 54.748  -4.264  1.00 8.11  ? 973  GLN A NE2 1 
ATOM   7709 N  N   . ARG A 1 974  ? 66.317 51.484  -5.610  1.00 10.25 ? 974  ARG A N   1 
ATOM   7710 C  CA  . ARG A 1 974  ? 65.046 50.864  -5.928  1.00 10.30 ? 974  ARG A CA  1 
ATOM   7711 C  C   . ARG A 1 974  ? 64.126 51.858  -6.606  1.00 7.79  ? 974  ARG A C   1 
ATOM   7712 O  O   . ARG A 1 974  ? 64.031 52.997  -6.136  1.00 9.03  ? 974  ARG A O   1 
ATOM   7713 C  CB  . ARG A 1 974  ? 64.356 50.349  -4.691  1.00 10.43 ? 974  ARG A CB  1 
ATOM   7714 C  CG  . ARG A 1 974  ? 65.211 49.258  -3.958  1.00 12.28 ? 974  ARG A CG  1 
ATOM   7715 C  CD  . ARG A 1 974  ? 64.661 49.007  -2.552  1.00 15.50 ? 974  ARG A CD  1 
ATOM   7716 N  NE  . ARG A 1 974  ? 63.469 48.180  -2.614  1.00 21.60 ? 974  ARG A NE  1 
ATOM   7717 C  CZ  . ARG A 1 974  ? 62.274 48.507  -2.128  1.00 18.72 ? 974  ARG A CZ  1 
ATOM   7718 N  NH1 . ARG A 1 974  ? 62.056 49.650  -1.517  1.00 19.52 ? 974  ARG A NH1 1 
ATOM   7719 N  NH2 . ARG A 1 974  ? 61.283 47.640  -2.274  1.00 16.90 ? 974  ARG A NH2 1 
ATOM   7720 N  N   . VAL A 1 975  ? 63.471 51.404  -7.660  1.00 9.34  ? 975  VAL A N   1 
ATOM   7721 C  CA  . VAL A 1 975  ? 62.511 52.272  -8.389  1.00 8.06  ? 975  VAL A CA  1 
ATOM   7722 C  C   . VAL A 1 975  ? 61.203 51.518  -8.503  1.00 9.33  ? 975  VAL A C   1 
ATOM   7723 O  O   . VAL A 1 975  ? 61.158 50.341  -8.946  1.00 8.92  ? 975  VAL A O   1 
ATOM   7724 C  CB  . VAL A 1 975  ? 63.014 52.627  -9.814  1.00 9.56  ? 975  VAL A CB  1 
ATOM   7725 C  CG1 . VAL A 1 975  ? 62.031 53.609  -10.522 1.00 9.07  ? 975  VAL A CG1 1 
ATOM   7726 C  CG2 . VAL A 1 975  ? 64.376 53.390  -9.693  1.00 12.90 ? 975  VAL A CG2 1 
ATOM   7727 N  N   . GLY A 1 976  ? 60.128 52.208  -8.115  1.00 8.44  ? 976  GLY A N   1 
ATOM   7728 C  CA  . GLY A 1 976  ? 58.786 51.620  -8.168  1.00 7.44  ? 976  GLY A CA  1 
ATOM   7729 C  C   . GLY A 1 976  ? 57.963 52.100  -9.358  1.00 6.80  ? 976  GLY A C   1 
ATOM   7730 O  O   . GLY A 1 976  ? 58.030 53.297  -9.749  1.00 7.59  ? 976  GLY A O   1 
ATOM   7731 N  N   . TYR A 1 977  ? 57.192 51.202  -9.928  1.00 6.74  ? 977  TYR A N   1 
ATOM   7732 C  CA  . TYR A 1 977  ? 56.319 51.516  -11.049 1.00 5.60  ? 977  TYR A CA  1 
ATOM   7733 C  C   . TYR A 1 977  ? 54.922 50.972  -10.773 1.00 6.21  ? 977  TYR A C   1 
ATOM   7734 O  O   . TYR A 1 977  ? 54.769 49.832  -10.272 1.00 7.29  ? 977  TYR A O   1 
ATOM   7735 C  CB  . TYR A 1 977  ? 56.793 50.815  -12.338 1.00 7.98  ? 977  TYR A CB  1 
ATOM   7736 C  CG  . TYR A 1 977  ? 58.175 51.155  -12.747 1.00 6.84  ? 977  TYR A CG  1 
ATOM   7737 C  CD1 . TYR A 1 977  ? 59.259 50.450  -12.246 1.00 8.70  ? 977  TYR A CD1 1 
ATOM   7738 C  CD2 . TYR A 1 977  ? 58.408 52.221  -13.625 1.00 9.39  ? 977  TYR A CD2 1 
ATOM   7739 C  CE1 . TYR A 1 977  ? 60.574 50.821  -12.655 1.00 9.38  ? 977  TYR A CE1 1 
ATOM   7740 C  CE2 . TYR A 1 977  ? 59.671 52.573  -14.008 1.00 9.03  ? 977  TYR A CE2 1 
ATOM   7741 C  CZ  . TYR A 1 977  ? 60.745 51.870  -13.530 1.00 7.94  ? 977  TYR A CZ  1 
ATOM   7742 O  OH  . TYR A 1 977  ? 62.035 52.252  -13.944 1.00 10.65 ? 977  TYR A OH  1 
ATOM   7743 N  N   . VAL A 1 978  ? 53.901 51.785  -11.071 1.00 6.04  ? 978  VAL A N   1 
ATOM   7744 C  CA  . VAL A 1 978  ? 52.529 51.288  -11.067 1.00 5.82  ? 978  VAL A CA  1 
ATOM   7745 C  C   . VAL A 1 978  ? 52.107 51.235  -12.563 1.00 6.32  ? 978  VAL A C   1 
ATOM   7746 O  O   . VAL A 1 978  ? 52.176 52.269  -13.278 1.00 7.32  ? 978  VAL A O   1 
ATOM   7747 C  CB  . VAL A 1 978  ? 51.546 52.185  -10.248 1.00 7.27  ? 978  VAL A CB  1 
ATOM   7748 C  CG1 . VAL A 1 978  ? 50.097 51.693  -10.431 1.00 8.39  ? 978  VAL A CG1 1 
ATOM   7749 C  CG2 . VAL A 1 978  ? 51.938 52.189  -8.793  1.00 7.85  ? 978  VAL A CG2 1 
ATOM   7750 N  N   . LEU A 1 979  ? 51.697 50.055  -13.006 1.00 7.15  ? 979  LEU A N   1 
ATOM   7751 C  CA  . LEU A 1 979  ? 51.291 49.825  -14.390 1.00 8.11  ? 979  LEU A CA  1 
ATOM   7752 C  C   . LEU A 1 979  ? 49.799 49.582  -14.429 1.00 8.61  ? 979  LEU A C   1 
ATOM   7753 O  O   . LEU A 1 979  ? 49.279 48.716  -13.707 1.00 11.30 ? 979  LEU A O   1 
ATOM   7754 C  CB  . LEU A 1 979  ? 52.036 48.590  -14.920 1.00 12.84 ? 979  LEU A CB  1 
ATOM   7755 C  CG  A LEU A 1 979  ? 52.076 48.301  -16.416 0.50 16.01 ? 979  LEU A CG  1 
ATOM   7756 C  CG  B LEU A 1 979  ? 53.324 48.910  -15.801 0.50 29.44 ? 979  LEU A CG  1 
ATOM   7757 C  CD1 A LEU A 1 979  ? 52.916 49.435  -17.014 0.50 20.85 ? 979  LEU A CD1 1 
ATOM   7758 C  CD1 B LEU A 1 979  ? 52.995 49.024  -17.269 0.50 27.64 ? 979  LEU A CD1 1 
ATOM   7759 C  CD2 A LEU A 1 979  ? 52.710 46.931  -16.754 0.50 19.45 ? 979  LEU A CD2 1 
ATOM   7760 C  CD2 B LEU A 1 979  ? 54.044 50.138  -15.303 0.50 27.74 ? 979  LEU A CD2 1 
ATOM   7761 N  N   . HIS A 1 980  ? 49.068 50.341  -15.236 1.00 8.18  ? 980  HIS A N   1 
ATOM   7762 C  CA  . HIS A 1 980  ? 47.625 50.156  -15.375 1.00 8.79  ? 980  HIS A CA  1 
ATOM   7763 C  C   . HIS A 1 980  ? 47.261 49.898  -16.822 1.00 8.78  ? 980  HIS A C   1 
ATOM   7764 O  O   . HIS A 1 980  ? 47.728 50.594  -17.705 1.00 10.69 ? 980  HIS A O   1 
ATOM   7765 C  CB  . HIS A 1 980  ? 46.866 51.407  -14.913 1.00 8.71  ? 980  HIS A CB  1 
ATOM   7766 C  CG  . HIS A 1 980  ? 45.390 51.287  -15.097 1.00 9.32  ? 980  HIS A CG  1 
ATOM   7767 N  ND1 . HIS A 1 980  ? 44.628 50.414  -14.359 1.00 12.80 ? 980  HIS A ND1 1 
ATOM   7768 C  CD2 . HIS A 1 980  ? 44.558 51.852  -15.996 1.00 6.04  ? 980  HIS A CD2 1 
ATOM   7769 C  CE1 . HIS A 1 980  ? 43.374 50.487  -14.763 1.00 7.34  ? 980  HIS A CE1 1 
ATOM   7770 N  NE2 . HIS A 1 980  ? 43.309 51.341  -15.766 1.00 13.88 ? 980  HIS A NE2 1 
ATOM   7771 N  N   . ARG A 1 981  ? 46.428 48.893  -17.060 1.00 6.93  ? 981  ARG A N   1 
ATOM   7772 C  CA  . ARG A 1 981  ? 45.926 48.685  -18.415 1.00 7.93  ? 981  ARG A CA  1 
ATOM   7773 C  C   . ARG A 1 981  ? 44.438 48.904  -18.392 1.00 6.32  ? 981  ARG A C   1 
ATOM   7774 O  O   . ARG A 1 981  ? 43.735 48.284  -17.592 1.00 8.56  ? 981  ARG A O   1 
ATOM   7775 C  CB  A ARG A 1 981  ? 46.197 47.268  -18.891 0.50 8.89  ? 981  ARG A CB  1 
ATOM   7776 C  CB  B ARG A 1 981  ? 46.290 47.357  -19.062 0.50 9.11  ? 981  ARG A CB  1 
ATOM   7777 C  CG  A ARG A 1 981  ? 45.843 47.092  -20.367 0.50 12.92 ? 981  ARG A CG  1 
ATOM   7778 C  CG  B ARG A 1 981  ? 46.090 47.372  -20.619 0.50 13.02 ? 981  ARG A CG  1 
ATOM   7779 C  CD  A ARG A 1 981  ? 46.269 45.715  -20.882 0.50 22.77 ? 981  ARG A CD  1 
ATOM   7780 C  CD  B ARG A 1 981  ? 46.059 45.967  -21.282 0.50 24.71 ? 981  ARG A CD  1 
ATOM   7781 N  NE  A ARG A 1 981  ? 46.869 45.899  -22.175 0.50 35.02 ? 981  ARG A NE  1 
ATOM   7782 N  NE  B ARG A 1 981  ? 47.288 45.219  -21.063 0.50 28.35 ? 981  ARG A NE  1 
ATOM   7783 C  CZ  A ARG A 1 981  ? 48.118 45.563  -22.480 0.50 26.33 ? 981  ARG A CZ  1 
ATOM   7784 C  CZ  B ARG A 1 981  ? 48.346 45.261  -21.872 0.50 25.75 ? 981  ARG A CZ  1 
ATOM   7785 N  NH1 A ARG A 1 981  ? 48.924 44.989  -21.583 0.50 27.33 ? 981  ARG A NH1 1 
ATOM   7786 N  NH1 B ARG A 1 981  ? 48.334 46.030  -22.969 0.50 28.53 ? 981  ARG A NH1 1 
ATOM   7787 N  NH2 A ARG A 1 981  ? 48.573 45.856  -23.676 0.50 24.09 ? 981  ARG A NH2 1 
ATOM   7788 N  NH2 B ARG A 1 981  ? 49.413 44.501  -21.607 0.50 25.05 ? 981  ARG A NH2 1 
ATOM   7789 N  N   . THR A 1 982  ? 43.965 49.830  -19.216 1.00 7.54  ? 982  THR A N   1 
ATOM   7790 C  CA  . THR A 1 982  ? 42.498 50.009  -19.301 1.00 7.08  ? 982  THR A CA  1 
ATOM   7791 C  C   . THR A 1 982  ? 41.971 48.955  -20.326 1.00 8.65  ? 982  THR A C   1 
ATOM   7792 O  O   . THR A 1 982  ? 42.705 48.035  -20.699 1.00 11.44 ? 982  THR A O   1 
ATOM   7793 C  CB  . THR A 1 982  ? 42.189 51.477  -19.749 1.00 8.04  ? 982  THR A CB  1 
ATOM   7794 O  OG1 . THR A 1 982  ? 40.780 51.731  -19.579 1.00 8.71  ? 982  THR A OG1 1 
ATOM   7795 C  CG2 . THR A 1 982  ? 42.659 51.776  -21.213 1.00 9.55  ? 982  THR A CG2 1 
ATOM   7796 N  N   . ASN A 1 983  ? 40.696 49.056  -20.665 1.00 7.72  ? 983  ASN A N   1 
ATOM   7797 C  CA  . ASN A 1 983  ? 40.155 48.159  -21.704 1.00 6.99  ? 983  ASN A CA  1 
ATOM   7798 C  C   . ASN A 1 983  ? 39.430 49.054  -22.725 1.00 7.92  ? 983  ASN A C   1 
ATOM   7799 O  O   . ASN A 1 983  ? 38.547 49.812  -22.346 1.00 9.60  ? 983  ASN A O   1 
ATOM   7800 C  CB  . ASN A 1 983  ? 39.160 47.138  -21.106 1.00 7.74  ? 983  ASN A CB  1 
ATOM   7801 C  CG  . ASN A 1 983  ? 38.676 46.171  -22.151 1.00 7.72  ? 983  ASN A CG  1 
ATOM   7802 O  OD1 . ASN A 1 983  ? 39.408 45.270  -22.546 1.00 10.98 ? 983  ASN A OD1 1 
ATOM   7803 N  ND2 . ASN A 1 983  ? 37.479 46.416  -22.656 1.00 9.69  ? 983  ASN A ND2 1 
ATOM   7804 N  N   . LEU A 1 984  ? 39.864 48.915  -23.965 1.00 8.26  ? 984  LEU A N   1 
ATOM   7805 C  CA  . LEU A 1 984  ? 39.309 49.710  -25.087 1.00 8.27  ? 984  LEU A CA  1 
ATOM   7806 C  C   . LEU A 1 984  ? 38.511 48.845  -25.991 1.00 11.06 ? 984  LEU A C   1 
ATOM   7807 O  O   . LEU A 1 984  ? 38.822 47.673  -26.186 1.00 11.87 ? 984  LEU A O   1 
ATOM   7808 C  CB  . LEU A 1 984  ? 40.457 50.359  -25.853 1.00 9.88  ? 984  LEU A CB  1 
ATOM   7809 C  CG  . LEU A 1 984  ? 41.357 51.256  -24.985 1.00 10.87 ? 984  LEU A CG  1 
ATOM   7810 C  CD1 . LEU A 1 984  ? 42.544 51.725  -25.905 1.00 12.50 ? 984  LEU A CD1 1 
ATOM   7811 C  CD2 . LEU A 1 984  ? 40.577 52.410  -24.357 1.00 10.74 ? 984  LEU A CD2 1 
ATOM   7812 N  N   . MET A 1 985  ? 37.455 49.380  -26.561 1.00 10.76 ? 985  MET A N   1 
ATOM   7813 C  CA  . MET A 1 985  ? 36.627 48.572  -27.439 1.00 13.97 ? 985  MET A CA  1 
ATOM   7814 C  C   . MET A 1 985  ? 37.313 48.194  -28.720 1.00 16.85 ? 985  MET A C   1 
ATOM   7815 O  O   . MET A 1 985  ? 38.065 48.955  -29.271 1.00 17.10 ? 985  MET A O   1 
ATOM   7816 C  CB  . MET A 1 985  ? 35.342 49.299  -27.730 1.00 16.71 ? 985  MET A CB  1 
ATOM   7817 C  CG  . MET A 1 985  ? 34.481 49.412  -26.529 1.00 17.89 ? 985  MET A CG  1 
ATOM   7818 S  SD  . MET A 1 985  ? 32.751 49.477  -27.011 1.00 20.41 ? 985  MET A SD  1 
ATOM   7819 C  CE  . MET A 1 985  ? 32.769 51.086  -27.797 1.00 19.92 ? 985  MET A CE  1 
ATOM   7820 N  N   . GLN A 1 986  ? 37.023 46.989  -29.182 1.00 18.47 ? 986  GLN A N   1 
ATOM   7821 C  CA  . GLN A 1 986  ? 37.433 46.514  -30.491 1.00 18.87 ? 986  GLN A CA  1 
ATOM   7822 C  C   . GLN A 1 986  ? 36.411 47.010  -31.489 1.00 17.91 ? 986  GLN A C   1 
ATOM   7823 O  O   . GLN A 1 986  ? 35.265 46.616  -31.408 1.00 16.98 ? 986  GLN A O   1 
ATOM   7824 C  CB  . GLN A 1 986  ? 37.396 44.989  -30.515 1.00 24.57 ? 986  GLN A CB  1 
ATOM   7825 C  CG  . GLN A 1 986  ? 38.293 44.319  -29.527 1.00 30.09 ? 986  GLN A CG  1 
ATOM   7826 C  CD  . GLN A 1 986  ? 39.716 44.265  -29.992 1.00 36.53 ? 986  GLN A CD  1 
ATOM   7827 O  OE1 . GLN A 1 986  ? 40.004 44.232  -31.189 1.00 41.15 ? 986  GLN A OE1 1 
ATOM   7828 N  NE2 . GLN A 1 986  ? 40.624 44.292  -29.049 1.00 35.57 ? 986  GLN A NE2 1 
ATOM   7829 N  N   . CYS A 1 987  ? 36.818 47.870  -32.406 1.00 15.04 ? 987  CYS A N   1 
ATOM   7830 C  CA  . CYS A 1 987  ? 35.859 48.362  -33.403 1.00 16.78 ? 987  CYS A CA  1 
ATOM   7831 C  C   . CYS A 1 987  ? 36.345 48.182  -34.853 1.00 19.06 ? 987  CYS A C   1 
ATOM   7832 O  O   . CYS A 1 987  ? 35.849 48.863  -35.755 1.00 22.26 ? 987  CYS A O   1 
ATOM   7833 C  CB  . CYS A 1 987  ? 35.521 49.829  -33.165 1.00 17.60 ? 987  CYS A CB  1 
ATOM   7834 S  SG  . CYS A 1 987  ? 34.947 50.218  -31.453 1.00 19.69 ? 987  CYS A SG  1 
ATOM   7835 N  N   . GLY A 1 988  ? 37.284 47.285  -35.081 1.00 17.99 ? 988  GLY A N   1 
ATOM   7836 C  CA  . GLY A 1 988  ? 37.689 47.075  -36.473 1.00 23.17 ? 988  GLY A CA  1 
ATOM   7837 C  C   . GLY A 1 988  ? 38.959 47.736  -36.952 1.00 26.77 ? 988  GLY A C   1 
ATOM   7838 O  O   . GLY A 1 988  ? 39.284 47.639  -38.147 1.00 25.47 ? 988  GLY A O   1 
ATOM   7839 N  N   . THR A 1 989  ? 39.671 48.431  -36.073 1.00 23.05 ? 989  THR A N   1 
ATOM   7840 C  CA  . THR A 1 989  ? 40.939 49.033  -36.477 1.00 25.92 ? 989  THR A CA  1 
ATOM   7841 C  C   . THR A 1 989  ? 42.068 48.042  -36.258 1.00 29.34 ? 989  THR A C   1 
ATOM   7842 O  O   . THR A 1 989  ? 42.274 47.554  -35.133 1.00 26.00 ? 989  THR A O   1 
ATOM   7843 C  CB  . THR A 1 989  ? 41.241 50.255  -35.678 1.00 25.10 ? 989  THR A CB  1 
ATOM   7844 O  OG1 . THR A 1 989  ? 40.117 51.140  -35.742 1.00 32.30 ? 989  THR A OG1 1 
ATOM   7845 C  CG2 . THR A 1 989  ? 42.469 50.936  -36.264 1.00 26.93 ? 989  THR A CG2 1 
ATOM   7846 N  N   . PRO A 1 990  ? 42.853 47.749  -37.284 1.00 29.99 ? 990  PRO A N   1 
ATOM   7847 C  CA  . PRO A 1 990  ? 44.010 46.878  -37.065 1.00 34.54 ? 990  PRO A CA  1 
ATOM   7848 C  C   . PRO A 1 990  ? 44.912 47.290  -35.890 1.00 37.55 ? 990  PRO A C   1 
ATOM   7849 O  O   . PRO A 1 990  ? 45.442 46.384  -35.259 1.00 38.59 ? 990  PRO A O   1 
ATOM   7850 C  CB  . PRO A 1 990  ? 44.745 46.944  -38.398 1.00 35.01 ? 990  PRO A CB  1 
ATOM   7851 C  CG  . PRO A 1 990  ? 43.658 47.119  -39.389 1.00 35.00 ? 990  PRO A CG  1 
ATOM   7852 C  CD  . PRO A 1 990  ? 42.615 47.986  -38.718 1.00 31.27 ? 990  PRO A CD  1 
ATOM   7853 N  N   . GLU A 1 991  ? 45.049 48.583  -35.578 1.00 39.33 ? 991  GLU A N   1 
ATOM   7854 C  CA  . GLU A 1 991  ? 45.933 49.046  -34.496 1.00 46.72 ? 991  GLU A CA  1 
ATOM   7855 C  C   . GLU A 1 991  ? 46.997 48.029  -34.080 1.00 47.97 ? 991  GLU A C   1 
ATOM   7856 O  O   . GLU A 1 991  ? 46.685 47.027  -33.439 1.00 51.01 ? 991  GLU A O   1 
ATOM   7857 C  CB  . GLU A 1 991  ? 45.159 49.498  -33.240 1.00 47.04 ? 991  GLU A CB  1 
ATOM   7858 C  CG  . GLU A 1 991  ? 43.923 50.357  -33.464 1.00 49.24 ? 991  GLU A CG  1 
ATOM   7859 C  CD  . GLU A 1 991  ? 43.535 51.152  -32.228 1.00 50.47 ? 991  GLU A CD  1 
ATOM   7860 O  OE1 . GLU A 1 991  ? 42.920 50.575  -31.305 1.00 53.01 ? 991  GLU A OE1 1 
ATOM   7861 O  OE2 . GLU A 1 991  ? 43.842 52.357  -32.185 1.00 45.84 ? 991  GLU A OE2 1 
ATOM   7862 N  N   . GLU A 1 992  ? 48.254 48.317  -34.409 1.00 45.27 ? 992  GLU A N   1 
ATOM   7863 C  CA  . GLU A 1 992  ? 49.274 47.279  -34.572 1.00 46.21 ? 992  GLU A CA  1 
ATOM   7864 C  C   . GLU A 1 992  ? 50.605 47.594  -33.874 1.00 42.16 ? 992  GLU A C   1 
ATOM   7865 O  O   . GLU A 1 992  ? 50.612 48.059  -32.750 1.00 37.25 ? 992  GLU A O   1 
ATOM   7866 C  CB  . GLU A 1 992  ? 49.499 47.004  -36.053 1.00 49.62 ? 992  GLU A CB  1 
ATOM   7867 C  CG  . GLU A 1 992  ? 48.250 46.508  -36.757 1.00 49.63 ? 992  GLU A CG  1 
ATOM   7868 C  CD  . GLU A 1 992  ? 48.001 45.035  -36.501 1.00 52.45 ? 992  GLU A CD  1 
ATOM   7869 O  OE1 . GLU A 1 992  ? 48.663 44.468  -35.612 1.00 54.57 ? 992  GLU A OE1 1 
ATOM   7870 O  OE2 . GLU A 1 992  ? 47.151 44.442  -37.189 1.00 51.84 ? 992  GLU A OE2 1 
ATOM   7871 N  N   . HIS A 1 993  ? 51.719 47.352  -34.570 1.00 41.01 ? 993  HIS A N   1 
ATOM   7872 C  CA  . HIS A 1 993  ? 53.078 47.330  -33.991 1.00 40.43 ? 993  HIS A CA  1 
ATOM   7873 C  C   . HIS A 1 993  ? 53.354 48.236  -32.795 1.00 37.25 ? 993  HIS A C   1 
ATOM   7874 O  O   . HIS A 1 993  ? 53.476 49.457  -32.922 1.00 36.83 ? 993  HIS A O   1 
ATOM   7875 C  CB  . HIS A 1 993  ? 54.108 47.645  -35.073 1.00 41.27 ? 993  HIS A CB  1 
ATOM   7876 C  CG  . HIS A 1 993  ? 53.656 48.698  -36.026 1.00 44.27 ? 993  HIS A CG  1 
ATOM   7877 N  ND1 . HIS A 1 993  ? 53.380 48.439  -37.349 1.00 47.45 ? 993  HIS A ND1 1 
ATOM   7878 C  CD2 . HIS A 1 993  ? 53.390 50.011  -35.835 1.00 45.72 ? 993  HIS A CD2 1 
ATOM   7879 C  CE1 . HIS A 1 993  ? 52.990 49.553  -37.940 1.00 47.81 ? 993  HIS A CE1 1 
ATOM   7880 N  NE2 . HIS A 1 993  ? 52.976 50.519  -37.039 1.00 44.54 ? 993  HIS A NE2 1 
ATOM   7881 N  N   . THR A 1 994  ? 53.506 47.605  -31.638 1.00 33.76 ? 994  THR A N   1 
ATOM   7882 C  CA  . THR A 1 994  ? 54.060 48.231  -30.449 1.00 27.58 ? 994  THR A CA  1 
ATOM   7883 C  C   . THR A 1 994  ? 55.075 47.287  -29.793 1.00 27.37 ? 994  THR A C   1 
ATOM   7884 O  O   . THR A 1 994  ? 55.177 46.132  -30.159 1.00 25.86 ? 994  THR A O   1 
ATOM   7885 C  CB  . THR A 1 994  ? 52.936 48.534  -29.446 1.00 23.33 ? 994  THR A CB  1 
ATOM   7886 O  OG1 . THR A 1 994  ? 52.282 47.313  -29.081 1.00 23.91 ? 994  THR A OG1 1 
ATOM   7887 C  CG2 . THR A 1 994  ? 51.915 49.449  -30.086 1.00 22.36 ? 994  THR A CG2 1 
ATOM   7888 N  N   . GLN A 1 995  ? 55.815 47.779  -28.811 1.00 20.01 ? 995  GLN A N   1 
ATOM   7889 C  CA  . GLN A 1 995  ? 56.844 46.964  -28.183 1.00 18.11 ? 995  GLN A CA  1 
ATOM   7890 C  C   . GLN A 1 995  ? 56.436 46.609  -26.759 1.00 14.73 ? 995  GLN A C   1 
ATOM   7891 O  O   . GLN A 1 995  ? 55.740 47.372  -26.105 1.00 16.62 ? 995  GLN A O   1 
ATOM   7892 C  CB  . GLN A 1 995  ? 58.167 47.724  -28.175 1.00 16.98 ? 995  GLN A CB  1 
ATOM   7893 C  CG  . GLN A 1 995  ? 58.569 48.228  -29.550 1.00 24.64 ? 995  GLN A CG  1 
ATOM   7894 C  CD  . GLN A 1 995  ? 59.373 49.512  -29.517 1.00 31.18 ? 995  GLN A CD  1 
ATOM   7895 O  OE1 . GLN A 1 995  ? 58.881 50.560  -29.125 1.00 19.78 ? 995  GLN A OE1 1 
ATOM   7896 N  NE2 . GLN A 1 995  ? 60.620 49.431  -29.952 1.00 35.52 ? 995  GLN A NE2 1 
ATOM   7897 N  N   . LYS A 1 996  ? 56.873 45.454  -26.280 1.00 15.47 ? 996  LYS A N   1 
ATOM   7898 C  CA  . LYS A 1 996  ? 56.564 45.069  -24.918 1.00 15.47 ? 996  LYS A CA  1 
ATOM   7899 C  C   . LYS A 1 996  ? 57.300 46.032  -23.988 1.00 15.08 ? 996  LYS A C   1 
ATOM   7900 O  O   . LYS A 1 996  ? 58.478 46.376  -24.206 1.00 15.89 ? 996  LYS A O   1 
ATOM   7901 C  CB  . LYS A 1 996  ? 57.037 43.596  -24.689 1.00 20.39 ? 996  LYS A CB  1 
ATOM   7902 C  CG  . LYS A 1 996  ? 56.977 43.087  -23.252 1.00 27.61 ? 996  LYS A CG  1 
ATOM   7903 C  CD  . LYS A 1 996  ? 57.261 41.556  -23.265 1.00 30.86 ? 996  LYS A CD  1 
ATOM   7904 C  CE  . LYS A 1 996  ? 57.400 40.969  -21.846 1.00 32.33 ? 996  LYS A CE  1 
ATOM   7905 N  NZ  . LYS A 1 996  ? 57.774 39.519  -22.002 1.00 42.60 ? 996  LYS A NZ  1 
ATOM   7906 N  N   . LEU A 1 997  ? 56.578 46.454  -22.940 1.00 14.12 ? 997  LEU A N   1 
ATOM   7907 C  CA  . LEU A 1 997  ? 57.208 47.312  -21.956 1.00 13.59 ? 997  LEU A CA  1 
ATOM   7908 C  C   . LEU A 1 997  ? 57.517 46.476  -20.732 1.00 11.65 ? 997  LEU A C   1 
ATOM   7909 O  O   . LEU A 1 997  ? 56.594 45.937  -20.113 1.00 15.44 ? 997  LEU A O   1 
ATOM   7910 C  CB  . LEU A 1 997  ? 56.219 48.422  -21.573 1.00 15.49 ? 997  LEU A CB  1 
ATOM   7911 C  CG  . LEU A 1 997  ? 56.675 49.310  -20.412 1.00 16.86 ? 997  LEU A CG  1 
ATOM   7912 C  CD1 . LEU A 1 997  ? 57.973 50.028  -20.734 1.00 20.06 ? 997  LEU A CD1 1 
ATOM   7913 C  CD2 . LEU A 1 997  ? 55.587 50.319  -20.131 1.00 19.98 ? 997  LEU A CD2 1 
ATOM   7914 N  N   . ASP A 1 998  ? 58.808 46.424  -20.428 1.00 11.86 ? 998  ASP A N   1 
ATOM   7915 C  CA  . ASP A 1 998  ? 59.303 45.755  -19.203 1.00 13.36 ? 998  ASP A CA  1 
ATOM   7916 C  C   . ASP A 1 998  ? 59.885 46.888  -18.343 1.00 12.31 ? 998  ASP A C   1 
ATOM   7917 O  O   . ASP A 1 998  ? 61.033 47.332  -18.528 1.00 12.53 ? 998  ASP A O   1 
ATOM   7918 C  CB  . ASP A 1 998  ? 60.391 44.708  -19.555 1.00 13.42 ? 998  ASP A CB  1 
ATOM   7919 C  CG  . ASP A 1 998  ? 61.090 44.192  -18.343 1.00 16.97 ? 998  ASP A CG  1 
ATOM   7920 O  OD1 . ASP A 1 998  ? 60.621 44.442  -17.210 1.00 15.36 ? 998  ASP A OD1 1 
ATOM   7921 O  OD2 . ASP A 1 998  ? 62.110 43.518  -18.550 1.00 16.93 ? 998  ASP A OD2 1 
ATOM   7922 N  N   . VAL A 1 999  ? 59.089 47.327  -17.358 1.00 12.12 ? 999  VAL A N   1 
ATOM   7923 C  CA  . VAL A 1 999  ? 59.582 48.448  -16.567 1.00 12.03 ? 999  VAL A CA  1 
ATOM   7924 C  C   . VAL A 1 999  ? 60.841 48.133  -15.779 1.00 11.45 ? 999  VAL A C   1 
ATOM   7925 O  O   . VAL A 1 999  ? 61.630 49.020  -15.471 1.00 12.53 ? 999  VAL A O   1 
ATOM   7926 C  CB  . VAL A 1 999  ? 58.497 49.021  -15.569 1.00 11.03 ? 999  VAL A CB  1 
ATOM   7927 C  CG1 . VAL A 1 999  ? 57.350 49.611  -16.377 1.00 12.98 ? 999  VAL A CG1 1 
ATOM   7928 C  CG2 . VAL A 1 999  ? 58.014 47.958  -14.607 1.00 12.06 ? 999  VAL A CG2 1 
ATOM   7929 N  N   . CYS A 1 1000 ? 61.090 46.851  -15.489 1.00 11.65 ? 1000 CYS A N   1 
ATOM   7930 C  CA  . CYS A 1 1000 ? 62.281 46.560  -14.718 1.00 13.85 ? 1000 CYS A CA  1 
ATOM   7931 C  C   . CYS A 1 1000 ? 63.584 46.772  -15.445 1.00 12.74 ? 1000 CYS A C   1 
ATOM   7932 O  O   . CYS A 1 1000 ? 64.620 46.816  -14.814 1.00 15.42 ? 1000 CYS A O   1 
ATOM   7933 C  CB  . CYS A 1 1000 ? 62.160 45.158  -14.138 1.00 15.41 ? 1000 CYS A CB  1 
ATOM   7934 S  SG  . CYS A 1 1000 ? 61.178 45.176  -12.540 1.00 18.75 ? 1000 CYS A SG  1 
ATOM   7935 N  N   . HIS A 1 1001 ? 63.516 46.901  -16.788 1.00 13.12 ? 1001 HIS A N   1 
ATOM   7936 C  CA  . HIS A 1 1001 ? 64.733 47.135  -17.562 1.00 14.30 ? 1001 HIS A CA  1 
ATOM   7937 C  C   . HIS A 1 1001 ? 64.797 48.572  -18.084 1.00 15.46 ? 1001 HIS A C   1 
ATOM   7938 O  O   . HIS A 1 1001 ? 65.617 48.893  -18.948 1.00 17.91 ? 1001 HIS A O   1 
ATOM   7939 C  CB  . HIS A 1 1001 ? 64.871 46.079  -18.676 1.00 14.26 ? 1001 HIS A CB  1 
ATOM   7940 C  CG  . HIS A 1 1001 ? 65.419 44.775  -18.180 1.00 15.83 ? 1001 HIS A CG  1 
ATOM   7941 N  ND1 . HIS A 1 1001 ? 64.619 43.739  -17.766 1.00 17.23 ? 1001 HIS A ND1 1 
ATOM   7942 C  CD2 . HIS A 1 1001 ? 66.699 44.361  -17.991 1.00 17.83 ? 1001 HIS A CD2 1 
ATOM   7943 C  CE1 . HIS A 1 1001 ? 65.373 42.728  -17.353 1.00 18.06 ? 1001 HIS A CE1 1 
ATOM   7944 N  NE2 . HIS A 1 1001 ? 66.640 43.078  -17.473 1.00 18.45 ? 1001 HIS A NE2 1 
ATOM   7945 N  N   . LEU A 1 1002 ? 63.946 49.467  -17.592 1.00 13.71 ? 1002 LEU A N   1 
ATOM   7946 C  CA  . LEU A 1 1002 ? 64.046 50.857  -18.039 1.00 12.99 ? 1002 LEU A CA  1 
ATOM   7947 C  C   . LEU A 1 1002 ? 65.304 51.529  -17.479 1.00 15.55 ? 1002 LEU A C   1 
ATOM   7948 O  O   . LEU A 1 1002 ? 65.805 52.507  -18.070 1.00 17.84 ? 1002 LEU A O   1 
ATOM   7949 C  CB  . LEU A 1 1002 ? 62.830 51.697  -17.561 1.00 13.63 ? 1002 LEU A CB  1 
ATOM   7950 C  CG  . LEU A 1 1002 ? 61.567 51.467  -18.377 1.00 12.01 ? 1002 LEU A CG  1 
ATOM   7951 C  CD1 . LEU A 1 1002 ? 60.395 52.177  -17.690 1.00 13.36 ? 1002 LEU A CD1 1 
ATOM   7952 C  CD2 . LEU A 1 1002 ? 61.685 52.037  -19.792 1.00 16.02 ? 1002 LEU A CD2 1 
ATOM   7953 N  N   . LEU A 1 1003 ? 65.805 51.096  -16.327 1.00 14.92 ? 1003 LEU A N   1 
ATOM   7954 C  CA  . LEU A 1 1003 ? 67.041 51.646  -15.771 1.00 14.66 ? 1003 LEU A CA  1 
ATOM   7955 C  C   . LEU A 1 1003 ? 68.107 50.543  -15.901 1.00 16.62 ? 1003 LEU A C   1 
ATOM   7956 O  O   . LEU A 1 1003 ? 67.792 49.354  -15.843 1.00 17.30 ? 1003 LEU A O   1 
ATOM   7957 C  CB  . LEU A 1 1003 ? 66.855 52.047  -14.313 1.00 14.75 ? 1003 LEU A CB  1 
ATOM   7958 C  CG  . LEU A 1 1003 ? 66.076 53.350  -14.257 1.00 20.31 ? 1003 LEU A CG  1 
ATOM   7959 C  CD1 . LEU A 1 1003 ? 65.562 53.494  -12.852 1.00 20.14 ? 1003 LEU A CD1 1 
ATOM   7960 C  CD2 . LEU A 1 1003 ? 66.931 54.526  -14.674 1.00 23.67 ? 1003 LEU A CD2 1 
ATOM   7961 N  N   . PRO A 1 1004 ? 69.367 50.934  -16.076 1.00 17.42 ? 1004 PRO A N   1 
ATOM   7962 C  CA  . PRO A 1 1004 ? 70.384 49.895  -16.221 1.00 15.73 ? 1004 PRO A CA  1 
ATOM   7963 C  C   . PRO A 1 1004 ? 70.813 49.232  -14.919 1.00 17.21 ? 1004 PRO A C   1 
ATOM   7964 O  O   . PRO A 1 1004 ? 70.452 49.598  -13.782 1.00 16.53 ? 1004 PRO A O   1 
ATOM   7965 C  CB  . PRO A 1 1004 ? 71.537 50.664  -16.895 1.00 19.61 ? 1004 PRO A CB  1 
ATOM   7966 C  CG  . PRO A 1 1004 ? 71.442 52.002  -16.236 1.00 20.61 ? 1004 PRO A CG  1 
ATOM   7967 C  CD  . PRO A 1 1004 ? 69.933 52.284  -16.093 1.00 18.44 ? 1004 PRO A CD  1 
ATOM   7968 N  N   . ASN A 1 1005 ? 71.557 48.155  -15.128 1.00 18.81 ? 1005 ASN A N   1 
ATOM   7969 C  CA  . ASN A 1 1005 ? 72.125 47.406  -14.017 1.00 18.64 ? 1005 ASN A CA  1 
ATOM   7970 C  C   . ASN A 1 1005 ? 71.091 46.820  -13.066 1.00 16.43 ? 1005 ASN A C   1 
ATOM   7971 O  O   . ASN A 1 1005 ? 71.287 46.859  -11.853 1.00 16.45 ? 1005 ASN A O   1 
ATOM   7972 C  CB  . ASN A 1 1005 ? 73.085 48.304  -13.221 1.00 21.65 ? 1005 ASN A CB  1 
ATOM   7973 C  CG  . ASN A 1 1005 ? 74.121 48.985  -14.119 1.00 27.17 ? 1005 ASN A CG  1 
ATOM   7974 O  OD1 . ASN A 1 1005 ? 74.309 50.211  -14.052 1.00 35.21 ? 1005 ASN A OD1 1 
ATOM   7975 N  ND2 . ASN A 1 1005 ? 74.769 48.201  -14.963 1.00 25.13 ? 1005 ASN A ND2 1 
ATOM   7976 N  N   . VAL A 1 1006 ? 70.039 46.253  -13.631 1.00 16.84 ? 1006 VAL A N   1 
ATOM   7977 C  CA  . VAL A 1 1006 ? 69.003 45.678  -12.796 1.00 16.85 ? 1006 VAL A CA  1 
ATOM   7978 C  C   . VAL A 1 1006 ? 69.530 44.374  -12.145 1.00 15.78 ? 1006 VAL A C   1 
ATOM   7979 O  O   . VAL A 1 1006 ? 70.126 43.523  -12.816 1.00 20.15 ? 1006 VAL A O   1 
ATOM   7980 C  CB  . VAL A 1 1006 ? 67.673 45.460  -13.609 1.00 17.53 ? 1006 VAL A CB  1 
ATOM   7981 C  CG1 . VAL A 1 1006 ? 67.823 44.433  -14.682 1.00 18.82 ? 1006 VAL A CG1 1 
ATOM   7982 C  CG2 . VAL A 1 1006 ? 66.572 45.000  -12.649 1.00 17.42 ? 1006 VAL A CG2 1 
ATOM   7983 N  N   . ALA A 1 1007 ? 69.296 44.237  -10.853 1.00 12.79 ? 1007 ALA A N   1 
ATOM   7984 C  CA  . ALA A 1 1007 ? 69.736 43.082  -10.054 1.00 14.77 ? 1007 ALA A CA  1 
ATOM   7985 C  C   . ALA A 1 1007 ? 68.555 42.252  -9.576  1.00 18.95 ? 1007 ALA A C   1 
ATOM   7986 O  O   . ALA A 1 1007 ? 68.707 41.052  -9.290  1.00 20.21 ? 1007 ALA A O   1 
ATOM   7987 C  CB  . ALA A 1 1007 ? 70.549 43.605  -8.857  1.00 15.94 ? 1007 ALA A CB  1 
ATOM   7988 N  N   . ARG A 1 1008 ? 67.359 42.849  -9.517  1.00 15.89 ? 1008 ARG A N   1 
ATOM   7989 C  CA  . ARG A 1 1008 ? 66.163 42.135  -9.051  1.00 14.16 ? 1008 ARG A CA  1 
ATOM   7990 C  C   . ARG A 1 1008 ? 64.912 42.864  -9.530  1.00 13.50 ? 1008 ARG A C   1 
ATOM   7991 O  O   . ARG A 1 1008 ? 64.964 44.106  -9.708  1.00 14.32 ? 1008 ARG A O   1 
ATOM   7992 C  CB  . ARG A 1 1008 ? 66.171 42.142  -7.534  1.00 16.35 ? 1008 ARG A CB  1 
ATOM   7993 C  CG  . ARG A 1 1008 ? 65.129 41.280  -6.849  1.00 24.22 ? 1008 ARG A CG  1 
ATOM   7994 C  CD  . ARG A 1 1008 ? 65.314 41.314  -5.333  1.00 29.14 ? 1008 ARG A CD  1 
ATOM   7995 N  NE  . ARG A 1 1008 ? 64.597 40.214  -4.679  1.00 36.65 ? 1008 ARG A NE  1 
ATOM   7996 C  CZ  . ARG A 1 1008 ? 65.055 38.956  -4.553  1.00 40.13 ? 1008 ARG A CZ  1 
ATOM   7997 N  NH1 . ARG A 1 1008 ? 66.258 38.600  -5.018  1.00 40.83 ? 1008 ARG A NH1 1 
ATOM   7998 N  NH2 . ARG A 1 1008 ? 64.282 38.023  -3.988  1.00 37.37 ? 1008 ARG A NH2 1 
ATOM   7999 N  N   . CYS A 1 1009 ? 63.838 42.132  -9.775  1.00 11.89 ? 1009 CYS A N   1 
ATOM   8000 C  CA  . CYS A 1 1009 ? 62.551 42.753  -10.161 1.00 11.84 ? 1009 CYS A CA  1 
ATOM   8001 C  C   . CYS A 1 1009 ? 61.520 42.021  -9.297  1.00 13.53 ? 1009 CYS A C   1 
ATOM   8002 O  O   . CYS A 1 1009 ? 61.461 40.766  -9.326  1.00 13.56 ? 1009 CYS A O   1 
ATOM   8003 C  CB  . CYS A 1 1009 ? 62.280 42.515  -11.635 1.00 13.42 ? 1009 CYS A CB  1 
ATOM   8004 S  SG  . CYS A 1 1009 ? 60.698 43.210  -12.283 1.00 19.71 ? 1009 CYS A SG  1 
ATOM   8005 N  N   . GLU A 1 1010 ? 60.696 42.754  -8.522  1.00 11.95 ? 1010 GLU A N   1 
ATOM   8006 C  CA  . GLU A 1 1010 ? 59.684 42.154  -7.679  1.00 10.71 ? 1010 GLU A CA  1 
ATOM   8007 C  C   . GLU A 1 1010 ? 58.312 42.761  -7.985  1.00 9.48  ? 1010 GLU A C   1 
ATOM   8008 O  O   . GLU A 1 1010 ? 58.209 43.989  -8.263  1.00 11.29 ? 1010 GLU A O   1 
ATOM   8009 C  CB  . GLU A 1 1010 ? 59.946 42.509  -6.221  1.00 13.12 ? 1010 GLU A CB  1 
ATOM   8010 C  CG  . GLU A 1 1010 ? 61.155 41.873  -5.561  1.00 19.46 ? 1010 GLU A CG  1 
ATOM   8011 C  CD  . GLU A 1 1010 ? 60.895 40.439  -5.126  1.00 23.31 ? 1010 GLU A CD  1 
ATOM   8012 O  OE1 . GLU A 1 1010 ? 59.744 40.083  -4.723  1.00 31.06 ? 1010 GLU A OE1 1 
ATOM   8013 O  OE2 . GLU A 1 1010 ? 61.874 39.659  -5.167  1.00 33.69 ? 1010 GLU A OE2 1 
ATOM   8014 N  N   . ARG A 1 1011 ? 57.275 41.955  -7.995  1.00 10.18 ? 1011 ARG A N   1 
ATOM   8015 C  CA  . ARG A 1 1011 ? 55.892 42.486  -8.049  1.00 8.70  ? 1011 ARG A CA  1 
ATOM   8016 C  C   . ARG A 1 1011 ? 55.549 42.804  -6.589  1.00 9.66  ? 1011 ARG A C   1 
ATOM   8017 O  O   . ARG A 1 1011 ? 55.862 41.995  -5.672  1.00 10.68 ? 1011 ARG A O   1 
ATOM   8018 C  CB  . ARG A 1 1011 ? 54.926 41.457  -8.585  1.00 11.05 ? 1011 ARG A CB  1 
ATOM   8019 C  CG  . ARG A 1 1011 ? 53.540 42.088  -8.813  1.00 13.97 ? 1011 ARG A CG  1 
ATOM   8020 C  CD  . ARG A 1 1011 ? 52.628 41.223  -9.597  1.00 16.30 ? 1011 ARG A CD  1 
ATOM   8021 N  NE  . ARG A 1 1011 ? 52.343 40.041  -8.815  1.00 18.70 ? 1011 ARG A NE  1 
ATOM   8022 C  CZ  . ARG A 1 1011 ? 51.444 39.950  -7.819  1.00 24.51 ? 1011 ARG A CZ  1 
ATOM   8023 N  NH1 . ARG A 1 1011 ? 50.700 40.999  -7.437  1.00 26.82 ? 1011 ARG A NH1 1 
ATOM   8024 N  NH2 . ARG A 1 1011 ? 51.253 38.779  -7.210  1.00 25.98 ? 1011 ARG A NH2 1 
ATOM   8025 N  N   . THR A 1 1012 ? 54.946 43.960  -6.309  1.00 8.63  ? 1012 THR A N   1 
ATOM   8026 C  CA  . THR A 1 1012 ? 54.612 44.373  -4.960  1.00 6.90  ? 1012 THR A CA  1 
ATOM   8027 C  C   . THR A 1 1012 ? 53.151 44.812  -4.869  1.00 8.01  ? 1012 THR A C   1 
ATOM   8028 O  O   . THR A 1 1012 ? 52.457 44.952  -5.884  1.00 8.18  ? 1012 THR A O   1 
ATOM   8029 C  CB  . THR A 1 1012 ? 55.504 45.595  -4.549  1.00 8.65  ? 1012 THR A CB  1 
ATOM   8030 O  OG1 . THR A 1 1012 ? 55.181 46.742  -5.380  1.00 8.87  ? 1012 THR A OG1 1 
ATOM   8031 C  CG2 . THR A 1 1012 ? 57.000 45.331  -4.747  1.00 9.02  ? 1012 THR A CG2 1 
ATOM   8032 N  N   . THR A 1 1013 ? 52.716 45.029  -3.643  1.00 7.70  ? 1013 THR A N   1 
ATOM   8033 C  CA  . THR A 1 1013 ? 51.451 45.712  -3.440  1.00 7.46  ? 1013 THR A CA  1 
ATOM   8034 C  C   . THR A 1 1013 ? 51.562 47.120  -4.100  1.00 7.49  ? 1013 THR A C   1 
ATOM   8035 O  O   . THR A 1 1013 ? 52.661 47.650  -4.331  1.00 7.19  ? 1013 THR A O   1 
ATOM   8036 C  CB  . THR A 1 1013 ? 51.153 45.867  -1.970  1.00 7.76  ? 1013 THR A CB  1 
ATOM   8037 O  OG1 . THR A 1 1013 ? 52.331 46.310  -1.293  1.00 8.53  ? 1013 THR A OG1 1 
ATOM   8038 C  CG2 . THR A 1 1013 ? 50.666 44.505  -1.382  1.00 10.58 ? 1013 THR A CG2 1 
ATOM   8039 N  N   . LEU A 1 1014 ? 50.399 47.750  -4.335  1.00 6.92  ? 1014 LEU A N   1 
ATOM   8040 C  CA  . LEU A 1 1014 ? 50.423 49.052  -5.069  1.00 6.50  ? 1014 LEU A CA  1 
ATOM   8041 C  C   . LEU A 1 1014 ? 51.099 50.196  -4.342  1.00 6.29  ? 1014 LEU A C   1 
ATOM   8042 O  O   . LEU A 1 1014 ? 51.454 51.195  -4.959  1.00 7.60  ? 1014 LEU A O   1 
ATOM   8043 C  CB  . LEU A 1 1014 ? 48.992 49.510  -5.453  1.00 7.75  ? 1014 LEU A CB  1 
ATOM   8044 C  CG  . LEU A 1 1014 ? 48.264 48.536  -6.375  1.00 6.75  ? 1014 LEU A CG  1 
ATOM   8045 C  CD1 . LEU A 1 1014 ? 46.966 49.249  -6.733  1.00 8.34  ? 1014 LEU A CD1 1 
ATOM   8046 C  CD2 . LEU A 1 1014 ? 49.070 48.136  -7.655  1.00 8.21  ? 1014 LEU A CD2 1 
ATOM   8047 N  N   . THR A 1 1015 ? 51.267 50.069  -3.018  1.00 6.48  ? 1015 THR A N   1 
ATOM   8048 C  CA  . THR A 1 1015 ? 51.926 51.036  -2.178  1.00 6.28  ? 1015 THR A CA  1 
ATOM   8049 C  C   . THR A 1 1015 ? 53.452 50.797  -2.125  1.00 6.67  ? 1015 THR A C   1 
ATOM   8050 O  O   . THR A 1 1015 ? 54.174 51.570  -1.482  1.00 7.43  ? 1015 THR A O   1 
ATOM   8051 C  CB  . THR A 1 1015 ? 51.414 50.934  -0.746  1.00 6.70  ? 1015 THR A CB  1 
ATOM   8052 O  OG1 . THR A 1 1015 ? 51.604 49.525  -0.383  1.00 7.20  ? 1015 THR A OG1 1 
ATOM   8053 C  CG2 . THR A 1 1015 ? 49.954 51.314  -0.611  1.00 7.72  ? 1015 THR A CG2 1 
ATOM   8054 N  N   . PHE A 1 1016 ? 53.916 49.732  -2.800  1.00 6.88  ? 1016 PHE A N   1 
ATOM   8055 C  CA  . PHE A 1 1016 ? 55.338 49.269  -2.839  1.00 7.90  ? 1016 PHE A CA  1 
ATOM   8056 C  C   . PHE A 1 1016 ? 55.796 48.698  -1.500  1.00 8.44  ? 1016 PHE A C   1 
ATOM   8057 O  O   . PHE A 1 1016 ? 57.002 48.394  -1.377  1.00 10.69 ? 1016 PHE A O   1 
ATOM   8058 C  CB  . PHE A 1 1016 ? 56.296 50.392  -3.277  1.00 8.81  ? 1016 PHE A CB  1 
ATOM   8059 C  CG  . PHE A 1 1016 ? 55.927 51.023  -4.581  1.00 7.43  ? 1016 PHE A CG  1 
ATOM   8060 C  CD1 . PHE A 1 1016 ? 55.798 50.259  -5.736  1.00 8.39  ? 1016 PHE A CD1 1 
ATOM   8061 C  CD2 . PHE A 1 1016 ? 55.756 52.415  -4.648  1.00 7.93  ? 1016 PHE A CD2 1 
ATOM   8062 C  CE1 . PHE A 1 1016 ? 55.494 50.906  -6.960  1.00 8.49  ? 1016 PHE A CE1 1 
ATOM   8063 C  CE2 . PHE A 1 1016 ? 55.453 53.019  -5.878  1.00 7.63  ? 1016 PHE A CE2 1 
ATOM   8064 C  CZ  . PHE A 1 1016 ? 55.325 52.263  -7.011  1.00 8.81  ? 1016 PHE A CZ  1 
ATOM   8065 N  N   . LEU A 1 1017 ? 54.905 48.469  -0.534  1.00 7.56  ? 1017 LEU A N   1 
ATOM   8066 C  CA  . LEU A 1 1017 ? 55.349 48.115  0.825   1.00 8.64  ? 1017 LEU A CA  1 
ATOM   8067 C  C   . LEU A 1 1017 ? 55.512 46.639  1.058   1.00 9.69  ? 1017 LEU A C   1 
ATOM   8068 O  O   . LEU A 1 1017 ? 56.135 46.303  2.085   1.00 14.45 ? 1017 LEU A O   1 
ATOM   8069 C  CB  . LEU A 1 1017 ? 54.399 48.734  1.860   1.00 8.59  ? 1017 LEU A CB  1 
ATOM   8070 C  CG  . LEU A 1 1017 ? 54.382 50.254  1.785   1.00 8.62  ? 1017 LEU A CG  1 
ATOM   8071 C  CD1 . LEU A 1 1017 ? 53.336 50.785  2.747   1.00 10.01 ? 1017 LEU A CD1 1 
ATOM   8072 C  CD2 . LEU A 1 1017 ? 55.722 50.892  2.181   1.00 11.33 ? 1017 LEU A CD2 1 
ATOM   8073 N  N   . GLN A 1 1018 ? 55.015 45.765  0.212   1.00 8.44  ? 1018 GLN A N   1 
ATOM   8074 C  CA  . GLN A 1 1018 ? 55.229 44.334  0.412   1.00 10.17 ? 1018 GLN A CA  1 
ATOM   8075 C  C   . GLN A 1 1018 ? 55.579 43.654  -0.897  1.00 10.35 ? 1018 GLN A C   1 
ATOM   8076 O  O   . GLN A 1 1018 ? 54.952 43.878  -1.903  1.00 10.36 ? 1018 GLN A O   1 
ATOM   8077 C  CB  . GLN A 1 1018 ? 53.975 43.692  1.008   1.00 11.59 ? 1018 GLN A CB  1 
ATOM   8078 C  CG  . GLN A 1 1018 ? 54.132 42.198  1.237   1.00 15.69 ? 1018 GLN A CG  1 
ATOM   8079 C  CD  . GLN A 1 1018 ? 52.869 41.490  1.705   1.00 22.43 ? 1018 GLN A CD  1 
ATOM   8080 O  OE1 . GLN A 1 1018 ? 51.781 42.047  1.729   1.00 24.62 ? 1018 GLN A OE1 1 
ATOM   8081 N  NE2 . GLN A 1 1018 ? 53.016 40.216  2.030   1.00 18.37 ? 1018 GLN A NE2 1 
ATOM   8082 N  N   . ASN A 1 1019 ? 56.591 42.803  -0.871  1.00 11.16 ? 1019 ASN A N   1 
ATOM   8083 C  CA  . ASN A 1 1019 ? 56.965 42.062  -2.073  1.00 12.49 ? 1019 ASN A CA  1 
ATOM   8084 C  C   . ASN A 1 1019 ? 56.063 40.840  -2.174  1.00 14.32 ? 1019 ASN A C   1 
ATOM   8085 O  O   . ASN A 1 1019 ? 55.898 40.102  -1.162  1.00 16.77 ? 1019 ASN A O   1 
ATOM   8086 C  CB  . ASN A 1 1019 ? 58.432 41.592  -2.002  1.00 15.50 ? 1019 ASN A CB  1 
ATOM   8087 C  CG  . ASN A 1 1019 ? 59.418 42.745  -1.960  1.00 18.76 ? 1019 ASN A CG  1 
ATOM   8088 O  OD1 . ASN A 1 1019 ? 59.184 43.827  -2.534  1.00 16.17 ? 1019 ASN A OD1 1 
ATOM   8089 N  ND2 . ASN A 1 1019 ? 60.571 42.527  -1.293  1.00 21.24 ? 1019 ASN A ND2 1 
ATOM   8090 N  N   . LEU A 1 1020 ? 55.459 40.631  -3.336  1.00 12.55 ? 1020 LEU A N   1 
ATOM   8091 C  CA  . LEU A 1 1020 ? 54.547 39.536  -3.559  1.00 14.50 ? 1020 LEU A CA  1 
ATOM   8092 C  C   . LEU A 1 1020 ? 55.108 38.449  -4.471  1.00 15.66 ? 1020 LEU A C   1 
ATOM   8093 O  O   . LEU A 1 1020 ? 54.632 37.299  -4.427  1.00 17.72 ? 1020 LEU A O   1 
ATOM   8094 C  CB  . LEU A 1 1020 ? 53.239 40.041  -4.181  1.00 15.91 ? 1020 LEU A CB  1 
ATOM   8095 C  CG  . LEU A 1 1020 ? 52.518 41.147  -3.369  1.00 14.16 ? 1020 LEU A CG  1 
ATOM   8096 C  CD1 . LEU A 1 1020 ? 51.321 41.687  -4.184  1.00 17.50 ? 1020 LEU A CD1 1 
ATOM   8097 C  CD2 . LEU A 1 1020 ? 51.982 40.590  -2.050  1.00 16.49 ? 1020 LEU A CD2 1 
ATOM   8098 N  N   . GLU A 1 1021 ? 56.058 38.781  -5.321  1.00 13.72 ? 1021 GLU A N   1 
ATOM   8099 C  CA  . GLU A 1 1021 ? 56.591 37.779  -6.277  1.00 17.25 ? 1021 GLU A CA  1 
ATOM   8100 C  C   . GLU A 1 1021 ? 57.967 38.187  -6.768  1.00 18.04 ? 1021 GLU A C   1 
ATOM   8101 O  O   . GLU A 1 1021 ? 58.184 39.347  -7.154  1.00 16.51 ? 1021 GLU A O   1 
ATOM   8102 C  CB  . GLU A 1 1021 ? 55.627 37.702  -7.475  1.00 18.79 ? 1021 GLU A CB  1 
ATOM   8103 C  CG  . GLU A 1 1021 ? 55.887 36.619  -8.517  1.00 26.90 ? 1021 GLU A CG  1 
ATOM   8104 C  CD  . GLU A 1 1021 ? 54.911 36.706  -9.706  1.00 28.93 ? 1021 GLU A CD  1 
ATOM   8105 O  OE1 . GLU A 1 1021 ? 53.998 37.586  -9.740  1.00 29.99 ? 1021 GLU A OE1 1 
ATOM   8106 O  OE2 . GLU A 1 1021 ? 55.079 35.882  -10.632 1.00 35.93 ? 1021 GLU A OE2 1 
ATOM   8107 N  N   . HIS A 1 1022 ? 58.931 37.263  -6.772  1.00 19.83 ? 1022 HIS A N   1 
ATOM   8108 C  CA  . HIS A 1 1022 ? 60.282 37.505  -7.279  1.00 19.94 ? 1022 HIS A CA  1 
ATOM   8109 C  C   . HIS A 1 1022 ? 60.169 37.084  -8.746  1.00 20.67 ? 1022 HIS A C   1 
ATOM   8110 O  O   . HIS A 1 1022 ? 59.753 35.957  -9.045  1.00 23.10 ? 1022 HIS A O   1 
ATOM   8111 C  CB  . HIS A 1 1022 ? 61.258 36.597  -6.516  1.00 23.48 ? 1022 HIS A CB  1 
ATOM   8112 C  CG  . HIS A 1 1022 ? 62.694 36.871  -6.818  1.00 30.53 ? 1022 HIS A CG  1 
ATOM   8113 N  ND1 . HIS A 1 1022 ? 63.682 35.925  -6.634  1.00 36.46 ? 1022 HIS A ND1 1 
ATOM   8114 C  CD2 . HIS A 1 1022 ? 63.318 37.982  -7.290  1.00 33.89 ? 1022 HIS A CD2 1 
ATOM   8115 C  CE1 . HIS A 1 1022 ? 64.852 36.437  -6.986  1.00 37.31 ? 1022 HIS A CE1 1 
ATOM   8116 N  NE2 . HIS A 1 1022 ? 64.659 37.685  -7.387  1.00 38.29 ? 1022 HIS A NE2 1 
ATOM   8117 N  N   . LEU A 1 1023 ? 60.532 37.963  -9.668  1.00 14.43 ? 1023 LEU A N   1 
ATOM   8118 C  CA  . LEU A 1 1023 ? 60.306 37.732  -11.078 1.00 17.59 ? 1023 LEU A CA  1 
ATOM   8119 C  C   . LEU A 1 1023 ? 61.459 37.188  -11.868 1.00 16.25 ? 1023 LEU A C   1 
ATOM   8120 O  O   . LEU A 1 1023 ? 62.563 37.755  -11.861 1.00 18.57 ? 1023 LEU A O   1 
ATOM   8121 C  CB  . LEU A 1 1023 ? 59.853 39.054  -11.686 1.00 17.13 ? 1023 LEU A CB  1 
ATOM   8122 C  CG  . LEU A 1 1023 ? 58.514 39.506  -11.073 1.00 18.10 ? 1023 LEU A CG  1 
ATOM   8123 C  CD1 . LEU A 1 1023 ? 58.289 40.977  -11.312 1.00 21.43 ? 1023 LEU A CD1 1 
ATOM   8124 C  CD2 . LEU A 1 1023 ? 57.383 38.686  -11.683 1.00 22.59 ? 1023 LEU A CD2 1 
ATOM   8125 N  N   . ASP A 1 1024 ? 61.163 36.099  -12.570 1.00 22.53 ? 1024 ASP A N   1 
ATOM   8126 C  CA  . ASP A 1 1024 ? 62.138 35.425  -13.411 1.00 23.99 ? 1024 ASP A CA  1 
ATOM   8127 C  C   . ASP A 1 1024 ? 62.709 36.358  -14.447 1.00 23.98 ? 1024 ASP A C   1 
ATOM   8128 O  O   . ASP A 1 1024 ? 61.973 37.117  -15.123 1.00 23.98 ? 1024 ASP A O   1 
ATOM   8129 C  CB  . ASP A 1 1024 ? 61.474 34.253  -14.145 1.00 28.99 ? 1024 ASP A CB  1 
ATOM   8130 C  CG  . ASP A 1 1024 ? 61.150 33.091  -13.234 1.00 36.94 ? 1024 ASP A CG  1 
ATOM   8131 O  OD1 . ASP A 1 1024 ? 61.396 33.206  -11.999 1.00 42.54 ? 1024 ASP A OD1 1 
ATOM   8132 O  OD2 . ASP A 1 1024 ? 60.656 32.054  -13.766 1.00 40.78 ? 1024 ASP A OD2 1 
ATOM   8133 N  N   . GLY A 1 1025 ? 64.019 36.258  -14.594 1.00 20.24 ? 1025 GLY A N   1 
ATOM   8134 C  CA  . GLY A 1 1025 ? 64.751 37.032  -15.575 1.00 22.54 ? 1025 GLY A CA  1 
ATOM   8135 C  C   . GLY A 1 1025 ? 64.688 38.511  -15.324 1.00 20.06 ? 1025 GLY A C   1 
ATOM   8136 O  O   . GLY A 1 1025 ? 65.079 39.259  -16.207 1.00 21.99 ? 1025 GLY A O   1 
ATOM   8137 N  N   . MET A 1 1026 ? 64.241 38.918  -14.128 1.00 18.30 ? 1026 MET A N   1 
ATOM   8138 C  CA  . MET A 1 1026 ? 64.112 40.333  -13.781 1.00 19.54 ? 1026 MET A CA  1 
ATOM   8139 C  C   . MET A 1 1026 ? 63.195 41.026  -14.776 1.00 16.63 ? 1026 MET A C   1 
ATOM   8140 O  O   . MET A 1 1026 ? 63.369 42.238  -15.019 1.00 18.83 ? 1026 MET A O   1 
ATOM   8141 C  CB  . MET A 1 1026 ? 65.473 41.029  -13.748 1.00 21.63 ? 1026 MET A CB  1 
ATOM   8142 C  CG  . MET A 1 1026 ? 66.428 40.371  -12.729 1.00 26.10 ? 1026 MET A CG  1 
ATOM   8143 S  SD  . MET A 1 1026 ? 68.107 41.018  -12.791 1.00 34.42 ? 1026 MET A SD  1 
ATOM   8144 C  CE  . MET A 1 1026 ? 68.640 40.431  -14.474 1.00 28.67 ? 1026 MET A CE  1 
ATOM   8145 N  N   . VAL A 1 1027 ? 62.211 40.304  -15.280 1.00 16.91 ? 1027 VAL A N   1 
ATOM   8146 C  CA  . VAL A 1 1027 ? 61.259 40.885  -16.234 1.00 17.54 ? 1027 VAL A CA  1 
ATOM   8147 C  C   . VAL A 1 1027 ? 59.902 41.092  -15.584 1.00 18.13 ? 1027 VAL A C   1 
ATOM   8148 O  O   . VAL A 1 1027 ? 59.342 40.218  -14.944 1.00 19.16 ? 1027 VAL A O   1 
ATOM   8149 C  CB  . VAL A 1 1027 ? 61.103 40.008  -17.496 1.00 15.45 ? 1027 VAL A CB  1 
ATOM   8150 C  CG1 . VAL A 1 1027 ? 59.972 40.533  -18.399 1.00 18.89 ? 1027 VAL A CG1 1 
ATOM   8151 C  CG2 . VAL A 1 1027 ? 62.438 39.988  -18.277 1.00 19.31 ? 1027 VAL A CG2 1 
ATOM   8152 N  N   . ALA A 1 1028 ? 59.361 42.297  -15.756 1.00 16.50 ? 1028 ALA A N   1 
ATOM   8153 C  CA  . ALA A 1 1028 ? 58.037 42.642  -15.194 1.00 18.85 ? 1028 ALA A CA  1 
ATOM   8154 C  C   . ALA A 1 1028 ? 57.063 42.446  -16.286 1.00 20.21 ? 1028 ALA A C   1 
ATOM   8155 O  O   . ALA A 1 1028 ? 57.089 43.182  -17.291 1.00 22.34 ? 1028 ALA A O   1 
ATOM   8156 C  CB  . ALA A 1 1028 ? 57.995 44.120  -14.769 1.00 17.08 ? 1028 ALA A CB  1 
ATOM   8157 N  N   . PRO A 1 1029 ? 56.156 41.498  -16.120 1.00 17.89 ? 1029 PRO A N   1 
ATOM   8158 C  CA  . PRO A 1 1029 ? 55.148 41.257  -17.176 1.00 18.93 ? 1029 PRO A CA  1 
ATOM   8159 C  C   . PRO A 1 1029 ? 54.116 42.388  -17.275 1.00 19.57 ? 1029 PRO A C   1 
ATOM   8160 O  O   . PRO A 1 1029 ? 53.838 43.063  -16.294 1.00 25.20 ? 1029 PRO A O   1 
ATOM   8161 C  CB  . PRO A 1 1029 ? 54.444 39.991  -16.717 1.00 20.12 ? 1029 PRO A CB  1 
ATOM   8162 C  CG  . PRO A 1 1029 ? 55.303 39.430  -15.584 1.00 23.66 ? 1029 PRO A CG  1 
ATOM   8163 C  CD  . PRO A 1 1029 ? 56.039 40.574  -14.981 1.00 15.89 ? 1029 PRO A CD  1 
ATOM   8164 N  N   . GLU A 1 1030 ? 53.558 42.586  -18.455 1.00 17.74 ? 1030 GLU A N   1 
ATOM   8165 C  CA  . GLU A 1 1030 ? 52.499 43.572  -18.568 1.00 17.55 ? 1030 GLU A CA  1 
ATOM   8166 C  C   . GLU A 1 1030 ? 51.242 42.970  -17.901 1.00 19.48 ? 1030 GLU A C   1 
ATOM   8167 O  O   . GLU A 1 1030 ? 51.099 41.726  -17.686 1.00 24.96 ? 1030 GLU A O   1 
ATOM   8168 C  CB  . GLU A 1 1030 ? 52.205 43.924  -20.038 1.00 19.15 ? 1030 GLU A CB  1 
ATOM   8169 C  CG  . GLU A 1 1030 ? 53.398 44.547  -20.787 1.00 19.19 ? 1030 GLU A CG  1 
ATOM   8170 C  CD  . GLU A 1 1030 ? 53.048 44.876  -22.222 1.00 19.55 ? 1030 GLU A CD  1 
ATOM   8171 O  OE1 . GLU A 1 1030 ? 52.045 44.317  -22.728 1.00 23.80 ? 1030 GLU A OE1 1 
ATOM   8172 O  OE2 . GLU A 1 1030 ? 53.804 45.679  -22.847 1.00 16.77 ? 1030 GLU A OE2 1 
ATOM   8173 N  N   . VAL A 1 1031 ? 50.318 43.842  -17.596 1.00 17.72 ? 1031 VAL A N   1 
ATOM   8174 C  CA  . VAL A 1 1031 ? 49.124 43.454  -16.902 1.00 14.18 ? 1031 VAL A CA  1 
ATOM   8175 C  C   . VAL A 1 1031 ? 47.942 43.271  -17.838 1.00 13.94 ? 1031 VAL A C   1 
ATOM   8176 O  O   . VAL A 1 1031 ? 47.989 43.665  -19.012 1.00 14.39 ? 1031 VAL A O   1 
ATOM   8177 C  CB  . VAL A 1 1031 ? 48.801 44.502  -15.820 1.00 17.27 ? 1031 VAL A CB  1 
ATOM   8178 C  CG1 . VAL A 1 1031 ? 50.011 44.589  -14.860 1.00 20.05 ? 1031 VAL A CG1 1 
ATOM   8179 C  CG2 . VAL A 1 1031 ? 48.502 45.825  -16.411 1.00 17.12 ? 1031 VAL A CG2 1 
ATOM   8180 N  N   . CYS A 1 1032 ? 46.911 42.602  -17.338 1.00 11.97 ? 1032 CYS A N   1 
ATOM   8181 C  CA  . CYS A 1 1032 ? 45.677 42.352  -18.102 1.00 13.40 ? 1032 CYS A CA  1 
ATOM   8182 C  C   . CYS A 1 1032 ? 44.744 43.569  -18.160 1.00 11.53 ? 1032 CYS A C   1 
ATOM   8183 O  O   . CYS A 1 1032 ? 44.864 44.491  -17.364 1.00 9.99  ? 1032 CYS A O   1 
ATOM   8184 C  CB  . CYS A 1 1032 ? 44.883 41.237  -17.432 1.00 11.53 ? 1032 CYS A CB  1 
ATOM   8185 S  SG  . CYS A 1 1032 ? 45.714 39.613  -17.621 1.00 21.28 ? 1032 CYS A SG  1 
ATOM   8186 N  N   . PRO A 1 1033 ? 43.809 43.600  -19.138 1.00 10.16 ? 1033 PRO A N   1 
ATOM   8187 C  CA  . PRO A 1 1033 ? 42.857 44.727  -19.187 1.00 9.31  ? 1033 PRO A CA  1 
ATOM   8188 C  C   . PRO A 1 1033 ? 42.128 44.855  -17.831 1.00 8.58  ? 1033 PRO A C   1 
ATOM   8189 O  O   . PRO A 1 1033 ? 41.605 43.887  -17.251 1.00 9.86  ? 1033 PRO A O   1 
ATOM   8190 C  CB  . PRO A 1 1033 ? 41.884 44.340  -20.346 1.00 10.12 ? 1033 PRO A CB  1 
ATOM   8191 C  CG  . PRO A 1 1033 ? 42.736 43.431  -21.232 1.00 12.61 ? 1033 PRO A CG  1 
ATOM   8192 C  CD  . PRO A 1 1033 ? 43.573 42.622  -20.226 1.00 11.93 ? 1033 PRO A CD  1 
ATOM   8193 N  N   . MET A 1 1034 ? 42.004 46.114  -17.426 1.00 8.39  ? 1034 MET A N   1 
ATOM   8194 C  CA  . MET A 1 1034 ? 41.404 46.580  -16.194 1.00 9.20  ? 1034 MET A CA  1 
ATOM   8195 C  C   . MET A 1 1034 ? 42.197 46.214  -14.944 1.00 10.29 ? 1034 MET A C   1 
ATOM   8196 O  O   . MET A 1 1034 ? 41.739 46.546  -13.838 1.00 14.55 ? 1034 MET A O   1 
ATOM   8197 C  CB  . MET A 1 1034 ? 39.934 46.146  -16.047 1.00 8.35  ? 1034 MET A CB  1 
ATOM   8198 C  CG  . MET A 1 1034 ? 39.099 46.686  -17.193 1.00 9.57  ? 1034 MET A CG  1 
ATOM   8199 S  SD  . MET A 1 1034 ? 39.087 48.454  -17.424 1.00 11.21 ? 1034 MET A SD  1 
ATOM   8200 C  CE  . MET A 1 1034 ? 38.172 48.985  -15.866 1.00 12.52 ? 1034 MET A CE  1 
ATOM   8201 N  N   . GLU A 1 1035 ? 43.394 45.725  -15.109 1.00 7.92  ? 1035 GLU A N   1 
ATOM   8202 C  CA  . GLU A 1 1035 ? 44.216 45.388  -13.962 1.00 9.30  ? 1035 GLU A CA  1 
ATOM   8203 C  C   . GLU A 1 1035 ? 45.286 46.464  -13.768 1.00 8.78  ? 1035 GLU A C   1 
ATOM   8204 O  O   . GLU A 1 1035 ? 45.660 47.205  -14.686 1.00 8.59  ? 1035 GLU A O   1 
ATOM   8205 C  CB  . GLU A 1 1035 ? 44.803 44.000  -14.150 1.00 13.74 ? 1035 GLU A CB  1 
ATOM   8206 C  CG  . GLU A 1 1035 ? 43.749 42.906  -13.904 1.00 22.06 ? 1035 GLU A CG  1 
ATOM   8207 C  CD  . GLU A 1 1035 ? 43.385 42.763  -12.417 1.00 30.06 ? 1035 GLU A CD  1 
ATOM   8208 O  OE1 . GLU A 1 1035 ? 42.737 43.679  -11.844 1.00 30.97 ? 1035 GLU A OE1 1 
ATOM   8209 O  OE2 . GLU A 1 1035 ? 43.782 41.727  -11.831 1.00 38.59 ? 1035 GLU A OE2 1 
ATOM   8210 N  N   . THR A 1 1036 ? 45.777 46.527  -12.522 1.00 8.72  ? 1036 THR A N   1 
ATOM   8211 C  CA  . THR A 1 1036 ? 46.837 47.439  -12.117 1.00 9.10  ? 1036 THR A CA  1 
ATOM   8212 C  C   . THR A 1 1036 ? 47.835 46.620  -11.297 1.00 9.33  ? 1036 THR A C   1 
ATOM   8213 O  O   . THR A 1 1036 ? 47.412 45.854  -10.404 1.00 10.42 ? 1036 THR A O   1 
ATOM   8214 C  CB  . THR A 1 1036 ? 46.267 48.576  -11.249 1.00 7.86  ? 1036 THR A CB  1 
ATOM   8215 O  OG1 . THR A 1 1036 ? 45.177 49.186  -11.936 1.00 9.54  ? 1036 THR A OG1 1 
ATOM   8216 C  CG2 . THR A 1 1036 ? 47.314 49.611  -10.877 1.00 9.38  ? 1036 THR A CG2 1 
ATOM   8217 N  N   . ALA A 1 1037 ? 49.137 46.726  -11.587 1.00 8.51  ? 1037 ALA A N   1 
ATOM   8218 C  CA  . ALA A 1 1037 ? 50.162 45.998  -10.838 1.00 8.84  ? 1037 ALA A CA  1 
ATOM   8219 C  C   . ALA A 1 1037 ? 51.258 46.964  -10.488 1.00 7.99  ? 1037 ALA A C   1 
ATOM   8220 O  O   . ALA A 1 1037 ? 51.374 48.046  -11.085 1.00 9.96  ? 1037 ALA A O   1 
ATOM   8221 C  CB  . ALA A 1 1037 ? 50.741 44.864  -11.694 1.00 11.20 ? 1037 ALA A CB  1 
ATOM   8222 N  N   . ALA A 1 1038 ? 52.051 46.620  -9.503  1.00 7.23  ? 1038 ALA A N   1 
ATOM   8223 C  CA  . ALA A 1 1038 ? 53.183 47.431  -9.116  1.00 7.63  ? 1038 ALA A CA  1 
ATOM   8224 C  C   . ALA A 1 1038 ? 54.429 46.562  -9.149  1.00 6.98  ? 1038 ALA A C   1 
ATOM   8225 O  O   . ALA A 1 1038 ? 54.386 45.372  -8.798  1.00 8.16  ? 1038 ALA A O   1 
ATOM   8226 C  CB  . ALA A 1 1038 ? 53.000 48.054  -7.748  1.00 8.39  ? 1038 ALA A CB  1 
ATOM   8227 N  N   . TYR A 1 1039 ? 55.532 47.186  -9.546  1.00 8.06  ? 1039 TYR A N   1 
ATOM   8228 C  CA  . TYR A 1 1039 ? 56.798 46.469  -9.641  1.00 8.45  ? 1039 TYR A CA  1 
ATOM   8229 C  C   . TYR A 1 1039 ? 57.875 47.340  -9.076  1.00 9.64  ? 1039 TYR A C   1 
ATOM   8230 O  O   . TYR A 1 1039 ? 57.825 48.574  -9.216  1.00 9.85  ? 1039 TYR A O   1 
ATOM   8231 C  CB  . TYR A 1 1039 ? 57.155 46.158  -11.102 1.00 9.42  ? 1039 TYR A CB  1 
ATOM   8232 C  CG  . TYR A 1 1039 ? 56.200 45.272  -11.781 1.00 9.38  ? 1039 TYR A CG  1 
ATOM   8233 C  CD1 . TYR A 1 1039 ? 56.165 43.892  -11.538 1.00 10.28 ? 1039 TYR A CD1 1 
ATOM   8234 C  CD2 . TYR A 1 1039 ? 55.272 45.798  -12.696 1.00 12.18 ? 1039 TYR A CD2 1 
ATOM   8235 C  CE1 . TYR A 1 1039 ? 55.263 43.066  -12.188 1.00 13.19 ? 1039 TYR A CE1 1 
ATOM   8236 C  CE2 . TYR A 1 1039 ? 54.363 44.949  -13.373 1.00 14.57 ? 1039 TYR A CE2 1 
ATOM   8237 C  CZ  . TYR A 1 1039 ? 54.379 43.598  -13.099 1.00 14.07 ? 1039 TYR A CZ  1 
ATOM   8238 O  OH  . TYR A 1 1039 ? 53.498 42.799  -13.828 1.00 17.17 ? 1039 TYR A OH  1 
ATOM   8239 N  N   . VAL A 1 1040 ? 58.881 46.735  -8.442  1.00 10.28 ? 1040 VAL A N   1 
ATOM   8240 C  CA  . VAL A 1 1040 ? 60.039 47.487  -7.946  1.00 9.20  ? 1040 VAL A CA  1 
ATOM   8241 C  C   . VAL A 1 1040 ? 61.282 46.830  -8.561  1.00 10.31 ? 1040 VAL A C   1 
ATOM   8242 O  O   . VAL A 1 1040 ? 61.497 45.593  -8.417  1.00 11.89 ? 1040 VAL A O   1 
ATOM   8243 C  CB  . VAL A 1 1040 ? 60.127 47.465  -6.408  1.00 9.73  ? 1040 VAL A CB  1 
ATOM   8244 C  CG1 . VAL A 1 1040 ? 61.496 48.137  -5.964  1.00 10.89 ? 1040 VAL A CG1 1 
ATOM   8245 C  CG2 . VAL A 1 1040 ? 58.956 48.248  -5.824  1.00 11.14 ? 1040 VAL A CG2 1 
ATOM   8246 N  N   . SER A 1 1041 ? 62.097 47.617  -9.261  1.00 9.13  ? 1041 SER A N   1 
ATOM   8247 C  CA  . SER A 1 1041 ? 63.367 47.136  -9.778  1.00 10.21 ? 1041 SER A CA  1 
ATOM   8248 C  C   . SER A 1 1041 ? 64.482 47.621  -8.837  1.00 9.99  ? 1041 SER A C   1 
ATOM   8249 O  O   . SER A 1 1041 ? 64.435 48.730  -8.277  1.00 10.40 ? 1041 SER A O   1 
ATOM   8250 C  CB  . SER A 1 1041 ? 63.556 47.640  -11.216 1.00 11.65 ? 1041 SER A CB  1 
ATOM   8251 O  OG  . SER A 1 1041 ? 63.656 49.058  -11.291 1.00 12.39 ? 1041 SER A OG  1 
ATOM   8252 N  N   . SER A 1 1042 ? 65.452 46.726  -8.596  1.00 10.78 ? 1042 SER A N   1 
ATOM   8253 C  CA  . SER A 1 1042 ? 66.601 47.025  -7.718  1.00 11.84 ? 1042 SER A CA  1 
ATOM   8254 C  C   . SER A 1 1042 ? 67.850 47.061  -8.633  1.00 10.65 ? 1042 SER A C   1 
ATOM   8255 O  O   . SER A 1 1042 ? 67.968 46.280  -9.580  1.00 15.57 ? 1042 SER A O   1 
ATOM   8256 C  CB  . SER A 1 1042 ? 66.758 45.926  -6.646  1.00 11.98 ? 1042 SER A CB  1 
ATOM   8257 O  OG  . SER A 1 1042 ? 65.654 45.933  -5.757  1.00 14.53 ? 1042 SER A OG  1 
ATOM   8258 N  N   . HIS A 1 1043 ? 68.735 47.998  -8.343  1.00 12.94 ? 1043 HIS A N   1 
ATOM   8259 C  CA  . HIS A 1 1043 ? 69.851 48.306  -9.225  1.00 13.18 ? 1043 HIS A CA  1 
ATOM   8260 C  C   . HIS A 1 1043 ? 71.103 48.430  -8.403  1.00 15.36 ? 1043 HIS A C   1 
ATOM   8261 O  O   . HIS A 1 1043 ? 71.112 49.032  -7.355  1.00 14.51 ? 1043 HIS A O   1 
ATOM   8262 C  CB  . HIS A 1 1043 ? 69.601 49.591  -9.997  1.00 14.51 ? 1043 HIS A CB  1 
ATOM   8263 C  CG  . HIS A 1 1043 ? 68.320 49.565  -10.748 1.00 12.69 ? 1043 HIS A CG  1 
ATOM   8264 N  ND1 . HIS A 1 1043 ? 68.238 49.166  -12.058 1.00 14.52 ? 1043 HIS A ND1 1 
ATOM   8265 C  CD2 . HIS A 1 1043 ? 67.052 49.779  -10.334 1.00 12.51 ? 1043 HIS A CD2 1 
ATOM   8266 C  CE1 . HIS A 1 1043 ? 66.973 49.183  -12.436 1.00 14.01 ? 1043 HIS A CE1 1 
ATOM   8267 N  NE2 . HIS A 1 1043 ? 66.237 49.561  -11.409 1.00 13.27 ? 1043 HIS A NE2 1 
ATOM   8268 N  N   . SER A 1 1044 ? 72.174 47.828  -8.906  1.00 19.83 ? 1044 SER A N   1 
ATOM   8269 C  CA  . SER A 1 1044 ? 73.382 47.863  -8.118  1.00 28.34 ? 1044 SER A CA  1 
ATOM   8270 C  C   . SER A 1 1044 ? 74.298 48.993  -8.474  1.00 32.01 ? 1044 SER A C   1 
ATOM   8271 O  O   . SER A 1 1044 ? 73.857 49.937  -9.171  1.00 29.35 ? 1044 SER A O   1 
ATOM   8272 C  CB  . SER A 1 1044 ? 74.121 46.519  -8.226  1.00 31.30 ? 1044 SER A CB  1 
ATOM   8273 O  OG  . SER A 1 1044 ? 73.777 45.848  -9.437  1.00 37.72 ? 1044 SER A OG  1 
HETATM 8274 C  C1  . NAG B 2 .    ? 58.303 44.815  12.796  1.00 31.48 ? 1046 NAG A C1  1 
HETATM 8275 C  C2  . NAG B 2 .    ? 59.383 44.452  13.811  1.00 36.31 ? 1046 NAG A C2  1 
HETATM 8276 C  C3  . NAG B 2 .    ? 59.885 43.041  13.585  1.00 38.95 ? 1046 NAG A C3  1 
HETATM 8277 C  C4  . NAG B 2 .    ? 58.720 42.070  13.626  1.00 40.01 ? 1046 NAG A C4  1 
HETATM 8278 C  C5  . NAG B 2 .    ? 57.663 42.506  12.609  1.00 40.87 ? 1046 NAG A C5  1 
HETATM 8279 C  C6  . NAG B 2 .    ? 56.422 41.635  12.642  1.00 42.62 ? 1046 NAG A C6  1 
HETATM 8280 C  C7  . NAG B 2 .    ? 60.595 46.354  14.621  1.00 43.06 ? 1046 NAG A C7  1 
HETATM 8281 C  C8  . NAG B 2 .    ? 60.217 46.016  16.068  1.00 44.11 ? 1046 NAG A C8  1 
HETATM 8282 N  N2  . NAG B 2 .    ? 60.494 45.377  13.721  1.00 40.76 ? 1046 NAG A N2  1 
HETATM 8283 O  O3  . NAG B 2 .    ? 60.818 42.729  14.608  1.00 41.37 ? 1046 NAG A O3  1 
HETATM 8284 O  O4  . NAG B 2 .    ? 59.193 40.767  13.304  1.00 43.80 ? 1046 NAG A O4  1 
HETATM 8285 O  O5  . NAG B 2 .    ? 57.235 43.871  12.878  1.00 36.62 ? 1046 NAG A O5  1 
HETATM 8286 O  O6  . NAG B 2 .    ? 55.329 42.271  11.983  1.00 46.78 ? 1046 NAG A O6  1 
HETATM 8287 O  O7  . NAG B 2 .    ? 60.959 47.497  14.327  1.00 47.12 ? 1046 NAG A O7  1 
HETATM 8288 ZN ZN  . ZN  C 3 .    ? 34.483 64.248  8.119   1.00 7.04  ? 1047 ZN  A ZN  1 
HETATM 8289 C  C1  . SWA D 4 .    ? 31.037 66.706  6.172   1.00 6.81  ? 1048 SWA A C1  1 
HETATM 8290 O  O1  . SWA D 4 .    ? 31.473 67.889  5.510   1.00 8.05  ? 1048 SWA A O1  1 
HETATM 8291 C  C3  . SWA D 4 .    ? 31.334 66.853  7.643   1.00 8.00  ? 1048 SWA A C3  1 
HETATM 8292 N  N4  . SWA D 4 .    ? 30.826 65.639  8.314   1.00 7.06  ? 1048 SWA A N4  1 
HETATM 8293 C  C5  . SWA D 4 .    ? 29.363 65.524  8.189   1.00 7.90  ? 1048 SWA A C5  1 
HETATM 8294 C  C6  . SWA D 4 .    ? 29.088 65.370  6.709   1.00 9.72  ? 1048 SWA A C6  1 
HETATM 8295 C  C2  . SWA D 4 .    ? 29.545 66.567  5.899   1.00 8.54  ? 1048 SWA A C2  1 
HETATM 8296 C  C9  . SWA D 4 .    ? 31.292 65.888  9.690   1.00 9.30  ? 1048 SWA A C9  1 
HETATM 8297 C  C8  . SWA D 4 .    ? 32.701 66.416  9.475   1.00 8.20  ? 1048 SWA A C8  1 
HETATM 8298 O  O13 . SWA D 4 .    ? 33.610 65.328  9.736   1.00 7.96  ? 1048 SWA A O13 1 
HETATM 8299 C  C7  . SWA D 4 .    ? 32.798 66.955  8.052   1.00 6.49  ? 1048 SWA A C7  1 
HETATM 8300 O  O11 . SWA D 4 .    ? 33.664 66.112  7.279   1.00 7.29  ? 1048 SWA A O11 1 
HETATM 8301 C  C1  . MRD E 5 .    ? 14.642 61.209  10.243  1.00 11.40 ? 1049 MRD A C1  1 
HETATM 8302 C  C2  . MRD E 5 .    ? 16.085 61.206  10.540  1.00 13.55 ? 1049 MRD A C2  1 
HETATM 8303 O  O2  . MRD E 5 .    ? 16.733 60.184  9.678   1.00 20.29 ? 1049 MRD A O2  1 
HETATM 8304 C  CM  . MRD E 5 .    ? 16.660 62.598  10.174  1.00 18.78 ? 1049 MRD A CM  1 
HETATM 8305 C  C3  . MRD E 5 .    ? 16.224 60.882  12.052  1.00 14.53 ? 1049 MRD A C3  1 
HETATM 8306 C  C4  . MRD E 5 .    ? 17.598 60.719  12.626  1.00 12.81 ? 1049 MRD A C4  1 
HETATM 8307 O  O4  . MRD E 5 .    ? 17.488 59.795  13.740  1.00 11.97 ? 1049 MRD A O4  1 
HETATM 8308 C  C5  . MRD E 5 .    ? 18.124 62.063  13.174  1.00 14.68 ? 1049 MRD A C5  1 
HETATM 8309 O  O   . HOH F 6 .    ? 27.863 46.955  -31.410 1.00 25.12 ? 1050 HOH A O   1 
HETATM 8310 O  O   . HOH F 6 .    ? 28.213 44.394  -29.544 1.00 25.32 ? 1051 HOH A O   1 
HETATM 8311 O  O   . HOH F 6 .    ? 26.116 44.270  -27.219 1.00 27.96 ? 1052 HOH A O   1 
HETATM 8312 O  O   . HOH F 6 .    ? 26.777 41.618  -27.546 1.00 31.68 ? 1053 HOH A O   1 
HETATM 8313 O  O   . HOH F 6 .    ? 27.618 39.652  -24.673 1.00 40.84 ? 1054 HOH A O   1 
HETATM 8314 O  O   . HOH F 6 .    ? 27.384 38.599  -22.259 1.00 28.99 ? 1055 HOH A O   1 
HETATM 8315 O  O   . HOH F 6 .    ? 28.426 41.312  -21.674 1.00 11.83 ? 1056 HOH A O   1 
HETATM 8316 O  O   . HOH F 6 .    ? 27.431 36.575  -19.744 1.00 25.62 ? 1057 HOH A O   1 
HETATM 8317 O  O   . HOH F 6 .    ? 29.378 35.080  -16.441 1.00 32.93 ? 1058 HOH A O   1 
HETATM 8318 O  O   . HOH F 6 .    ? 30.155 35.153  -12.396 1.00 21.67 ? 1059 HOH A O   1 
HETATM 8319 O  O   . HOH F 6 .    ? 30.492 34.678  -9.682  1.00 31.13 ? 1060 HOH A O   1 
HETATM 8320 O  O   . HOH F 6 .    ? 28.077 35.322  -6.782  1.00 19.22 ? 1061 HOH A O   1 
HETATM 8321 O  O   . HOH F 6 .    ? 25.255 34.336  -6.807  1.00 42.28 ? 1062 HOH A O   1 
HETATM 8322 O  O   . HOH F 6 .    ? 26.943 33.854  -3.255  1.00 29.44 ? 1063 HOH A O   1 
HETATM 8323 O  O   . HOH F 6 .    ? 29.872 34.086  -1.506  1.00 24.69 ? 1064 HOH A O   1 
HETATM 8324 O  O   . HOH F 6 .    ? 31.912 34.365  -3.217  1.00 21.09 ? 1065 HOH A O   1 
HETATM 8325 O  O   . HOH F 6 .    ? 33.122 36.670  -4.358  1.00 14.80 ? 1066 HOH A O   1 
HETATM 8326 O  O   . HOH F 6 .    ? 32.169 39.176  -4.883  1.00 10.11 ? 1067 HOH A O   1 
HETATM 8327 O  O   . HOH F 6 .    ? 35.826 35.993  -4.469  1.00 19.41 ? 1068 HOH A O   1 
HETATM 8328 O  O   . HOH F 6 .    ? 39.751 38.772  -3.445  1.00 21.37 ? 1069 HOH A O   1 
HETATM 8329 O  O   . HOH F 6 .    ? 39.820 39.735  -0.287  1.00 25.09 ? 1070 HOH A O   1 
HETATM 8330 O  O   . HOH F 6 .    ? 41.835 40.370  0.682   1.00 39.20 ? 1071 HOH A O   1 
HETATM 8331 O  O   . HOH F 6 .    ? 42.478 39.428  -1.449  1.00 29.07 ? 1072 HOH A O   1 
HETATM 8332 O  O   . HOH F 6 .    ? 44.388 41.822  -0.466  1.00 15.89 ? 1073 HOH A O   1 
HETATM 8333 O  O   . HOH F 6 .    ? 45.919 39.759  0.076   1.00 32.38 ? 1074 HOH A O   1 
HETATM 8334 O  O   . HOH F 6 .    ? 48.266 40.813  -0.972  1.00 21.50 ? 1075 HOH A O   1 
HETATM 8335 O  O   . HOH F 6 .    ? 49.489 40.889  1.443   1.00 26.47 ? 1076 HOH A O   1 
HETATM 8336 O  O   . HOH F 6 .    ? 48.009 41.775  3.764   1.00 15.78 ? 1077 HOH A O   1 
HETATM 8337 O  O   . HOH F 6 .    ? 47.577 40.101  5.878   1.00 38.49 ? 1078 HOH A O   1 
HETATM 8338 O  O   . HOH F 6 .    ? 48.977 41.721  8.293   1.00 29.05 ? 1079 HOH A O   1 
HETATM 8339 O  O   . HOH F 6 .    ? 49.917 44.093  7.162   1.00 16.64 ? 1080 HOH A O   1 
HETATM 8340 O  O   . HOH F 6 .    ? 49.272 44.150  4.474   1.00 13.48 ? 1081 HOH A O   1 
HETATM 8341 O  O   . HOH F 6 .    ? 51.543 44.434  3.118   1.00 19.80 ? 1082 HOH A O   1 
HETATM 8342 O  O   . HOH F 6 .    ? 51.777 46.537  1.353   1.00 10.36 ? 1083 HOH A O   1 
HETATM 8343 O  O   . HOH F 6 .    ? 49.787 48.431  1.419   1.00 9.06  ? 1084 HOH A O   1 
HETATM 8344 O  O   . HOH F 6 .    ? 47.373 45.979  3.748   1.00 10.11 ? 1085 HOH A O   1 
HETATM 8345 O  O   . HOH F 6 .    ? 53.790 45.842  4.779   1.00 35.33 ? 1086 HOH A O   1 
HETATM 8346 O  O   . HOH F 6 .    ? 52.741 43.710  7.659   1.00 38.29 ? 1087 HOH A O   1 
HETATM 8347 O  O   . HOH F 6 .    ? 51.315 45.067  9.911   1.00 28.91 ? 1088 HOH A O   1 
HETATM 8348 O  O   . HOH F 6 .    ? 47.066 45.930  11.311  1.00 33.28 ? 1089 HOH A O   1 
HETATM 8349 O  O   . HOH F 6 .    ? 46.976 48.528  11.587  1.00 16.49 ? 1090 HOH A O   1 
HETATM 8350 O  O   . HOH F 6 .    ? 47.844 49.498  13.869  1.00 12.47 ? 1091 HOH A O   1 
HETATM 8351 O  O   . HOH F 6 .    ? 48.001 48.305  16.499  1.00 15.80 ? 1092 HOH A O   1 
HETATM 8352 O  O   . HOH F 6 .    ? 46.001 46.045  16.456  1.00 27.84 ? 1093 HOH A O   1 
HETATM 8353 O  O   . HOH F 6 .    ? 43.890 44.904  19.355  1.00 38.87 ? 1094 HOH A O   1 
HETATM 8354 O  O   . HOH F 6 .    ? 45.758 45.132  23.348  1.00 29.70 ? 1095 HOH A O   1 
HETATM 8355 O  O   . HOH F 6 .    ? 46.907 45.757  26.478  1.00 30.17 ? 1096 HOH A O   1 
HETATM 8356 O  O   . HOH F 6 .    ? 49.515 46.121  26.740  1.00 32.55 ? 1097 HOH A O   1 
HETATM 8357 O  O   . HOH F 6 .    ? 50.926 43.933  26.620  1.00 35.90 ? 1098 HOH A O   1 
HETATM 8358 O  O   . HOH F 6 .    ? 49.958 47.457  29.095  1.00 18.57 ? 1099 HOH A O   1 
HETATM 8359 O  O   . HOH F 6 .    ? 49.509 45.736  31.172  1.00 23.40 ? 1100 HOH A O   1 
HETATM 8360 O  O   . HOH F 6 .    ? 47.762 43.857  30.388  1.00 34.18 ? 1101 HOH A O   1 
HETATM 8361 O  O   . HOH F 6 .    ? 49.237 50.042  28.346  1.00 13.26 ? 1102 HOH A O   1 
HETATM 8362 O  O   . HOH F 6 .    ? 51.951 50.480  27.430  1.00 24.44 ? 1103 HOH A O   1 
HETATM 8363 O  O   . HOH F 6 .    ? 52.324 48.863  25.687  1.00 27.71 ? 1104 HOH A O   1 
HETATM 8364 O  O   . HOH F 6 .    ? 53.327 52.601  26.334  1.00 18.48 ? 1105 HOH A O   1 
HETATM 8365 O  O   . HOH F 6 .    ? 55.768 52.021  27.490  1.00 25.02 ? 1106 HOH A O   1 
HETATM 8366 O  O   . HOH F 6 .    ? 56.111 53.407  29.869  1.00 33.73 ? 1107 HOH A O   1 
HETATM 8367 O  O   . HOH F 6 .    ? 57.774 55.457  29.412  1.00 33.49 ? 1108 HOH A O   1 
HETATM 8368 O  O   . HOH F 6 .    ? 58.878 56.714  31.337  1.00 33.43 ? 1109 HOH A O   1 
HETATM 8369 O  O   . HOH F 6 .    ? 59.076 55.374  27.130  1.00 23.59 ? 1110 HOH A O   1 
HETATM 8370 O  O   . HOH F 6 .    ? 58.023 52.824  26.217  1.00 26.16 ? 1111 HOH A O   1 
HETATM 8371 O  O   . HOH F 6 .    ? 59.484 50.947  24.800  1.00 25.29 ? 1112 HOH A O   1 
HETATM 8372 O  O   . HOH F 6 .    ? 58.559 51.096  22.235  1.00 19.77 ? 1113 HOH A O   1 
HETATM 8373 O  O   . HOH F 6 .    ? 60.336 50.954  20.385  1.00 32.69 ? 1114 HOH A O   1 
HETATM 8374 O  O   . HOH F 6 .    ? 58.748 48.735  19.155  1.00 27.61 ? 1115 HOH A O   1 
HETATM 8375 O  O   . HOH F 6 .    ? 57.229 48.871  21.359  1.00 18.96 ? 1116 HOH A O   1 
HETATM 8376 O  O   . HOH F 6 .    ? 56.675 47.149  23.368  1.00 37.30 ? 1117 HOH A O   1 
HETATM 8377 O  O   . HOH F 6 .    ? 57.454 49.325  16.642  1.00 28.02 ? 1118 HOH A O   1 
HETATM 8378 O  O   . HOH F 6 .    ? 55.129 50.400  16.859  1.00 22.97 ? 1119 HOH A O   1 
HETATM 8379 O  O   . HOH F 6 .    ? 54.181 47.606  15.560  1.00 21.65 ? 1120 HOH A O   1 
HETATM 8380 O  O   . HOH F 6 .    ? 56.748 46.575  15.765  1.00 26.43 ? 1121 HOH A O   1 
HETATM 8381 O  O   . HOH F 6 .    ? 58.786 50.966  14.838  1.00 32.71 ? 1122 HOH A O   1 
HETATM 8382 O  O   . HOH F 6 .    ? 60.363 54.253  14.762  1.00 27.58 ? 1123 HOH A O   1 
HETATM 8383 O  O   . HOH F 6 .    ? 60.652 56.727  15.907  1.00 26.83 ? 1124 HOH A O   1 
HETATM 8384 O  O   . HOH F 6 .    ? 61.607 58.877  14.890  1.00 24.25 ? 1125 HOH A O   1 
HETATM 8385 O  O   . HOH F 6 .    ? 60.838 61.211  13.626  1.00 32.91 ? 1126 HOH A O   1 
HETATM 8386 O  O   . HOH F 6 .    ? 61.021 63.530  15.146  1.00 22.59 ? 1127 HOH A O   1 
HETATM 8387 O  O   . HOH F 6 .    ? 63.512 59.596  16.897  1.00 31.51 ? 1128 HOH A O   1 
HETATM 8388 O  O   . HOH F 6 .    ? 65.372 55.840  21.297  1.00 36.57 ? 1129 HOH A O   1 
HETATM 8389 O  O   . HOH F 6 .    ? 63.330 57.705  25.790  1.00 40.55 ? 1130 HOH A O   1 
HETATM 8390 O  O   . HOH F 6 .    ? 62.189 62.528  25.715  1.00 15.58 ? 1131 HOH A O   1 
HETATM 8391 O  O   . HOH F 6 .    ? 59.140 62.303  25.766  1.00 20.92 ? 1132 HOH A O   1 
HETATM 8392 O  O   . HOH F 6 .    ? 56.858 64.913  24.323  1.00 21.95 ? 1133 HOH A O   1 
HETATM 8393 O  O   . HOH F 6 .    ? 57.181 67.406  22.710  1.00 31.51 ? 1134 HOH A O   1 
HETATM 8394 O  O   . HOH F 6 .    ? 52.910 69.684  18.346  1.00 22.39 ? 1135 HOH A O   1 
HETATM 8395 O  O   . HOH F 6 .    ? 52.534 72.479  18.315  1.00 22.44 ? 1136 HOH A O   1 
HETATM 8396 O  O   . HOH F 6 .    ? 50.885 76.402  14.461  1.00 19.73 ? 1137 HOH A O   1 
HETATM 8397 O  O   . HOH F 6 .    ? 47.315 78.512  11.627  1.00 33.25 ? 1138 HOH A O   1 
HETATM 8398 O  O   . HOH F 6 .    ? 46.074 77.763  9.491   1.00 20.06 ? 1139 HOH A O   1 
HETATM 8399 O  O   . HOH F 6 .    ? 48.172 76.723  8.241   1.00 33.25 ? 1140 HOH A O   1 
HETATM 8400 O  O   . HOH F 6 .    ? 46.685 74.556  7.779   1.00 10.62 ? 1141 HOH A O   1 
HETATM 8401 O  O   . HOH F 6 .    ? 49.176 76.522  5.496   1.00 31.59 ? 1142 HOH A O   1 
HETATM 8402 O  O   . HOH F 6 .    ? 45.928 79.761  4.894   1.00 27.67 ? 1143 HOH A O   1 
HETATM 8403 O  O   . HOH F 6 .    ? 43.351 80.725  5.215   1.00 23.40 ? 1144 HOH A O   1 
HETATM 8404 O  O   . HOH F 6 .    ? 35.903 81.143  6.424   1.00 16.99 ? 1145 HOH A O   1 
HETATM 8405 O  O   . HOH F 6 .    ? 31.813 80.327  7.233   1.00 36.48 ? 1146 HOH A O   1 
HETATM 8406 O  O   . HOH F 6 .    ? 27.866 82.106  6.734   1.00 32.37 ? 1147 HOH A O   1 
HETATM 8407 O  O   . HOH F 6 .    ? 27.480 82.414  3.329   1.00 27.75 ? 1148 HOH A O   1 
HETATM 8408 O  O   . HOH F 6 .    ? 29.749 83.063  2.488   1.00 19.93 ? 1149 HOH A O   1 
HETATM 8409 O  O   . HOH F 6 .    ? 31.574 83.609  4.325   1.00 29.86 ? 1150 HOH A O   1 
HETATM 8410 O  O   . HOH F 6 .    ? 32.697 84.267  0.292   1.00 27.05 ? 1151 HOH A O   1 
HETATM 8411 O  O   . HOH F 6 .    ? 31.250 81.797  0.503   1.00 16.31 ? 1152 HOH A O   1 
HETATM 8412 O  O   . HOH F 6 .    ? 37.543 80.553  -0.587  1.00 22.86 ? 1153 HOH A O   1 
HETATM 8413 O  O   . HOH F 6 .    ? 37.939 83.243  -1.035  1.00 29.35 ? 1154 HOH A O   1 
HETATM 8414 O  O   . HOH F 6 .    ? 37.341 83.525  -4.082  1.00 28.73 ? 1155 HOH A O   1 
HETATM 8415 O  O   . HOH F 6 .    ? 38.678 80.408  -3.190  1.00 29.45 ? 1156 HOH A O   1 
HETATM 8416 O  O   . HOH F 6 .    ? 41.005 81.830  -3.663  1.00 33.73 ? 1157 HOH A O   1 
HETATM 8417 O  O   . HOH F 6 .    ? 41.130 84.096  -2.254  1.00 40.16 ? 1158 HOH A O   1 
HETATM 8418 O  O   . HOH F 6 .    ? 36.228 79.222  -5.064  1.00 19.30 ? 1159 HOH A O   1 
HETATM 8419 O  O   . HOH F 6 .    ? 35.705 77.631  -7.366  1.00 12.03 ? 1160 HOH A O   1 
HETATM 8420 O  O   . HOH F 6 .    ? 34.491 79.214  -9.196  1.00 9.84  ? 1161 HOH A O   1 
HETATM 8421 O  O   . HOH F 6 .    ? 32.705 81.108  -11.753 1.00 9.84  ? 1162 HOH A O   1 
HETATM 8422 O  O   . HOH F 6 .    ? 33.503 83.616  -10.476 1.00 14.09 ? 1163 HOH A O   1 
HETATM 8423 O  O   . HOH F 6 .    ? 31.998 85.279  -8.593  1.00 20.63 ? 1164 HOH A O   1 
HETATM 8424 O  O   . HOH F 6 .    ? 32.788 85.448  -5.633  1.00 16.93 ? 1165 HOH A O   1 
HETATM 8425 O  O   . HOH F 6 .    ? 35.464 86.150  -8.146  1.00 34.68 ? 1166 HOH A O   1 
HETATM 8426 O  O   . HOH F 6 .    ? 34.116 87.185  -10.545 1.00 32.99 ? 1167 HOH A O   1 
HETATM 8427 O  O   . HOH F 6 .    ? 30.165 87.200  -15.071 1.00 22.90 ? 1168 HOH A O   1 
HETATM 8428 O  O   . HOH F 6 .    ? 27.656 86.412  -14.633 1.00 26.68 ? 1169 HOH A O   1 
HETATM 8429 O  O   . HOH F 6 .    ? 27.446 88.699  -12.508 1.00 27.76 ? 1170 HOH A O   1 
HETATM 8430 O  O   . HOH F 6 .    ? 29.397 87.450  -17.803 1.00 28.47 ? 1171 HOH A O   1 
HETATM 8431 O  O   . HOH F 6 .    ? 31.609 85.925  -19.967 1.00 18.80 ? 1172 HOH A O   1 
HETATM 8432 O  O   . HOH F 6 .    ? 33.358 84.404  -18.319 1.00 15.80 ? 1173 HOH A O   1 
HETATM 8433 O  O   . HOH F 6 .    ? 35.357 86.341  -18.040 1.00 28.16 ? 1174 HOH A O   1 
HETATM 8434 O  O   . HOH F 6 .    ? 34.984 87.882  -19.786 1.00 32.29 ? 1175 HOH A O   1 
HETATM 8435 O  O   . HOH F 6 .    ? 38.191 86.854  -17.321 1.00 30.23 ? 1176 HOH A O   1 
HETATM 8436 O  O   . HOH F 6 .    ? 40.204 85.918  -22.101 1.00 25.15 ? 1177 HOH A O   1 
HETATM 8437 O  O   . HOH F 6 .    ? 39.615 81.702  -22.206 1.00 32.33 ? 1178 HOH A O   1 
HETATM 8438 O  O   . HOH F 6 .    ? 41.842 79.371  -23.450 1.00 22.97 ? 1179 HOH A O   1 
HETATM 8439 O  O   . HOH F 6 .    ? 44.032 79.220  -21.506 1.00 32.09 ? 1180 HOH A O   1 
HETATM 8440 O  O   . HOH F 6 .    ? 46.689 80.363  -22.506 1.00 27.25 ? 1181 HOH A O   1 
HETATM 8441 O  O   . HOH F 6 .    ? 45.848 82.812  -25.470 1.00 32.36 ? 1182 HOH A O   1 
HETATM 8442 O  O   . HOH F 6 .    ? 43.455 81.057  -25.424 1.00 34.57 ? 1183 HOH A O   1 
HETATM 8443 O  O   . HOH F 6 .    ? 44.307 83.757  -27.869 1.00 23.48 ? 1184 HOH A O   1 
HETATM 8444 O  O   . HOH F 6 .    ? 44.821 82.628  -30.593 1.00 18.83 ? 1185 HOH A O   1 
HETATM 8445 O  O   . HOH F 6 .    ? 41.479 82.770  -28.951 1.00 29.17 ? 1186 HOH A O   1 
HETATM 8446 O  O   . HOH F 6 .    ? 40.517 82.946  -31.357 1.00 24.85 ? 1187 HOH A O   1 
HETATM 8447 O  O   . HOH F 6 .    ? 38.113 81.749  -31.454 1.00 11.03 ? 1188 HOH A O   1 
HETATM 8448 O  O   . HOH F 6 .    ? 39.071 83.128  -27.388 1.00 21.77 ? 1189 HOH A O   1 
HETATM 8449 O  O   . HOH F 6 .    ? 42.435 79.985  -31.751 1.00 29.02 ? 1190 HOH A O   1 
HETATM 8450 O  O   . HOH F 6 .    ? 42.781 78.424  -29.903 1.00 30.45 ? 1191 HOH A O   1 
HETATM 8451 O  O   . HOH F 6 .    ? 44.624 79.300  -33.378 1.00 18.75 ? 1192 HOH A O   1 
HETATM 8452 O  O   . HOH F 6 .    ? 47.979 74.490  -28.944 1.00 32.89 ? 1193 HOH A O   1 
HETATM 8453 O  O   . HOH F 6 .    ? 47.022 75.023  -26.397 1.00 34.40 ? 1194 HOH A O   1 
HETATM 8454 O  O   . HOH F 6 .    ? 47.248 73.107  -24.778 1.00 35.16 ? 1195 HOH A O   1 
HETATM 8455 O  O   . HOH F 6 .    ? 48.581 72.213  -26.300 1.00 25.93 ? 1196 HOH A O   1 
HETATM 8456 O  O   . HOH F 6 .    ? 50.288 73.519  -25.320 1.00 23.72 ? 1197 HOH A O   1 
HETATM 8457 O  O   . HOH F 6 .    ? 50.835 70.811  -23.630 1.00 16.69 ? 1198 HOH A O   1 
HETATM 8458 O  O   . HOH F 6 .    ? 49.669 73.399  -21.833 1.00 22.49 ? 1199 HOH A O   1 
HETATM 8459 O  O   . HOH F 6 .    ? 51.217 71.403  -20.244 1.00 17.08 ? 1200 HOH A O   1 
HETATM 8460 O  O   . HOH F 6 .    ? 53.563 72.601  -19.237 1.00 13.44 ? 1201 HOH A O   1 
HETATM 8461 O  O   . HOH F 6 .    ? 49.920 70.786  -17.624 1.00 25.88 ? 1202 HOH A O   1 
HETATM 8462 O  O   . HOH F 6 .    ? 47.462 69.927  -16.788 1.00 29.87 ? 1203 HOH A O   1 
HETATM 8463 O  O   . HOH F 6 .    ? 45.529 69.810  -18.564 1.00 24.09 ? 1204 HOH A O   1 
HETATM 8464 O  O   . HOH F 6 .    ? 46.936 72.502  -17.632 1.00 25.71 ? 1205 HOH A O   1 
HETATM 8465 O  O   . HOH F 6 .    ? 47.362 71.803  -20.269 1.00 20.46 ? 1206 HOH A O   1 
HETATM 8466 O  O   . HOH F 6 .    ? 46.833 68.138  -24.701 1.00 25.26 ? 1207 HOH A O   1 
HETATM 8467 O  O   . HOH F 6 .    ? 45.375 67.775  -27.724 1.00 17.97 ? 1208 HOH A O   1 
HETATM 8468 O  O   . HOH F 6 .    ? 45.865 65.454  -28.609 1.00 32.40 ? 1209 HOH A O   1 
HETATM 8469 O  O   . HOH F 6 .    ? 48.081 64.350  -28.550 1.00 20.67 ? 1210 HOH A O   1 
HETATM 8470 O  O   . HOH F 6 .    ? 48.034 64.816  -25.904 1.00 22.03 ? 1211 HOH A O   1 
HETATM 8471 O  O   . HOH F 6 .    ? 46.613 61.717  -25.991 1.00 17.10 ? 1212 HOH A O   1 
HETATM 8472 O  O   . HOH F 6 .    ? 47.760 59.250  -25.717 1.00 11.97 ? 1213 HOH A O   1 
HETATM 8473 O  O   . HOH F 6 .    ? 49.155 59.238  -28.663 1.00 16.31 ? 1214 HOH A O   1 
HETATM 8474 O  O   . HOH F 6 .    ? 49.865 58.370  -31.013 1.00 30.02 ? 1215 HOH A O   1 
HETATM 8475 O  O   . HOH F 6 .    ? 50.271 60.979  -31.153 1.00 15.75 ? 1216 HOH A O   1 
HETATM 8476 O  O   . HOH F 6 .    ? 49.551 61.908  -33.982 1.00 35.45 ? 1217 HOH A O   1 
HETATM 8477 O  O   . HOH F 6 .    ? 46.036 60.143  -30.964 1.00 48.11 ? 1218 HOH A O   1 
HETATM 8478 O  O   . HOH F 6 .    ? 47.319 61.326  -28.910 1.00 24.96 ? 1219 HOH A O   1 
HETATM 8479 O  O   . HOH F 6 .    ? 43.718 63.009  -28.709 1.00 8.82  ? 1220 HOH A O   1 
HETATM 8480 O  O   . HOH F 6 .    ? 41.547 61.241  -29.808 1.00 16.97 ? 1221 HOH A O   1 
HETATM 8481 O  O   . HOH F 6 .    ? 42.966 59.558  -31.512 1.00 21.79 ? 1222 HOH A O   1 
HETATM 8482 O  O   . HOH F 6 .    ? 42.766 56.771  -31.569 1.00 20.86 ? 1223 HOH A O   1 
HETATM 8483 O  O   . HOH F 6 .    ? 40.749 56.045  -33.354 1.00 24.18 ? 1224 HOH A O   1 
HETATM 8484 O  O   . HOH F 6 .    ? 38.526 55.184  -31.762 1.00 13.89 ? 1225 HOH A O   1 
HETATM 8485 O  O   . HOH F 6 .    ? 36.509 56.505  -32.864 1.00 31.87 ? 1226 HOH A O   1 
HETATM 8486 O  O   . HOH F 6 .    ? 36.958 58.961  -33.581 1.00 21.97 ? 1227 HOH A O   1 
HETATM 8487 O  O   . HOH F 6 .    ? 37.517 61.385  -32.543 1.00 22.30 ? 1228 HOH A O   1 
HETATM 8488 O  O   . HOH F 6 .    ? 40.147 62.471  -32.093 1.00 14.49 ? 1229 HOH A O   1 
HETATM 8489 O  O   . HOH F 6 .    ? 43.068 64.373  -31.543 1.00 29.91 ? 1230 HOH A O   1 
HETATM 8490 O  O   . HOH F 6 .    ? 42.948 68.450  -30.268 1.00 26.69 ? 1231 HOH A O   1 
HETATM 8491 O  O   . HOH F 6 .    ? 43.006 68.963  -28.015 1.00 35.84 ? 1232 HOH A O   1 
HETATM 8492 O  O   . HOH F 6 .    ? 43.333 68.246  -25.085 1.00 12.42 ? 1233 HOH A O   1 
HETATM 8493 O  O   . HOH F 6 .    ? 45.372 71.637  -25.964 1.00 33.01 ? 1234 HOH A O   1 
HETATM 8494 O  O   . HOH F 6 .    ? 47.036 68.466  -30.346 1.00 13.97 ? 1235 HOH A O   1 
HETATM 8495 O  O   . HOH F 6 .    ? 41.167 68.359  -32.657 1.00 12.95 ? 1236 HOH A O   1 
HETATM 8496 O  O   . HOH F 6 .    ? 39.307 69.116  -35.480 1.00 12.61 ? 1237 HOH A O   1 
HETATM 8497 O  O   . HOH F 6 .    ? 38.556 69.189  -38.252 1.00 14.48 ? 1238 HOH A O   1 
HETATM 8498 O  O   . HOH F 6 .    ? 34.243 66.273  -42.603 1.00 32.55 ? 1239 HOH A O   1 
HETATM 8499 O  O   . HOH F 6 .    ? 33.876 70.006  -45.120 1.00 34.15 ? 1240 HOH A O   1 
HETATM 8500 O  O   . HOH F 6 .    ? 31.071 69.171  -45.576 1.00 36.08 ? 1241 HOH A O   1 
HETATM 8501 O  O   . HOH F 6 .    ? 27.921 68.779  -46.682 1.00 34.20 ? 1242 HOH A O   1 
HETATM 8502 O  O   . HOH F 6 .    ? 23.140 65.892  -43.522 1.00 32.19 ? 1243 HOH A O   1 
HETATM 8503 O  O   . HOH F 6 .    ? 20.773 61.025  -40.421 1.00 32.42 ? 1244 HOH A O   1 
HETATM 8504 O  O   . HOH F 6 .    ? 18.997 60.481  -38.200 1.00 19.39 ? 1245 HOH A O   1 
HETATM 8505 O  O   . HOH F 6 .    ? 19.898 58.207  -36.997 1.00 32.15 ? 1246 HOH A O   1 
HETATM 8506 O  O   . HOH F 6 .    ? 20.706 58.876  -34.699 1.00 19.18 ? 1247 HOH A O   1 
HETATM 8507 O  O   . HOH F 6 .    ? 18.901 57.908  -32.973 1.00 21.72 ? 1248 HOH A O   1 
HETATM 8508 O  O   . HOH F 6 .    ? 19.319 54.883  -33.471 1.00 41.19 ? 1249 HOH A O   1 
HETATM 8509 O  O   . HOH F 6 .    ? 20.898 55.103  -35.783 1.00 28.26 ? 1250 HOH A O   1 
HETATM 8510 O  O   . HOH F 6 .    ? 22.423 56.802  -34.273 1.00 17.62 ? 1251 HOH A O   1 
HETATM 8511 O  O   . HOH F 6 .    ? 21.603 61.450  -34.943 1.00 20.46 ? 1252 HOH A O   1 
HETATM 8512 O  O   . HOH F 6 .    ? 22.230 63.449  -33.047 1.00 14.72 ? 1253 HOH A O   1 
HETATM 8513 O  O   . HOH F 6 .    ? 18.290 65.065  -26.914 1.00 20.87 ? 1254 HOH A O   1 
HETATM 8514 O  O   . HOH F 6 .    ? 17.098 67.376  -25.983 1.00 32.59 ? 1255 HOH A O   1 
HETATM 8515 O  O   . HOH F 6 .    ? 17.227 70.212  -23.459 1.00 15.87 ? 1256 HOH A O   1 
HETATM 8516 O  O   . HOH F 6 .    ? 14.525 70.477  -23.095 1.00 20.91 ? 1257 HOH A O   1 
HETATM 8517 O  O   . HOH F 6 .    ? 15.078 73.817  -22.114 1.00 34.34 ? 1258 HOH A O   1 
HETATM 8518 O  O   . HOH F 6 .    ? 15.950 75.208  -24.019 1.00 35.07 ? 1259 HOH A O   1 
HETATM 8519 O  O   . HOH F 6 .    ? 16.552 74.634  -28.729 1.00 45.56 ? 1260 HOH A O   1 
HETATM 8520 O  O   . HOH F 6 .    ? 18.735 70.514  -30.264 1.00 32.44 ? 1261 HOH A O   1 
HETATM 8521 O  O   . HOH F 6 .    ? 20.813 68.864  -31.689 1.00 38.24 ? 1262 HOH A O   1 
HETATM 8522 O  O   . HOH F 6 .    ? 22.766 78.680  -30.440 1.00 17.04 ? 1263 HOH A O   1 
HETATM 8523 O  O   . HOH F 6 .    ? 22.752 77.385  -27.421 1.00 26.24 ? 1264 HOH A O   1 
HETATM 8524 O  O   . HOH F 6 .    ? 23.252 78.503  -24.889 1.00 15.43 ? 1265 HOH A O   1 
HETATM 8525 O  O   . HOH F 6 .    ? 21.006 79.477  -23.702 1.00 19.07 ? 1266 HOH A O   1 
HETATM 8526 O  O   . HOH F 6 .    ? 19.305 79.209  -25.642 1.00 32.83 ? 1267 HOH A O   1 
HETATM 8527 O  O   . HOH F 6 .    ? 19.354 81.839  -27.525 1.00 38.15 ? 1268 HOH A O   1 
HETATM 8528 O  O   . HOH F 6 .    ? 19.046 83.398  -25.853 1.00 31.43 ? 1269 HOH A O   1 
HETATM 8529 O  O   . HOH F 6 .    ? 21.327 86.088  -31.004 1.00 34.30 ? 1270 HOH A O   1 
HETATM 8530 O  O   . HOH F 6 .    ? 23.225 87.008  -32.743 1.00 27.33 ? 1271 HOH A O   1 
HETATM 8531 O  O   . HOH F 6 .    ? 25.625 86.260  -32.010 1.00 16.46 ? 1272 HOH A O   1 
HETATM 8532 O  O   . HOH F 6 .    ? 27.139 89.787  -31.800 1.00 38.35 ? 1273 HOH A O   1 
HETATM 8533 O  O   . HOH F 6 .    ? 25.874 91.786  -32.316 1.00 38.39 ? 1274 HOH A O   1 
HETATM 8534 O  O   . HOH F 6 .    ? 26.680 91.747  -27.509 1.00 27.69 ? 1275 HOH A O   1 
HETATM 8535 O  O   . HOH F 6 .    ? 28.069 90.924  -25.311 1.00 19.11 ? 1276 HOH A O   1 
HETATM 8536 O  O   . HOH F 6 .    ? 29.497 88.805  -26.268 1.00 10.18 ? 1277 HOH A O   1 
HETATM 8537 O  O   . HOH F 6 .    ? 26.833 87.916  -23.715 1.00 21.02 ? 1278 HOH A O   1 
HETATM 8538 O  O   . HOH F 6 .    ? 25.165 88.862  -25.549 1.00 29.39 ? 1279 HOH A O   1 
HETATM 8539 O  O   . HOH F 6 .    ? 23.718 90.983  -26.141 1.00 36.68 ? 1280 HOH A O   1 
HETATM 8540 O  O   . HOH F 6 .    ? 21.567 86.263  -19.338 1.00 26.86 ? 1281 HOH A O   1 
HETATM 8541 O  O   . HOH F 6 .    ? 22.970 85.307  -17.074 1.00 32.87 ? 1282 HOH A O   1 
HETATM 8542 O  O   . HOH F 6 .    ? 24.833 83.182  -17.015 1.00 19.59 ? 1283 HOH A O   1 
HETATM 8543 O  O   . HOH F 6 .    ? 19.671 84.309  -18.329 1.00 26.26 ? 1284 HOH A O   1 
HETATM 8544 O  O   . HOH F 6 .    ? 17.503 81.518  -17.290 1.00 38.75 ? 1285 HOH A O   1 
HETATM 8545 O  O   . HOH F 6 .    ? 18.733 80.758  -11.750 1.00 30.07 ? 1286 HOH A O   1 
HETATM 8546 O  O   . HOH F 6 .    ? 15.611 79.857  -11.937 1.00 33.23 ? 1287 HOH A O   1 
HETATM 8547 O  O   . HOH F 6 .    ? 15.622 77.427  -13.630 1.00 29.54 ? 1288 HOH A O   1 
HETATM 8548 O  O   . HOH F 6 .    ? 15.754 75.377  -11.843 1.00 18.08 ? 1289 HOH A O   1 
HETATM 8549 O  O   . HOH F 6 .    ? 12.197 75.200  -13.534 1.00 26.84 ? 1290 HOH A O   1 
HETATM 8550 O  O   . HOH F 6 .    ? 12.753 74.873  -19.299 1.00 32.13 ? 1291 HOH A O   1 
HETATM 8551 O  O   . HOH F 6 .    ? 16.019 72.119  -19.006 1.00 15.19 ? 1292 HOH A O   1 
HETATM 8552 O  O   . HOH F 6 .    ? 17.024 70.391  -16.381 1.00 9.62  ? 1293 HOH A O   1 
HETATM 8553 O  O   . HOH F 6 .    ? 16.419 67.948  -19.871 1.00 16.03 ? 1294 HOH A O   1 
HETATM 8554 O  O   . HOH F 6 .    ? 20.446 66.235  -19.663 1.00 10.86 ? 1295 HOH A O   1 
HETATM 8555 O  O   . HOH F 6 .    ? 14.337 63.920  -16.392 1.00 12.75 ? 1296 HOH A O   1 
HETATM 8556 O  O   . HOH F 6 .    ? 14.427 61.961  -14.469 1.00 18.85 ? 1297 HOH A O   1 
HETATM 8557 O  O   . HOH F 6 .    ? 14.126 62.961  -12.161 1.00 19.45 ? 1298 HOH A O   1 
HETATM 8558 O  O   . HOH F 6 .    ? 12.377 64.750  -12.398 1.00 33.16 ? 1299 HOH A O   1 
HETATM 8559 O  O   . HOH F 6 .    ? 10.571 62.570  -12.190 1.00 29.53 ? 1300 HOH A O   1 
HETATM 8560 O  O   . HOH F 6 .    ? 10.189 62.864  -14.780 1.00 37.79 ? 1301 HOH A O   1 
HETATM 8561 O  O   . HOH F 6 .    ? 8.675  65.081  -14.951 1.00 28.01 ? 1302 HOH A O   1 
HETATM 8562 O  O   . HOH F 6 .    ? 11.600 63.524  -16.888 1.00 21.70 ? 1303 HOH A O   1 
HETATM 8563 O  O   . HOH F 6 .    ? 11.287 61.232  -18.392 1.00 19.02 ? 1304 HOH A O   1 
HETATM 8564 O  O   . HOH F 6 .    ? 13.307 62.352  -19.969 1.00 14.52 ? 1305 HOH A O   1 
HETATM 8565 O  O   . HOH F 6 .    ? 13.761 60.787  -22.430 1.00 12.75 ? 1306 HOH A O   1 
HETATM 8566 O  O   . HOH F 6 .    ? 12.073 61.272  -24.284 1.00 19.64 ? 1307 HOH A O   1 
HETATM 8567 O  O   . HOH F 6 .    ? 14.847 63.728  -25.834 1.00 18.74 ? 1308 HOH A O   1 
HETATM 8568 O  O   . HOH F 6 .    ? 16.628 60.638  -28.220 1.00 13.52 ? 1309 HOH A O   1 
HETATM 8569 O  O   . HOH F 6 .    ? 14.706 54.565  -26.328 1.00 24.47 ? 1310 HOH A O   1 
HETATM 8570 O  O   . HOH F 6 .    ? 16.358 52.916  -22.578 1.00 26.95 ? 1311 HOH A O   1 
HETATM 8571 O  O   . HOH F 6 .    ? 16.855 50.743  -19.418 1.00 19.91 ? 1312 HOH A O   1 
HETATM 8572 O  O   . HOH F 6 .    ? 18.293 48.709  -19.930 1.00 33.38 ? 1313 HOH A O   1 
HETATM 8573 O  O   . HOH F 6 .    ? 21.306 46.713  -17.517 1.00 27.28 ? 1314 HOH A O   1 
HETATM 8574 O  O   . HOH F 6 .    ? 23.491 45.988  -15.920 1.00 20.62 ? 1315 HOH A O   1 
HETATM 8575 O  O   . HOH F 6 .    ? 22.539 45.307  -13.505 1.00 18.75 ? 1316 HOH A O   1 
HETATM 8576 O  O   . HOH F 6 .    ? 21.884 42.684  -13.202 1.00 29.10 ? 1317 HOH A O   1 
HETATM 8577 O  O   . HOH F 6 .    ? 24.056 42.149  -14.408 1.00 23.83 ? 1318 HOH A O   1 
HETATM 8578 O  O   . HOH F 6 .    ? 26.633 41.583  -13.205 1.00 11.80 ? 1319 HOH A O   1 
HETATM 8579 O  O   . HOH F 6 .    ? 28.747 42.737  -11.896 1.00 9.96  ? 1320 HOH A O   1 
HETATM 8580 O  O   . HOH F 6 .    ? 24.262 39.049  -11.480 1.00 23.42 ? 1321 HOH A O   1 
HETATM 8581 O  O   . HOH F 6 .    ? 22.171 40.690  -11.274 1.00 28.74 ? 1322 HOH A O   1 
HETATM 8582 O  O   . HOH F 6 .    ? 21.759 40.380  -8.760  1.00 27.42 ? 1323 HOH A O   1 
HETATM 8583 O  O   . HOH F 6 .    ? 20.572 42.679  -7.426  1.00 20.48 ? 1324 HOH A O   1 
HETATM 8584 O  O   . HOH F 6 .    ? 19.569 41.581  -4.961  1.00 24.77 ? 1325 HOH A O   1 
HETATM 8585 O  O   . HOH F 6 .    ? 19.099 42.792  -2.530  1.00 28.04 ? 1326 HOH A O   1 
HETATM 8586 O  O   . HOH F 6 .    ? 16.506 43.049  -2.428  1.00 29.79 ? 1327 HOH A O   1 
HETATM 8587 O  O   . HOH F 6 .    ? 13.318 48.334  1.460   1.00 29.01 ? 1328 HOH A O   1 
HETATM 8588 O  O   . HOH F 6 .    ? 14.267 50.846  1.027   1.00 26.29 ? 1329 HOH A O   1 
HETATM 8589 O  O   . HOH F 6 .    ? 13.330 50.955  -1.670  1.00 21.13 ? 1330 HOH A O   1 
HETATM 8590 O  O   . HOH F 6 .    ? 11.522 48.636  -2.450  1.00 30.26 ? 1331 HOH A O   1 
HETATM 8591 O  O   . HOH F 6 .    ? 10.267 51.277  -0.597  1.00 21.93 ? 1332 HOH A O   1 
HETATM 8592 O  O   . HOH F 6 .    ? 10.360 51.886  2.314   1.00 32.13 ? 1333 HOH A O   1 
HETATM 8593 O  O   . HOH F 6 .    ? 13.298 53.603  1.767   1.00 15.56 ? 1334 HOH A O   1 
HETATM 8594 O  O   . HOH F 6 .    ? 13.705 54.219  4.371   1.00 13.37 ? 1335 HOH A O   1 
HETATM 8595 O  O   . HOH F 6 .    ? 12.282 56.328  5.348   1.00 13.81 ? 1336 HOH A O   1 
HETATM 8596 O  O   . HOH F 6 .    ? 11.553 58.789  7.734   1.00 24.06 ? 1337 HOH A O   1 
HETATM 8597 O  O   . HOH F 6 .    ? 9.687  59.998  6.581   1.00 39.25 ? 1338 HOH A O   1 
HETATM 8598 O  O   . HOH F 6 .    ? 13.594 60.883  7.741   1.00 24.27 ? 1339 HOH A O   1 
HETATM 8599 O  O   . HOH F 6 .    ? 14.310 60.133  5.189   1.00 11.83 ? 1340 HOH A O   1 
HETATM 8600 O  O   . HOH F 6 .    ? 10.145 62.269  2.141   1.00 30.60 ? 1341 HOH A O   1 
HETATM 8601 O  O   . HOH F 6 .    ? 7.538  58.358  -0.079  1.00 27.49 ? 1342 HOH A O   1 
HETATM 8602 O  O   . HOH F 6 .    ? 10.124 58.066  -3.342  1.00 27.52 ? 1343 HOH A O   1 
HETATM 8603 O  O   . HOH F 6 .    ? 11.604 59.612  -5.031  1.00 17.54 ? 1344 HOH A O   1 
HETATM 8604 O  O   . HOH F 6 .    ? 13.945 59.896  -3.440  1.00 13.27 ? 1345 HOH A O   1 
HETATM 8605 O  O   . HOH F 6 .    ? 12.676 62.095  -2.440  1.00 24.33 ? 1346 HOH A O   1 
HETATM 8606 O  O   . HOH F 6 .    ? 13.878 58.063  -1.399  1.00 18.68 ? 1347 HOH A O   1 
HETATM 8607 O  O   . HOH F 6 .    ? 8.688  55.084  -6.086  1.00 20.42 ? 1348 HOH A O   1 
HETATM 8608 O  O   . HOH F 6 .    ? 7.974  53.119  -7.699  1.00 29.20 ? 1349 HOH A O   1 
HETATM 8609 O  O   . HOH F 6 .    ? 7.308  54.449  -10.090 1.00 31.14 ? 1350 HOH A O   1 
HETATM 8610 O  O   . HOH F 6 .    ? 8.482  57.704  -6.840  1.00 20.74 ? 1351 HOH A O   1 
HETATM 8611 O  O   . HOH F 6 .    ? 4.266  56.294  -6.568  1.00 23.46 ? 1352 HOH A O   1 
HETATM 8612 O  O   . HOH F 6 .    ? 11.726 55.044  -12.395 1.00 15.93 ? 1353 HOH A O   1 
HETATM 8613 O  O   . HOH F 6 .    ? 12.130 55.780  -15.111 1.00 18.62 ? 1354 HOH A O   1 
HETATM 8614 O  O   . HOH F 6 .    ? 14.184 54.368  -16.192 1.00 15.52 ? 1355 HOH A O   1 
HETATM 8615 O  O   . HOH F 6 .    ? 13.256 52.020  -15.167 1.00 29.99 ? 1356 HOH A O   1 
HETATM 8616 O  O   . HOH F 6 .    ? 12.603 51.786  -12.029 1.00 28.52 ? 1357 HOH A O   1 
HETATM 8617 O  O   . HOH F 6 .    ? 18.486 51.064  -12.466 1.00 10.36 ? 1358 HOH A O   1 
HETATM 8618 O  O   . HOH F 6 .    ? 19.548 53.543  -11.806 1.00 10.16 ? 1359 HOH A O   1 
HETATM 8619 O  O   . HOH F 6 .    ? 22.190 54.401  -12.034 1.00 9.64  ? 1360 HOH A O   1 
HETATM 8620 O  O   . HOH F 6 .    ? 24.613 52.956  -11.779 1.00 7.88  ? 1361 HOH A O   1 
HETATM 8621 O  O   . HOH F 6 .    ? 25.476 51.256  -9.517  1.00 10.49 ? 1362 HOH A O   1 
HETATM 8622 O  O   . HOH F 6 .    ? 22.859 51.801  -8.622  1.00 15.16 ? 1363 HOH A O   1 
HETATM 8623 O  O   . HOH F 6 .    ? 24.038 53.230  -6.275  1.00 17.07 ? 1364 HOH A O   1 
HETATM 8624 O  O   . HOH F 6 .    ? 23.217 54.021  -3.652  1.00 11.73 ? 1365 HOH A O   1 
HETATM 8625 O  O   . HOH F 6 .    ? 24.234 55.735  -1.800  1.00 11.41 ? 1366 HOH A O   1 
HETATM 8626 O  O   . HOH F 6 .    ? 20.473 57.435  -5.304  1.00 8.97  ? 1367 HOH A O   1 
HETATM 8627 O  O   . HOH F 6 .    ? 21.420 58.001  -7.852  1.00 8.51  ? 1368 HOH A O   1 
HETATM 8628 O  O   . HOH F 6 .    ? 19.715 57.448  -11.827 1.00 12.87 ? 1369 HOH A O   1 
HETATM 8629 O  O   . HOH F 6 .    ? 25.986 49.626  -13.704 1.00 8.36  ? 1370 HOH A O   1 
HETATM 8630 O  O   . HOH F 6 .    ? 26.159 48.935  -10.977 1.00 9.27  ? 1371 HOH A O   1 
HETATM 8631 O  O   . HOH F 6 .    ? 31.637 47.047  -8.071  1.00 7.28  ? 1372 HOH A O   1 
HETATM 8632 O  O   . HOH F 6 .    ? 33.372 48.131  -10.126 1.00 7.65  ? 1373 HOH A O   1 
HETATM 8633 O  O   . HOH F 6 .    ? 35.024 48.256  -16.418 1.00 32.30 ? 1374 HOH A O   1 
HETATM 8634 O  O   . HOH F 6 .    ? 35.075 50.582  -17.603 1.00 12.86 ? 1375 HOH A O   1 
HETATM 8635 O  O   . HOH F 6 .    ? 37.478 51.558  -18.542 1.00 16.88 ? 1376 HOH A O   1 
HETATM 8636 O  O   . HOH F 6 .    ? 37.515 52.138  -21.154 1.00 10.08 ? 1377 HOH A O   1 
HETATM 8637 O  O   . HOH F 6 .    ? 39.574 53.953  -20.803 1.00 12.56 ? 1378 HOH A O   1 
HETATM 8638 O  O   . HOH F 6 .    ? 39.958 56.242  -19.148 1.00 23.38 ? 1379 HOH A O   1 
HETATM 8639 O  O   . HOH F 6 .    ? 41.400 54.837  -17.248 1.00 27.96 ? 1380 HOH A O   1 
HETATM 8640 O  O   . HOH F 6 .    ? 40.944 52.278  -16.909 1.00 12.39 ? 1381 HOH A O   1 
HETATM 8641 O  O   . HOH F 6 .    ? 38.436 54.294  -17.546 1.00 29.50 ? 1382 HOH A O   1 
HETATM 8642 O  O   . HOH F 6 .    ? 39.577 58.892  -18.089 1.00 20.15 ? 1383 HOH A O   1 
HETATM 8643 O  O   . HOH F 6 .    ? 41.618 58.685  -16.054 1.00 13.96 ? 1384 HOH A O   1 
HETATM 8644 O  O   . HOH F 6 .    ? 44.450 58.755  -15.997 1.00 14.67 ? 1385 HOH A O   1 
HETATM 8645 O  O   . HOH F 6 .    ? 44.412 56.057  -15.391 1.00 15.52 ? 1386 HOH A O   1 
HETATM 8646 O  O   . HOH F 6 .    ? 47.223 55.776  -15.366 1.00 14.60 ? 1387 HOH A O   1 
HETATM 8647 O  O   . HOH F 6 .    ? 46.518 57.345  -18.750 1.00 12.42 ? 1388 HOH A O   1 
HETATM 8648 O  O   . HOH F 6 .    ? 45.621 59.975  -18.321 1.00 11.95 ? 1389 HOH A O   1 
HETATM 8649 O  O   . HOH F 6 .    ? 42.896 59.545  -18.876 1.00 21.79 ? 1390 HOH A O   1 
HETATM 8650 O  O   . HOH F 6 .    ? 44.628 54.953  -18.043 1.00 17.95 ? 1391 HOH A O   1 
HETATM 8651 O  O   . HOH F 6 .    ? 45.879 52.725  -19.153 1.00 18.15 ? 1392 HOH A O   1 
HETATM 8652 O  O   . HOH F 6 .    ? 46.548 53.919  -20.925 1.00 26.90 ? 1393 HOH A O   1 
HETATM 8653 O  O   . HOH F 6 .    ? 48.507 54.884  -22.769 1.00 14.72 ? 1394 HOH A O   1 
HETATM 8654 O  O   . HOH F 6 .    ? 46.809 55.809  -25.495 1.00 13.86 ? 1395 HOH A O   1 
HETATM 8655 O  O   . HOH F 6 .    ? 43.813 54.967  -26.818 1.00 26.64 ? 1396 HOH A O   1 
HETATM 8656 O  O   . HOH F 6 .    ? 49.727 55.035  -29.105 1.00 14.88 ? 1397 HOH A O   1 
HETATM 8657 O  O   . HOH F 6 .    ? 51.062 52.712  -28.719 1.00 16.66 ? 1398 HOH A O   1 
HETATM 8658 O  O   . HOH F 6 .    ? 53.365 53.223  -30.191 1.00 25.01 ? 1399 HOH A O   1 
HETATM 8659 O  O   . HOH F 6 .    ? 53.088 54.984  -31.974 1.00 32.49 ? 1400 HOH A O   1 
HETATM 8660 O  O   . HOH F 6 .    ? 51.959 56.286  -30.364 1.00 19.51 ? 1401 HOH A O   1 
HETATM 8661 O  O   . HOH F 6 .    ? 48.819 50.747  -29.605 1.00 19.89 ? 1402 HOH A O   1 
HETATM 8662 O  O   . HOH F 6 .    ? 49.862 46.685  -30.700 1.00 28.91 ? 1403 HOH A O   1 
HETATM 8663 O  O   . HOH F 6 .    ? 52.474 45.429  -27.279 1.00 27.42 ? 1404 HOH A O   1 
HETATM 8664 O  O   . HOH F 6 .    ? 53.167 47.015  -25.082 1.00 16.36 ? 1405 HOH A O   1 
HETATM 8665 O  O   . HOH F 6 .    ? 50.385 45.019  -24.826 1.00 23.10 ? 1406 HOH A O   1 
HETATM 8666 O  O   . HOH F 6 .    ? 53.782 40.629  -20.498 1.00 33.17 ? 1407 HOH A O   1 
HETATM 8667 O  O   . HOH F 6 .    ? 56.838 38.954  -19.337 1.00 32.30 ? 1408 HOH A O   1 
HETATM 8668 O  O   . HOH F 6 .    ? 56.870 43.107  -20.000 1.00 20.25 ? 1409 HOH A O   1 
HETATM 8669 O  O   . HOH F 6 .    ? 56.436 46.127  -17.333 1.00 13.22 ? 1410 HOH A O   1 
HETATM 8670 O  O   . HOH F 6 .    ? 62.069 48.104  -20.969 1.00 36.43 ? 1411 HOH A O   1 
HETATM 8671 O  O   . HOH F 6 .    ? 62.828 42.693  -20.968 1.00 27.05 ? 1412 HOH A O   1 
HETATM 8672 O  O   . HOH F 6 .    ? 68.922 41.575  -17.017 1.00 34.68 ? 1413 HOH A O   1 
HETATM 8673 O  O   . HOH F 6 .    ? 70.901 43.040  -15.264 1.00 29.28 ? 1414 HOH A O   1 
HETATM 8674 O  O   . HOH F 6 .    ? 72.863 43.143  -12.453 1.00 46.15 ? 1415 HOH A O   1 
HETATM 8675 O  O   . HOH F 6 .    ? 72.089 47.264  -17.893 1.00 32.74 ? 1416 HOH A O   1 
HETATM 8676 O  O   . HOH F 6 .    ? 68.543 46.973  -16.633 1.00 31.30 ? 1417 HOH A O   1 
HETATM 8677 O  O   . HOH F 6 .    ? 63.722 50.078  -13.975 1.00 11.78 ? 1418 HOH A O   1 
HETATM 8678 O  O   . HOH F 6 .    ? 70.483 52.195  -12.518 1.00 20.28 ? 1419 HOH A O   1 
HETATM 8679 O  O   . HOH F 6 .    ? 69.845 53.440  -10.377 1.00 33.71 ? 1420 HOH A O   1 
HETATM 8680 O  O   . HOH F 6 .    ? 70.091 56.286  -12.491 1.00 33.03 ? 1421 HOH A O   1 
HETATM 8681 O  O   . HOH F 6 .    ? 72.144 58.786  -11.326 1.00 20.31 ? 1422 HOH A O   1 
HETATM 8682 O  O   . HOH F 6 .    ? 74.269 60.037  -9.605  1.00 33.18 ? 1423 HOH A O   1 
HETATM 8683 O  O   . HOH F 6 .    ? 72.971 65.011  -7.747  1.00 18.46 ? 1424 HOH A O   1 
HETATM 8684 O  O   . HOH F 6 .    ? 73.067 66.426  -10.124 1.00 18.55 ? 1425 HOH A O   1 
HETATM 8685 O  O   . HOH F 6 .    ? 77.514 66.229  -11.946 1.00 34.85 ? 1426 HOH A O   1 
HETATM 8686 O  O   . HOH F 6 .    ? 78.581 68.589  -12.505 1.00 31.48 ? 1427 HOH A O   1 
HETATM 8687 O  O   . HOH F 6 .    ? 78.998 70.030  -10.405 1.00 35.12 ? 1428 HOH A O   1 
HETATM 8688 O  O   . HOH F 6 .    ? 81.013 68.661  -11.451 1.00 24.86 ? 1429 HOH A O   1 
HETATM 8689 O  O   . HOH F 6 .    ? 81.412 67.165  -13.556 1.00 19.87 ? 1430 HOH A O   1 
HETATM 8690 O  O   . HOH F 6 .    ? 83.250 66.445  -15.380 1.00 16.47 ? 1431 HOH A O   1 
HETATM 8691 O  O   . HOH F 6 .    ? 84.119 68.295  -17.301 1.00 12.88 ? 1432 HOH A O   1 
HETATM 8692 O  O   . HOH F 6 .    ? 83.341 70.208  -20.277 1.00 19.53 ? 1433 HOH A O   1 
HETATM 8693 O  O   . HOH F 6 .    ? 83.340 67.614  -22.940 1.00 20.90 ? 1434 HOH A O   1 
HETATM 8694 O  O   . HOH F 6 .    ? 80.251 64.042  -21.359 1.00 16.24 ? 1435 HOH A O   1 
HETATM 8695 O  O   . HOH F 6 .    ? 78.747 62.384  -22.961 1.00 29.29 ? 1436 HOH A O   1 
HETATM 8696 O  O   . HOH F 6 .    ? 72.723 63.915  -21.155 1.00 24.95 ? 1437 HOH A O   1 
HETATM 8697 O  O   . HOH F 6 .    ? 70.155 61.772  -20.486 1.00 31.22 ? 1438 HOH A O   1 
HETATM 8698 O  O   . HOH F 6 .    ? 71.707 62.601  -18.107 1.00 28.74 ? 1439 HOH A O   1 
HETATM 8699 O  O   . HOH F 6 .    ? 73.877 65.811  -17.660 1.00 13.38 ? 1440 HOH A O   1 
HETATM 8700 O  O   . HOH F 6 .    ? 74.608 64.349  -15.496 1.00 31.35 ? 1441 HOH A O   1 
HETATM 8701 O  O   . HOH F 6 .    ? 69.977 69.836  -12.592 1.00 11.73 ? 1442 HOH A O   1 
HETATM 8702 O  O   . HOH F 6 .    ? 66.472 71.483  -6.851  1.00 18.97 ? 1443 HOH A O   1 
HETATM 8703 O  O   . HOH F 6 .    ? 64.066 70.659  -5.336  1.00 14.97 ? 1444 HOH A O   1 
HETATM 8704 O  O   . HOH F 6 .    ? 66.708 74.482  -4.461  1.00 24.66 ? 1445 HOH A O   1 
HETATM 8705 O  O   . HOH F 6 .    ? 65.344 76.926  -3.654  1.00 26.95 ? 1446 HOH A O   1 
HETATM 8706 O  O   . HOH F 6 .    ? 65.437 78.662  -5.740  1.00 27.07 ? 1447 HOH A O   1 
HETATM 8707 O  O   . HOH F 6 .    ? 65.209 79.772  -8.963  1.00 32.97 ? 1448 HOH A O   1 
HETATM 8708 O  O   . HOH F 6 .    ? 66.942 81.326  -11.396 1.00 29.00 ? 1449 HOH A O   1 
HETATM 8709 O  O   . HOH F 6 .    ? 66.396 81.746  -14.295 1.00 26.85 ? 1450 HOH A O   1 
HETATM 8710 O  O   . HOH F 6 .    ? 63.538 82.016  -14.380 1.00 36.81 ? 1451 HOH A O   1 
HETATM 8711 O  O   . HOH F 6 .    ? 62.220 82.869  -17.409 1.00 40.43 ? 1452 HOH A O   1 
HETATM 8712 O  O   . HOH F 6 .    ? 61.982 80.738  -18.901 1.00 23.58 ? 1453 HOH A O   1 
HETATM 8713 O  O   . HOH F 6 .    ? 62.860 83.199  -21.175 1.00 41.45 ? 1454 HOH A O   1 
HETATM 8714 O  O   . HOH F 6 .    ? 62.430 85.241  -23.094 1.00 26.12 ? 1455 HOH A O   1 
HETATM 8715 O  O   . HOH F 6 .    ? 65.662 84.781  -22.659 1.00 30.47 ? 1456 HOH A O   1 
HETATM 8716 O  O   . HOH F 6 .    ? 65.160 87.810  -24.152 1.00 22.97 ? 1457 HOH A O   1 
HETATM 8717 O  O   . HOH F 6 .    ? 67.801 88.165  -23.553 1.00 23.99 ? 1458 HOH A O   1 
HETATM 8718 O  O   . HOH F 6 .    ? 71.687 84.558  -20.162 1.00 28.09 ? 1459 HOH A O   1 
HETATM 8719 O  O   . HOH F 6 .    ? 73.310 82.298  -21.191 1.00 25.08 ? 1460 HOH A O   1 
HETATM 8720 O  O   . HOH F 6 .    ? 74.408 76.789  -20.200 1.00 29.59 ? 1461 HOH A O   1 
HETATM 8721 O  O   . HOH F 6 .    ? 73.044 76.758  -18.262 1.00 33.68 ? 1462 HOH A O   1 
HETATM 8722 O  O   . HOH F 6 .    ? 75.207 74.069  -19.402 1.00 16.79 ? 1463 HOH A O   1 
HETATM 8723 O  O   . HOH F 6 .    ? 77.680 74.969  -18.629 1.00 39.76 ? 1464 HOH A O   1 
HETATM 8724 O  O   . HOH F 6 .    ? 79.728 73.963  -17.853 1.00 23.88 ? 1465 HOH A O   1 
HETATM 8725 O  O   . HOH F 6 .    ? 74.634 76.702  -13.937 1.00 25.53 ? 1466 HOH A O   1 
HETATM 8726 O  O   . HOH F 6 .    ? 74.039 80.154  -11.023 1.00 40.84 ? 1467 HOH A O   1 
HETATM 8727 O  O   . HOH F 6 .    ? 75.342 75.989  -5.853  1.00 38.48 ? 1468 HOH A O   1 
HETATM 8728 O  O   . HOH F 6 .    ? 73.714 74.029  -5.710  1.00 21.52 ? 1469 HOH A O   1 
HETATM 8729 O  O   . HOH F 6 .    ? 77.846 72.500  -10.479 1.00 25.49 ? 1470 HOH A O   1 
HETATM 8730 O  O   . HOH F 6 .    ? 68.533 78.898  -18.030 1.00 23.97 ? 1471 HOH A O   1 
HETATM 8731 O  O   . HOH F 6 .    ? 67.745 78.871  -25.372 1.00 10.43 ? 1472 HOH A O   1 
HETATM 8732 O  O   . HOH F 6 .    ? 67.748 81.643  -25.722 1.00 10.50 ? 1473 HOH A O   1 
HETATM 8733 O  O   . HOH F 6 .    ? 68.306 79.361  -28.610 1.00 14.95 ? 1474 HOH A O   1 
HETATM 8734 O  O   . HOH F 6 .    ? 70.770 80.451  -27.732 1.00 35.60 ? 1475 HOH A O   1 
HETATM 8735 O  O   . HOH F 6 .    ? 70.530 78.060  -26.240 1.00 18.27 ? 1476 HOH A O   1 
HETATM 8736 O  O   . HOH F 6 .    ? 72.232 75.881  -27.077 1.00 30.31 ? 1477 HOH A O   1 
HETATM 8737 O  O   . HOH F 6 .    ? 71.688 73.674  -29.207 1.00 24.72 ? 1478 HOH A O   1 
HETATM 8738 O  O   . HOH F 6 .    ? 76.589 74.043  -26.755 1.00 28.04 ? 1479 HOH A O   1 
HETATM 8739 O  O   . HOH F 6 .    ? 69.273 76.984  -34.113 1.00 26.02 ? 1480 HOH A O   1 
HETATM 8740 O  O   . HOH F 6 .    ? 67.937 75.046  -35.147 1.00 27.12 ? 1481 HOH A O   1 
HETATM 8741 O  O   . HOH F 6 .    ? 67.914 77.132  -38.612 1.00 39.65 ? 1482 HOH A O   1 
HETATM 8742 O  O   . HOH F 6 .    ? 69.931 74.040  -40.021 1.00 60.30 ? 1483 HOH A O   1 
HETATM 8743 O  O   . HOH F 6 .    ? 63.995 78.551  -38.027 1.00 26.82 ? 1484 HOH A O   1 
HETATM 8744 O  O   . HOH F 6 .    ? 64.249 77.825  -35.417 1.00 12.29 ? 1485 HOH A O   1 
HETATM 8745 O  O   . HOH F 6 .    ? 68.298 79.560  -34.864 1.00 23.86 ? 1486 HOH A O   1 
HETATM 8746 O  O   . HOH F 6 .    ? 69.671 82.044  -34.133 1.00 32.76 ? 1487 HOH A O   1 
HETATM 8747 O  O   . HOH F 6 .    ? 69.407 83.723  -36.138 1.00 29.49 ? 1488 HOH A O   1 
HETATM 8748 O  O   . HOH F 6 .    ? 67.361 85.584  -36.481 1.00 30.55 ? 1489 HOH A O   1 
HETATM 8749 O  O   . HOH F 6 .    ? 68.077 88.116  -35.332 1.00 31.72 ? 1490 HOH A O   1 
HETATM 8750 O  O   . HOH F 6 .    ? 65.478 87.506  -41.427 1.00 39.09 ? 1491 HOH A O   1 
HETATM 8751 O  O   . HOH F 6 .    ? 61.745 83.098  -38.399 1.00 25.56 ? 1492 HOH A O   1 
HETATM 8752 O  O   . HOH F 6 .    ? 60.620 78.811  -41.665 1.00 27.46 ? 1493 HOH A O   1 
HETATM 8753 O  O   . HOH F 6 .    ? 61.304 76.620  -39.888 1.00 18.13 ? 1494 HOH A O   1 
HETATM 8754 O  O   . HOH F 6 .    ? 58.353 77.198  -38.636 1.00 12.05 ? 1495 HOH A O   1 
HETATM 8755 O  O   . HOH F 6 .    ? 51.308 76.208  -40.946 1.00 22.43 ? 1496 HOH A O   1 
HETATM 8756 O  O   . HOH F 6 .    ? 47.453 78.989  -40.624 1.00 16.91 ? 1497 HOH A O   1 
HETATM 8757 O  O   . HOH F 6 .    ? 46.489 80.298  -42.759 1.00 28.11 ? 1498 HOH A O   1 
HETATM 8758 O  O   . HOH F 6 .    ? 43.865 79.909  -42.640 1.00 29.99 ? 1499 HOH A O   1 
HETATM 8759 O  O   . HOH F 6 .    ? 44.825 82.983  -43.422 1.00 38.25 ? 1500 HOH A O   1 
HETATM 8760 O  O   . HOH F 6 .    ? 49.845 82.372  -44.061 1.00 16.51 ? 1501 HOH A O   1 
HETATM 8761 O  O   . HOH F 6 .    ? 54.269 82.616  -44.792 1.00 45.08 ? 1502 HOH A O   1 
HETATM 8762 O  O   . HOH F 6 .    ? 59.208 86.977  -45.913 1.00 38.58 ? 1503 HOH A O   1 
HETATM 8763 O  O   . HOH F 6 .    ? 56.623 89.809  -43.797 1.00 32.25 ? 1504 HOH A O   1 
HETATM 8764 O  O   . HOH F 6 .    ? 53.638 92.732  -40.936 1.00 37.39 ? 1505 HOH A O   1 
HETATM 8765 O  O   . HOH F 6 .    ? 61.082 92.803  -39.034 1.00 49.76 ? 1506 HOH A O   1 
HETATM 8766 O  O   . HOH F 6 .    ? 61.503 90.697  -37.136 1.00 47.13 ? 1507 HOH A O   1 
HETATM 8767 O  O   . HOH F 6 .    ? 59.568 91.171  -35.504 1.00 23.11 ? 1508 HOH A O   1 
HETATM 8768 O  O   . HOH F 6 .    ? 60.286 91.097  -31.389 1.00 25.75 ? 1509 HOH A O   1 
HETATM 8769 O  O   . HOH F 6 .    ? 60.514 91.847  -28.432 1.00 25.44 ? 1510 HOH A O   1 
HETATM 8770 O  O   . HOH F 6 .    ? 58.434 92.997  -26.851 1.00 28.74 ? 1511 HOH A O   1 
HETATM 8771 O  O   . HOH F 6 .    ? 58.154 93.214  -24.587 1.00 24.41 ? 1512 HOH A O   1 
HETATM 8772 O  O   . HOH F 6 .    ? 56.330 91.000  -25.748 1.00 21.26 ? 1513 HOH A O   1 
HETATM 8773 O  O   . HOH F 6 .    ? 54.949 90.228  -23.467 1.00 32.23 ? 1514 HOH A O   1 
HETATM 8774 O  O   . HOH F 6 .    ? 52.688 91.980  -23.384 1.00 30.08 ? 1515 HOH A O   1 
HETATM 8775 O  O   . HOH F 6 .    ? 54.240 93.516  -25.037 1.00 35.44 ? 1516 HOH A O   1 
HETATM 8776 O  O   . HOH F 6 .    ? 49.522 92.153  -25.017 1.00 30.47 ? 1517 HOH A O   1 
HETATM 8777 O  O   . HOH F 6 .    ? 50.835 90.650  -21.574 1.00 35.86 ? 1518 HOH A O   1 
HETATM 8778 O  O   . HOH F 6 .    ? 53.118 86.859  -21.370 1.00 25.69 ? 1519 HOH A O   1 
HETATM 8779 O  O   . HOH F 6 .    ? 56.615 87.588  -19.931 1.00 30.47 ? 1520 HOH A O   1 
HETATM 8780 O  O   . HOH F 6 .    ? 54.884 80.523  -19.327 1.00 26.85 ? 1521 HOH A O   1 
HETATM 8781 O  O   . HOH F 6 .    ? 52.541 79.019  -17.503 1.00 19.80 ? 1522 HOH A O   1 
HETATM 8782 O  O   . HOH F 6 .    ? 50.548 79.062  -15.638 1.00 21.43 ? 1523 HOH A O   1 
HETATM 8783 O  O   . HOH F 6 .    ? 47.416 79.618  -18.475 1.00 19.44 ? 1524 HOH A O   1 
HETATM 8784 O  O   . HOH F 6 .    ? 47.279 81.430  -17.077 1.00 24.13 ? 1525 HOH A O   1 
HETATM 8785 O  O   . HOH F 6 .    ? 49.656 84.077  -19.002 1.00 29.72 ? 1526 HOH A O   1 
HETATM 8786 O  O   . HOH F 6 .    ? 45.714 85.206  -19.036 1.00 34.08 ? 1527 HOH A O   1 
HETATM 8787 O  O   . HOH F 6 .    ? 46.986 89.679  -23.463 1.00 37.07 ? 1528 HOH A O   1 
HETATM 8788 O  O   . HOH F 6 .    ? 45.238 90.086  -25.630 1.00 18.81 ? 1529 HOH A O   1 
HETATM 8789 O  O   . HOH F 6 .    ? 44.880 92.560  -25.286 1.00 34.74 ? 1530 HOH A O   1 
HETATM 8790 O  O   . HOH F 6 .    ? 45.683 95.166  -26.838 1.00 33.25 ? 1531 HOH A O   1 
HETATM 8791 O  O   . HOH F 6 .    ? 44.404 95.494  -30.672 1.00 27.66 ? 1532 HOH A O   1 
HETATM 8792 O  O   . HOH F 6 .    ? 42.142 94.695  -29.930 1.00 32.02 ? 1533 HOH A O   1 
HETATM 8793 O  O   . HOH F 6 .    ? 36.385 93.728  -29.484 1.00 37.80 ? 1534 HOH A O   1 
HETATM 8794 O  O   . HOH F 6 .    ? 34.266 93.505  -30.470 1.00 28.16 ? 1535 HOH A O   1 
HETATM 8795 O  O   . HOH F 6 .    ? 34.985 94.792  -32.806 1.00 29.00 ? 1536 HOH A O   1 
HETATM 8796 O  O   . HOH F 6 .    ? 31.689 92.481  -36.931 1.00 21.96 ? 1537 HOH A O   1 
HETATM 8797 O  O   . HOH F 6 .    ? 28.575 93.813  -38.507 1.00 21.13 ? 1538 HOH A O   1 
HETATM 8798 O  O   . HOH F 6 .    ? 28.408 90.461  -42.929 1.00 28.34 ? 1539 HOH A O   1 
HETATM 8799 O  O   . HOH F 6 .    ? 28.176 87.968  -41.794 1.00 22.39 ? 1540 HOH A O   1 
HETATM 8800 O  O   . HOH F 6 .    ? 25.677 87.724  -42.965 1.00 35.40 ? 1541 HOH A O   1 
HETATM 8801 O  O   . HOH F 6 .    ? 23.110 88.755  -38.030 1.00 29.06 ? 1542 HOH A O   1 
HETATM 8802 O  O   . HOH F 6 .    ? 23.278 82.591  -40.734 1.00 21.10 ? 1543 HOH A O   1 
HETATM 8803 O  O   . HOH F 6 .    ? 22.182 80.700  -42.458 1.00 30.54 ? 1544 HOH A O   1 
HETATM 8804 O  O   . HOH F 6 .    ? 19.512 81.757  -42.515 1.00 38.48 ? 1545 HOH A O   1 
HETATM 8805 O  O   . HOH F 6 .    ? 21.260 82.065  -38.153 1.00 32.92 ? 1546 HOH A O   1 
HETATM 8806 O  O   . HOH F 6 .    ? 21.936 80.268  -36.098 1.00 21.66 ? 1547 HOH A O   1 
HETATM 8807 O  O   . HOH F 6 .    ? 20.437 80.479  -33.793 1.00 41.22 ? 1548 HOH A O   1 
HETATM 8808 O  O   . HOH F 6 .    ? 28.886 81.844  -35.771 1.00 15.06 ? 1549 HOH A O   1 
HETATM 8809 O  O   . HOH F 6 .    ? 27.991 84.638  -35.577 1.00 13.67 ? 1550 HOH A O   1 
HETATM 8810 O  O   . HOH F 6 .    ? 29.880 81.685  -43.118 1.00 40.85 ? 1551 HOH A O   1 
HETATM 8811 O  O   . HOH F 6 .    ? 31.293 79.102  -43.028 1.00 24.68 ? 1552 HOH A O   1 
HETATM 8812 O  O   . HOH F 6 .    ? 35.620 77.358  -43.101 1.00 30.77 ? 1553 HOH A O   1 
HETATM 8813 O  O   . HOH F 6 .    ? 37.565 75.601  -42.543 1.00 17.23 ? 1554 HOH A O   1 
HETATM 8814 O  O   . HOH F 6 .    ? 39.558 75.503  -40.394 1.00 15.66 ? 1555 HOH A O   1 
HETATM 8815 O  O   . HOH F 6 .    ? 42.160 74.677  -41.557 1.00 20.37 ? 1556 HOH A O   1 
HETATM 8816 O  O   . HOH F 6 .    ? 43.716 72.494  -42.028 1.00 17.95 ? 1557 HOH A O   1 
HETATM 8817 O  O   . HOH F 6 .    ? 44.625 72.084  -44.704 1.00 38.80 ? 1558 HOH A O   1 
HETATM 8818 O  O   . HOH F 6 .    ? 46.130 70.285  -39.851 1.00 27.85 ? 1559 HOH A O   1 
HETATM 8819 O  O   . HOH F 6 .    ? 46.484 70.277  -36.804 1.00 15.27 ? 1560 HOH A O   1 
HETATM 8820 O  O   . HOH F 6 .    ? 48.978 69.109  -37.110 1.00 23.76 ? 1561 HOH A O   1 
HETATM 8821 O  O   . HOH F 6 .    ? 51.596 70.052  -38.118 1.00 19.93 ? 1562 HOH A O   1 
HETATM 8822 O  O   . HOH F 6 .    ? 53.886 71.179  -36.925 1.00 11.99 ? 1563 HOH A O   1 
HETATM 8823 O  O   . HOH F 6 .    ? 55.245 68.990  -37.820 1.00 27.06 ? 1564 HOH A O   1 
HETATM 8824 O  O   . HOH F 6 .    ? 56.536 69.895  -39.967 1.00 25.43 ? 1565 HOH A O   1 
HETATM 8825 O  O   . HOH F 6 .    ? 60.139 68.585  -38.815 1.00 31.80 ? 1566 HOH A O   1 
HETATM 8826 O  O   . HOH F 6 .    ? 61.526 68.879  -41.756 1.00 33.99 ? 1567 HOH A O   1 
HETATM 8827 O  O   . HOH F 6 .    ? 59.280 67.163  -34.740 1.00 24.86 ? 1568 HOH A O   1 
HETATM 8828 O  O   . HOH F 6 .    ? 56.691 67.621  -35.578 1.00 20.41 ? 1569 HOH A O   1 
HETATM 8829 O  O   . HOH F 6 .    ? 56.046 65.012  -36.236 1.00 18.66 ? 1570 HOH A O   1 
HETATM 8830 O  O   . HOH F 6 .    ? 61.533 63.830  -30.970 1.00 28.83 ? 1571 HOH A O   1 
HETATM 8831 O  O   . HOH F 6 .    ? 63.757 65.493  -30.534 1.00 33.64 ? 1572 HOH A O   1 
HETATM 8832 O  O   . HOH F 6 .    ? 63.087 67.795  -31.784 1.00 25.29 ? 1573 HOH A O   1 
HETATM 8833 O  O   . HOH F 6 .    ? 69.599 63.822  -28.811 1.00 24.78 ? 1574 HOH A O   1 
HETATM 8834 O  O   . HOH F 6 .    ? 71.275 62.505  -27.142 1.00 42.53 ? 1575 HOH A O   1 
HETATM 8835 O  O   . HOH F 6 .    ? 69.763 62.740  -23.924 1.00 29.32 ? 1576 HOH A O   1 
HETATM 8836 O  O   . HOH F 6 .    ? 67.897 58.656  -24.162 1.00 17.64 ? 1577 HOH A O   1 
HETATM 8837 O  O   . HOH F 6 .    ? 67.889 57.217  -26.946 1.00 34.96 ? 1578 HOH A O   1 
HETATM 8838 O  O   . HOH F 6 .    ? 66.799 59.943  -27.192 1.00 18.68 ? 1579 HOH A O   1 
HETATM 8839 O  O   . HOH F 6 .    ? 66.490 56.163  -20.294 1.00 15.89 ? 1580 HOH A O   1 
HETATM 8840 O  O   . HOH F 6 .    ? 67.488 54.537  -18.313 1.00 24.85 ? 1581 HOH A O   1 
HETATM 8841 O  O   . HOH F 6 .    ? 68.648 56.808  -16.288 1.00 31.88 ? 1582 HOH A O   1 
HETATM 8842 O  O   . HOH F 6 .    ? 66.437 62.525  -13.218 1.00 18.63 ? 1583 HOH A O   1 
HETATM 8843 O  O   . HOH F 6 .    ? 65.599 60.269  -7.706  1.00 9.90  ? 1584 HOH A O   1 
HETATM 8844 O  O   . HOH F 6 .    ? 67.426 60.630  -5.694  1.00 11.39 ? 1585 HOH A O   1 
HETATM 8845 O  O   . HOH F 6 .    ? 68.811 58.222  -5.065  1.00 12.22 ? 1586 HOH A O   1 
HETATM 8846 O  O   . HOH F 6 .    ? 69.108 61.391  -2.367  1.00 13.47 ? 1587 HOH A O   1 
HETATM 8847 O  O   . HOH F 6 .    ? 67.947 65.519  -3.418  1.00 13.43 ? 1588 HOH A O   1 
HETATM 8848 O  O   . HOH F 6 .    ? 65.915 66.045  -0.511  1.00 21.33 ? 1589 HOH A O   1 
HETATM 8849 O  O   . HOH F 6 .    ? 62.390 60.656  0.473   1.00 28.36 ? 1590 HOH A O   1 
HETATM 8850 O  O   . HOH F 6 .    ? 63.109 58.587  -1.377  1.00 15.16 ? 1591 HOH A O   1 
HETATM 8851 O  O   . HOH F 6 .    ? 63.692 57.102  0.946   1.00 31.19 ? 1592 HOH A O   1 
HETATM 8852 O  O   . HOH F 6 .    ? 66.992 55.242  1.067   1.00 15.37 ? 1593 HOH A O   1 
HETATM 8853 O  O   . HOH F 6 .    ? 66.006 50.316  0.512   1.00 39.48 ? 1594 HOH A O   1 
HETATM 8854 O  O   . HOH F 6 .    ? 68.069 49.340  -0.901  1.00 19.62 ? 1595 HOH A O   1 
HETATM 8855 O  O   . HOH F 6 .    ? 67.441 46.559  -1.267  1.00 21.46 ? 1596 HOH A O   1 
HETATM 8856 O  O   . HOH F 6 .    ? 65.943 45.493  -3.077  1.00 26.49 ? 1597 HOH A O   1 
HETATM 8857 O  O   . HOH F 6 .    ? 63.016 44.941  -3.372  1.00 34.94 ? 1598 HOH A O   1 
HETATM 8858 O  O   . HOH F 6 .    ? 63.372 44.661  -6.599  1.00 15.34 ? 1599 HOH A O   1 
HETATM 8859 O  O   . HOH F 6 .    ? 64.237 39.271  -10.218 1.00 18.48 ? 1600 HOH A O   1 
HETATM 8860 O  O   . HOH F 6 .    ? 66.961 38.474  -9.595  1.00 30.94 ? 1601 HOH A O   1 
HETATM 8861 O  O   . HOH F 6 .    ? 59.213 37.660  -15.295 1.00 27.66 ? 1602 HOH A O   1 
HETATM 8862 O  O   . HOH F 6 .    ? 57.192 35.915  -14.245 1.00 29.28 ? 1603 HOH A O   1 
HETATM 8863 O  O   . HOH F 6 .    ? 58.434 34.831  -12.365 1.00 36.25 ? 1604 HOH A O   1 
HETATM 8864 O  O   . HOH F 6 .    ? 58.007 34.629  -5.830  1.00 29.98 ? 1605 HOH A O   1 
HETATM 8865 O  O   . HOH F 6 .    ? 56.113 38.714  1.531   1.00 47.39 ? 1606 HOH A O   1 
HETATM 8866 O  O   . HOH F 6 .    ? 58.079 42.412  1.594   1.00 26.56 ? 1607 HOH A O   1 
HETATM 8867 O  O   . HOH F 6 .    ? 58.809 46.318  -1.334  1.00 18.42 ? 1608 HOH A O   1 
HETATM 8868 O  O   . HOH F 6 .    ? 59.208 49.938  -0.529  1.00 14.55 ? 1609 HOH A O   1 
HETATM 8869 O  O   . HOH F 6 .    ? 58.691 52.591  -0.151  1.00 12.96 ? 1610 HOH A O   1 
HETATM 8870 O  O   . HOH F 6 .    ? 56.068 53.420  -0.634  1.00 7.29  ? 1611 HOH A O   1 
HETATM 8871 O  O   . HOH F 6 .    ? 56.286 55.769  -2.090  1.00 9.44  ? 1612 HOH A O   1 
HETATM 8872 O  O   . HOH F 6 .    ? 58.812 56.763  -1.361  1.00 11.98 ? 1613 HOH A O   1 
HETATM 8873 O  O   . HOH F 6 .    ? 58.851 58.138  1.046   1.00 21.98 ? 1614 HOH A O   1 
HETATM 8874 O  O   . HOH F 6 .    ? 56.413 58.623  1.428   1.00 27.78 ? 1615 HOH A O   1 
HETATM 8875 O  O   . HOH F 6 .    ? 56.909 61.009  1.625   1.00 16.65 ? 1616 HOH A O   1 
HETATM 8876 O  O   . HOH F 6 .    ? 55.202 59.016  3.904   1.00 14.42 ? 1617 HOH A O   1 
HETATM 8877 O  O   . HOH F 6 .    ? 57.465 58.571  5.587   1.00 23.13 ? 1618 HOH A O   1 
HETATM 8878 O  O   . HOH F 6 .    ? 57.557 62.387  7.873   1.00 27.50 ? 1619 HOH A O   1 
HETATM 8879 O  O   . HOH F 6 .    ? 56.348 66.955  5.246   1.00 30.39 ? 1620 HOH A O   1 
HETATM 8880 O  O   . HOH F 6 .    ? 59.279 68.186  2.495   1.00 22.01 ? 1621 HOH A O   1 
HETATM 8881 O  O   . HOH F 6 .    ? 60.450 73.313  -0.213  1.00 45.31 ? 1622 HOH A O   1 
HETATM 8882 O  O   . HOH F 6 .    ? 58.838 77.270  1.172   1.00 35.19 ? 1623 HOH A O   1 
HETATM 8883 O  O   . HOH F 6 .    ? 56.767 75.864  0.206   1.00 35.13 ? 1624 HOH A O   1 
HETATM 8884 O  O   . HOH F 6 .    ? 57.132 75.435  -2.880  1.00 26.50 ? 1625 HOH A O   1 
HETATM 8885 O  O   . HOH F 6 .    ? 59.090 76.854  -4.173  1.00 27.91 ? 1626 HOH A O   1 
HETATM 8886 O  O   . HOH F 6 .    ? 60.233 74.959  -4.562  1.00 35.92 ? 1627 HOH A O   1 
HETATM 8887 O  O   . HOH F 6 .    ? 59.458 76.526  -9.000  1.00 13.90 ? 1628 HOH A O   1 
HETATM 8888 O  O   . HOH F 6 .    ? 61.818 76.404  -10.501 1.00 16.52 ? 1629 HOH A O   1 
HETATM 8889 O  O   . HOH F 6 .    ? 61.254 77.502  -12.993 1.00 21.08 ? 1630 HOH A O   1 
HETATM 8890 O  O   . HOH F 6 .    ? 56.230 79.113  -14.939 1.00 30.23 ? 1631 HOH A O   1 
HETATM 8891 O  O   . HOH F 6 .    ? 49.977 79.879  -11.077 1.00 35.97 ? 1632 HOH A O   1 
HETATM 8892 O  O   . HOH F 6 .    ? 48.290 78.137  -9.623  1.00 26.17 ? 1633 HOH A O   1 
HETATM 8893 O  O   . HOH F 6 .    ? 45.682 79.239  -7.882  1.00 20.24 ? 1634 HOH A O   1 
HETATM 8894 O  O   . HOH F 6 .    ? 42.906 82.314  -9.868  1.00 23.63 ? 1635 HOH A O   1 
HETATM 8895 O  O   . HOH F 6 .    ? 40.353 82.870  -10.734 1.00 15.49 ? 1636 HOH A O   1 
HETATM 8896 O  O   . HOH F 6 .    ? 40.787 85.171  -12.110 1.00 24.25 ? 1637 HOH A O   1 
HETATM 8897 O  O   . HOH F 6 .    ? 41.255 77.626  -14.127 1.00 11.45 ? 1638 HOH A O   1 
HETATM 8898 O  O   . HOH F 6 .    ? 42.096 75.289  -16.013 1.00 13.06 ? 1639 HOH A O   1 
HETATM 8899 O  O   . HOH F 6 .    ? 46.334 67.710  -15.657 1.00 12.67 ? 1640 HOH A O   1 
HETATM 8900 O  O   . HOH F 6 .    ? 39.151 64.795  -14.772 1.00 10.41 ? 1641 HOH A O   1 
HETATM 8901 O  O   . HOH F 6 .    ? 39.157 62.870  -19.181 1.00 7.64  ? 1642 HOH A O   1 
HETATM 8902 O  O   . HOH F 6 .    ? 34.004 56.323  -26.385 1.00 9.23  ? 1643 HOH A O   1 
HETATM 8903 O  O   . HOH F 6 .    ? 31.975 58.618  -28.541 1.00 12.01 ? 1644 HOH A O   1 
HETATM 8904 O  O   . HOH F 6 .    ? 34.653 59.498  -35.043 1.00 16.54 ? 1645 HOH A O   1 
HETATM 8905 O  O   . HOH F 6 .    ? 33.516 57.108  -36.032 1.00 15.34 ? 1646 HOH A O   1 
HETATM 8906 O  O   . HOH F 6 .    ? 33.199 56.747  -38.876 1.00 31.56 ? 1647 HOH A O   1 
HETATM 8907 O  O   . HOH F 6 .    ? 30.933 58.176  -40.212 1.00 36.02 ? 1648 HOH A O   1 
HETATM 8908 O  O   . HOH F 6 .    ? 28.539 59.771  -39.241 1.00 32.14 ? 1649 HOH A O   1 
HETATM 8909 O  O   . HOH F 6 .    ? 28.993 62.249  -39.894 1.00 19.01 ? 1650 HOH A O   1 
HETATM 8910 O  O   . HOH F 6 .    ? 26.006 58.772  -39.137 1.00 37.96 ? 1651 HOH A O   1 
HETATM 8911 O  O   . HOH F 6 .    ? 17.185 57.080  -36.822 1.00 32.46 ? 1652 HOH A O   1 
HETATM 8912 O  O   . HOH F 6 .    ? 19.287 52.441  -31.551 1.00 33.17 ? 1653 HOH A O   1 
HETATM 8913 O  O   . HOH F 6 .    ? 19.487 52.589  -27.199 1.00 29.79 ? 1654 HOH A O   1 
HETATM 8914 O  O   . HOH F 6 .    ? 20.002 52.655  -24.401 1.00 15.99 ? 1655 HOH A O   1 
HETATM 8915 O  O   . HOH F 6 .    ? 22.706 53.089  -24.465 1.00 11.32 ? 1656 HOH A O   1 
HETATM 8916 O  O   . HOH F 6 .    ? 24.619 51.101  -24.149 1.00 12.02 ? 1657 HOH A O   1 
HETATM 8917 O  O   . HOH F 6 .    ? 23.760 48.437  -24.170 1.00 35.73 ? 1658 HOH A O   1 
HETATM 8918 O  O   . HOH F 6 .    ? 26.804 47.631  -23.839 1.00 27.43 ? 1659 HOH A O   1 
HETATM 8919 O  O   . HOH F 6 .    ? 27.386 48.488  -21.682 1.00 14.70 ? 1660 HOH A O   1 
HETATM 8920 O  O   . HOH F 6 .    ? 25.068 46.983  -20.903 1.00 22.25 ? 1661 HOH A O   1 
HETATM 8921 O  O   . HOH F 6 .    ? 28.560 49.722  -24.404 1.00 13.95 ? 1662 HOH A O   1 
HETATM 8922 O  O   . HOH F 6 .    ? 31.202 49.939  -24.076 1.00 10.01 ? 1663 HOH A O   1 
HETATM 8923 O  O   . HOH F 6 .    ? 35.526 45.221  -27.506 1.00 15.01 ? 1664 HOH A O   1 
HETATM 8924 O  O   . HOH F 6 .    ? 37.320 45.265  -25.486 1.00 18.46 ? 1665 HOH A O   1 
HETATM 8925 O  O   . HOH F 6 .    ? 36.012 42.070  -26.593 1.00 33.83 ? 1666 HOH A O   1 
HETATM 8926 O  O   . HOH F 6 .    ? 36.935 41.261  -24.593 1.00 24.03 ? 1667 HOH A O   1 
HETATM 8927 O  O   . HOH F 6 .    ? 38.606 42.161  -22.133 1.00 27.17 ? 1668 HOH A O   1 
HETATM 8928 O  O   . HOH F 6 .    ? 40.725 40.628  -21.556 1.00 23.64 ? 1669 HOH A O   1 
HETATM 8929 O  O   . HOH F 6 .    ? 43.153 40.596  -22.954 1.00 30.26 ? 1670 HOH A O   1 
HETATM 8930 O  O   . HOH F 6 .    ? 43.463 42.806  -24.791 1.00 31.61 ? 1671 HOH A O   1 
HETATM 8931 O  O   . HOH F 6 .    ? 41.403 44.597  -24.461 1.00 20.82 ? 1672 HOH A O   1 
HETATM 8932 O  O   . HOH F 6 .    ? 42.100 47.305  -24.590 1.00 12.80 ? 1673 HOH A O   1 
HETATM 8933 O  O   . HOH F 6 .    ? 42.509 47.190  -27.561 1.00 45.74 ? 1674 HOH A O   1 
HETATM 8934 O  O   . HOH F 6 .    ? 41.185 48.184  -29.401 1.00 46.13 ? 1675 HOH A O   1 
HETATM 8935 O  O   . HOH F 6 .    ? 39.182 48.855  -32.980 1.00 24.80 ? 1676 HOH A O   1 
HETATM 8936 O  O   . HOH F 6 .    ? 38.423 45.181  -33.850 1.00 17.95 ? 1677 HOH A O   1 
HETATM 8937 O  O   . HOH F 6 .    ? 38.547 51.388  -29.889 1.00 28.21 ? 1678 HOH A O   1 
HETATM 8938 O  O   . HOH F 6 .    ? 34.944 54.910  -34.630 1.00 38.70 ? 1679 HOH A O   1 
HETATM 8939 O  O   . HOH F 6 .    ? 31.787 51.242  -35.379 1.00 19.53 ? 1680 HOH A O   1 
HETATM 8940 O  O   . HOH F 6 .    ? 22.873 48.798  -36.243 1.00 38.65 ? 1681 HOH A O   1 
HETATM 8941 O  O   . HOH F 6 .    ? 21.658 47.042  -34.494 1.00 32.51 ? 1682 HOH A O   1 
HETATM 8942 O  O   . HOH F 6 .    ? 21.486 48.811  -39.004 1.00 34.29 ? 1683 HOH A O   1 
HETATM 8943 O  O   . HOH F 6 .    ? 23.631 55.553  -23.460 1.00 8.43  ? 1684 HOH A O   1 
HETATM 8944 O  O   . HOH F 6 .    ? 20.214 58.819  -22.033 1.00 8.77  ? 1685 HOH A O   1 
HETATM 8945 O  O   . HOH F 6 .    ? 13.483 57.791  -21.908 1.00 9.82  ? 1686 HOH A O   1 
HETATM 8946 O  O   . HOH F 6 .    ? 10.465 57.928  -21.030 1.00 31.23 ? 1687 HOH A O   1 
HETATM 8947 O  O   . HOH F 6 .    ? 9.848  60.251  -20.555 1.00 29.17 ? 1688 HOH A O   1 
HETATM 8948 O  O   . HOH F 6 .    ? 12.493 66.396  -9.638  1.00 18.78 ? 1689 HOH A O   1 
HETATM 8949 O  O   . HOH F 6 .    ? 13.970 68.319  -8.030  1.00 18.73 ? 1690 HOH A O   1 
HETATM 8950 O  O   . HOH F 6 .    ? 13.426 70.252  -9.593  1.00 31.50 ? 1691 HOH A O   1 
HETATM 8951 O  O   . HOH F 6 .    ? 13.005 66.846  -4.848  1.00 13.55 ? 1692 HOH A O   1 
HETATM 8952 O  O   . HOH F 6 .    ? 13.070 68.865  0.829   1.00 19.05 ? 1693 HOH A O   1 
HETATM 8953 O  O   . HOH F 6 .    ? 12.118 67.250  2.760   1.00 47.39 ? 1694 HOH A O   1 
HETATM 8954 O  O   . HOH F 6 .    ? 11.709 70.999  2.649   1.00 33.02 ? 1695 HOH A O   1 
HETATM 8955 O  O   . HOH F 6 .    ? 12.745 71.258  -0.540  1.00 27.40 ? 1696 HOH A O   1 
HETATM 8956 O  O   . HOH F 6 .    ? 16.712 74.685  -3.083  1.00 12.33 ? 1697 HOH A O   1 
HETATM 8957 O  O   . HOH F 6 .    ? 19.959 74.411  -6.864  1.00 10.92 ? 1698 HOH A O   1 
HETATM 8958 O  O   . HOH F 6 .    ? 24.505 70.577  -8.766  1.00 10.56 ? 1699 HOH A O   1 
HETATM 8959 O  O   . HOH F 6 .    ? 26.717 69.017  -9.281  1.00 7.29  ? 1700 HOH A O   1 
HETATM 8960 O  O   . HOH F 6 .    ? 32.569 64.681  -10.009 1.00 16.48 ? 1701 HOH A O   1 
HETATM 8961 O  O   . HOH F 6 .    ? 34.143 58.580  -8.772  1.00 7.27  ? 1702 HOH A O   1 
HETATM 8962 O  O   . HOH F 6 .    ? 30.086 58.490  -11.803 1.00 7.31  ? 1703 HOH A O   1 
HETATM 8963 O  O   . HOH F 6 .    ? 26.672 60.968  -3.350  1.00 8.95  ? 1704 HOH A O   1 
HETATM 8964 O  O   . HOH F 6 .    ? 32.477 60.149  -1.787  1.00 8.11  ? 1705 HOH A O   1 
HETATM 8965 O  O   . HOH F 6 .    ? 32.984 62.819  0.101   1.00 6.47  ? 1706 HOH A O   1 
HETATM 8966 O  O   . HOH F 6 .    ? 37.336 57.054  1.813   1.00 9.67  ? 1707 HOH A O   1 
HETATM 8967 O  O   . HOH F 6 .    ? 39.507 55.712  3.080   1.00 13.57 ? 1708 HOH A O   1 
HETATM 8968 O  O   . HOH F 6 .    ? 40.018 56.291  5.821   1.00 12.29 ? 1709 HOH A O   1 
HETATM 8969 O  O   . HOH F 6 .    ? 42.888 56.794  6.212   1.00 10.14 ? 1710 HOH A O   1 
HETATM 8970 O  O   . HOH F 6 .    ? 42.600 56.471  2.828   1.00 15.35 ? 1711 HOH A O   1 
HETATM 8971 O  O   . HOH F 6 .    ? 38.767 53.054  2.107   1.00 27.63 ? 1712 HOH A O   1 
HETATM 8972 O  O   . HOH F 6 .    ? 35.819 53.142  1.345   1.00 11.21 ? 1713 HOH A O   1 
HETATM 8973 O  O   . HOH F 6 .    ? 34.138 52.436  -0.942  1.00 7.73  ? 1714 HOH A O   1 
HETATM 8974 O  O   . HOH F 6 .    ? 36.621 51.694  3.824   1.00 11.74 ? 1715 HOH A O   1 
HETATM 8975 O  O   . HOH F 6 .    ? 30.684 57.275  4.635   1.00 15.11 ? 1716 HOH A O   1 
HETATM 8976 O  O   . HOH F 6 .    ? 27.429 59.281  8.652   1.00 21.70 ? 1717 HOH A O   1 
HETATM 8977 O  O   . HOH F 6 .    ? 26.901 61.409  10.522  1.00 26.64 ? 1718 HOH A O   1 
HETATM 8978 O  O   . HOH F 6 .    ? 28.603 63.548  10.711  1.00 17.54 ? 1719 HOH A O   1 
HETATM 8979 O  O   . HOH F 6 .    ? 29.233 65.603  12.463  1.00 18.06 ? 1720 HOH A O   1 
HETATM 8980 O  O   . HOH F 6 .    ? 27.768 67.497  11.665  1.00 33.24 ? 1721 HOH A O   1 
HETATM 8981 O  O   . HOH F 6 .    ? 28.765 69.669  12.756  1.00 27.78 ? 1722 HOH A O   1 
HETATM 8982 O  O   . HOH F 6 .    ? 29.692 72.262  12.302  1.00 16.58 ? 1723 HOH A O   1 
HETATM 8983 O  O   . HOH F 6 .    ? 31.867 71.188  13.652  1.00 23.67 ? 1724 HOH A O   1 
HETATM 8984 O  O   . HOH F 6 .    ? 34.607 70.518  13.174  1.00 12.57 ? 1725 HOH A O   1 
HETATM 8985 O  O   . HOH F 6 .    ? 34.237 67.815  12.513  1.00 9.75  ? 1726 HOH A O   1 
HETATM 8986 O  O   . HOH F 6 .    ? 30.949 68.351  14.138  1.00 19.89 ? 1727 HOH A O   1 
HETATM 8987 O  O   . HOH F 6 .    ? 29.154 67.099  15.713  1.00 26.09 ? 1728 HOH A O   1 
HETATM 8988 O  O   . HOH F 6 .    ? 28.454 64.701  14.825  1.00 20.15 ? 1729 HOH A O   1 
HETATM 8989 O  O   . HOH F 6 .    ? 26.357 63.765  17.043  1.00 15.28 ? 1730 HOH A O   1 
HETATM 8990 O  O   . HOH F 6 .    ? 25.488 66.164  17.481  1.00 23.19 ? 1731 HOH A O   1 
HETATM 8991 O  O   . HOH F 6 .    ? 26.320 66.709  19.896  1.00 24.14 ? 1732 HOH A O   1 
HETATM 8992 O  O   . HOH F 6 .    ? 28.648 65.158  19.720  1.00 13.68 ? 1733 HOH A O   1 
HETATM 8993 O  O   . HOH F 6 .    ? 29.873 67.196  18.378  1.00 19.82 ? 1734 HOH A O   1 
HETATM 8994 O  O   . HOH F 6 .    ? 31.952 65.614  19.088  1.00 11.85 ? 1735 HOH A O   1 
HETATM 8995 O  O   . HOH F 6 .    ? 33.089 67.039  21.335  1.00 18.29 ? 1736 HOH A O   1 
HETATM 8996 O  O   . HOH F 6 .    ? 32.605 69.562  22.124  1.00 27.18 ? 1737 HOH A O   1 
HETATM 8997 O  O   . HOH F 6 .    ? 32.702 69.308  24.564  1.00 22.69 ? 1738 HOH A O   1 
HETATM 8998 O  O   . HOH F 6 .    ? 36.024 68.604  24.445  1.00 19.45 ? 1739 HOH A O   1 
HETATM 8999 O  O   . HOH F 6 .    ? 36.588 66.752  25.683  1.00 24.99 ? 1740 HOH A O   1 
HETATM 9000 O  O   . HOH F 6 .    ? 35.754 68.040  20.642  1.00 29.47 ? 1741 HOH A O   1 
HETATM 9001 O  O   . HOH F 6 .    ? 38.208 73.717  18.248  1.00 26.13 ? 1742 HOH A O   1 
HETATM 9002 O  O   . HOH F 6 .    ? 46.120 74.352  22.494  1.00 27.12 ? 1743 HOH A O   1 
HETATM 9003 O  O   . HOH F 6 .    ? 46.320 68.443  26.523  1.00 31.33 ? 1744 HOH A O   1 
HETATM 9004 O  O   . HOH F 6 .    ? 47.778 66.011  27.026  1.00 34.32 ? 1745 HOH A O   1 
HETATM 9005 O  O   . HOH F 6 .    ? 50.711 61.882  26.521  1.00 17.93 ? 1746 HOH A O   1 
HETATM 9006 O  O   . HOH F 6 .    ? 51.916 60.319  28.244  1.00 28.10 ? 1747 HOH A O   1 
HETATM 9007 O  O   . HOH F 6 .    ? 51.971 58.026  29.207  1.00 38.08 ? 1748 HOH A O   1 
HETATM 9008 O  O   . HOH F 6 .    ? 45.186 58.261  32.355  1.00 30.16 ? 1749 HOH A O   1 
HETATM 9009 O  O   . HOH F 6 .    ? 43.668 56.778  33.765  1.00 24.67 ? 1750 HOH A O   1 
HETATM 9010 O  O   . HOH F 6 .    ? 42.683 53.383  35.763  1.00 21.57 ? 1751 HOH A O   1 
HETATM 9011 O  O   . HOH F 6 .    ? 39.832 52.719  36.303  1.00 29.09 ? 1752 HOH A O   1 
HETATM 9012 O  O   . HOH F 6 .    ? 39.320 49.868  36.555  1.00 35.57 ? 1753 HOH A O   1 
HETATM 9013 O  O   . HOH F 6 .    ? 41.743 50.608  33.817  1.00 30.93 ? 1754 HOH A O   1 
HETATM 9014 O  O   . HOH F 6 .    ? 48.339 50.931  35.167  1.00 23.21 ? 1755 HOH A O   1 
HETATM 9015 O  O   . HOH F 6 .    ? 49.891 50.202  36.902  1.00 28.59 ? 1756 HOH A O   1 
HETATM 9016 O  O   . HOH F 6 .    ? 47.558 53.602  35.945  1.00 33.23 ? 1757 HOH A O   1 
HETATM 9017 O  O   . HOH F 6 .    ? 49.474 50.790  32.695  1.00 27.20 ? 1758 HOH A O   1 
HETATM 9018 O  O   . HOH F 6 .    ? 53.832 49.847  29.547  1.00 36.04 ? 1759 HOH A O   1 
HETATM 9019 O  O   . HOH F 6 .    ? 51.821 63.923  24.615  1.00 22.60 ? 1760 HOH A O   1 
HETATM 9020 O  O   . HOH F 6 .    ? 42.516 66.979  29.481  1.00 25.91 ? 1761 HOH A O   1 
HETATM 9021 O  O   . HOH F 6 .    ? 39.783 66.954  31.395  1.00 29.03 ? 1762 HOH A O   1 
HETATM 9022 O  O   . HOH F 6 .    ? 42.066 61.379  33.468  1.00 38.72 ? 1763 HOH A O   1 
HETATM 9023 O  O   . HOH F 6 .    ? 37.892 62.228  35.488  1.00 34.28 ? 1764 HOH A O   1 
HETATM 9024 O  O   . HOH F 6 .    ? 35.519 61.993  34.218  1.00 28.89 ? 1765 HOH A O   1 
HETATM 9025 O  O   . HOH F 6 .    ? 30.908 61.771  35.607  1.00 31.90 ? 1766 HOH A O   1 
HETATM 9026 O  O   . HOH F 6 .    ? 30.061 59.334  35.224  1.00 24.91 ? 1767 HOH A O   1 
HETATM 9027 O  O   . HOH F 6 .    ? 31.448 57.455  37.524  1.00 29.34 ? 1768 HOH A O   1 
HETATM 9028 O  O   . HOH F 6 .    ? 28.303 55.348  40.134  1.00 26.69 ? 1769 HOH A O   1 
HETATM 9029 O  O   . HOH F 6 .    ? 25.764 57.563  40.488  1.00 31.69 ? 1770 HOH A O   1 
HETATM 9030 O  O   . HOH F 6 .    ? 23.866 57.466  38.751  1.00 31.12 ? 1771 HOH A O   1 
HETATM 9031 O  O   . HOH F 6 .    ? 21.594 55.373  40.166  1.00 24.45 ? 1772 HOH A O   1 
HETATM 9032 O  O   . HOH F 6 .    ? 17.626 53.455  35.074  1.00 18.87 ? 1773 HOH A O   1 
HETATM 9033 O  O   . HOH F 6 .    ? 18.643 48.864  37.609  1.00 12.67 ? 1774 HOH A O   1 
HETATM 9034 O  O   . HOH F 6 .    ? 20.908 47.545  39.072  1.00 14.07 ? 1775 HOH A O   1 
HETATM 9035 O  O   . HOH F 6 .    ? 18.686 46.483  40.352  1.00 23.99 ? 1776 HOH A O   1 
HETATM 9036 O  O   . HOH F 6 .    ? 20.113 41.440  34.925  1.00 40.21 ? 1777 HOH A O   1 
HETATM 9037 O  O   . HOH F 6 .    ? 20.012 43.373  33.849  1.00 22.14 ? 1778 HOH A O   1 
HETATM 9038 O  O   . HOH F 6 .    ? 16.807 41.846  32.075  1.00 30.53 ? 1779 HOH A O   1 
HETATM 9039 O  O   . HOH F 6 .    ? 15.778 39.882  33.907  1.00 35.98 ? 1780 HOH A O   1 
HETATM 9040 O  O   . HOH F 6 .    ? 21.154 35.462  34.603  1.00 34.93 ? 1781 HOH A O   1 
HETATM 9041 O  O   . HOH F 6 .    ? 24.317 34.572  35.782  1.00 27.81 ? 1782 HOH A O   1 
HETATM 9042 O  O   . HOH F 6 .    ? 27.760 34.833  32.239  1.00 32.01 ? 1783 HOH A O   1 
HETATM 9043 O  O   . HOH F 6 .    ? 26.911 35.073  29.543  1.00 22.37 ? 1784 HOH A O   1 
HETATM 9044 O  O   . HOH F 6 .    ? 25.870 32.747  28.699  1.00 28.41 ? 1785 HOH A O   1 
HETATM 9045 O  O   . HOH F 6 .    ? 22.312 31.240  29.516  1.00 27.81 ? 1786 HOH A O   1 
HETATM 9046 O  O   . HOH F 6 .    ? 21.420 29.251  27.945  1.00 30.10 ? 1787 HOH A O   1 
HETATM 9047 O  O   . HOH F 6 .    ? 18.467 32.082  25.737  1.00 28.80 ? 1788 HOH A O   1 
HETATM 9048 O  O   . HOH F 6 .    ? 19.720 35.530  25.539  1.00 24.45 ? 1789 HOH A O   1 
HETATM 9049 O  O   . HOH F 6 .    ? 19.095 36.456  22.299  1.00 26.24 ? 1790 HOH A O   1 
HETATM 9050 O  O   . HOH F 6 .    ? 18.532 37.597  19.776  1.00 23.23 ? 1791 HOH A O   1 
HETATM 9051 O  O   . HOH F 6 .    ? 19.525 39.257  17.524  1.00 16.25 ? 1792 HOH A O   1 
HETATM 9052 O  O   . HOH F 6 .    ? 21.426 38.101  15.712  1.00 21.26 ? 1793 HOH A O   1 
HETATM 9053 O  O   . HOH F 6 .    ? 23.206 36.948  13.433  1.00 25.14 ? 1794 HOH A O   1 
HETATM 9054 O  O   . HOH F 6 .    ? 21.958 34.630  12.642  1.00 37.90 ? 1795 HOH A O   1 
HETATM 9055 O  O   . HOH F 6 .    ? 25.149 33.335  13.269  1.00 30.11 ? 1796 HOH A O   1 
HETATM 9056 O  O   . HOH F 6 .    ? 24.084 34.372  15.606  1.00 23.54 ? 1797 HOH A O   1 
HETATM 9057 O  O   . HOH F 6 .    ? 20.985 30.276  17.740  1.00 33.80 ? 1798 HOH A O   1 
HETATM 9058 O  O   . HOH F 6 .    ? 16.185 33.977  15.609  1.00 33.18 ? 1799 HOH A O   1 
HETATM 9059 O  O   . HOH F 6 .    ? 16.393 36.502  16.777  1.00 28.52 ? 1800 HOH A O   1 
HETATM 9060 O  O   . HOH F 6 .    ? 17.647 35.372  13.375  1.00 35.21 ? 1801 HOH A O   1 
HETATM 9061 O  O   . HOH F 6 .    ? 20.331 37.927  12.231  1.00 21.99 ? 1802 HOH A O   1 
HETATM 9062 O  O   . HOH F 6 .    ? 24.869 39.989  14.282  1.00 14.94 ? 1803 HOH A O   1 
HETATM 9063 O  O   . HOH F 6 .    ? 27.093 41.394  13.344  1.00 12.88 ? 1804 HOH A O   1 
HETATM 9064 O  O   . HOH F 6 .    ? 28.171 43.932  13.244  1.00 9.23  ? 1805 HOH A O   1 
HETATM 9065 O  O   . HOH F 6 .    ? 27.104 46.400  13.724  1.00 16.67 ? 1806 HOH A O   1 
HETATM 9066 O  O   . HOH F 6 .    ? 28.041 48.951  12.307  1.00 14.30 ? 1807 HOH A O   1 
HETATM 9067 O  O   . HOH F 6 .    ? 26.381 51.650  13.117  1.00 22.37 ? 1808 HOH A O   1 
HETATM 9068 O  O   . HOH F 6 .    ? 25.363 53.698  11.255  1.00 12.39 ? 1809 HOH A O   1 
HETATM 9069 O  O   . HOH F 6 .    ? 19.208 55.277  11.488  1.00 10.12 ? 1810 HOH A O   1 
HETATM 9070 O  O   . HOH F 6 .    ? 18.179 55.017  14.085  1.00 11.35 ? 1811 HOH A O   1 
HETATM 9071 O  O   . HOH F 6 .    ? 19.975 54.822  16.106  1.00 10.23 ? 1812 HOH A O   1 
HETATM 9072 O  O   . HOH F 6 .    ? 16.624 57.161  12.931  1.00 11.93 ? 1813 HOH A O   1 
HETATM 9073 O  O   . HOH F 6 .    ? 16.905 56.342  10.276  1.00 11.80 ? 1814 HOH A O   1 
HETATM 9074 O  O   . HOH F 6 .    ? 19.181 53.593  8.182   1.00 9.24  ? 1815 HOH A O   1 
HETATM 9075 O  O   . HOH F 6 .    ? 17.437 52.815  6.312   1.00 9.81  ? 1816 HOH A O   1 
HETATM 9076 O  O   . HOH F 6 .    ? 19.951 56.075  7.152   1.00 10.20 ? 1817 HOH A O   1 
HETATM 9077 O  O   . HOH F 6 .    ? 21.597 57.159  5.066   1.00 10.32 ? 1818 HOH A O   1 
HETATM 9078 O  O   . HOH F 6 .    ? 23.790 58.121  6.313   1.00 10.05 ? 1819 HOH A O   1 
HETATM 9079 O  O   . HOH F 6 .    ? 24.495 61.532  9.017   1.00 11.94 ? 1820 HOH A O   1 
HETATM 9080 O  O   . HOH F 6 .    ? 23.382 63.806  7.924   1.00 16.97 ? 1821 HOH A O   1 
HETATM 9081 O  O   . HOH F 6 .    ? 25.990 64.516  8.497   1.00 17.00 ? 1822 HOH A O   1 
HETATM 9082 O  O   . HOH F 6 .    ? 26.319 67.106  9.393   1.00 17.86 ? 1823 HOH A O   1 
HETATM 9083 O  O   . HOH F 6 .    ? 23.322 66.307  9.806   1.00 29.73 ? 1824 HOH A O   1 
HETATM 9084 O  O   . HOH F 6 .    ? 20.580 68.155  8.556   1.00 29.09 ? 1825 HOH A O   1 
HETATM 9085 O  O   . HOH F 6 .    ? 20.402 65.446  7.674   1.00 22.34 ? 1826 HOH A O   1 
HETATM 9086 O  O   . HOH F 6 .    ? 18.393 70.014  4.209   1.00 13.14 ? 1827 HOH A O   1 
HETATM 9087 O  O   . HOH F 6 .    ? 17.261 70.693  6.427   1.00 41.89 ? 1828 HOH A O   1 
HETATM 9088 O  O   . HOH F 6 .    ? 15.425 73.710  5.429   1.00 30.58 ? 1829 HOH A O   1 
HETATM 9089 O  O   . HOH F 6 .    ? 17.656 74.514  3.867   1.00 22.17 ? 1830 HOH A O   1 
HETATM 9090 O  O   . HOH F 6 .    ? 18.940 76.628  4.669   1.00 27.78 ? 1831 HOH A O   1 
HETATM 9091 O  O   . HOH F 6 .    ? 21.291 79.966  5.292   1.00 25.07 ? 1832 HOH A O   1 
HETATM 9092 O  O   . HOH F 6 .    ? 22.100 76.895  8.651   1.00 28.95 ? 1833 HOH A O   1 
HETATM 9093 O  O   . HOH F 6 .    ? 25.311 74.090  8.697   1.00 17.79 ? 1834 HOH A O   1 
HETATM 9094 O  O   . HOH F 6 .    ? 25.946 72.851  5.595   1.00 10.68 ? 1835 HOH A O   1 
HETATM 9095 O  O   . HOH F 6 .    ? 26.368 75.048  2.117   1.00 18.64 ? 1836 HOH A O   1 
HETATM 9096 O  O   . HOH F 6 .    ? 21.209 78.542  -1.427  1.00 18.00 ? 1837 HOH A O   1 
HETATM 9097 O  O   . HOH F 6 .    ? 16.218 80.242  -1.199  1.00 36.88 ? 1838 HOH A O   1 
HETATM 9098 O  O   . HOH F 6 .    ? 16.405 82.297  -5.064  1.00 35.26 ? 1839 HOH A O   1 
HETATM 9099 O  O   . HOH F 6 .    ? 17.161 80.814  -7.652  1.00 21.62 ? 1840 HOH A O   1 
HETATM 9100 O  O   . HOH F 6 .    ? 20.960 84.074  -12.521 1.00 31.21 ? 1841 HOH A O   1 
HETATM 9101 O  O   . HOH F 6 .    ? 26.777 88.163  -4.052  1.00 37.00 ? 1842 HOH A O   1 
HETATM 9102 O  O   . HOH F 6 .    ? 24.708 83.794  2.642   1.00 30.94 ? 1843 HOH A O   1 
HETATM 9103 O  O   . HOH F 6 .    ? 29.578 75.818  10.947  1.00 26.19 ? 1844 HOH A O   1 
HETATM 9104 O  O   . HOH F 6 .    ? 29.863 74.995  22.208  1.00 28.07 ? 1845 HOH A O   1 
HETATM 9105 O  O   . HOH F 6 .    ? 28.846 72.484  22.320  1.00 27.43 ? 1846 HOH A O   1 
HETATM 9106 O  O   . HOH F 6 .    ? 25.366 71.081  22.253  1.00 25.30 ? 1847 HOH A O   1 
HETATM 9107 O  O   . HOH F 6 .    ? 24.865 68.337  21.800  1.00 16.88 ? 1848 HOH A O   1 
HETATM 9108 O  O   . HOH F 6 .    ? 22.538 68.225  20.353  1.00 20.63 ? 1849 HOH A O   1 
HETATM 9109 O  O   . HOH F 6 .    ? 22.739 66.925  17.926  1.00 33.70 ? 1850 HOH A O   1 
HETATM 9110 O  O   . HOH F 6 .    ? 22.890 64.108  18.244  1.00 23.15 ? 1851 HOH A O   1 
HETATM 9111 O  O   . HOH F 6 .    ? 22.542 62.596  16.076  1.00 17.35 ? 1852 HOH A O   1 
HETATM 9112 O  O   . HOH F 6 .    ? 27.900 60.995  19.526  1.00 9.12  ? 1853 HOH A O   1 
HETATM 9113 O  O   . HOH F 6 .    ? 30.096 55.799  17.253  1.00 7.54  ? 1854 HOH A O   1 
HETATM 9114 O  O   . HOH F 6 .    ? 27.543 53.363  20.112  1.00 13.16 ? 1855 HOH A O   1 
HETATM 9115 O  O   . HOH F 6 .    ? 26.818 51.600  22.649  1.00 18.99 ? 1856 HOH A O   1 
HETATM 9116 O  O   . HOH F 6 .    ? 22.922 56.212  30.862  1.00 13.24 ? 1857 HOH A O   1 
HETATM 9117 O  O   . HOH F 6 .    ? 18.124 59.593  31.749  1.00 28.11 ? 1858 HOH A O   1 
HETATM 9118 O  O   . HOH F 6 .    ? 17.370 61.800  33.281  1.00 30.57 ? 1859 HOH A O   1 
HETATM 9119 O  O   . HOH F 6 .    ? 19.657 62.764  34.797  1.00 33.06 ? 1860 HOH A O   1 
HETATM 9120 O  O   . HOH F 6 .    ? 22.009 62.878  33.731  1.00 24.70 ? 1861 HOH A O   1 
HETATM 9121 O  O   . HOH F 6 .    ? 22.108 65.560  32.422  1.00 29.54 ? 1862 HOH A O   1 
HETATM 9122 O  O   . HOH F 6 .    ? 22.301 66.793  28.926  1.00 23.08 ? 1863 HOH A O   1 
HETATM 9123 O  O   . HOH F 6 .    ? 20.337 65.645  27.175  1.00 21.28 ? 1864 HOH A O   1 
HETATM 9124 O  O   . HOH F 6 .    ? 17.788 65.990  27.870  1.00 19.57 ? 1865 HOH A O   1 
HETATM 9125 O  O   . HOH F 6 .    ? 17.841 66.512  30.624  1.00 26.06 ? 1866 HOH A O   1 
HETATM 9126 O  O   . HOH F 6 .    ? 16.907 68.529  26.672  1.00 26.65 ? 1867 HOH A O   1 
HETATM 9127 O  O   . HOH F 6 .    ? 17.862 68.513  24.202  1.00 35.56 ? 1868 HOH A O   1 
HETATM 9128 O  O   . HOH F 6 .    ? 15.813 68.747  21.867  1.00 27.86 ? 1869 HOH A O   1 
HETATM 9129 O  O   . HOH F 6 .    ? 20.503 68.422  22.220  1.00 21.08 ? 1870 HOH A O   1 
HETATM 9130 O  O   . HOH F 6 .    ? 14.144 69.301  27.071  1.00 23.32 ? 1871 HOH A O   1 
HETATM 9131 O  O   . HOH F 6 .    ? 14.037 63.216  30.069  1.00 29.55 ? 1872 HOH A O   1 
HETATM 9132 O  O   . HOH F 6 .    ? 15.939 57.654  31.587  1.00 31.25 ? 1873 HOH A O   1 
HETATM 9133 O  O   . HOH F 6 .    ? 14.474 55.439  27.215  1.00 28.33 ? 1874 HOH A O   1 
HETATM 9134 O  O   . HOH F 6 .    ? 13.143 52.795  25.894  1.00 34.60 ? 1875 HOH A O   1 
HETATM 9135 O  O   . HOH F 6 .    ? 13.990 50.663  24.244  1.00 17.92 ? 1876 HOH A O   1 
HETATM 9136 O  O   . HOH F 6 .    ? 16.322 49.238  24.032  1.00 11.89 ? 1877 HOH A O   1 
HETATM 9137 O  O   . HOH F 6 .    ? 14.272 47.352  26.587  1.00 36.91 ? 1878 HOH A O   1 
HETATM 9138 O  O   . HOH F 6 .    ? 13.919 44.863  27.084  1.00 29.42 ? 1879 HOH A O   1 
HETATM 9139 O  O   . HOH F 6 .    ? 17.130 43.563  27.418  1.00 22.78 ? 1880 HOH A O   1 
HETATM 9140 O  O   . HOH F 6 .    ? 17.791 41.870  25.296  1.00 22.35 ? 1881 HOH A O   1 
HETATM 9141 O  O   . HOH F 6 .    ? 18.493 39.472  26.161  1.00 32.33 ? 1882 HOH A O   1 
HETATM 9142 O  O   . HOH F 6 .    ? 25.884 37.577  29.429  1.00 14.96 ? 1883 HOH A O   1 
HETATM 9143 O  O   . HOH F 6 .    ? 29.788 36.563  29.265  1.00 21.68 ? 1884 HOH A O   1 
HETATM 9144 O  O   . HOH F 6 .    ? 36.730 37.247  25.239  1.00 35.45 ? 1885 HOH A O   1 
HETATM 9145 O  O   . HOH F 6 .    ? 37.029 40.167  26.572  1.00 28.30 ? 1886 HOH A O   1 
HETATM 9146 O  O   . HOH F 6 .    ? 34.910 43.519  28.874  1.00 12.86 ? 1887 HOH A O   1 
HETATM 9147 O  O   . HOH F 6 .    ? 35.644 45.115  30.903  1.00 16.77 ? 1888 HOH A O   1 
HETATM 9148 O  O   . HOH F 6 .    ? 37.356 46.903  29.821  1.00 19.81 ? 1889 HOH A O   1 
HETATM 9149 O  O   . HOH F 6 .    ? 36.937 45.610  27.603  1.00 13.68 ? 1890 HOH A O   1 
HETATM 9150 O  O   . HOH F 6 .    ? 39.616 45.401  25.991  1.00 30.11 ? 1891 HOH A O   1 
HETATM 9151 O  O   . HOH F 6 .    ? 38.869 42.971  22.879  1.00 24.15 ? 1892 HOH A O   1 
HETATM 9152 O  O   . HOH F 6 .    ? 39.479 39.584  20.108  1.00 29.66 ? 1893 HOH A O   1 
HETATM 9153 O  O   . HOH F 6 .    ? 39.089 38.925  17.329  1.00 16.10 ? 1894 HOH A O   1 
HETATM 9154 O  O   . HOH F 6 .    ? 41.764 39.191  16.701  1.00 27.39 ? 1895 HOH A O   1 
HETATM 9155 O  O   . HOH F 6 .    ? 38.217 36.300  17.781  1.00 34.71 ? 1896 HOH A O   1 
HETATM 9156 O  O   . HOH F 6 .    ? 34.102 34.362  16.244  1.00 20.87 ? 1897 HOH A O   1 
HETATM 9157 O  O   . HOH F 6 .    ? 31.826 33.613  17.046  1.00 27.87 ? 1898 HOH A O   1 
HETATM 9158 O  O   . HOH F 6 .    ? 29.421 31.534  22.051  1.00 34.41 ? 1899 HOH A O   1 
HETATM 9159 O  O   . HOH F 6 .    ? 29.651 30.000  24.526  1.00 38.19 ? 1900 HOH A O   1 
HETATM 9160 O  O   . HOH F 6 .    ? 20.710 31.849  31.878  1.00 41.41 ? 1901 HOH A O   1 
HETATM 9161 O  O   . HOH F 6 .    ? 11.302 33.350  22.702  1.00 35.89 ? 1902 HOH A O   1 
HETATM 9162 O  O   . HOH F 6 .    ? 11.381 41.342  19.623  1.00 25.06 ? 1903 HOH A O   1 
HETATM 9163 O  O   . HOH F 6 .    ? 12.218 43.356  20.160  1.00 37.15 ? 1904 HOH A O   1 
HETATM 9164 O  O   . HOH F 6 .    ? 10.963 46.805  21.563  1.00 29.31 ? 1905 HOH A O   1 
HETATM 9165 O  O   . HOH F 6 .    ? 12.361 45.305  23.583  1.00 28.65 ? 1906 HOH A O   1 
HETATM 9166 O  O   . HOH F 6 .    ? 11.321 46.960  17.854  1.00 19.67 ? 1907 HOH A O   1 
HETATM 9167 O  O   . HOH F 6 .    ? 12.286 49.584  17.709  1.00 17.04 ? 1908 HOH A O   1 
HETATM 9168 O  O   . HOH F 6 .    ? 14.107 49.920  19.724  1.00 13.28 ? 1909 HOH A O   1 
HETATM 9169 O  O   . HOH F 6 .    ? 13.222 51.598  21.693  1.00 15.70 ? 1910 HOH A O   1 
HETATM 9170 O  O   . HOH F 6 .    ? 10.575 51.661  21.356  1.00 24.21 ? 1911 HOH A O   1 
HETATM 9171 O  O   . HOH F 6 .    ? 10.048 50.851  18.845  1.00 22.82 ? 1912 HOH A O   1 
HETATM 9172 O  O   . HOH F 6 .    ? 9.161  52.509  16.835  1.00 16.93 ? 1913 HOH A O   1 
HETATM 9173 O  O   . HOH F 6 .    ? 7.296  54.548  17.260  1.00 31.22 ? 1914 HOH A O   1 
HETATM 9174 O  O   . HOH F 6 .    ? 11.628 51.633  14.303  1.00 12.99 ? 1915 HOH A O   1 
HETATM 9175 O  O   . HOH F 6 .    ? 13.829 49.109  15.416  1.00 12.91 ? 1916 HOH A O   1 
HETATM 9176 O  O   . HOH F 6 .    ? 8.216  48.490  19.387  1.00 35.84 ? 1917 HOH A O   1 
HETATM 9177 O  O   . HOH F 6 .    ? 5.965  46.753  15.968  1.00 30.98 ? 1918 HOH A O   1 
HETATM 9178 O  O   . HOH F 6 .    ? 8.486  44.691  12.858  1.00 28.37 ? 1919 HOH A O   1 
HETATM 9179 O  O   . HOH F 6 .    ? 7.861  48.210  11.934  1.00 22.38 ? 1920 HOH A O   1 
HETATM 9180 O  O   . HOH F 6 .    ? 7.376  50.961  12.423  1.00 35.83 ? 1921 HOH A O   1 
HETATM 9181 O  O   . HOH F 6 .    ? 6.871  51.692  9.280   1.00 41.64 ? 1922 HOH A O   1 
HETATM 9182 O  O   . HOH F 6 .    ? 8.888  50.468  8.034   1.00 26.15 ? 1923 HOH A O   1 
HETATM 9183 O  O   . HOH F 6 .    ? 8.251  49.778  5.751   1.00 32.59 ? 1924 HOH A O   1 
HETATM 9184 O  O   . HOH F 6 .    ? 11.217 53.208  6.811   1.00 14.60 ? 1925 HOH A O   1 
HETATM 9185 O  O   . HOH F 6 .    ? 5.215  57.619  6.893   1.00 29.80 ? 1926 HOH A O   1 
HETATM 9186 O  O   . HOH F 6 .    ? 13.136 62.944  11.896  1.00 24.51 ? 1927 HOH A O   1 
HETATM 9187 O  O   . HOH F 6 .    ? 13.705 62.531  14.616  1.00 23.43 ? 1928 HOH A O   1 
HETATM 9188 O  O   . HOH F 6 .    ? 15.374 60.440  15.429  1.00 13.32 ? 1929 HOH A O   1 
HETATM 9189 O  O   . HOH F 6 .    ? 13.856 58.330  16.275  1.00 13.38 ? 1930 HOH A O   1 
HETATM 9190 O  O   . HOH F 6 .    ? 13.818 57.823  18.945  1.00 16.55 ? 1931 HOH A O   1 
HETATM 9191 O  O   . HOH F 6 .    ? 11.408 58.470  19.920  1.00 27.01 ? 1932 HOH A O   1 
HETATM 9192 O  O   . HOH F 6 .    ? 10.371 57.311  21.824  1.00 45.72 ? 1933 HOH A O   1 
HETATM 9193 O  O   . HOH F 6 .    ? 12.003 55.482  22.302  1.00 29.72 ? 1934 HOH A O   1 
HETATM 9194 O  O   . HOH F 6 .    ? 11.782 62.317  22.703  1.00 34.02 ? 1935 HOH A O   1 
HETATM 9195 O  O   . HOH F 6 .    ? 17.996 60.747  24.324  1.00 14.38 ? 1936 HOH A O   1 
HETATM 9196 O  O   . HOH F 6 .    ? 11.383 61.780  16.118  1.00 40.95 ? 1937 HOH A O   1 
HETATM 9197 O  O   . HOH F 6 .    ? 19.044 72.478  2.927   1.00 15.73 ? 1938 HOH A O   1 
HETATM 9198 O  O   . HOH F 6 .    ? 19.347 67.399  -2.815  1.00 21.10 ? 1939 HOH A O   1 
HETATM 9199 O  O   . HOH F 6 .    ? 10.439 77.307  -5.391  1.00 29.16 ? 1940 HOH A O   1 
HETATM 9200 O  O   . HOH F 6 .    ? 13.987 88.226  -20.093 1.00 30.58 ? 1941 HOH A O   1 
HETATM 9201 O  O   . HOH F 6 .    ? 27.020 98.956  -26.062 1.00 36.60 ? 1942 HOH A O   1 
HETATM 9202 O  O   . HOH F 6 .    ? 31.697 96.518  -27.412 1.00 23.81 ? 1943 HOH A O   1 
HETATM 9203 O  O   . HOH F 6 .    ? 40.043 100.051 -32.066 1.00 34.18 ? 1944 HOH A O   1 
HETATM 9204 O  O   . HOH F 6 .    ? 46.262 99.934  -31.114 1.00 48.16 ? 1945 HOH A O   1 
HETATM 9205 O  O   . HOH F 6 .    ? 47.477 99.975  -33.269 1.00 33.87 ? 1946 HOH A O   1 
HETATM 9206 O  O   . HOH F 6 .    ? 48.555 97.884  -33.941 1.00 30.65 ? 1947 HOH A O   1 
HETATM 9207 O  O   . HOH F 6 .    ? 48.250 98.043  -28.689 1.00 26.01 ? 1948 HOH A O   1 
HETATM 9208 O  O   . HOH F 6 .    ? 48.271 89.183  -30.911 1.00 12.80 ? 1949 HOH A O   1 
HETATM 9209 O  O   . HOH F 6 .    ? 56.446 92.845  -29.926 1.00 23.99 ? 1950 HOH A O   1 
HETATM 9210 O  O   . HOH F 6 .    ? 45.973 94.783  -37.943 1.00 28.26 ? 1951 HOH A O   1 
HETATM 9211 O  O   . HOH F 6 .    ? 43.372 93.845  -37.853 1.00 19.36 ? 1952 HOH A O   1 
HETATM 9212 O  O   . HOH F 6 .    ? 41.300 94.777  -39.730 1.00 24.11 ? 1953 HOH A O   1 
HETATM 9213 O  O   . HOH F 6 .    ? 40.744 96.338  -37.596 1.00 25.79 ? 1954 HOH A O   1 
HETATM 9214 O  O   . HOH F 6 .    ? 43.130 98.025  -37.354 1.00 29.46 ? 1955 HOH A O   1 
HETATM 9215 O  O   . HOH F 6 .    ? 46.116 96.979  -43.933 1.00 21.64 ? 1956 HOH A O   1 
HETATM 9216 O  O   . HOH F 6 .    ? 39.562 95.961  -43.827 1.00 21.25 ? 1957 HOH A O   1 
HETATM 9217 O  O   . HOH F 6 .    ? 38.580 93.994  -42.372 1.00 22.67 ? 1958 HOH A O   1 
HETATM 9218 O  O   . HOH F 6 .    ? 42.065 87.705  -41.064 1.00 15.35 ? 1959 HOH A O   1 
HETATM 9219 O  O   . HOH F 6 .    ? 43.561 88.388  -38.783 1.00 13.79 ? 1960 HOH A O   1 
HETATM 9220 O  O   . HOH F 6 .    ? 38.936 86.612  -41.704 1.00 26.22 ? 1961 HOH A O   1 
HETATM 9221 O  O   . HOH F 6 .    ? 38.534 83.551  -39.995 1.00 23.83 ? 1962 HOH A O   1 
HETATM 9222 O  O   . HOH F 6 .    ? 34.063 86.655  -43.840 1.00 31.17 ? 1963 HOH A O   1 
HETATM 9223 O  O   . HOH F 6 .    ? 32.417 89.091  -43.209 1.00 24.40 ? 1964 HOH A O   1 
HETATM 9224 O  O   . HOH F 6 .    ? 34.068 73.714  -43.769 1.00 38.09 ? 1965 HOH A O   1 
HETATM 9225 O  O   . HOH F 6 .    ? 28.678 69.687  -39.551 1.00 18.24 ? 1966 HOH A O   1 
HETATM 9226 O  O   . HOH F 6 .    ? 24.662 71.756  -40.025 1.00 25.52 ? 1967 HOH A O   1 
HETATM 9227 O  O   . HOH F 6 .    ? 30.225 74.966  -29.337 1.00 10.82 ? 1968 HOH A O   1 
HETATM 9228 O  O   . HOH F 6 .    ? 32.297 77.687  -29.735 1.00 12.10 ? 1969 HOH A O   1 
HETATM 9229 O  O   . HOH F 6 .    ? 33.859 64.531  -32.364 1.00 12.80 ? 1970 HOH A O   1 
HETATM 9230 O  O   . HOH F 6 .    ? 35.982 63.544  -34.035 1.00 25.78 ? 1971 HOH A O   1 
HETATM 9231 O  O   . HOH F 6 .    ? 36.325 62.689  -38.528 1.00 33.64 ? 1972 HOH A O   1 
HETATM 9232 O  O   . HOH F 6 .    ? 36.464 63.308  -45.898 1.00 42.58 ? 1973 HOH A O   1 
HETATM 9233 O  O   . HOH F 6 .    ? 53.703 60.509  31.070  1.00 46.06 ? 1974 HOH A O   1 
HETATM 9234 O  O   . HOH F 6 .    ? 56.213 49.874  -30.074 1.00 41.72 ? 1975 HOH A O   1 
HETATM 9235 O  O   . HOH F 6 .    ? 59.999 52.730  -30.558 1.00 28.62 ? 1976 HOH A O   1 
HETATM 9236 O  O   . HOH F 6 .    ? 61.242 54.241  -29.034 1.00 20.86 ? 1977 HOH A O   1 
HETATM 9237 O  O   . HOH F 6 .    ? 58.681 53.670  -22.209 1.00 18.99 ? 1978 HOH A O   1 
HETATM 9238 O  O   . HOH F 6 .    ? 51.172 53.247  -23.942 1.00 9.40  ? 1979 HOH A O   1 
HETATM 9239 O  O   . HOH F 6 .    ? 53.565 64.787  -19.870 1.00 7.72  ? 1980 HOH A O   1 
HETATM 9240 O  O   . HOH F 6 .    ? 60.350 60.924  -18.158 1.00 8.86  ? 1981 HOH A O   1 
HETATM 9241 O  O   . HOH F 6 .    ? 55.519 59.334  -11.454 1.00 8.12  ? 1982 HOH A O   1 
HETATM 9242 O  O   . HOH F 6 .    ? 53.589 59.862  -9.375  1.00 10.96 ? 1983 HOH A O   1 
HETATM 9243 O  O   . HOH F 6 .    ? 50.799 59.896  -8.955  1.00 11.28 ? 1984 HOH A O   1 
HETATM 9244 O  O   . HOH F 6 .    ? 49.473 62.295  -8.627  1.00 10.91 ? 1985 HOH A O   1 
HETATM 9245 O  O   . HOH F 6 .    ? 49.903 59.516  -11.519 1.00 11.00 ? 1986 HOH A O   1 
HETATM 9246 O  O   . HOH F 6 .    ? 49.715 57.650  -7.543  1.00 10.16 ? 1987 HOH A O   1 
HETATM 9247 O  O   . HOH F 6 .    ? 51.365 56.672  -5.592  1.00 8.84  ? 1988 HOH A O   1 
HETATM 9248 O  O   . HOH F 6 .    ? 52.097 54.084  -4.826  1.00 7.97  ? 1989 HOH A O   1 
HETATM 9249 O  O   . HOH F 6 .    ? 52.675 58.891  -1.750  1.00 13.97 ? 1990 HOH A O   1 
HETATM 9250 O  O   . HOH F 6 .    ? 54.927 57.594  -0.407  1.00 14.51 ? 1991 HOH A O   1 
HETATM 9251 O  O   . HOH F 6 .    ? 60.461 54.786  -0.315  1.00 13.06 ? 1992 HOH A O   1 
HETATM 9252 O  O   . HOH F 6 .    ? 63.305 51.905  -0.506  1.00 26.91 ? 1993 HOH A O   1 
HETATM 9253 O  O   . HOH F 6 .    ? 59.430 52.143  2.615   1.00 30.19 ? 1994 HOH A O   1 
HETATM 9254 O  O   . HOH F 6 .    ? 58.430 52.732  4.700   1.00 28.63 ? 1995 HOH A O   1 
HETATM 9255 O  O   . HOH F 6 .    ? 59.441 48.955  2.259   1.00 29.83 ? 1996 HOH A O   1 
HETATM 9256 O  O   . HOH F 6 .    ? 52.068 50.550  6.372   1.00 10.10 ? 1997 HOH A O   1 
HETATM 9257 O  O   . HOH F 6 .    ? 44.339 46.063  10.079  1.00 15.06 ? 1998 HOH A O   1 
HETATM 9258 O  O   . HOH F 6 .    ? 42.924 48.058  11.328  1.00 13.92 ? 1999 HOH A O   1 
HETATM 9259 O  O   . HOH F 6 .    ? 41.542 43.258  8.073   1.00 16.03 ? 2000 HOH A O   1 
HETATM 9260 O  O   . HOH F 6 .    ? 40.007 39.344  9.166   1.00 20.96 ? 2001 HOH A O   1 
HETATM 9261 O  O   . HOH F 6 .    ? 40.659 36.286  8.589   1.00 27.94 ? 2002 HOH A O   1 
HETATM 9262 O  O   . HOH F 6 .    ? 39.930 35.425  11.378  1.00 22.26 ? 2003 HOH A O   1 
HETATM 9263 O  O   . HOH F 6 .    ? 37.248 33.662  5.874   1.00 41.12 ? 2004 HOH A O   1 
HETATM 9264 O  O   . HOH F 6 .    ? 34.719 36.470  3.411   1.00 30.18 ? 2005 HOH A O   1 
HETATM 9265 O  O   . HOH F 6 .    ? 37.135 37.571  2.935   1.00 33.00 ? 2006 HOH A O   1 
HETATM 9266 O  O   . HOH F 6 .    ? 38.162 40.081  1.788   1.00 10.75 ? 2007 HOH A O   1 
HETATM 9267 O  O   . HOH F 6 .    ? 36.637 44.941  -5.462  1.00 9.68  ? 2008 HOH A O   1 
HETATM 9268 O  O   . HOH F 6 .    ? 41.341 44.768  -6.829  1.00 12.82 ? 2009 HOH A O   1 
HETATM 9269 O  O   . HOH F 6 .    ? 43.475 41.855  -7.559  1.00 21.03 ? 2010 HOH A O   1 
HETATM 9270 O  O   . HOH F 6 .    ? 42.174 40.501  -9.704  1.00 31.50 ? 2011 HOH A O   1 
HETATM 9271 O  O   . HOH F 6 .    ? 42.421 39.436  -15.768 1.00 20.20 ? 2012 HOH A O   1 
HETATM 9272 O  O   . HOH F 6 .    ? 41.475 41.180  -17.618 1.00 16.50 ? 2013 HOH A O   1 
HETATM 9273 O  O   . HOH F 6 .    ? 47.145 41.337  -14.781 1.00 22.38 ? 2014 HOH A O   1 
HETATM 9274 O  O   . HOH F 6 .    ? 51.691 40.886  -13.159 1.00 27.37 ? 2015 HOH A O   1 
HETATM 9275 O  O   . HOH F 6 .    ? 50.946 44.193  -7.996  1.00 10.28 ? 2016 HOH A O   1 
HETATM 9276 O  O   . HOH F 6 .    ? 48.653 44.172  -6.085  1.00 17.14 ? 2017 HOH A O   1 
HETATM 9277 O  O   . HOH F 6 .    ? 47.928 43.942  -8.605  1.00 18.64 ? 2018 HOH A O   1 
HETATM 9278 O  O   . HOH F 6 .    ? 47.859 41.586  -5.353  1.00 27.40 ? 2019 HOH A O   1 
HETATM 9279 O  O   . HOH F 6 .    ? 48.363 39.239  -3.385  1.00 36.35 ? 2020 HOH A O   1 
HETATM 9280 O  O   . HOH F 6 .    ? 47.336 42.931  -2.333  1.00 14.45 ? 2021 HOH A O   1 
HETATM 9281 O  O   . HOH F 6 .    ? 46.384 43.160  9.769   1.00 33.89 ? 2022 HOH A O   1 
HETATM 9282 O  O   . HOH F 6 .    ? 39.313 57.364  14.884  1.00 8.37  ? 2023 HOH A O   1 
HETATM 9283 O  O   . HOH F 6 .    ? 41.173 58.986  13.559  1.00 9.29  ? 2024 HOH A O   1 
HETATM 9284 O  O   . HOH F 6 .    ? 37.753 59.056  11.126  1.00 9.37  ? 2025 HOH A O   1 
HETATM 9285 O  O   . HOH F 6 .    ? 36.858 57.757  13.461  1.00 8.70  ? 2026 HOH A O   1 
HETATM 9286 O  O   . HOH F 6 .    ? 38.692 62.360  8.449   1.00 11.21 ? 2027 HOH A O   1 
HETATM 9287 O  O   . HOH F 6 .    ? 40.247 62.786  6.171   1.00 7.85  ? 2028 HOH A O   1 
HETATM 9288 O  O   . HOH F 6 .    ? 49.296 68.263  6.708   1.00 26.78 ? 2029 HOH A O   1 
HETATM 9289 O  O   . HOH F 6 .    ? 49.833 67.458  4.239   1.00 16.80 ? 2030 HOH A O   1 
HETATM 9290 O  O   . HOH F 6 .    ? 51.937 68.913  4.241   1.00 34.01 ? 2031 HOH A O   1 
HETATM 9291 O  O   . HOH F 6 .    ? 52.294 70.950  5.933   1.00 32.15 ? 2032 HOH A O   1 
HETATM 9292 O  O   . HOH F 6 .    ? 52.667 72.992  4.275   1.00 37.16 ? 2033 HOH A O   1 
HETATM 9293 O  O   . HOH F 6 .    ? 50.432 72.422  9.208   1.00 21.25 ? 2034 HOH A O   1 
HETATM 9294 O  O   . HOH F 6 .    ? 51.222 66.535  8.548   1.00 23.71 ? 2035 HOH A O   1 
HETATM 9295 O  O   . HOH F 6 .    ? 43.485 73.148  5.825   1.00 10.27 ? 2036 HOH A O   1 
HETATM 9296 O  O   . HOH F 6 .    ? 45.951 70.990  0.050   1.00 14.73 ? 2037 HOH A O   1 
HETATM 9297 O  O   . HOH F 6 .    ? 37.814 73.402  -2.262  1.00 9.66  ? 2038 HOH A O   1 
HETATM 9298 O  O   . HOH F 6 .    ? 36.979 71.933  -4.569  1.00 7.26  ? 2039 HOH A O   1 
HETATM 9299 O  O   . HOH F 6 .    ? 36.541 72.711  0.263   1.00 8.29  ? 2040 HOH A O   1 
HETATM 9300 O  O   . HOH F 6 .    ? 33.272 78.665  -5.153  1.00 11.34 ? 2041 HOH A O   1 
HETATM 9301 O  O   . HOH F 6 .    ? 31.280 76.810  -6.334  1.00 10.37 ? 2042 HOH A O   1 
HETATM 9302 O  O   . HOH F 6 .    ? 41.946 63.504  -7.163  1.00 6.68  ? 2043 HOH A O   1 
HETATM 9303 O  O   . HOH F 6 .    ? 59.459 60.610  -6.210  1.00 12.94 ? 2044 HOH A O   1 
HETATM 9304 O  O   . HOH F 6 .    ? 60.972 59.664  -8.231  1.00 7.57  ? 2045 HOH A O   1 
HETATM 9305 O  O   . HOH F 6 .    ? 63.056 61.311  -7.583  1.00 8.86  ? 2046 HOH A O   1 
HETATM 9306 O  O   . HOH F 6 .    ? 63.015 61.051  -4.840  1.00 13.55 ? 2047 HOH A O   1 
HETATM 9307 O  O   . HOH F 6 .    ? 60.638 60.864  -3.572  1.00 11.96 ? 2048 HOH A O   1 
HETATM 9308 O  O   . HOH F 6 .    ? 60.450 62.210  -1.248  1.00 12.67 ? 2049 HOH A O   1 
HETATM 9309 O  O   . HOH F 6 .    ? 60.670 58.241  -2.785  1.00 10.76 ? 2050 HOH A O   1 
HETATM 9310 O  O   . HOH F 6 .    ? 64.784 59.247  -3.610  1.00 12.43 ? 2051 HOH A O   1 
HETATM 9311 O  O   . HOH F 6 .    ? 71.249 59.775  1.292   1.00 31.04 ? 2052 HOH A O   1 
HETATM 9312 O  O   . HOH F 6 .    ? 73.511 62.924  -0.700  1.00 34.28 ? 2053 HOH A O   1 
HETATM 9313 O  O   . HOH F 6 .    ? 74.146 52.113  1.524   1.00 32.14 ? 2054 HOH A O   1 
HETATM 9314 O  O   . HOH F 6 .    ? 72.340 50.779  2.029   1.00 35.96 ? 2055 HOH A O   1 
HETATM 9315 O  O   . HOH F 6 .    ? 70.839 49.427  0.015   1.00 20.67 ? 2056 HOH A O   1 
HETATM 9316 O  O   . HOH F 6 .    ? 71.928 46.826  -0.328  1.00 35.68 ? 2057 HOH A O   1 
HETATM 9317 O  O   . HOH F 6 .    ? 75.551 48.233  -5.656  1.00 40.21 ? 2058 HOH A O   1 
HETATM 9318 O  O   . HOH F 6 .    ? 10.263 50.496  -8.882  1.00 33.29 ? 2059 HOH A O   1 
HETATM 9319 O  O   . HOH F 6 .    ? 10.314 50.853  -11.253 1.00 46.98 ? 2060 HOH A O   1 
HETATM 9320 O  O   . HOH F 6 .    ? 73.229 51.402  -11.249 1.00 40.71 ? 2061 HOH A O   1 
HETATM 9321 O  O   . HOH F 6 .    ? 58.598 43.991  -28.018 1.00 29.93 ? 2062 HOH A O   1 
HETATM 9322 O  O   . HOH F 6 .    ? 36.304 36.129  -18.309 1.00 40.14 ? 2063 HOH A O   1 
HETATM 9323 O  O   . HOH F 6 .    ? 36.581 35.075  -15.935 1.00 30.48 ? 2064 HOH A O   1 
HETATM 9324 O  O   . HOH F 6 .    ? 35.520 38.747  -16.129 1.00 28.83 ? 2065 HOH A O   1 
HETATM 9325 O  O   . HOH F 6 .    ? 32.813 40.950  -18.000 1.00 22.73 ? 2066 HOH A O   1 
HETATM 9326 O  O   . HOH F 6 .    ? 25.574 36.196  -15.364 1.00 33.28 ? 2067 HOH A O   1 
HETATM 9327 O  O   . HOH F 6 .    ? 21.221 35.625  -5.143  1.00 30.77 ? 2068 HOH A O   1 
HETATM 9328 O  O   . HOH F 6 .    ? 21.826 36.850  0.146   1.00 19.29 ? 2069 HOH A O   1 
HETATM 9329 O  O   . HOH F 6 .    ? 24.763 34.186  0.415   1.00 40.44 ? 2070 HOH A O   1 
HETATM 9330 O  O   . HOH F 6 .    ? 24.673 33.125  6.660   1.00 20.55 ? 2071 HOH A O   1 
HETATM 9331 O  O   . HOH F 6 .    ? 24.375 33.113  9.585   1.00 24.95 ? 2072 HOH A O   1 
HETATM 9332 O  O   . HOH F 6 .    ? 26.115 40.087  7.993   1.00 10.32 ? 2073 HOH A O   1 
HETATM 9333 O  O   . HOH F 6 .    ? 25.716 39.779  5.277   1.00 10.36 ? 2074 HOH A O   1 
HETATM 9334 O  O   . HOH F 6 .    ? 23.880 41.977  6.943   1.00 9.67  ? 2075 HOH A O   1 
HETATM 9335 O  O   . HOH F 6 .    ? 27.995 39.644  11.285  1.00 10.73 ? 2076 HOH A O   1 
HETATM 9336 O  O   . HOH F 6 .    ? 31.025 33.580  2.826   1.00 20.40 ? 2077 HOH A O   1 
HETATM 9337 O  O   . HOH F 6 .    ? 30.963 29.787  5.629   1.00 33.02 ? 2078 HOH A O   1 
HETATM 9338 O  O   . HOH F 6 .    ? 36.691 29.114  12.999  1.00 29.54 ? 2079 HOH A O   1 
HETATM 9339 O  O   . HOH F 6 .    ? 18.248 36.682  5.806   1.00 29.70 ? 2080 HOH A O   1 
HETATM 9340 O  O   . HOH F 6 .    ? 17.097 41.659  9.261   1.00 32.09 ? 2081 HOH A O   1 
HETATM 9341 O  O   . HOH F 6 .    ? 12.720 42.507  12.449  1.00 17.94 ? 2082 HOH A O   1 
HETATM 9342 O  O   . HOH F 6 .    ? 12.323 46.721  30.557  1.00 29.62 ? 2083 HOH A O   1 
HETATM 9343 O  O   . HOH F 6 .    ? 14.362 47.155  32.511  1.00 20.14 ? 2084 HOH A O   1 
HETATM 9344 O  O   . HOH F 6 .    ? 27.713 49.491  38.497  1.00 22.23 ? 2085 HOH A O   1 
HETATM 9345 O  O   . HOH F 6 .    ? 28.791 47.076  37.217  1.00 17.25 ? 2086 HOH A O   1 
HETATM 9346 O  O   . HOH F 6 .    ? 31.276 47.379  38.093  1.00 32.42 ? 2087 HOH A O   1 
HETATM 9347 O  O   . HOH F 6 .    ? 34.110 47.862  36.219  1.00 36.08 ? 2088 HOH A O   1 
HETATM 9348 O  O   . HOH F 6 .    ? 34.432 45.735  33.366  1.00 17.26 ? 2089 HOH A O   1 
HETATM 9349 O  O   . HOH F 6 .    ? 27.815 44.419  38.271  1.00 30.19 ? 2090 HOH A O   1 
HETATM 9350 O  O   . HOH F 6 .    ? 29.908 51.287  39.867  1.00 45.70 ? 2091 HOH A O   1 
HETATM 9351 O  O   . HOH F 6 .    ? 27.389 52.234  42.562  1.00 26.28 ? 2092 HOH A O   1 
HETATM 9352 O  O   . HOH F 6 .    ? 26.620 50.932  45.335  1.00 32.49 ? 2093 HOH A O   1 
HETATM 9353 O  O   . HOH F 6 .    ? 26.964 47.547  45.712  1.00 42.15 ? 2094 HOH A O   1 
HETATM 9354 O  O   . HOH F 6 .    ? 28.963 47.598  47.157  1.00 49.54 ? 2095 HOH A O   1 
HETATM 9355 O  O   . HOH F 6 .    ? 24.008 61.031  36.074  1.00 25.47 ? 2096 HOH A O   1 
HETATM 9356 O  O   . HOH F 6 .    ? 29.483 65.581  32.578  1.00 27.97 ? 2097 HOH A O   1 
HETATM 9357 O  O   . HOH F 6 .    ? 28.818 64.388  30.177  1.00 17.53 ? 2098 HOH A O   1 
HETATM 9358 O  O   . HOH F 6 .    ? 27.740 67.549  28.230  1.00 17.14 ? 2099 HOH A O   1 
HETATM 9359 O  O   . HOH F 6 .    ? 61.396 92.413  -33.930 1.00 31.00 ? 2100 HOH A O   1 
HETATM 9360 O  O   . HOH F 6 .    ? 63.787 92.251  -34.394 1.00 22.68 ? 2101 HOH A O   1 
HETATM 9361 O  O   . HOH F 6 .    ? 33.601 60.237  23.285  1.00 11.45 ? 2102 HOH A O   1 
HETATM 9362 O  O   . HOH F 6 .    ? 51.199 79.403  -1.767  1.00 24.75 ? 2103 HOH A O   1 
HETATM 9363 O  O   . HOH F 6 .    ? 64.219 77.002  0.401   1.00 41.73 ? 2104 HOH A O   1 
HETATM 9364 O  O   . HOH F 6 .    ? 64.638 78.668  -1.558  1.00 24.30 ? 2105 HOH A O   1 
HETATM 9365 O  O   . HOH F 6 .    ? 65.381 77.443  2.912   1.00 35.07 ? 2106 HOH A O   1 
HETATM 9366 O  O   . HOH F 6 .    ? 54.876 81.000  -23.641 1.00 13.69 ? 2107 HOH A O   1 
HETATM 9367 O  O   . HOH F 6 .    ? 70.008 82.976  -29.948 1.00 20.96 ? 2108 HOH A O   1 
HETATM 9368 O  O   . HOH F 6 .    ? 72.254 95.652  -31.503 1.00 25.81 ? 2109 HOH A O   1 
HETATM 9369 O  O   . HOH F 6 .    ? 70.384 95.518  -35.281 1.00 40.23 ? 2110 HOH A O   1 
HETATM 9370 O  O   . HOH F 6 .    ? 62.086 81.629  -44.469 1.00 34.88 ? 2111 HOH A O   1 
HETATM 9371 O  O   . HOH F 6 .    ? 36.381 92.106  -17.688 1.00 34.18 ? 2112 HOH A O   1 
HETATM 9372 O  O   . HOH F 6 .    ? 29.552 102.088 -16.476 1.00 30.53 ? 2113 HOH A O   1 
HETATM 9373 O  O   . HOH F 6 .    ? 28.078 102.409 -19.169 1.00 24.21 ? 2114 HOH A O   1 
HETATM 9374 O  O   . HOH F 6 .    ? 19.808 46.783  -14.405 1.00 18.79 ? 2115 HOH A O   1 
HETATM 9375 O  O   . HOH F 6 .    ? 17.320 45.551  -14.170 1.00 37.11 ? 2116 HOH A O   1 
HETATM 9376 O  O   . HOH F 6 .    ? 15.870 44.885  -11.770 1.00 37.11 ? 2117 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 ?    ?   ?   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    1046 1    NAG NAG A . 
C 3 ZN  1    1047 1    ZN  ZN  A . 
D 4 SWA 1    1048 1    SWA SWA A . 
E 5 MRD 1    1049 1    MRD MRD A . 
F 6 HOH 1    1050 1    HOH HOH A . 
F 6 HOH 2    1051 2    HOH HOH A . 
F 6 HOH 3    1052 3    HOH HOH A . 
F 6 HOH 4    1053 4    HOH HOH A . 
F 6 HOH 5    1054 5    HOH HOH A . 
F 6 HOH 6    1055 6    HOH HOH A . 
F 6 HOH 7    1056 7    HOH HOH A . 
F 6 HOH 8    1057 8    HOH HOH A . 
F 6 HOH 9    1058 9    HOH HOH A . 
F 6 HOH 10   1059 10   HOH HOH A . 
F 6 HOH 11   1060 11   HOH HOH A . 
F 6 HOH 12   1061 12   HOH HOH A . 
F 6 HOH 13   1062 13   HOH HOH A . 
F 6 HOH 14   1063 14   HOH HOH A . 
F 6 HOH 15   1064 15   HOH HOH A . 
F 6 HOH 16   1065 16   HOH HOH A . 
F 6 HOH 17   1066 17   HOH HOH A . 
F 6 HOH 18   1067 18   HOH HOH A . 
F 6 HOH 19   1068 19   HOH HOH A . 
F 6 HOH 20   1069 20   HOH HOH A . 
F 6 HOH 21   1070 21   HOH HOH A . 
F 6 HOH 22   1071 22   HOH HOH A . 
F 6 HOH 23   1072 23   HOH HOH A . 
F 6 HOH 24   1073 24   HOH HOH A . 
F 6 HOH 25   1074 25   HOH HOH A . 
F 6 HOH 26   1075 26   HOH HOH A . 
F 6 HOH 27   1076 27   HOH HOH A . 
F 6 HOH 28   1077 28   HOH HOH A . 
F 6 HOH 29   1078 29   HOH HOH A . 
F 6 HOH 30   1079 30   HOH HOH A . 
F 6 HOH 31   1080 31   HOH HOH A . 
F 6 HOH 32   1081 32   HOH HOH A . 
F 6 HOH 33   1082 33   HOH HOH A . 
F 6 HOH 34   1083 34   HOH HOH A . 
F 6 HOH 35   1084 35   HOH HOH A . 
F 6 HOH 36   1085 36   HOH HOH A . 
F 6 HOH 37   1086 37   HOH HOH A . 
F 6 HOH 38   1087 38   HOH HOH A . 
F 6 HOH 39   1088 39   HOH HOH A . 
F 6 HOH 40   1089 40   HOH HOH A . 
F 6 HOH 41   1090 41   HOH HOH A . 
F 6 HOH 42   1091 42   HOH HOH A . 
F 6 HOH 43   1092 43   HOH HOH A . 
F 6 HOH 44   1093 44   HOH HOH A . 
F 6 HOH 45   1094 45   HOH HOH A . 
F 6 HOH 46   1095 46   HOH HOH A . 
F 6 HOH 47   1096 47   HOH HOH A . 
F 6 HOH 48   1097 48   HOH HOH A . 
F 6 HOH 49   1098 49   HOH HOH A . 
F 6 HOH 50   1099 50   HOH HOH A . 
F 6 HOH 51   1100 51   HOH HOH A . 
F 6 HOH 52   1101 52   HOH HOH A . 
F 6 HOH 53   1102 53   HOH HOH A . 
F 6 HOH 54   1103 54   HOH HOH A . 
F 6 HOH 55   1104 55   HOH HOH A . 
F 6 HOH 56   1105 56   HOH HOH A . 
F 6 HOH 57   1106 57   HOH HOH A . 
F 6 HOH 58   1107 58   HOH HOH A . 
F 6 HOH 59   1108 59   HOH HOH A . 
F 6 HOH 60   1109 60   HOH HOH A . 
F 6 HOH 61   1110 61   HOH HOH A . 
F 6 HOH 62   1111 62   HOH HOH A . 
F 6 HOH 63   1112 63   HOH HOH A . 
F 6 HOH 64   1113 64   HOH HOH A . 
F 6 HOH 65   1114 65   HOH HOH A . 
F 6 HOH 66   1115 66   HOH HOH A . 
F 6 HOH 67   1116 67   HOH HOH A . 
F 6 HOH 68   1117 68   HOH HOH A . 
F 6 HOH 69   1118 69   HOH HOH A . 
F 6 HOH 70   1119 70   HOH HOH A . 
F 6 HOH 71   1120 71   HOH HOH A . 
F 6 HOH 72   1121 72   HOH HOH A . 
F 6 HOH 73   1122 73   HOH HOH A . 
F 6 HOH 74   1123 74   HOH HOH A . 
F 6 HOH 75   1124 75   HOH HOH A . 
F 6 HOH 76   1125 76   HOH HOH A . 
F 6 HOH 77   1126 77   HOH HOH A . 
F 6 HOH 78   1127 78   HOH HOH A . 
F 6 HOH 79   1128 79   HOH HOH A . 
F 6 HOH 80   1129 80   HOH HOH A . 
F 6 HOH 81   1130 81   HOH HOH A . 
F 6 HOH 82   1131 82   HOH HOH A . 
F 6 HOH 83   1132 83   HOH HOH A . 
F 6 HOH 84   1133 84   HOH HOH A . 
F 6 HOH 85   1134 85   HOH HOH A . 
F 6 HOH 86   1135 86   HOH HOH A . 
F 6 HOH 87   1136 87   HOH HOH A . 
F 6 HOH 88   1137 88   HOH HOH A . 
F 6 HOH 89   1138 89   HOH HOH A . 
F 6 HOH 90   1139 90   HOH HOH A . 
F 6 HOH 91   1140 91   HOH HOH A . 
F 6 HOH 92   1141 92   HOH HOH A . 
F 6 HOH 93   1142 93   HOH HOH A . 
F 6 HOH 94   1143 94   HOH HOH A . 
F 6 HOH 95   1144 95   HOH HOH A . 
F 6 HOH 96   1145 96   HOH HOH A . 
F 6 HOH 97   1146 97   HOH HOH A . 
F 6 HOH 98   1147 98   HOH HOH A . 
F 6 HOH 99   1148 99   HOH HOH A . 
F 6 HOH 100  1149 100  HOH HOH A . 
F 6 HOH 101  1150 101  HOH HOH A . 
F 6 HOH 102  1151 102  HOH HOH A . 
F 6 HOH 103  1152 103  HOH HOH A . 
F 6 HOH 104  1153 104  HOH HOH A . 
F 6 HOH 105  1154 105  HOH HOH A . 
F 6 HOH 106  1155 106  HOH HOH A . 
F 6 HOH 107  1156 107  HOH HOH A . 
F 6 HOH 108  1157 108  HOH HOH A . 
F 6 HOH 109  1158 109  HOH HOH A . 
F 6 HOH 110  1159 110  HOH HOH A . 
F 6 HOH 111  1160 111  HOH HOH A . 
F 6 HOH 112  1161 112  HOH HOH A . 
F 6 HOH 113  1162 113  HOH HOH A . 
F 6 HOH 114  1163 114  HOH HOH A . 
F 6 HOH 115  1164 115  HOH HOH A . 
F 6 HOH 116  1165 116  HOH HOH A . 
F 6 HOH 117  1166 117  HOH HOH A . 
F 6 HOH 118  1167 118  HOH HOH A . 
F 6 HOH 119  1168 119  HOH HOH A . 
F 6 HOH 120  1169 120  HOH HOH A . 
F 6 HOH 121  1170 121  HOH HOH A . 
F 6 HOH 122  1171 122  HOH HOH A . 
F 6 HOH 123  1172 123  HOH HOH A . 
F 6 HOH 124  1173 124  HOH HOH A . 
F 6 HOH 125  1174 125  HOH HOH A . 
F 6 HOH 126  1175 126  HOH HOH A . 
F 6 HOH 127  1176 127  HOH HOH A . 
F 6 HOH 128  1177 128  HOH HOH A . 
F 6 HOH 129  1178 129  HOH HOH A . 
F 6 HOH 130  1179 130  HOH HOH A . 
F 6 HOH 131  1180 131  HOH HOH A . 
F 6 HOH 132  1181 132  HOH HOH A . 
F 6 HOH 133  1182 133  HOH HOH A . 
F 6 HOH 134  1183 134  HOH HOH A . 
F 6 HOH 135  1184 135  HOH HOH A . 
F 6 HOH 136  1185 136  HOH HOH A . 
F 6 HOH 137  1186 137  HOH HOH A . 
F 6 HOH 138  1187 138  HOH HOH A . 
F 6 HOH 139  1188 139  HOH HOH A . 
F 6 HOH 140  1189 140  HOH HOH A . 
F 6 HOH 141  1190 141  HOH HOH A . 
F 6 HOH 142  1191 142  HOH HOH A . 
F 6 HOH 143  1192 143  HOH HOH A . 
F 6 HOH 144  1193 144  HOH HOH A . 
F 6 HOH 145  1194 145  HOH HOH A . 
F 6 HOH 146  1195 146  HOH HOH A . 
F 6 HOH 147  1196 147  HOH HOH A . 
F 6 HOH 148  1197 148  HOH HOH A . 
F 6 HOH 149  1198 149  HOH HOH A . 
F 6 HOH 150  1199 150  HOH HOH A . 
F 6 HOH 151  1200 151  HOH HOH A . 
F 6 HOH 152  1201 152  HOH HOH A . 
F 6 HOH 153  1202 153  HOH HOH A . 
F 6 HOH 154  1203 154  HOH HOH A . 
F 6 HOH 155  1204 155  HOH HOH A . 
F 6 HOH 156  1205 156  HOH HOH A . 
F 6 HOH 157  1206 157  HOH HOH A . 
F 6 HOH 158  1207 158  HOH HOH A . 
F 6 HOH 159  1208 159  HOH HOH A . 
F 6 HOH 160  1209 160  HOH HOH A . 
F 6 HOH 161  1210 161  HOH HOH A . 
F 6 HOH 162  1211 162  HOH HOH A . 
F 6 HOH 163  1212 163  HOH HOH A . 
F 6 HOH 164  1213 164  HOH HOH A . 
F 6 HOH 165  1214 165  HOH HOH A . 
F 6 HOH 166  1215 166  HOH HOH A . 
F 6 HOH 167  1216 167  HOH HOH A . 
F 6 HOH 168  1217 168  HOH HOH A . 
F 6 HOH 169  1218 169  HOH HOH A . 
F 6 HOH 170  1219 170  HOH HOH A . 
F 6 HOH 171  1220 171  HOH HOH A . 
F 6 HOH 172  1221 172  HOH HOH A . 
F 6 HOH 173  1222 173  HOH HOH A . 
F 6 HOH 174  1223 174  HOH HOH A . 
F 6 HOH 175  1224 175  HOH HOH A . 
F 6 HOH 176  1225 176  HOH HOH A . 
F 6 HOH 177  1226 177  HOH HOH A . 
F 6 HOH 178  1227 178  HOH HOH A . 
F 6 HOH 179  1228 179  HOH HOH A . 
F 6 HOH 180  1229 180  HOH HOH A . 
F 6 HOH 181  1230 181  HOH HOH A . 
F 6 HOH 182  1231 182  HOH HOH A . 
F 6 HOH 183  1232 183  HOH HOH A . 
F 6 HOH 184  1233 184  HOH HOH A . 
F 6 HOH 185  1234 185  HOH HOH A . 
F 6 HOH 186  1235 186  HOH HOH A . 
F 6 HOH 187  1236 187  HOH HOH A . 
F 6 HOH 188  1237 188  HOH HOH A . 
F 6 HOH 189  1238 189  HOH HOH A . 
F 6 HOH 190  1239 190  HOH HOH A . 
F 6 HOH 191  1240 191  HOH HOH A . 
F 6 HOH 192  1241 192  HOH HOH A . 
F 6 HOH 193  1242 193  HOH HOH A . 
F 6 HOH 194  1243 194  HOH HOH A . 
F 6 HOH 195  1244 195  HOH HOH A . 
F 6 HOH 196  1245 196  HOH HOH A . 
F 6 HOH 197  1246 197  HOH HOH A . 
F 6 HOH 198  1247 198  HOH HOH A . 
F 6 HOH 199  1248 199  HOH HOH A . 
F 6 HOH 200  1249 200  HOH HOH A . 
F 6 HOH 201  1250 201  HOH HOH A . 
F 6 HOH 202  1251 202  HOH HOH A . 
F 6 HOH 203  1252 203  HOH HOH A . 
F 6 HOH 204  1253 204  HOH HOH A . 
F 6 HOH 205  1254 205  HOH HOH A . 
F 6 HOH 206  1255 206  HOH HOH A . 
F 6 HOH 207  1256 207  HOH HOH A . 
F 6 HOH 208  1257 208  HOH HOH A . 
F 6 HOH 209  1258 209  HOH HOH A . 
F 6 HOH 210  1259 210  HOH HOH A . 
F 6 HOH 211  1260 211  HOH HOH A . 
F 6 HOH 212  1261 212  HOH HOH A . 
F 6 HOH 213  1262 213  HOH HOH A . 
F 6 HOH 214  1263 214  HOH HOH A . 
F 6 HOH 215  1264 215  HOH HOH A . 
F 6 HOH 216  1265 216  HOH HOH A . 
F 6 HOH 217  1266 217  HOH HOH A . 
F 6 HOH 218  1267 218  HOH HOH A . 
F 6 HOH 219  1268 219  HOH HOH A . 
F 6 HOH 220  1269 220  HOH HOH A . 
F 6 HOH 221  1270 221  HOH HOH A . 
F 6 HOH 222  1271 222  HOH HOH A . 
F 6 HOH 223  1272 223  HOH HOH A . 
F 6 HOH 224  1273 224  HOH HOH A . 
F 6 HOH 225  1274 225  HOH HOH A . 
F 6 HOH 226  1275 226  HOH HOH A . 
F 6 HOH 227  1276 227  HOH HOH A . 
F 6 HOH 228  1277 228  HOH HOH A . 
F 6 HOH 229  1278 229  HOH HOH A . 
F 6 HOH 230  1279 230  HOH HOH A . 
F 6 HOH 231  1280 231  HOH HOH A . 
F 6 HOH 232  1281 232  HOH HOH A . 
F 6 HOH 233  1282 233  HOH HOH A . 
F 6 HOH 234  1283 234  HOH HOH A . 
F 6 HOH 235  1284 235  HOH HOH A . 
F 6 HOH 236  1285 236  HOH HOH A . 
F 6 HOH 237  1286 237  HOH HOH A . 
F 6 HOH 238  1287 238  HOH HOH A . 
F 6 HOH 239  1288 239  HOH HOH A . 
F 6 HOH 240  1289 240  HOH HOH A . 
F 6 HOH 241  1290 241  HOH HOH A . 
F 6 HOH 242  1291 242  HOH HOH A . 
F 6 HOH 243  1292 243  HOH HOH A . 
F 6 HOH 244  1293 244  HOH HOH A . 
F 6 HOH 245  1294 245  HOH HOH A . 
F 6 HOH 246  1295 246  HOH HOH A . 
F 6 HOH 247  1296 247  HOH HOH A . 
F 6 HOH 248  1297 248  HOH HOH A . 
F 6 HOH 249  1298 249  HOH HOH A . 
F 6 HOH 250  1299 250  HOH HOH A . 
F 6 HOH 251  1300 251  HOH HOH A . 
F 6 HOH 252  1301 252  HOH HOH A . 
F 6 HOH 253  1302 253  HOH HOH A . 
F 6 HOH 254  1303 254  HOH HOH A . 
F 6 HOH 255  1304 255  HOH HOH A . 
F 6 HOH 256  1305 256  HOH HOH A . 
F 6 HOH 257  1306 257  HOH HOH A . 
F 6 HOH 258  1307 258  HOH HOH A . 
F 6 HOH 259  1308 259  HOH HOH A . 
F 6 HOH 260  1309 260  HOH HOH A . 
F 6 HOH 261  1310 261  HOH HOH A . 
F 6 HOH 262  1311 262  HOH HOH A . 
F 6 HOH 263  1312 263  HOH HOH A . 
F 6 HOH 264  1313 264  HOH HOH A . 
F 6 HOH 265  1314 265  HOH HOH A . 
F 6 HOH 266  1315 266  HOH HOH A . 
F 6 HOH 267  1316 267  HOH HOH A . 
F 6 HOH 268  1317 268  HOH HOH A . 
F 6 HOH 269  1318 269  HOH HOH A . 
F 6 HOH 270  1319 270  HOH HOH A . 
F 6 HOH 271  1320 271  HOH HOH A . 
F 6 HOH 272  1321 272  HOH HOH A . 
F 6 HOH 273  1322 273  HOH HOH A . 
F 6 HOH 274  1323 274  HOH HOH A . 
F 6 HOH 275  1324 275  HOH HOH A . 
F 6 HOH 276  1325 276  HOH HOH A . 
F 6 HOH 277  1326 277  HOH HOH A . 
F 6 HOH 278  1327 278  HOH HOH A . 
F 6 HOH 279  1328 279  HOH HOH A . 
F 6 HOH 280  1329 280  HOH HOH A . 
F 6 HOH 281  1330 281  HOH HOH A . 
F 6 HOH 282  1331 282  HOH HOH A . 
F 6 HOH 283  1332 283  HOH HOH A . 
F 6 HOH 284  1333 284  HOH HOH A . 
F 6 HOH 285  1334 285  HOH HOH A . 
F 6 HOH 286  1335 286  HOH HOH A . 
F 6 HOH 287  1336 287  HOH HOH A . 
F 6 HOH 288  1337 288  HOH HOH A . 
F 6 HOH 289  1338 289  HOH HOH A . 
F 6 HOH 290  1339 290  HOH HOH A . 
F 6 HOH 291  1340 291  HOH HOH A . 
F 6 HOH 292  1341 292  HOH HOH A . 
F 6 HOH 293  1342 293  HOH HOH A . 
F 6 HOH 294  1343 294  HOH HOH A . 
F 6 HOH 295  1344 295  HOH HOH A . 
F 6 HOH 296  1345 296  HOH HOH A . 
F 6 HOH 297  1346 297  HOH HOH A . 
F 6 HOH 298  1347 298  HOH HOH A . 
F 6 HOH 299  1348 299  HOH HOH A . 
F 6 HOH 300  1349 300  HOH HOH A . 
F 6 HOH 301  1350 301  HOH HOH A . 
F 6 HOH 302  1351 302  HOH HOH A . 
F 6 HOH 303  1352 303  HOH HOH A . 
F 6 HOH 304  1353 304  HOH HOH A . 
F 6 HOH 305  1354 305  HOH HOH A . 
F 6 HOH 306  1355 306  HOH HOH A . 
F 6 HOH 307  1356 307  HOH HOH A . 
F 6 HOH 308  1357 308  HOH HOH A . 
F 6 HOH 309  1358 309  HOH HOH A . 
F 6 HOH 310  1359 310  HOH HOH A . 
F 6 HOH 311  1360 311  HOH HOH A . 
F 6 HOH 312  1361 312  HOH HOH A . 
F 6 HOH 313  1362 313  HOH HOH A . 
F 6 HOH 314  1363 314  HOH HOH A . 
F 6 HOH 315  1364 315  HOH HOH A . 
F 6 HOH 316  1365 316  HOH HOH A . 
F 6 HOH 317  1366 317  HOH HOH A . 
F 6 HOH 318  1367 318  HOH HOH A . 
F 6 HOH 319  1368 319  HOH HOH A . 
F 6 HOH 320  1369 320  HOH HOH A . 
F 6 HOH 321  1370 321  HOH HOH A . 
F 6 HOH 322  1371 322  HOH HOH A . 
F 6 HOH 323  1372 323  HOH HOH A . 
F 6 HOH 324  1373 324  HOH HOH A . 
F 6 HOH 325  1374 325  HOH HOH A . 
F 6 HOH 326  1375 326  HOH HOH A . 
F 6 HOH 327  1376 327  HOH HOH A . 
F 6 HOH 328  1377 328  HOH HOH A . 
F 6 HOH 329  1378 329  HOH HOH A . 
F 6 HOH 330  1379 330  HOH HOH A . 
F 6 HOH 331  1380 331  HOH HOH A . 
F 6 HOH 332  1381 332  HOH HOH A . 
F 6 HOH 333  1382 333  HOH HOH A . 
F 6 HOH 334  1383 334  HOH HOH A . 
F 6 HOH 335  1384 335  HOH HOH A . 
F 6 HOH 336  1385 336  HOH HOH A . 
F 6 HOH 337  1386 337  HOH HOH A . 
F 6 HOH 338  1387 338  HOH HOH A . 
F 6 HOH 339  1388 339  HOH HOH A . 
F 6 HOH 340  1389 340  HOH HOH A . 
F 6 HOH 341  1390 341  HOH HOH A . 
F 6 HOH 342  1391 342  HOH HOH A . 
F 6 HOH 343  1392 343  HOH HOH A . 
F 6 HOH 344  1393 344  HOH HOH A . 
F 6 HOH 345  1394 345  HOH HOH A . 
F 6 HOH 346  1395 346  HOH HOH A . 
F 6 HOH 347  1396 347  HOH HOH A . 
F 6 HOH 348  1397 348  HOH HOH A . 
F 6 HOH 349  1398 349  HOH HOH A . 
F 6 HOH 350  1399 350  HOH HOH A . 
F 6 HOH 351  1400 351  HOH HOH A . 
F 6 HOH 352  1401 352  HOH HOH A . 
F 6 HOH 353  1402 353  HOH HOH A . 
F 6 HOH 354  1403 354  HOH HOH A . 
F 6 HOH 355  1404 355  HOH HOH A . 
F 6 HOH 356  1405 356  HOH HOH A . 
F 6 HOH 357  1406 357  HOH HOH A . 
F 6 HOH 358  1407 358  HOH HOH A . 
F 6 HOH 359  1408 359  HOH HOH A . 
F 6 HOH 360  1409 360  HOH HOH A . 
F 6 HOH 361  1410 361  HOH HOH A . 
F 6 HOH 362  1411 362  HOH HOH A . 
F 6 HOH 363  1412 363  HOH HOH A . 
F 6 HOH 364  1413 364  HOH HOH A . 
F 6 HOH 365  1414 365  HOH HOH A . 
F 6 HOH 366  1415 366  HOH HOH A . 
F 6 HOH 367  1416 367  HOH HOH A . 
F 6 HOH 368  1417 368  HOH HOH A . 
F 6 HOH 369  1418 369  HOH HOH A . 
F 6 HOH 370  1419 370  HOH HOH A . 
F 6 HOH 371  1420 371  HOH HOH A . 
F 6 HOH 372  1421 372  HOH HOH A . 
F 6 HOH 373  1422 373  HOH HOH A . 
F 6 HOH 374  1423 374  HOH HOH A . 
F 6 HOH 375  1424 375  HOH HOH A . 
F 6 HOH 376  1425 376  HOH HOH A . 
F 6 HOH 377  1426 377  HOH HOH A . 
F 6 HOH 378  1427 378  HOH HOH A . 
F 6 HOH 379  1428 379  HOH HOH A . 
F 6 HOH 380  1429 380  HOH HOH A . 
F 6 HOH 381  1430 381  HOH HOH A . 
F 6 HOH 382  1431 382  HOH HOH A . 
F 6 HOH 383  1432 383  HOH HOH A . 
F 6 HOH 384  1433 384  HOH HOH A . 
F 6 HOH 385  1434 385  HOH HOH A . 
F 6 HOH 386  1435 386  HOH HOH A . 
F 6 HOH 387  1436 387  HOH HOH A . 
F 6 HOH 388  1437 388  HOH HOH A . 
F 6 HOH 389  1438 389  HOH HOH A . 
F 6 HOH 390  1439 390  HOH HOH A . 
F 6 HOH 391  1440 391  HOH HOH A . 
F 6 HOH 392  1441 392  HOH HOH A . 
F 6 HOH 393  1442 393  HOH HOH A . 
F 6 HOH 394  1443 394  HOH HOH A . 
F 6 HOH 395  1444 395  HOH HOH A . 
F 6 HOH 396  1445 396  HOH HOH A . 
F 6 HOH 397  1446 397  HOH HOH A . 
F 6 HOH 398  1447 398  HOH HOH A . 
F 6 HOH 399  1448 399  HOH HOH A . 
F 6 HOH 400  1449 400  HOH HOH A . 
F 6 HOH 401  1450 401  HOH HOH A . 
F 6 HOH 402  1451 402  HOH HOH A . 
F 6 HOH 403  1452 403  HOH HOH A . 
F 6 HOH 404  1453 404  HOH HOH A . 
F 6 HOH 405  1454 405  HOH HOH A . 
F 6 HOH 406  1455 406  HOH HOH A . 
F 6 HOH 407  1456 407  HOH HOH A . 
F 6 HOH 408  1457 408  HOH HOH A . 
F 6 HOH 409  1458 409  HOH HOH A . 
F 6 HOH 410  1459 410  HOH HOH A . 
F 6 HOH 411  1460 411  HOH HOH A . 
F 6 HOH 412  1461 412  HOH HOH A . 
F 6 HOH 413  1462 413  HOH HOH A . 
F 6 HOH 414  1463 414  HOH HOH A . 
F 6 HOH 415  1464 415  HOH HOH A . 
F 6 HOH 416  1465 416  HOH HOH A . 
F 6 HOH 417  1466 417  HOH HOH A . 
F 6 HOH 418  1467 418  HOH HOH A . 
F 6 HOH 419  1468 419  HOH HOH A . 
F 6 HOH 420  1469 420  HOH HOH A . 
F 6 HOH 421  1470 421  HOH HOH A . 
F 6 HOH 422  1471 422  HOH HOH A . 
F 6 HOH 423  1472 423  HOH HOH A . 
F 6 HOH 424  1473 424  HOH HOH A . 
F 6 HOH 425  1474 425  HOH HOH A . 
F 6 HOH 426  1475 426  HOH HOH A . 
F 6 HOH 427  1476 427  HOH HOH A . 
F 6 HOH 428  1477 428  HOH HOH A . 
F 6 HOH 429  1478 429  HOH HOH A . 
F 6 HOH 430  1479 430  HOH HOH A . 
F 6 HOH 431  1480 431  HOH HOH A . 
F 6 HOH 432  1481 432  HOH HOH A . 
F 6 HOH 433  1482 433  HOH HOH A . 
F 6 HOH 434  1483 434  HOH HOH A . 
F 6 HOH 435  1484 435  HOH HOH A . 
F 6 HOH 436  1485 436  HOH HOH A . 
F 6 HOH 437  1486 437  HOH HOH A . 
F 6 HOH 438  1487 438  HOH HOH A . 
F 6 HOH 439  1488 439  HOH HOH A . 
F 6 HOH 440  1489 440  HOH HOH A . 
F 6 HOH 441  1490 441  HOH HOH A . 
F 6 HOH 442  1491 442  HOH HOH A . 
F 6 HOH 443  1492 443  HOH HOH A . 
F 6 HOH 444  1493 444  HOH HOH A . 
F 6 HOH 445  1494 445  HOH HOH A . 
F 6 HOH 446  1495 446  HOH HOH A . 
F 6 HOH 447  1496 447  HOH HOH A . 
F 6 HOH 448  1497 448  HOH HOH A . 
F 6 HOH 449  1498 449  HOH HOH A . 
F 6 HOH 450  1499 450  HOH HOH A . 
F 6 HOH 451  1500 451  HOH HOH A . 
F 6 HOH 452  1501 452  HOH HOH A . 
F 6 HOH 453  1502 453  HOH HOH A . 
F 6 HOH 454  1503 454  HOH HOH A . 
F 6 HOH 455  1504 455  HOH HOH A . 
F 6 HOH 456  1505 456  HOH HOH A . 
F 6 HOH 457  1506 457  HOH HOH A . 
F 6 HOH 458  1507 458  HOH HOH A . 
F 6 HOH 459  1508 459  HOH HOH A . 
F 6 HOH 460  1509 460  HOH HOH A . 
F 6 HOH 461  1510 461  HOH HOH A . 
F 6 HOH 462  1511 462  HOH HOH A . 
F 6 HOH 463  1512 463  HOH HOH A . 
F 6 HOH 464  1513 464  HOH HOH A . 
F 6 HOH 465  1514 465  HOH HOH A . 
F 6 HOH 466  1515 466  HOH HOH A . 
F 6 HOH 467  1516 467  HOH HOH A . 
F 6 HOH 468  1517 468  HOH HOH A . 
F 6 HOH 469  1518 469  HOH HOH A . 
F 6 HOH 470  1519 470  HOH HOH A . 
F 6 HOH 471  1520 471  HOH HOH A . 
F 6 HOH 472  1521 472  HOH HOH A . 
F 6 HOH 473  1522 473  HOH HOH A . 
F 6 HOH 474  1523 474  HOH HOH A . 
F 6 HOH 475  1524 475  HOH HOH A . 
F 6 HOH 476  1525 476  HOH HOH A . 
F 6 HOH 477  1526 477  HOH HOH A . 
F 6 HOH 478  1527 478  HOH HOH A . 
F 6 HOH 479  1528 479  HOH HOH A . 
F 6 HOH 480  1529 480  HOH HOH A . 
F 6 HOH 481  1530 481  HOH HOH A . 
F 6 HOH 482  1531 482  HOH HOH A . 
F 6 HOH 483  1532 483  HOH HOH A . 
F 6 HOH 484  1533 484  HOH HOH A . 
F 6 HOH 485  1534 485  HOH HOH A . 
F 6 HOH 486  1535 486  HOH HOH A . 
F 6 HOH 487  1536 487  HOH HOH A . 
F 6 HOH 488  1537 488  HOH HOH A . 
F 6 HOH 489  1538 489  HOH HOH A . 
F 6 HOH 490  1539 490  HOH HOH A . 
F 6 HOH 491  1540 491  HOH HOH A . 
F 6 HOH 492  1541 492  HOH HOH A . 
F 6 HOH 493  1542 493  HOH HOH A . 
F 6 HOH 494  1543 494  HOH HOH A . 
F 6 HOH 495  1544 495  HOH HOH A . 
F 6 HOH 496  1545 496  HOH HOH A . 
F 6 HOH 497  1546 497  HOH HOH A . 
F 6 HOH 498  1547 498  HOH HOH A . 
F 6 HOH 499  1548 499  HOH HOH A . 
F 6 HOH 500  1549 500  HOH HOH A . 
F 6 HOH 501  1550 501  HOH HOH A . 
F 6 HOH 502  1551 502  HOH HOH A . 
F 6 HOH 503  1552 503  HOH HOH A . 
F 6 HOH 504  1553 504  HOH HOH A . 
F 6 HOH 505  1554 505  HOH HOH A . 
F 6 HOH 506  1555 506  HOH HOH A . 
F 6 HOH 507  1556 507  HOH HOH A . 
F 6 HOH 508  1557 508  HOH HOH A . 
F 6 HOH 509  1558 509  HOH HOH A . 
F 6 HOH 510  1559 510  HOH HOH A . 
F 6 HOH 511  1560 511  HOH HOH A . 
F 6 HOH 512  1561 512  HOH HOH A . 
F 6 HOH 513  1562 513  HOH HOH A . 
F 6 HOH 514  1563 514  HOH HOH A . 
F 6 HOH 515  1564 515  HOH HOH A . 
F 6 HOH 516  1565 516  HOH HOH A . 
F 6 HOH 517  1566 517  HOH HOH A . 
F 6 HOH 518  1567 518  HOH HOH A . 
F 6 HOH 519  1568 519  HOH HOH A . 
F 6 HOH 520  1569 520  HOH HOH A . 
F 6 HOH 521  1570 521  HOH HOH A . 
F 6 HOH 522  1571 522  HOH HOH A . 
F 6 HOH 523  1572 523  HOH HOH A . 
F 6 HOH 524  1573 524  HOH HOH A . 
F 6 HOH 525  1574 525  HOH HOH A . 
F 6 HOH 526  1575 526  HOH HOH A . 
F 6 HOH 527  1576 527  HOH HOH A . 
F 6 HOH 528  1577 528  HOH HOH A . 
F 6 HOH 529  1578 529  HOH HOH A . 
F 6 HOH 530  1579 530  HOH HOH A . 
F 6 HOH 531  1580 531  HOH HOH A . 
F 6 HOH 532  1581 532  HOH HOH A . 
F 6 HOH 533  1582 533  HOH HOH A . 
F 6 HOH 534  1583 534  HOH HOH A . 
F 6 HOH 535  1584 535  HOH HOH A . 
F 6 HOH 536  1585 536  HOH HOH A . 
F 6 HOH 537  1586 537  HOH HOH A . 
F 6 HOH 538  1587 538  HOH HOH A . 
F 6 HOH 539  1588 539  HOH HOH A . 
F 6 HOH 540  1589 540  HOH HOH A . 
F 6 HOH 541  1590 541  HOH HOH A . 
F 6 HOH 542  1591 542  HOH HOH A . 
F 6 HOH 543  1592 543  HOH HOH A . 
F 6 HOH 544  1593 544  HOH HOH A . 
F 6 HOH 545  1594 545  HOH HOH A . 
F 6 HOH 546  1595 546  HOH HOH A . 
F 6 HOH 547  1596 547  HOH HOH A . 
F 6 HOH 548  1597 548  HOH HOH A . 
F 6 HOH 549  1598 549  HOH HOH A . 
F 6 HOH 550  1599 550  HOH HOH A . 
F 6 HOH 551  1600 551  HOH HOH A . 
F 6 HOH 552  1601 552  HOH HOH A . 
F 6 HOH 553  1602 553  HOH HOH A . 
F 6 HOH 554  1603 554  HOH HOH A . 
F 6 HOH 555  1604 555  HOH HOH A . 
F 6 HOH 556  1605 556  HOH HOH A . 
F 6 HOH 557  1606 557  HOH HOH A . 
F 6 HOH 558  1607 558  HOH HOH A . 
F 6 HOH 559  1608 559  HOH HOH A . 
F 6 HOH 560  1609 560  HOH HOH A . 
F 6 HOH 561  1610 561  HOH HOH A . 
F 6 HOH 562  1611 562  HOH HOH A . 
F 6 HOH 563  1612 563  HOH HOH A . 
F 6 HOH 564  1613 564  HOH HOH A . 
F 6 HOH 565  1614 565  HOH HOH A . 
F 6 HOH 566  1615 566  HOH HOH A . 
F 6 HOH 567  1616 567  HOH HOH A . 
F 6 HOH 568  1617 568  HOH HOH A . 
F 6 HOH 569  1618 569  HOH HOH A . 
F 6 HOH 570  1619 570  HOH HOH A . 
F 6 HOH 571  1620 571  HOH HOH A . 
F 6 HOH 572  1621 572  HOH HOH A . 
F 6 HOH 573  1622 573  HOH HOH A . 
F 6 HOH 574  1623 574  HOH HOH A . 
F 6 HOH 575  1624 575  HOH HOH A . 
F 6 HOH 576  1625 576  HOH HOH A . 
F 6 HOH 577  1626 577  HOH HOH A . 
F 6 HOH 578  1627 578  HOH HOH A . 
F 6 HOH 579  1628 579  HOH HOH A . 
F 6 HOH 580  1629 580  HOH HOH A . 
F 6 HOH 581  1630 581  HOH HOH A . 
F 6 HOH 582  1631 582  HOH HOH A . 
F 6 HOH 583  1632 583  HOH HOH A . 
F 6 HOH 584  1633 584  HOH HOH A . 
F 6 HOH 585  1634 585  HOH HOH A . 
F 6 HOH 586  1635 586  HOH HOH A . 
F 6 HOH 587  1636 587  HOH HOH A . 
F 6 HOH 588  1637 588  HOH HOH A . 
F 6 HOH 589  1638 589  HOH HOH A . 
F 6 HOH 590  1639 590  HOH HOH A . 
F 6 HOH 591  1640 591  HOH HOH A . 
F 6 HOH 592  1641 592  HOH HOH A . 
F 6 HOH 593  1642 593  HOH HOH A . 
F 6 HOH 594  1643 594  HOH HOH A . 
F 6 HOH 595  1644 595  HOH HOH A . 
F 6 HOH 596  1645 596  HOH HOH A . 
F 6 HOH 597  1646 597  HOH HOH A . 
F 6 HOH 598  1647 598  HOH HOH A . 
F 6 HOH 599  1648 599  HOH HOH A . 
F 6 HOH 600  1649 600  HOH HOH A . 
F 6 HOH 601  1650 601  HOH HOH A . 
F 6 HOH 602  1651 602  HOH HOH A . 
F 6 HOH 603  1652 603  HOH HOH A . 
F 6 HOH 604  1653 604  HOH HOH A . 
F 6 HOH 605  1654 605  HOH HOH A . 
F 6 HOH 606  1655 606  HOH HOH A . 
F 6 HOH 607  1656 607  HOH HOH A . 
F 6 HOH 608  1657 608  HOH HOH A . 
F 6 HOH 609  1658 609  HOH HOH A . 
F 6 HOH 610  1659 610  HOH HOH A . 
F 6 HOH 611  1660 611  HOH HOH A . 
F 6 HOH 612  1661 612  HOH HOH A . 
F 6 HOH 613  1662 613  HOH HOH A . 
F 6 HOH 614  1663 614  HOH HOH A . 
F 6 HOH 615  1664 615  HOH HOH A . 
F 6 HOH 616  1665 616  HOH HOH A . 
F 6 HOH 617  1666 617  HOH HOH A . 
F 6 HOH 618  1667 618  HOH HOH A . 
F 6 HOH 619  1668 619  HOH HOH A . 
F 6 HOH 620  1669 620  HOH HOH A . 
F 6 HOH 621  1670 621  HOH HOH A . 
F 6 HOH 622  1671 622  HOH HOH A . 
F 6 HOH 623  1672 623  HOH HOH A . 
F 6 HOH 624  1673 624  HOH HOH A . 
F 6 HOH 625  1674 625  HOH HOH A . 
F 6 HOH 626  1675 626  HOH HOH A . 
F 6 HOH 627  1676 627  HOH HOH A . 
F 6 HOH 628  1677 628  HOH HOH A . 
F 6 HOH 629  1678 629  HOH HOH A . 
F 6 HOH 630  1679 630  HOH HOH A . 
F 6 HOH 631  1680 631  HOH HOH A . 
F 6 HOH 632  1681 632  HOH HOH A . 
F 6 HOH 633  1682 633  HOH HOH A . 
F 6 HOH 634  1683 634  HOH HOH A . 
F 6 HOH 635  1684 635  HOH HOH A . 
F 6 HOH 636  1685 636  HOH HOH A . 
F 6 HOH 637  1686 637  HOH HOH A . 
F 6 HOH 638  1687 638  HOH HOH A . 
F 6 HOH 639  1688 639  HOH HOH A . 
F 6 HOH 640  1689 640  HOH HOH A . 
F 6 HOH 641  1690 641  HOH HOH A . 
F 6 HOH 642  1691 642  HOH HOH A . 
F 6 HOH 643  1692 643  HOH HOH A . 
F 6 HOH 644  1693 644  HOH HOH A . 
F 6 HOH 645  1694 645  HOH HOH A . 
F 6 HOH 646  1695 646  HOH HOH A . 
F 6 HOH 647  1696 647  HOH HOH A . 
F 6 HOH 648  1697 648  HOH HOH A . 
F 6 HOH 649  1698 649  HOH HOH A . 
F 6 HOH 650  1699 650  HOH HOH A . 
F 6 HOH 651  1700 651  HOH HOH A . 
F 6 HOH 652  1701 652  HOH HOH A . 
F 6 HOH 653  1702 653  HOH HOH A . 
F 6 HOH 654  1703 654  HOH HOH A . 
F 6 HOH 655  1704 655  HOH HOH A . 
F 6 HOH 656  1705 656  HOH HOH A . 
F 6 HOH 657  1706 657  HOH HOH A . 
F 6 HOH 658  1707 658  HOH HOH A . 
F 6 HOH 659  1708 659  HOH HOH A . 
F 6 HOH 660  1709 660  HOH HOH A . 
F 6 HOH 661  1710 661  HOH HOH A . 
F 6 HOH 662  1711 662  HOH HOH A . 
F 6 HOH 663  1712 663  HOH HOH A . 
F 6 HOH 664  1713 664  HOH HOH A . 
F 6 HOH 665  1714 665  HOH HOH A . 
F 6 HOH 666  1715 666  HOH HOH A . 
F 6 HOH 667  1716 667  HOH HOH A . 
F 6 HOH 668  1717 668  HOH HOH A . 
F 6 HOH 669  1718 669  HOH HOH A . 
F 6 HOH 670  1719 670  HOH HOH A . 
F 6 HOH 671  1720 671  HOH HOH A . 
F 6 HOH 672  1721 672  HOH HOH A . 
F 6 HOH 673  1722 673  HOH HOH A . 
F 6 HOH 674  1723 674  HOH HOH A . 
F 6 HOH 675  1724 675  HOH HOH A . 
F 6 HOH 676  1725 676  HOH HOH A . 
F 6 HOH 677  1726 677  HOH HOH A . 
F 6 HOH 678  1727 678  HOH HOH A . 
F 6 HOH 679  1728 679  HOH HOH A . 
F 6 HOH 680  1729 680  HOH HOH A . 
F 6 HOH 681  1730 681  HOH HOH A . 
F 6 HOH 682  1731 682  HOH HOH A . 
F 6 HOH 683  1732 683  HOH HOH A . 
F 6 HOH 684  1733 684  HOH HOH A . 
F 6 HOH 685  1734 685  HOH HOH A . 
F 6 HOH 686  1735 686  HOH HOH A . 
F 6 HOH 687  1736 687  HOH HOH A . 
F 6 HOH 688  1737 688  HOH HOH A . 
F 6 HOH 689  1738 689  HOH HOH A . 
F 6 HOH 690  1739 690  HOH HOH A . 
F 6 HOH 691  1740 691  HOH HOH A . 
F 6 HOH 692  1741 692  HOH HOH A . 
F 6 HOH 693  1742 693  HOH HOH A . 
F 6 HOH 694  1743 694  HOH HOH A . 
F 6 HOH 695  1744 695  HOH HOH A . 
F 6 HOH 696  1745 696  HOH HOH A . 
F 6 HOH 697  1746 697  HOH HOH A . 
F 6 HOH 698  1747 698  HOH HOH A . 
F 6 HOH 699  1748 699  HOH HOH A . 
F 6 HOH 700  1749 700  HOH HOH A . 
F 6 HOH 701  1750 701  HOH HOH A . 
F 6 HOH 702  1751 702  HOH HOH A . 
F 6 HOH 703  1752 703  HOH HOH A . 
F 6 HOH 704  1753 704  HOH HOH A . 
F 6 HOH 705  1754 705  HOH HOH A . 
F 6 HOH 706  1755 706  HOH HOH A . 
F 6 HOH 707  1756 707  HOH HOH A . 
F 6 HOH 708  1757 708  HOH HOH A . 
F 6 HOH 709  1758 709  HOH HOH A . 
F 6 HOH 710  1759 710  HOH HOH A . 
F 6 HOH 711  1760 711  HOH HOH A . 
F 6 HOH 712  1761 712  HOH HOH A . 
F 6 HOH 713  1762 713  HOH HOH A . 
F 6 HOH 714  1763 714  HOH HOH A . 
F 6 HOH 715  1764 715  HOH HOH A . 
F 6 HOH 716  1765 716  HOH HOH A . 
F 6 HOH 717  1766 717  HOH HOH A . 
F 6 HOH 718  1767 718  HOH HOH A . 
F 6 HOH 719  1768 719  HOH HOH A . 
F 6 HOH 720  1769 720  HOH HOH A . 
F 6 HOH 721  1770 721  HOH HOH A . 
F 6 HOH 722  1771 722  HOH HOH A . 
F 6 HOH 723  1772 723  HOH HOH A . 
F 6 HOH 724  1773 724  HOH HOH A . 
F 6 HOH 725  1774 725  HOH HOH A . 
F 6 HOH 726  1775 726  HOH HOH A . 
F 6 HOH 727  1776 727  HOH HOH A . 
F 6 HOH 728  1777 728  HOH HOH A . 
F 6 HOH 729  1778 729  HOH HOH A . 
F 6 HOH 730  1779 730  HOH HOH A . 
F 6 HOH 731  1780 731  HOH HOH A . 
F 6 HOH 732  1781 732  HOH HOH A . 
F 6 HOH 733  1782 733  HOH HOH A . 
F 6 HOH 734  1783 734  HOH HOH A . 
F 6 HOH 735  1784 735  HOH HOH A . 
F 6 HOH 736  1785 736  HOH HOH A . 
F 6 HOH 737  1786 737  HOH HOH A . 
F 6 HOH 738  1787 738  HOH HOH A . 
F 6 HOH 739  1788 739  HOH HOH A . 
F 6 HOH 740  1789 740  HOH HOH A . 
F 6 HOH 741  1790 741  HOH HOH A . 
F 6 HOH 742  1791 742  HOH HOH A . 
F 6 HOH 743  1792 743  HOH HOH A . 
F 6 HOH 744  1793 744  HOH HOH A . 
F 6 HOH 745  1794 745  HOH HOH A . 
F 6 HOH 746  1795 746  HOH HOH A . 
F 6 HOH 747  1796 747  HOH HOH A . 
F 6 HOH 748  1797 748  HOH HOH A . 
F 6 HOH 749  1798 749  HOH HOH A . 
F 6 HOH 750  1799 750  HOH HOH A . 
F 6 HOH 751  1800 751  HOH HOH A . 
F 6 HOH 752  1801 752  HOH HOH A . 
F 6 HOH 753  1802 753  HOH HOH A . 
F 6 HOH 754  1803 754  HOH HOH A . 
F 6 HOH 755  1804 755  HOH HOH A . 
F 6 HOH 756  1805 756  HOH HOH A . 
F 6 HOH 757  1806 757  HOH HOH A . 
F 6 HOH 758  1807 758  HOH HOH A . 
F 6 HOH 759  1808 759  HOH HOH A . 
F 6 HOH 760  1809 760  HOH HOH A . 
F 6 HOH 761  1810 761  HOH HOH A . 
F 6 HOH 762  1811 762  HOH HOH A . 
F 6 HOH 763  1812 763  HOH HOH A . 
F 6 HOH 764  1813 764  HOH HOH A . 
F 6 HOH 765  1814 765  HOH HOH A . 
F 6 HOH 766  1815 766  HOH HOH A . 
F 6 HOH 767  1816 767  HOH HOH A . 
F 6 HOH 768  1817 768  HOH HOH A . 
F 6 HOH 769  1818 769  HOH HOH A . 
F 6 HOH 770  1819 770  HOH HOH A . 
F 6 HOH 771  1820 771  HOH HOH A . 
F 6 HOH 772  1821 772  HOH HOH A . 
F 6 HOH 773  1822 773  HOH HOH A . 
F 6 HOH 774  1823 774  HOH HOH A . 
F 6 HOH 775  1824 775  HOH HOH A . 
F 6 HOH 776  1825 776  HOH HOH A . 
F 6 HOH 777  1826 777  HOH HOH A . 
F 6 HOH 778  1827 778  HOH HOH A . 
F 6 HOH 779  1828 779  HOH HOH A . 
F 6 HOH 780  1829 780  HOH HOH A . 
F 6 HOH 781  1830 781  HOH HOH A . 
F 6 HOH 782  1831 782  HOH HOH A . 
F 6 HOH 783  1832 783  HOH HOH A . 
F 6 HOH 784  1833 784  HOH HOH A . 
F 6 HOH 785  1834 785  HOH HOH A . 
F 6 HOH 786  1835 786  HOH HOH A . 
F 6 HOH 787  1836 787  HOH HOH A . 
F 6 HOH 788  1837 788  HOH HOH A . 
F 6 HOH 789  1838 789  HOH HOH A . 
F 6 HOH 790  1839 790  HOH HOH A . 
F 6 HOH 791  1840 791  HOH HOH A . 
F 6 HOH 792  1841 792  HOH HOH A . 
F 6 HOH 793  1842 793  HOH HOH A . 
F 6 HOH 794  1843 794  HOH HOH A . 
F 6 HOH 795  1844 795  HOH HOH A . 
F 6 HOH 796  1845 796  HOH HOH A . 
F 6 HOH 797  1846 797  HOH HOH A . 
F 6 HOH 798  1847 798  HOH HOH A . 
F 6 HOH 799  1848 799  HOH HOH A . 
F 6 HOH 800  1849 800  HOH HOH A . 
F 6 HOH 801  1850 801  HOH HOH A . 
F 6 HOH 802  1851 802  HOH HOH A . 
F 6 HOH 803  1852 803  HOH HOH A . 
F 6 HOH 804  1853 804  HOH HOH A . 
F 6 HOH 805  1854 805  HOH HOH A . 
F 6 HOH 806  1855 806  HOH HOH A . 
F 6 HOH 807  1856 807  HOH HOH A . 
F 6 HOH 808  1857 808  HOH HOH A . 
F 6 HOH 809  1858 809  HOH HOH A . 
F 6 HOH 810  1859 810  HOH HOH A . 
F 6 HOH 811  1860 811  HOH HOH A . 
F 6 HOH 812  1861 812  HOH HOH A . 
F 6 HOH 813  1862 813  HOH HOH A . 
F 6 HOH 814  1863 814  HOH HOH A . 
F 6 HOH 815  1864 815  HOH HOH A . 
F 6 HOH 816  1865 816  HOH HOH A . 
F 6 HOH 817  1866 817  HOH HOH A . 
F 6 HOH 818  1867 818  HOH HOH A . 
F 6 HOH 819  1868 819  HOH HOH A . 
F 6 HOH 820  1869 820  HOH HOH A . 
F 6 HOH 821  1870 821  HOH HOH A . 
F 6 HOH 822  1871 822  HOH HOH A . 
F 6 HOH 823  1872 823  HOH HOH A . 
F 6 HOH 824  1873 824  HOH HOH A . 
F 6 HOH 825  1874 825  HOH HOH A . 
F 6 HOH 826  1875 826  HOH HOH A . 
F 6 HOH 827  1876 827  HOH HOH A . 
F 6 HOH 828  1877 828  HOH HOH A . 
F 6 HOH 829  1878 829  HOH HOH A . 
F 6 HOH 830  1879 830  HOH HOH A . 
F 6 HOH 831  1880 831  HOH HOH A . 
F 6 HOH 832  1881 832  HOH HOH A . 
F 6 HOH 833  1882 833  HOH HOH A . 
F 6 HOH 834  1883 834  HOH HOH A . 
F 6 HOH 835  1884 835  HOH HOH A . 
F 6 HOH 836  1885 836  HOH HOH A . 
F 6 HOH 837  1886 837  HOH HOH A . 
F 6 HOH 838  1887 838  HOH HOH A . 
F 6 HOH 839  1888 839  HOH HOH A . 
F 6 HOH 840  1889 840  HOH HOH A . 
F 6 HOH 841  1890 841  HOH HOH A . 
F 6 HOH 842  1891 842  HOH HOH A . 
F 6 HOH 843  1892 843  HOH HOH A . 
F 6 HOH 844  1893 844  HOH HOH A . 
F 6 HOH 845  1894 845  HOH HOH A . 
F 6 HOH 846  1895 846  HOH HOH A . 
F 6 HOH 847  1896 847  HOH HOH A . 
F 6 HOH 848  1897 848  HOH HOH A . 
F 6 HOH 849  1898 849  HOH HOH A . 
F 6 HOH 850  1899 850  HOH HOH A . 
F 6 HOH 851  1900 851  HOH HOH A . 
F 6 HOH 852  1901 852  HOH HOH A . 
F 6 HOH 853  1902 853  HOH HOH A . 
F 6 HOH 854  1903 854  HOH HOH A . 
F 6 HOH 855  1904 855  HOH HOH A . 
F 6 HOH 856  1905 856  HOH HOH A . 
F 6 HOH 857  1906 857  HOH HOH A . 
F 6 HOH 858  1907 858  HOH HOH A . 
F 6 HOH 859  1908 859  HOH HOH A . 
F 6 HOH 860  1909 860  HOH HOH A . 
F 6 HOH 861  1910 861  HOH HOH A . 
F 6 HOH 862  1911 862  HOH HOH A . 
F 6 HOH 863  1912 863  HOH HOH A . 
F 6 HOH 864  1913 864  HOH HOH A . 
F 6 HOH 865  1914 865  HOH HOH A . 
F 6 HOH 866  1915 866  HOH HOH A . 
F 6 HOH 867  1916 867  HOH HOH A . 
F 6 HOH 868  1917 868  HOH HOH A . 
F 6 HOH 869  1918 869  HOH HOH A . 
F 6 HOH 870  1919 870  HOH HOH A . 
F 6 HOH 871  1920 871  HOH HOH A . 
F 6 HOH 872  1921 872  HOH HOH A . 
F 6 HOH 873  1922 873  HOH HOH A . 
F 6 HOH 874  1923 874  HOH HOH A . 
F 6 HOH 875  1924 875  HOH HOH A . 
F 6 HOH 876  1925 876  HOH HOH A . 
F 6 HOH 877  1926 877  HOH HOH A . 
F 6 HOH 878  1927 878  HOH HOH A . 
F 6 HOH 879  1928 879  HOH HOH A . 
F 6 HOH 880  1929 880  HOH HOH A . 
F 6 HOH 881  1930 881  HOH HOH A . 
F 6 HOH 882  1931 882  HOH HOH A . 
F 6 HOH 883  1932 883  HOH HOH A . 
F 6 HOH 884  1933 884  HOH HOH A . 
F 6 HOH 885  1934 885  HOH HOH A . 
F 6 HOH 886  1935 886  HOH HOH A . 
F 6 HOH 887  1936 887  HOH HOH A . 
F 6 HOH 888  1937 888  HOH HOH A . 
F 6 HOH 889  1938 889  HOH HOH A . 
F 6 HOH 890  1939 890  HOH HOH A . 
F 6 HOH 891  1940 891  HOH HOH A . 
F 6 HOH 892  1941 892  HOH HOH A . 
F 6 HOH 893  1942 893  HOH HOH A . 
F 6 HOH 894  1943 894  HOH HOH A . 
F 6 HOH 895  1944 895  HOH HOH A . 
F 6 HOH 896  1945 896  HOH HOH A . 
F 6 HOH 897  1946 897  HOH HOH A . 
F 6 HOH 898  1947 898  HOH HOH A . 
F 6 HOH 899  1948 899  HOH HOH A . 
F 6 HOH 900  1949 900  HOH HOH A . 
F 6 HOH 901  1950 901  HOH HOH A . 
F 6 HOH 902  1951 902  HOH HOH A . 
F 6 HOH 903  1952 903  HOH HOH A . 
F 6 HOH 904  1953 904  HOH HOH A . 
F 6 HOH 905  1954 905  HOH HOH A . 
F 6 HOH 906  1955 906  HOH HOH A . 
F 6 HOH 907  1956 907  HOH HOH A . 
F 6 HOH 908  1957 908  HOH HOH A . 
F 6 HOH 909  1958 909  HOH HOH A . 
F 6 HOH 910  1959 910  HOH HOH A . 
F 6 HOH 911  1960 911  HOH HOH A . 
F 6 HOH 912  1961 912  HOH HOH A . 
F 6 HOH 913  1962 913  HOH HOH A . 
F 6 HOH 914  1963 914  HOH HOH A . 
F 6 HOH 915  1964 915  HOH HOH A . 
F 6 HOH 916  1965 916  HOH HOH A . 
F 6 HOH 917  1966 917  HOH HOH A . 
F 6 HOH 918  1967 918  HOH HOH A . 
F 6 HOH 919  1968 919  HOH HOH A . 
F 6 HOH 920  1969 920  HOH HOH A . 
F 6 HOH 921  1970 921  HOH HOH A . 
F 6 HOH 922  1971 922  HOH HOH A . 
F 6 HOH 923  1972 923  HOH HOH A . 
F 6 HOH 924  1973 924  HOH HOH A . 
F 6 HOH 925  1974 925  HOH HOH A . 
F 6 HOH 926  1975 926  HOH HOH A . 
F 6 HOH 927  1976 927  HOH HOH A . 
F 6 HOH 928  1977 928  HOH HOH A . 
F 6 HOH 929  1978 929  HOH HOH A . 
F 6 HOH 930  1979 930  HOH HOH A . 
F 6 HOH 931  1980 931  HOH HOH A . 
F 6 HOH 932  1981 932  HOH HOH A . 
F 6 HOH 933  1982 933  HOH HOH A . 
F 6 HOH 934  1983 934  HOH HOH A . 
F 6 HOH 935  1984 935  HOH HOH A . 
F 6 HOH 936  1985 936  HOH HOH A . 
F 6 HOH 937  1986 937  HOH HOH A . 
F 6 HOH 938  1987 938  HOH HOH A . 
F 6 HOH 939  1988 939  HOH HOH A . 
F 6 HOH 940  1989 940  HOH HOH A . 
F 6 HOH 941  1990 941  HOH HOH A . 
F 6 HOH 942  1991 942  HOH HOH A . 
F 6 HOH 943  1992 943  HOH HOH A . 
F 6 HOH 944  1993 944  HOH HOH A . 
F 6 HOH 945  1994 945  HOH HOH A . 
F 6 HOH 946  1995 946  HOH HOH A . 
F 6 HOH 947  1996 947  HOH HOH A . 
F 6 HOH 948  1997 948  HOH HOH A . 
F 6 HOH 949  1998 949  HOH HOH A . 
F 6 HOH 950  1999 950  HOH HOH A . 
F 6 HOH 951  2000 951  HOH HOH A . 
F 6 HOH 952  2001 952  HOH HOH A . 
F 6 HOH 953  2002 953  HOH HOH A . 
F 6 HOH 954  2003 954  HOH HOH A . 
F 6 HOH 955  2004 955  HOH HOH A . 
F 6 HOH 956  2005 956  HOH HOH A . 
F 6 HOH 957  2006 957  HOH HOH A . 
F 6 HOH 958  2007 958  HOH HOH A . 
F 6 HOH 959  2008 959  HOH HOH A . 
F 6 HOH 960  2009 960  HOH HOH A . 
F 6 HOH 961  2010 961  HOH HOH A . 
F 6 HOH 962  2011 962  HOH HOH A . 
F 6 HOH 963  2012 963  HOH HOH A . 
F 6 HOH 964  2013 964  HOH HOH A . 
F 6 HOH 965  2014 965  HOH HOH A . 
F 6 HOH 966  2015 966  HOH HOH A . 
F 6 HOH 967  2016 967  HOH HOH A . 
F 6 HOH 968  2017 968  HOH HOH A . 
F 6 HOH 969  2018 969  HOH HOH A . 
F 6 HOH 970  2019 970  HOH HOH A . 
F 6 HOH 971  2020 971  HOH HOH A . 
F 6 HOH 972  2021 972  HOH HOH A . 
F 6 HOH 973  2022 973  HOH HOH A . 
F 6 HOH 974  2023 974  HOH HOH A . 
F 6 HOH 975  2024 975  HOH HOH A . 
F 6 HOH 976  2025 976  HOH HOH A . 
F 6 HOH 977  2026 977  HOH HOH A . 
F 6 HOH 978  2027 978  HOH HOH A . 
F 6 HOH 979  2028 979  HOH HOH A . 
F 6 HOH 980  2029 980  HOH HOH A . 
F 6 HOH 981  2030 981  HOH HOH A . 
F 6 HOH 982  2031 982  HOH HOH A . 
F 6 HOH 983  2032 983  HOH HOH A . 
F 6 HOH 984  2033 984  HOH HOH A . 
F 6 HOH 985  2034 985  HOH HOH A . 
F 6 HOH 986  2035 986  HOH HOH A . 
F 6 HOH 987  2036 987  HOH HOH A . 
F 6 HOH 988  2037 988  HOH HOH A . 
F 6 HOH 989  2038 989  HOH HOH A . 
F 6 HOH 990  2039 990  HOH HOH A . 
F 6 HOH 991  2040 991  HOH HOH A . 
F 6 HOH 992  2041 992  HOH HOH A . 
F 6 HOH 993  2042 993  HOH HOH A . 
F 6 HOH 994  2043 994  HOH HOH A . 
F 6 HOH 995  2044 995  HOH HOH A . 
F 6 HOH 996  2045 996  HOH HOH A . 
F 6 HOH 997  2046 997  HOH HOH A . 
F 6 HOH 998  2047 998  HOH HOH A . 
F 6 HOH 999  2048 999  HOH HOH A . 
F 6 HOH 1000 2049 1000 HOH HOH A . 
F 6 HOH 1001 2050 1001 HOH HOH A . 
F 6 HOH 1002 2051 1002 HOH HOH A . 
F 6 HOH 1003 2052 1003 HOH HOH A . 
F 6 HOH 1004 2053 1004 HOH HOH A . 
F 6 HOH 1005 2054 1005 HOH HOH A . 
F 6 HOH 1006 2055 1006 HOH HOH A . 
F 6 HOH 1007 2056 1007 HOH HOH A . 
F 6 HOH 1008 2057 1008 HOH HOH A . 
F 6 HOH 1009 2058 1009 HOH HOH A . 
F 6 HOH 1010 2059 1010 HOH HOH A . 
F 6 HOH 1011 2060 1011 HOH HOH A . 
F 6 HOH 1012 2061 1012 HOH HOH A . 
F 6 HOH 1013 2062 1013 HOH HOH A . 
F 6 HOH 1014 2063 1014 HOH HOH A . 
F 6 HOH 1015 2064 1015 HOH HOH A . 
F 6 HOH 1016 2065 1016 HOH HOH A . 
F 6 HOH 1017 2066 1017 HOH HOH A . 
F 6 HOH 1018 2067 1018 HOH HOH A . 
F 6 HOH 1019 2068 1019 HOH HOH A . 
F 6 HOH 1020 2069 1020 HOH HOH A . 
F 6 HOH 1021 2070 1021 HOH HOH A . 
F 6 HOH 1022 2071 1022 HOH HOH A . 
F 6 HOH 1023 2072 1023 HOH HOH A . 
F 6 HOH 1024 2073 1024 HOH HOH A . 
F 6 HOH 1025 2074 1025 HOH HOH A . 
F 6 HOH 1026 2075 1026 HOH HOH A . 
F 6 HOH 1027 2076 1027 HOH HOH A . 
F 6 HOH 1028 2077 1028 HOH HOH A . 
F 6 HOH 1029 2078 1029 HOH HOH A . 
F 6 HOH 1030 2079 1030 HOH HOH A . 
F 6 HOH 1031 2080 1031 HOH HOH A . 
F 6 HOH 1032 2081 1032 HOH HOH A . 
F 6 HOH 1033 2082 1033 HOH HOH A . 
F 6 HOH 1034 2083 1034 HOH HOH A . 
F 6 HOH 1035 2084 1035 HOH HOH A . 
F 6 HOH 1036 2085 1036 HOH HOH A . 
F 6 HOH 1037 2086 1037 HOH HOH A . 
F 6 HOH 1038 2087 1038 HOH HOH A . 
F 6 HOH 1039 2088 1039 HOH HOH A . 
F 6 HOH 1040 2089 1040 HOH HOH A . 
F 6 HOH 1041 2090 1041 HOH HOH A . 
F 6 HOH 1042 2091 1042 HOH HOH A . 
F 6 HOH 1043 2092 1043 HOH HOH A . 
F 6 HOH 1044 2093 1044 HOH HOH A . 
F 6 HOH 1045 2094 1045 HOH HOH A . 
F 6 HOH 1046 2095 1046 HOH HOH A . 
F 6 HOH 1047 2096 1047 HOH HOH A . 
F 6 HOH 1048 2097 1048 HOH HOH A . 
F 6 HOH 1049 2098 1049 HOH HOH A . 
F 6 HOH 1050 2099 1050 HOH HOH A . 
F 6 HOH 1051 2100 1051 HOH HOH A . 
F 6 HOH 1052 2101 1052 HOH HOH A . 
F 6 HOH 1053 2102 1053 HOH HOH A . 
F 6 HOH 1054 2103 1054 HOH HOH A . 
F 6 HOH 1055 2104 1055 HOH HOH A . 
F 6 HOH 1056 2105 1056 HOH HOH A . 
F 6 HOH 1057 2106 1057 HOH HOH A . 
F 6 HOH 1058 2107 1058 HOH HOH A . 
F 6 HOH 1059 2108 1059 HOH HOH A . 
F 6 HOH 1060 2109 1060 HOH HOH A . 
F 6 HOH 1061 2110 1061 HOH HOH A . 
F 6 HOH 1062 2111 1062 HOH HOH A . 
F 6 HOH 1063 2112 1063 HOH HOH A . 
F 6 HOH 1064 2113 1064 HOH HOH A . 
F 6 HOH 1065 2114 1065 HOH HOH A . 
F 6 HOH 1066 2115 1066 HOH HOH A . 
F 6 HOH 1067 2116 1067 HOH HOH A . 
F 6 HOH 1068 2117 1068 HOH HOH A . 
# 
_pdbx_struct_mod_residue.id               1 
_pdbx_struct_mod_residue.label_asym_id    A 
_pdbx_struct_mod_residue.label_comp_id    ASN 
_pdbx_struct_mod_residue.label_seq_id     194 
_pdbx_struct_mod_residue.auth_asym_id     A 
_pdbx_struct_mod_residue.auth_comp_id     ASN 
_pdbx_struct_mod_residue.auth_seq_id      194 
_pdbx_struct_mod_residue.PDB_ins_code     ? 
_pdbx_struct_mod_residue.parent_comp_id   ASN 
_pdbx_struct_mod_residue.details          'GLYCOSYLATION SITE' 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 90  ? A HIS 90   ? 1_555 ZN ? C ZN . ? A ZN 1047 ? 1_555 OD1 ? A ASP 92  ? A ASP 92   ? 1_555 93.0  ? 
2  NE2 ? A HIS 90  ? A HIS 90   ? 1_555 ZN ? C ZN . ? A ZN 1047 ? 1_555 OD2 ? A ASP 204 ? A ASP 204  ? 1_555 98.0  ? 
3  OD1 ? A ASP 92  ? A ASP 92   ? 1_555 ZN ? C ZN . ? A ZN 1047 ? 1_555 OD2 ? A ASP 204 ? A ASP 204  ? 1_555 165.8 ? 
4  NE2 ? A HIS 90  ? A HIS 90   ? 1_555 ZN ? C ZN . ? A ZN 1047 ? 1_555 NE2 ? A HIS 471 ? A HIS 471  ? 1_555 104.9 ? 
5  OD1 ? A ASP 92  ? A ASP 92   ? 1_555 ZN ? C ZN . ? A ZN 1047 ? 1_555 NE2 ? A HIS 471 ? A HIS 471  ? 1_555 91.9  ? 
6  OD2 ? A ASP 204 ? A ASP 204  ? 1_555 ZN ? C ZN . ? A ZN 1047 ? 1_555 NE2 ? A HIS 471 ? A HIS 471  ? 1_555 93.8  ? 
7  NE2 ? A HIS 90  ? A HIS 90   ? 1_555 ZN ? C ZN . ? A ZN 1047 ? 1_555 O11 ? D SWA .   ? A SWA 1048 ? 1_555 161.9 ? 
8  OD1 ? A ASP 92  ? A ASP 92   ? 1_555 ZN ? C ZN . ? A ZN 1047 ? 1_555 O11 ? D SWA .   ? A SWA 1048 ? 1_555 85.9  ? 
9  OD2 ? A ASP 204 ? A ASP 204  ? 1_555 ZN ? C ZN . ? A ZN 1047 ? 1_555 O11 ? D SWA .   ? A SWA 1048 ? 1_555 80.8  ? 
10 NE2 ? A HIS 471 ? A HIS 471  ? 1_555 ZN ? C ZN . ? A ZN 1047 ? 1_555 O11 ? D SWA .   ? A SWA 1048 ? 1_555 93.2  ? 
11 NE2 ? A HIS 90  ? A HIS 90   ? 1_555 ZN ? C ZN . ? A ZN 1047 ? 1_555 O13 ? D SWA .   ? A SWA 1048 ? 1_555 88.8  ? 
12 OD1 ? A ASP 92  ? A ASP 92   ? 1_555 ZN ? C ZN . ? A ZN 1047 ? 1_555 O13 ? D SWA .   ? A SWA 1048 ? 1_555 83.8  ? 
13 OD2 ? A ASP 204 ? A ASP 204  ? 1_555 ZN ? C ZN . ? A ZN 1047 ? 1_555 O13 ? D SWA .   ? A SWA 1048 ? 1_555 87.5  ? 
14 NE2 ? A HIS 471 ? A HIS 471  ? 1_555 ZN ? C ZN . ? A ZN 1047 ? 1_555 O13 ? D SWA .   ? A SWA 1048 ? 1_555 165.8 ? 
15 O11 ? D SWA .   ? A SWA 1048 ? 1_555 ZN ? C ZN . ? A ZN 1047 ? 1_555 O13 ? D SWA .   ? A SWA 1048 ? 1_555 73.0  ? 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2008-01-08 
2 'Structure model' 1 1 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' 'Non-polymer description'   
2 2 'Structure model' 'Version format compliance' 
# 
loop_
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
_software.pdbx_ordinal 
CNS         1.1     ?                package 'Axel T. Brunger' axel.brunger@yale.edu    refinement        
http://cns.csb.yale.edu/v1.1/    Fortran_77 ? 1 
PDB_EXTRACT 2.000   'April. 3, 2006' package PDB               sw-help@rcsb.rutgers.edu 'data extraction' 
http://pdb.rutgers.edu/software/ C++        ? 2 
ADSC        Quantum ?                ?       ?                 ?                        'data collection' ? ?          ? 3 
DENZO       .       ?                ?       ?                 ?                        'data reduction'  ? ?          ? 4 
SCALEPACK   .       ?                ?       ?                 ?                        'data scaling'    ? ?          ? 5 
CNS         .       ?                ?       ?                 ?                        phasing           ? ?          ? 6 
# 
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 ASN 155 ? B CA A ASN 155 ? ? C  A ASN 155 ? ? 126.30 110.40 15.90  2.00 N 
2 1 CA A MET 264 ? ? CB A MET 264 ? ? CG A MET 264 ? B 103.06 113.30 -10.24 1.70 N 
3 1 CB A SER 677 ? A CA A SER 677 ? ? C  A SER 677 ? ? 124.70 110.10 14.60  1.90 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 HIS A 79  ? ? -153.87 84.80   
2  1 TRP A 95  ? ? -170.08 -87.02  
3  1 ASP A 106 ? ? -131.17 -59.41  
4  1 THR A 162 ? ? 61.79   -62.92  
5  1 GLN A 227 ? ? -136.25 -47.45  
6  1 ASP A 340 ? ? -170.29 -169.61 
7  1 SER A 411 ? ? 50.44   -127.71 
8  1 ILE A 549 ? ? -141.88 -50.38  
9  1 LEU A 550 ? ? -168.49 118.49  
10 1 PRO A 562 ? ? -81.78  38.98   
11 1 ASN A 732 ? ? -91.67  57.55   
12 1 SER A 762 ? ? 69.85   -2.92   
13 1 SER A 833 ? ? -149.60 -15.44  
14 1 ASP A 839 ? ? -123.24 -160.63 
15 1 GLU A 991 ? ? 19.04   109.40  
16 1 GLU A 992 ? ? -133.66 -135.74 
17 1 HIS A 993 ? ? -30.64  108.76  
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A ARG 1    ? A ARG 1    
2  1 Y 1 A SER 2    ? A SER 2    
3  1 Y 1 A SER 3    ? A SER 3    
4  1 Y 1 A HIS 4    ? A HIS 4    
5  1 Y 1 A HIS 5    ? A HIS 5    
6  1 Y 1 A HIS 6    ? A HIS 6    
7  1 Y 1 A HIS 7    ? A HIS 7    
8  1 Y 1 A HIS 8    ? A HIS 8    
9  1 Y 1 A HIS 9    ? A HIS 9    
10 1 Y 1 A GLY 10   ? A GLY 10   
11 1 Y 1 A GLU 11   ? A GLU 11   
12 1 Y 1 A PHE 12   ? A PHE 12   
13 1 Y 1 A ASP 13   ? A ASP 13   
14 1 Y 1 A ASP 14   ? A ASP 14   
15 1 Y 1 A PRO 15   ? A PRO 15   
16 1 Y 1 A ILE 16   ? A ILE 16   
17 1 Y 1 A ARG 17   ? A ARG 17   
18 1 Y 1 A PRO 18   ? A PRO 18   
19 1 Y 1 A PRO 19   ? A PRO 19   
20 1 Y 1 A LEU 20   ? A LEU 20   
21 1 Y 1 A LYS 21   ? A LYS 21   
22 1 Y 1 A VAL 22   ? A VAL 22   
23 1 Y 1 A ALA 23   ? A ALA 23   
24 1 Y 1 A ARG 24   ? A ARG 24   
25 1 Y 1 A SER 25   ? A SER 25   
26 1 Y 1 A PRO 26   ? A PRO 26   
27 1 Y 1 A ARG 27   ? A ARG 27   
28 1 Y 1 A PRO 28   ? A PRO 28   
29 1 Y 1 A GLY 29   ? A GLY 29   
30 1 Y 1 A GLN 30   ? A GLN 30   
31 1 Y 1 A SER 1045 ? A SER 1045 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 N-ACETYL-D-GLUCOSAMINE                       NAG 
3 'ZINC ION'                                   ZN  
4 1S-8AB-OCTAHYDRO-INDOLIZIDINE-1A,2A,8B-TRIOL SWA 
5 '(4R)-2-METHYLPENTANE-2,4-DIOL'              MRD 
6 water                                        HOH 
# 
